Entry
stringlengths 6
10
| Entry Name
stringlengths 5
11
| Sequence
stringlengths 2
35.2k
| EC number
stringlengths 7
118
⌀ | Cofactor
stringlengths 38
1.77k
⌀ | Gene Ontology (biological process)
stringlengths 18
11.3k
⌀ | Gene Ontology (cellular component)
stringlengths 17
1.75k
⌀ | Gene Ontology (molecular function)
stringlengths 24
2.09k
⌀ | Pfam
stringlengths 8
232
⌀ | Gene3D
stringlengths 10
250
⌀ | Protein families
stringlengths 9
237
⌀ | Post-translational modification
stringlengths 16
8.52k
⌀ | Subcellular location [CC]
stringlengths 29
6.18k
⌀ | Catalytic activity
stringlengths 64
35.7k
⌀ | Kinetics
stringlengths 69
11.7k
⌀ | Pathway
stringlengths 27
908
⌀ | pH dependence
stringlengths 64
955
⌀ | Temperature dependence
stringlengths 70
1.16k
⌀ | Function [CC]
stringlengths 17
15.3k
⌀ | Organism
stringlengths 8
196
|
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
O17087
|
GLD2_CAEEL
|
MVMAQQQKNAERNDEHTRRNRSPSVDSVSRVQQQSGGFAFYNQQSNHQYQQSHPRRTSFSRDGNTGYYNNHSGNKRQTYNNQRGGRSYNHRGNSNYQQNGEYSGNQGCVPKYHQRNQNYPQLQPKYSYFQPHQRPIFNSTQGYGTYSVRRSSPPSPSALSSSTANSTSNRAPTQPPILLRHAEPASDKNHQGSDHEQNHDPKIHLYRSAGTAPGGYTQCPSPYKQPPPQPPSTPSSSDKRIEQQQAEDWPTRFQHPPPQFRRGQDPMPASIELQHKTANQTMPVDIVQTNQQKTVSSYERAAQFRASASELPTDSVDAKHPCFANERMQSALIGISPQLKTQQQSPGIPIQNEAEASAVMKAMRSFQFHNWPQMSHGSYYPMPYHLENQMRPMKSGDQLPLNQQNHNLSGFPAFVGKSSLVGSSLNTRNSSEADPEEMPRIMEKLDDEVTGADHDKTIDENRRRIHKSQEPRIGTEEKALNELPRKANRRNSSCSSISSVSESSSPSALDESTLTKILPTDNFRGGRGFASPSPPTSLLSEPLSRMDVLSEKIWDYHNKVSQTDEMLQRKLHLRDMLYTAISPVFPLSGLYVVGSSLNGFGNNSSDMDLCLMITNKDLDQKNDAVVVLNLILSTLQYEKFVESQKLILAKVPILRINFAAPFDDITVDLNANNSVAIRNTHLLCYYSSYDWRVRPLVSVVKEWAKRKGINDANKSSFTSYSLVLMVIHFLQCGPTKVLPNLQQSYPNRFSNKVDVRTLNVTMALEEVADDIDQSLSEKTTLGELLIGFLDYYANEFNYDRDAISIRQGRRVERAALAVRPKIHSNSEGDKETPPPSSSASTSSIHNGGTPGIPMHHSISNPHFWRSQWRCVCIEEPFTNSNTAHSIYDEMVFEAIKKAFREAHGELQHNHDLDKLMECEPIKASTTNTGAAVFAATYEGERPLAQQPNTIACASLRVLNSIPVSSGPGHYHYQQQSNQNLSRPQRPGSNQGYQMNNNRGFNGNNQQQHQNRRSFNNQSSSNPGNGSTGPRSSRSNENVRDSSRQQNSQKGSSGVSVSKENVASTTGVPVDKKQQNSNRKDDGNRTKRSPMVQSPEPAKTKSEKTPMASSNVSQ
|
2.7.7.19
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
|
cytoplasmic polyadenylation [GO:0180011]; embryo development ending in birth or egg hatching [GO:0009792]; meiotic cell cycle [GO:0051321]; mRNA polyadenylation [GO:0006378]; mRNA processing [GO:0006397]; nucleus organization [GO:0006997]; positive regulation of meiosis I [GO:0060903]; positive regulation of mitotic nuclear division [GO:0045840]; regulation of cell division [GO:0051302]; RNA 3' uridylation [GO:0071076]
|
cytoplasm [GO:0005737]; P granule [GO:0043186]; protein-containing complex [GO:0032991]; RNA polymerase complex [GO:0030880]; RNA-directed RNA polymerase complex [GO:0031379]
|
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; poly(A) RNA polymerase activity [GO:1990817]; RNA uridylyltransferase activity [GO:0050265]
|
PF03828;
|
1.10.1410.10;3.30.460.10;
|
DNA polymerase type-B-like family, GLD2 subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12239571}.
|
CATALYTIC ACTIVITY: Reaction=ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide; Xref=Rhea:RHEA:11332, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17347, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:140395, ChEBI:CHEBI:173115; EC=2.7.7.19; Evidence={ECO:0000269|PubMed:12239571}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11333; Evidence={ECO:0000269|PubMed:12239571};
| null | null | null | null |
FUNCTION: Cytoplasmic poly(A) RNA polymerase that adds successive AMP monomers to the 3'-end of specific RNAs, forming a poly(A) tail. Acts as a regulator of mitosis/meiosis required for progression through meiotic prophase during oogenesis and spermatogenesis and for promotion of the entry into meiosis from the mitotic cell cycle. May act by regulating and activating gld-1 mRNA activity in germline. Required for polyadenylation of neg-1 mRNA during embryogenesis (PubMed:26096734). {ECO:0000269|PubMed:12239571, ECO:0000269|PubMed:14660440, ECO:0000269|PubMed:15063172, ECO:0000269|PubMed:15514056, ECO:0000269|PubMed:15911573, ECO:0000269|PubMed:17012378, ECO:0000269|PubMed:26096734, ECO:0000269|PubMed:9550713}.
|
Caenorhabditis elegans
|
O17185
|
SUP9_CAEEL
|
MKRQNIRTLSLIVCTLTYLLVGAAVFDALETENEILQRKLVQRVREKLKTKYNMSNADYEILEATIVKSVPHKAGYQWKFSGAFYFATTVITTIGYGHSTPMTDAGKVFCMLYALAGIPLGLIMFQSIGERMNTFAAKLLRFIRRAAGKQPIVTSSDLIIFCTGWGGLLIFGGAFMFSSYENWTYFDAVYYCFVTLTTIGFGDYVALQKRGSLQTQPEYVFFSLVFILFGLTVISAAMNLLVLRFLTMNTEDERRDEQEAILAAQGLVRVGDPTADDDFGRLPLSDNVSLASCSCYQLPDEKLRHRHRKHTEPHGGPPTFSGMTTRPKY
| null | null |
potassium ion transmembrane transport [GO:0071805]; potassium ion transport [GO:0006813]; regulation of muscle contraction [GO:0006937]; stabilization of membrane potential [GO:0030322]
|
muscle cell projection membrane [GO:0036195]; plasma membrane [GO:0005886]; striated muscle dense body [GO:0055120]
|
outward rectifier potassium channel activity [GO:0015271]; potassium channel activity [GO:0005267]; potassium ion leak channel activity [GO:0022841]
|
PF07885;
|
1.10.287.70;
|
Two pore domain potassium channel (TC 1.A.1.8) family
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=Associated with dense bodies. {ECO:0000269|PubMed:14534247}.
| null | null | null | null | null |
FUNCTION: Potassium channel involved in coordination of muscle contraction (PubMed:14534247). Activity is regulated by sup-18 (PubMed:24586202). {ECO:0000269|PubMed:14534247, ECO:0000269|PubMed:24586202}.
|
Caenorhabditis elegans
|
O17286
|
NFYB1_CAEEL
|
MDPKPINEGMLLEDHDHGMPEEEEITEDDMNGIHNIEEDTRTISEIAMELHHPNKSQVLLDQERFLPIANVVRIMKTQMDPQAKLAKDAKECAQECVSEFISFIASEAAEICNITKRKTITADDLLTAMEATGFDNYAEPMRIFLQKYRQAHKITGPIHRTHPDYVRPPQFQMDPFVRPLFFDTEQGRRCTETQYVINGSEIVKNAPLGEEWNEQTGTLNTRADGYYMEEPMEPMPMEEVEIEEHEEIIEQDSLGAIALEQQGQMQIYVDPKTKQHFAAKETPNGMELYPLIIQDTPLQLENVSGPNQFVMNMPDGRAIPHGMGQEEPQPVSSSSVMRKIGQNPSSYAQQHHHVSHVEQHDDVEYEEEEEVDQVEEDTVPVPIAPRPAATRVQPKRTPTKRKK
| null | null |
negative regulation of transcription by RNA polymerase II [GO:0000122]; regulation of gene expression [GO:0010468]; regulation of transcription by RNA polymerase II [GO:0006357]; tissue development [GO:0009888]
|
CCAAT-binding factor complex [GO:0016602]; cytoplasm [GO:0005737]; perikaryon [GO:0043204]
|
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity [GO:0001217]; protein heterodimerization activity [GO:0046982]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF00808;
|
1.10.20.10;
|
NFYB/HAP3 subunit family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17574230}. Cytoplasm {ECO:0000269|PubMed:15704008, ECO:0000269|PubMed:17574230}. Perikaryon {ECO:0000269|PubMed:15704008}. Note=Localizes to the cytoplasm of secretory cells and cell bodies of the small ganglia surrounding the pharynx. {ECO:0000269|PubMed:15704008}.
| null | null | null | null | null |
FUNCTION: Component of sequence-specific heterotrimeric transcription factor (nfya-1-NF-Y and nfya-2-NF-Y) complexes which specifically recognize a 5'-CCAAT-3' box motif found in the promoters of its target genes to regulate their expression and control cellular identity in particular tissue types (PubMed:17574230). In association with the components in the NF-Y complexes, represses the expression of the T-box transcription factor tbx-2 throughout larval development, which most likely restricts its expression to certain tissues (PubMed:23933492, PubMed:25873636). May act to repress txb-2 expression in conjunction with tbx-2 itself, which has an autoregulatory role (PubMed:25873636). In association with the components in the nfya-1-NF-Y complex, negatively regulates the expression of the homeobox protein egl-5 to spatially restrict its expression in tissues such as the head (PubMed:17574230). May regulate spatial egl-5 expression in association with the mes-2-mes-3-mes-6 complex (PubMed:17574230). {ECO:0000269|PubMed:17574230, ECO:0000269|PubMed:23933492, ECO:0000269|PubMed:25873636}.
|
Caenorhabditis elegans
|
O17323
|
HDA4_CAEEL
|
MEEASSSTGSAGGAGPSVPNLPSTSEAAIGQTNLEPESIALLQSQLQEYRQKQMDLIGHFQRAQQELSVQHMHNLYAALQQQQQLQNLQTERSAVNPLLISQQHSTEDQNSGPAAPLSLANSLTNLLSSSNGNLSVPQTPTKEHHPTAPTSNRKCDLPRSNSTTISQLTKDRLKNMIANRSKGESNSQSNLMSNSVTANGNGHDNGRKLKNSNSQVNVSSPHFEPYRLPTSLANAHNLQQASEFQLRKVNSEPNLKMRIRAKLLSKGSSPVQHVQQNNSQFNFTHPQLKRSDSETSQNVPLDFMQSSSQTNLPHLMLPSPSLPNLAAAGAFHGLNLPVGQDLNAFMAVANLSPFLSLPSLLNKKLELGGLTDEGDRNGLIGSSSTSSLASNVSMGSHQYQSLLKQQIRDLVLRRKSLVREDPEGEGLAELYNGLLPQAKLQQLQALAAESGFLAKQEPTCTTGLGYDQAMVRHECCCGNNASHVENGGRIQSIWSKLIEHGHVQKCEKVTAKKASLEQLQLVHSQTYTTFFAVSPTACLKIDANSLPLKRFLQLPCGGIGVDSDTYFNDASTQTAARLAAGTLIELSSQVAEGRLKNGFACIRPPGHHAEHEQAMGFCFFNNVAVAVKVLQTKYPAQCAKIAIIDWDVHHGNGTQLSFENDPNVLYMSLHRHDKGNFFPGTGSVTEVGKNDAKGLTVNVPFSGDVMRDPEYLAAWRTVIEPVMASFCPDFIIVSAGFDACHGHPNALGGYEVTPEMFGYMTKSLLNYASGKVVLALEGGYDLKSISEAAQQCVQALIGESDDAGRLSSVALESLPNPSAVETLQKVIAIHKSYWPALHGQEAAINTTEMQWRNLKLQVQMQQQQQQQQT
|
3.5.1.98
| null |
chromatin organization [GO:0006325]; negative regulation of transcription by RNA polymerase II [GO:0000122]; receptor guanylyl cyclase signaling pathway [GO:0007168]; regulation of neuron differentiation [GO:0045664]; signal transduction [GO:0007165]
|
cytoplasm [GO:0005737]; histone deacetylase complex [GO:0000118]; nucleus [GO:0005634]
|
calmodulin binding [GO:0005516]; histone deacetylase activity [GO:0004407]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; transcription corepressor activity [GO:0003714]
|
PF00850;
|
3.40.800.20;
|
Histone deacetylase family, HD type 2 subfamily
|
PTM: Phosphorylated by serine/threonine-protein kinase kin-29 at Ser-251; the phosphorylation inhibits repression of transcription by mef-2 (PubMed:17170704). May be phosphorylated by either cyclic-AMP dependent or cyclic-GMP dependent protein kinases (PubMed:18832350). {ECO:0000269|PubMed:17170704, ECO:0000269|PubMed:18832350}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-[histone]; Xref=Rhea:RHEA:58196, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:11338, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089, ChEBI:CHEBI:61930; EC=3.5.1.98;
| null | null | null | null |
FUNCTION: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4) (By similarity). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events (By similarity). Histone deacetylases act via the formation of large multiprotein complexes (By similarity). Involved in transduction of sensory signals, together with egl-4, kin-29 and mef-2; binding to transcription factor mef-2 enables negative modulation of chemoreceptor gene expression in chemosensory neurons (PubMed:17170704, PubMed:18832350). May be involved in muscle development (By similarity). {ECO:0000250|UniProtKB:P56524, ECO:0000269|PubMed:17170704, ECO:0000269|PubMed:18832350}.
|
Caenorhabditis elegans
|
O17386
|
CED8_CAEEL
|
MFLKKHKSKLLLVPRDEEQEDAGIVAVLTDRIPSVLLVRWFDLFCFGFAMCSYALDFFSDIGIAIFHFWAGRYLSGSLVLAFALLPSVIINIISMVWMLDDEMHWKRRAHPRRTGTFELNQKRFIPLSKMIVLCICQMGPLFWYYKALYYGWMFRKSSNENTDGEKRKCFSKMVEAERDATLLRFFEAFLESAPQLIIQGSIAASYFQNYYQTGTYPYWLYFQAASLLLSIISISWSVVVQNRSLRMIRDDKVNIWPHEAVLQFCWRFLTILARIITLVALVLIFGINVVPLISVHLLVTLVHVIFLQAIHIDACTHIEKLLLLINTFIHIFIPFNMVEGNTRWRYLTAYSVEFIEMMLVCWLLPLSLNTFPYIEKVQVGVPISFIAGIAIMMMYYQFFHPNRRQLIVTQSQEDLSLNVQKSVETLTPKLESSLEISGEQNTSQDLVSELLLDVEHEN
| null | null |
apoptotic process involved in development [GO:1902742]; embryo development ending in birth or egg hatching [GO:0009792]; engulfment of apoptotic cell [GO:0043652]; execution phase of apoptosis [GO:0097194]; phosphatidylserine exposure on apoptotic cell surface [GO:0070782]; programmed cell death [GO:0012501]
|
plasma membrane [GO:0005886]
|
phospholipid scramblase activity [GO:0017128]
|
PF09815;
| null |
XK family
|
PTM: Cleavage by ced-3 activates ced-8 function in promoting phosphatidylserine exposure at the surface of apoptotic cells. {ECO:0000269|PubMed:24225442}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10882128, ECO:0000269|PubMed:24225442}; Multi-pass membrane protein {ECO:0000269|PubMed:10882128}.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) = a 1,2-diacyl-sn-glycero-3-phospho-L-serine(out); Xref=Rhea:RHEA:38663, ChEBI:CHEBI:57262; Evidence={ECO:0000305|PubMed:23845944};
| null | null | null | null |
FUNCTION: Phospholipid scramblase that acts downstream of ced-9 and caspase ced-3 to promote phosphatidylserine exposure on apoptotic cell surface (PubMed:23845944, PubMed:24225442). Phosphatidylserine is a specific marker only present at the surface of apoptotic cells and acts as a specific signal for engulfment (PubMed:23845944, PubMed:24225442). Regulates apoptosis kinetics during embryonic development (PubMed:10882128, PubMed:1936965, PubMed:23845944, PubMed:24225442). Not required for engulfment of germ cell corpses (PubMed:9927601). {ECO:0000269|PubMed:10882128, ECO:0000269|PubMed:1936965, ECO:0000269|PubMed:23845944, ECO:0000269|PubMed:24225442, ECO:0000269|PubMed:9927601}.
|
Caenorhabditis elegans
|
O17389
|
TYB_CAEEL
|
MAAVTELPKMNQELAGAVREGLELKKVETTEKNVLPTKEDVAEEKQHVERIHEIEHFDSTKLHSTPVKEKIVLPSADDIKQEKQHLELTDKINNFPSENLKKTETIEKNVLPSPTDVAREKTLQMAASFDKSALHHVETIVSTDVRVTEAQ
| null | null |
actin filament organization [GO:0007015]
|
anchoring junction [GO:0070161]; cell cortex [GO:0005938]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]
|
actin monomer binding [GO:0003785]
|
PF01290;
|
1.20.5.520;
|
Thymosin beta family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000269|PubMed:15269284}. Cytoplasm {ECO:0000269|PubMed:15269284}. Cell junction {ECO:0000269|PubMed:15269284}. Cytoplasm, cytoskeleton {ECO:0000305|PubMed:15269284}. Note=Localizes to the cell cortex and the cytoplasm in oocytes and at the inside edges of membrane cubicles surrounding germ cell nuclei. Co-localizes with actin at the cell-cell contact in two-cell stage embryo. {ECO:0000269|PubMed:15269284}.
| null | null | null | null | null |
FUNCTION: Plays an important role in the organization of the cytoskeleton by regulating actin polymerization in two ways. Firstly, by binding to and sequestering actin monomers (G actin) inhibits actin polymerization. Secondly, by binding directly filamentous actin (F actin) promotes actin polymerization. Regulates the formation of cortical actin in oocytes conferring them enough rigidity to sustain the contractions during ovulation. {ECO:0000269|PubMed:15269284}.
|
Caenorhabditis elegans
|
O17468
|
HIRA_DROME
|
MRLLKPAWVHHDDKQIFSVDIHKDCTKFATGGQGSDCGRVVIWNLLPVLSDKAEFDADVPKMLCQMDQHLACVNCVRWSQNGQNLASGSDDKLIMIWRKSAGSSGVFGTGGMQKNHESWKCFYTLRGHDGDVLDLAWSPNDVYLASCSIDNTVIIWDAQAFPHSVATLKGHTGLVKGVSWDPLGRFLASQSDDRSIKIWNTMNWSLSHTITEPFEECGGTTHILRLSWSPDGQYLVSAHAMNGGGPTAQIIEREGWKCDKDFVGHRKAVTCVRFHNSILSRQENDGSPSKPLQYCCLAVGSRDRSLSVWMTALQRPMVVIHELFNASILDLTWGPQECLLMACSVDGSIACLKFTEEELGKAISEEEQNAIIRKMYGKNYVNGLGKSAPVLEHPQRLLLPQGDKPTKFPLSNNNEANQRPISKQTETRTKDGKRRITPMFIPLHEDGPTSLSMNIVSSSGSSTTALTSCSAAIGTLPAAAPTESAATPLMPLEPLVSKIDLGRLDSRLKTQPASQRRQSLPFDPGQSNELLRTPRLEEHQSSTCSPSNLNVTATGKSEFVKAALDYRLHVSNGHLKTQHGMLAKVTASDSKEMLWEFYVGSPLVNLNLCEKYAMLCSLDGSMRLISMETGCPVFPAISLTSSAVHCAFSPDNSLVGVLTECGLLRIWDIAKKVVSLAAGCLELLNKHGTAAQFSVTNQGMPLIGFPSGNSYSYSTSLQSWLVLATKDAIMYHGIRGTLPRDMDQMQQKFPLLSMQASSQNYFSFTGSMELRHSESWQQCAKIRFIENQIKLCEALQSLDELQHWHKMLTFQLATHGSEKRMRVFLDDLLSMPEPGISQFVPKLELMQCVLDTLKPHSEWNRLHSEYTELLKECKSERQKDIFATPAPPQQKTASSAGSSPRSGEATGEEVTEKDGATAVAAAVVAGSRMAVTTGTSTTTTTTASSSLSSSGSSSSTSGSGSSSSSSSTSSLSVPQPAPSLSPEIQTLDSPTVCIDDEILSASSSLPPLDTSPVEVSPASTSGGAASTSPAASVAGSAPVSSSKTDQT
| null | null |
chromatin organization [GO:0006325]; chromatin remodeling [GO:0006338]; DNA-templated transcription [GO:0006351]; regulation of DNA-templated transcription [GO:0006355]; sperm DNA decondensation [GO:0035041]
|
germinal vesicle [GO:0042585]; HIR complex [GO:0000417]; male germ cell nucleus [GO:0001673]; nucleus [GO:0005634]
|
chromatin binding [GO:0003682]; histone chaperone activity [GO:0140713]; nucleosome binding [GO:0031491]
|
PF07569;PF09453;PF00400;
|
2.130.10.10;
|
WD repeat HIR1 family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16251970}. Note=Maternally contributed protein localizes specifically to the male nucleus in fertilized eggs. This localization persists from the initiation of sperm nucleus decondensation to the end of pronucleus formation.
| null | null | null | null | null |
FUNCTION: Required for the periodic repression of histone gene transcription during the cell cycle (By similarity). Required for replication-independent chromatin assembly. Promotes remodeling of sperm chromatin following fertilization via the incorporation of histone H3.3 and histone H4. {ECO:0000250, ECO:0000269|PubMed:10837127, ECO:0000269|PubMed:11735001, ECO:0000269|PubMed:15988027, ECO:0000269|PubMed:16251970}.
|
Drosophila melanogaster (Fruit fly)
|
O17514
|
MES2_CAEEL
|
MSNSEPSTSTPSGKTKKRGKKCETSMGKSKKSKNLPRFVKIQPIFSSEKIKETVCEQGIEECKRMLKGHFNAIKDDYDIRVKDELDTDIKDWLKDASSSVNEYRRRLQENLGEGRTIAKFSFKNCEKYEENDYKVSDSTVTWIKPDRTEEGDLMKKFRAPCSRIEVGDISPPMIYWVPIEQSVATPDQLRLTHMPYFGDGIDDGNIYEHLIDMFPDGIHGFSDNWSYVNDWILYKLCRAALKDYQGSPDVFYYTLYRLWPNKSSQREFSSAFPVLCENFAEKGFDPSSLEPWKKTKIAEGAQNLRNPTCYACLAYTCAIHGFKAEIPIEFPNGEFYNAMLPLPNNPENDGKMCSGNCWKSVTMKEVSEVLVPDSEEILQKEVKIYFMKSRIAKMPIEDGALIVNIYVFNTYIPFCEFVKKYVDEDDEESKIRSCRDAYHLMMSMAENVSARRLKMGQPSNRLSIKDRVNNFRRNQLSQEKAKRKLRHDSLRIQALRDGLDAEKLIREDDMRDSQRNSEKVRMTAVTPITACRHAGPCNATAENCACRENGVCSYMCKCDINCSQRFPGCNCAAGQCYTKACQCYRANWECNPMTCNMCKCDAIDSNIIKCRNFGMTRMIQKRTYCGPSKIAGNGLFLLEPAEKDEFITEYTGERISDDEAERRGAIYDRYQCSYIFNIETGGAIDSYKIGNLARFANHDSKNPTCYARTMVVAGEHRIGFYAKRRLEISEELTFDYSYSGEHQIAFRMVQTKERSEKPSRPKSQKLSKPMTSE
|
2.1.1.356
| null |
epigenetic regulation of gene expression [GO:0040029]; gamete generation [GO:0007276]; germ cell development [GO:0007281]; germ-line stem cell division [GO:0042078]; heterochromatin formation [GO:0031507]; methylation [GO:0032259]; negative regulation of gene expression [GO:0010629]; regulation of gene expression [GO:0010468]; regulation of transcription by RNA polymerase II [GO:0006357]; tissue development [GO:0009888]
|
ESC/E(Z) complex [GO:0035098]; nucleosome [GO:0000786]; nucleus [GO:0005634]; PcG protein complex [GO:0031519]
|
chromatin binding [GO:0003682]; histone H3K27 methyltransferase activity [GO:0046976]; histone H3K27 trimethyltransferase activity [GO:0140951]; histone methyltransferase activity [GO:0042054]
|
PF18264;PF00856;
|
2.170.270.10;
|
Class V-like SAM-binding methyltransferase superfamily, Histone-lysine methyltransferase family, EZ subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9609829}.
|
CATALYTIC ACTIVITY: Reaction=L-lysyl(27)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(27)-[histone H3] + 3 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60292, Rhea:RHEA-COMP:15535, Rhea:RHEA-COMP:15548, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.356;
| null | null | null | null |
FUNCTION: Polycomb group (PcG) protein. Catalytic subunit of a the mes-2/mes-3/mes-6 complex, which methylates 'Lys-27' of histone H3, leading to transcriptional repression of the affected target genes. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development. In association with the nfya-1-NF-Y complex, may play a role in repressing the expression of the homeobox protein egl-5 in tissues such as the head (PubMed:17574230). PcG proteins are not required to initiate repression, but to maintain it during later stages of development. The mes-2/mes-3/mes-6 complex may participate in the global inactivation of the X chromosomes in germline cells. This complex is required to exclude mes-4 from the inactivated X-chromosomes in germline cells (PubMed:12077420, PubMed:15380065). Required for small-RNA-induced H3K27 trimethylation (PubMed:26365259). Involved in the negative regulation of lifespan in a germline-independent fashion (PubMed:22212395). {ECO:0000269|PubMed:12077420, ECO:0000269|PubMed:15380065, ECO:0000269|PubMed:17574230, ECO:0000269|PubMed:22212395, ECO:0000269|PubMed:26365259}.
|
Caenorhabditis elegans
|
O17528
|
TMED2_CAEEL
|
MNSLTWILAVLFVTPAASYFIHVDANEEQCFFDRLTSGTKMGLMFEVAEGGFLDIDVKITGPDNKEIYKGERESSGKFTFAAHMDGVYTYCFGNKMSTMTPKAVMFTVEITEPHQQAPGAAANQDAADNAKLEEMVRELSSALMSVKHEQEYMEVRERVHRNINENTNSRVVMWAAFEAFVLVGMTVGQIFYLKRFFEVRTMV
| null | null |
endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; Golgi organization [GO:0007030]; intracellular protein transport [GO:0006886]; regulation of Notch signaling pathway [GO:0008593]; regulation of transport [GO:0051049]
|
COPI-coated vesicle membrane [GO:0030663]; COPII-coated ER to Golgi transport vesicle [GO:0030134]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; ER to Golgi transport vesicle membrane [GO:0012507]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]
|
cargo receptor activity [GO:0038024]
|
PF01105;
| null |
EMP24/GP25L family
| null |
SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Single-pass type I membrane protein. Cytoplasmic vesicle, COPI-coated vesicle membrane; Single-pass type I membrane protein. Golgi apparatus membrane; Single-pass type I membrane protein. Note=Golgi-derived coatomer-coated vesicles.
| null | null | null | null | null |
FUNCTION: May have a role in the negative regulation of lin-12 and glp-1 transport to the cell surface (PubMed:10366590). May also have a role in a quality control mechanism for endoplasmic reticulum-Golgi transport; the budding of coatomer-coated and other species of coated vesicles, could bind cargo molecules to collect them into budding vesicles (PubMed:10366590). Involved in regulating the expression of proteasomal subunits such as rpt-3 in order to confer resistance to proteasomal dysfunction (PubMed:27528192). {ECO:0000269|PubMed:10366590, ECO:0000269|PubMed:27528192}.
|
Caenorhabditis elegans
|
O17581
|
SCC4_CAEEL
|
MNQDAVAKALLGMAEALRTQDPPKLKMAIKCARSTLSMEISDEMKAICNLQLGKLLFFYTDNFELAKNHLQCAYDKMSAMGTFYTRDKMNAISMLADLHIHYQQWPLTSIKATIRHEITTTRGFPALSNKLMFQLIELMKIDKDVEGAIEMCQLAINSSHADPKMELYFRIAKTLVTYQLMHEEPDISDVTRIGSMIKVMENSTTSDKAHLECIKDFYVCTKLAYMFYEGKSRTSRQLLRQIQKSQTSGETKIHGIRWLGEPSITLLACVMNQICALVQSNTDRVEKYYHLVIKHADEIIFKSTRSPQEPGVVRCINMIKMTTLEMMACCNVLACRPQKTLHNVRDMLEWSNRTSGPLLTRYFTPHIHYILGLQCCYFRQHENAENHFRAAMKKLHKEDITAHNTMALLNLNLAITYLNQLKMADYYEVSENLTAPKISSCSQMLKNNVKLLSAFFAYITNKLNECKLLSHEVLDDSKAEDFFRLHGLGLLLLSLVTDVDEKGVRPTVDWSKKSHDHVVILFSHSLYEKILLAAGYDPKSELMKMVVSEQLASRRMLSVENLTPLVANMPASKLLQWFDGDPFKLLPRDETVL
| null | null |
anterior/posterior axon guidance [GO:0033564]; cell division [GO:0051301]; chromosome segregation [GO:0007059]; dorsal/ventral axon guidance [GO:0033563]; egg-laying behavior [GO:0018991]; maintenance of mitotic sister chromatid cohesion [GO:0034088]
|
axon [GO:0030424]; chromatin [GO:0000785]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; SMC loading complex [GO:0032116]
|
double-stranded DNA binding [GO:0003690]
| null | null |
SCC4/mau-2 family
| null |
SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:15539489}. Cytoplasm {ECO:0000269|PubMed:15539489}. Note=Binds to chromatin from the end of mitosis until prophase. Localizes to the cytoplasm of neurons.
| null | null | null | null | null |
FUNCTION: Plays an important role in the loading of the cohesin complex on to DNA (By similarity). Forms a heterodimeric complex (also known as cohesin loading complex) with scc-2/SCC2 which mediates the loading of the cohesin complex onto chromatin (By similarity). Required for normal development until the fourth larval stage. Functions cell autonomously to guide migrations during the development of the nervous system. Participates in the guidance of mechanosensory neuron AVM by a slt-1-independent mechanism. Regulates chromosome segregation in early embryos. {ECO:0000250|UniProtKB:Q9Y6X3, ECO:0000269|PubMed:15539489}.
|
Caenorhabditis elegans
|
O17583
|
LIN10_CAEEL
|
MSSEAVAQATAATTSPEHGVPTSSATPTPPPSKGGGAGGGGGGEQQQVPFQMIPPGHFFANPFLNPYIPTAGAPAQEGEAQPQMVFSPAQYQEVMHHYFQQMMAASGAQFPIPFPMQFQPALQQPRPSSQASSSHRSEDDNGRQTAGSVVSSNVSPNHREVRPAEDSTETSGVVQNNDELLVPTSTSSDVTIGDVIEKSDSPENSQESAGGEEKSEEKRKLSGDRTDSLIRKQMSEMEKEITRRSQNKNIKTIDDDGLAELIGGSSTRTVADDFSPFVDKSGLSYTAPAPPSTEKSAPKESLNQLRSSFNLPDDSTTVGPVGPSTVPQQSQQFANNSMFMANAGNFVQNAFPIGVTMTPQATFGAAPGFQMMQPHQHNLFMQQPNPTFVNNGTNPFLQTQATLPNFVQNGTAPLVPTVSAQQFTPEQLAAAFAQQQIAQSAAPTPFDSPPPSMPSTSSGPSGALAPPPPPSHPIPRRVSGNGWPEENKENGTSTSTTNGAQSVPAAAGTDDPVWVLRDSYLKKMQREQRTSEEEEMSWQEAATAAQEAAENGGGDDQEEQETDRLLNGGTTGASTKGAERRGSVDKKKNSKETMVHEPAVLIEGVLFRARYLGSTQMLCESRGSKAARMAQAQEAVARVKAPEGDVQPSTEIDLFISTEKIMVLNTDLQRISDTDVRQDILMDHALRTISYIADIGDLVVLMARRMSTSHSDESCSDGDSSGGGVRKTPKVICHVFESDEASFIAQSIGQAFQVAYVEFLRANGIDDPSYLRQIDYQEVLNSQELLGDELEMFAKKETQKEVVVPKKAGEPLGIVVVESGWGSMLPTVVLAHMNPVGPAAHSNKLNIGDQIININGISLVGLPLSAAQTQIKNMKTATAVRMTVVSTPPVVEVRIRRPDTKYQLGFSVQNGVICSLLRGGIAERGGIRVGHRIIEINGTSVVAVAHDRIVNMLATAVGEIHMKTMPTSMFRLLTGQEQPQYI
| null | null |
chemical synaptic transmission [GO:0007268]; nervous system development [GO:0007399]; neuron-neuron synaptic transmission [GO:0007270]; positive regulation of backward locomotion [GO:1905852]; positive regulation of vulval development [GO:0040026]; protein localization [GO:0008104]; protein localization to basolateral plasma membrane [GO:1903361]; protein localization to early endosome [GO:1902946]; receptor localization to synapse [GO:0097120]; regulation of backward locomotion [GO:0043058]; response to mechanical stimulus [GO:0009612]; sensory perception of touch [GO:0050975]
|
cytoplasm [GO:0005737]; dendrite [GO:0030425]; dendritic spine [GO:0043197]; Golgi apparatus [GO:0005794]; Golgi cisterna membrane [GO:0032580]; Golgi trans cisterna [GO:0000138]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; synapse [GO:0045202]; trans-Golgi network transport vesicle [GO:0030140]
|
amyloid-beta binding [GO:0001540]; small GTPase binding [GO:0031267]
|
PF00595;PF00640;
|
2.30.42.10;2.30.29.30;
| null |
PTM: Phosphorylated on multiple Ser and Thr residues by cdk-5 which regulates its localization (PubMed:17671168, PubMed:22252129). {ECO:0000269|PubMed:17671168, ECO:0000269|PubMed:22252129}.; PTM: May be hydroxylated by egl-9 isoform e on multiple Pro residues which may prevent phosphorylation by cdk-5. {ECO:0000269|PubMed:22252129}.
|
SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:10359617}; Peripheral membrane protein {ECO:0000269|PubMed:10359617}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:10359617}; Peripheral membrane protein {ECO:0000269|PubMed:10359617}. Cytoplasm {ECO:0000269|PubMed:22252129}. Synapse {ECO:0000269|PubMed:17671168}. Perikaryon {ECO:0000269|PubMed:22213799}. Note=In trans cisternae of Golgi or trans-Golgi network (PubMed:10359617). Localizes to Golgi-associated structures (PubMed:22213799). Partially co-localizes with glr-1 at the synapse (PubMed:17671168). Localizes in endosome-like structures in ventral cord dendrites. During hypoxia, diffused cytoplasmic localization. Localization in the ventral nerve cord is regulated by egl-9 isoform e and cdk-5 (PubMed:22252129). Co-localizes with rab-6.2 in neuronal cell bodies (PubMed:22213799). Co-localizes with rme-8 in puntate structures in neuronal cell bodies and in the intestine (PubMed:22213799). {ECO:0000269|PubMed:10359617, ECO:0000269|PubMed:17671168, ECO:0000269|PubMed:22213799, ECO:0000269|PubMed:22252129}.
| null | null | null | null | null |
FUNCTION: Required specifically for the determination of 3 vulval precursor cell fates P5.p, P6.p and P7.p during late second and early third larval stages; required for basolateral localization of receptor tyrosine kinase let-23. Could have a general but redundant role in development, functioning in diverse cell lineages to control cell fates (PubMed:10359617, PubMed:2159938). Regulates the trafficking of the glr-1 subunit of AMPA-type glutamate receptors (AMPRs) in the ventral nerve cord (PubMed:17671168, PubMed:22213799, PubMed:22252129). This may be partly through interacting with the small GTPase rab-6.2 in its active GTP-bound state (PubMed:22213799). {ECO:0000269|PubMed:10359617, ECO:0000269|PubMed:17671168, ECO:0000269|PubMed:2159938, ECO:0000269|PubMed:22213799, ECO:0000269|PubMed:22252129}.
|
Caenorhabditis elegans
|
O17607
|
RUVB1_CAEEL
|
MDMEVDEAISGTSSSRLAPIEEVKPTPKQIKRIAAHSHVKGLGIDTETQEAHYEAAGFVGQAPARTAASIVVDMIRLKCMAGRAVLIAGPPATGKTAIALAMSQELGDGVPFVPLVASEVFSNEVKKTEVLMRSFRRAIGLRVKETKDVYEGEVTELSPVEASDNSGMGKTISHLVLSLKTAKGSKQLKLDPSIYDSILKQRVEVGDVIYIEANSGIVKRVGRCDVYASEFDLEADEFVPMPKGDVRKSKDIVQNVSLHDLDIANARPQGRQGDVSNIVSQLMTPKKTEVTDRLRSEINKVVNEYIESGVAELMPGVLFIDEVHMLDVECFTYLYRALESPMAPVVVFATNRGTTTVRGLGDKAPHGIPPEMLDRLMIIPTMKYNEEDIRKILVHRTEAENVQFEEKAFDLLSKVGAEKSLRYALQLIAPARLCAQTCGREVIEVEDVDRCTKLFMDRGESLKKAEEEMRQPKNKK
|
3.6.4.12
| null |
box C/D snoRNP assembly [GO:0000492]; chromatin remodeling [GO:0006338]; DNA repair [GO:0006281]; nematode larval development [GO:0002119]; positive regulation of translation [GO:0045727]; regulation of transcription by RNA polymerase II [GO:0006357]; TOR signaling [GO:0031929]
|
cytoplasm [GO:0005737]; Ino80 complex [GO:0031011]; NuA4 histone acetyltransferase complex [GO:0035267]; nucleus [GO:0005634]; R2TP complex [GO:0097255]; Swr1 complex [GO:0000812]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA helicase activity [GO:0003678]
|
PF06068;PF17856;
|
1.10.8.60;3.40.50.300;2.40.50.360;
|
RuvB family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25437307}. Nucleus {ECO:0000269|PubMed:25437307}.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; Evidence={ECO:0000250|UniProtKB:P0A812};
| null | null | null | null |
FUNCTION: Possesses single-stranded DNA-stimulated ATPase and ATP dependent DNA helicase (3' to 5') activity suggesting a role in nuclear processes such as recombination and transcription (By similarity). May participate in several chromatin remodeling complexes that mediate the ATP-dependent exchange of histones and remodel chromatin by shifting nucleosomes (By similarity). Involvement in these complexes is likely required for transcriptional activation of selected genes and DNA repair in response to DNA damage (By similarity). Involved in the Ce-Tor signaling pathway whereby it is required for the accumulation and localization of box C/D snoRNP to nucleoli to regulate ribosomal maturation and thus protein synthesis (PubMed:18804378). Antagonizes the transcriptional activity of transcription factor pha-4, to control postembryonic development and adult longevity (PubMed:17720918, PubMed:18804378). Has a role in pharyngeal development (PubMed:17720918). Has a role in gonadal development (PubMed:25437307). {ECO:0000250|UniProtKB:Q03940, ECO:0000250|UniProtKB:Q9Y265, ECO:0000269|PubMed:17720918, ECO:0000269|PubMed:18804378, ECO:0000269|PubMed:25437307}.
|
Caenorhabditis elegans
|
O17622
|
KCY1_CAEEL
|
MYNVVFVLGPPGSGKGTICTQIHENLGYVHLSAGDLLRAERERAGSEYGALIEGHIKNGSIVPVEITCALLENAMIASKDANGFLIDGFPRNEDNWSGWNKQMGGKVNEQFVLFLSCPVDVCIDRCLHRGQGRTDDNVESLKKRVETYNQSTFPIIEHFEKVGMVREVNSERPVTEVYEDVVKVFAAANQK
|
2.7.4.14
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_03172}; Note=Binds 1 Mg(2+) ion per monomer. {ECO:0000255|HAMAP-Rule:MF_03172};
|
'de novo' pyrimidine nucleobase biosynthetic process [GO:0006207]; CDP biosynthetic process [GO:0046705]; phosphorylation [GO:0016310]; UDP biosynthetic process [GO:0006225]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; CMP kinase activity [GO:0036430]; cytidylate kinase activity [GO:0004127]; dCMP kinase activity [GO:0036431]; UMP kinase activity [GO:0033862]
|
PF00406;
|
3.40.50.300;
|
Adenylate kinase family, UMP-CMP kinase subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03172}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03172}.
|
CATALYTIC ACTIVITY: Reaction=ATP + CMP = ADP + CDP; Xref=Rhea:RHEA:11600, ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377, ChEBI:CHEBI:456216; EC=2.7.4.14; Evidence={ECO:0000255|HAMAP-Rule:MF_03172, ECO:0000269|PubMed:19645718}; CATALYTIC ACTIVITY: Reaction=ATP + dCMP = ADP + dCDP; Xref=Rhea:RHEA:25094, ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593, ChEBI:CHEBI:456216; EC=2.7.4.14; Evidence={ECO:0000255|HAMAP-Rule:MF_03172, ECO:0000269|PubMed:19645718}; CATALYTIC ACTIVITY: Reaction=ATP + UMP = ADP + UDP; Xref=Rhea:RHEA:24400, ChEBI:CHEBI:30616, ChEBI:CHEBI:57865, ChEBI:CHEBI:58223, ChEBI:CHEBI:456216; EC=2.7.4.14; Evidence={ECO:0000255|HAMAP-Rule:MF_03172, ECO:0000269|PubMed:19645718};
| null | null | null | null |
FUNCTION: Catalyzes the phosphorylation of pyrimidine nucleoside monophosphates at the expense of ATP. Plays an important role in de novo pyrimidine nucleotide biosynthesis. Has preference for UMP and CMP as phosphate acceptors. {ECO:0000255|HAMAP-Rule:MF_03172, ECO:0000269|PubMed:19645718}.
|
Caenorhabditis elegans
|
O17645
|
HST2_CAEEL
|
MLWKKRKVLYFAGISVFILILLLLKLNSKPKANVWPTSSKIVIYNRIPKTGSTTFTNAIAYDLYKENGFSVLHVNMTKNRQVMSLPDQYTFVNNITTWTERLPAFYHGHVAFIDFQRFGIANPIYINIIREPLERLLSHYYFLRYGDNYRIGLKRSRAGNNETFDECYSRGGKDCDMKQMWIQIPYFCGHYHFCTEVGNPEALRVAKQNVLEKYLLVGTTSRMRDMIALLEVTVPDFFKGALGHFDSLDANRAHLRYTKKKIPPNDQTLSMIRRDEVYKMEREFYDFINNLFDAVFKKATNGISKADDLVKLPLQYHFEKIKPS
|
2.8.2.-
| null |
heparan sulfate proteoglycan biosynthetic process, enzymatic modification [GO:0015015]; heparan sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process [GO:0015014]; positive regulation of multicellular organism growth [GO:0040018]; regulation of axon guidance [GO:1902667]; regulation of cell migration [GO:0030334]
|
Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]
|
heparan sulfate 2-O-sulfotransferase activity [GO:0004394]
|
PF03567;
|
3.40.50.300;
|
Sulfotransferase 3 family
| null |
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Catalyzes the transfer of sulfate to the C2-position of selected hexuronic acid residues within the maturing heparan sulfate (HS). Involved in cell adhesion and guidance by specifically modifying proteoglycans in the extracellular matrix and on the cell surface that are essential for axon migrations. {ECO:0000269|PubMed:12653634, ECO:0000269|PubMed:15003172, ECO:0000269|PubMed:15671174}.
|
Caenorhabditis elegans
|
O17670
|
EYA1_CAEEL
|
MLPDSEGQKLKTFLLGTGTTLDPSLDPTGNSNFSMATTSDSSTIWTALPASQPGDKDIPTVDLAAISEAYGSTSSTTSLTSSVTSQYQYNSYPQYAMYTSANPANYYQQVTANLRAGTTAFPYSLTTPSYYGSYPVDYTSAAAAYQNPYYTNLRGGTAAPYYNPLNATTAAAYASVASSVLGTDAVNLGTSSDGSTGVPSTVTSFSLKEKKPKVSKKKKTGSCSPGDETYARVFIWDIDDIAVISRNYLASVTHTNEFYARAANSVSHLMERIALNNFADVNEFLEGDITNIEDAVVDETTMDSGPIDNLRGLDVMRRVAPKYSAFRQFYTENSTKNDVAGFKQEQNGFNFELLERVGFGAREATELYQSAIQLQTLPNFGQRWPCAQRCMDLVVEKSKLSAEKYANVVLSNDGLVLGAAQLMISGLNSSVPVENIYSISKQGKESVFEKIQSRFGKKCSFICITSGDTANSAKRLNIPVWPLNSNTDLDKLYSALDNFLLGG
|
3.1.3.48
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|RuleBase:RU362036}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|RuleBase:RU362036};
|
cell differentiation [GO:0030154]; egg-laying behavior [GO:0018991]; embryonic morphogenesis [GO:0048598]; locomotion [GO:0040011]; mesodermal cell fate specification [GO:0007501]; negative regulation of apoptotic process [GO:0043066]; negative regulation of extrinsic apoptotic signaling pathway in absence of ligand [GO:2001240]; nematode larval development [GO:0002119]; positive regulation of apoptotic process involved in development [GO:1904747]; positive regulation of cellular response to heat [GO:1900036]; positive regulation of DNA repair [GO:0045739]; positive regulation of response to oxidative stress [GO:1902884]; regulation of DNA-templated transcription [GO:0006355]; tissue morphogenesis [GO:0048729]
|
nucleus [GO:0005634]
|
metal ion binding [GO:0046872]; protein tyrosine phosphatase activity [GO:0004725]; transcription coactivator activity [GO:0003713]
| null |
3.40.50.12350;
|
HAD-like hydrolase superfamily, EYA family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16154558, ECO:0000269|PubMed:19427847}.
|
CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|RuleBase:RU362036};
| null | null | null | null |
FUNCTION: Tyrosine protein phosphatase (By similarity). Acts probably as a transcription regulator in the embryonic and postembryonic development of several tissues including pharynx, vulva and gonads (PubMed:16154558). Required for the development of anterior tissues during late embryogenesis (PubMed:16154558). Together with ceh-34, required to specify the coelomocyte fate in embryonic and postembryonic precursors (PubMed:19427847). In the anterior part of the embryo, prevents apoptosis in cells that are not fated to die (PubMed:16154558). Together with ceh-34 activates proapoptotic factor egl-1 expression to promote motor neuron M4 sister cell apoptosis (PubMed:20713707). Also promotes apoptosis of I1 pharyngeal neuron sister cell (PubMed:20713707). Plays a role in locomotion and fertility (PubMed:16154558). May play a role in resistance to heat and oxidative stresses (PubMed:25108328). May cooperate with the transcription factors vab-3 and ceh-32 to repress transcription factor ets-5 expression in non BAG neuronal cells (PubMed:30890567). {ECO:0000250|UniProtKB:Q05201, ECO:0000269|PubMed:16154558, ECO:0000269|PubMed:19427847, ECO:0000269|PubMed:20713707, ECO:0000269|PubMed:25108328, ECO:0000269|PubMed:30890567}.
|
Caenorhabditis elegans
|
O17679
|
SET6_CAEEL
|
MERSRTGGSSTYSMSTANVPIITISDDDDELTIWEEPRKSPISSNSYSDERNHSLSSTSNSSVERSIIITISDDESEATERNQQEVVDRAISNNLTEKRRRSVESFHRLHSKERKLEVKSRKKSRTSSSSMEASTSCTFPARQTKTKRHKRKTYSTISSFAPHHSTICAELRNVNPARIADFRHPSIFEYSDMSLNERREHWKKEMKVIKKHNDIRLMHEEAVRFDDIIELDPTLNGYYRRFMGAEQSTRALFMAVRCLATFGRNFYEEPERDHGEEEIPEELDRYFEKLIYVAPRTRIRITDDIHLSNDTHRIPVYTDAKGETLKTVKIPNPLLYDHIINNMVDKVKEPLLYEAIKIAGSSENVIRCKCCSQDPVVNCFDNKDCPCFIANQFLQSRNKTTDTNEKLKFHTFQPLMYNDGNPTYYNTVGFACSPKCACKGACTNNATYLIQKKLYSIEIYRADPQIGFGIRSTLFIPAGTPIIEYCGELVDGERLHSSLENYSYQLTDCEGDKHLYNLLREKYKNNPEYYDVLDELSKHHFHLDAKMQGSVGRFANHSCTPNMEPLRLFKEGFTPANMRMIFFTLKDIFPGEPLTLDYGSEYKVFRRQRCLCRTFACRSGPHYEKFSNLDGKLIASCFVRLHHASRIRYSVDLQLIERFYSVGKVEEVRVDPCVSFSKYNLKWRRQLSTATCERLENVIEIELSDEDS
|
2.1.1.-; 2.1.1.366
| null |
epigenetic regulation of gene expression [GO:0040029]; methylation [GO:0032259]
|
chromatin [GO:0000785]; nucleus [GO:0005634]
|
histone H3K9 dimethyltransferase activity [GO:0140942]; histone H3K9 trimethyltransferase activity [GO:0140949]; histone H3K9me2 methyltransferase activity [GO:0140947]
|
PF00856;
|
2.170.270.10;
|
Class V-like SAM-binding methyltransferase superfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:32103178}. Chromosome {ECO:0000269|PubMed:32103178}.
|
CATALYTIC ACTIVITY: Reaction=N(6)-methyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-methionine = H(+) + N(6),N(6)-dimethyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60284, Rhea:RHEA-COMP:15541, Rhea:RHEA-COMP:15542, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61929, ChEBI:CHEBI:61976; Evidence={ECO:0000269|PubMed:32103178}; CATALYTIC ACTIVITY: Reaction=N(6),N(6)-dimethyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-methionine = H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60288, Rhea:RHEA-COMP:15538, Rhea:RHEA-COMP:15541, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961, ChEBI:CHEBI:61976; EC=2.1.1.366; Evidence={ECO:0000269|PubMed:32103178};
| null | null | null | null |
FUNCTION: Histone methyltransferase that specifically di- and trimethylates 'Lys-9' of histone H3 (H3K9me2 and H3K9me3, respectively); involved in positively modulating the rate of age-related behavioral deterioration (PubMed:32103178). May repress the expression of mitochondrial function-related genes by occupying their promoter regions, working in concert with probable chromatin reader protein, baz-2 (PubMed:32103178). Involved in modulation of the mitochondrial unfolded protein response (UPR) (PubMed:32103178). Regulates level of expression of bas-1, a serotonin (5-HT) and dopamine synthesizing enzyme (DOPA decarboxylase) (PubMed:32103178). Negatively modulates levels of endogenous 5-HT and dopamine with aging (PubMed:32103178). Involved in modulating longevity, probably as a result of enhanced stress resistance via mechanisms related to dietary restriction and mitochondrial function (PubMed:32103178). {ECO:0000269|PubMed:32103178}.
|
Caenorhabditis elegans
|
O17695
|
HDA1_CAEEL
|
MNSNGPLMEHGKRRVAYYYDSNIGNYYYGQGHVMKPHRIRMTHHLVLNYGLYRNLEIFRPFPASFEDMTRFHSDEYMTFLKSANPDNLKSFNKQMLKFNVGEDCPLFDGLYEFCQLSSGGSLAAATKLNKQKVDIAINWMGGLHHAKKSEASGFCYTNDIVLGILELLKYHKRVLYVDIDVHHGDGVEEAFYTTDRVMTVSFHKYGDFFPGTGDLKDIGAGKGKLYSVNVPLRDGITDVSYQSIFKPIMTKVMERFDPCAVVLQCGADSLNGDRLGPFNLTLKGHGECARFFRSYNVPLMMVGGGGYTPRNVARCWTYETSIAVDKEVPNELPYNDYFEYFGPNYRLHIESSNAANENSSDMLAKLQTDVIANLEQLTFVPSVQMRPIPEDALSALNDDSLIADQANPDKRLPPQITDGMIQDDGDFYDGEREGDDRRNESDAKRAAQFESEGGEKRQKTE
|
3.5.1.98
| null |
cell differentiation [GO:0030154]; chromatin organization [GO:0006325]; determination of adult lifespan [GO:0008340]; embryo development ending in birth or egg hatching [GO:0009792]; embryonic digestive tract morphogenesis [GO:0048557]; gonad development [GO:0008406]; hermaphrodite somatic sex determination [GO:0042001]; mitochondrial unfolded protein response [GO:0034514]; negative regulation of Notch signaling pathway [GO:0045746]; negative regulation of Ras protein signal transduction [GO:0046580]; negative regulation of stress response to copper ion [GO:1903854]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of vulval development [GO:0040027]; nematode male tail tip morphogenesis [GO:0045138]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of cell differentiation [GO:0045595]; regulation of cell migration [GO:0030334]; regulation of innate immune response [GO:0045088]
|
chromatin [GO:0000785]; cytoplasm [GO:0005737]; germ cell nucleus [GO:0043073]; histone deacetylase complex [GO:0000118]; nucleus [GO:0005634]; NuRD complex [GO:0016581]
|
histone deacetylase activity [GO:0004407]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]
|
PF00850;
|
3.40.800.20;
|
Histone deacetylase family, HD type 1 subfamily
|
PTM: Sumoylated. {ECO:0000305|PubMed:15990876}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:32934238}. Cytoplasm. Chromosome {ECO:0000269|PubMed:32934238}. Note=Except in the germ line where it is also cytoplasmic.
|
CATALYTIC ACTIVITY: Reaction=H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-[histone]; Xref=Rhea:RHEA:58196, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:11338, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089, ChEBI:CHEBI:61930; EC=3.5.1.98;
| null | null | null | null |
FUNCTION: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression. Plays an important role in transcriptional regulation, cell cycle progression and developmental events (PubMed:25446273). Histone deacetylases act via the formation of large multiprotein complexes. Involved in the endoderm determination possibly by repressing end-1 expression. Also involved in vulval development, possibly by repressing lag-2 expression. Required during mitochondrial stress for the activation of genes involved in the mitochondrial unfolded protein response (mtUPR), in concert with homeobox protein dve-1 (PubMed:32934238). Promotes normal hermaphrodite (XX) development, in concert with zinc finger protein tra-4 and nasp-1, perhaps as components of a complex (PubMed:17011494). Plays a role in the regulation of longevity and mtUPR-associated innate immunity (PubMed:32934238). In association with akir-1, plays a role in regulating the transcription of antimicrobial peptide genes in response to fungal infection (PubMed:30036395). {ECO:0000269|PubMed:11742996, ECO:0000269|PubMed:11940660, ECO:0000269|PubMed:17011494, ECO:0000269|PubMed:25446273, ECO:0000269|PubMed:30036395, ECO:0000269|PubMed:32934238}.
|
Caenorhabditis elegans
|
O17736
|
ETC1_CAEEL
|
MIKSLNERDNFLNRLREMEHKREKDEKQEKAARKVQKFWRGHRVQHNQRLLFRAEFDAVSDRQRGLEETIKMAQLLVNFYETNKDEERLVMTLSELVKLKTSDKEFEKRIRETQRLLLARCCIKFLKNATENTIFFHIFRYLEDYVTCHSKLFEASSKLGLFNAEFHLLEALIGKPTGKTVERASLNPRILQLLTRIFETFVNPSRSTSVSVNVANRLLKTICVNITDLNFSNYILYYIKDHIKPTSPNFTNLFEAMKSVDILNNWKVRPEIAETASLRLQSIFVSQIVHVSNTQSEDVKQYFNSLAVFLEHHSKIMRSLNVKEDLSEFGRLRTSVNNHLKQYCEEMLISNEFRRAACIYANLPGVQVETIISLRKYFSQFLDLLAASNTFVEALYAFIARLCPNGEFDPIDAKSPKVNALELFCNCLNKRVSSVADSDFVPTDIFVDFDHTVEFLRDVSIKLIHLMFPTMARGDLYSGNLKEKMYKAETDWKDVTESVFSILGAIYQKDIRLKYFPEEFWTNHGREVLSGIGEHRRMPRRRMPNGRLQIERTMDTEFVERLAAIYEMDSDSENDDEDEDNNLPAVLRRAICVMKHIPFIVPFMDRVKLFTRLLNQDKEKHYTSTFGMGFNGPSVTVRRDQVYMDAFETFAPKMQGDKVNDLKSMVRVKMVNWAGMNESGIDGGGIFREFLSELLKTAFNVERGFFTFTESKLLYPNPTAPFLLGVDCLAHFQFIGRMIGKLIYERQLQEVRFAEFFIAQIFETDKNKDVDLQHMKSFDPIIFKHLKALQKMNNRELDELQLDFSVVTSDMGLVRNVNLKPNGSKFRVTVENVHEYVRLYVNYHLKQRIASMVDAVRKGISEIISIEWMRMFAPHELQIMIAGYEEVFTAKELRKFCELRFAAGTQDINYEEMFWDVIDKLSNDDKKALLKFVTGCSRAPVDGFKSIQPRMGVLVIPSSDDELPTSATCMNMLRIPKYSNRTKLEEKLRYAINSGAGFELA
|
2.3.2.26
| null |
meiotic cell cycle [GO:0051321]; positive regulation of metaphase/anaphase transition of meiotic cell cycle [GO:1902104]; protein polyubiquitination [GO:0000209]; regulation of metaphase/anaphase transition of meiosis II [GO:1905189]; ubiquitin-dependent protein catabolic process [GO:0006511]
| null |
ubiquitin protein ligase activity [GO:0061630]
|
PF00632;
|
3.30.2160.10;3.30.2410.10;3.90.1750.10;
| null | null | null |
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.26; Evidence={ECO:0000255, ECO:0000269|PubMed:23578927};
| null |
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:23578927}.
| null | null |
FUNCTION: E3 ubiquitin-protein ligase that accepts ubiquitin from E2 ubiquitin-conjugating enzymes, such as ubc-18, in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Ubiquitinates ify-1 and cyb-1 targeting them for degradation in post-meiotic embryos. {ECO:0000269|PubMed:23578927}.
|
Caenorhabditis elegans
|
O17754
|
CBPE_CAEEL
|
MLHAMRPVLLVAALLAVTAHAFLGFGSGSTHKDDAEWGHYHNQAQLEAKLGEINEKCPEITTLYEIGQSVEGRPLVVIQFSTTPGEHIPTKPEVKLIGNMHGNEPIGRELLLRFAETLCNGAINNDKEIVQLLNSTSIHILPSMNPDGFELALGTEPAQRQWLTGRSNINGVDLNRDFPDLDSIFYELQKIGVPKFDHLLSLFEDNVDRQPETIAVGQWTLSLPFVLSANFHEGDLVANYPFDAAIDENSQKTAYSASPDDGTFRWLAKSYADNHAHMSKNDHAPCDGTSQDAFARQGGITNGAKWYSVAGGMQDFNYLATNAMEITLELSCEKMPEGSQLPRFWEDNQKSIFEYVWKSHSGVKGMVVDAMTGEPIKRAVVWIRNGTETVPVKHPVTTWSEGDFYRVLPAGKYEIIVAAEGYDIAAKNVTVENKVRDSALVVNFALSPAADEPSENEQEQIAELVNEIARRR
|
3.4.17.10
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P00730}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P00730};
|
acetylcholine secretion, neurotransmission [GO:0014055]; cellular response to carbon dioxide [GO:0071244]; larval feeding behavior [GO:0030536]; negative regulation of nematode pharyngeal pumping [GO:1903745]; neuropeptide processing [GO:0061837]; peptide metabolic process [GO:0006518]; positive regulation of acetylcholine secretion, neurotransmission [GO:0014057]; positive regulation of defecation [GO:2000294]; positive regulation of digestive system process [GO:0060456]; positive regulation of locomotion involved in locomotory behavior [GO:0090326]; positive regulation of synaptic assembly at neuromuscular junction [GO:0045887]; protein processing [GO:0016485]; regulation of eating behavior [GO:1903998]; regulation of muscle contraction [GO:0006937]
|
axon [GO:0030424]; cytoplasmic vesicle [GO:0031410]; extracellular space [GO:0005615]; neuronal cell body [GO:0043025]; perikaryon [GO:0043204]; presynapse [GO:0098793]
|
carboxypeptidase activity [GO:0004180]; metallocarboxypeptidase activity [GO:0004181]; zinc ion binding [GO:0008270]
|
PF13620;PF00246;
|
2.60.40.1120;3.40.630.10;
|
Peptidase M14 family
| null |
SUBCELLULAR LOCATION: Cell projection, axon {ECO:0000269|PubMed:12657671}. Perikaryon {ECO:0000269|PubMed:12657671}. Cytoplasmic vesicle, secretory vesicle lumen {ECO:0000303|PubMed:12657671}. Note=Predominantly localizes to axons in the nerve ring. {ECO:0000269|PubMed:12657671}.
|
CATALYTIC ACTIVITY: Reaction=Release of C-terminal arginine or lysine residues from polypeptides.; EC=3.4.17.10; Evidence={ECO:0000303|PubMed:12657671, ECO:0000303|PubMed:17564681};
| null | null | null | null |
FUNCTION: During FMRFamide-like peptide (FaRPs or FLP) and neuropeptide-like protein (NLP) precursor processing, catalyzes the removal of Arg or Lys residues from the C-terminus following the initial endoprotease cleavage (PubMed:12657671, PubMed:17564681). By processing neuropeptides, modulates basal acetylcholine release at the ventral cord neuromuscular junctions (PubMed:12657671, PubMed:22275875). Involved in egg-laying, defecation and locomotion (PubMed:11813735, PubMed:17564681, PubMed:22275875). By processing FLP neuropeptides, regulates the turning step of male mating behavior (PubMed:17611271). Involved in reducing pharyngeal pumping in response to high CO(2) levels (PubMed:25101962). {ECO:0000269|PubMed:11813735, ECO:0000269|PubMed:12657671, ECO:0000269|PubMed:17564681, ECO:0000269|PubMed:17611271, ECO:0000269|PubMed:22275875, ECO:0000269|PubMed:25101962}.
|
Caenorhabditis elegans
|
O17798
|
FKPC1_CAEEL
|
MSNISWYRHCSVRLQLVTLALFLLLGSASLGSAHIDEEFEDDVTTTISSIASPMRRTYTNEWAVRIAGGKVEEANRLANKYGYTNLGPIIPGDEYYLFRDDRKKSRSSRKTRSLSANQLQHEEDVMWMEQQVAKRRVKRGYRRIRRHTDDNDIFEEDDDGTQISKSRNRKHPDPNDPLWTDMWYLNRGEHHSDSTTRMDHNVKEAWDLGYTGKGVVVTILDDGLERTHPDISPNYDERASYDVNDRDNDPMPRYEFSDENRHGTRCAGEVAAIFNNSLCIVGIAYNANIGGIRMLDGDVTDAVEAASVGHNADYIDIYSASWGPDDDGRTVDGPAKLTRSAFEKGITMGRKGKGSIFVWASGNGGKDADSCNCDGYTNSIYTLSISSATENGNIPWYSEACSSTLATTYSSGATGEKMILTTDLHHACTNMHTGTSASAPLAAGIVALALEANPNLTWRDLQHIVIRTAKPINLRAGDWTTNGVGRNVSHSFGYGLMDAGAMVKLAKIWKKVDEQHRCRQFYPSRYKNIPNGNRLQLQLYSDGCYGGADENKVSYVEHVQAIVTLKAPKRGDLQIYLTSPSGTKSTLLTKRARDTSRSGFTDWAFMTTHNWGEQAAGLWILEIDNDGWDDAELVKWELVLYGTDRETGDFGGQHASPLAVRSVQMEATSSGTQYSIFHVITLVILTFSQILY
|
3.4.21.-
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P09958}; Note=Binds 3 calcium ions per subunit. {ECO:0000250|UniProtKB:P09958};
|
dendrite morphogenesis [GO:0048813]; dendrite self-avoidance [GO:0070593]; gene expression [GO:0010467]; insulin processing [GO:0030070]; negative regulation of dauer entry [GO:1905910]; negative regulation of protein localization to cell surface [GO:2000009]; peptide hormone processing [GO:0016486]; positive regulation of dendrite development [GO:1900006]; positive regulation of dendrite extension [GO:1903861]; positive regulation of dendrite morphogenesis [GO:0050775]; positive regulation of synaptic assembly at neuromuscular junction [GO:0045887]; protein localization to endosome [GO:0036010]; regulation of dendrite extension [GO:1903859]; regulation of dendrite morphogenesis [GO:0048814]; regulation of neuron migration [GO:2001222]; zymogen activation [GO:0031638]
|
axon [GO:0030424]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; trans-Golgi network [GO:0005802]
|
metal ion binding [GO:0046872]; serine-type endopeptidase activity [GO:0004252]; signaling receptor binding [GO:0005102]
|
PF01483;PF00082;PF16470;
|
2.60.120.260;3.30.70.850;3.40.50.200;
|
Peptidase S8 family, Furin subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:26974341}; Single-pass type I membrane protein {ECO:0000305}. Perikaryon {ECO:0000269|PubMed:23932402}. Cell projection, axon {ECO:0000269|PubMed:23932402}. Note=In most neurons, localizes exclusively within the cell bodies, but in ventral cord neurons, localizes in both the neuronal cell bodies and processes. {ECO:0000269|PubMed:23932402}.
| null | null | null | null | null |
FUNCTION: Furin-like protease which cleaves proproteins at the RX(K/R)R consensus motif (PubMed:24671950). During neuronal development, regulates the formation and extension of dendrite branches and cellular positioning of various type of neurons (PubMed:23932402, PubMed:25232734, PubMed:26974341, PubMed:28846083). Together with chin-1 and cdc-42, plays a role in the development of the neuropil and is required for the guidance of axons from neurons, including SubL pioneer neurons and AIY interneurons, into the nerve ring (PubMed:28846083). Its role in axon guidance in glia and pioneer neurons may be through ensuring the fmi-1 protein is correctly localized to the nerve ring (PubMed:28846083). Promotes the formation, extension and self-avoidance of dendritic branches of PVD and FLP mechanosensory neurons (PubMed:23932402, PubMed:25232734, PubMed:26974341). In PVD neurons, regulates plasma membrane levels of branching receptor dma-1 by targeting it to late endosomes and thus promotes normal dendrite branching and dendrite self-avoidance (PubMed:26974341). Also controls dendrite extension in AIY and D-type motoneurons, dendrite branching in AQR sensory neurons and VC4/5 motoneurons, the normal number of dendritic branches in AVL neurons and the positioning of HSN and ALM/PLM neurons (PubMed:25232734). Dispensable for maintaining dendrite branching in adults (PubMed:25232734). Also regulates dauer-specific dendritic branching of IL2 neurons and dauer-specific nictation behavior (PubMed:23932402). Under adverse environmental conditions, may promote dauer formation by processing insulin-like proteins ins-1 and ins-18, two daf-2/InsR antagonists (PubMed:24671950). {ECO:0000269|PubMed:23932402, ECO:0000269|PubMed:24671950, ECO:0000269|PubMed:25232734, ECO:0000269|PubMed:26974341, ECO:0000269|PubMed:28846083}.
|
Caenorhabditis elegans
|
O17850
|
ATX3_CAEEL
|
MSKDDPINSIFFEHQEAALCAQHALNMLLQDALYKWQDLRDLAIQMDKMEQQILGNANPTPGRSENMNESGYFSIQVLEKALETFSLKLTNIENPAMVDYKNNPLTARAYICNLREHWFVLRKFGNQWFELNSVNRGPKLLSDTYVSMFLHQVSSEGYSIFVVQGVLPRSDADDLISLCPVVPPKVTPKKEQKLEKVMTKFFNTVGKRLGGGSGAPPDSQEEKDLAIAFAMSMETKDGSEVSRSSAEIDEENLRKAIELSQAPGPSEPAEIPLLTRSRSSTPPGASEPFSNAEQQRRDRQKFLERFEKKKEERNDEK
|
3.4.19.12
| null |
chemical synaptic transmission [GO:0007268]; proteolysis [GO:0006508]
|
cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleus [GO:0005634]; synapse [GO:0045202]
|
cysteine-type deubiquitinase activity [GO:0004843]
|
PF02099;PF02809;
|
3.90.70.40;1.10.287.10;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17234717, ECO:0000269|PubMed:21526185}. Nucleus {ECO:0000269|PubMed:17234717, ECO:0000269|PubMed:21526185}. Nucleus, nucleolus {ECO:0000269|PubMed:27669035}. Note=Localizes predominantly in the cytoplasm (PubMed:17234717). In the germline, following ionizing radiation-induced DNA damage, localizes to foci within nucleoli where it colocalizes with cdc-48.1 and/or cdc-48.2 and ufd-2, proteasome alpha subunit and ubiquitinated proteins (PubMed:27669035). {ECO:0000269|PubMed:17234717, ECO:0000269|PubMed:27669035}.
|
CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000269|PubMed:17234717, ECO:0000269|PubMed:21317884};
| null | null | null | null |
FUNCTION: Acts as a chain editing deubiquitinating enzyme that binds and cleaves 'Lys-48'-linked polyubiquitin chains, with a preference for chains containing four or more ubiquitin molecules thereby modulating protein degradation by the ubiquitin-proteasome pathway (PubMed:17234717, PubMed:19545544, PubMed:21317884). Probably by regulating the IGF-1-insulin-like pathway, regulates lifespan (PubMed:21317884). Regulates germline DNA double-strand-break repair and apoptosis in response to DNA damage by recruiting E4 ubiquitin-protein ligase ufd-2 to DNA repair foci (PubMed:27669035). Interacts with key regulators of transcription and represses transcription (By similarity). Acts as a histone-binding protein that regulates transcription (By similarity). {ECO:0000250|UniProtKB:P54252, ECO:0000269|PubMed:17234717, ECO:0000269|PubMed:19545544, ECO:0000269|PubMed:21317884, ECO:0000269|PubMed:27669035}.
|
Caenorhabditis elegans
|
O17894
|
HM35_CAEEL
|
MTDHPPIDTSSYFDCYQQHQLPLQYTFTSSSNSNTSNSSTSPSHISDQFSSSGGPPYELSSHILTPSSVIPTPSPSVASASISSPTIPAFGCTMSEYSMEQMEAISTSLFQARDGDRLVAFFKQLESLYGPNAVDHLRSEAIIVAYTYALYHSNEFETLFHLLSNRHFQQRHYNDLQDIWHHARYKESQLKRGKELNPVEKYRLRRKFPAPKTIWDGEEIVYSFKDSSRKFLKQFFRNVSEYPTQEQKREISRATGLKIVQISNWFKNRRQRDKSNNSAKCSPPSSSSSTNGGSDFLPIITPQSFNLAAAPFNMNMIYGTLRDSQSDNDQFTFNP
| null | null |
axon guidance [GO:0007411]; egg-laying behavior [GO:0018991]; locomotion [GO:0040011]; mesodermal cell migration [GO:0008078]; neuron migration [GO:0001764]; positive regulation of locomotion [GO:0040017]; regulation of cell migration [GO:0030334]; regulation of nematode male tail tip morphogenesis [GO:0110037]; regulation of transcription by RNA polymerase II [GO:0006357]
|
nucleus [GO:0005634]; transcription regulator complex [GO:0005667]
|
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF00046;PF16878;
|
1.10.10.60;
|
SIX/Sine oculis homeobox family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:15282156}.
| null | null | null | null | null |
FUNCTION: Probable transcription factor required for differentiation and migration of neuronal cells, such as RID and CAN neurons (PubMed:15282156, PubMed:2361334). Specifically, plays a role in the terminal differentiation of RID peptidergic neurons (PubMed:27855782). Also required for CAN neuron axon guidance (PubMed:15282156). {ECO:0000269|PubMed:15282156, ECO:0000269|PubMed:2361334, ECO:0000269|PubMed:27855782}.
|
Caenorhabditis elegans
|
O17966
|
TOP1_CAEEL
|
MSVVSNHHSNGNGNSTVYDTNGNDEIKKEVKDEPMASDSEVPFGELMKRDKKEKKQKKRKAESGSDEDDYKPEKRKSSAKNGKKKDVGSDSEDDYKPEKKKSKKNNKKKAQESSEDDDEESEGDVSEEDVKPQIHSDDELEEEDEAPTTDDEEEQKRKEKERRKKEKREKKERKEKKRLEKENRKIKEEDDEDSDDEDDEKAKKKKRKSKGAEKSKPSTSKKDAGGKKEPPKKKVKKEEDIEDIWEWWKEEKKPAGVKWNSLQHCGPLFAPPYIPLPSHVHFKYGGEKMKLTLETEEIAQFYAGVLDHEYSTKEAFNKNFMKDWRKVMTVEERERIHDLKKCDFRAIDAYQKEQREIRKAMTKEEKLKIKEEKEAEVKIYGIAIIDGHRQKVANFRIEPPGVFRGRGGHPKMGLIKKRIMPEDVIINCGKDTEIPKPPPGHKWKEVRHDNTVTWLCSWTESVLGQNKYIMLNPSSKIKGEKDFEKYETARRLKKKIGGIRERYTDDFKSKEMRVRQRATALYFIDKLALRAGNEKDVDEAADTVGCCSLRVEHIKLFDSAKLNEDDKKEKEFVVEFDFLGKDSIRYFNRVSVEKRVYKNLKIFMEGKAPSDDLFDRLDTATLNDHLRSLMDGLTVKVFRTYNASITLQEQLIKLTNPKDNVAAKILSYNRANRQVAILCNHQRAVSKGFDESMQKLEQKIKDKKKEVKEAEAALKSARGAEKEKAQKKYDRLKEQLKKLKISRTDKDENKQIALGTSKLNYIDPRITVAWCKKFEVPLEKVFTKTHREKFRWAIDMTNSSDEEYVF
|
5.6.2.1
| null |
chromosome segregation [GO:0007059]; DNA replication [GO:0006260]; DNA topological change [GO:0006265]
|
chromosome [GO:0005694]; nucleolus [GO:0005730]; nucleus [GO:0005634]; spindle pole centrosome [GO:0031616]
|
DNA binding [GO:0003677]; DNA topoisomerase type I (single strand cut, ATP-independent) activity [GO:0003917]
|
PF14370;PF01028;PF02919;
|
1.10.132.10;2.170.11.10;1.10.10.41;
|
Type IB topoisomerase family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P11387}. Nucleus, nucleolus {ECO:0000269|PubMed:16943775}. Chromosome {ECO:0000269|PubMed:16943775}. Note=Localizes around sperm chromatids. {ECO:0000269|PubMed:16943775}.
|
CATALYTIC ACTIVITY: Reaction=ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.; EC=5.6.2.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10130};
| null | null | null | null |
FUNCTION: Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 5'-OH DNA strand. The free DNA strand then rotates around the intact phosphodiester bond on the opposing strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 5'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone (By similarity). Required for normal spermatogenesis and oogenesis (PubMed:16943775). {ECO:0000250|UniProtKB:Q13472, ECO:0000269|PubMed:16943775}.
|
Caenorhabditis elegans
|
O17972
|
NPHP1_CAEEL
|
MSIFGSILSLQDAINRFPQFEYQINRLEKEQKDTEAASRASFRKHFVRQCQELHRQLDDHRNRIEKAKTDETYKKENALEQLDKLKQRLTALSPEKEQLSFSVSVDSQSEEEKPKMAAIGRRKSTMYNDDESEDSDNDSEIIETDVQLDDPLPSQPQPPQQQHQQPQPKPRQPITITKPLESKTLNERQELDEVISRLQNPSRGDSGEVMEPVVVRGNVFVAIDSWDAEAEGDLELIKGKKYRITQTRSDGWWTALDEYGQRGLVPKTYLQHVKEKPKNVPSKVSSRLGVRDSVIGISTTTDPSRREANRQASRVDDCLGKAYDNDTHLSLVCHMAPRLSTSNIGFHDLFWSHYKDQVYKRTVHISKIIRLVRFEKMPLIEHKALVRMALVDITNPKSTQIVSNVHTLVPRVKSSTWYFEKKESQTRSCIEFSDFVLRSNYRSPTVVLVVEASHLVKTQIGIEEKSLGHTYLRLIIDDKAVPSRTNVLYLDDEVMTKMKLPEASKRRVLVQVMDVPKDKVSYVDSLPDVIVFNALYLPFFHFYRRRAGTILIRDNRNPLSAEFISDPLLSVFPFVCDQHDIMDIMLKIWKTKKKVLAKKNEAEQTAEFFQTFLHTAFFIHGIRMISYDVKDDLTLSIRQQTMQRFVDALNKGLFKQFIADQQCKPINIIDYSLDLLGNHSID
| null | null |
determination of adult lifespan [GO:0008340]; neuronal signal transduction [GO:0023041]; non-motile cilium assembly [GO:1905515]; protein localization [GO:0008104]; protein localization involved in establishment of planar polarity [GO:0090251]; response to hermaphrodite contact [GO:0034606]; turning behavior involved in mating [GO:0034607]
|
ciliary basal body [GO:0036064]; ciliary base [GO:0097546]; ciliary transition zone [GO:0035869]; cilium [GO:0005929]; cytoplasm [GO:0005737]; non-motile cilium [GO:0097730]
| null |
PF00018;
|
2.30.30.40;
|
Nephrocystin-1 family
| null | null | null | null | null | null | null |
FUNCTION: Plays a role in the extension of dendrites from phasmid ciliated sensory neurons (PubMed:34115759). May be necessary for initial assembly of the cilium. {ECO:0000269|PubMed:15659564, ECO:0000269|PubMed:34115759}.
|
Caenorhabditis elegans
|
O18017
|
BLM_CAEEL
|
MIKNREIEVAPPRRTIQFGGYTFVEPDLNFKAPIFSCCGSIRDPSCEEREEEYIDNGHDEEPPVEVNRIQESTSFDEPVSSPPRYRPSENPGPSSSSYEPGHYSFNEYQQFPSRPQKRLVDPPIVDLDEEPPIVDLDDSFDNFHVGSTSEEVVSGDIAPEEEEEEGHDSFDDFESVPAQPPSKNTLASLQKSDSEIALNQQRHDMHGRFRGFLQDDSEEFSDEVGLLGADMNKELYDTLKSKFGFNQFRHRQKQCILSTLMGHDTFVLMPTGAGKSLCYQLPAVILPGVTVVVSPLRSLIEDQKMKMKELGIGCEALTADLGAPAQEKIYAELGSGNPSIKLLYVTPEKISASGRLNSVFFDLHRRGLLARFVIDEAHCVSQWGHDFRPDYTKLSSLREKYANPPVPIIALTATATPKIVTDARDHLKMQNSKLFISSFVRDNLKYDLIPKAARSLINVVEKMKQLYPGKSGIVYCLSRKECETVQMMLTKAGLSAEVYHAGLNDNLRVSVQRSWIANKFDVICATIAFGMGIDKPDVRFVIHYSLPKSIEGYYQETGRAGRDGMPSYCLMLYSYHDSIRLRRMIEEGNTTTGVRSMHLNNVLQVVAYCENVSVCRRKMLVEHFGEVYDEQSCRNSKTPCDICERQRKNAEAIRLFDVSTDALSILKCLPRMQKATLKYISELYRGALIKKSQEQAMRLGHTKLPFYSKGQGMSEQDALRFVRKLVIEGYIHERLYSVPNQAAAVFAYAELTEAGRDLANGKKTAKVYLHIVTCERKRKNAGLIELSNMNIVSEAQALKERHMVKHGDVFTRCLQDLTHLITAVAESSGLSGPYSIVSREGIEQIAALLPRTNSDLLRIDSMTQIKVTKYGRLIMELLATYWKQVDEREEEEMRNQLDKLKSGEIVMGGFATLQSDPGFPSVPYMKPLGGGGGCRGRGKKRAFSGFSSGRATKKPRATAPSARGKTSGRGGAKPATSLKRNMYPATSM
|
5.6.2.4
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P54132}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P54132};
|
chromosome organization [GO:0051276]; chromosome segregation [GO:0007059]; determination of adult lifespan [GO:0008340]; DNA damage checkpoint signaling [GO:0000077]; DNA unwinding involved in DNA replication [GO:0006268]; double-strand break repair via homologous recombination [GO:0000724]; G-quadruplex DNA unwinding [GO:0044806]; meiotic cell cycle [GO:0051321]; meiotic chromosome separation [GO:0051307]; meiotic DNA double-strand break processing involved in reciprocal meiotic recombination [GO:0010705]; mitotic cell cycle [GO:0000278]; negative regulation of apoptotic process [GO:0043066]; reciprocal meiotic recombination [GO:0007131]; resolution of DNA recombination intermediates [GO:0071139]; resolution of meiotic recombination intermediates [GO:0000712]; response to X-ray [GO:0010165]; telomere maintenance [GO:0000723]
|
chromosome [GO:0005694]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; replisome [GO:0030894]
|
3'-5' DNA helicase activity [GO:0043138]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent activity, acting on DNA [GO:0008094]; DNA binding [GO:0003677]; enzyme binding [GO:0019899]; four-way junction helicase activity [GO:0009378]; isomerase activity [GO:0016853]; metal ion binding [GO:0046872]
|
PF00270;PF00271;PF00570;PF16124;PF09382;
|
1.10.150.80;3.40.50.300;1.10.10.10;
|
Helicase family, RecQ subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27011106, ECO:0000269|PubMed:34252074}. Chromosome {ECO:0000269|PubMed:27011106}. Note=Localizes on chromosomes during pachytene in meiotic prophase I in oocytes. Co-localizes with rmh-1 at mid-pachytene and late-pachytene in meiotic prophase I (PubMed:27011106). Localization at nuclear foci is dependent on rmh-1 during meiotic recombination (PubMed:27011106). {ECO:0000269|PubMed:27011106, ECO:0000269|PubMed:34252074}.
|
CATALYTIC ACTIVITY: Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.; EC=5.6.2.4; Evidence={ECO:0000250|UniProtKB:P54132}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P54132};
| null | null | null | null |
FUNCTION: Component of the BTR double Holliday Junction dissolution complex, which is involved in homologous recombination during meiotic double strand break in the germline (Probable). Stabilizes and positively regulates the localization of the BTR double Holliday Junction dissolution complex component rmh-1 at nuclear foci during meiotic recombination (PubMed:27011106). Participates in DNA replication and repair (By similarity). Exhibits a magnesium-dependent ATP-dependent DNA-helicase activity that unwinds single- and double-stranded DNA in a 3'-5' direction (By similarity). Negatively regulates sister chromatid exchange (SCE) (PubMed:27010650). {ECO:0000250|UniProtKB:Q9DEY9, ECO:0000269|PubMed:27010650, ECO:0000269|PubMed:27011106, ECO:0000305|PubMed:34252074}.; FUNCTION: ATP-dependent DNA helicase that unwinds single- and double-stranded DNA in a 3'-5' direction. Participates in DNA replication and repair. Negatively regulates sister chromatid exchange (SCE) (PubMed:27010650). Stimulates DNA 4-way junction branch migration and DNA Holliday junction dissolution. Binds single-stranded DNA (ssDNA), forked duplex DNA and DNA Holliday junction. {ECO:0000250|UniProtKB:P54132, ECO:0000250|UniProtKB:Q9DEY9, ECO:0000269|PubMed:27010650}.
|
Caenorhabditis elegans
|
O18158
|
OGT1_CAEEL
|
MEKPNYFQSYNKVIGATGEQLAPGAVPPHPVLAPSIAPGGVAGVSAANMANIMQTPGFANLVQQAIRTQLENQAAQQLAVNQQFQLNGATAVQQQLLLTPQQSLAQPIALAPQPTVVLNGVSETLKKVTELAHRQFQSGNYVEAEKYCNLVFQSDPNNLPTLLLLSAINFQTKNLEKSMQYSMLAIKVNNQCAEAYSNLGNYYKEKGQLQDALENYKLAVKLKPEFIDAYINLAAALVSGGDLEQAVTAYFNALQINPDLYCVRSDLGNLLKAMGRLEEAKVCYLKAIETQPQFAVAWSNLGCVFNSQGEIWLAIHHFEKAVTLDPNFLDAYINLGNVLKEARIFDRAVSAYLRALNLSGNHAVVHGNLACVYYEQGLIDLAIDTYKKAIDLQPHFPDAYCNLANALKEKGSVVEAEQMYMKALELCPTHADSQNNLANIKREQGKIEDATRLYLKALEIYPEFAAAHSNLASILQQQGKLNDAILHYKEAIRIAPTFADAYSNMGNTLKEMGDSSAAIACYNRAIQINPAFADAHSNLASIHKDAGNMAEAIQSYSTALKLKPDFPDAYCNLAHCHQIICDWNDYDKRVRKLVQIVEDQLCKKRLPSVHPHHSMLYPLSHAARIAIAAKHASLCFDKVHVQMLGKTPLIHADRFSVQNGQRLRIGYVSSDFGNHPTSHLMQSIPGMHDRSRVEVFCYALSVNDGTNFRSKLMNESEHFVDLSQIPCNGKAAEKIAQDGIHILINMNGYTKGARNEIFALRPAPIQVMWLGYPSTSGATFMDYIITDAVTSPLRLANAFTEKLAYMPHTFFIGDHAQMLRHLTDKVVVKDKETTERDSCLIMNTANMDPILAKSEIKEQVLDTEVVSGPNKELVRAEMVLPVLEVPTEPIKQMIMTGQMTMNVMEDMNVQNGLGQSQMHHKAATGEEIPNSVLLTSRAQYQLPDDAIVFCNFNQLYKIDPSTLDMWIKILENVPKSILWLLRFPYQGEEHIRKYCVERGLDPSRIVFSNVAAKEEHVRRGQLADVCLDTPLCNGHTTGMDILWTGTPMVTMPLESLASRVATSQLYALGVPELVAKTRQEYVSIAVRLGTDADHLANMRAKVWMARTSSTLFDVKQYCHDMEDLLGQMWKRYESGMPIDHITNNTETPHGL
|
2.4.1.255
| null |
dauer larval development [GO:0040024]; energy reserve metabolic process [GO:0006112]; glycogen metabolic process [GO:0005977]; glycoprotein metabolic process [GO:0009100]; lipid storage [GO:0019915]; protein O-linked glycosylation [GO:0006493]; reproduction [GO:0000003]; response to temperature stimulus [GO:0009266]
|
nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]
|
protein O-acetylglucosaminyltransferase activity [GO:0097363]; protein serine/threonine phosphatase activity [GO:0004722]
|
PF13844;PF00515;PF13414;PF13431;PF13181;
|
3.30.720.150;3.40.50.11380;3.40.50.2000;1.25.40.10;
|
Glycosyltransferase 41 family, O-GlcNAc transferase subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9083068}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:9083068}.
|
CATALYTIC ACTIVITY: Reaction=L-seryl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-(N-acetyl-beta-D-glucosaminyl)-L-seryl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:48904, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:12251, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:90838; EC=2.4.1.255; Evidence={ECO:0000250|UniProtKB:O15294}; CATALYTIC ACTIVITY: Reaction=L-threonyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-(N-acetyl-beta-D-glucosaminyl)-L-threonyl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:48908, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:12252, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:90840; EC=2.4.1.255; Evidence={ECO:0000250|UniProtKB:O15294};
| null |
PATHWAY: Protein modification; protein glycosylation.
| null | null |
FUNCTION: Addition of nucleotide-activated sugars directly onto the polypeptide through O-glycosidic linkage with the hydroxyl of serine or threonine. {ECO:0000250|UniProtKB:O15294}.
|
Caenorhabditis elegans
|
O18178
|
2A51_CAEEL
|
MHGSGHSLTGAPHQIPPPRTQGAATGGQQLSATANQFVDKIDPFHNKRGTSRRLRINNSSRYNVDSAQELVQLALIKDTAANEQPALVIEKLVQCQHVFDFYDPVAQLKCKEIKRAALNELIDHITSTKGAIVETIYPAVIKMVAKNIFRVLPPSENCEFDPEEDEPTLEVSWPHLQLVYELFLRFLESPDFQASIGKKYIDQRFVLKLLDLFDSEDPRERDFLKTVLHRIYGKFLGLRAFIRKHINNMFLRFVYETDSFNGVGELLEILGSIINGFALPLKQEHKVFLVKVLLPLHKPKCLSLYHAQLAYCVVQFIEKDSSLTPQVFEALLKFWPRTCSSKEVMFLGEVEEILDIIEPEQFKKIIDPLFRQLAKCVSSPHFQVAERALYFWNNEYILSLIEDTSSLVMPIMFPALYRISKEHWNQTIVALVYNVLKTFMEMNGKLFDELTSTYKGERLREKQREKDRDAFWKKMEALELNPPAEGKEVTPSLFPEKLTDYLKKDGPNMTPLPVATAGGGDKSPSVVKKSSTGSETTTPAKK
| null | null |
dauer larval development [GO:0040024]; determination of adult lifespan [GO:0008340]; negative regulation of insulin receptor signaling pathway [GO:0046627]; P granule assembly [GO:1903863]; regulation of lipid storage [GO:0010883]; response to heat [GO:0009408]; signal transduction [GO:0007165]
|
cytosol [GO:0005829]; nucleus [GO:0005634]; protein phosphatase type 2A complex [GO:0000159]
|
protein kinase binding [GO:0019901]; protein phosphatase activator activity [GO:0072542]
|
PF01603;
|
1.25.10.10;
|
Phosphatase 2A regulatory subunit B56 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19249087}.
| null | null | null | null | null |
FUNCTION: Probable regulatory subunit of serine/threonine-protein phosphatase let-92 which negatively regulates the insulin receptor signaling cascade composed of daf-2, age-1, akt-1, akt-2 and sgk-1 by promoting the dephosphorylation of akt-1 on 'Thr-350' (PubMed:19249087). Negatively regulates several functions controlled by the insulin pathway including dauer formation, lifespan, fat storage and stress resistance (PubMed:19249087). Plays a role in the asymmetric segregation of the P granule components during embryonic cell divisions but does not play an essential role in specifying germ cell fate (PubMed:21127218). Within a PP2A phosphatase complex, acts redundantly with pptr-2, to dephosphorylate P granule components including meg-1 and meg-3 to promote the assembly and accumulation of zygotic P granules in the posterior cytoplasm during zygote polarization, and thus maintain P granule distribution and segregation in early stage embryos following meiosis (PubMed:25535836). In adults, required to promote germ cell proliferation and differentiation when exposed to thermic stress (PubMed:21127218). {ECO:0000269|PubMed:19249087, ECO:0000269|PubMed:21127218, ECO:0000269|PubMed:25535836}.
|
Caenorhabditis elegans
|
O18191
|
APC1_CAEEL
|
MRKYVLFFISGNNDSQIWATTPNTPRVIARGGLERNIHTRTLARMVNEDAPGTSTPAAQSRLQTTASPFHRTHLTQMCRRGDTNASLLRDFTRMIRDTPRNFSKNTQHGNDRDFGDLERDPDVDLLLSKVCLECVYVEPKEGAIPKANKIFISNFLSDMYINLVSVTGEVMKIIPIWKNAETTRKNLLEKGKHEPCVVDCVDAAFVMKSGITVVLGSDFTTAMFGGNERIAPIFIKEMSNQRVGRKFRLFSFAENRIFAVNEMRCIVVEIPETVTCKSATELMRTCFLHLDRDLSRKLLIKWRSVKRDVDTERLDLDRKEMIDVAIFMLDNVGVRVTNVVAQERADSPEGHGGKQMRPRMSDSEVLSMMRQFFEEMTFRPKSEVITEDGYKCHLSVELDPNGEGFVHTQDLLHAFHSQCEDWSINTMMHSILLELIPYAYLLAKVMNYRAFEEYYVQLFKHLLSQIAIEFKIPPEIHEKFVGAIHIPKPCWSLNNVIAHIICERTTPETMESIPKFISKSSVRLLTILAVGRKFIGMGTNIDMDCERWLGKDWKRRIGLSGDILKSFRRIMNGKSSNSAGRASQLIELFEIGSITIDFMVLAVKVLMLKFQTDAFAGAQSIEPKKCIYATADEMISIAHLRWKNDIRMHNVQLMLNSSRPILIATNILRKNEDDNMKELQDRFLTQTSYRTFSQPFGRAFLDFRTAVPSLLTSIYIPRLNVGGMIYPSRVTCDPPTTEIFKLCTEWGNFYNSLASALRIGSSETVRIDNEWIVMVSKNIKSTAVIGGMTLGFGLNGHLAPFNMYHAHQMLSTFDKFHSVALLIGLSASNFTTCDVQIHKILATYLSFLMGPTPLEIKLDFTIQTAAISGLGLLFADSGNMTIAKKLVNEIGRAPNRDEEPVTDRNAYKLSAGFSLGLIMLGKGNGSASTVIPFKQNIPPMSQRLIYMMNGMRRDKCVFLPQVAPPVVNDVPNLPFSNGGMMTSSQVANHVKESEYINIHQSAEPAAIALGMMFMKMNNEFIANALALPGTITELERLKPDSMYSRVLAQCLVMWDSIEPTHDFVKSLIPPVIREYATAALHFGVPIRRDEDGEEVHEAINDAEEKYWAEIVDKGTVSQTFLYAVSAACMAIALKFSSCGGPNEKNIVNTAFRIIEYYTKIVMPDGKSNKDMGSIRMCIYSGAYTRTSCLSMLITAMAILRVGTGDLEVMRYARLLRLCDKPESDWIATGKKHFEQMVAHQALGILMLGEGRYAFKKDDLSIALTIISTFPTIPQSVSDNSHYHQPLRFLWSMAVEPRLLVPFDIAESCVVEVDVTIVMKPKDGNEPIVYKEKAPYLLPPLEDLQSISIGGGNYQLVHISLQSEDQVKVMKDIMTIGQGRVMLKRYGVDSSEMKIKEATTLYDDTPSLMSMFNNEDTAVELDEYEIQCMMEKIDEGINLNSSDEYPNVQIELSCVRDVTERTTMDLAQLQKRSLKLLSESLDLWQDEVNVSNTINGLADAVQDMQI
| null | null |
anaphase-promoting complex-dependent catabolic process [GO:0031145]; asymmetric cell division [GO:0008356]; establishment of meiotic spindle localization [GO:0051295]; metaphase/anaphase transition of meiotic cell cycle [GO:0044785]; metaphase/anaphase transition of mitotic cell cycle [GO:0007091]; neurotransmitter transport [GO:0006836]; polarity specification of anterior/posterior axis [GO:0009949]; protein K11-linked ubiquitination [GO:0070979]; regulation of meiotic cell cycle [GO:0051445]; regulation of mitotic cell cycle [GO:0007346]
|
anaphase-promoting complex [GO:0005680]
|
molecular adaptor activity [GO:0060090]
| null |
1.25.10.10;
|
APC1 family
| null | null | null | null |
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000305}.
| null | null |
FUNCTION: Probable component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle (PubMed:11861581). The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins (PubMed:11861581). Developmental role in early embryogenesis and the metaphase to anaphase transition in oocyte and spermatocyte meiosis and mitosis in germ cells (PubMed:11134076, PubMed:11861581). Required for embryonic anterior-posterior axis formation (PubMed:11832245). Plays a role in regulating the abundance of glr-1 receptors in postmitotic neurons, which may in turn control animal locomotion (PubMed:15556870). Involved in regulating GABA neurotransmitter release at neuromuscular junctions in GABA motor neurons (PubMed:24321454). {ECO:0000269|PubMed:11134076, ECO:0000269|PubMed:11832245, ECO:0000269|PubMed:11861581, ECO:0000269|PubMed:15556870, ECO:0000269|PubMed:24321454}.
|
Caenorhabditis elegans
|
O18195
|
WASH1_CAEEL
|
MYHVPLIPRDAGREETIFRINQSLQKLLRVSDEIFDRVEHRITRIHGKAEAIDRRTEVLEKKLESLQESDKVITFTLPRQLPKLPEEPPTSTSLFRINIDTEHFPGSEELPAFRRADDHVLRPCEPIDFTYELNKPDKFFLTSQVLKEYEQKGWERYKKRLLGGLRELSRSPEHIAELFYAGTSIPAFEGVSGDFSKKALDADDDGGTSRSGRTTDELAQLRLHEQLLEDTALSSTLMQEDSLDDNHPLAFRINFNEKKKKTAKMVEMPDSLPNLKGHAHDFTLRDPEIDEDRLLDILPADDQIPEASEPTEAEADAPTTFILPPPPPPMKLDPSPQPAATPVEITEIPPIISPPAPPPPPPPPPPPPPPQTPSASSSVTFSPTKSVDGGRSDLMAAIRAAGGAGNAKLSRIAEKPKRKGKFDGILESSALLGASETPRNSAPAPDGGGGGGDLMSALSKALDARRKAINGKVEAQPPAKVSSTIPAPPNFDDEEWD
| null | null |
Arp2/3 complex-mediated actin nucleation [GO:0034314]; cytoplasmic sequestering of protein [GO:0051220]; determination of adult lifespan [GO:0008340]; endocytic recycling [GO:0032456]; exocytosis [GO:0006887]; regulation of gene expression [GO:0010468]; retrograde transport, endosome to Golgi [GO:0042147]
|
cytosol [GO:0005829]; early endosome [GO:0005769]; recycling endosome [GO:0055037]; WASH complex [GO:0071203]
|
actin binding [GO:0003779]; alpha-tubulin binding [GO:0043014]; gamma-tubulin binding [GO:0043015]
|
PF11945;
| null |
WASH1 family
| null | null | null | null | null | null | null |
FUNCTION: Acts as a component of the WASH core complex that functions as a nucleation-promoting factor (NPF) at the surface of endosomes, where it recruits and activates the Arp2/3 complex to induce actin polymerization, playing a key role in the fission of tubules that serve as transport intermediates during endosome sorting (By similarity). Acts as a component of the DHIC (ddl-1-containing hsf-1 inhibitory complex) which modulates lifespan by sequestering the heat shock transcription factor hsf-1 to negatively regulate its binding to DNA and its transcriptional activity (PubMed:22265419). {ECO:0000250|UniProtKB:A8K0Z3, ECO:0000269|PubMed:22265419}.
|
Caenorhabditis elegans
|
O18209
|
PMY13_CAEEL
|
MDDTEGNSSMDSIRNGQSSPLPQVTPRLPQIPMMMRETPLSTKRERQAITPRFRRPAPKMIKTMPPTRSIWSVRKESVPLLVTPQGPKPLESPKYDHTNAQSFFEQVFQIDEIIGRGSFGEVFAARCREDSQLYAVKVSLAPIRQHSISKYREAESHMIIPPHKNLVKFYRAWEETGRLYIQTELCDQSLLKYCTEKHALPEDEIWNIFVDLLQAVHHLHSNDMIHDDIKPENIFLTKDMICKLGDFGLVINLKNPNDVKSAEEGDSKYLAPEVLNGRPTKSSDIFSLGMTILEATTDLDVPSNGDSWHQIRNGQIPDRFFAGISTDLRSLIALMLDSDPRIRPTSRDLLDHPVIKKKLMKRGTYVKCISILNGFFYAFSAVLVWVMAFFSVLFHPIVRFHAAIKDRQSEICAQFVNNQQHTPIQTPETSKVYLESLTGVAVRQASQIVSPFDFSDDENPPNAQRRLFTGAVPCRLNFDNDQDDDEEQATCSSSNSSAIEPQLDEPESPPRMNDVIDKLGKRGTPRSARRNLTFNRHRQVAASVAPKSSLNHYNHHTGSGDGFSNNSLIPISDQERTEKYLRMRLTEQQLDWADQNNVIDEAPPPMSCPPRIRRSIRDLPRMPVLNFNVLDEPSNKPTVDHHTILEQSESPRRRLNRGAKPVPRNRMMSFGSSGDEV
|
2.7.11.1
| null |
embryo development ending in birth or egg hatching [GO:0009792]; meiotic cell cycle [GO:0051321]; meiotic nuclear membrane disassembly [GO:0051078]; negative regulation of G2/MI transition of meiotic cell cycle [GO:0110031]; negative regulation of meiotic cell cycle process involved in oocyte maturation [GO:1904145]; negative regulation of ovulation [GO:0060280]; nematode larval development [GO:0002119]; nematode male tail tip morphogenesis [GO:0045138]; oocyte maturation [GO:0001556]; oogenesis [GO:0048477]; phosphorylation [GO:0016310]; spermatogenesis [GO:0007283]
|
condensed chromosome [GO:0000793]; cytoplasm [GO:0005737]; extrinsic component of membrane [GO:0019898]; Golgi membrane [GO:0000139]; nuclear envelope [GO:0005635]; nucleus [GO:0005634]; perinuclear endoplasmic reticulum [GO:0097038]; plasma membrane [GO:0005886]
|
ATP binding [GO:0005524]; cyclin-dependent protein serine/threonine kinase inhibitor activity [GO:0004861]; metal ion binding [GO:0046872]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein tyrosine kinase activity [GO:0004713]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family, WEE1 subfamily
| null |
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:16466390}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
| null | null | null | null |
FUNCTION: Acts as a negative regulator of entry into mitosis (G2 to M transition) by phosphorylation of the CDK1 kinase during oocyte maturation (PubMed:16338136, PubMed:16421191, PubMed:16466390). Required for oocyte maturation, embryonic development, germline proliferation and initiation of meiosis during spermatogenesis (PubMed:11702779, PubMed:12397109, PubMed:27104746). Required for chromosome structure during mitosis and negative regulation of nuclear envelope breakdown (PubMed:16421191). {ECO:0000269|PubMed:11702779, ECO:0000269|PubMed:12397109, ECO:0000269|PubMed:16338136, ECO:0000269|PubMed:16421191, ECO:0000269|PubMed:16466390, ECO:0000269|PubMed:27104746}.
|
Caenorhabditis elegans
|
O18214
|
MAB3_CAEEL
|
MLTEDPVSEICEAKAVDELAEQEKNYYCQRCLNHGELKPRKGHKPDCRYLKCPCRECTMVEQRRQLNNLLSKKKIHCTPATQTRDGKRVRDPHCARCSAHGVLVPLRGHKRTMCQFVTCECTLCTLVEHRRNLMAAQIKLRRSQQKSRDGKEPKRNSRRKSKDMDMEMMVVTATDGQKIIGTSASPSPSSTTDTMSPSLSMSPPCSPSPLLAQYTLTLAAPIPIYPPIPMNQQLISLQQQQFLMSIIQNMAPSIGQQAPLLPGISAGSVSSAAILNEFWSMYLKNYGLQA
| null | null |
cell differentiation [GO:0030154]; negative regulation of transcription by RNA polymerase II [GO:0000122]; nematode male tail tip morphogenesis [GO:0045138]; positive regulation of nematode male tail tip morphogenesis [GO:0110039]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]; sex differentiation [GO:0007548]
|
nucleus [GO:0005634]
|
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]
|
PF00751;
|
4.10.1040.10;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00070}.
| null | null | null | null | null |
FUNCTION: Transcription factor which binds the DNA motif 5'-[CGA][TCA][TA]ACAATGT[AT][TGA]C-3', probably as a monomer (PubMed:9490411). Acts partially redundantly with the transcription factor dmd-3 to coordinate tail tip cell fusion and retraction and thereby regulate male tail tip morphogenesis (PubMed:18550714, PubMed:21408209). Promotes male-specific development of two tissues, the peripheral nervous system and the intestine (PubMed:9490411). In the peripheral nervous system, directs differentiation of sensory ray neuroblasts into peripheral sense organs (PubMed:9490411). In the intestine, causes repression of vitellogenin gene transcription (PubMed:9490411). {ECO:0000269|PubMed:18550714, ECO:0000269|PubMed:21408209, ECO:0000269|PubMed:9490411}.
|
Caenorhabditis elegans
|
O18276
|
GBRB_CAEEL
|
MRRSKTRRIFHVSITLLLVSTIFCQNGTKPHNNSTSDQMSSSWSNRSQTMYSNASSLLSDLLLDYDIRLRPGFGGDALLLTMDIIIASFDSISEVDMDYTLTMYLHQYWTDERLRWSNEIPIDEMTLSGEFSQNIWVPDTFLANDKHSYLHEVTERNKMLRINVDGKVAYGMRLTSTLSCSMNLRNFPLDSQNCTVEIESYGYTTSEVLMKWNYPLAVHGVEQADVPQFTITGFHTEDSIVSTATGSYQRLSLVFQLRRSVGYFIFQTYLPCVLIVMLSWVSFWINHEATSARVALGITTVLTMTTISTGVRQSLPRISYVKSIDIYLVMCFVFVFAALLEYAAVNYSYWGRERGKGGGGNEWPVNGANKEDRESAVNVQKWVPSGLMDGVPQPQDRRVEALEEAMSTSNTAAQNNNFESTSKPKKRSSSPIPPLCRAGNTISEESESPDYPRYSTTSLKGARPHASLNHKTHHLKGRSSARAKRRMTLARMNVSMKQSISGIGRRARKVIPTIRVRDVNLIDKYSRVVFPVCFIVFNLFYWSYYMMVPS
| null | null |
chemical synaptic transmission [GO:0007268]; chloride transmembrane transport [GO:1902476]; monoatomic ion transport [GO:0006811]; nervous system process [GO:0050877]; regulation of membrane potential [GO:0042391]; signal transduction [GO:0007165]
|
chloride channel complex [GO:0034707]; GABA-A receptor complex [GO:1902711]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; synapse [GO:0045202]; transmembrane transporter complex [GO:1902495]
|
chloride channel activity [GO:0005254]; extracellular ligand-gated monoatomic ion channel activity [GO:0005230]; GABA-A receptor activity [GO:0004890]; neurotransmitter receptor activity [GO:0030594]
|
PF02931;PF02932;
|
2.70.170.10;1.20.58.390;
|
Ligand-gated ion channel (TC 1.A.9) family, Gamma-aminobutyric acid receptor (TC 1.A.9.5) subfamily
| null |
SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: GABA, an inhibitory neurotransmitter, mediates neuronal inhibition by binding to the GABA receptor and opening an integral chloride channel. {ECO:0000250, ECO:0000269|PubMed:12421359}.
|
Caenorhabditis elegans
|
O18330
|
MRJP1_APIME
|
MTRLFMLVCLGIVCQGTTGNILRGESLNKSLPILHEWKFFDYDFGSDERRQDAILSGEYDYKNNYPSDIDQWHDKIFVTMLRYNGVPSSLNVISKKVGDGGPLLQPYPDWSFAKYDDCSGIVSASKLAIDKCDRLWVLDSGLVNNTQPMCSPKLLTFDLTTSQLLKQVEIPHDVAVNATTGKGRLSSLAVQSLDCNTNSDTMVYIADEKGEGLIVYHNSDDSFHRLTSNTFDYDPKFTKMTIDGESYTAQDGISGMALSPMTNNLYYSPVASTSLYYVNTEQFRTSDYQQNDIHYEGVQNILDTQSSAKVVSKSGVLFFGLVGDSALGCWNEHRTLERHNIRTVAQSDETLQMIASMKIKEALPHVPIFDRYINREYILVLSNKMQKMVNNDFNFDDVNFRIMNANVNELILNTRCENPDNDRTPFKISIHL
| null | null |
caste determination, influence by environmental factors [GO:0048650]; defense response to fungus [GO:0050832]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; killing of cells of another organism [GO:0031640]
|
extracellular region [GO:0005576]
| null |
PF03022;
|
2.120.10.30;
|
Major royal jelly protein family
|
PTM: Glycosylated. {ECO:0000269|PubMed:9395329}.; PTM: Jellein-2 is probably processed to yield jellein-1 and jellein-4.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15203237, ECO:0000269|PubMed:9395329}. Note=Royal jelly. {ECO:0000269|PubMed:9395329}.
| null | null | null | null | null |
FUNCTION: [Major royal jelly protein 1]: Induces the differentiation of honeybee larvae into queens through an Egfr-mediated signaling pathway. Promotes body size increase by activating p70 S6 kinase, stimulates ovary development by augmenting the titer of vitellogenin (Vg) and juvenile hormone, and reduces developmental time by increasing the activity of mitogen-activated protein kinase and inducing the 20-hydroxyecdysone protein (20E). Most abundant protein found in the royal jelly which is the food of the queen honey bee larva. The royal jelly determines the development of the young larvae and is responsible for the high reproductive ability of the honeybee queen. {ECO:0000269|PubMed:21516106}.; FUNCTION: [Jellein-1]: Has antibacterial activity against the Gram-positive bacteria S.aureus ATCC 6535, S.saprophyticus and B.subtilis CCT2471, and the Gram-negative bacteria E.coli CCT1371, E.cloacae ATCC 23355, K.pneumoniae ATCC 13883 and P.aeruginosa ATCC 27853, and antifungal activity against C.albicans. Lack cytolytic activity and does not induce rat peritoneal mast cell degranulation. {ECO:0000269|PubMed:15203237}.; FUNCTION: [Jellein-2]: Has antibacterial activity against the Gram-positive bacteria S.aureus ATCC 6535, S.saprophyticus and B.subtilis CCT2471, and the Gram-negative bacteria E.coli CCT1371, E.cloacae ATCC 23355, K.pneumoniae ATCC 13883 and P.aeruginosa ATCC 27853, and antifungal activity against C.albicans. Lack cytolytic activity and does not induce rat peritoneal mast cell degranulation. {ECO:0000269|PubMed:15203237}.; FUNCTION: [Jellein-4]: Lacks antibacterial and antifungal activity. Lacks cytolytic activity and does not induce rat peritoneal mast cell degranulation. {ECO:0000269|PubMed:15203237}.
|
Apis mellifera (Honeybee)
|
O18333
|
RAB2_DROME
|
MSYAYLFKYIIIGDTGVGKSCLLLQFTDKRFQPVHDLTIGVEFGARMITIDGKQIKLQIWDTAGQEAFRSITRSYYRGAAGALLVYDITRRETFNHLTTWLEDARQHSNSNMVIMLIGNKSDLDSRREVKKEEGEAFAREHGLVFMETSARTAANVEEAFINTAKEIYEKIQEGVFDINNEANGIKIGQQHSPTNPSLPGAGGAAGAANSGCC
|
3.6.5.2
| null |
autophagosome-lysosome fusion [GO:0061909]; endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; eye pigment granule organization [GO:0008057]; protein secretion [GO:0009306]; Rab protein signal transduction [GO:0032482]; regulation of glutamate receptor clustering [GO:0106104]; regulation of postsynapse organization [GO:0099175]; symbiont entry into host cell [GO:0046718]; T-tubule organization [GO:0033292]; vesicle fusion [GO:0006906]; vesicle-mediated transport [GO:0016192]
|
autolysosome membrane [GO:0120281]; autophagosome membrane [GO:0000421]; cytoplasmic vesicle [GO:0031410]; endoplasmic reticulum exit site [GO:0070971]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; neuronal cell body [GO:0043025]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; postsynapse of neuromuscular junction [GO:0098975]; presynaptic active zone [GO:0048786]; type II terminal bouton [GO:0061175]; vesicle [GO:0031982]
|
GTP binding [GO:0005525]; GTPase activity [GO:0003924]; magnesium ion binding [GO:0000287]
|
PF00071;
|
3.40.50.300;
|
Small GTPase superfamily, Rab family
| null |
SUBCELLULAR LOCATION: Vesicle {ECO:0000269|PubMed:33822845}. Cytoplasmic vesicle {ECO:0000269|PubMed:33822845}. Cell projection, axon {ECO:0000269|PubMed:33822845}. Presynapse {ECO:0000269|PubMed:33822845}. Presynaptic active zone {ECO:0000269|PubMed:33822845}. Golgi apparatus {ECO:0000269|PubMed:33822845}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:33822845}. Perikaryon {ECO:0000269|PubMed:33822845}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000269|PubMed:28063257}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Autolysosome membrane {ECO:0000269|PubMed:28483915}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Autophagosome localization is not dependent on Rab7, Syx17 or Vps39 (PubMed:28063257). Associated with autolysosomes in its active GTP-bound form (PubMed:28483915). {ECO:0000269|PubMed:28063257, ECO:0000269|PubMed:28483915}.
|
CATALYTIC ACTIVITY: [Ras-related protein Rab-2]: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000250|UniProtKB:P53994};
| null | null | null | null |
FUNCTION: May be involved in bidirectional endoplasmic reticulum (ER) to Golgi trafficking (PubMed:33822845). Together with Rab7 involved in promoting fusion of autophagosomes and endosomes with lysosomes, probably through recruitment of the HOPS tethering complex (PubMed:28063257, PubMed:28483915, PubMed:31194677, PubMed:33822845). Involved in biosynthetic transport to lysosomes (PubMed:28483915). In larval motor neurons, mediates the biogenesis of presynaptic cargo vesicles and their long-range axonal trafficking to synaptic termini (PubMed:33822845). Not involved in axonal trafficking of mitochondria (PubMed:33822845). During vesicle biogenesis, active zone proteins (including brp/Bruchpilot) and synaptic vesicle proteins (including VGlut) are sorted from the trans-Golgi in a Rab2-dependent manner via, at least, two independent routes (PubMed:33822845). Acts upstream of Arl8 during presynaptic precursor vesicle biogenesis (PubMed:33822845). Associated with lysosomal marker positive presynaptic cargo vesicles during anterograde and retrograde axonal trafficking, probably while in its GTP-bound active state (PubMed:33822845). Involved in the delivery of presynaptic cargos, but not presynapse assembly or active zone function at synaptic termini (PubMed:33822845). Required for autophagocytosis-dependent remodeling of myofibrils and transverse-tubules (T-tubules) during metamorphosis (PubMed:28063257). {ECO:0000269|PubMed:28063257, ECO:0000269|PubMed:28483915, ECO:0000269|PubMed:31194677, ECO:0000269|PubMed:33822845}.
|
Drosophila melanogaster (Fruit fly)
|
O18334
|
RAB6_DROME
|
MSSGDFGNPLRKFKLVFLGEQSVGKTSLITRFMYDSFDNTYQATIGIDFLSKTMYLEDRTVRLQLWDTAGQERFRSLIPSYIRDSTVAVVVYDITNTNSFHQTSKWIDDVRTERGSDVIIMLVGNKTDLSDKRQVSTEEGERKAKELNVMFIETSAKAGYNVKQLFRRVAAALPGMDSTENKPSEDMQEVVLKDSPNETKDPEGGCAC
| null | null |
axon guidance [GO:0007411]; compound eye morphogenesis [GO:0001745]; defense response to fungus [GO:0050832]; exocytosis [GO:0006887]; germarium-derived egg chamber formation [GO:0007293]; intra-Golgi vesicle-mediated transport [GO:0006891]; intracellular protein transport [GO:0006886]; oocyte microtubule cytoskeleton polarization [GO:0008103]; phototransduction [GO:0007602]; pole plasm oskar mRNA localization [GO:0045451]; protein targeting to Golgi apparatus [GO:0140450]; R7 cell development [GO:0045467]; Rab protein signal transduction [GO:0032482]; receptor recycling [GO:0001881]; regulation of postsynaptic membrane potential [GO:0060078]; retrograde transport, endosome to Golgi [GO:0042147]; retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum [GO:0006890]; vesicle-mediated transport [GO:0016192]
|
autophagosome [GO:0005776]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; endomembrane system [GO:0012505]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; lysosome [GO:0005764]; neuronal cell body [GO:0043025]; perikaryon [GO:0043204]; synapse [GO:0045202]
|
actin binding [GO:0003779]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]
|
PF00071;
|
3.40.50.300;
|
Small GTPase superfamily, Rab family
| null |
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:17827179, ECO:0000269|PubMed:21835342, ECO:0000269|PubMed:22000105}. Synapse {ECO:0000269|PubMed:17827179, ECO:0000269|PubMed:21835342, ECO:0000269|PubMed:22000105}. Perikaryon {ECO:0000269|PubMed:17827179, ECO:0000269|PubMed:21835342, ECO:0000269|PubMed:22000105}. Note=Colocalizes with Rich at the Golgi apparatus. During oogenesis, first accumulates transiently in a central position during stages 7-8, then is uniformly distributed at the beginning of stage 9 to end up juxtaposed to the entire oocyte cortex. {ECO:0000269|PubMed:17827179, ECO:0000269|PubMed:21835342, ECO:0000269|PubMed:22000105}.
| null | null | null | null | null |
FUNCTION: Protein transport (PubMed:17329360, PubMed:17827179, PubMed:18833296, PubMed:21835342, PubMed:22928698, PubMed:33704067, PubMed:9685396). Regulator of membrane traffic from the Golgi apparatus towards the endoplasmic reticulum (ER) (PubMed:21795785). Mediates membrane trafficking during egg chamber growth and organization, possibly upstream of exocyst component Sec5. Also during oogenesis, plays a role, together with BicD but independently of Sec5, in the polarization of the oocyte microtubule cytoskeleton, in the localization of oskar mRNA and in the anterodorsal secretion of grk. Required for anterograde opsin transport through the ER-Golgi complex. Plays a role, together with Rich, in regulating CadN transport in photoreceptor cells which is required for the formation of normal synaptic connections between axons from the inner photoreceptor cells in the eye and postsynaptic cells in the brain medulla layer M6 (PubMed:21835342). Necessary for proper development of bristle shafts of macrochaete and microchaete on the head, thorax and scutellum. Modulates Notch signaling (PubMed:10459009). As a key regulator of vesicular traffic, plays a critical role in the regulation of actin organization and is required for normal rates of phagocytic uptake during phagocytosis involved in defense against viral and fungal infection. {ECO:0000269|PubMed:10459009, ECO:0000269|PubMed:17329360, ECO:0000269|PubMed:17827179, ECO:0000269|PubMed:18833296, ECO:0000269|PubMed:21795785, ECO:0000269|PubMed:21835342, ECO:0000269|PubMed:22928698, ECO:0000269|PubMed:33704067, ECO:0000269|PubMed:9685396}.
|
Drosophila melanogaster (Fruit fly)
|
O18381
|
PAX6_DROME
|
MRNLPCLGTAGGSGLGGIAGKPSPTMEAVEASTASHRHSTSSYFATTYYHLTDDECHSGVNQLGGVFVGGRPLPDSTRQKIVELAHSGARPCDISRILQVSNGCVSKILGRYYETGSIRPRAIGGSKPRVATAEVVSKISQYKRECPSIFAWEIRDRLLQENVCTNDNIPSVSSINRVLRNLAAQKEQQSTGSGSSSTSAGNSISAKVSVSIGGNVSNVASGSRGTLSSSTDLMQTATPLNSSESGGASNSGEGSEQEAIYEKLRLLNTQHAAGPGPLEPARAAPLVGQSPNHLGTRSSHPQLVHGNHQALQQHQQQSWPPRHYSGSWYPTSLSEIPISSAPNIASVTAYASGPSLAHSLSPPNDIESLASIGHQRNCPVATEDIHLKKELDGHQSDETGSGEGENSNGGASNIGNTEDDQARLILKRKLQRNRTSFTNDQIDSLEKEFERTHYPDVFARERLAGKIGLPEARIQVWFSNRRAKWRREEKLRNQRRTPNSTGASATSSSTSATASLTDSPNSLSACSSLLSGSAGGPSVSTINGLSSPSTLSTNVNAPTLGAGIDSSESPTPIPHIRPSCTSDNDNGRQSEDCRRVCSPCPLGVGGHQNTHHIQSNGHAQGHALVPAISPRLNFNSGSFGAMYSNMHHTALSMSDSYGAVTPIPSFNHSAVGPLAPPSPIPQQGDLTPSSLYPCHMTLRPPPMAPAHHHIVPGDGGRPAGVGLGSGQSANLGASCSGSGYEVLSAYALPPPPMASSSAADSSFSAASSASANVTPHHTIAQESCPSPCSSASHFGVAHSSGFSSDPISPAVSSYAHMSYNYASSANTMTPSSASGTSAHVAPGKQQFFASCFYSPWV
| null | null |
adult walking behavior [GO:0007628]; brain development [GO:0007420]; brain morphogenesis [GO:0048854]; central complex development [GO:0048036]; compound eye development [GO:0048749]; compound eye morphogenesis [GO:0001745]; eye-antennal disc morphogenesis [GO:0007455]; glial cell migration [GO:0008347]; glucose homeostasis [GO:0042593]; mushroom body development [GO:0016319]; neuron differentiation [GO:0030182]; photoreceptor cell fate specification [GO:0043704]; positive regulation of cell growth [GO:0030307]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of multicellular organism growth [GO:0040018]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of insulin-like growth factor receptor signaling pathway [GO:0043567]; regulation of transcription by RNA polymerase II [GO:0006357]
|
nucleus [GO:0005634]
|
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; sequence-specific DNA binding [GO:0043565]
|
PF00046;PF00292;
|
1.10.10.60;1.10.10.10;
|
Paired homeobox family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|PROSITE-ProRule:PRU00381, ECO:0000269|PubMed:7914031}.
| null | null | null | null | null |
FUNCTION: Involved in eye morphogenesis. {ECO:0000269|PubMed:7914031}.
|
Drosophila melanogaster (Fruit fly)
|
O18388
|
IMB_DROME
|
MTSDIAMQLIAILEKTVSPDKNELLSAKNFLEQAAASNLPEFLKALSEILVNTANSAVARMAAGLQLKNHLTSKDEKVSQQYQDRWHQFPSEIRELIKNNILAALGTENTRPSCAAQCVAYVAVIELPINRWPMLIQTLVNKVVSEGSSEMHRESALEAIGYICQDIRFGVMENQSNDVLTAIIHGMRKVEPSNHVRLAATTALHNSLEFTKSNFEKDMERNFIMEVVCEATQCQDSQICVAALQCLVKIMTLYYQYMEPYMAQALFPITLAAMKSDNDAVALQGIEFWSNVCDEEIDLAIESQEATDQGRAPQRVSKHYARGALQFLTPVLVEKLTKQDECDDEDTWSPAKAASVCLMVLATCCEDEIVPHVLPFIKENIESPNWRFRDAAVMTFGSVLNGLETNTLKPLVEQAMPTLIRLMYDSSVIVRDTIAWTFGRICDIIPEAAINETYLQTLLECFVKSLKSEPRVAANVCWAFIGLSDAAWEAAVTNDGETPETYALSPYFEYIITQLLETTDRSDGAQANLRCAAYQALMDMIKNSPLDCYLVVQRTTLVILERLNQVMQMETQINNHSDRHQFNDLQSLLCATLQSVLRKVHEQDAPQISDAIMTALLTMFNSSAGKSGVVQEEAFLAVSTLVELLGAQFAKYMPAFKDFLVMGLKNFQEYQVCCAAVGLTGDIFRALKDLMVPYSNEIMTVLINNLTEPTIHRTVKPQVLSAFGDIALSIGNHFLPYLSMVLDMLRVASNLQTDANNFDMNEYINELRESILEAYTGIIQGLKGVDQTAHTDVMHMEPHLMHIISFIKRIAQEGDVSDSMLASAAGFIGDLCTSFGPRLYPLLDDAIITQFLAEGKRSKAQRTKMLCTWAVKEIKKINTQVITQ
| null | null |
chorion-containing eggshell formation [GO:0007304]; mitotic cell cycle [GO:0000278]; NLS-bearing protein import into nucleus [GO:0006607]; protein import into nucleus [GO:0006606]; regulation of nucleocytoplasmic transport [GO:0046822]
|
cytoplasm [GO:0005737]; nuclear envelope [GO:0005635]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; P granule [GO:0043186]
|
nuclear import signal receptor activity [GO:0061608]; nuclear localization sequence binding [GO:0008139]; small GTPase binding [GO:0031267]
|
PF13513;PF03810;
|
1.25.10.10;
|
Importin beta family, Importin beta-1 subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11102382}. Note=In cleavage embryos.
| null | null | null | null | null |
FUNCTION: Required for nuclear protein import and mediates docking of import substrate to distinct nucleoporins (PubMed:11102382). In Drosophila, may not function as a snRNP import receptor as it does not interact with components of the snRNP complex such as snRNP U1, U2, U4/U6 and Snup (PubMed:23885126). {ECO:0000269|PubMed:11102382, ECO:0000269|PubMed:23885126}.
|
Drosophila melanogaster (Fruit fly)
|
O18404
|
HCD2_DROME
|
MIKNAVSLVTGGASGLGRATAERLAKQGASVILADLPSSKGNEVAKELGDKVVFVPVDVTSEKDVSAALQTAKDKFGRLDLTVNCAGTATAVKTFNFNKNVAHRLEDFQRVININTVGTFNVIRLSAGLMGANEPNQDGQRGVIVNTASVAAFDGQIGQAAYSASKAAVVGMTLPIARDLSTQGIRICTIAPGLFNTPMLAALPEKVRTFLAKSIPFPQRLGEPSEYAHLVQAIYENPLLNGEVIRIDGALRMMP
|
1.1.1.-; 1.1.1.35; 1.1.1.51; 1.1.1.53; 1.1.1.62
| null |
acyl-CoA metabolic process [GO:0006637]; androgen metabolic process [GO:0008209]; ecdysone metabolic process [GO:0008205]; estrogen metabolic process [GO:0008210]; fatty acid metabolic process [GO:0006631]; mitochondrial tRNA processing [GO:0090646]; steroid catabolic process [GO:0006706]; steroid metabolic process [GO:0008202]
|
cytosol [GO:0005829]; mitochondrial ribonuclease P complex [GO:0030678]; mitochondrion [GO:0005739]
|
3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity [GO:0047015]; 3-hydroxyacyl-CoA dehydrogenase activity [GO:0003857]; 7-beta-hydroxysteroid dehydrogenase (NADP+) activity [GO:0047022]; acetoacetyl-CoA reductase activity [GO:0018454]; dihydrotestosterone 17-beta-dehydrogenase activity [GO:0035410]; estradiol 17-beta-dehydrogenase [NAD(P)] activity [GO:0004303]; isoursodeoxycholate 7-beta-dehydrogenase (NAD+) activity [GO:0106282]; steroid dehydrogenase activity [GO:0016229]; testosterone dehydrogenase (NAD+) activity [GO:0047035]; ursodeoxycholate 7-beta-dehydrogenase (NAD+) activity [GO:0106283]
|
PF00106;
|
3.40.50.720;
|
Short-chain dehydrogenases/reductases (SDR) family
| null |
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:27131785, ECO:0000269|PubMed:34199774}. Note=Localizes to the lipid droplet fraction in early embryos (PubMed:16979555). {ECO:0000269|PubMed:16979555}.
|
CATALYTIC ACTIVITY: Reaction=a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:22432, ChEBI:CHEBI:15378, ChEBI:CHEBI:57318, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726; EC=1.1.1.35; Evidence={ECO:0000269|PubMed:12917011}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22433; Evidence={ECO:0000269|PubMed:12917011}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:22434; Evidence={ECO:0000269|PubMed:12917011}; CATALYTIC ACTIVITY: Reaction=(3S)-3-hydroxybutanoyl-CoA + NAD(+) = acetoacetyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:30799, ChEBI:CHEBI:15378, ChEBI:CHEBI:57286, ChEBI:CHEBI:57316, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000269|PubMed:12917011}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30800; Evidence={ECO:0000269|PubMed:12917011}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:30801; Evidence={ECO:0000269|PubMed:12917011}; CATALYTIC ACTIVITY: Reaction=NAD(+) + testosterone = androst-4-ene-3,17-dione + H(+) + NADH; Xref=Rhea:RHEA:14929, ChEBI:CHEBI:15378, ChEBI:CHEBI:16422, ChEBI:CHEBI:17347, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.51; Evidence={ECO:0000269|PubMed:12917011}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14930; Evidence={ECO:0000269|PubMed:12917011}; CATALYTIC ACTIVITY: Reaction=5alpha-androstane-3alpha,17beta-diol + NAD(+) = 17beta-hydroxy-5alpha-androstan-3-one + H(+) + NADH; Xref=Rhea:RHEA:42004, ChEBI:CHEBI:15378, ChEBI:CHEBI:16330, ChEBI:CHEBI:36713, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.53; Evidence={ECO:0000269|PubMed:12917011}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:42006; Evidence={ECO:0000269|PubMed:12917011}; CATALYTIC ACTIVITY: Reaction=17beta-estradiol + NAD(+) = estrone + H(+) + NADH; Xref=Rhea:RHEA:24612, ChEBI:CHEBI:15378, ChEBI:CHEBI:16469, ChEBI:CHEBI:17263, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.62; Evidence={ECO:0000269|PubMed:12917011}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24613; Evidence={ECO:0000269|PubMed:12917011}; CATALYTIC ACTIVITY: Reaction=NAD(+) + ursodeoxycholate = 7-oxolithocholate + H(+) + NADH; Xref=Rhea:RHEA:42028, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78604, ChEBI:CHEBI:78605; Evidence={ECO:0000269|PubMed:12917011}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42029; Evidence={ECO:0000269|PubMed:12917011}; CATALYTIC ACTIVITY: Reaction=3beta,7beta-dihydroxy-5beta-cholan-24-oate + NAD(+) = 3beta-hydroxy-7-oxo-5beta-cholan-24-oate + H(+) + NADH; Xref=Rhea:RHEA:42024, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78602, ChEBI:CHEBI:78603; Evidence={ECO:0000269|PubMed:12917011}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42025; Evidence={ECO:0000269|PubMed:12917011}; CATALYTIC ACTIVITY: Reaction=11-dehydrocorticosterone + NAD(+) = H(+) + NADH + pregn-4-ene-3,11,20,21-tetraone; Xref=Rhea:RHEA:42020, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78600, ChEBI:CHEBI:78601; Evidence={ECO:0000269|PubMed:12917011}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42021; Evidence={ECO:0000269|PubMed:12917011}; CATALYTIC ACTIVITY: Reaction=cortisone + NAD(+) = 17alpha-hydroxypregn-4-en-3,11,20-trione-21-al + H(+) + NADH; Xref=Rhea:RHEA:42016, ChEBI:CHEBI:15378, ChEBI:CHEBI:16962, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78596; Evidence={ECO:0000269|PubMed:12917011}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42017; Evidence={ECO:0000269|PubMed:12917011}; CATALYTIC ACTIVITY: Reaction=cortisol + NAD(+) = 11beta,17alpha-dihydroxypregn-4-ene-3,20,21-trione + H(+) + NADH; Xref=Rhea:RHEA:42012, ChEBI:CHEBI:15378, ChEBI:CHEBI:17650, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78595; Evidence={ECO:0000269|PubMed:12917011}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42013; Evidence={ECO:0000269|PubMed:12917011}; CATALYTIC ACTIVITY: Reaction=5alpha-pregnan-20beta-ol-3-one + NAD(+) = 5alpha-pregnane-3,20-dione + H(+) + NADH; Xref=Rhea:RHEA:42008, ChEBI:CHEBI:15378, ChEBI:CHEBI:28952, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:78594; Evidence={ECO:0000269|PubMed:12917011}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42009; Evidence={ECO:0000269|PubMed:12917011}; CATALYTIC ACTIVITY: Reaction=17beta-hydroxy-5alpha-androstan-3-one + NAD(+) = 5alpha-androstan-3,17-dione + H(+) + NADH; Xref=Rhea:RHEA:41992, ChEBI:CHEBI:15378, ChEBI:CHEBI:15994, ChEBI:CHEBI:16330, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000269|PubMed:12917011}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41993; Evidence={ECO:0000269|PubMed:12917011};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=33.7 uM for acetoacetyl-CoA (in the presence of 0.2 mM NADH, at pH 6.4 and 25 degrees Celsius) {ECO:0000269|PubMed:12917011}; KM=101 uM for (3S)-3-hydroxybutanoyl-CoA (beta-hydroxybutyryl-CoA) (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius) {ECO:0000269|PubMed:12917011}; KM=37.3 uM for androsterone (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius) {ECO:0000269|PubMed:12917011}; KM=12.3 uM for 17beta-hydroxy-5alpha-androstan-3-one (5-alpha-dihydrotestosterone) (in the presence of 0.2 mM NADH, at pH 6.4 and 25 degrees Celsius) {ECO:0000269|PubMed:12917011}; KM=11.1 uM for 17-beta-estradiol (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius) {ECO:0000269|PubMed:12917011}; KM=9 uM for 5alpha-pregnan-20beta-ol-3-one (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius) {ECO:0000269|PubMed:12917011}; KM=3 uM for 3beta,7beta-dihydroxy-5beta-cholan-24-oate (also known as isoursodeoxycholate or 7beta-hydroxyisolithocholate) (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius) {ECO:0000269|PubMed:12917011}; KM=32.5 uM for NADH (in the presence of acetoacetyl-CoA, at pH 7.0 and 25 degrees Celsius) {ECO:0000269|PubMed:12917011}; KM=64.4 uM for NAD (in the presence of (3S)-3-hydroxybutanoyl-CoA, at pH 9.3 and 25 degrees Celsius) {ECO:0000269|PubMed:12917011}; KM=124 uM for NAD (in the presence of aldosterone, at pH 9.3 and 25 degrees Celsius) {ECO:0000269|PubMed:12917011};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.3 for the dehydrogenase reaction, and 6.4 for the reductase reaction. {ECO:0000269|PubMed:12917011};
| null |
FUNCTION: Mitochondrial dehydrogenase involved in pathways of fatty acid, and steroid metabolism (PubMed:12917011). Versatile enzyme presenting two types of activity; L-3-hydroxyacyl-CoA dehydrogenase ((3S)-3-hydroxyacyl-CoA dehydrogenase) activity and hydroxysteroid dehydrogenase (HSD) activity with a wide substrate spectrum. As a (3S)-3-hydroxyacyl-CoA dehydrogenase, it functions in the third step of the fatty acid beta-oxidation pathway, a major metabolic process in which fatty acids are oxidized to provide a significant source of energy, while also generating acyl-CoA metabolites used by many metabolic routes (Probable) (PubMed:12917011). As a HSD, it functions in the degradation pathways of glucocorticoids and sex steroids and epimerization of bile acids; catalyzes the beta-oxidation at position 17 of androgens and estrogens, has 3-alpha-hydroxysteroid dehydrogenase activity with androsterone, and carries out oxidative conversions of 7-beta-hydroxylated bile acids like ursodeoxycholate or isoursodeoxycholate (also known as 3-beta,7-beta-dihydroxy-5-beta-cholan-24-oate or 7-beta-hydroxyisolithocholate, respectively). Also exhibits 20-beta-OH and 21-OH dehydrogenase activities with C21 steroids (PubMed:12917011). Essential for structural and functional integrity of mitochondria (PubMed:27131785, PubMed:34199774, PubMed:35663400). Required for cell survival during embryonic development (PubMed:9585418). May play a role in germline formation (PubMed:12917011, PubMed:9585418). {ECO:0000269|PubMed:12917011, ECO:0000269|PubMed:27131785, ECO:0000269|PubMed:34199774, ECO:0000269|PubMed:35663400, ECO:0000269|PubMed:9585418, ECO:0000305|PubMed:9585418}.; FUNCTION: In addition to mitochondrial dehydrogenase activity, moonlights as a component of mitochondrial ribonuclease P, a complex that cleaves tRNA molecules in their 5'-ends (PubMed:27131785, PubMed:34199774, PubMed:35663400). Essential for the structural and functional integrity of mitochondria (PubMed:27131785, PubMed:34199774, PubMed:35663400). Function is essential for pupal development (PubMed:27131785, PubMed:34199774). {ECO:0000269|PubMed:27131785, ECO:0000269|PubMed:34199774, ECO:0000269|PubMed:35663400}.
|
Drosophila melanogaster (Fruit fly)
|
O18412
|
FZO_DROME
|
MAESDSGESTSSVSSFISSSSSSRLSEFVDAKTELQDIYHDLSNYLSNFLTILEETVLLKDRQMLEHLCAFSSRVEAIAKVLSRDRMKVAFFGRTSNGKSAVINALLHEKILPSAMGHTTSCFCQVQANGSNETEHVKVEQEDEHMELSALSQLASAHSPGALKPSTLLQVNMAKNRCSILDYDVVLMDTPGVDVTAQLDDCLDSYCMDADVFILVLNAESTVSRVERQFFKDVASKLSRPNLFILNNRWDKASSLEPEMEQKVKDQHMERCVNLLVDELGVYSTAQEAWERIYHVSALEALHIRNGQITNPSGQTQQRYQEFLRFENDFSNCLAVSALKTKFGPHLLSAQKILNQLKSTLICPFIEKVSRLIDENKERRANLNAEIEDWLILMQEDREALQYCFEELTEMTQRVGRCVLNDQIKTLIPSSVLSFSQPFHPEFPAQIGQYQRSLCAHLDKLLEDRVLQCLSIPLQRKILDIEKEIGLPIAENSCDWQLIYGLDCQSYMSDFQPDLRFRFSLGFTALWHRLEGNLPLHASPFRIQKLQNGHKKCSPLPPLVNGNHWQMLESLVKSKGSLGTVLLSAMAIRSFNWPIVLILGGLVGSFYIYEYAAWTTAAQERSFKSQYARLLQQRLRSDVQQTVSGFELQLRQHLATVRNCWEAQSNETLNDLNVRTAELTKQIQSMEVLQLSLKKFRDKGQLLASRLGDFQETYLTKS
|
3.6.5.-
| null |
mitochondrial fusion [GO:0008053]; mitochondrion localization [GO:0051646]; Nebenkern assembly [GO:0007287]; positive regulation of mitochondrial fusion [GO:0010636]; sperm mitochondrion organization [GO:0030382]; spermatogenesis [GO:0007283]
|
membrane [GO:0016020]; mitochondrial envelope [GO:0005740]; mitochondrial outer membrane [GO:0005741]
|
GTP binding [GO:0005525]; GTPase activity [GO:0003924]
|
PF00350;PF04799;
|
1.20.5.110;3.40.50.300;
|
TRAFAC class dynamin-like GTPase superfamily, Dynamin/Fzo/YdjA family, Mitofusin subfamily
| null |
SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:9230308}; Multi-pass membrane protein {ECO:0000269|PubMed:9230308}.
|
CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:Q8IWA4};
| null | null | null | null |
FUNCTION: Essential transmembrane GTPase, which mediates mitochondrial fusion during spermatogenesis (PubMed:18799731, PubMed:9230308). In early spermatocytes, fusion of mitochondria give rise to two organelles named Nebenkern and constitutes an important step in mitochondria morphology, which is balanced between fusion and fission (PubMed:18799731, PubMed:9230308). Essential for fertility (PubMed:9230308). {ECO:0000269|PubMed:18799731, ECO:0000269|PubMed:9230308}.
|
Drosophila melanogaster (Fruit fly)
|
O18413
|
PRS8_DROME
|
MTVTNRMEIESAYHKGEGFRSYYIQKIEELQLVVAEKHQNLRRLQAQRNELNAKVRMLREELQLLQEQGSYVGEVVKPMDKKKVLVKVHPEGKFVVDLDKNIDINDVTPNCRVALRNESYTLHKILPNKVDPLVSLMMVEKVPDSTYEMVGGLDKQIKEIKEVIELPVKHPELFDALGIAQPKGVLLYGPPGTGKTLLARAVAHHTECTFIRVSGSELVQKFIGEGSRMVRELFVMAREHAPSIIFMDEIDSIGSSRIESGSGGDSEVQRTMLELLNQLDGFEATKNIKVIMATNRIDILDPALLRPGRIDRKIEFPPPNEEARLDILKIHSRKMNLTRGINLRKIAELMPGASGAEVKGVCTEAGMYALRERRVHVTQEDFEMAVAKVMQKDSEKNMSIKKLWK
| null | null |
proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; proteasome regulatory particle [GO:0005838]; proteasome regulatory particle, base subcomplex [GO:0008540]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; proteasome-activating activity [GO:0036402]
|
PF00004;PF17862;PF16450;
|
1.10.8.60;2.40.50.140;3.40.50.300;
|
AAA ATPase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: The 26S proteasome is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex (By similarity). {ECO:0000250}.
|
Drosophila melanogaster (Fruit fly)
|
O18423
|
TXL_EISFE
|
MSAKAAEGYEQIEVDVVAVWKEGYVYENRGSTSVDQKITITKGMKNVNSETRTVTATHSIGSTISTGDAFEIGSVEVSYSHSHEESQVSMTETEVYESKVIEHTITIPPTSKFTRWQLNADVGGADIEYMYLIDEVTPIGGTQSIPQVITSRAKIIVGRQIILGKTEIRIKHAERKEYMTVVSRKSWPAATLGHSKLFKFVLYEDWGGFRIKTLNTMYSGYEYAYSSDQGGIYFDQGTDNPKQRWAINKSLPLRHGDVVTFMNKYFTRSGLCYDDGPATNVYCLDKREDKWILEVVG
| null | null |
defense response to bacterium [GO:0042742]; killing of cells of another organism [GO:0031640]; monoatomic ion transport [GO:0006811]
|
extracellular region [GO:0005576]; membrane [GO:0016020]; other organism cell membrane [GO:0044218]
|
toxin activity [GO:0090729]
| null |
2.60.120.980;2.80.10.50;
|
Lysenin family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9210594}. Target cell membrane {ECO:0000269|PubMed:9210594}. Note=Forms a beta-barrel pore in the membrane. {ECO:0000269|PubMed:27048994, ECO:0000269|PubMed:27176125}.
| null | null | null | null | null |
FUNCTION: Pore-forming toxin that defensively acts against parasitic microorganisms by forming pores in sphingomyelin-containing membranes (PubMed:12676961, PubMed:9478988). Has hemolytic activity and is also cytotoxic to spermatozoa of some species of invertebrates and many species of vertebrates and to amphibian larvae, guinea pig polymorphonuclear leukocytes, chicken fibroblasts, normal spleen cells and various tumor cells (PubMed:10684578). Is lethal for various species of reptiles, amphibian, birds and mammals. Induces smooth muscle contraction (PubMed:9210594). It binds sphingomyelin and induces hemolysis in the same manner as lysenin-related protein 2, and is 10-fold more effective than lysenin-related protein 1 (PubMed:15274631). {ECO:0000269|PubMed:10684578, ECO:0000269|PubMed:12676961, ECO:0000269|PubMed:15274631, ECO:0000269|PubMed:16971770, ECO:0000269|PubMed:9210594, ECO:0000269|PubMed:9478988}.
|
Eisenia fetida (Red wiggler worm)
|
O18475
|
DPOLQ_DROME
|
MAFSQSFNFGNSTLMALEKGMQADDKENAQPGNGNIQVQSAGNEVNSEIQEINSEFFRDEFSYEVNQAHKPAEQSVVNVSQVQQHMAVVSNQDSEDQSRSSALNDQICTQSSFEGEDAGADAVLDQPNLDENSFLCPAQDEEASEQLKEDILHSHSVLAKQEFYQEISQVTQNLSSMSPNQLRVSPNSSRIREAMPERPAMPLDLNTLRSISAWNLPMSIQAEYKKKGVVDMFDWQVECLSKPRLLFEHCNLVYSAPTSAGKTLVSEILMLKTVLERGKKVLLILPFISVVREKMFYMQDLLTPAGYRVEGFYGGYTPPGGFESLHVAICTIEKANSIVNKLMEQGKLETIGMVVVDEVHLISDKGRGYILELLLAKILYMSRRNGLQIQVITMSATLENVQLLQSWLDAELYITNYRPVALKEMIKVGTVIYDHRLKLVRDVAKQKVLLKGLENDSDDVALLCIETLLEGCSVIVFCPSKDWCENLAVQLATAIHVQIKSETVLGQRLRTNLNPRAIAEVKQQLRDIPTGLDGVMSKAITYACAFHHAGLTTEERDIIEASFKAGALKVLVATSTLSSGVNLPARRVLIRSPLFGGKQMSSLTYRQMIGRAGRMGKDTLGESILICNEINARMGRDLVVSELQPITSCLDMDGSTHLKRALLEVISSGVANTKEDIDFFVNCTLLSAQKAFHAKEKPPDEESDANYINDALDFLVEYEFVRLQRNEERETAVYVATRLGAACLASSMPPTDGLILFAELQKSRRSFVLESELHAVYLVTPYSVCYQLQDIDWLLYVHMWEKLSSPMKKVGELVGVRDAFLYKALRGQTKLDYKQMQIHKRFYIALALEELVNETPINVVVHKYKCHRGMLQSLQQMASTFAGIVTAFCNSLQWSTLALIVSQFKDRLFFGIHRDLIDLMRIPDLSQKRARALFDAGITSLVELAGADPVELEKVLYNSISFDSAKQHDHENADEAAKRNVVRNFYITGKAGMTVSEAAKLLIGEARQFVQHEIGLGTIKWTQTQAGVEIASRAIHDGGEVDLHMSLEEEQPPVKRKLSIEENGTANSQKNPRLETVVDTQRGYKVDKNIANQSKMNPNLKEIDAQNKARRNSTAHMDNLNPISNDPCQNNVNVKTAQPIISNLNDIQKQGSQIEKMKINPATVVCSPQLANEEKPSTSQSARRKLVNEGMAERRRVALMKIQQRTQKENQSKDQPIQASRSNQLSSPVNRTPANRWTQSENPNNEMNNSQLPRRNPRNQSPVPNANRTASRKVSNAEEDLFMADDSFMLNTGLAAALTAAESKIASCTEADVIPSSQPKEPEVIGALTPHASRLKRSDQLRSQRIQSPSPTPQREIEIDLESKNESNGVSSMEISDMSMENPLMKNPLHLNASHIMSCSKVDETASSFSSIDIIDVCGHRNAFQAAIIEINNATRLGFSVGLQAQAGKQKPLIGSNLLINQVAAAENREAAARERVLFQVDDTNFISGVSFCLADNVAYYWNMQIDERAAYQGVPTPLKVQELCNLMARKDLTLVMHDGKEQLKMLRKAIPQLKRISAKLEDAKVANWLLQPDKTVNFLNMCQTFAPECTGLANLCGSGRGYSSYGLDTSSAILPRIRTAIESCVTLHILQGQTENLSRIGNGDLLKFFHDIEMPIQLTLCQMELVGFPAQKQRLQQLYQRMVAVMKKVETKIYEQHGSRFNLGSSQAVAKVLGLHRKAKGRVTTSRQVLEKLNSPISHLILGYRKLSGLLAKSIQPLMECCQADRIHGQSITYTATGRISMTEPNLQNVAKEFSIQVGSDVVHISCRSPFMPTDESRCLLSADFCQLEMRILAHMSQDKALLEVMKSSQDLFIAIAAHWNKIEESEVTQDLRNSTKQVCYGIVYGMGMRSLAESLNCSEQEARMISDQFHQAYKGIRDYTTRVVNFARSKGFVETITGRRRYLENINSDVEHLKNQAERQAVNSTIQGSAADIAKNAILKMEKNIERYREKLALGDNSVDLVMHLHDELIFEVPTGKAKKIAKVLSLTMENCVKLSVPLKVKLRIGRSWGEFKEVSV
|
2.7.7.7
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:10343651};
|
DNA biosynthetic process [GO:0071897]; DNA synthesis involved in DNA repair [GO:0000731]; double-strand break repair via alternative nonhomologous end joining [GO:0097681]; nucleotide-excision repair involved in interstrand cross-link repair [GO:1901255]; replication fork processing [GO:0031297]
|
nucleus [GO:0005634]
|
5'-deoxyribose-5-phosphate lyase activity [GO:0051575]; ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; hydrolase activity [GO:0016787]; single-stranded DNA helicase activity [GO:0017116]
|
PF00270;PF00476;PF00271;PF20470;PF21099;
|
1.10.3380.20;3.30.70.370;1.10.150.20;3.40.50.300;3.30.420.10;
|
DNA polymerase type-A family
|
PTM: In adult males, cleaved to produce a 100 kDa form. {ECO:0000269|PubMed:15961355}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15961355}.
|
CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7; Evidence={ECO:0000269|PubMed:10343651, ECO:0000269|PubMed:15961355, ECO:0000269|PubMed:28542210};
| null | null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:10343651};
| null |
FUNCTION: Multifunctional protein with both DNA polymerase and ATPase activities (PubMed:10343651, PubMed:15961355). Might have 3' to 5' exonuclease activity (PubMed:10343651). Plays a role in different DNA repair pathways such as DNA strand cross-link repair and microhomology-mediated end-joining (MMEJ), an alternative non-homologous end-joining (NHEJ) machinery triggered in response to double-strand breaks (PubMed:20617203, PubMed:20936147, PubMed:28542210). MMEJ is an error-prone repair pathway that produces deletions of sequences from the strand being repaired and promotes genomic rearrangements, such as telomere fusions (PubMed:20617203). Utilizes short microhomologies present in partially and fully single-stranded DNA (ssDNA) as primers for DNA synthesis (PubMed:28542210). Prefers poly(dA)/oligo(dT) as a template-primer (PubMed:10343651). The ATPase activity is necessary during interstrand cross-link (ICL) repair and has a critical role in generating templated insertions during MMEJ (PubMed:28542210). Necessary for processing DNA damage induced by oxygen and N-ethylation (PubMed:10732683, PubMed:20936147). In follicle cells, contributes to double-strand break repair at physiological rereplication forks necessary for survival of fertilized eggs (PubMed:20936147, PubMed:27849606). {ECO:0000269|PubMed:10343651, ECO:0000269|PubMed:10732683, ECO:0000269|PubMed:15961355, ECO:0000269|PubMed:20617203, ECO:0000269|PubMed:20936147, ECO:0000269|PubMed:27849606, ECO:0000269|PubMed:28542210}.
|
Drosophila melanogaster (Fruit fly)
|
O18497
|
MAN2_SPOFR
|
MRTRVLRCRPFSTRILLLLLFVLAFGVYCYFYNASPQNYNKPRISYPASMEHFKSSLTHTVKSRDEPTPDQCPALKESEADIDTVAIYPTFDFQPSWLRTKEFWDKSFEDRYERIHNDTTRPRLKVIVVPHSHNDPGWLKTFEQYFEWKTKNIINNIVNKLHQYPNMTFIWTEISFLNAWWERSHPVKQKALKKLIKEGRLEITTGGWVMPDEACTHIYALIDQFIEGHHWVKTNLGVIPKTGWSIDPFGHGATVPYLLDQSGLEGTIIQRIHYAWKQWLAERQIEEFYWLASWATTKPSMIVHNQPFDIYSIKSTCGPHPSICLSFDFRKIPGEYSEYTAKHEDITEHNLHSKAKTLIEEYDRIGSLTPHNVVLVPLGDDFRYEYSVEFDAQYVNYMKMFNYINAHKEIFNADVQFGTPLDYFNAMKERHQNIPSLKGDFFVYSDIFSEGKPAYWSGYYTTRPYQKILARQFEHQLRSAEILFTLVSNYIRQMGRQGEFGASEKKLEKSYEQLIYARRNLGLFQHHDAITGTSKSSVMQDYGTKLFTSLYHCIRLQEAALTTIMLPDQSLHSQSIIQSEVEWETYGKPPKKLQVSFIDKKKVILFNPLAETRTEVVTVRSNTSNIRVYDTHKRKHVLYQIMPSITIQDNGKSIVSDTTFDIMFVATIPPLTSISYKLQEHTNTSHHCVIFCNNCEQYQKSNVFQIKKMMPGDIQLENAVLKLLVNRNTGFLRQVYRKDIRKRTVVDVQFGAYQSAQRHSGAYLFMPHYDSPEKNVLHPYTNQNNMQDDNIIIVSGPISTEITTMYLPFLVHTIRIYNVPDPVLSRAILLETDVDFEAPPKNRETELFMRLQTDIQNGDIPEFYTDQNGFQYQKRVKVNKLGIEANYYPITTMACLQDEETRLTLLTNHAQGAAAYEPGRLEVMLDRRTLYDDFRGIGEGVVDNKPTTFQNWILIESMPGVTRAKRDTSEPGFKFVNERRFGPGQKESPYQVPSQTADYLSRMFNYPVNVYLVDTSEVGEIEVKPYQSFLQSFPPGIHLVTLRTITDDVLELFPSNESYMVLHRPGYSCAVGEKPVAKSPKFSSKTRFNGLNIQNITAVSLTGLKSLRPLTGLSDIHLNAMEVKTYKIRF
|
3.2.1.114
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|RuleBase:RU361199}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|RuleBase:RU361199};
|
mannose metabolic process [GO:0006013]; N-glycan processing [GO:0006491]; protein glycosylation [GO:0006486]
|
endoplasmic reticulum [GO:0005783]; Golgi membrane [GO:0000139]
|
carbohydrate binding [GO:0030246]; mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase activity [GO:0004572]; metal ion binding [GO:0046872]
|
PF09261;PF07748;PF01074;
|
3.20.110.10;1.20.1270.50;2.60.40.1180;
|
Glycosyl hydrolase 38 family
|
PTM: N-glycosylated. {ECO:0000269|PubMed:9061370}.
|
SUBCELLULAR LOCATION: Microsome membrane {ECO:0000269|PubMed:9061370}; Single-pass type II membrane protein {ECO:0000269|PubMed:9061370}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q24451}; Single-pass type II membrane protein {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=2 H2O + N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] = 2 alpha-D-mannopyranose + N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein]; Xref=Rhea:RHEA:56052, Rhea:RHEA-COMP:14368, Rhea:RHEA-COMP:14369, ChEBI:CHEBI:15377, ChEBI:CHEBI:28729, ChEBI:CHEBI:60615, ChEBI:CHEBI:60625; EC=3.2.1.114; Evidence={ECO:0000269|PubMed:9061370};
| null |
PATHWAY: Protein modification; protein glycosylation. {ECO:0000250|UniProtKB:P28494}.
| null | null |
FUNCTION: Catalyzes the first committed step in the biosynthesis of complex N-glycans. It controls conversion of high mannose to complex N-glycans; the final hydrolytic step in the N-glycan maturation pathway. {ECO:0000250|UniProtKB:P28494}.
|
Spodoptera frugiperda (Fall armyworm)
|
O18498
|
MA1A1_SPOFR
|
MTGILPTYQRFVNGVPVPSISRRSFRLREKYLIVSVLLTFGIVWLGALFYLPEFKSSNSVNDSVYNVYKRIQKAGPELLMPPPLAQNDVGDFPVIGIAHHGEGGDDPHVIEDRNRLRAKIEEDMGMKVLERPQFDVAPSVSSSRGPSKPPVDAIEEPAVGNNAANKDVSPSGPKAESSDKFVAVALAPGADPEIKHKLETVKKMMLHAWYNYKLYAWGKNELKPMSKRAHLSSVFGAGELGATIVDGLDTLYLMGLNDEFREGRDWVAEHLHINEIDSDLSVFETTIRFVGGLLSCYALTGDTMFRDKAAEVGDALLPAFDTPTGLPYALINPSTKASRQYHWAGPNSILSELGTLHLEFTYLSDVTGRDIYRQKVSRIREVLDQIDKPGDLYPNFINPRTGQWGQRHMSLGALGDSFYEYLLKAWLMSGGADEQARIMFDTAMQAALDKMLRVSPSGLAYLAELKYGRIIEEKMDHLSCFAGGMFALASTTLDNSMSERYMDVAKKLTNTCHESYARSETKLGPEAFRFSNAAEARAQKSNEKVYLLRPETFESYFIMWRLTKQQMYRDWAWEAVQALEKHCRVEGGYTGLVNVYHANPQGDDVQQSFFLAETLKYLYLIFGDDSFLPLDEWVFNTEAHPFPIRGKNPLYRAVDKPVLPEPAHAQNNRI
|
3.2.1.113
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:Q2ULB2};
|
carbohydrate metabolic process [GO:0005975]; N-glycan processing [GO:0006491]; protein glycosylation [GO:0006486]
|
endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]
|
calcium ion binding [GO:0005509]; mannosyl-oligosaccharide 1,2-alpha-mannosidase activity [GO:0004571]
|
PF01532;
|
1.50.10.10;
|
Glycosyl hydrolase 47 family
|
PTM: N-glycosylated (PubMed:10764822, PubMed:11222938). Contains high mannose-type oligosaccharides (PubMed:11222938). {ECO:0000269|PubMed:10764822, ECO:0000269|PubMed:11222938}.
|
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305|PubMed:11222938}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q8H116}. Note=Localizes in cytoplasmic punctate structures representing Golgi elements. {ECO:0000269|PubMed:11222938}.
|
CATALYTIC ACTIVITY: Reaction=4 H2O + N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 9A1,2,3B1,2,3) = 4 beta-D-mannose + N(4)-(alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 5A1,2); Xref=Rhea:RHEA:56008, Rhea:RHEA-COMP:14356, Rhea:RHEA-COMP:14367, ChEBI:CHEBI:15377, ChEBI:CHEBI:28563, ChEBI:CHEBI:59087, ChEBI:CHEBI:139493; EC=3.2.1.113; Evidence={ECO:0000269|PubMed:10764822, ECO:0000269|PubMed:9147053}; CATALYTIC ACTIVITY: Reaction=3 H2O + N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 8A1,2,3B1,3) = 3 beta-D-mannose + N(4)-(alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 5A1,2); Xref=Rhea:RHEA:56028, Rhea:RHEA-COMP:14358, Rhea:RHEA-COMP:14367, ChEBI:CHEBI:15377, ChEBI:CHEBI:28563, ChEBI:CHEBI:59087, ChEBI:CHEBI:60628; EC=3.2.1.113; Evidence={ECO:0000269|PubMed:10764822};
| null |
PATHWAY: Protein modification; protein glycosylation. {ECO:0000250|UniProtKB:P32906}.
| null | null |
FUNCTION: Involved in the maturation of Asn-linked oligosaccharides. Converts Man(9)GlcNAc(2) to Man(5)GlcNAc(2) primarily through the Man(7)GlcNAc(2) isomer C processing intermediate. {ECO:0000269|PubMed:10764822}.
|
Spodoptera frugiperda (Fall armyworm)
|
O18640
|
GBLP_DROME
|
MSETLQLRGTLIGHNGWVTQIATNPKDPDTIISASRDKTLIVWKLTRDEDTNYGYPQKRLYGHSHFISDVVLSSDGNYALSGSWDQTLRLWDLAAGKTTRRFEGHTKDVLSVAFSADNRQIVSGSRDKTIKLWNTLAECKFTIQEDGHTDWVSCVRFSPNHSNPIIVSCGWDRTVKVWNLANCKLKNNHHGHNGYLNTVTVSPDGSLCTSGGKDSKALLWDLNDGKNLYTLEHNDIINALCFSPNRYWLCVAYGPSIKIWDLACKKTVEELRPEVVSPTSKADQPQCLSLAWSTDGQTLFAGYSDNTIRVWQVSVSAH
| null | null |
cellular response to starvation [GO:0009267]; cuticle development [GO:0042335]; cytoplasmic translation [GO:0002181]; egg-laying behavior [GO:0018991]; IRES-dependent viral translational initiation [GO:0075522]; locomotory behavior [GO:0007626]; muscle cell cellular homeostasis [GO:0046716]; negative regulation of protein phosphorylation [GO:0001933]; negative regulation of smoothened signaling pathway [GO:0045879]; oogenesis [GO:0048477]; positive regulation by host of viral genome replication [GO:0044829]; positive regulation of actin filament polymerization [GO:0030838]; positive regulation of glycogen biosynthetic process [GO:0045725]; positive regulation of protein deubiquitination [GO:1903003]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of protein ubiquitination [GO:0031398]; regulation of autophagosome size [GO:0016243]; rescue of stalled ribosome [GO:0072344]; wing disc development [GO:0035220]
|
autophagosome [GO:0005776]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic ribosome [GO:0022626]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:1990904]
|
protein kinase C binding [GO:0005080]; protein-macromolecule adaptor activity [GO:0030674]; ribosome binding [GO:0043022]; structural constituent of ribosome [GO:0003735]; translation regulator activity [GO:0045182]
|
PF00400;
|
2.130.10.10;
|
WD repeat G protein beta family, Ribosomal protein RACK1 subfamily
| null | null | null | null | null | null | null |
FUNCTION: Involved in the recruitment, assembly and/or regulation of a variety of signaling molecules. Interacts with a wide variety of proteins and plays a role in many cellular processes (By similarity). {ECO:0000250}.
|
Drosophila melanogaster (Fruit fly)
|
O18696
|
PDE1_CAEEL
|
MNRARKTSSCGCFRSAFCLLKPSTSSASEEHGDSDKKLLSVQLITPRDEEEQTSSRSIKIPPLDLNGLDCKKNAVAARRAGRRRTSEGGGVRGKGHFAEVVLDGLQRPVSLLRNQKEKSNSDDNCQEKEPTSPSSSRKKSYDNAPALESLEKLRYILHQLNSGQLPLEDLKRNIEYAALVLETAYMDETRRICDEDDDLAEVTPETVPDEVREWLAATFTRQNAGKKRDKPKFKSVANAIRTGIFFEKLFRKQQVVQCPIPPEIAELMKEVCTWSFSPFQLNEVSEGHALKYVGFELFNRYGFMDRFKVPLTALENYLSALEVGYSKHNNPYHNVVHAADVTQSSHFMLSQTGLANSLGDLELLAVLFGALIHDYEHTGHTNNFHIQSQSQFAMLYNDRSVLENHHVSSCFRLMKEDDKNILTHLTRDEYKELRNMVIEIVLATDMSTHFMQIKTMKSMLSLPEGIDKNKALCLIVHACDISHPAKPWNLHERWTEGVLEEFFRQGDLEASMGLPYSPLCDRHTVHVADSQIGFIDFIVEPTMVVCGELLVKMVEPLVSLPPTDSLFPPSVDGGDDKSPSNALSPLPDLRNSSTSPSSIRRIPLNYAGKLDIPTPWMKFLHENKAHWKERAAKEEEERKIKEAAEAEAAAKQVEENKENGVTTN
|
3.1.4.17
|
COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000250}; Note=Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions, while site 2 has a preference for magnesium and/or manganese ions. {ECO:0000250};
|
cAMP-mediated signaling [GO:0019933]; chemosensory behavior [GO:0007635]; chemotaxis [GO:0006935]; determination of adult lifespan [GO:0008340]; microvillus organization [GO:0032528]; negative regulation of cGMP-mediated signaling [GO:0010754]; negative regulation of protein kinase C signaling [GO:0090038]; phototransduction [GO:0007602]; positive regulation of gene expression [GO:0010628]; regulation of establishment of cell polarity [GO:2000114]; response to alkaline pH [GO:0010446]; response to hydrogen peroxide [GO:0042542]; response to oxygen levels [GO:0070482]
|
neuronal cell body [GO:0043025]
|
3',5'-cyclic-AMP phosphodiesterase activity [GO:0004115]; 3',5'-cyclic-GMP phosphodiesterase activity [GO:0047555]; calmodulin binding [GO:0005516]; calmodulin-activated 3',5'-cyclic-GMP phosphodiesterase activity [GO:0048101]; calmodulin-activated dual specificity 3',5'-cyclic-GMP, 3',5'-cyclic-AMP phosphodiesterase activity [GO:0004117]; metal ion binding [GO:0046872]
|
PF00233;PF08499;
|
1.10.1300.10;
|
Cyclic nucleotide phosphodiesterase family
| null | null |
CATALYTIC ACTIVITY: Reaction=a nucleoside 3',5'-cyclic phosphate + H2O = a nucleoside 5'-phosphate + H(+); Xref=Rhea:RHEA:14653, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57867, ChEBI:CHEBI:58464; EC=3.1.4.17;
| null | null | null | null |
FUNCTION: Redundantly with pde-5, plays a role in the AFD thermosensory neurons to regulate microvilli receptive ending morphology, possibly by regulating cGMP levels. {ECO:0000269|PubMed:27062922}.
|
Caenorhabditis elegans
|
O18733
|
MMP9_CANLF
|
MSPRQPLVLVFLVLGCCSAAPRPHKPTVVVFPGDLRTNLTDKQLAEEYLFRYGYTQVAELSNDKQSLSRGLRLLQRRLALPETGELDKTTLEAMRAPRCGVPDLGKFQTFEGDLKWHHNDITYWIQNYSEDLPRDVIDDAFARAFAVWSAVTPLTFTRVYGPEADIIIQFGVREHGDGYPFDGKNGLLAHAFPPGPGIQGDAHFDDEELWTLGKGVVVPTHFGNADGAPCHFPFTFEGRSYSACTTDGRSDDTPWCSTTADYDTDRRFGFCPSEKLYAQDGNGDGKPCVFPFTFEGRSYSTCTTDGRSDGYRWCSTTADYDQDKLYGFCPTRVDSAVTGGNSAGEPCVFPFIFLGKQYSTCTREGRGDGHLWCATTSNFDRDKKWGFCPDQGYSLFLVAAHEFGHALGLDHSSVPEALMYPMYSFTEGPPLHEDDVRGIQHLYGPRPEPEPQPPTAPPTAPPTVCATGPPTTRPSERPTAGPTGPPAAGPTGPPTAGPSEAPTVPVDPAEDICKVNIFDAIAEIRNYLHFFKEGKYWRFSKGKGRRVQGPFLSPSTWPALPRKLDSAFEDGLTKKTFFFSGRQVWVYTGTSVVGPRRLDKLGLGPEVTQVTGALPQGGGKVLLFSRQRFWSFDVKTQTVDPRSAGSVEQMYPGVPLNTHDIFQYQEKAYFCQDRFYWRVNSRNEVNQVDEVGYVTFDILQCPED
|
3.4.24.35
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P14780}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P14780}; COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P14780}; Note=Binds 3 Ca(2+) ions per subunit. {ECO:0000250|UniProtKB:P14780};
|
collagen catabolic process [GO:0030574]; extracellular matrix organization [GO:0030198]; proteolysis [GO:0006508]; response to stimulus [GO:0050896]
|
extracellular matrix [GO:0031012]; extracellular space [GO:0005615]
|
metalloendopeptidase activity [GO:0004222]; peptidase activity [GO:0008233]; zinc ion binding [GO:0008270]
|
PF00040;PF00045;PF00413;PF04886;
|
3.40.390.10;2.10.10.10;2.110.10.10;
|
Peptidase M10A family
|
PTM: N- and O-glycosylated. {ECO:0000250|UniProtKB:P14780}.
|
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P14780}.
|
CATALYTIC ACTIVITY: Reaction=Cleavage of gelatin types I and V and collagen types IV and V.; EC=3.4.24.35; Evidence={ECO:0000250|UniProtKB:P14780};
| null | null | null | null |
FUNCTION: Matrix metalloproteinase that plays an essential role in local proteolysis of the extracellular matrix and in leukocyte migration (By similarity). Could play a role in bone osteoclastic resorption (By similarity). Cleaves KiSS1 at a Gly-|-Leu bond (By similarity). Cleaves NINJ1 to generate the Secreted ninjurin-1 form (By similarity). Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. Degrades fibronectin but not laminin or Pz-peptide (By similarity). {ECO:0000250|UniProtKB:P14780, ECO:0000250|UniProtKB:P41245}.
|
Canis lupus familiaris (Dog) (Canis familiaris)
|
O18734
|
PP14A_PIG
|
MAAQRLGKRVLSKLQSPSRARGPGGSPGGLQKRHARVTVKYDRRELQRRLDVEKWIDGRLEELYRGREADMPDEVNIDELLELESEEERSRKIQGLLKSCTNPTENFVQELLVKLRGLHKQPGLRQPSPSGDGSLSPRQDRARTAPP
| null | null |
regulation of phosphorylation [GO:0042325]
|
cytoplasm [GO:0005737]
|
protein serine/threonine phosphatase inhibitor activity [GO:0004865]
|
PF05361;
|
1.10.150.220;
|
PP1 inhibitor family
|
PTM: Phosphorylation of Thr-38 induces a conformation change. {ECO:0000269|PubMed:10869555, ECO:0000269|PubMed:10924361, ECO:0000269|PubMed:8720121}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11517233}.
| null | null | null | null | null |
FUNCTION: Inhibitor of PPP1CA. Has over 1000-fold higher inhibitory activity when phosphorylated, creating a molecular switch for regulating the phosphorylation status of PPP1CA substrates and smooth muscle contraction. {ECO:0000269|PubMed:10869555, ECO:0000269|PubMed:10924361, ECO:0000269|PubMed:8720121, ECO:0000269|PubMed:9237662}.
|
Sus scrofa (Pig)
|
O18735
|
ERBB2_CANLF
|
MELAAWCRWGLLLALLPSGAAGTQVCTGTDMKLRLPASPETHLDMLRHLYQGCQVVQGNLELTYLPANASLSFLQDIQEVQGYVLIAHSQVRQIPLQRLRIVRGTQLFEDNYALAVLDNGDPLEGGIPAPGAAQGGLRELQLRSLTEILKGGVLIQRSPQLCHQDTILWKDVFHKNNQLALTLIDTNRFSACPPCSPACKDAHCWGASSGDCQSLTRTVCAGGCARCKGPQPTDCCHEQCAAGCTGPKHSDCLACLHFNHSGICELHCPALVTYNTDTFESMPNPEGRYTFGASCVTSCPYNYLSTDVGSCTLVCPLNNQEVTAEDGTQRCEKCSKPCARVCYGLGMEHLREVRAVTSANIQEFAGCKKIFGSLAFLPESFDGDPASNTAPLQPEQLRVFEALEEITGYLYISAWPDSLPNLSVFQNLRVIRGRVLHDGAYSLTLQGLGISWLGLRSLRELGSGLALIHRNARLCFVHTVPWDQLFRNPHQALLHSANRPEEECVGEGLACYPCAHGHCWGPGPTQCVNCSQFLRGQECVEECRVLQGLPREYVKDRYCLPCHSECQPQNGSVTCFGSEADQCVACAHYKDPPFCVARCPSGVKPDLSFMPIWKFADEEGTCQPCPINCTHSCADLDEKGCPAEQRASPVTSIIAAVVGILLAVVVGLVLGILIKRRRQKIRKYTMRRLLQETELVEPLTPSGAMPNQAQMRILKETELRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVGSPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVREHRGRLGSQDLLNWCVQIAKGMSYLEDVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESIPPRRFTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKCWMIDSECRPRFRELVAEFSRMARDPQRFVVIQNEDLGPASPLDSTFYRSLLEDDDMGDLVDAEEYLVPQQGFFCPEPTPGAGGTAHRRHRSSSTRNGGGELTLGLEPSEEEPPKSPLAPSEGAGSDVFDGDLGMGAAKGLQSLPSQDPSPLQRYSEDPTVPLPPETDGKVAPLTCSPQPEYVNQPEVWPQPPLALEGPLPPSRPAGATLERPKTLSPKTLSPGKNGVVKDVFAFGSAVENPEYLAPRGRAAPQPHPPPAFSPAFDNLYYWDQDPSERGSPPSTFEGTPTAENPEYLGLDVPV
|
2.7.10.1
| null |
cellular response to epidermal growth factor stimulus [GO:0071364]; cellular response to growth factor stimulus [GO:0071363]; ERBB signaling pathway [GO:0038127]; intracellular signal transduction [GO:0035556]; negative regulation of apoptotic process [GO:0043066]; neurogenesis [GO:0022008]; neuron differentiation [GO:0030182]; phosphorylation [GO:0016310]; positive regulation of cell growth [GO:0030307]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of protein targeting to membrane [GO:0090314]; positive regulation of transcription by RNA polymerase I [GO:0045943]; positive regulation of translation [GO:0045727]; regulation of ERK1 and ERK2 cascade [GO:0070372]; regulation of microtubule-based process [GO:0032886]
|
basal plasma membrane [GO:0009925]; early endosome [GO:0005769]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]; ruffle membrane [GO:0032587]
|
ATP binding [GO:0005524]; RNA polymerase I core binding [GO:0001042]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]
|
PF00757;PF14843;PF07714;PF01030;PF21314;
|
1.20.5.100;4.10.1140.10;3.80.20.20;1.10.510.10;
|
Protein kinase superfamily, Tyr protein kinase family, EGF receptor subfamily
|
PTM: Autophosphorylated. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Ligand-binding increases phosphorylation on tyrosine residues. Signaling via SEMA4C promotes phosphorylation at Tyr-1252. Dephosphorylated by PTPN12. {ECO:0000250|UniProtKB:P04626}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P04626}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P04626}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:P04626}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P04626}. Early endosome {ECO:0000250|UniProtKB:P04626}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P04626}. Nucleus {ECO:0000250|UniProtKB:P04626}. Note=Translocation to the nucleus requires endocytosis, probably endosomal sorting and is mediated by importin beta-1/KPNB1. Also detected in endosome-to-TGN retrograde vesicles. Internalized from the cell membrane in response to EGF stimulation. {ECO:0000250|UniProtKB:P04626}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
| null | null | null | null |
FUNCTION: Protein tyrosine kinase that is part of several cell surface receptor complexes, but that apparently needs a coreceptor for ligand binding. Essential component of a neuregulin-receptor complex, although neuregulins do not interact with it alone. GP30 is a potential ligand for this receptor. Regulates outgrowth and stabilization of peripheral microtubules (MTs). Upon ERBB2 activation, the MEMO1-RHOA-DIAPH1 signaling pathway elicits the phosphorylation and thus the inhibition of GSK3B at cell membrane. This prevents the phosphorylation of APC and CLASP2, allowing its association with the cell membrane. In turn, membrane-bound APC allows the localization of MACF1 to the cell membrane, which is required for microtubule capture and stabilization (By similarity). {ECO:0000250}.; FUNCTION: In the nucleus is involved in transcriptional regulation. Associates with the 5'-TCAAATTC-3' sequence in the PTGS2/COX-2 promoter and activates its transcription. Implicated in transcriptional activation of CDKN1A; the function involves STAT3 and SRC. Involved in the transcription of rRNA genes by RNA Pol I and enhances protein synthesis and cell growth (By similarity). {ECO:0000250}.
|
Canis lupus familiaris (Dog) (Canis familiaris)
|
O18738
|
DAG1_BOVIN
|
MRMSVGSAVPLPLWGRTFLLLLSVAVTQSHWPSEPSEAVRDWENQLEASMHSALSDLHETVPTVVGIPDGTAVVGRSFRVTIPTDLIASNGEVIKVSAAGKEALPSWLHWDPQSHTLEGLPLDTDKGVHYISVSAARLGANGSHVPQTSSVFSIEVYPEDHSEPQSLRAASPDPGEVVSLVCAADEPVTVLTVILDADLTKMTPKQRIDLLRRMRGFSEVEPHNMKLVPVVNNRLFDMSAFMAGPGNAKKVVENGALLSWKLGCCLNQNSVPDIRGVEVPAREGAMSAQLGYPVVGWHIANKKPSLPKRIRRQIHATPTPVTAIGPPTTAIQEPPSRIVPTPTSPAIAPPTETMAPPVRDPVPGKPTVTIRTRGAIIQTPTLGPIQPTRVSEAGTTVPSQIRPTMTIPGYMEPSTVTTPPTTTTKKPRVSTPRPATPSTDSSTTTTRRPTKKPRTSRPVPRVTTKAPITRLETASPATRMRTTTSGVPHGGEPNQRPELKNHIDRVDAWVGTYFEVKIPSDTFYDNEDTTTDKLKLTLKLREQQLVGEKSWVQFNSNSQLMYGLPDSSHVGKHEYFMHATDKGGLSAVDAFEIHVHRRPQGDKAPARFKAKLTGDPAAVTNDIHKKIALVKKLAFAFGDRNCSTITLQNITRGSIVVEWTNNTLPLEPCPKEQITALSRRIAEDDGKPRGAFVNALEPDFQAMSITVTGSGSCRHLQFVPVAPPMRVPSEAPATEVPDRDPEKSSEDDVYLHTVIPAVVVAAILLIAGIIAMICYRKKRKGKLTLEDQATFIKKGVPIIFADELDDSKPPPSSSMPLILQEEKAPLPPPEYPNQSMPETTPLNQDTVGEYAPLRDEDPSAPPYQPPPPFTAPMEGKGSRPKNMTPYRSPPPYVPP
| null | null |
axon guidance [GO:0007411]; morphogenesis of an epithelium [GO:0002009]; muscle attachment [GO:0016203]; nerve development [GO:0021675]
|
basement membrane [GO:0005604]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; dystroglycan complex [GO:0016011]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; sarcolemma [GO:0042383]
|
calcium ion binding [GO:0005509]; laminin binding [GO:0043236]
|
PF18424;PF05454;PF05345;
|
3.30.70.1040;2.60.40.10;
| null |
PTM: [Alpha-dystroglycan]: O-glycosylated (PubMed:16709410, PubMed:8999917). POMGNT1 catalyzes the initial addition of N-acetylglucosamine, giving rise to the GlcNAc(beta1-2)Man(alpha1-)O-Ser/Thr moiety and thus providing the necessary basis for the addition of further carbohydrate moieties. Heavily O-glycosylated comprising of up to two thirds of its mass and the carbohydrate composition differs depending on tissue type. Mucin-type O-glycosylation is important for ligand binding activity. O-mannosylation is found in high abundance in both brain and muscle where the most abundant glycan is Sia-alpha-2-3-Gal-beta-1-4-Glc-NAc-beta-1-2-Man. In muscle, glycosylation on Thr-317, Thr-319 and Thr-379 by a phosphorylated O-mannosyl glycan with the structure 2-(N-acetylamido)-2-deoxygalactosyl-beta-1,3-2-(N-acetylamido)-2-deoxyglucosyl-beta-1,4-6-phosphomannose is mediated by like-acetylglucosaminyltransferase (LARGE1) protein amd is required for laminin binding. O-glycosylated in the N-terminal region with a core 1 or possibly core 8 glycan. The brain form displays a unique glycosylation pattern which is absent in other tissues; this form shows enhanced binding to laminin LAMA5 compared to the skeletal muscle form (PubMed:16709410). {ECO:0000250|UniProtKB:Q14118, ECO:0000269|PubMed:16709410, ECO:0000269|PubMed:8999917}.; PTM: [Beta-dystroglycan]: N-glycosylated. {ECO:0000250|UniProtKB:Q14118}.; PTM: Autolytic cleavage produces the alpha and beta subunits. In cutaneous cells, as well as in certain pathological conditions, shedding of beta-dystroglycan can occur releasing a peptide of about 30 kDa (By similarity). {ECO:0000250}.; PTM: SRC-mediated phosphorylation of the PPXY motif of the beta subunit recruits SH2 domain-containing proteins, but inhibits binding to WWW domain-containing proteins, DMD and UTRN. This phosphorylation also inhibits nuclear entry (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: [Alpha-dystroglycan]: Secreted, extracellular space {ECO:0000250}.; SUBCELLULAR LOCATION: [Beta-dystroglycan]: Cell membrane {ECO:0000250}; Single-pass type I membrane protein. Cytoplasm, cytoskeleton. Nucleus, nucleoplasm. Cell membrane, sarcolemma {ECO:0000250}. Postsynaptic cell membrane {ECO:0000250}. Note=The monomeric form translocates to the nucleus via the action of importins and depends on RAN. Nuclear transport is inhibited by Tyr-892 phosphorylation. In skeletal muscle, this phosphorylated form locates to a vesicular internal membrane compartment. In muscle cells, sarcolemma localization requires the presence of ANK2, while localization to costameres requires the presence of ANK3. Localizes to neuromuscular junctions (NMJs) in the presence of ANK2 (By similarity). Colocalizes with ERM proteins in Schwann-cell microvilli (By similarity). In peripheral nerves, localizes to the Schwann cell membrane. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: The dystroglycan complex is involved in a number of processes including laminin and basement membrane assembly, sarcolemmal stability, cell survival, peripheral nerve myelination, nodal structure, cell migration, and epithelial polarization. {ECO:0000250}.; FUNCTION: [Alpha-dystroglycan]: Extracellular peripheral glycoprotein that acts as a receptor for extracellular matrix proteins containing laminin-G domains. Receptor for laminin-2 (LAMA2) and agrin in peripheral nerve Schwann cells (PubMed:8798547). Also acts as a receptor for laminin LAMA5 (PubMed:16709410). {ECO:0000269|PubMed:16709410, ECO:0000269|PubMed:8798547}.; FUNCTION: [Beta-dystroglycan]: Transmembrane protein that plays important roles in connecting the extracellular matrix to the cytoskeleton. Acts as a cell adhesion receptor in both muscle and non-muscle tissues. Receptor for both DMD and UTRN and, through these interactions, scaffolds axin to the cytoskeleton. Also functions in cell adhesion-mediated signaling and implicated in cell polarity (By similarity). {ECO:0000250}.
|
Bos taurus (Bovine)
|
O18756
|
GLCE_BOVIN
|
MRCLAARVNYKTLIIICALFTLVTVLLWNKCSSDKAIQVPRHLSSGFRVDALEKKAAASESNNYVNHMAKQSEEAFPQEQQKAPPVVGGFNNNGGGRVLGLKYEEIDCLINDEHTIKGRREGNEVFLPFTWVEKYFDVYGKVVQYDGYDRFEFSHSYSKVYAQRAPYHPDGVFMSFEGYNVEVRDRVKCISGVEGVPLSTQWGPQGYFYPIQIAQYGLSHYSKNLTEKPPHIEVYETAEDRDKNSKPNDWTVPKGCFMASVADKSRFTNVKQFIAPETSEGVSLQLGNTKDFIISFDLKFLTNGSVSVVLETTEKNQLFTVHYVSNTQLIAFKERDIYYGIGPRTSWSTVTRDLVTDLRKGVGLSNTKAVKPTRIMPKKVVRLIAKGKGFLDNITISTTAHMAAFFAASDWLVRNQDEKGGWPIMVTRKLGEGFKSLEPGWYSAMAQGQAISTLVRAYLLTKDHIFLNSALRATAPYKFLSEQHGVKAVFMNKHDWYEEYPTTPSSFVLNGFMYSLIGLYDLKETAGEKLGKEARSLYERGMESLKAMLPLYDTGSGTIYDLRHFMLGIAPNLARWDYHTTHINQLQLLSTIDESPIFKEFVKRWKSYLKGSRAKHN
|
5.1.3.17
| null |
heparan sulfate proteoglycan biosynthetic process [GO:0015012]; heparin biosynthetic process [GO:0030210]
|
Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]
|
calcium ion binding [GO:0005509]; heparosan-N-sulfate-glucuronate 5-epimerase activity [GO:0047464]; protein homodimerization activity [GO:0042803]; racemase and epimerase activity, acting on carbohydrates and derivatives [GO:0016857]
|
PF06662;PF21174;
| null |
D-glucuronyl C5-epimerase family
| null |
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9EPS3}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9EPS3}.
|
CATALYTIC ACTIVITY: Reaction=[heparosan-N-sulfate](n) = [heparan-N-sulfate](n); Xref=Rhea:RHEA:20197, Rhea:RHEA-COMP:9556, Rhea:RHEA-COMP:9557, ChEBI:CHEBI:58041, ChEBI:CHEBI:58287; EC=5.1.3.17; Evidence={ECO:0000269|PubMed:10727403};
| null |
PATHWAY: Glycan metabolism; heparan sulfate biosynthesis. {ECO:0000305|PubMed:10727403}.; PATHWAY: Glycan metabolism; heparin biosynthesis. {ECO:0000305|PubMed:10727403}.
| null | null |
FUNCTION: Converts D-glucuronic acid residues adjacent to N-sulfate sugar residues to L-iduronic acid residues, both in maturing heparan sulfate (HS) and heparin chains. This is important for further modifications that determine the specificity of interactions between these glycosaminoglycans and proteins. {ECO:0000269|PubMed:10727403, ECO:0000269|PubMed:11274177}.
|
Bos taurus (Bovine)
|
O18757
|
SCMC1_RABIT
|
MLRWLRGFVLPTAACQGAEPPTRYETLFQALDRNGDGVVDIRELQEGLKSLGIPLGQDAEEKIFTTGDVNKDGKLDFEEFMKYLKDHEKKMKLAFKSLDKNNDGKIEASEIVQSLQTLGLTISEQQAELILQSIDADGTMTVDWNEWRDYFLFNPVADIEEIIRFWKHSTGIDIGDSLTIPDEFTEEERKSGQWWRQLLAGGIAGAVSRTSTAPLDRLKVMMQVHGSKSMNIFGGFRQMIKEGGVRSLWRGNGTNVIKIAPETAVKFWVYEQYKKLLTEEGQKIGTFERFISGSMAGATAQTFIYPMEVMKTRLAVGKTGQYSGIYDCAKKILKYEGFGAFYKGYVPNLLGIIPYAGIDLAVYELLKSHWLDNFAKDSVNPGVLVLLGCGALSSTCGQLASYPLALVRTRMQAQAMLEGAPQLNMVGLFRRIISKEGLPGLYRGITPNFMKVLPAVGISYVVYENMKQTLGVTQK
| null | null |
adenine nucleotide transport [GO:0051503]; cellular response to calcium ion [GO:0071277]; mitochondrial ATP transmembrane transport [GO:1990544]
|
membrane [GO:0016020]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; peroxisomal membrane [GO:0005778]
|
adenine nucleotide transmembrane transporter activity [GO:0000295]; ADP:inorganic phosphate antiporter activity [GO:0140988]; ATP:inorganic phosphate antiporter activity [GO:0140987]; calcium ion binding [GO:0005509]
|
PF13499;PF00153;
|
1.10.238.10;1.50.40.10;
|
Mitochondrial carrier (TC 2.A.29) family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:9238007}; Multi-pass membrane protein {ECO:0000255}. Peroxisome membrane {ECO:0000269|PubMed:9238007}; Multi-pass membrane protein {ECO:0000255}. Note=The physiological relevance of the localization to the peroxisome is unclear. {ECO:0000269|PubMed:9238007}.
|
CATALYTIC ACTIVITY: Reaction=ATP(out) + Mg(2+)(out) + phosphate(in) = ATP(in) + Mg(2+)(in) + phosphate(out); Xref=Rhea:RHEA:65840, ChEBI:CHEBI:18420, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474; Evidence={ECO:0000250|UniProtKB:Q6NUK1}; CATALYTIC ACTIVITY: Reaction=ADP(out) + H(+)(out) + phosphate(in) = ADP(in) + H(+)(in) + phosphate(out); Xref=Rhea:RHEA:65844, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q6NUK1}; CATALYTIC ACTIVITY: Reaction=AMP(out) + phosphate(in) = AMP(in) + phosphate(out); Xref=Rhea:RHEA:70259, ChEBI:CHEBI:43474, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q6NUK1}; CATALYTIC ACTIVITY: Reaction=ATP(out) + 2 H(+)(out) + phosphate(in) = ATP(in) + 2 H(+)(in) + phosphate(out); Xref=Rhea:RHEA:72035, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474; Evidence={ECO:0000250|UniProtKB:Q6NUK1}; CATALYTIC ACTIVITY: Reaction=ADP(out) + dADP(in) = ADP(in) + dADP(out); Xref=Rhea:RHEA:72855, ChEBI:CHEBI:57667, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q6NUK1}; CATALYTIC ACTIVITY: Reaction=ADP(out) + ATP(in) + H(+)(out) + Mg(2+)(in) = ADP(in) + ATP(out) + H(+)(in) + Mg(2+)(out); Xref=Rhea:RHEA:73659, ChEBI:CHEBI:15378, ChEBI:CHEBI:18420, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q6NUK1}; CATALYTIC ACTIVITY: Reaction=ADP(out) + diphosphate(in) = ADP(in) + diphosphate(out); Xref=Rhea:RHEA:73671, ChEBI:CHEBI:33019, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q6NUK1}; CATALYTIC ACTIVITY: Reaction=ADP(out) + dAMP(in) + H(+)(out) = ADP(in) + dAMP(out) + H(+)(in); Xref=Rhea:RHEA:73675, ChEBI:CHEBI:15378, ChEBI:CHEBI:58245, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q6NUK1}; CATALYTIC ACTIVITY: Reaction=3'-AMP(in) + ADP(out) + H(+)(out) = 3'-AMP(out) + ADP(in) + H(+)(in); Xref=Rhea:RHEA:73679, ChEBI:CHEBI:15378, ChEBI:CHEBI:60880, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q6NUK1}; CATALYTIC ACTIVITY: Reaction=dAMP(out) + phosphate(in) = dAMP(in) + phosphate(out); Xref=Rhea:RHEA:73687, ChEBI:CHEBI:43474, ChEBI:CHEBI:58245; Evidence={ECO:0000250|UniProtKB:Q6NUK1}; CATALYTIC ACTIVITY: Reaction=3'-AMP(out) + phosphate(in) = 3'-AMP(in) + phosphate(out); Xref=Rhea:RHEA:73691, ChEBI:CHEBI:43474, ChEBI:CHEBI:60880; Evidence={ECO:0000250|UniProtKB:Q6NUK1}; CATALYTIC ACTIVITY: Reaction=dADP(out) + H(+)(out) + phosphate(in) = dADP(in) + H(+)(in) + phosphate(out); Xref=Rhea:RHEA:73695, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57667; Evidence={ECO:0000250|UniProtKB:Q6NUK1};
| null | null | null | null |
FUNCTION: Electroneutral antiporter that mediates the transport of adenyl nucleotides through the inner mitochondrial membrane. Originally identified as an ATP-magnesium/inorganic phosphate antiporter, it also acts as a broad specificity adenyl nucleotide antiporter. By regulating the mitochondrial matrix adenyl nucleotide pool could adapt to changing cellular energetic demands and indirectly regulate adenyl nucleotide-dependent metabolic pathways. In vitro, a low activity is also observed with guanyl and pyrimidine nucleotides. May play a role in protecting cells against oxidative stress-induced cell death, by buffering calcium levels in the mitochondrial matrix through the formation of calcium-phosphate precipitates. {ECO:0000250|UniProtKB:Q6NUK1}.
|
Oryctolagus cuniculus (Rabbit)
|
O18766
|
OPSD_PIG
|
MNGTEGPNFYVPFSNKTGVVRSPFEYPQYYLAEPWQFSMLAAYMFMLIVLGFPINFLTLYVTVQHKKLRTPLNYILLNLAVADLFMVFGGFTTTLYTSLHGYFVFGPTGCNLEGFFATLGGEIALWSLVVLAIERYVVVCKPMSNFRFGENHAIMGLALTWVMALACAAPPLVGWSRYIPEGLQCSCGIDYYTLKPEVNNESFVIYMFVVHFSIPLVIIFFCYGQLVFTVKEAAAQQQESATTQKAEKEVTRMVIIMVVAFLICWLPYASVAFYIFTHQGSDFGPIFMTIPAFFAKSASIYNPVIYIMMNKQFRNCMLTTLCCGKNPLGDDEASTTTSKTETSQVAPA
| null | null |
absorption of visible light [GO:0016038]; adaptation of rhodopsin mediated signaling [GO:0016062]; cellular response to light stimulus [GO:0071482]; detection of temperature stimulus involved in thermoception [GO:0050960]; G protein-coupled receptor signaling pathway [GO:0007186]; gene expression [GO:0010467]; microtubule cytoskeleton organization [GO:0000226]; photoreceptor cell maintenance [GO:0045494]; phototransduction [GO:0007602]; podosome assembly [GO:0071800]; rhodopsin mediated signaling pathway [GO:0016056]; rod bipolar cell differentiation [GO:1904389]; thermotaxis [GO:0043052]; visual perception [GO:0007601]
|
cell-cell junction [GO:0005911]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; photoreceptor disc membrane [GO:0097381]; photoreceptor inner segment membrane [GO:0060342]; photoreceptor outer segment [GO:0001750]; photoreceptor outer segment membrane [GO:0042622]; plasma membrane [GO:0005886]; rod photoreceptor outer segment [GO:0120200]; sperm head plasma membrane [GO:1990913]; sperm midpiece [GO:0097225]
|
11-cis retinal binding [GO:0005502]; G protein-coupled photoreceptor activity [GO:0008020]; metal ion binding [GO:0046872]
|
PF00001;PF10413;
|
1.20.1070.10;
|
G-protein coupled receptor 1 family, Opsin subfamily
|
PTM: Phosphorylated on some or all of the serine and threonine residues present in the C-terminal region. {ECO:0000250|UniProtKB:P02699}.; PTM: Contains one covalently linked retinal chromophore. Upon light absorption, the covalently bound 11-cis-retinal is converted to all-trans-retinal. After hydrolysis of the Schiff base and release of the covalently bound all-trans-retinal, active rhodopsin is regenerated by binding of a fresh molecule of 11-cis-retinal. {ECO:0000250|UniProtKB:P02699}.
|
SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P02699}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P02699}. Cell projection, cilium, photoreceptor outer segment {ECO:0000250|UniProtKB:P02699}. Note=Synthesized in the inner segment (IS) of rod photoreceptor cells before vectorial transport to disk membranes in the rod outer segment (OS) photosensory cilia. {ECO:0000250|UniProtKB:P08100}.
| null | null | null | null | null |
FUNCTION: Photoreceptor required for image-forming vision at low light intensity. Required for photoreceptor cell viability after birth (PubMed:9335046). Light-induced isomerization of 11-cis to all-trans retinal triggers a conformational change that activates signaling via G-proteins. Subsequent receptor phosphorylation mediates displacement of the bound G-protein alpha subunit by the arrestin SAG and terminates signaling (By similarity). {ECO:0000250|UniProtKB:P02699, ECO:0000250|UniProtKB:P08100, ECO:0000269|PubMed:9335046}.
|
Sus scrofa (Pig)
|
O18778
|
PAHX_BOVIN
|
MDRNRASARLTVLLRHLGCRSAGTIIAHHTSGVGSLASFHPQQFQYTRENNVLSLEQRKFYEENGFLVIKNLVSDADIQRFRNEFERICRKEVKPLGLSVMRDVTITKSEYVPSEKVVSKVQDFQEDEELFRYCTLPEILKYVECFTGPNIMAMHTMLINKPPDSGKKTSRHPLHQDLHYFPFRPSNSIVCAWTAMEHIDRNNGCLVVLPGTHKGPLQPHDYPQWEGGVNIMFHGIQDYDKNNARVHLVMEKGDTVFFHPLLIHGSGRNKSQGFRKAISCHFADANCHYIDVEGTSQENIEKEVVDIVRKKYGFKDVTLKDVWTFRGRVVKGERINL
|
1.14.11.18
|
COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250|UniProtKB:O14832}; COFACTOR: Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250|UniProtKB:O14832}; COFACTOR: Name=ATP; Xref=ChEBI:CHEBI:30616; Evidence={ECO:0000250|UniProtKB:O14832}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O14832};
|
2-oxoglutarate metabolic process [GO:0006103]; fatty acid alpha-oxidation [GO:0001561]; isoprenoid metabolic process [GO:0006720]; methyl-branched fatty acid metabolic process [GO:0097089]
|
9+0 non-motile cilium [GO:0097731]; peroxisome [GO:0005777]
|
ferrous iron binding [GO:0008198]; L-ascorbic acid binding [GO:0031418]; phytanoyl-CoA dioxygenase activity [GO:0048244]
|
PF05721;
|
2.60.120.620;
|
PhyH family
| null |
SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:O14832}.
|
CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + O2 + phytanoyl-CoA = 2-hydroxyphytanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:16065, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:57334, ChEBI:CHEBI:57391; EC=1.14.11.18; Evidence={ECO:0000250|UniProtKB:O14832}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16066; Evidence={ECO:0000250|UniProtKB:O14832}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + 3-methylhexadecanoyl-CoA + O2 = 2-hydroxy-3-methylhexadecanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:44000, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:58784, ChEBI:CHEBI:83969; Evidence={ECO:0000250|UniProtKB:O14832}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44001; Evidence={ECO:0000250|UniProtKB:O14832}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + hexadecanoyl-CoA + O2 = 2-hydroxyhexadecanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:54596, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:57379, ChEBI:CHEBI:74115; Evidence={ECO:0000250|UniProtKB:O14832}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54597; Evidence={ECO:0000250|UniProtKB:O14832}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + O2 + octanoyl-CoA = 2-hydroxyoctanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:54600, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:57386, ChEBI:CHEBI:138290; Evidence={ECO:0000250|UniProtKB:O14832}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54601; Evidence={ECO:0000250|UniProtKB:O14832}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + decanoyl-CoA + O2 = 2-hydroxydecanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:54604, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:61430, ChEBI:CHEBI:138292; Evidence={ECO:0000250|UniProtKB:O14832}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54605; Evidence={ECO:0000250|UniProtKB:O14832}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + 3-methylbutanoyl-CoA + O2 = 2-hydroxy-3-methylbutanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:54612, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:57345, ChEBI:CHEBI:138296; Evidence={ECO:0000250|UniProtKB:O14832}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54613; Evidence={ECO:0000250|UniProtKB:O14832}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + heptadecanoyl-CoA + O2 = 2-hydroxyheptadecanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:54616, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:74307, ChEBI:CHEBI:138297; Evidence={ECO:0000250|UniProtKB:O14832}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54617; Evidence={ECO:0000250|UniProtKB:O14832}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + eicosanoyl-CoA + O2 = 2-hydroxyeicosanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:54620, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:57380, ChEBI:CHEBI:138298; Evidence={ECO:0000250|UniProtKB:O14832}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54621; Evidence={ECO:0000250|UniProtKB:O14832}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + O2 + octadecanoyl-CoA = 2-hydroxyoctadecanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:54624, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:57394, ChEBI:CHEBI:74116; Evidence={ECO:0000250|UniProtKB:O14832}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54625; Evidence={ECO:0000250|UniProtKB:O14832}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + dodecanoyl-CoA + O2 = 2-hydroxydodecanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:54628, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:57375, ChEBI:CHEBI:138299; Evidence={ECO:0000250|UniProtKB:O14832}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54629; Evidence={ECO:0000250|UniProtKB:O14832}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + O2 + tetradecanoyl-CoA = 2-hydroxytetradecanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:54632, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:57385, ChEBI:CHEBI:138300; Evidence={ECO:0000250|UniProtKB:O14832}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54633; Evidence={ECO:0000250|UniProtKB:O14832}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + hexanoyl-CoA + O2 = 2-hydroxyhexanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:55172, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:62620, ChEBI:CHEBI:138630; Evidence={ECO:0000250|UniProtKB:O14832}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55173; Evidence={ECO:0000250|UniProtKB:O14832}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + butanoyl-CoA + O2 = 2-hydroxybutanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:55176, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:57371, ChEBI:CHEBI:138628; Evidence={ECO:0000250|UniProtKB:O14832}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55177; Evidence={ECO:0000250|UniProtKB:O14832}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + 3-methylnonanoyl-CoA + O2 = 2-hydroxy-3-methylnonanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:55180, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:138633, ChEBI:CHEBI:138634; Evidence={ECO:0000250|UniProtKB:O14832}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55181; Evidence={ECO:0000250|UniProtKB:O14832}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + 3-methylundecanoyl-CoA + O2 = 2-hydroxy-3-methylundecanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:55184, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:84183, ChEBI:CHEBI:138632; Evidence={ECO:0000250|UniProtKB:O14832}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55185; Evidence={ECO:0000250|UniProtKB:O14832}; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + 3-methyldodecanoyl-CoA + O2 = 2-hydroxy-3-methyldodecanoyl-CoA + CO2 + succinate; Xref=Rhea:RHEA:55192, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:138636, ChEBI:CHEBI:138637; Evidence={ECO:0000250|UniProtKB:O14832}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55193; Evidence={ECO:0000250|UniProtKB:O14832};
| null |
PATHWAY: Lipid metabolism; fatty acid metabolism.
| null | null |
FUNCTION: Catalyzes the 2-hydroxylation of not only racemic phytanoyl-CoA and the isomers of 3-methylhexadecanoyl-CoA, but also a variety of other mono- branched 3-methylacyl-CoA esters (with a chain length of at least seven carbon atoms) and straight-chain acyl-CoA esters (with a chain length longer than four carbon atoms) (By similarity). Does not hydroxylate long and very long straight chain acyl-CoAs or 2-methyl-and 4-methyl-branched acyl-CoAs (By similarity). {ECO:0000250|UniProtKB:O14832}.
|
Bos taurus (Bovine)
|
O18793
|
CCR2_MACMU
|
MLSTSRSRFIRNTNGSGEEVTTFFDYDYGAPCHKFDVKQIGAQLLPPLYSLVFIFGFVGNMLVVLILINCKKLKSLTDIYLLNLAISDLLFLITLPLWAHSAANEWVFGNAMCKLFTGLYHIGYLGGIFFIILLTIDRYLAIVHAVFALKARTVTFGVVTSVITWLVAVFASVPGIIFTKCQEEDSVYICGPYFPRGWNNFHTIMRNILGLVLPLLIMVICYSGILKTLLRCRNEKKRHRAVRLIFTIMIVYFLFWTPYNIVILLNTFQEFFGLSNCESTRQLDQATQVTETLGMTHCCINPIIYAFVGEKFRRYLSMFFRKYITKRFCKQCPVFYRETVDGVTSTNTPSTAEQEVSVGL
| null | null |
blood vessel remodeling [GO:0001974]; calcium-mediated signaling [GO:0019722]; cell chemotaxis [GO:0060326]; immune response [GO:0006955]; inflammatory response [GO:0006954]; inflammatory response to wounding [GO:0090594]; macrophage migration [GO:1905517]; monocyte extravasation [GO:0035696]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of monocyte chemotaxis [GO:0090026]; positive regulation of synaptic transmission, glutamatergic [GO:0051968]; positive regulation of thymocyte migration [GO:2000412]; regulation of inflammatory response [GO:0050727]; regulation of T cell cytokine production [GO:0002724]; regulation of T cell differentiation [GO:0045580]; sensory perception of pain [GO:0019233]
|
cytoplasm [GO:0005737]; external side of plasma membrane [GO:0009897]; plasma membrane [GO:0005886]
|
C-C chemokine binding [GO:0019957]; C-C chemokine receptor activity [GO:0016493]
|
PF00001;
|
1.20.1070.10;
|
G-protein coupled receptor 1 family
|
PTM: N-glycosylated. {ECO:0000250|UniProtKB:P41597}.; PTM: Sulfation increases the affinity for both monomeric and dimeric CCL2 with stronger binding to the monomeric form (By similarity). Binding of sulfated CCR2 to CCL2 promotes conversion of CCL2 from dimer to monomer (By similarity). {ECO:0000250|UniProtKB:P41597}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P41597}; Multi-pass membrane protein {ECO:0000255}. Note=The chemoattractant receptors are distributed throughout the cell surface; after stimulation with a ligand, such as CCL2, they are rapidly recruited into microdomain clusters at the cell membrane. {ECO:0000250|UniProtKB:P41597}.
| null | null | null | null | null |
FUNCTION: Key functional receptor for CCL2 but can also bind CCL7 and CCL12 (By similarity). Its binding with CCL2 on monocytes and macrophages mediates chemotaxis and migration induction through the activation of the PI3K cascade, the small G protein Rac and lamellipodium protrusion (By similarity). Also acts as a receptor for the beta-defensin DEFB106A/DEFB106B (By similarity). Regulates the expression of T-cell inflammatory cytokines and T-cell differentiation, promoting the differentiation of T-cells into T-helper 17 cells (Th17) during inflammation (By similarity). Facilitates the export of mature thymocytes by enhancing directional movement of thymocytes to sphingosine-1-phosphate stimulation and up-regulation of S1P1R expression; signals through the JAK-STAT pathway to regulate FOXO1 activity leading to an increased expression of S1P1R (By similarity). Plays an important role in mediating peripheral nerve injury-induced neuropathic pain (By similarity). Increases NMDA-mediated synaptic transmission in both dopamine D1 and D2 receptor-containing neurons, which may be caused by MAPK/ERK-dependent phosphorylation of GRIN2B/NMDAR2B (By similarity). Mediates the recruitment of macrophages and monocytes to the injury site following brain injury (By similarity). {ECO:0000250|UniProtKB:P41597, ECO:0000250|UniProtKB:P51683}.
|
Macaca mulatta (Rhesus macaque)
|
O18796
|
IL6RA_PIG
|
MLAVGCALLTALLAAPGMALAPRGCSKLEVAQDVLTSLPGASVTLTCPGGEPGDNATIHWVLRNQVTGSPDGRPAGVGRRLLLKSVQLSDSGNYSCYQDGVPAGSVRLLVDAPPEEPQLSCFRKSPLSNVGCEWRPRSPPSPTTKAVLLVRKFQNSPVEDFQEPCQYSLEAQRFFCQLAVPEGDNSFHIVTLCVANSAGSQSSTPQTFEGYGILQPDPPVNITVSAVDRNPRWLSVTWQDPPSWNSYFYRLQFELRYRAERSKTFTTWMVKELQHHCIIHDAWSGMRHVVQLRAQEEFGHGLWSEWSQEVTGIPWTESRSSPAETELPLSTQAPTTNEDDEDISSKESANATSLPVQDSASVPLPTFLVAGGSLAFGTLLCIGIILRFKKTGQLQALKEGKTNMHPPYSLGQLVPERPKSTPVLVPLISPPVSPNSLGDNTSRNSRPEARGPQSPYDVSNRDYFFPR
| null | null |
ciliary neurotrophic factor-mediated signaling pathway [GO:0070120]; interleukin-6-mediated signaling pathway [GO:0070102]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of tyrosine phosphorylation of STAT protein [GO:0042531]; T-helper 17 cell lineage commitment [GO:0072540]; vascular endothelial growth factor production [GO:0010573]
|
external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]; interleukin-6 receptor complex [GO:0005896]; receptor complex [GO:0043235]
|
interleukin-11 binding [GO:0019970]; interleukin-11 receptor activity [GO:0004921]; interleukin-6 binding [GO:0019981]; interleukin-6 receptor activity [GO:0004915]
|
PF00047;PF09240;
|
2.60.40.10;
|
Type I cytokine receptor family, Type 3 subfamily
|
PTM: A short soluble form is also released from the membrane by proteolysis. The sIL6R is formed by limited proteolysis of membrane-bound receptors, a process referred to as ectodomain shedding. mIL6R is cleaved by the proteases ADAM10 and ADAM17. {ECO:0000250|UniProtKB:P22272}.; PTM: Glycosylated. Glycosylation is dispensable for transport, signaling, and cell-surface turnover. Glycosylation at Asn-55 is a protease-regulatory exosite. Glycosylation is required for ADAM17-mediated proteolysis. {ECO:0000250|UniProtKB:P08887}.
|
SUBCELLULAR LOCATION: [Interleukin-6 receptor subunit alpha]: Cell membrane {ECO:0000250|UniProtKB:P22272}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Soluble interleukin-6 receptor subunit alpha]: Secreted {ECO:0000250|UniProtKB:P22272}.
| null | null | null | null | null |
FUNCTION: Part of the receptor for interleukin 6. Binds to IL6 with low affinity, but does not transduce a signal. Signal activation necessitate an association with IL6ST. Activation leads to the regulation of the immune response, acute-phase reactions and hematopoiesis. The interaction with membrane-bound IL6R and IL6ST stimulates 'classic signaling', the restricted expression of the IL6R limits classic IL6 signaling to only a few tissues such as the liver and some cells of the immune system. Whereas the binding of IL6 and soluble IL6R to IL6ST stimulates 'trans-signaling'. Alternatively, 'cluster signaling' occurs when membrane-bound IL6:IL6R complexes on transmitter cells activate IL6ST receptors on neighboring receiver cells. {ECO:0000250|UniProtKB:P22272}.; FUNCTION: [Interleukin-6 receptor subunit alpha]: Signaling via the membrane-bound IL6R is mostly regenerative and anti-inflammatory. Drives naive CD4(+) T cells to the Th17 lineage, through 'cluster signaling' by dendritic cells. {ECO:0000250|UniProtKB:P22272}.; FUNCTION: [Soluble interleukin-6 receptor subunit alpha]: Soluble form of IL6 receptor (sIL6R) that acts as an agonist of IL6 activity (By similarity). The IL6:sIL6R complex (hyper-IL6) binds to IL6ST/gp130 on cell surfaces and induces signaling also on cells that do not express membrane-bound IL6R in a process called IL6 'trans-signaling'. sIL6R is causative for the pro-inflammatory properties of IL6 and an important player in the development of chronic inflammatory diseases. In complex with IL6, is required for induction of VEGF production (By similarity). Plays a protective role during liver injury, being required for maintenance of tissue regeneration. 'Trans-signaling' in central nervous system regulates energy and glucose homeostasis (By similarity). {ECO:0000250|UniProtKB:P08887, ECO:0000250|UniProtKB:P22272}.
|
Sus scrofa (Pig)
|
O18805
|
DAXX_CHLAE
|
MATANSIIVLDDDDENEAAAQPGPSHPLPSTASPEAEAPSSSEPHGARGSSSSGGKKCYKLENEKLFQEFLELCKTQTADHPEVVPFLCNRQQRAHSLFLASAEFCNILSRVLSRAQSRPFKLYVYINELCTVLKGHSAKKKLNLAPVATTSNEPSGNNPPTHLSLDPTNAENTASQAPRTRGSRRQIQRLEQLLALYVAEIRRLQERELDLSELDDPDSTYLQEARLKRKLIRLFGRLCELKDCSSLTGRVIKQRIPYRGTRYPKVNRRIERLINKPGPDTFPDYGDVLRAVKKAAARHSLGLPRQQLQLMAQDAFRNVGIRLQEQRHLDLIYNFGCHLTNDYRPGVDPALSYPVLARRLRENRILALIRLDQVISFYAMLQDGGEEGKKKKRRARLHGPSSHSANPPEPSLDSGEGPIGMASQGCPSASRAETDDEDDEESDEEEEEEEEEEEEEATDFEEEEDLEQMQEGQEDDEEEEEEEEAAGKDGDGSPMSSPQISTEKNLEPGKQISRSSGEQQNKVSPLLLSEEPLAPSSIDAESNGEQPEELTLEEESPVSQLFELEIEALPLDTPSFVEMDISFFRKQSEEPFTTVLENGAGMVSSTSFNGGVSPHNWGDSGPPCKKSRKEKKQTGSGPLGNSYVERQRSVHEKNGKKICTLPSPPSPLASLAPVADSSTRVDSPSHGLVTSSLCNPSPAQLSQTPQSQPPRPSTYKTSVATQCDPEEIIVLSDSD
| null | null |
apoptotic process [GO:0006915]; cellular response to cadmium ion [GO:0071276]; cellular response to copper ion [GO:0071280]; cellular response to diamide [GO:0072738]; cellular response to heat [GO:0034605]; cellular response to sodium arsenite [GO:1903936]; cellular response to unfolded protein [GO:0034620]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of gene expression [GO:0010629]; nucleosome assembly [GO:0006334]; regulation of apoptotic process [GO:0042981]; regulation of protein ubiquitination [GO:0031396]
|
chromosome, centromeric region [GO:0000775]; cytosol [GO:0005829]; nucleolus [GO:0005730]; nucleus [GO:0005634]; PML body [GO:0016605]
|
histone binding [GO:0042393]; nuclear androgen receptor binding [GO:0050681]; protein homodimerization activity [GO:0042803]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; transcription coactivator activity [GO:0003713]; transcription corepressor activity [GO:0003714]
|
PF03344;PF20920;
|
1.20.58.2170;1.10.8.810;
|
DAXX family
|
PTM: Sumoylated with SUMO1 on multiple lysine residues. {ECO:0000250}.; PTM: Polyubiquitinated; which is promoted by CUL3 and SPOP and results in proteasomal degradation. Ubiquitinated by MDM2; inducing its degradation. Deubiquitinated by USP7; leading to stabilize it (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UER7}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9UER7}. Nucleus, PML body {ECO:0000250|UniProtKB:Q9UER7}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9UER7}. Chromosome, centromere {ECO:0000250|UniProtKB:Q9UER7}. Note=Dispersed throughout the nucleoplasm, in PML/POD/ND10 nuclear bodies, and in nucleoli. Colocalizes with histone H3.3, ATRX, HIRA and ASF1A at PML-nuclear bodies. Colocalizes with a subset of interphase centromeres, but is absent from mitotic centromeres. Detected in cytoplasmic punctate structures. Translocates from the nucleus to the cytoplasm upon glucose deprivation or oxidative stress. Colocalizes with RASSF1 in the nucleus. Colocalizes with USP7 in nucleoplasma with accumulation in speckled structures. {ECO:0000250|UniProtKB:Q9UER7}.
| null | null | null | null | null |
FUNCTION: Transcription corepressor known to repress transcriptional potential of several sumoylated transcription factors. Down-regulates basal and activated transcription. Its transcription repressor activity is modulated by recruiting it to subnuclear compartments like the nucleolus or PML/POD/ND10 nuclear bodies through interactions with MCSR1 and PML, respectively. Seems to regulate transcription in PML/POD/ND10 nuclear bodies together with PML and may influence TNFRSF6-dependent apoptosis thereby. Inhibits transcriptional activation of PAX3 and ETS1 through direct protein-protein interactions. Modulates PAX5 activity; the function seems to involve CREBBP. Acts as an adapter protein in a MDM2-DAXX-USP7 complex by regulating the RING-finger E3 ligase MDM2 ubiquitination activity. Under non-stress condition, in association with the deubiquitinating USP7, prevents MDM2 self-ubiquitination and enhances the intrinsic E3 ligase activity of MDM2 towards TP53, thereby promoting TP53 ubiquitination and subsequent proteasomal degradation. Upon DNA damage, its association with MDM2 and USP7 is disrupted, resulting in increased MDM2 autoubiquitination and consequently, MDM2 degradation, which leads to TP53 stabilization. Acts as a histone chaperone that facilitates deposition of histone H3.3. Acts as a targeting component of the chromatin remodeling complex ATRX:DAXX which has ATP-dependent DNA translocase activity and catalyzes the replication-independent deposition of histone H3.3 in pericentric DNA repeats outside S-phase and telomeres, and the in vitro remodeling of H3.3-containing nucleosomes. Does not affect the ATPase activity of ATRX but alleviates its transcription repression activity. Upon neuronal activation associates with regulatory elements of selected immediate early genes where it promotes deposition of histone H3.3 which may be linked to transcriptional induction of these genes. Required for the recruitment of histone H3.3:H4 dimers to PML-nuclear bodies (PML-NBs); the process is independent of ATRX and facilitated by ASF1A; PML-NBs are suggested to function as regulatory sites for the incorporation of newly synthesized histone H3.3 into chromatin. Proposed to mediate activation of the JNK pathway and apoptosis via MAP3K5 in response to signaling from TNFRSF6 and TGFBR2. Interaction with HSPB1/HSP27 may prevent interaction with TNFRSF6 and MAP3K5 and block DAXX-mediated apoptosis. In contrast, in lymphoid cells JNC activation and TNFRSF6-mediated apoptosis may not involve DAXX (By similarity). {ECO:0000250}.
|
Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops)
|
O18823
|
AOAH_RABIT
|
MKSPWRILVVSPLLLLPLHSSTSRAHDNQPGTIRSDHYTCVGCVLVVSVIEQLAQVHNSTVQASMERLCSYLPEEWVLKTACYMMVHVFGADIIKLFDKDVNADVVCHTLEFCKQEPGQPLCHLYPLPKESWKFTLEKARHIVKQSPIMKYTRSGAGICSLPFLAKICQKIKLAIKNSVPIKDVDSDKYSIFPTLRGYHWRGRDCNDSDKTVYPGRRPDNWDAHRDSNCNGIWGVDPKDGIPYEKKFCEGSQPRGIILLGDSAGAHFHIPPEWLTVSQMSVNSFLNLPTAVTNELDWPQLSGTTGFLDSASKIKENSIYLRLRKRNRCNHRDYQNISKNGASSRNVKSLIESLSRNQLLDHPAIVIYAMIGNDVCNGRKTDPVSAMTTPEQLYANVLKMLEALNSHLPTGSHVILYGLAHGAFLWDTLHSRYHPLGQLNKDVTYTQLYSFLGCLQVSPCPGWMSANETLRALTSERAQQLSETLRKIAASKKFTNFNLFYLDFAFQEVVEEWQKMGGQPWELIEAVDGFHPNEVALLLFADQLWEKVQRQWPDVLGKENPFNPQIEEVFGDQGGH
|
3.1.1.77
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:29343645}; Note=Binds 3 Ca(2+) ions per subunit. The calcium ions probably have a structural role. {ECO:0000269|PubMed:29343645};
|
fatty acid metabolic process [GO:0006631]; lipopolysaccharide catabolic process [GO:0009104]; negative regulation of inflammatory response [GO:0050728]
|
cytoplasmic vesicle [GO:0031410]; extracellular region [GO:0005576]
|
acyloxyacyl hydrolase activity [GO:0050528]; calcium ion binding [GO:0005509]
|
PF00657;PF20825;
|
1.10.225.10;3.40.50.1110;
| null |
PTM: Cleaved into a large and a small subunit. {ECO:0000250|UniProtKB:P28039}.; PTM: The small subunit is N-glycosylated. {ECO:0000250|UniProtKB:P28039}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P28039}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:P28039}. Note=Detected in urine. {ECO:0000250|UniProtKB:O35298}.
|
CATALYTIC ACTIVITY: Reaction=a 3-(acyloxy)acyl derivative of bacterial toxin + H2O = 3-hydroxyacyl derivative of bacterial toxin + a fatty acid + H(+); Xref=Rhea:RHEA:12032, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:136853, ChEBI:CHEBI:140675; EC=3.1.1.77; Evidence={ECO:0000250|UniProtKB:P28039};
| null | null | null | null |
FUNCTION: Removes the secondary (acyloxyacyl-linked) fatty acyl chains from the lipid A region of bacterial lipopolysaccharides (LPS). By breaking down LPS, terminates the host response to bacterial infection and prevents prolonged and damaging inflammatory responses. In peritoneal macrophages, seems to be important for recovery from a state of immune tolerance following infection by Gram-negative bacteria. {ECO:0000250|UniProtKB:O35298}.
|
Oryctolagus cuniculus (Rabbit)
|
O18836
|
GDF8_BOVIN
|
MQKLQISVYIYLFMLIVAGPVDLNENSEQKENVEKEGLCNACLWRENTTSSRLEAIKIQILSKLRLETAPNISKDAIRQLLPKAPPLLELIDQFDVQRDASSDGSLEDDDYHARTETVITMPTESDLLTQVEGKPKCCFFKFSSKIQYNKLVKAQLWIYLRPVKTPATVFVQILRLIKPMKDGTRYTGIRSLKLDMNPGTGIWQSIDVKTVLQNWLKQPESNLGIEIKALDENGHDLAVTFPEPGEDGLTPFLEVKVTDTPKRSRRDFGLDCDEHSTESRCCRYPLTVDFEAFGWDWIIAPKRYKANYCSGECEFVFLQKYPHTHLVHQANPRGSAGPCCTPTKMSPINMLYFNGEGQIIYGKIPAMVVDRCGCS
| null | null |
myoblast migration involved in skeletal muscle regeneration [GO:0014839]; negative regulation of fibroblast proliferation [GO:0048147]; positive regulation of lamellipodium assembly [GO:0010592]; positive regulation of macrophage chemotaxis [GO:0010759]
|
extracellular space [GO:0005615]
|
cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]
|
PF00019;PF00688;
|
2.60.120.970;2.10.90.10;
|
TGF-beta family
|
PTM: Synthesized as large precursor molecule that undergoes proteolytic cleavage to generate an N-terminal propeptide and a disulfide linked C-terminal dimer, which is the biologically active molecule. The circulating form consists of a latent complex of the C-terminal dimer and other proteins, including its propeptide, which maintain the C-terminal dimer in a latent, inactive state. Ligand activation requires additional cleavage of the prodomain by a tolloid-like metalloproteinase. {ECO:0000250|UniProtKB:O08689}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O08689}.
| null | null | null | null | null |
FUNCTION: Acts specifically as a negative regulator of skeletal muscle growth. {ECO:0000250|UniProtKB:O08689}.
|
Bos taurus (Bovine)
|
O18839
|
KCNJ2_PIG
|
MGSVRTNRYSIVSSEEDGMKLATLAVANGFGNGKSKVHTRQQCRSRFVKKDGHCNVQFINVGEKGQRYLADIFTTCVDIRWRWMLVIFCLAFVLSWLFFGCVFWLIALLHGDLDASKESKACVSEVNSFTAAFLFSIETQTTIGYGFRCVTDECPIAVFMVVFQSIVGCIIDAFIIGAVMAKMAKPKKRNETLVFSHNAVIAMRDGKLCLMWRVGNLRKSHLVEAHVRAQLLKSRITSEGEYIPLDQIDINVGFDSGIDRIFLVSPITIVHEIDEDSPLYDLSKQDIDNADFEIVVILEGMVEATAMTTQCRSSYLANEILWGHRYEPVLFEEKHYYKVDYSRFHKTYEVPNTPLCSARDLAEKKYILSNANSFCYENEVALTSKEEDDSENGVPESTSTDTPPDIDLHNQASVPLEPRPLRRESEI
| null | null |
cardiac muscle cell action potential involved in contraction [GO:0086002]; magnesium ion transport [GO:0015693]; potassium ion import across plasma membrane [GO:1990573]; potassium ion transport [GO:0006813]; protein homotetramerization [GO:0051289]; regulation of heart rate by cardiac conduction [GO:0086091]; regulation of membrane repolarization [GO:0060306]; regulation of monoatomic ion transmembrane transport [GO:0034765]; regulation of skeletal muscle contraction via regulation of action potential [GO:0014861]; relaxation of cardiac muscle [GO:0055119]; relaxation of skeletal muscle [GO:0090076]
|
membrane [GO:0016020]; plasma membrane [GO:0005886]; voltage-gated potassium channel complex [GO:0008076]
|
identical protein binding [GO:0042802]; inward rectifier potassium channel activity [GO:0005242]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; voltage-gated potassium channel activity involved in cardiac muscle cell action potential repolarization [GO:0086008]
|
PF01007;PF17655;PF08466;
|
1.10.287.70;2.60.40.1400;
|
Inward rectifier-type potassium channel (TC 1.A.2.1) family, KCNJ2 subfamily
|
PTM: S-nitrosylation increases the open probability and inward rectifying currents. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Membrane; Lipid-anchor {ECO:0000250|UniProtKB:P63252}.
| null | null | null | null | null |
FUNCTION: Probably participates in establishing action potential waveform and excitability of neuronal and muscle tissues. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by extracellular barium and cesium (By similarity). {ECO:0000250}.
|
Sus scrofa (Pig)
|
O18840
|
ACTB_CANLF
|
MDDDIAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF
|
3.6.4.-
| null |
axonogenesis [GO:0007409]; cell motility [GO:0048870]
|
actin cytoskeleton [GO:0015629]; actin filament [GO:0005884]; axon [GO:0030424]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; dense body [GO:0097433]; focal adhesion [GO:0005925]; membrane [GO:0016020]; NuA4 histone acetyltransferase complex [GO:0035267]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]; synapse [GO:0045202]
|
ATP binding [GO:0005524]; hydrolase activity [GO:0016787]; protein kinase binding [GO:0019901]; structural constituent of postsynaptic actin cytoskeleton [GO:0098973]
|
PF00022;
|
3.30.420.40;
|
Actin family
|
PTM: [Actin, cytoplasmic 1]: N-terminal cleavage of acetylated methionine of immature cytoplasmic actin by ACTMAP. {ECO:0000250|UniProtKB:P60709}.; PTM: ISGylated. {ECO:0000250|UniProtKB:P60709}.; PTM: Oxidation of Met-44 and Met-47 by MICALs (MICAL1, MICAL2 or MICAL3) to form methionine sulfoxide promotes actin filament depolymerization. MICAL1 and MICAL2 produce the (R)-S-oxide form. The (R)-S-oxide form is reverted by MSRB1 and MSRB2, which promote actin repolymerization. {ECO:0000250|UniProtKB:P60710}.; PTM: Monomethylation at Lys-84 (K84me1) regulates actin-myosin interaction and actomyosin-dependent processes. Demethylation by ALKBH4 is required for maintaining actomyosin dynamics supporting normal cleavage furrow ingression during cytokinesis and cell migration. {ECO:0000250|UniProtKB:P60709}.; PTM: [Actin, cytoplasmic 1, N-terminally processed]: N-terminal acetylation by NAA80 affects actin filament depolymerization and elongation, including elongation driven by formins. In contrast, filament nucleation by the Arp2/3 complex is not affected. {ECO:0000250|UniProtKB:P60709}.; PTM: Methylated at His-73 by SETD3 (By similarity). Methylation at His-73 is required for smooth muscle contraction of the laboring uterus during delivery (By similarity). {ECO:0000250|UniProtKB:P60709, ECO:0000250|UniProtKB:P60710}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P60709}. Nucleus {ECO:0000250|UniProtKB:P60709}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. {ECO:0000250|UniProtKB:P60709}.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P68137};
| null | null | null | null |
FUNCTION: Actin is a highly conserved protein that polymerizes to produce filaments that form cross-linked networks in the cytoplasm of cells. Actin exists in both monomeric (G-actin) and polymeric (F-actin) forms, both forms playing key functions, such as cell motility and contraction. In addition to their role in the cytoplasmic cytoskeleton, G- and F-actin also localize in the nucleus, and regulate gene transcription and motility and repair of damaged DNA. Part of the ACTR1A/ACTB filament around which the dynactin complex is built. The dynactin multiprotein complex activates the molecular motor dynein for ultra-processive transport along microtubules (By similarity). {ECO:0000250|UniProtKB:P60709, ECO:0000250|UniProtKB:Q6QAQ1}.
|
Canis lupus familiaris (Dog) (Canis familiaris)
|
O18866
|
KCMA1_PIG
|
MSSNIHANHLSLDASSSSSSSSSSSSSSSSSSSSVHEPKMDALIIPVTMEVPCDSRGQRMWWAFLASSMVTFFGGLFIILLWRTLKYLWTVCCHCGGKTKEAQKINNGASQADGTLKPVDEKEEVVAAEVGWMTSVKDWAGVMISAQTLTGRVLVVLVFALSIGALVIYFIDSSNPIESCQNFYKDFTLQIDMAFNVFFLLYFGLRFIAANDKLWFWLEVNSVVDFFTVPPVFVSVYLNRSWLGLRFLRALRLIQFSEILQFLNILKTSNSIKLVNLLSIFISTWLTAAGFIHLVENSGDPWENFQNNQALTYWECVYLLMVTMSTVGYGDVYAKTTLGRLFMVFFILGGLAMFASYVPEIIELIGNRKKYGGSYSAVSGRKHIVVCGHITLESVSNFLKDFLHKDRDDVNVEIVFLHNISPNLELEALFKRHFTQVEFYQGSVLNPHDLARVKIESADACLILANKYCADPDAEDASNIMRVISIKNYHPKIRIITQMLQYHNKAHLLNIPSWNWKEGDDAICLAELKLGFIAQSCLAQGLSTMLANLFSMRSFIKIEEDTWQKYYLEGVSNEMYTEYLSSAFVGLSFPTVCELCFVKLKLLMIAIEYKSANRESRILINPGNHLKIQEGTLGFFIASDAKEVKRAFFYCKACHDDITDPKRIKKCGCKRLEDEQPSTLSPKKKQRNGGMRNSPSSSPKLMRHDPLLIPGNDQIDNMDSNVKKYDSTGMFHWCAPKEIEKVILTRSEAAMTVLSGHVVVCIFGDVSSALIGLRNLVMPLRASNFHYHELKHIVFVGSIEYLKREWETLHNFPKVSILPGTPLSRADLRAVNINLCDMCVILSANQNNIDDTSLQDKECILASLNIKSMQFDDSIGVLQANSQGFTPPGMDRSSPDNSPVHGMLRQPSITTGVNIPIITELVNDTNVQFLDQDDDDDPDTELYLTQPFACGTAFAVSVLDSLMSATYFNDNILTLIRTLVTGGATPELEALIAEENALRGGYSTPQTLANRDRCRVAQLALLDGPFADLGDGGCYGDLFCKALKTYNMLCFGIYRLRDAHLSTPSQCTKRYVITNPPYEFELVPTDLIFCLMQFDHNAGQSRASLSHSSHSSQSSSKKSSSVHSIPSTANRQNRPKSRESRDKQKYVQEERL
| null | null |
positive regulation of membrane hyperpolarization [GO:1902632]; potassium ion transmembrane transport [GO:0071805]; regulation of membrane potential [GO:0042391]; relaxation of vascular associated smooth muscle [GO:0060087]; vasodilation [GO:0042311]
|
monoatomic ion channel complex [GO:0034702]; postsynaptic membrane [GO:0045211]
|
large conductance calcium-activated potassium channel activity [GO:0060072]; metal ion binding [GO:0046872]
|
PF03493;PF00520;PF21014;
|
1.10.287.70;3.40.50.720;
|
Potassium channel family, Calcium-activated (TC 1.A.1.3) subfamily, KCa1.1/KCNMA1 sub-subfamily
|
PTM: Phosphorylated (Probable). Phosphorylation by kinases such as PKA and/or PKG. In smooth muscles, phosphorylation affects its activity (By similarity). {ECO:0000250|UniProtKB:Q12791, ECO:0000305}.; PTM: Palmitoylation by ZDHHC22 and ZDHHC23 within the intracellular linker between the S0 and S1 transmembrane domains regulates localization to the plasma membrane. Depalmitoylated by LYPLA1 and LYPLAL1, leading to retard exit from the trans-Golgi network (By similarity). {ECO:0000250|UniProtKB:Q12791}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q12791}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; Evidence={ECO:0000250|UniProtKB:Q12791};
| null | null | null | null |
FUNCTION: Potassium channel activated by both membrane depolarization or increase in cytosolic Ca(2+) that mediates export of K(+). It is also activated by the concentration of cytosolic Mg(2+). Its activation dampens the excitatory events that elevate the cytosolic Ca(2+) concentration and/or depolarize the cell membrane. It therefore contributes to repolarization of the membrane potential. Plays a key role in controlling excitability in a number of systems, such as regulation of the contraction of smooth muscle, the tuning of hair cells in the cochlea, regulation of transmitter release, and innate immunity. In smooth muscles, its activation by high level of Ca(2+), caused by ryanodine receptors in the sarcoplasmic reticulum, regulates the membrane potential. In cochlea cells, its number and kinetic properties partly determine the characteristic frequency of each hair cell and thereby helps to establish a tonotopic map. Kinetics of KCNMA1 channels are determined by alternative splicing, phosphorylation status and its combination with modulating beta subunits. Highly sensitive to both iberiotoxin (IbTx) and charybdotoxin (CTX) (By similarity). {ECO:0000250|UniProtKB:Q12791}.
|
Sus scrofa (Pig)
|
O18867
|
KCMA1_MACMU
|
MSSNIHANHLSLDASSSSSSSSSSSSSSSSSSSVHEPKMDALIIPVTMEVPCDSRGQRMWWAFLASSMVTFFGGLFIILLWRTLKYLWTVCCHCGGKTKEAQKINNGSSQADGTLKPVDEKEEAVAAEVGWMTSVKDWAGVMISAQTLTGRVLVVLVFALSIGALVIYFIDSSNPIESCQNFYKDFTLQIDMAFNVFFLLYFGLRFIAANDKLWFWLEVNSVVDFFTVPPVFVSVYLNRSWLGLRFLRALRLIQFSEILQFLNILKTSNSIKLVNLLSIFISTWLTAAGFIHLVENSGDPWENFQNNQALTYWECVYLLMVTMSTVGYGDVYAKTTLGRLFMVFFILGGLAMFASYVPEIIELIGNRKKYGGSYSAVSGRKHIVVCGHITLESVSNFLKDFLHKDRDDVNVEIVFLHNISPNLELEALFKRHFTQVEFYQGSVLNPHDLARVKIESADACLILANKYCADPDAEDASNIMRVISIKNYHPKIRIITQMLQYHNKAHLLNIPSWNWKEGDDAICLAELKLGFIAQSCLAQGLSTMLANLFSMRSFIKIEEDTWQKYYLEGVSNEMYTEYLSSAFVGLSFPTVCELCFVKLKLLMIAIEYKSANRESRILINPGNHLKIQEGTLGFFIASDAKEVKRAFFYCKACHDDITDPKRIKKCGCKRLEDEQPSTLSPKKKQRNGGMRNSPNSSPKLMRHDPLLIPGNDQIDNMDSNVKKYDSTGMFHWCAPKEIEKVILTRSEAAMTVLSGHVVVCIFGDVSSALIGLRNLVMPLRASNFHYHELKHIVFVGSIEYLKREWETLHNFPKVSILPGTPLSRADLRAVNINLCDMCVILSANQNNIDDTSLQDKECILASLNIKSMQFDDSIGVLQANSQGFTPPGMDRSSPDNSPVHGMLRQPSITTGVNIPIITELVNDTNVQFLDQDDDDDPDTELYLTQPFACGTAFAVSVLDSLMSATYFNDNILTLIRTLVTGGATPELEALIAEENALRGGYSTPQTLANRDRCRVAQLALLDGPFADLGDGGCYGDLFCKALKTYNMLCFGIYRLRDAHLSTPSQCTKRYVITNPPYEFELVPTDLIFCLMQFDHNAGQSRASLSHSSHSSQSSSKKSSSVHSIPSTANRQNRPKSRESRDKQKYVQEERL
| null | null |
potassium ion transmembrane transport [GO:0071805]; regulation of membrane potential [GO:0042391]; vasodilation [GO:0042311]
|
monoatomic ion channel complex [GO:0034702]; postsynaptic membrane [GO:0045211]
|
large conductance calcium-activated potassium channel activity [GO:0060072]; metal ion binding [GO:0046872]
|
PF03493;PF00520;PF21014;
|
1.10.287.70;3.40.50.720;
|
Potassium channel family, Calcium-activated (TC 1.A.1.3) subfamily, KCa1.1/KCNMA1 sub-subfamily
|
PTM: Phosphorylated (Probable). Phosphorylation by kinases such as PKA and/or PKG. In smooth muscles, phosphorylation affects its activity (By similarity). {ECO:0000250|UniProtKB:Q12791, ECO:0000305}.; PTM: Palmitoylation by ZDHHC22 and ZDHHC23 within the intracellular linker between the S0 and S1 transmembrane domains regulates localization to the plasma membrane. Depalmitoylated by LYPLA1 and LYPLAL1, leading to retard exit from the trans-Golgi network (By similarity). {ECO:0000250|UniProtKB:Q12791}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q12791}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; Evidence={ECO:0000250|UniProtKB:Q12791};
| null | null | null | null |
FUNCTION: Potassium channel activated by both membrane depolarization or increase in cytosolic Ca(2+) that mediates export of K(+). It is also activated by the concentration of cytosolic Mg(2+). Its activation dampens the excitatory events that elevate the cytosolic Ca(2+) concentration and/or depolarize the cell membrane. It therefore contributes to repolarization of the membrane potential. Plays a key role in controlling excitability in a number of systems, such as regulation of the contraction of smooth muscle, the tuning of hair cells in the cochlea, regulation of transmitter release, and innate immunity. In smooth muscles, its activation by high level of Ca(2+), caused by ryanodine receptors in the sarcoplasmic reticulum, regulates the membrane potential. In cochlea cells, its number and kinetic properties partly determine the characteristic frequency of each hair cell and thereby helps to establish a tonotopic map. Kinetics of KCNMA1 channels are determined by alternative splicing, phosphorylation status and its combination with modulating beta subunits. Highly sensitive to both iberiotoxin (IbTx) and charybdotoxin (CTX) (By similarity). {ECO:0000250|UniProtKB:Q12791}.
|
Macaca mulatta (Rhesus macaque)
|
O18868
|
KCNB1_PIG
|
MPAGMTKHGSRSTSSLPPEPMEIVRSKACSRRVRLNVGGLAHEVLWRTLDRLPRTRLGKLRDCNTHDSLLEVCDDYSLDDNEYFFDRHPGAFTSILNFYRTGRLHMMEEMCALSFSQELDYWGIDEIYLESCCQARYHQKKEQMNEELKREAETLREREGEEFDNTCCAEKRKKLWDLLEKPNSSVAAKILAIISIMFIVLSTIALSLNTLPELQSLDEFGQTTDNPQLAHVEAVCIAWFTMEYLLRFLSSPKKWKFFKGPLNAIDLLAILPYYVTIFLTESNKSVLQFQNVRRVVQIFRIMRILRILKLARHSTGLQSLGFTLRRSYNELGLLILFLAMGIMIFSSLVFFAEKDEDDTKFKSIPASFWWATITMTTVGYGDIYPKTLLGKIVGGLCCIAGVLVIALPIPIIVNNFSEFYKEQKRQEKAIKRREALERAKRNGSIVSMNMKDAFPRSIEMMDIVVEKNVENMGQKDKVQDNHLSPNKWKWTKRTLSETSSSKSFETKEQGSPEKARSSSSPQHLNVQQLEDMYNKMAKTQSQPILNTKESATQSKPKEELEMESIPSPVAPLPTRTEGVIDMRSMSSIDSFISCATDFPEATRFSHSPLASLPSKSGGSMAPEVGWRGALGATGGRFVEANPTPDASHHSTFFIESPKSSMKTTNPLKLRALKVNFMEGDPSPLVPVLGMYHDPLRNRGGAAAAVAGLECATLLDRPVLSPESSIYTTASARTPPRSPEKHTAIAFNFEAGIHQYIDADTDDEGQVLYSVDSSPPKSLHGSTSPKFSIGTRSEKNHFESSPLPTSPKFLRQNCIYSTEALTGKAPSGQEKCKLENHISPDVRVLPGGGAHGSTRDQSI
| null | null |
action potential [GO:0001508]; cellular response to glucose stimulus [GO:0071333]; cellular response to nutrient levels [GO:0031669]; glucose homeostasis [GO:0042593]; glutamate receptor signaling pathway [GO:0007215]; negative regulation of insulin secretion [GO:0046676]; positive regulation of calcium ion-dependent exocytosis [GO:0045956]; positive regulation of catecholamine secretion [GO:0033605]; positive regulation of long-term synaptic depression [GO:1900454]; positive regulation of norepinephrine secretion [GO:0010701]; positive regulation of protein targeting to membrane [GO:0090314]; potassium ion transmembrane transport [GO:0071805]; potassium ion transport [GO:0006813]; protein homooligomerization [GO:0051260]; protein localization to plasma membrane [GO:0072659]; regulation of action potential [GO:0098900]; regulation of motor neuron apoptotic process [GO:2000671]; vesicle docking involved in exocytosis [GO:0006904]
|
axon [GO:0030424]; dendrite [GO:0030425]; dendrite membrane [GO:0032590]; lateral plasma membrane [GO:0016328]; neuronal cell body membrane [GO:0032809]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; sarcolemma [GO:0042383]; voltage-gated potassium channel complex [GO:0008076]
|
delayed rectifier potassium channel activity [GO:0005251]; protein heterodimerization activity [GO:0046982]
|
PF02214;PF00520;PF03521;
|
1.10.287.70;1.20.120.350;
|
Potassium channel family, B (Shab) (TC 1.A.1.2) subfamily, Kv2.1/KCNB1 sub-subfamily
|
PTM: Phosphorylated. Differential C-terminal phosphorylation on a subset of serines allows graded activity-dependent regulation of channel gating in hippocampal neurons. Ser-607 and Tyr-128 are significant sites of voltage-gated regulation through phosphorylation/dephosphorylation activities. Tyr-128 can be phosphorylated by Src and dephosphorylated by cytoplasmic form of the phosphatase PTPRE. CDK5-induced Ser-607 phosphorylation increases in response to acute blockade of neuronal activity. Phosphorylated on Tyr-128 by Src and on Ser-805 by MAPK14/P38MAPK; phosphorylations are necessary and sufficient for an increase in plasma membrane insertion, apoptotic potassium current surge and completion of the neuronal cell death program. Phosphorylated on Ser-520, Ser-607, Ser-656 and Ser-805 by CDK5; phosphorylation is necessary for KCNB1 channel clustering formation. The Ser-607 phosphorylation state differs between KCNB1-containing clusters on the proximal and distal portions of the axon initial segment (AIS). Highly phosphorylated on serine residues in the C-terminal cytoplasmic tail in resting neurons. Phosphorylated in pancreatic beta cells in response to incretin hormones stimulation in a PKA- and RPS6KA5/MSK1-dependent signaling pathway, promoting beta cell survival. Phosphorylation on Ser-567 is reduced during postnatal development with low levels at P2 and P5; levels then increase to reach adult levels by P14. Phosphorylation on Ser-457, Ser-541, Ser-567, Ser-607, Ser-656 and Ser-720 as well as the N-terminal Ser-15 are sensitive to calcineurin-mediated dephosphorylation contributing to the modulation of the voltage-dependent gating properties. Dephosphorylation by phosphatase PTPRE confers neuroprotection by its inhibitory influence on the neuronal apoptotic potassium current surge in a Zn(2+)-dependent manner. Dephosphorylated at Ser-607 by protein phosphatase PPP1CA. Hypoxia-, seizure- or glutamate-induced neuronal activity promote calcium/calcineurin-dependent dephosphorylation resulting in a loss of KCNB1-containing clustering and enhanced channel activity. In response to brain ischemia, Ser-567 and Ser-607 are strongly dephosphorylated while Ser-457 and Ser-720 are less dephosphorylated. In response to brain seizures, phosphorylation levels on Ser-567 and Ser-607 are greatly reduced. Phosphorylated/dephosphorylated by Src or FYN tyrosine-protein kinases and tyrosine phosphatase PTPRE in primary Schwann cells and sciatic nerve tissue. Phosphorylation at Ser-593 of the FFAT motif activates interaction with MOSPD2, VAPA and VAPB (By similarity). {ECO:0000250|UniProtKB:P15387, ECO:0000250|UniProtKB:Q03717, ECO:0000250|UniProtKB:Q14721}.; PTM: Acetylated. Acetylation occurs in pancreatic beta cells in response to stimulation by incretin hormones in a histone acetyltransferase (HAT)/histone deacetylase (HDAC)-dependent signaling pathway, promoting beta cell survival. {ECO:0000250|UniProtKB:P15387}.; PTM: Sumoylated on Lys-475, preferentially with SUMO1; sumoylation induces a positive shift in the voltage-dependence of activation and inhibits channel activity. Sumoylation increases the frequency of repetitive action potential firing at the cell surface of hippocampal neurons and decreases its frequency in pancreatic beta cells. Desumoylated by SENP1. {ECO:0000250|UniProtKB:P15387, ECO:0000250|UniProtKB:Q14721}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P15387}. Perikaryon {ECO:0000250|UniProtKB:P15387}. Cell projection, axon {ECO:0000250|UniProtKB:P15387}. Cell projection, dendrite {ECO:0000250|UniProtKB:P15387}. Membrane; Multi-pass membrane protein. Postsynaptic cell membrane {ECO:0000250|UniProtKB:P15387}. Synapse {ECO:0000250|UniProtKB:P15387}. Synapse, synaptosome {ECO:0000250|UniProtKB:P15387}. Lateral cell membrane {ECO:0000250|UniProtKB:P15387}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P15387}. Note=Localizes to high-density somatodendritic clusters and non-clustered sites on the surface of neocortical and hippocampal pyramidal neurons in a cortical actin cytoskeleton-dependent manner. Localizes also to high-density clusters in the axon initial segment (AIS), at ankyrin-G-deficient sites, on the surface of neocortical and hippocampal pyramidal neurons. KCNB1-containing AIS clusters localize either in close apposition to smooth endoplasmic reticulum cisternal organelles or with GABA-A receptor-containing synapses of hippocampal and cortical pyramidal neurons, respectively. Localizes to high-density clusters on the cell surface of atrial and ventricular myocytes and at the lateral plasma membrane in epithelial cells. Localizes both to the axial and transverse tubules (T tubule) and sarcolemma in ventricular myocytes. Associated with lipid raft domains. In cortical neurons, apoptotic injuries induce de novo plasma membrane insertion in a SNARE-dependent manner causing an apoptotic potassium current surge. {ECO:0000250|UniProtKB:P15387, ECO:0000250|UniProtKB:Q03717, ECO:0000250|UniProtKB:Q14721}.
| null |
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Note=Homotetrameric channels expressed in xenopus oocytes or in mammalian non-neuronal cells display delayed-rectifier voltage-dependent potassium currents which are activated during membrane depolarization, i.e within a risetime of more than 20 msec. After that, inactivate very slowly, i.e within more than 5 sec. Their activation requires low threshold potentials at about -20 to -30 mV with a midpoint activation at about 10 mV. For inactivation, the voltage at half-maximal amplitude is about -20 mV. The time constant for recovery after inactivation is about 1.6 sec. Channels have an unitary conductance of about 8 pS. The voltage-dependence of activation and inactivation and other channel characteristics vary depending on the experimental conditions, the expression system, the presence or absence of ancillary subunits and post-translational modifications. {ECO:0000305|PubMed:10414301, ECO:0000305|PubMed:15858231};
| null | null | null |
FUNCTION: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain, but also in the pancreas and cardiovascular system. Contributes to the regulation of the action potential (AP) repolarization, duration and frequency of repetitive AP firing in neurons, muscle cells and endocrine cells and plays a role in homeostatic attenuation of electrical excitability throughout the brain. Also plays a role in the regulation of exocytosis independently of its electrical function. Forms tetrameric potassium-selective channels through which potassium ions pass in accordance with their electrochemical gradient. The channel alternates between opened and closed conformations in response to the voltage difference across the membrane. Homotetrameric channels mediate a delayed-rectifier voltage-dependent outward potassium current that display rapid activation and slow inactivation in response to membrane depolarization. Can form functional homotetrameric and heterotetrameric channels that contain variable proportions of KCNB2; channel properties depend on the type of alpha subunits that are part of the channel. Can also form functional heterotetrameric channels with other alpha subunits that are non-conducting when expressed alone, such as KCNF1, KCNG1, KCNG3, KCNG4, KCNH1, KCNH2, KCNS1, KCNS2, KCNS3 and KCNV1, creating a functionally diverse range of channel complexes (By similarity). Heterotetrameric channel activity formed with KCNS3 show increased current amplitude with the threshold for action potential activation shifted towards more negative values in hypoxic-treated pulmonary artery smooth muscle cells. Channel properties are also modulated by cytoplasmic ancillary beta subunits, such as AMIGO1, KCNE1, KCNE2 and KCNE3, slowing activation and inactivation rate of the delayed rectifier potassium channels. In vivo, membranes probably contain a mixture of heteromeric potassium channel complexes, making it difficult to assign currents observed in intact tissues to any particular potassium channel family member. Major contributor to the delayed-rectifier voltage-gated potassium current in neurons of the central nervous system, sympathetic ganglion neurons, neuroendocrine cells, pancreatic beta cells, cardiomyocytes and smooth muscle. Mediates the major part of the somatodendritic delayed-rectifier potassium current in hippocampal and cortical pyramidal neurons and sympathetic superior cervical ganglion (CGC) neurons that acts to slow down periods of firing, especially during high frequency stimulation. Plays a role in the induction of long-term potentiation (LTP) of neuron excitability in the CA3 layer of the hippocampus. Contributes to the regulation of the glucose-induced amplitude and duration of action potentials in pancreatic beta-cells, hence limiting calcium influx and insulin secretion. Plays a role in the regulation of resting membrane potential and contraction in hypoxia-treated pulmonary artery smooth muscle cells. May contribute to the regulation of the duration of both the action potential of cardiomyocytes and the heart ventricular repolarization QT interval. Contributes to the pronounced pro-apoptotic potassium current surge during neuronal apoptotic cell death in response to oxidative injury. May confer neuroprotection in response to hypoxia/ischemic insults by suppressing pyramidal neurons hyperexcitability in hippocampal and cortical regions. Promotes trafficking of KCNG3, KCNH1 and KCNH2 to the cell surface membrane, presumably by forming heterotetrameric channels with these subunits. Plays a role in the calcium-dependent recruitment and release of fusion-competent vesicles from the soma of neurons, neuroendocrine and glucose-induced pancreatic beta cells by binding key components of the fusion machinery in a pore-independent manner. {ECO:0000250|UniProtKB:P15387, ECO:0000250|UniProtKB:Q03717, ECO:0000250|UniProtKB:Q14721}.
|
Sus scrofa (Pig)
|
O18896
|
SOX9_PIG
|
MNLLDPFMKMTDEQEKGLSGAPSPTMSEGSRGSPCPSGSGSDTENTRPQENTFPKGEPDLKKESEEDKFPVCIREAVSQVLKGYDWTLVPMPVRVNGSSKNKPHVKRPMNAFMVWAQAARRKLADQYPHLHNAELSKTLGKLWRLLNESEKRPFVEEAERLRVQHKKDHPDYKYQPRRRKSVKNGQAEAEEATEQTHISPNAIFKALQADSPHSSSGMSEVHSPGEHSGQSQGPPTPPTTPKTDVQPGKADLKREGRPLPEGGRQPPIDFRDVDIGELSSDVISNIETFDVNEFDQYLPPNGHPGVPATHGQVTYTGSYGISSTAATPAGAGHVWMSKQQAPPPPPHPPQQPPPVPQAPAQPQAALPQQPQAPPQQPQAHTLTTLSSEPGQSQRTHIKTEQLSPSHYSEQQQHSPQQIAYSPFNLPHYSPSYPPITRSQYDYTDHQNSGSYYSHARSQGSVLYSTFTYMNPAHGPMYTPIADTSGVPSIPQTHSPQHWEQPVYTQLTRP
| null | null |
cAMP-mediated signaling [GO:0019933]; cartilage condensation [GO:0001502]; cartilage development [GO:0051216]; cell fate specification [GO:0001708]; cellular response to BMP stimulus [GO:0071773]; cellular response to epidermal growth factor stimulus [GO:0071364]; cellular response to heparin [GO:0071504]; cellular response to mechanical stimulus [GO:0071260]; cellular response to transforming growth factor beta stimulus [GO:0071560]; chondrocyte differentiation [GO:0002062]; chondrocyte differentiation involved in endochondral bone morphogenesis [GO:0003413]; chondrocyte hypertrophy [GO:0003415]; chromatin remodeling [GO:0006338]; cochlea morphogenesis [GO:0090103]; endocardial cushion morphogenesis [GO:0003203]; epidermal growth factor receptor signaling pathway [GO:0007173]; epithelial cell proliferation involved in prostatic bud elongation [GO:0060517]; epithelial to mesenchymal transition [GO:0001837]; ERK1 and ERK2 cascade [GO:0070371]; growth plate cartilage chondrocyte growth [GO:0003430]; hair follicle development [GO:0001942]; heart development [GO:0007507]; heart valve development [GO:0003170]; heart valve morphogenesis [GO:0003179]; intestinal epithelial structure maintenance [GO:0060729]; male germ-line sex determination [GO:0019100]; male gonad development [GO:0008584]; metanephric nephron tubule formation [GO:0072289]; morphogenesis of a branching epithelium [GO:0061138]; morphogenesis of an epithelium [GO:0002009]; negative regulation of apoptotic process [GO:0043066]; negative regulation of biomineral tissue development [GO:0070168]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of chondrocyte differentiation [GO:0032331]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of epithelial cell proliferation [GO:0050680]; negative regulation of fatty acid oxidation [GO:0046322]; negative regulation of immune system process [GO:0002683]; negative regulation of myoblast differentiation [GO:0045662]; negative regulation of ossification [GO:0030279]; negative regulation of osteoblast differentiation [GO:0045668]; negative regulation of photoreceptor cell differentiation [GO:0046533]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neural crest cell fate specification [GO:0014036]; nucleosome assembly [GO:0006334]; oligodendrocyte differentiation [GO:0048709]; otic vesicle formation [GO:0030916]; phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0043491]; positive regulation of branching involved in ureteric bud morphogenesis [GO:0090190]; positive regulation of cartilage development [GO:0061036]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of chondrocyte differentiation [GO:0032332]; positive regulation of epithelial cell differentiation [GO:0030858]; positive regulation of epithelial cell migration [GO:0010634]; positive regulation of epithelial cell proliferation [GO:0050679]; positive regulation of gene expression [GO:0010628]; positive regulation of kidney development [GO:0090184]; positive regulation of male gonad development [GO:2000020]; positive regulation of mesenchymal cell proliferation [GO:0002053]; positive regulation of mesenchymal stem cell differentiation [GO:2000741]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein-containing complex assembly [GO:0065003]; regulation of apoptotic process [GO:0042981]; regulation of cartilage development [GO:0061035]; regulation of cell cycle process [GO:0010564]; regulation of cell population proliferation [GO:0042127]; regulation of cell proliferation involved in tissue homeostasis [GO:0060784]; renal vesicle induction [GO:0072034]; response to fatty acid [GO:0070542]; retina development in camera-type eye [GO:0060041]; retinal rod cell differentiation [GO:0060221]; Sertoli cell differentiation [GO:0060008]; signal transduction [GO:0007165]; skeletal system development [GO:0001501]; somatic stem cell population maintenance [GO:0035019]; spermatogenesis [GO:0007283]; tissue homeostasis [GO:0001894]
|
nucleus [GO:0005634]; protein-containing complex [GO:0032991]
|
chromatin binding [GO:0003682]; cis-regulatory region sequence-specific DNA binding [GO:0000987]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]
|
PF00505;PF12444;
|
1.10.30.10;
| null |
PTM: Acetylated; acetylation impairs nuclear localization and ability to transactivate expression of target genes. Deacetylated by SIRT1. {ECO:0000250|UniProtKB:Q04887}.; PTM: Phosphorylation at Ser-64 and Ser-211 by PKA increases transcriptional activity and may help delay chondrocyte maturation downstream of PTHLH/PTHrP signaling. Phosphorylation at either Ser-64 or Ser-211 is required for sumoylation, but phosphorylation is not dependent on sumoylation. Phosphorylated on tyrosine residues; tyrosine dephosphorylation by PTPN11/SHP2 blocks SOX9 phosphorylation by PKA and subsequent SUMOylation. {ECO:0000250|UniProtKB:Q04887}.; PTM: Sumoylated; phosphorylation at either Ser-64 or Ser-211 is required for sumoylation. Sumoylation is induced by BMP signaling pathway. {ECO:0000250|UniProtKB:Q04887}.; PTM: Ubiquitinated; ubiquitination leads to proteasomal degradation and is negatively regulated by DDRGK1. {ECO:0000250|UniProtKB:Q04887}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q04887, ECO:0000255|PROSITE-ProRule:PRU00267}.
| null | null | null | null | null |
FUNCTION: Transcription factor that plays a key role in chondrocytes differentiation and skeletal development. Specifically binds the 5'-ACAAAG-3' DNA motif present in enhancers and super-enhancers and promotes expression of genes important for chondrogenesis, including cartilage matrix protein-coding genes COL2A1, COL4A2, COL9A1, COL11A2 and ACAN, SOX5 and SOX6. Also binds to some promoter regions. Plays a central role in successive steps of chondrocyte differentiation. Absolutely required for precartilaginous condensation, the first step in chondrogenesis during which skeletal progenitors differentiate into prechondrocytes. Together with SOX5 and SOX6, required for overt chondrogenesis when condensed prechondrocytes differentiate into early stage chondrocytes, the second step in chondrogenesis. Later, required to direct hypertrophic maturation and block osteoblast differentiation of growth plate chondrocytes: maintains chondrocyte columnar proliferation, delays prehypertrophy and then prevents osteoblastic differentiation of chondrocytes by lowering beta-catenin (CTNNB1) signaling and RUNX2 expression. Also required for chondrocyte hypertrophy, both indirectly, by keeping the lineage fate of chondrocytes, and directly, by remaining present in upper hypertrophic cells and transactivating COL10A1 along with MEF2C. Low lipid levels are the main nutritional determinant for chondrogenic commitment of skeletal progenitor cells: when lipids levels are low, FOXO (FOXO1 and FOXO3) transcription factors promote expression of SOX9, which induces chondrogenic commitment and suppresses fatty acid oxidation. Mechanistically, helps, but is not required, to remove epigenetic signatures of transcriptional repression and deposit active promoter and enhancer marks at chondrocyte-specific genes. Acts in cooperation with the Hedgehog pathway-dependent GLI (GLI1 and GLI3) transcription factors. In addition to cartilage development, also acts as a regulator of proliferation and differentiation in epithelial stem/progenitor cells: involved in the lung epithelium during branching morphogenesis, by balancing proliferation and differentiation and regulating the extracellular matrix. Controls epithelial branching during kidney development. {ECO:0000250|UniProtKB:Q04887}.
|
Sus scrofa (Pig)
|
O18910
|
OPSG_RABIT
|
MTQPWGPQMLAGGQPPESHEDSTQASIFTYTNSNSTRGPFEGPNFHIAPRWVYHLTSAWMILVVIASVFTNGLVLVATMRFKKLRHPLNWILVNLAVADLAETVIASTISVVNQFYGYFVLGHPLCVVEGYTVSLCGITGLWSLAIISWERWLVVCKPFGNVRFDAKLAIAGIAFSWIWAAVWTAPPIFGWSRYWPYGLKTSCGPDVFSGTSYPGVQSYMMVLMVTCCIIPLSVIVLCYLQVWMAIRTVAKQQKESESTQKAEKEVTRMVVVMVFAYCLCWGPYTFFACFATAHPGYSFHPLVAAIPSYFAKSATIYNPIIYVFMNRQFRNCILQLFGKKVEDSSELSSASRTEASSVSSVSPA
| null | null |
cellular response to light stimulus [GO:0071482]; phototransduction [GO:0007602]; visual perception [GO:0007601]
|
photoreceptor outer segment [GO:0001750]; plasma membrane [GO:0005886]
|
G protein-coupled photoreceptor activity [GO:0008020]; identical protein binding [GO:0042802]
|
PF00001;
|
1.20.1070.10;
|
G-protein coupled receptor 1 family, Opsin subfamily
|
PTM: O-glycosylated. {ECO:0000250|UniProtKB:O35599}.; PTM: Phosphorylated on some or all of the serine and threonine residues present in the C-terminal region.
|
SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
| null | null | null | null | null |
FUNCTION: Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal. May increase spectral sensitivity in dim light.
|
Oryctolagus cuniculus (Rabbit)
|
O18924
|
PPARG_MACMU
|
MGETLGDSPIDPESDSFTDTLSANISQEITMVDTEMPFWPTNFGISSVDLSVMDDHSHSFDIKPFTTVDFSSISAPHYEDIPFTRTDPMVADYKYDLKLQEYQSAIKVEPASPPYYSEKTQLYNKPHEEPSNSLMAIECRVCGDKASGFHYGVHACEGCKGFFRRTIRLKLIYDRCDLNCRIHKKSRNKCQYCRFQKCLAVGMSHNAIRFGRMPQAEKEKLLAEISSDIDQLNPESADLRALAKHLYDSYIKSFPLTKAKARAILTGKTTDKSPFVIYDMNSLMMGEDKIKFKHITPLQEQSKEVAIRIFQGCQFRSVEAVQEITEYAKSIPGFVNLDLNDQVTLLKYGVHEIIYTMLASLMNKDGVLISEGQGFMTREFLKSLRKPFGDFMEPKFEFAVKFNALELDDSDLAIFIAVIILSGDRPGLLNVKPIEDIQDNLLQALELQLKLNHPESSQLFAKLLQKMTDLRQIVTEHVQLLQVIKKTETDMSLHPLLQEIYKDLY
| null | null |
cell differentiation [GO:0030154]; cellular response to insulin stimulus [GO:0032869]; fatty acid metabolic process [GO:0006631]; hormone-mediated signaling pathway [GO:0009755]; macrophage derived foam cell differentiation [GO:0010742]; negative regulation of cholesterol storage [GO:0010887]; negative regulation of inflammatory response [GO:0050728]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of fatty acid metabolic process [GO:0045923]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of circadian rhythm [GO:0042752]; regulation of DNA-templated transcription [GO:0006355]; regulation of transcription by RNA polymerase II [GO:0006357]; retinoic acid receptor signaling pathway [GO:0048384]; rhythmic process [GO:0048511]
|
cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]
|
chromatin binding [GO:0003682]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; E-box binding [GO:0070888]; nuclear receptor activity [GO:0004879]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; transcription cis-regulatory region binding [GO:0000976]; zinc ion binding [GO:0008270]
|
PF00104;PF12577;PF00105;
|
3.30.50.10;1.10.565.10;
|
Nuclear hormone receptor family, NR1 subfamily
|
PTM: O-GlcNAcylation at Thr-84 reduces transcriptional activity in adipocytes. {ECO:0000250|UniProtKB:P37238}.; PTM: Phosphorylated at basal conditions and dephosphorylated when treated with the ligand. May be dephosphorylated by PPP5C. The phosphorylated form may be inactive and dephosphorylation induces adipogenic activity (By similarity). {ECO:0000250|UniProtKB:P37231}.; PTM: Ubiquitinated by E3 ubiquitin-protein ligase complex containing FBXO9; leading to proteasomal degradation (By similarity). Ubiquitinated at Lys-252 by TRIM55 leading to proteasomal degradation (By similarity). {ECO:0000250|UniProtKB:P37231, ECO:0000250|UniProtKB:P37238}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}. Cytoplasm {ECO:0000250}. Note=Redistributed from the nucleus to the cytosol through a MAP2K1/MEK1-dependent manner. NOCT enhances its nuclear translocation (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Nuclear receptor that binds peroxisome proliferators such as hypolipidemic drugs and fatty acids. Once activated by a ligand, the nuclear receptor binds to DNA specific PPAR response elements (PPRE) and modulates the transcription of its target genes, such as acyl-CoA oxidase. It therefore controls the peroxisomal beta-oxidation pathway of fatty acids. Key regulator of adipocyte differentiation and glucose homeostasis. ARF6 acts as a key regulator of the tissue-specific adipocyte P2 (aP2) enhancer. Acts as a critical regulator of gut homeostasis by suppressing NF-kappa-B-mediated pro-inflammatory responses. Plays a role in the regulation of cardiovascular circadian rhythms by regulating the transcription of BMAL1 in the blood vessels. {ECO:0000250|UniProtKB:P37231, ECO:0000250|UniProtKB:P37238}.
|
Macaca mulatta (Rhesus macaque)
|
O18927
|
MMP13_HORSE
|
MHPGVLAAFLFLSWTRCWSLPVPNDDDDDDDMSEEDFQLAERYLKSYYYPLNPAGILKKTAANSVVDRLREMQSFFGLEVTGKLDDNTLDIMKKPRCGVPDVGEYNVFPRTLKWPKMNLTYRIVNYTPDLTHSEVEKAFKKAFKVWSDVTPLNFTRLYNGTADIMISFGTKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDDDETWTSSSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYTGKSHFVLPDDDVQGIQYLYGPGDEDPNPKHPKTPDKCDPSLSLDAITSLRGETMVFKDRFFWRLHPQLVDAELFLTKSFWPELPNRIDAAYEHPSKDLIFIFRGRKFWALNGYDILEGYPQKISELGFPKDVKKISAAVHFEDTGKTLFFSGNQVWRYDDTNRMMDKDYPRLIEEDFPGIGDKVDAVYEKNGYIYFFNGPIQFEYSIWSNRIVRVMPTNSLLWC
|
3.4.24.-
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Can bind about 5 Ca(2+) ions per subunit. {ECO:0000250}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
|
bone morphogenesis [GO:0060349]; collagen catabolic process [GO:0030574]; extracellular matrix disassembly [GO:0022617]; extracellular matrix organization [GO:0030198]; proteolysis [GO:0006508]
|
extracellular matrix [GO:0031012]; extracellular space [GO:0005615]
|
calcium ion binding [GO:0005509]; collagen binding [GO:0005518]; endopeptidase activity [GO:0004175]; metalloendopeptidase activity [GO:0004222]; zinc ion binding [GO:0008270]
|
PF00045;PF00413;PF01471;
|
3.40.390.10;2.110.10.10;
|
Peptidase M10A family
|
PTM: The proenzyme is activated by removal of the propeptide; this cleavage can be effected by other matrix metalloproteinases, such as MMP2, MMP3 and MMP14 and may involve several cleavage steps. Cleavage can also be autocatalytic, after partial maturation by another protease or after treatment with 4-aminophenylmercuric acetate (APMA) (in vitro) (By similarity). {ECO:0000250}.; PTM: N-glycosylated. {ECO:0000250}.; PTM: Tyrosine phosphorylated by PKDCC/VLK. {ECO:0000250|UniProtKB:P45452}.
|
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000305}. Secreted {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Plays a role in the degradation of extracellular matrix proteins including fibrillar collagen, fibronectin, TNC and ACAN. Cleaves triple helical collagens, including type I, type II and type III collagen, but has the highest activity with soluble type II collagen. Can also degrade collagen type IV, type XIV and type X. May also function by activating or degrading key regulatory proteins, such as TGFB1 and CCN2. Plays a role in wound healing, tissue remodeling, cartilage degradation, bone development, bone mineralization and ossification. Required for normal embryonic bone development and ossification. Plays a role in the healing of bone fractures via endochondral ossification. Plays a role in wound healing, probably by a mechanism that involves proteolytic activation of TGFB1 and degradation of CCN2. Plays a role in keratinocyte migration during wound healing. May play a role in cell migration and in tumor cell invasion (By similarity). {ECO:0000250}.
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Equus caballus (Horse)
|
O18937
|
RNAS2_AOTTR
|
MVPKLFTSQICLLLLLGLLGVEGSLHAAPQKFTRAQWFSIQHIQTTPLRCTNAMRAINKYQHRCKNQNTFLHTTFAAVVNVCGNTNITCPRNASLNNCHHSRVQVPLTYCNLTGPPTITNCVYSSTQANMFYVVACDNRDQRDPPQYPVVPVHLDTTI
|
4.6.1.18
| null |
chemotaxis [GO:0006935]; defense response to virus [GO:0051607]; innate immune response in mucosa [GO:0002227]
|
extracellular space [GO:0005615]; lysosome [GO:0005764]
|
lyase activity [GO:0016829]; nucleic acid binding [GO:0003676]; ribonuclease A activity [GO:0004522]
|
PF00074;
|
3.10.130.10;
|
Pancreatic ribonuclease family
| null |
SUBCELLULAR LOCATION: Lysosome {ECO:0000305}. Cytoplasmic granule. Note=Matrix of eosinophil's large specific granule.
|
CATALYTIC ACTIVITY: Reaction=an [RNA] containing cytidine + H2O = an [RNA]-3'-cytidine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA].; EC=4.6.1.18; Evidence={ECO:0000269|PubMed:9254715}; CATALYTIC ACTIVITY: Reaction=an [RNA] containing uridine + H2O = an [RNA]-3'-uridine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA].; EC=4.6.1.18; Evidence={ECO:0000269|PubMed:9254715};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2 uM for yeast tRNA (in the presence of 40 mM sodium phosphate at pH 7.0) {ECO:0000269|PubMed:9254715};
| null | null | null |
FUNCTION: This is a non-secretory ribonuclease. It is a pyrimidine specific nuclease with a slight preference for U. Cytotoxin and helminthotoxin. Possesses a wide variety of biological activities. {ECO:0000269|PubMed:9254715}.
|
Aotus trivirgatus (Three-striped night monkey) (Douroucouli)
|
O18956
|
ENTP1_BOVIN
|
MEDRRESELKVFCSKNILSILGFSCIIAVIALLALGLTQNKALPENVKFGIVLDAGSSHTSLYIYRWPAEKENDTGVVTQIEESNVKGPGISGFAKKVNEINVYLTACMERAQKVIPSIQHMETPVYLGATAGMRLLRMENKQMADKILAAVASSISEYPFDFQGARIISGQEEGAYGWITVNYLLGKFTQKLSWFNLKPSKDDTQETYGALDLGGASTQITFVPQNETTESPNNNLYFRLYGKNYSVYTHSFLCYGKDQALLQKLALGLQGTNGIIHEPCFHSRYMRKIKMSVLNEGFCTKRHELNSSFYPLVDIEIRGAGNFQRCRQSIIQLFNTSYCPYSSCSFNGVFLPPLHGQFGAFSAFYYVMEFLNLTSEESVSVEQLTEKLEEFCAQRWEEVQKNFGEVKEKYLSEYCFSGTYILVLLLNGYHFTAESWKNIHFMNKVRSTDVGWTLGYMLNLTNKIPAEEPMSPPLPHSTYVFLMVLFSLILLAVIIVGIVVFHKPSYFWKDMV
|
3.6.1.5
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P49961}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P49961};
|
nucleoside diphosphate catabolic process [GO:0009134]; platelet aggregation [GO:0070527]
|
caveola [GO:0005901]; plasma membrane [GO:0005886]
|
ADP phosphatase activity [GO:0043262]; apyrase activity [GO:0004050]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; CDP phosphatase activity [GO:0036384]; CTPase activity [GO:0043273]; GDP phosphatase activity [GO:0004382]; GTPase activity [GO:0003924]; IDP phosphatase activity [GO:1990003]; ITPase activity [GO:0103023]; nucleoside diphosphate phosphatase activity [GO:0017110]; ribonucleoside triphosphate phosphatase activity [GO:0017111]; UDP phosphatase activity [GO:0045134]
|
PF01150;
|
3.30.420.40;3.30.420.150;
|
GDA1/CD39 NTPase family
|
PTM: N-glycosylated. {ECO:0000250|UniProtKB:P97687}.; PTM: The N-terminus is blocked. {ECO:0000250|UniProtKB:P49961}.; PTM: Palmitoylated on Cys-13; which is required for caveola targeting. {ECO:0000250|UniProtKB:P49961}.
|
SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P49961}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P49961}. Membrane, caveola {ECO:0000250|UniProtKB:P49961}.
|
CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + 2 H2O = a ribonucleoside 5'-phosphate + 2 H(+) + 2 phosphate; Xref=Rhea:RHEA:36795, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58043, ChEBI:CHEBI:61557; EC=3.6.1.5; Evidence={ECO:0000250|UniProtKB:P49961}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36796; Evidence={ECO:0000250|UniProtKB:P49961}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; Evidence={ECO:0000250|UniProtKB:P49961}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23681; Evidence={ECO:0000250|UniProtKB:P49961}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-diphosphate + H2O = a ribonucleoside 5'-phosphate + H(+) + phosphate; Xref=Rhea:RHEA:36799, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:58043; Evidence={ECO:0000250|UniProtKB:P49961}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36800; Evidence={ECO:0000250|UniProtKB:P49961}; CATALYTIC ACTIVITY: Reaction=ATP + 2 H2O = AMP + 2 H(+) + 2 phosphate; Xref=Rhea:RHEA:20988, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:P49961}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20989; Evidence={ECO:0000250|UniProtKB:P49961}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P49961}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066; Evidence={ECO:0000250|UniProtKB:P49961}; CATALYTIC ACTIVITY: Reaction=ADP + H2O = AMP + H(+) + phosphate; Xref=Rhea:RHEA:61436, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P49961}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61437; Evidence={ECO:0000250|UniProtKB:P49961}; CATALYTIC ACTIVITY: Reaction=CTP + 2 H2O = CMP + 2 H(+) + 2 phosphate; Xref=Rhea:RHEA:64908, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37563, ChEBI:CHEBI:43474, ChEBI:CHEBI:60377; Evidence={ECO:0000250|UniProtKB:P49961}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64909; Evidence={ECO:0000250|UniProtKB:P49961}; CATALYTIC ACTIVITY: Reaction=CTP + H2O = CDP + H(+) + phosphate; Xref=Rhea:RHEA:29387, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37563, ChEBI:CHEBI:43474, ChEBI:CHEBI:58069; Evidence={ECO:0000250|UniProtKB:P49961}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29388; Evidence={ECO:0000250|UniProtKB:P49961}; CATALYTIC ACTIVITY: Reaction=CDP + H2O = CMP + H(+) + phosphate; Xref=Rhea:RHEA:64880, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377; Evidence={ECO:0000250|UniProtKB:P49961}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64881; Evidence={ECO:0000250|UniProtKB:P49961}; CATALYTIC ACTIVITY: Reaction=GTP + 2 H2O = GMP + 2 H(+) + 2 phosphate; Xref=Rhea:RHEA:64904, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58115; Evidence={ECO:0000250|UniProtKB:P49961}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64905; Evidence={ECO:0000250|UniProtKB:P49961}; CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:P49961}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:P49961}; CATALYTIC ACTIVITY: Reaction=GDP + H2O = GMP + H(+) + phosphate; Xref=Rhea:RHEA:22156, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58115, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:P49961}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22157; Evidence={ECO:0000250|UniProtKB:P49961}; CATALYTIC ACTIVITY: Reaction=2 H2O + ITP = 2 H(+) + IMP + 2 phosphate; Xref=Rhea:RHEA:77735, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58053, ChEBI:CHEBI:61402; Evidence={ECO:0000250|UniProtKB:P49961}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77736; Evidence={ECO:0000250|UniProtKB:P49961}; CATALYTIC ACTIVITY: Reaction=H2O + ITP = H(+) + IDP + phosphate; Xref=Rhea:RHEA:28330, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58280, ChEBI:CHEBI:61402; Evidence={ECO:0000250|UniProtKB:P49961}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28331; Evidence={ECO:0000250|UniProtKB:P49961}; CATALYTIC ACTIVITY: Reaction=H2O + IDP = H(+) + IMP + phosphate; Xref=Rhea:RHEA:35207, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58053, ChEBI:CHEBI:58280; Evidence={ECO:0000250|UniProtKB:P49961}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35208; Evidence={ECO:0000250|UniProtKB:P49961}; CATALYTIC ACTIVITY: Reaction=2 H2O + UTP = 2 H(+) + 2 phosphate + UMP; Xref=Rhea:RHEA:64896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:46398, ChEBI:CHEBI:57865; Evidence={ECO:0000250|UniProtKB:P97687}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64897; Evidence={ECO:0000250|UniProtKB:P97687}; CATALYTIC ACTIVITY: Reaction=H2O + UTP = H(+) + phosphate + UDP; Xref=Rhea:RHEA:64900, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:46398, ChEBI:CHEBI:58223; Evidence={ECO:0000250|UniProtKB:P97687}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64901; Evidence={ECO:0000250|UniProtKB:P97687}; CATALYTIC ACTIVITY: Reaction=H2O + UDP = H(+) + phosphate + UMP; Xref=Rhea:RHEA:64876, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57865, ChEBI:CHEBI:58223; Evidence={ECO:0000250|UniProtKB:P97687}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64877; Evidence={ECO:0000250|UniProtKB:P97687};
| null | null | null | null |
FUNCTION: Catalyzes the hydrolysis of both di- and triphosphate nucleotides (NDPs and NTPs) and hydrolyze NTPs to nucleotide monophosphates (NMPs) in two distinct successive phosphate-releasing steps, with NDPs as intermediates and participates in the regulation of extracellular levels of nucleotides. By hydrolyzing proinflammatory ATP and platelet-activating ADP to AMP, it blocks platelet aggregation and supports blood flow. {ECO:0000250|UniProtKB:P49961}.
|
Bos taurus (Bovine)
|
O18963
|
CP2E1_BOVIN
|
MAALGITVALLVWMATLLFISIWKHIYSSWKLPPGPFPLPIIGNLLQLDIKNIPKSFTRLAERYGPVFTLYLGSQRAVVVHGYKPVKEVLLDYKNEFSGRGENPGFQMHKNNGIIFNNGSTWRDTRRFSLTTLRDLGMGKQGNEQRIQREAHFLLEVLRKTQGQPFDPTFVVGFAPYNVISDILFHKRFDYKDQTSLRLMSLFNENFYLLSSPWIQLYNNFPDYLQYLPGSHRKLLKNVSEVKSYALERVKDHQKSLEPSCPRGFLDTMLIEMAKERHSVDPMYTLENIAVTVADLLFAGTETTSTTLRYGLLILMKYPEVEEKLHEEIDRVIGPSRIPAVKDRLDMPYLDAVVHEIQRFIDLLPSNLLHEATQDTVFRGYVIPKGTVVIPTLDSVLHDRQEFPEPEKFKPEHFLNENGKFKYSDHFKAFSAGKRVCVGEGLARMELFLLLAAILQHFNLKSLVDPKDIDLSPIAIGFGKIPPRYKLCLIPRSKV
|
1.14.13.n7; 1.14.14.1
|
COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
|
epoxygenase P450 pathway [GO:0019373]; xenobiotic metabolic process [GO:0006805]
|
cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231]; mitochondrial inner membrane [GO:0005743]
|
arachidonic acid epoxygenase activity [GO:0008392]; aromatase activity [GO:0070330]; heme binding [GO:0020037]; Hsp70 protein binding [GO:0030544]; Hsp90 protein binding [GO:0051879]; iron ion binding [GO:0005506]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen [GO:0016712]
|
PF00067;
|
1.10.630.10;
|
Cytochrome P450 family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P05182}; Peripheral membrane protein {ECO:0000250|UniProtKB:P05182}. Microsome membrane {ECO:0000250|UniProtKB:P05182}; Peripheral membrane protein {ECO:0000250|UniProtKB:P05182}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:P05182}; Peripheral membrane protein {ECO:0000250|UniProtKB:P05182}. Note=Post-translationally targeted to mitochondria. TOMM70 is required for the translocation across the mitochondrial outer membrane. After translocation into the matrix, associates with the inner membrane as a membrane extrinsic protein. {ECO:0000250|UniProtKB:P05182}.
|
CATALYTIC ACTIVITY: Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30879, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:142491; EC=1.14.14.1; Evidence={ECO:0000250|UniProtKB:P05181}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17150; Evidence={ECO:0000250|UniProtKB:P05181}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z)-eicosatrienoate + O2 + reduced [NADPH--hemoprotein reductase] = 19-hydroxy-(5Z,8Z,11Z)-eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:50076, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:78043, ChEBI:CHEBI:132024; Evidence={ECO:0000250|UniProtKB:P05181}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50077; Evidence={ECO:0000250|UniProtKB:P05181}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced [NADPH--hemoprotein reductase] = 19-hydroxy-(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:39787, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:58562, ChEBI:CHEBI:76636; Evidence={ECO:0000250|UniProtKB:P05181}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39788; Evidence={ECO:0000250|UniProtKB:P05181}; CATALYTIC ACTIVITY: Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 + reduced [NADPH--hemoprotein reductase] = 21-hydroxy-(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:50088, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:77016, ChEBI:CHEBI:132025; Evidence={ECO:0000250|UniProtKB:P05181}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50089; Evidence={ECO:0000250|UniProtKB:P05181}; CATALYTIC ACTIVITY: Reaction=dodecanoate + O2 + reduced [NADPH--hemoprotein reductase] = 11-hydroxydodecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:39751, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:18262, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:76628; Evidence={ECO:0000250|UniProtKB:P05181}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39752; Evidence={ECO:0000250|UniProtKB:P05181}; CATALYTIC ACTIVITY: Reaction=O2 + reduced [NADPH--hemoprotein reductase] + tetradecanoate = 13-hydroxytetradecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:50096, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30807, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:132031; Evidence={ECO:0000250|UniProtKB:P05181}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50097; Evidence={ECO:0000250|UniProtKB:P05181}; CATALYTIC ACTIVITY: Reaction=4-nitrophenol + H(+) + NADPH + O2 = 4-nitrocatechol + H2O + NADP(+); Xref=Rhea:RHEA:26205, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57730, ChEBI:CHEBI:57783, ChEBI:CHEBI:57917, ChEBI:CHEBI:58349; EC=1.14.13.n7; Evidence={ECO:0000250|UniProtKB:P05181}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26206; Evidence={ECO:0000250|UniProtKB:P05181};
| null |
PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000250|UniProtKB:P05181}.
| null | null |
FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of fatty acids. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase). Catalyzes the hydroxylation of carbon-hydrogen bonds. Hydroxylates fatty acids specifically at the omega-1 position displaying the highest catalytic activity for saturated fatty acids. May be involved in the oxidative metabolism of xenobiotics. {ECO:0000250|UniProtKB:P05181}.
|
Bos taurus (Bovine)
|
O18964
|
SYNJ1_BOVIN
|
MAFSKGFRIYHKLDPPPFSLIVETRHKEECLMFESGAVAVLSSAEKEAIKGTYSKVLDAYGLLGVLRLNLGDIMLHYLVLVTGCMSVGKIQESEVFRVTSTEFISLRVDSSDEDRISEVRKVLNSGNFYFAWSASGVSLDLSLNAHRSLQEHTTDNRFSWNQSLHLHLKHYGVNCADWLLRLMCGGVEIRTIYAAHKQAKACLISRLSCERAGTRFNVRGTNDDGHVANFVETEQVVYLDDSVSSFIQIRGSVPLFWEQPGLQVGSHRVRMSRGFEANAPAFDRHFRTLKNLYGKQIIVNLLGSKEGEHMLSKAFQSHLKASEHAADIQMVNFDYHQMVKGGKAEKLHSVLKPQVQKFLDYGIFHFDGSEVQRCQSGTVRTNCLDCLDRTNSVQAFLGLEMLTKQLEALGLAEKPQLVTRFQEVFRSMWSVNGDSISKIYAGTGALEGKAKLKDGARSVSRTIQNNFFDSSKQEAIDVLLLGNTLNSDLADKARALLTTGSLRVSEQTLQSASSKVLKSMCENFYKYSKPKKIRVCVGTWNVNGGKQFRSIAFKNQTLTDWLLDAPKLAGIQEFQDKRSKPMDIFPIGFEEMVELNAGNIVNASTTNQKLWAAELQKTISRDNKYVLLASEQLVGVCLFVFIRPQHAPFIRDVAVDTVKTGMGGATGNKGAVAIRMLFHTTSLCFVCSHFAAGQSQVKERNDDFLEIARKLSFPMGRLLFSHDYVFWCGDFNYRIDLPNEEVKELIRQQNWDSLIAGDQLINQKNAGQIFRGFLEGKVTFAPTYKYDLFSDDYDTSEKCRTPAWTDRVLWRRRKWPFDRSAEDLDLLNASFQDESKILYTWTPGTLLHYGRAELKTSDHRPVVALIDIDIFEVEAEERQNIYKEVIAVQGPPDGTVLVSIKSSLPENNFFNDALIDELLQQFTNFGEVILIRFVEDKMWVTFLEGSSALNVLNLNGKELLGRTITITLKSPDWIKTLEEEMSLEKINVPLPSSTSSTLLGEDAEVTADFDMEGDVDDYSAEVEEILPQHLQPSSSSALARPPVLHPGPVPASHLPYRRGPVPSLPVRPSRAPSRTPGPPASQSSPVDTLPATQLQQKDSSQTLEPKRPPPPRPVAPPARPAPPQRPPPPSGARSPAPARERVWSTRKAQERPRRDNLGGSQLPPQGGLPGPGLAGHSAARPIIPPRAGVISAPESHGRVSAGRLTPESQRKTXEVLKGPALLPEPLKPQAALPVPPSLAPPSQEMQEPLIAVAAPLAQSALQPSLETPPQPPPRSRSSHSLPSDAPAAAAGATIRVTGEKQTGVSAVRLDCPLKSDPFEDLSLN
|
3.1.3.36
| null |
phosphatidylinositol dephosphorylation [GO:0046856]; synaptic vesicle endocytosis [GO:0048488]
|
perinuclear region of cytoplasm [GO:0048471]; presynapse [GO:0098793]
|
phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity [GO:0004439]; RNA binding [GO:0003723]; SH3 domain binding [GO:0017124]
|
PF08952;PF02383;
|
3.30.70.330;3.60.10.10;
|
Synaptojanin family; Inositol 1,4,5-trisphosphate 5-phosphatase family
| null |
SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:9199318}.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + phosphate; Xref=Rhea:RHEA:22764, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58178, ChEBI:CHEBI:58456; EC=3.1.3.36; Evidence={ECO:0000269|PubMed:9199318};
| null | null | null | null |
FUNCTION: Phosphatase that acts on various phosphoinositides, including phosphatidylinositol 4-phosphate, phosphatidylinositol (4,5)-bisphosphate and phosphatidylinositol (3,4,5)-trisphosphate (PubMed:9199318). Has a role in clathrin-mediated endocytosis (By similarity). Hydrolyzes PIP2 bound to actin regulatory proteins resulting in the rearrangement of actin filaments downstream of tyrosine kinase and ASH/GRB2 (PubMed:9199318). {ECO:0000250|UniProtKB:Q62910, ECO:0000269|PubMed:9199318}.
|
Bos taurus (Bovine)
|
O18965
|
KCNH1_BOVIN
|
MTMAGGRKGLVAPQNTFLENIVRRSNDTNFVLGNAQIVDWPIVYSNDGFCKLSGYHRAEVMQKSSTCSFMYGELTDKDTIEKVRQTFENYEMNSFEILMYKKNRTPVWFFVKIAPIRNEQDKVVLFLCTFSDITAFKQPIEDDSCKGWGKFARLTRALTSSRGVLQQLAPSVQKGENVHKHSRLAEVLQLGSDILPQYKQEAPKTPPHIILHYCVFKTTWDWIILILTFYTAILVPYNVSFKTRQNNVAWLVVDSIVDVIFLVDIVLNFHTTFVGPAGEVISDPKLIRMNYLKTWFVIDLLSCLPYDVINAFENVDEVSAFMGDPGKIGFADQIPPPLEGRESQGISSLFSSLKVVRLLRLGRVARKLDHYIEYGAAVLVLLVCVFGLAAHWMACIWYSIGDYEIFDEDTKTIRNNSWLYQLAMDIGTPYQFNGSGSGKWEGGPSKNSVYISSLYFTMTSLTSVGFGNIAPSTDIEKIFAVAIMMIGSLLYATIFGNVTTIFQQMYANTNRYHEMLNSVRDFLKLYQVPKGLSERVMDYIVSTWSMSRGIDTEKVLQICPKDMRADICVHLNRKVFKEHPAFRLASDGCLRALAMEFQTVHCAPGDLIYHAGESVDSLCFVVSGSLEVIQDDEVVAILGKGDVFGDVFWKEATLAQSCANVRALTYCDLHVIKRDALQKVLEFYTAFSHSFSRNLILTYNLRKRIVFRKISDVKREEEERMKRKNEAPLILPPDHPVRRLFQRFRQQKEARLAAERGGRDLDDLDVEKGSVLTEHSHHGLAKASVVTVRESPATPVAFPAAAAPAGLDHARLQAPGAEGLGPKAGGADCAKRKGWARFKDACGQAEDWSKVSKAESMETLPERTKAAGEATLKKTDSCDSGITKSDLRLDNVGEARSPQDRSPILAEVKHSFYPIPEQTLQAAVLEVKHELKEDIKALSTKMTSIEKQLSEILRILTSRRSSQSPQELFEISRPQSPESERDIFGAS
| null | null |
cellular response to calcium ion [GO:0071277]; potassium ion transmembrane transport [GO:0071805]; regulation of cell population proliferation [GO:0042127]; regulation of membrane potential [GO:0042391]
|
axon [GO:0030424]; dendrite [GO:0030425]; early endosome membrane [GO:0031901]; nuclear inner membrane [GO:0005637]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; postsynaptic density membrane [GO:0098839]; presynaptic membrane [GO:0042734]; voltage-gated potassium channel complex [GO:0008076]
|
calmodulin binding [GO:0005516]; delayed rectifier potassium channel activity [GO:0005251]; phosphatidylinositol bisphosphate binding [GO:1902936]; voltage-gated potassium channel activity [GO:0005249]
|
PF00027;PF00520;PF13426;
|
1.10.1200.260;1.10.287.70;2.60.120.10;3.30.450.20;
|
Potassium channel family, H (Eag) (TC 1.A.1.20) subfamily, Kv10.1/KCNH1 sub-subfamily
|
PTM: Channel activity is regulated via tyrosine phosphorylation/dephosphorylation by SRC and PTPN6. {ECO:0000250|UniProtKB:O95259}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9524140}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O95259}. Nucleus inner membrane {ECO:0000250|UniProtKB:O95259}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O95259}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q63472}. Cell projection, axon {ECO:0000250|UniProtKB:Q63472}. Presynaptic cell membrane {ECO:0000250|UniProtKB:Q63472}. Perikaryon {ECO:0000250|UniProtKB:Q63472}. Postsynaptic density membrane {ECO:0000250|UniProtKB:Q63472}. Early endosome membrane {ECO:0000250|UniProtKB:O95259}. Note=Perinuclear KCNH1 is located to NPC-free islands. {ECO:0000250|UniProtKB:O95259}.
| null | null | null | null | null |
FUNCTION: Pore-forming (alpha) subunit of a voltage-gated delayed rectifier potassium channel (PubMed:9524140). Channel properties are modulated by subunit assembly. Mediates IK(NI) current in myoblasts. Involved in the regulation of cell proliferation and differentiation, in particular adipogenic and osteogenic differentiation in bone marrow-derived mesenchymal stem cells (MSCs) (By similarity). {ECO:0000250|UniProtKB:O95259, ECO:0000269|PubMed:9524140}.
|
Bos taurus (Bovine)
|
O18971
|
PPARG_BOVIN
|
MGETLGDALIDPESEPFAVTVSARTSQEITMVDTEMPFWPTNFGISSVDLSMMDDHSHAFDIKPFTTVDFSSISTPHYEDIPFPRADPMVADYKYDLKLQEYQSAIKVEPVSPPYYSEKTQLYSKPHEEPSNSLMAIECRVCGDKASGFHYGVHACEGCKGFFRRTIRLKLIYDRCDLNCRIHKKSRNKCQYCRFQKCLAVGMSHNAIRFGRMPQAEKEKLLAEISSDIDQLNPESADLRALAKHLYDSYIKSFPLTKAKARAILTGKTTDKSPFVIYDMNSLMMGEDKIKFKHISPLQEPSKEVAIRIFQGCQFRSVEAVQEITEYAKNIPGFVNLDLNDQVTLLKYGVHEIIYTMLASLMNKDGVLISEGQGFMTREFLKSLRKPFGDFMEPKFEFAVKFNALELDDSDLAIFIAVIILSGDRPGLLNVKPIEDIQDNLLQALELQLKLNHPESSQLFAKLLQKMTDLRQIVTEHVQLLQVIKKTETDMSLHPLLQEIYKDLY
| null | null |
cell differentiation [GO:0030154]; cell fate commitment [GO:0045165]; cellular response to insulin stimulus [GO:0032869]; epithelial cell differentiation [GO:0030855]; fatty acid metabolic process [GO:0006631]; hormone-mediated signaling pathway [GO:0009755]; macrophage derived foam cell differentiation [GO:0010742]; negative regulation of cholesterol storage [GO:0010887]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of inflammatory response [GO:0050728]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of fatty acid metabolic process [GO:0045923]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of circadian rhythm [GO:0042752]; regulation of DNA-templated transcription [GO:0006355]; regulation of fat cell differentiation [GO:0045598]; regulation of transcription by RNA polymerase II [GO:0006357]; retinoic acid receptor signaling pathway [GO:0048384]; rhythmic process [GO:0048511]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; E-box binding [GO:0070888]; nuclear receptor activity [GO:0004879]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; transcription cis-regulatory region binding [GO:0000976]; zinc ion binding [GO:0008270]
|
PF00104;PF12577;PF00105;
|
3.30.50.10;1.10.565.10;
|
Nuclear hormone receptor family, NR1 subfamily
|
PTM: Phosphorylated at basal conditions and dephosphorylated when treated with the ligand. May be dephosphorylated by PPP5C. The phosphorylated form may be inactive and dephosphorylation induces adipogenic activity (By similarity). {ECO:0000250|UniProtKB:P37231}.; PTM: Ubiquitinated by E3 ubiquitin-protein ligase complex containing FBXO9; leading to proteasomal degradation (By similarity). Ubiquitinated at Lys-252 by TRIM55 leading to proteasomal degradation (By similarity). {ECO:0000250|UniProtKB:P37231, ECO:0000250|UniProtKB:P37238}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}. Cytoplasm {ECO:0000250}. Note=Redistributed from the nucleus to the cytosol through a MAP2K1/MEK1-dependent manner. NOCT enhances its nuclear translocation (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Nuclear receptor that binds peroxisome proliferators such as hypolipidemic drugs and fatty acids. Once activated by a ligand, the nuclear receptor binds to DNA specific PPAR response elements (PPRE) and modulates the transcription of its target genes, such as acyl-CoA oxidase. It therefore controls the peroxisomal beta-oxidation pathway of fatty acids. Key regulator of adipocyte differentiation and glucose homeostasis. ARF6 acts as a key regulator of the tissue-specific adipocyte P2 (aP2) enhancer. Acts as a critical regulator of gut homeostasis by suppressing NF-kappa-B-mediated pro-inflammatory responses. Plays a role in the regulation of cardiovascular circadian rhythms by regulating the transcription of BMAL1 in the blood vessels. {ECO:0000250|UniProtKB:P37231, ECO:0000250|UniProtKB:P37238}.
|
Bos taurus (Bovine)
|
O18973
|
RABX5_BOVIN
|
MSLKSERRGIHVDQSELLCKKGCGYYGNPAWQGFCSKCWREEYHKARQKQIQEDWELAERLQREEEEAFASSQSSQGAQSLTFSKFEEKKTNEKTRKVTTVKKFFSASSRVGAKKAEIQEAKAPSPSINRQTSIETDRVSKEFIEFLKTFHKTGQEIYKQTKLFLEAMHYKRDLSIEEQSECTQDFYQNVAERMQTRGKVPPERVEKIMDQIEKYIMTRLYKYVFCPETTDDEKKDLAIQKRIRALHWVTPQMLCVPVNEEIPEVSDMVVKAITDIIEMDSKRVPRDKLACITKCSKHIFNAIKITKNEPASADDFLPTLIYIVLKGNPPRLQSNIQYITRFCNPSRLMTGEDGYYFTNLCCAVAFIEKLDAQSLNLSQEDFDRYMSGQTSPRKQESENWSPDACLGVKQMYKNLDLLSQLNERQERIMNEAKKLEKDLIDWTDGIAKEVQDIVEKYPLEIRPPNQSVAAIDSENVENDKLPPPLQPQVYAG
| null | null |
endocytosis [GO:0006897]; protein transport [GO:0015031]
|
cytosol [GO:0005829]; early endosome [GO:0005769]; endocytic vesicle [GO:0030139]; recycling endosome [GO:0055037]
|
DNA binding [GO:0003677]; guanyl-nucleotide exchange factor activity [GO:0005085]; small GTPase binding [GO:0031267]; zinc ion binding [GO:0008270]
|
PF18151;PF02204;PF01754;
|
1.10.246.120;1.20.5.4770;1.20.1050.80;
| null |
PTM: Monoubiquitinated.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9323142}. Early endosome {ECO:0000269|PubMed:9323142}. Recycling endosome {ECO:0000269|PubMed:9323142}.
| null | null | null | null | null |
FUNCTION: Rab effector protein acting as linker between gamma-adaptin and RAB5A. Involved in endocytic membrane fusion and membrane trafficking of recycling endosomes. Stimulates nucleotide exchange on RAB5A. Can act as a ubiquitin ligase. {ECO:0000269|PubMed:16462746, ECO:0000269|PubMed:9323142}.
|
Bos taurus (Bovine)
|
O18998
|
DNAS1_RABIT
|
MRSEMLTALLTLAVLLQVAGSLKIAAFNIRSFGETKMSNATLTSYIVRILQRYDIALIQEVRDSHLTAVGKLLDKLNEKAADTYRFVASEPLGRRTYKERYLFVYRPDQVSVLDSYYYDDGCEPCGTDTFSREPAVVRFSSPSTKVREFAIVPLHSAPEDAVAEIDALYDVYLDVQKKWGLQDVMLMGDFNADYSYVTSSQWSSIRLRTNPAFKWLIPDTADTTATSTNCAYDRIVVAGPLLQDAVVPNSAAPFNFQAAYGLSNQLAQAISDHYPVEVTLA
|
3.1.21.1
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P24855}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P24855}; Note=Divalent metal cations. Prefers Ca(2+) or Mg(2+). {ECO:0000250|UniProtKB:P24855};
|
apoptotic process [GO:0006915]; DNA catabolic process [GO:0006308]; neutrophil activation involved in immune response [GO:0002283]; regulation of acute inflammatory response [GO:0002673]; regulation of neutrophil mediated cytotoxicity [GO:0070948]
|
extracellular region [GO:0005576]; nuclear envelope [GO:0005635]; zymogen granule [GO:0042588]
|
actin binding [GO:0003779]; deoxyribonuclease I activity [GO:0004530]; DNA binding [GO:0003677]
|
PF03372;
|
3.60.10.10;
|
DNase I family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P24855}. Zymogen granule {ECO:0000250|UniProtKB:P24855}. Nucleus envelope {ECO:0000250|UniProtKB:P24855}. Note=Secretory protein, stored in zymogen granules and found in the nuclear envelope. {ECO:0000250|UniProtKB:P24855}.
|
CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-phosphooligonucleotide end-products.; EC=3.1.21.1; Evidence={ECO:0000269|PubMed:9230129};
| null | null | null | null |
FUNCTION: Serum endocuclease secreted into body fluids by a wide variety of exocrine and endocrine organs (PubMed:9230129). Expressed by non-hematopoietic tissues and preferentially cleaves protein-free DNA (By similarity). Among other functions, seems to be involved in cell death by apoptosis. Binds specifically to G-actin and blocks actin polymerization (PubMed:9230129). Preferentially attacks double-stranded DNA and produces oligonucleotides with 5'-phospho and 3'-hydroxy termini (PubMed:9230129). Together with DNASE1L3, plays a key role in degrading neutrophil extracellular traps (NETs) (By similarity). NETs are mainly composed of DNA fibers and are released by neutrophils to bind pathogens during inflammation (By similarity). Degradation of intravascular NETs by DNASE1 and DNASE1L3 is required to prevent formation of clots that obstruct blood vessels and cause organ damage following inflammation (By similarity). {ECO:0000250|UniProtKB:P21704, ECO:0000250|UniProtKB:P49183, ECO:0000269|PubMed:9230129}.
|
Oryctolagus cuniculus (Rabbit)
|
O19011
|
TGFB1_HORSE
|
MPPSGLRLLPLLLPLLWLLVLTPGRPAAGLSTCKTIDMELVKRKRIEAIRGQILSKLRLASPPSQGEVPPGPLPEAVLALYNSTRAQVAGESAETEPEPEADYYAKEVTRVLMVEKENEIYKTVETGSHSIYMFFNTSELRAAVPDPMLLSRAELRLLRLKLSVEQHVELYQKYSNNSWRYLSNRLLTPSDSPEWLSFDVTGVVRQWLSQGGAMEGFRLSAHCSCDSKDNTLRVGINGFSSSRRGDLATIDGMNRPFLLLMATPLERAQQLHSSRHRRALDTNYCFSSTEKNCCVRQLYIDFRKDLGWKWIHEPKGYHANFCLGPCPYIWSLDTQYSKVLALYNQHNPGASAAPCCVPQVLEPLPIVYYVGRKPKVEQLSNMIVRSCKCS
| null | null |
ATP biosynthetic process [GO:0006754]; cell-cell junction organization [GO:0045216]; cellular response to transforming growth factor beta stimulus [GO:0071560]; chondrocyte differentiation [GO:0002062]; epithelial to mesenchymal transition [GO:0001837]; extracellular matrix assembly [GO:0085029]; extrinsic apoptotic signaling pathway [GO:0097191]; hematopoietic progenitor cell differentiation [GO:0002244]; hyaluronan catabolic process [GO:0030214]; membrane protein intracellular domain proteolysis [GO:0031293]; negative regulation of blood vessel endothelial cell migration [GO:0043537]; negative regulation of cell cycle [GO:0045786]; negative regulation of cell growth [GO:0030308]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of cell-cell adhesion [GO:0022408]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of epithelial cell proliferation [GO:0050680]; negative regulation of fat cell differentiation [GO:0045599]; negative regulation of gene expression [GO:0010629]; negative regulation of hyaluronan biosynthetic process [GO:1900126]; negative regulation of macrophage cytokine production [GO:0010936]; negative regulation of myoblast differentiation [GO:0045662]; negative regulation of protein phosphorylation [GO:0001933]; negative regulation of skeletal muscle tissue development [GO:0048642]; odontoblast differentiation [GO:0071895]; phosphate-containing compound metabolic process [GO:0006796]; positive regulation of blood vessel endothelial cell migration [GO:0043536]; positive regulation of cell division [GO:0051781]; positive regulation of cell migration [GO:0030335]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of chemotaxis [GO:0050921]; positive regulation of collagen biosynthetic process [GO:0032967]; positive regulation of epidermal growth factor receptor signaling pathway [GO:0045742]; positive regulation of epithelial to mesenchymal transition [GO:0010718]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of fibroblast migration [GO:0010763]; positive regulation of gene expression [GO:0010628]; positive regulation of interleukin-17 production [GO:0032740]; positive regulation of isotype switching to IgA isotypes [GO:0048298]; positive regulation of microglia differentiation [GO:0014008]; positive regulation of protein dephosphorylation [GO:0035307]; positive regulation of protein import into nucleus [GO:0042307]; positive regulation of protein metabolic process [GO:0051247]; positive regulation of protein secretion [GO:0050714]; positive regulation of protein-containing complex assembly [GO:0031334]; positive regulation of SMAD protein signal transduction [GO:0060391]; positive regulation of superoxide anion generation [GO:0032930]; positive regulation of transcription by RNA polymerase II [GO:0045944]; receptor catabolic process [GO:0032801]; regulation of cell population proliferation [GO:0042127]; regulation of transforming growth factor beta receptor signaling pathway [GO:0017015]; response to cholesterol [GO:0070723]; response to estradiol [GO:0032355]; response to progesterone [GO:0032570]; response to wounding [GO:0009611]; salivary gland morphogenesis [GO:0007435]; transforming growth factor beta receptor signaling pathway [GO:0007179]
|
blood microparticle [GO:0072562]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; extracellular space [GO:0005615]; nucleus [GO:0005634]
|
antigen binding [GO:0003823]; cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; type I transforming growth factor beta receptor binding [GO:0034713]; type II transforming growth factor beta receptor binding [GO:0005114]; type III transforming growth factor beta receptor binding [GO:0034714]
|
PF00019;PF00688;
|
2.60.120.970;2.10.90.10;
|
TGF-beta family
|
PTM: Transforming growth factor beta-1 proprotein: The precursor proprotein is cleaved in the Golgi apparatus by FURIN to form Transforming growth factor beta-1 (TGF-beta-1) and Latency-associated peptide (LAP) chains, which remain non-covalently linked, rendering TGF-beta-1 inactive. {ECO:0000250|UniProtKB:P01137}.; PTM: [Latency-associated peptide]: N-glycosylated. Deglycosylation leads to activation of Transforming growth factor beta-1 (TGF-beta-1); mechanisms triggering deglycosylation-driven activation of TGF-beta-1 are however unclear. {ECO:0000250|UniProtKB:P01137}.
|
SUBCELLULAR LOCATION: [Latency-associated peptide]: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P01137}.; SUBCELLULAR LOCATION: [Transforming growth factor beta-1]: Secreted {ECO:0000250|UniProtKB:P01137}.
| null | null | null | null | null |
FUNCTION: Transforming growth factor beta-1 proprotein: Precursor of the Latency-associated peptide (LAP) and Transforming growth factor beta-1 (TGF-beta-1) chains, which constitute the regulatory and active subunit of TGF-beta-1, respectively. {ECO:0000250|UniProtKB:P01137}.; FUNCTION: [Latency-associated peptide]: Required to maintain the Transforming growth factor beta-1 (TGF-beta-1) chain in a latent state during storage in extracellular matrix. Associates non-covalently with TGF-beta-1 and regulates its activation via interaction with 'milieu molecules', such as LTBP1, LRRC32/GARP and LRRC33/NRROS, that control activation of TGF-beta-1. Interaction with LRRC33/NRROS regulates activation of TGF-beta-1 in macrophages and microglia. Interaction with LRRC32/GARP controls activation of TGF-beta-1 on the surface of activated regulatory T-cells (Tregs). Interaction with integrins (ITGAV:ITGB6 or ITGAV:ITGB8) results in distortion of the Latency-associated peptide chain and subsequent release of the active TGF-beta-1. {ECO:0000250|UniProtKB:P01137}.; FUNCTION: [Transforming growth factor beta-1]: Multifunctional protein that regulates the growth and differentiation of various cell types and is involved in various processes, such as normal development, immune function, microglia function and responses to neurodegeneration (By similarity). Activation into mature form follows different steps: following cleavage of the proprotein in the Golgi apparatus, Latency-associated peptide (LAP) and Transforming growth factor beta-1 (TGF-beta-1) chains remain non-covalently linked rendering TGF-beta-1 inactive during storage in extracellular matrix. At the same time, LAP chain interacts with 'milieu molecules', such as LTBP1, LRRC32/GARP and LRRC33/NRROS that control activation of TGF-beta-1 and maintain it in a latent state during storage in extracellular milieus. TGF-beta-1 is released from LAP by integrins (ITGAV:ITGB6 or ITGAV:ITGB8): integrin-binding to LAP stabilizes an alternative conformation of the LAP bowtie tail and results in distortion of the LAP chain and subsequent release of the active TGF-beta-1. Once activated following release of LAP, TGF-beta-1 acts by binding to TGF-beta receptors (TGFBR1 and TGFBR2), which transduce signal (By similarity). While expressed by many cells types, TGF-beta-1 only has a very localized range of action within cell environment thanks to fine regulation of its activation by Latency-associated peptide chain (LAP) and 'milieu molecules'. Plays an important role in bone remodeling: acts as a potent stimulator of osteoblastic bone formation, causing chemotaxis, proliferation and differentiation in committed osteoblasts. Can promote either T-helper 17 cells (Th17) or regulatory T-cells (Treg) lineage differentiation in a concentration-dependent manner. At high concentrations, leads to FOXP3-mediated suppression of RORC and down-regulation of IL-17 expression, favoring Treg cell development. At low concentrations in concert with IL-6 and IL-21, leads to expression of the IL-17 and IL-23 receptors, favoring differentiation to Th17 cells (By similarity). Stimulates sustained production of collagen through the activation of CREB3L1 by regulated intramembrane proteolysis (RIP). Mediates SMAD2/3 activation by inducing its phosphorylation and subsequent translocation to the nucleus. Positively regulates odontoblastic differentiation in dental papilla cells, via promotion of IPO7-mediated translocation of phosphorylated SMAD2 to the nucleus and subsequent transcription of target genes (By similarity). Can induce epithelial-to-mesenchymal transition (EMT) and cell migration in various cell types (By similarity). {ECO:0000250|UniProtKB:P01137, ECO:0000250|UniProtKB:P04202}.
|
Equus caballus (Horse)
|
O19045
|
FA10_RABIT
|
MANPLHLVLLGAALAGLLLSGSSVFISRRAANDVLARTRRANSFLEELKKGNLERECMEENCSYEEALEVFEDREKTNEFWNKYVDGDQCESNPCQNQGTCKDGLGMYTCSCVEGYEGQDCEPVTRKLCSLDNGGCDQFCKEEENSVLCSCASGYTLGDNGKSCISTELFPCGKVTLGRWRRSPATNSSEGPPEAPGPEQQDDGNLTATENPFNLLDSPEPPPEDDSSSLVRIVGGQDCRDGECPWQALLVNEENEGFCGGTILSEYHVLTAAHCLHQAKRFKVRVGDRDTEHEEGNEETHEVEVVVKHNRFVKETYDFDIAVLRLKTPITFRRNVAPACLPQKDWAESTLMAQKTGIVSGFGRTHEMGRLSTTLKMLEVPYVDRNSCKRSSSFTITQNMFCAGYDARPEDACQGDSGGPHVTRFRDTYFVTGIVSWGEGCARKGKFGVYTKVSNFLKWIEKSMRARAVPVAEAAGTPGPTQPTIKGSPS
|
3.4.21.6
| null |
blood coagulation [GO:0007596]; positive regulation of leukocyte chemotaxis [GO:0002690]; proteolysis [GO:0006508]
|
extracellular space [GO:0005615]
|
calcium ion binding [GO:0005509]; serine-type endopeptidase activity [GO:0004252]
|
PF00008;PF14670;PF00594;PF00089;
|
4.10.740.10;2.10.25.10;2.40.10.10;
|
Peptidase S1 family
|
PTM: The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium. {ECO:0000250}.; PTM: N- and O-glycosylated. {ECO:0000250}.; PTM: Proteolytically cleaved and activated by cathepsin CTSG (By similarity). The activation peptide is cleaved by factor IXa (in the intrinsic pathway), or by factor VIIa (in the extrinsic pathway) (By similarity). {ECO:0000250|UniProtKB:P00742, ECO:0000250|UniProtKB:P00743}.; PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in prothrombin to form thrombin.; EC=3.4.21.6;
| null | null | null | null |
FUNCTION: Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting.
|
Oryctolagus cuniculus (Rabbit)
|
O19052
|
PPARG_RABIT
|
MVDTEMPFWPTNFGIGSVDLSVMDDHSHSFDIKPFTTVDFSSISAPHYEDLPFARADPMVADYKYDLKLQEYQSAIKVEPASPPYYSEKTQLYNKTHEEPSNSLMAIECRVCSDKASGFHYGVHACEGCKGFFRRTIRLKLIYDRCDLNCRIHKKSRNKCQYCRFQKCLAVGMSHNAIRFGRMPQAEKEKLLAEISSDIDQLNPESADLRALAKHLYDSYIKSFPLTKAKARAILTGKTTDKSPFVIYDMNSLMMGEDKIKFKHITPLQEQSKEVAIRIFQGCQFRSVEAVQEITEYAKNIPGFVSLDLNDQVTLLKYGVHEIIYTMLASLMNKDGVLISEGQGFMTREFLKSLRKPFGDFMEPKFEFAVKFNALELDDSDLAIFIAVIILSGDRPGLLNVKPIEDIQDNLLQALELQLKLNHPEASQLFAKLLQKMTDLRQIVTEHVQLLQVIKKTETDMSLHPLLQEIYKDLY
| null | null |
cellular response to insulin stimulus [GO:0032869]; fatty acid metabolic process [GO:0006631]; hormone-mediated signaling pathway [GO:0009755]; macrophage derived foam cell differentiation [GO:0010742]; negative regulation of cholesterol storage [GO:0010887]; negative regulation of inflammatory response [GO:0050728]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of fat cell differentiation [GO:0045600]; positive regulation of fatty acid metabolic process [GO:0045923]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of circadian rhythm [GO:0042752]; regulation of DNA-templated transcription [GO:0006355]; regulation of transcription by RNA polymerase II [GO:0006357]; retinoic acid receptor signaling pathway [GO:0048384]; rhythmic process [GO:0048511]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
chromatin binding [GO:0003682]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; E-box binding [GO:0070888]; nuclear receptor activity [GO:0004879]; transcription cis-regulatory region binding [GO:0000976]; zinc ion binding [GO:0008270]
|
PF00104;PF12577;PF00105;
|
3.30.50.10;1.10.565.10;
|
Nuclear hormone receptor family, NR1 subfamily
|
PTM: Phosphorylated at basal conditions and dephosphorylated when treated with the ligand. May be dephosphorylated by PPP5C. The phosphorylated form may be inactive and dephosphorylation induces adipogenic activity (By similarity). {ECO:0000250|UniProtKB:P37231}.; PTM: Ubiquitinated by E3 ubiquitin-protein ligase complex containing FBXO9; leading to proteasomal degradation (By similarity). Ubiquitinated at Lys-222 by TRIM55 leading to proteasomal degradation (By similarity). {ECO:0000250|UniProtKB:P37231, ECO:0000250|UniProtKB:P37238}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}. Cytoplasm {ECO:0000250}. Note=Redistributed from the nucleus to the cytosol through a MAP2K1/MEK1-dependent manner. NOCT enhances its nuclear translocation (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Nuclear receptor that binds peroxisome proliferators such as hypolipidemic drugs and fatty acids. Once activated by a ligand, the nuclear receptor binds to DNA specific PPAR response elements (PPRE) and modulates the transcription of its target genes, such as acyl-CoA oxidase. It therefore controls the peroxisomal beta-oxidation pathway of fatty acids. Key regulator of adipocyte differentiation and glucose homeostasis. ARF6 acts as a key regulator of the tissue-specific adipocyte P2 (aP2) enhancer. Acts as a critical regulator of gut homeostasis by suppressing NF-kappa-B-mediated pro-inflammatory responses. Plays a role in the regulation of cardiovascular circadian rhythms by regulating the transcription of BMAL1 in the blood vessels. {ECO:0000250|UniProtKB:P37231, ECO:0000250|UniProtKB:P37238}.
|
Oryctolagus cuniculus (Rabbit)
|
O19053
|
ADHX_RABIT
|
MANKVIKCKAAVAWEAGKPLSIEEIEVAPPKAHEVRIKIFATAVCHTDAYTLSGADPEGCFPVILGHEGAGIVESVGEGVTNLKAGDTVIPLYIPQCGECKFCLNPKTNLCQKIRVTQGKGLMPDGTSRFTCKGKTILHYMGTSTFSEYTVVADISVAKIDPSAPLDKVCLLGCGISTGYGAALNTAKVEPGSTCAVFGLGGVGLAAIMGCKAAGASRIIAVDINKDKFARAKEFGATECINPQDFSKPIQEVLVEKTDGGVDYSFECIGNVKVMRAALEACHKGWGVSVVVGVAGAGEEISTRPFQLVTGRTWKGTAFGGWKSVESVPKLVSEYMSKKINVDEFVTNTLSFDQINEAFELMHSGKSIRTVVKI
|
1.1.1.-; 1.1.1.1; 1.1.1.284
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P11766}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P11766};
|
ethanol oxidation [GO:0006069]; fatty acid omega-oxidation [GO:0010430]; formaldehyde catabolic process [GO:0046294]
|
cytosol [GO:0005829]
|
alcohol dehydrogenase activity, zinc-dependent [GO:0004024]; S-(hydroxymethyl)glutathione dehydrogenase NAD activity [GO:0106322]; S-(hydroxymethyl)glutathione dehydrogenase NADP activity [GO:0106321]; zinc ion binding [GO:0008270]
|
PF08240;PF00107;
|
3.90.180.10;3.40.50.720;
|
Zinc-containing alcohol dehydrogenase family, Class-III subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH; Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734, ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1; Evidence={ECO:0000250|UniProtKB:P11766}; CATALYTIC ACTIVITY: Reaction=a secondary alcohol + NAD(+) = a ketone + H(+) + NADH; Xref=Rhea:RHEA:10740, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087, ChEBI:CHEBI:35681, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1; Evidence={ECO:0000250|UniProtKB:P11766}; CATALYTIC ACTIVITY: Reaction=NADP(+) + S-(hydroxymethyl)glutathione = H(+) + NADPH + S-formylglutathione; Xref=Rhea:RHEA:19981, ChEBI:CHEBI:15378, ChEBI:CHEBI:57688, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:58758; EC=1.1.1.284; Evidence={ECO:0000250|UniProtKB:P11766}; CATALYTIC ACTIVITY: Reaction=NAD(+) + S-(hydroxymethyl)glutathione = H(+) + NADH + S-formylglutathione; Xref=Rhea:RHEA:19985, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57688, ChEBI:CHEBI:57945, ChEBI:CHEBI:58758; EC=1.1.1.284; Evidence={ECO:0000250|UniProtKB:P11766}; CATALYTIC ACTIVITY: Reaction=20-oxo-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H2O + NAD(+) = (5Z,8Z,11Z,14Z)-eicosatetraenedioate + 2 H(+) + NADH; Xref=Rhea:RHEA:39803, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:76645, ChEBI:CHEBI:76647; Evidence={ECO:0000250|UniProtKB:P11766}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39804; Evidence={ECO:0000250|UniProtKB:P11766}; CATALYTIC ACTIVITY: Reaction=20-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + NAD(+) = 20-oxo-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + NADH; Xref=Rhea:RHEA:39799, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:76624, ChEBI:CHEBI:76645; Evidence={ECO:0000250|UniProtKB:P11766}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39800; Evidence={ECO:0000250|UniProtKB:P11766}; CATALYTIC ACTIVITY: Reaction=H(+) + NADH + S-nitrosoglutathione = NAD(+) + sulfinamide glutathione; Xref=Rhea:RHEA:78371, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:145544, ChEBI:CHEBI:145547; Evidence={ECO:0000250|UniProtKB:P28474}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78372; Evidence={ECO:0000250|UniProtKB:P28474};
| null | null | null | null |
FUNCTION: Catalyzes the oxidation of long-chain primary alcohols and the oxidation of S-(hydroxymethyl) glutathione. Also oxidizes long chain omega-hydroxy fatty acids, such as 20-HETE, producing both the intermediate aldehyde, 20-oxoarachidonate and the end product, a dicarboxylic acid, (5Z,8Z,11Z,14Z)-eicosatetraenedioate. Class-III ADH is remarkably ineffective in oxidizing ethanol. Required for clearance of cellular formaldehyde, a cytotoxic and carcinogenic metabolite that induces DNA damage (By similarity). Also acts as a S-nitroso-glutathione reductase by catalyzing the NADH-dependent reduction of S-nitrosoglutathione, thereby regulating protein S-nitrosylation (By similarity). {ECO:0000250|UniProtKB:P11766, ECO:0000250|UniProtKB:P28474}.
|
Oryctolagus cuniculus (Rabbit)
|
O19058
|
FUT3_PANTR
|
MDPLGAAKPQWPWRRCLAALLFQLLVAVCFFSYLRVSRDDATGSPRPGLMAVEPVTGAPSGSSRQDTTPTRPTLLILLWTWPFHIPVALSRCSEMVPGAADCHITADRKVYPQADAVIVHHWDIMYNPKSRLPPSPRPQGQRWIWFNLEPPPNCQHLEALDRYFNLTMSYRSDSDIFTPYGWLEPWSGQPAHPPLNLSAKTELVAWAVSNWKLDSARVRYYQSLQAHLKVDVYGRSHKPLPKGTMMETLSRYKFYLAFENSLHPDYITEKLWRNALEAWAVPVVLGPSRSNYERFLPPDAFIHVDDFQSPKDLARYLQELDKDHARYLSYFRWRETLRPRSFSWALDFCKACWKLQQESRYQTMRSIAAWFT
|
2.4.1.-; 2.4.1.152; 2.4.1.65
| null |
fucosylation [GO:0036065]; lipid metabolic process [GO:0006629]; oligosaccharide metabolic process [GO:0009311]; positive regulation of cell-cell adhesion [GO:0022409]; protein N-linked glycosylation [GO:0006487]; protein O-linked glycosylation [GO:0006493]; regulation of cell migration [GO:0030334]; regulation of cell population proliferation [GO:0042127]
|
Golgi cisterna membrane [GO:0032580]
|
3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase activity [GO:0017060]; 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase activity [GO:0017083]; alpha-(1->3)-fucosyltransferase activity [GO:0046920]
|
PF17039;PF00852;
|
3.40.50.11660;
|
Glycosyltransferase 10 family
|
PTM: Glycosylated. {ECO:0000250|UniProtKB:P21217}.
|
SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:P21217}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P21217}. Note=Membrane-bound form in trans cisternae of Golgi. {ECO:0000250|UniProtKB:P21217}.
|
CATALYTIC ACTIVITY: Reaction=a beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl derivative + GDP-beta-L-fucose = a beta-D-galactosyl-(1->3)-[alpha-L-fucosyl-(1->4)]-N-acetyl-beta-D-glucosaminyl derivative + GDP + H(+); Xref=Rhea:RHEA:23628, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:133506, ChEBI:CHEBI:140304; EC=2.4.1.65; Evidence={ECO:0000250|UniProtKB:P21217}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23629; Evidence={ECO:0000250|UniProtKB:P21217}; CATALYTIC ACTIVITY: Reaction=an N-acetyl-alpha-neuraminyl-(2->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + GDP-beta-L-fucose = an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc derivative + GDP + H(+); Xref=Rhea:RHEA:56076, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:136545, ChEBI:CHEBI:139509; Evidence={ECO:0000250|UniProtKB:P21217}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56077; Evidence={ECO:0000250|UniProtKB:P21217}; CATALYTIC ACTIVITY: Reaction=a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + GDP-beta-L-fucose = a beta-D-galactosyl-(1->4)-[alpha-L-fucosyl-(1->3)]-N-acetyl-beta-D-glucosaminyl derivative + GDP + H(+); Xref=Rhea:RHEA:14257, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:133507, ChEBI:CHEBI:137941; EC=2.4.1.152; Evidence={ECO:0000250|UniProtKB:P21217}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14258; Evidence={ECO:0000250|UniProtKB:P21217}; CATALYTIC ACTIVITY: Reaction=an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc derivative + GDP-beta-L-fucose = an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-beta-D-GlcNAc derivative + GDP + H(+); Xref=Rhea:RHEA:52864, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:145342, ChEBI:CHEBI:145343; Evidence={ECO:0000250|UniProtKB:P21217}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52865; Evidence={ECO:0000250|UniProtKB:P21217}; CATALYTIC ACTIVITY: Reaction=GDP-beta-L-fucose + Lc4Cer = a lactoside III(4)-a-Fuc-Lc4Cer + GDP + H(+); Xref=Rhea:RHEA:48824, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:90800, ChEBI:CHEBI:90811; Evidence={ECO:0000250|UniProtKB:P21217}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48825; Evidence={ECO:0000250|UniProtKB:P21217}; CATALYTIC ACTIVITY: Reaction=a beta-D-Gal-(1->3)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-Glc-(1<->1')-Cer(d18:1(4E)) + GDP-beta-L-fucose = a III(4)-a-Fuc-Lc4Cer(d18:1(4E)) + GDP + H(+); Xref=Rhea:RHEA:48328, ChEBI:CHEBI:15378, ChEBI:CHEBI:17292, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:90292; Evidence={ECO:0000250|UniProtKB:P21217}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48329; Evidence={ECO:0000250|UniProtKB:P21217}; CATALYTIC ACTIVITY: Reaction=GDP-beta-L-fucose + N-acetyl-alpha-neuraminosyl-(2->3)-beta-D-galactosyl-(1->3)-[N-acetyl-alpha-neuraminosyl-(2->6)]-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-N-acyl-sphing-4-enine = GDP + H(+) + N-acetyl-alpha-neuraminosyl-(2->3)-beta-D-galactosyl-(1->3)-alpha-L-fucosyl-(1->4)-[N-acetyl-alpha-neuraminosyl-(2->6)-N-acetyl-beta-D-glucosaminyl-(1->3)]-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-N-acyl-sphing-4-enine; Xref=Rhea:RHEA:47892, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:88079, ChEBI:CHEBI:88089; Evidence={ECO:0000250|UniProtKB:P21217}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47893; Evidence={ECO:0000250|UniProtKB:P21217}; CATALYTIC ACTIVITY: Reaction=GDP-beta-L-fucose + N-acetyl-alpha-neuraminosyl-(2->3)-beta-D-galactosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-N-acyl-sphing-4-enine = GDP + H(+) + N-acetyl-alpha-neuraminosyl-(2->3)-beta-D-galactosyl-(1->3)-alpha-L-fucosyl-(1->4)-[N-acetyl-beta-D-glucosaminyl-(1->3)]-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-N-acyl-sphing-4-enine; Xref=Rhea:RHEA:47888, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:88073, ChEBI:CHEBI:88088; Evidence={ECO:0000250|UniProtKB:P21217}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47889; Evidence={ECO:0000250|UniProtKB:P21217}; CATALYTIC ACTIVITY: Reaction=beta-D-galactosyl-(1->3)-N-acetyl-D-glucosamine + GDP-beta-L-fucose = beta-D-galactosyl-(1->3)-[alpha-L-fucosyl-(1->4)]-N-acetyl-D-glucosamine + GDP + H(+); Xref=Rhea:RHEA:62844, ChEBI:CHEBI:15378, ChEBI:CHEBI:27707, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:62265; Evidence={ECO:0000250|UniProtKB:P21217}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62845; Evidence={ECO:0000250|UniProtKB:P21217}; CATALYTIC ACTIVITY: Reaction=alpha-L-Fuc-(1->2)-beta-D-Gal-(1->3)-D-GlcNAc + GDP-beta-L-fucose = alpha-L-Fuc-(1->2)-beta-D-Gal-(1->3)-[alpha-L-Fuc-(1->4)]-D-GlcNAc + GDP + H(+); Xref=Rhea:RHEA:62896, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:59440, ChEBI:CHEBI:62259; Evidence={ECO:0000250|UniProtKB:P21217}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62897; Evidence={ECO:0000250|UniProtKB:P21217}; CATALYTIC ACTIVITY: Reaction=alpha-L-Fuc-(1->2)-beta-D-Gal-(1->4)-D-GlcNAc + GDP-beta-L-fucose = alpha-L-Fuc-(1->2)-beta-D-Gal-(1->4)-[alpha-L-Fuc-(1->3)]-D-GlcNAc + GDP + H(+); Xref=Rhea:RHEA:62900, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:62263, ChEBI:CHEBI:62507; Evidence={ECO:0000250|UniProtKB:P21217}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62901; Evidence={ECO:0000250|UniProtKB:P21217}; CATALYTIC ACTIVITY: Reaction=beta-D-galactosyl-(1->4)-N-acetyl-D-glucosamine + GDP-beta-L-fucose = beta-D-galactosyl-(1->4)-[alpha-L-fucosyl-(1->3)]-N-acetyl-D-glucosamine + GDP + H(+); Xref=Rhea:RHEA:62824, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:60152, ChEBI:CHEBI:62287; Evidence={ECO:0000250|UniProtKB:P21217}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62825; Evidence={ECO:0000250|UniProtKB:P21217}; CATALYTIC ACTIVITY: Reaction=GDP-beta-L-fucose + lactose = beta-D-galactosyl-(1->4)-[alpha-L-fucosyl-(1->3)]-D-glucose + GDP + H(+); Xref=Rhea:RHEA:62888, ChEBI:CHEBI:15378, ChEBI:CHEBI:17716, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:90065; Evidence={ECO:0000250|UniProtKB:P21217}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62889; Evidence={ECO:0000250|UniProtKB:P21217}; CATALYTIC ACTIVITY: Reaction=an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-D-GlcNAc derivative + GDP-beta-L-fucose = an alpha-Neu5Ac-(2->3)-beta-D-Gal-(1->3)-[alpha-L-Fuc-(1->4)]-beta-D-GlcNAc derivative + GDP + H(+); Xref=Rhea:RHEA:62904, ChEBI:CHEBI:15378, ChEBI:CHEBI:57273, ChEBI:CHEBI:58189, ChEBI:CHEBI:146021, ChEBI:CHEBI:146022; Evidence={ECO:0000250|UniProtKB:P21217}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62905; Evidence={ECO:0000250|UniProtKB:P21217};
| null |
PATHWAY: Protein modification; protein glycosylation. {ECO:0000250|UniProtKB:P21217}.
| null | null |
FUNCTION: Catalyzes the transfer of L-fucose, from a guanosine diphosphate-beta-L-fucose, to both the subterminal N-acetyl glucosamine (GlcNAc) of type 1 chain (beta-D-Gal-(1->3)-beta-D-GlcNAc) glycolipids and oligosaccharides via an alpha(1,4) linkage, and the subterminal glucose (Glc) or GlcNAc of type 2 chain (beta-D-Gal-(1->4)-beta-D-GlcNAc) oligosaccharides via an alpha(1,3) linkage, independently of the presence of terminal alpha-L-fucosyl-(1,2) moieties on the terminal galactose of these acceptors and participates in the blood groups Lewis determination and expression of Lewis a (Le(a)), lewis b (Le(b)), Lewis x/SSEA-1 (Le(x)) and lewis y (Le(y)) antigens. Also catalyzes the transfer of L-fucose to subterminal GlcNAc of sialyl- and disialyl-lactotetraosylceramide to produce sialyl Lewis a (sLe(a)) and disialyl Lewis a via an alpha(1,4) linkage and therefore may regulate cell surface sialyl Lewis a expression and consequently regulates adhesive properties to E-selectin, cell proliferation and migration. Catalyzes the transfer of an L-fucose to 3'-sialyl-N-acetyllactosamine by an alpha(1,3) linkage, which allows the formation of sialyl-Lewis x structure and therefore may regulate the sialyl-Lewis x surface antigen expression and consequently adhesive properties to E-selectin. Prefers type 1 chain over type 2 acceptors. Type 1 tetrasaccharide is a better acceptor than type 1 disaccharide suggesting that a beta anomeric configuration of GlcNAc in the substrate is preferred. Lewis-positive (Le(+)) individuals have an active enzyme while Lewis-negative (Le(-)) individuals have an inactive enzyme. {ECO:0000250|UniProtKB:P21217}.
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Pan troglodytes (Chimpanzee)
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O19064
|
JAK2_PIG
|
MGMACLTMTEMEGTSTSPVHQNGDIPGNANSVKQIDPVLQVYLYHSLGKAEGDYLKFPAGEYVAEEICVAASKACGITPVYHSMFALMNETERIWYPPNHVFHVDESTRHNVLYRIRFYFPYWYCNGSNRTYRHGISRGAEAPLLDDFVMSYLFAQWRHDFLYGWVKIPVTHETQEECLGMAVLDMMRIAKEKDQTPLDIYSSVSYKTFLPKCVRAKIQDYHILTRKRIRYRFRRFIEQFSHCKATARNLKLKYLINLETLQSAFYTEQFEVKEPGRGPSGEEIFATIIITGNGGIQWSRGKHKESETLTEQDLQLYCDFPDIIDVSIKQANQEGSNESRIVTIHKQDGKSLEIELSSLREALSFVSLIDGYYRLTADAHHYLCKEVAPPMVLENIQSNCHGPISMDFAISKLKKAGNQTGLFVLRCSPKDFNKYFLTFAVERENVTEYKHCLITKNENGEYNLSGTRKNFSNLKDLLNCYQMETVRSDSIIFQFTKCCPPKPKDKSNLLVFRTNGISDVPTSPTLQRHNNVNQMVFHKIRNEDLIFNESLGQGTFTKIFKGVRREVGDYGQLHETEVLLKVLDKAHRNYSESFFEAASMMSQLSHKHLVLNYGVCVCGEENILVQEFVKFGSLDTYLKKNKNSINILWKLEVAKQLAWAMHFLEEKTLIHGNVCAKNILLIREEDRKTGNPPFIKLSDPGISITVLPKDILQERIPWVPPECIENPKNLNLATDKWSFGTTLWEICSGGDKPLNALDSQRKLQFYEDRHQLPAPKWTELANLINNCMDYEPDFRPSFRAIIRDLNSLFTPDYELLTENDMLPNMRIGALGFSGAFEDRDPTQFEERHLKFLQQLGKGNFGSVEMCRYDPLQDNTGEVVAVKKLQHSTEEHLRDFEREIEILKSLQHDNIVKYKGVCYSAGRRNLRLIMEYLPYGSLRDYLQKHKERIDHKKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTKVLPQDKEYYKVKEPGESPIFWYAPESLTESKFSVASDVWSFGVVLYELFTYIEKSKSPPAEFMRMIGNDKQGQMIVFHLIELLKNNGRLPRPDGCPDEIYIIMTECWNNNVNQRPSFRDLALRVDQIRDSMA
|
2.7.10.2
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305}; Note=Mn(2+) was used in the in vitro kinase assay but Mg(2+) is likely to be the in vivo cofactor. {ECO:0000305};
|
activation of Janus kinase activity [GO:0042976]; adaptive immune response [GO:0002250]; cellular response to dexamethasone stimulus [GO:0071549]; cellular response to interleukin-3 [GO:0036016]; cellular response to lipopolysaccharide [GO:0071222]; collagen-activated signaling pathway [GO:0038065]; cytokine-mediated signaling pathway [GO:0019221]; erythrocyte differentiation [GO:0030218]; extrinsic apoptotic signaling pathway [GO:0097191]; granulocyte-macrophage colony-stimulating factor signaling pathway [GO:0038157]; growth hormone receptor signaling pathway via JAK-STAT [GO:0060397]; innate immune response [GO:0045087]; interleukin-12-mediated signaling pathway [GO:0035722]; interleukin-3-mediated signaling pathway [GO:0038156]; interleukin-5-mediated signaling pathway [GO:0038043]; intracellular signal transduction [GO:0035556]; mammary gland epithelium development [GO:0061180]; microglial cell activation [GO:0001774]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell population proliferation [GO:0008285]; positive regulation of apoptotic signaling pathway [GO:2001235]; positive regulation of cell-substrate adhesion [GO:0010811]; positive regulation of cold-induced thermogenesis [GO:0120162]; positive regulation of growth hormone receptor signaling pathway [GO:0060399]; positive regulation of interleukin-1 beta production [GO:0032731]; positive regulation of MHC class II biosynthetic process [GO:0045348]; positive regulation of natural killer cell proliferation [GO:0032819]; positive regulation of nitric-oxide synthase biosynthetic process [GO:0051770]; positive regulation of NK T cell proliferation [GO:0051142]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of platelet activation [GO:0010572]; positive regulation of platelet aggregation [GO:1901731]; positive regulation of SMAD protein signal transduction [GO:0060391]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of tumor necrosis factor production [GO:0032760]; positive regulation of type II interferon production [GO:0032729]; positive regulation of tyrosine phosphorylation of STAT protein [GO:0042531]; post-embryonic hemopoiesis [GO:0035166]; post-translational protein modification [GO:0043687]; protein autophosphorylation [GO:0046777]; receptor signaling pathway via JAK-STAT [GO:0007259]; regulation of apoptotic process [GO:0042981]; regulation of inflammatory response [GO:0050727]; response to antibiotic [GO:0046677]; signal transduction [GO:0007165]; symbiont-induced defense-related programmed cell death [GO:0034050]; transcription by RNA polymerase II [GO:0006366]; tumor necrosis factor-mediated signaling pathway [GO:0033209]
|
caveola [GO:0005901]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; endomembrane system [GO:0012505]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; focal adhesion [GO:0005925]; granulocyte macrophage colony-stimulating factor receptor complex [GO:0030526]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; growth hormone receptor binding [GO:0005131]; heme binding [GO:0020037]; histone binding [GO:0042393]; histone H3Y41 kinase activity [GO:0035401]; identical protein binding [GO:0042802]; interleukin-12 receptor binding [GO:0005143]; metal ion binding [GO:0046872]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein kinase binding [GO:0019901]; protein tyrosine kinase activity [GO:0004713]; SH2 domain binding [GO:0042169]
|
PF18379;PF18377;PF17887;PF07714;PF00017;
|
2.30.29.30;3.30.505.10;1.10.510.10;
|
Protein kinase superfamily, Tyr protein kinase family, JAK subfamily
|
PTM: Autophosphorylated, leading to regulate its activity. Leptin promotes phosphorylation on tyrosine residues, including phosphorylation on Tyr-813. Autophosphorylation on Tyr-119 in response to EPO down-regulates its kinase activity. Autophosphorylation on Tyr-868, Tyr-966 and Tyr-972 in response to growth hormone (GH) are required for maximal kinase activity. Also phosphorylated by TEC (By similarity). Phosphorylated on tyrosine residues in response to interferon gamma signaling. Phosphorylated on tyrosine residues in response to a signaling cascade that is activated by increased cellular retinol (By similarity). {ECO:0000250|UniProtKB:O60674, ECO:0000250|UniProtKB:Q62120}.; PTM: Undergoes Notch-induced ubiquitination and subsequent proteasomal degradation which is mediated by ASB1 or ASB2, the substrate-recognition components of probable ECS E3 ubiquitin-protein ligase complexes. {ECO:0000250|UniProtKB:O60674}.
|
SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
| null | null | null | null |
FUNCTION: Non-receptor tyrosine kinase involved in various processes such as cell growth, development, differentiation or histone modifications. Mediates essential signaling events in both innate and adaptive immunity. In the cytoplasm, plays a pivotal role in signal transduction via its association with type I receptors such as growth hormone (GHR), prolactin (PRLR), leptin (LEPR), erythropoietin (EPOR), thrombopoietin (THPO); or type II receptors including IFN-alpha, IFN-beta, IFN-gamma and multiple interleukins. Following ligand-binding to cell surface receptors, phosphorylates specific tyrosine residues on the cytoplasmic tails of the receptor, creating docking sites for STATs proteins. Subsequently, phosphorylates the STATs proteins once they are recruited to the receptor. Phosphorylated STATs then form homodimer or heterodimers and translocate to the nucleus to activate gene transcription. For example, cell stimulation with erythropoietin (EPO) during erythropoiesis leads to JAK2 autophosphorylation, activation, and its association with erythropoietin receptor (EPOR) that becomes phosphorylated in its cytoplasmic domain. Then, STAT5 (STAT5A or STAT5B) is recruited, phosphorylated and activated by JAK2. Once activated, dimerized STAT5 translocates into the nucleus and promotes the transcription of several essential genes involved in the modulation of erythropoiesis. Part of a signaling cascade that is activated by increased cellular retinol and that leads to the activation of STAT5 (STAT5A or STAT5B). In addition, JAK2 mediates angiotensin-2-induced ARHGEF1 phosphorylation. Plays a role in cell cycle by phosphorylating CDKN1B. Cooperates with TEC through reciprocal phosphorylation to mediate cytokine-driven activation of FOS transcription. In the nucleus, plays a key role in chromatin by specifically mediating phosphorylation of 'Tyr-41' of histone H3 (H3Y41ph), a specific tag that promotes exclusion of CBX5 (HP1 alpha) from chromatin. {ECO:0000250|UniProtKB:O60674}.
|
Sus scrofa (Pig)
|
O19069
|
SUCA_PIG
|
MTAALVAAPAAATMASGSSGLAAARLLSRSFLLQQNGIRHCSYTASRKHLYVDKNTKVICQGFTGKQGTFHSQQALEYGTNLVGGTTPGKGGKTHLGLPVFNTVKEAKEQTGATASVIYVPPPFAAAAINEAIDAEVPLVVCITEGIPQQDMVRVKHRLLRQGKTRLIGPNCPGVINPGECKIGIMPGHIHKKGRIGIVSRSGTLTYEAVHQTTQVGLGQSLCVGIGGDPFNGTDFTDCLEIFLNDPATEGIILIGEIGGNAEENAAEFLKQHNSGPKSKPVVSFIAGLTAPPGRRMGHAGAIIAGGKGGAKEKITALQSAGVVVSMSPAQLGTTIYKEFEKRKML
|
6.2.1.4; 6.2.1.5
| null |
tricarboxylic acid cycle [GO:0006099]
|
cytosol [GO:0005829]; mitochondrion [GO:0005739]; succinate-CoA ligase complex (ADP-forming) [GO:0009361]
|
nucleotide binding [GO:0000166]; succinate-CoA ligase (ADP-forming) activity [GO:0004775]; succinate-CoA ligase (GDP-forming) activity [GO:0004776]
|
PF02629;PF00549;
|
3.40.50.720;3.40.50.261;
|
Succinate/malate CoA ligase alpha subunit family
| null |
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03222}.
|
CATALYTIC ACTIVITY: Reaction=ATP + CoA + succinate = ADP + phosphate + succinyl-CoA; Xref=Rhea:RHEA:17661, ChEBI:CHEBI:30031, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:456216; EC=6.2.1.5; Evidence={ECO:0000255|HAMAP-Rule:MF_03222}; CATALYTIC ACTIVITY: Reaction=CoA + GTP + succinate = GDP + phosphate + succinyl-CoA; Xref=Rhea:RHEA:22120, ChEBI:CHEBI:30031, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:58189; EC=6.2.1.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03222, ECO:0000269|PubMed:27487822};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.76 mM for succinate {ECO:0000269|PubMed:27487822}; Vmax=5.99 umol/min/mg enzyme {ECO:0000269|PubMed:27487822};
|
PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate from succinyl-CoA (ligase route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_03222}.
| null | null |
FUNCTION: Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and specificity for either ATP or GTP is provided by different beta subunits. {ECO:0000255|HAMAP-Rule:MF_03222}.
|
Sus scrofa (Pig)
|
O19073
|
IL18_PIG
|
MAAEPEDNCISFVEMKFINNTLYFVAENDEDLESDYFGKLEPKLSIIRNLNDQVLFINQGHQAVFEDMPDSDCSDNAPQTVFIIYMYKDSLTRGLAVTISVQCKKMSTLSCKNKTLSFKEMSPPDNIDDEGNDIIFFQRSVPGHDDKIQFESSLYKGYFLACKKENDLFKLILKEKDECGDKSIMFTVQNKN
| null | null |
angiogenesis [GO:0001525]; cellular response to lipopolysaccharide [GO:0071222]; defense response to Gram-positive bacterium [GO:0050830]; establishment of skin barrier [GO:0061436]; extrinsic apoptotic signaling pathway via death domain receptors [GO:0008625]; immune response [GO:0006955]; inflammatory response [GO:0006954]; interleukin-18-mediated signaling pathway [GO:0035655]; positive regulation of activated T cell proliferation [GO:0042104]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of inflammatory response [GO:0050729]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of T-helper 1 cell cytokine production [GO:2000556]; positive regulation of type II interferon production [GO:0032729]
|
cytosol [GO:0005829]; extracellular space [GO:0005615]
|
cytokine activity [GO:0005125]; interleukin-18 receptor binding [GO:0045515]
|
PF00340;
|
2.80.10.50;
|
IL-1 family
|
PTM: The pro-IL-18 precursor is processed by CASP1, CASP4 or CASP5 to yield its mature, active form. The pro-IL-18 precursor features autoinhibitory interactions between the propeptide and the post-cleavage-site region, preventing recognition by the IL18R1 receptor. Processing by CASP1, CASP4 or CASP5 induces conformational changes to generate critical receptor-binding sites. The mature form is then secreted and released in the extracellular milieu by passing through the gasdermin-D (GSDMD) pore. In contrast, cleavage by CASP3 inactivates IL18. {ECO:0000250|UniProtKB:Q14116}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q14116}. Secreted {ECO:0000250|UniProtKB:Q14116}. Note=The precursor is cytosolic. In response to inflammasome-activating signals, cleaved and secreted. Mature form is secreted and released in the extracellular milieu by passing through the gasdermin-D (GSDMD) pore. In contrast, the precursor form is not released, due to the presence of an acidic region that is proteolytically removed by CASP1, CASP4 or CASP5 during maturation. The secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10. {ECO:0000250|UniProtKB:Q14116}.
| null | null | null | null | null |
FUNCTION: Pro-inflammatory cytokine primarily involved in epithelial barrier repair, polarized T-helper 1 (Th1) cell and natural killer (NK) cell immune responses. Upon binding to IL18R1 and IL18RAP, forms a signaling ternary complex which activates NF-kappa-B, triggering synthesis of inflammatory mediators. Synergizes with IL12/interleukin-12 to induce IFNG synthesis from T-helper 1 (Th1) cells and natural killer (NK) cells. Involved in transduction of inflammation downstream of pyroptosis: its mature form is specifically released in the extracellular milieu by passing through the gasdermin-D (GSDMD) pore. {ECO:0000250|UniProtKB:Q14116}.
|
Sus scrofa (Pig)
|
O19105
|
AAAT_RABIT
|
MVADPPKGDPKGLAAVEPTANGAPAQDPLEDSGAAVGRCCSSRDQVRRCLRANLLVLLTVVAVVAGVALGLAVSGAGGALALGPARLIAFAFPGELLLRLLKMIILPLVVCSLVGGAASLDPSALGRLGAWALLFFLVTTLLASALGVGLALALQPGAAFAAMNASLSSTGAVEQTPSKQVLDSFLDLLRNIFPSNLVSAAFRSYSTSYEEKNFNGTLVKVPVAHEEEGMNILGLVVFAIVFGVALRKLGPEGEPLIRFFNSFNDATMVLVSWIMWYAPVGILFLVASKIVEMDDVGVLFASLGKYILCCLLGHAIHGLLVLPLIYFLFTRKNPYRFLWGILTPLAMAFGTSSSSATLPLMMKCVEERNGVAKHISRFVLPIGATVNMDGAALFQCVAAVFIAQLNRQSLDFVKIITILVTATASSVGAAGIPAGGVLTLAIILEAVSLPVSEISLILAVDWLVDRSCTIINVEGDAFGAGLLQHYVDRTEQRGSEPELTQVKSEVPLGSLPAPNEEGNPLLRHSPGAAGDAGACEKESVM
| null | null |
glutamine transport [GO:0006868]; L-aspartate import across plasma membrane [GO:0140009]; protein homotrimerization [GO:0070207]
|
melanosome [GO:0042470]; membrane [GO:0016020]; plasma membrane [GO:0005886]
|
antiporter activity [GO:0015297]; L-aspartate transmembrane transporter activity [GO:0015183]; L-glutamine transmembrane transporter activity [GO:0015186]; metal ion binding [GO:0046872]; symporter activity [GO:0015293]
|
PF00375;
|
1.10.3860.10;
|
Dicarboxylate/amino acid:cation symporter (DAACS) (TC 2.A.23) family, SLC1A5 subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9227483}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q15758}. Melanosome {ECO:0000250|UniProtKB:Q15758}.
|
CATALYTIC ACTIVITY: Reaction=L-glutamine(out) + L-serine(in) + Na(+)(out) = L-glutamine(in) + L-serine(out) + Na(+)(in); Xref=Rhea:RHEA:70855, ChEBI:CHEBI:29101, ChEBI:CHEBI:33384, ChEBI:CHEBI:58359; Evidence={ECO:0000250|UniProtKB:Q15758}; CATALYTIC ACTIVITY: Reaction=L-glutamine(in) + L-serine(out) + Na(+)(out) = L-glutamine(out) + L-serine(in) + Na(+)(in); Xref=Rhea:RHEA:70887, ChEBI:CHEBI:29101, ChEBI:CHEBI:33384, ChEBI:CHEBI:58359; Evidence={ECO:0000250|UniProtKB:Q15758}; CATALYTIC ACTIVITY: Reaction=L-glutamine(out) + L-threonine(in) + Na(+)(out) = L-glutamine(in) + L-threonine(out) + Na(+)(in); Xref=Rhea:RHEA:70863, ChEBI:CHEBI:29101, ChEBI:CHEBI:57926, ChEBI:CHEBI:58359; Evidence={ECO:0000250|UniProtKB:Q15758}; CATALYTIC ACTIVITY: Reaction=L-glutamine(in) + L-threonine(out) + Na(+)(out) = L-glutamine(out) + L-threonine(in) + Na(+)(in); Xref=Rhea:RHEA:70879, ChEBI:CHEBI:29101, ChEBI:CHEBI:57926, ChEBI:CHEBI:58359; Evidence={ECO:0000250|UniProtKB:Q15758}; CATALYTIC ACTIVITY: Reaction=L-asparagine(in) + L-glutamine(out) + Na(+)(out) = L-asparagine(out) + L-glutamine(in) + Na(+)(in); Xref=Rhea:RHEA:70859, ChEBI:CHEBI:29101, ChEBI:CHEBI:58048, ChEBI:CHEBI:58359; Evidence={ECO:0000250|UniProtKB:Q15758}; CATALYTIC ACTIVITY: Reaction=L-asparagine(out) + L-glutamine(in) + Na(+)(out) = L-asparagine(in) + L-glutamine(out) + Na(+)(in); Xref=Rhea:RHEA:70891, ChEBI:CHEBI:29101, ChEBI:CHEBI:58048, ChEBI:CHEBI:58359; Evidence={ECO:0000250|UniProtKB:Q15758}; CATALYTIC ACTIVITY: Reaction=L-alanine(out) + L-glutamine(in) + Na(+)(out) = L-alanine(in) + L-glutamine(out) + Na(+)(in); Xref=Rhea:RHEA:70867, ChEBI:CHEBI:29101, ChEBI:CHEBI:57972, ChEBI:CHEBI:58359; Evidence={ECO:0000250|UniProtKB:Q15758}; CATALYTIC ACTIVITY: Reaction=L-glutamine(in) + L-valine(out) + Na(+)(out) = L-glutamine(out) + L-valine(in) + Na(+)(in); Xref=Rhea:RHEA:70871, ChEBI:CHEBI:29101, ChEBI:CHEBI:57762, ChEBI:CHEBI:58359; Evidence={ECO:0000250|UniProtKB:Q15758}; CATALYTIC ACTIVITY: Reaction=L-glutamine(in) + L-methionine(out) + Na(+)(out) = L-glutamine(out) + L-methionine(in) + Na(+)(in); Xref=Rhea:RHEA:70875, ChEBI:CHEBI:29101, ChEBI:CHEBI:57844, ChEBI:CHEBI:58359; Evidence={ECO:0000250|UniProtKB:Q15758}; CATALYTIC ACTIVITY: Reaction=H(+)(out) + L-glutamate(out) + L-glutamine(in) + Na(+)(out) = H(+)(in) + L-glutamate(in) + L-glutamine(out) + Na(+)(in); Xref=Rhea:RHEA:70883, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; Evidence={ECO:0000250|UniProtKB:Q15758}; CATALYTIC ACTIVITY: Reaction=D-serine(in) + L-glutamine(out) + Na(+)(out) = D-serine(out) + L-glutamine(in) + Na(+)(in); Xref=Rhea:RHEA:75307, ChEBI:CHEBI:29101, ChEBI:CHEBI:35247, ChEBI:CHEBI:58359; Evidence={ECO:0000250|UniProtKB:Q15758}; CATALYTIC ACTIVITY: Reaction=D-serine(in) + L-alanine(out) + Na(+)(out) = D-serine(out) + L-alanine(in) + Na(+)(in); Xref=Rhea:RHEA:75311, ChEBI:CHEBI:29101, ChEBI:CHEBI:35247, ChEBI:CHEBI:57972; Evidence={ECO:0000250|UniProtKB:Q15758}; CATALYTIC ACTIVITY: Reaction=nitrate(in) = nitrate(out); Xref=Rhea:RHEA:34923, ChEBI:CHEBI:17632; Evidence={ECO:0000250|UniProtKB:D3ZJ25}; CATALYTIC ACTIVITY: Reaction=iodide(out) = iodide(in); Xref=Rhea:RHEA:66324, ChEBI:CHEBI:16382; Evidence={ECO:0000250|UniProtKB:D3ZJ25}; CATALYTIC ACTIVITY: Reaction=thiocyanate(in) = thiocyanate(out); Xref=Rhea:RHEA:75347, ChEBI:CHEBI:18022; Evidence={ECO:0000250|UniProtKB:D3ZJ25};
| null | null | null | null |
FUNCTION: Sodium-coupled antiporter of neutral amino acids. In a tri-substrate transport cycle, exchanges neutral amino acids between the extracellular and intracellular compartments, coupled to the inward cotransport of at least one sodium ion (By similarity) (PubMed:9227483). The preferred substrate is the essential amino acid L-glutamine, a precursor for biosynthesis of proteins, nucleotides and amine sugars as well as an alternative fuel for mitochondrial oxidative phosphorylation. Exchanges L-glutamine with other neutral amino acids such as L-serine, L-threonine and L-asparagine in a bidirectional way. Provides L-glutamine to proliferating stem and activated cells driving the metabolic switch toward cell differentiation (By similarity). The transport cycle is usually pH-independent, with the exception of L-glutamate. Transports extracellular L-glutamate coupled to the cotransport of one proton and one sodium ion in exchange for intracellular L-glutamine counter-ion. May provide for L-glutamate uptake in glial cells regulating glutamine/glutamate cycle in the nervous system (By similarity). Can transport D-amino acids. Mediates D-serine release from the retinal glia potentially affecting NMDA receptor function in retinal neurons (By similarity). Displays sodium- and amino acid-dependent but uncoupled channel-like anion conductance with a preference SCN(-) >> NO3(-) > I(-) > Cl(-) (By similarity). Through binding of the fusogenic protein syncytin-1/ERVW-1 may mediate trophoblasts syncytialization, the spontaneous fusion of their plasma membranes, an essential process in placental development (By similarity). {ECO:0000250|UniProtKB:D3ZJ25, ECO:0000250|UniProtKB:Q15758, ECO:0000269|PubMed:9227483}.
|
Oryctolagus cuniculus (Rabbit)
|
O19111
|
KPCZ_RABIT
|
MPSRAGPKMDGSGGRVRLKAHYSGDIFITSVDAATTFEELCEEVRDMCGLHQHHPLTLKWVDSEGDPRTVSSQMELGEAFRLAGQHRDDGLILHVFPSTPEQPGMPCPGEDKSIYRRGARRWRKLYRANGHLFQAKRFNRRAYCGQCSERIWGLARQGYRCINCKLLVHKRCHGLVPLTCRRHMDSVMPSQEPPVADKSDDADLPSQETDGIAFISTRKQDSGQEDAEDLKPVIDGVDGIKISQGLGLQDFDLIRVIGRGSYAKVLLVRLKKNGQVYAMKVVKKELVHDDEDIDWVQTEKHVFEQASGNPFLVGLHSCFQTTSRLFLVIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPGDTTSTFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFDIITDNPDMNTEDYLFQVILEKPIRIPRFLSVKASHVLKGFLNKDPKERLGCRPQTGFSDIKSHAFFRSIDWDLLEKKQALPPFQPQITDDYGLDNSDTQFTSEPVQLTPDDEDVIKRIDQSEFEGFEYINPLLLSTEESV
|
2.7.11.13
| null |
establishment of cell polarity [GO:0030010]; inflammatory response [GO:0006954]; long-term synaptic potentiation [GO:0060291]; phosphorylation [GO:0016310]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of excitatory postsynaptic potential [GO:2000463]; positive regulation of insulin receptor signaling pathway [GO:0046628]; positive regulation of interleukin-10 production [GO:0032733]; positive regulation of interleukin-13 production [GO:0032736]; positive regulation of interleukin-4 production [GO:0032753]; positive regulation of interleukin-5 production [GO:0032754]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; positive regulation of T-helper 2 cell cytokine production [GO:2000553]; positive regulation of T-helper 2 cell differentiation [GO:0045630]
|
cell-cell junction [GO:0005911]; endosome [GO:0005768]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
ATP binding [GO:0005524]; diacylglycerol-dependent serine/threonine kinase activity [GO:0004697]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00130;PF00564;PF00069;PF00433;
|
3.30.60.20;1.10.510.10;
|
Protein kinase superfamily, AGC Ser/Thr protein kinase family, PKC subfamily
|
PTM: CDH5 is required for its phosphorylation at Thr-409. Phosphorylated by protein kinase PDPK1; phosphorylation is inhibited by the apoptotic C-terminal cleavage product of PKN2. Phosphorylation at Thr-409 by PI3K activates the kinase (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q05513}. Endosome {ECO:0000250|UniProtKB:Q05513}. Cell junction {ECO:0000250|UniProtKB:Q05513}. Membrane {ECO:0000250|UniProtKB:P09217}; Peripheral membrane protein {ECO:0000305}. Note=In the retina, localizes in the terminals of the rod bipolar cells (By similarity). Associated with endosomes (By similarity). Presence of KRIT1, CDH5 and RAP1B is required for its localization to the cell junction (By similarity). Colocalizes with VAMP2 and WDFY2 in intracellular vesicles (By similarity). Transiently translocates to the membrane of CA1 hippocampal cells in response to the induction of long term potentiation (By similarity). {ECO:0000250|UniProtKB:P09217, ECO:0000250|UniProtKB:Q05513}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.13; Evidence={ECO:0000250|UniProtKB:Q05513}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.13; Evidence={ECO:0000250|UniProtKB:Q05513};
| null | null | null | null |
FUNCTION: Calcium- and diacylglycerol-independent serine/threonine-protein kinase that functions in phosphatidylinositol 3-kinase (PI3K) pathway and mitogen-activated protein (MAP) kinase cascade, and is involved in NF-kappa-B activation, mitogenic signaling, cell proliferation, cell polarity, inflammatory response and maintenance of long-term potentiation (LTP). Upon lipopolysaccharide (LPS) treatment in macrophages, or following mitogenic stimuli, functions downstream of PI3K to activate MAP2K1/MEK1-MAPK1/ERK2 signaling cascade independently of RAF1 activation. Required for insulin-dependent activation of AKT3, but may function as an adapter rather than a direct activator. Upon insulin treatment may act as a downstream effector of PI3K and contribute to the activation of translocation of the glucose transporter SLC2A4/GLUT4 and subsequent glucose transport in adipocytes. In EGF-induced cells, binds and activates MAP2K5/MEK5-MAPK7/ERK5 independently of its kinase activity and can activate JUN promoter through MEF2C. Through binding with SQSTM1/p62, functions in interleukin-1 signaling and activation of NF-kappa-B with the specific adapters RIPK1 and TRAF6. Participates in TNF-dependent transactivation of NF-kappa-B by phosphorylating and activating IKBKB kinase, which in turn leads to the degradation of NF-kappa-B inhibitors. In migrating astrocytes, forms a cytoplasmic complex with PARD6A and is recruited by CDC42 to function in the establishment of cell polarity along with the microtubule motor and dynein. In association with FEZ1, stimulates neuronal differentiation in PC12 cells. In the inflammatory response, is required for the T-helper 2 (Th2) differentiation process, including interleukin production, efficient activation of JAK1 and the subsequent phosphorylation and nuclear translocation of STAT6. May be involved in development of allergic airway inflammation (asthma), a process dependent on Th2 immune response. In the NF-kappa-B-mediated inflammatory response, can relieve SETD6-dependent repression of NF-kappa-B target genes by phosphorylating the RELA subunit at 'Ser-311'. Phosphorylates VAMP2 in vitro (By similarity). {ECO:0000250|UniProtKB:P09217, ECO:0000250|UniProtKB:Q05513}.
|
Oryctolagus cuniculus (Rabbit)
|
O19116
|
SFRP1_BOVIN
|
MGGGRWAAAGALLALAAGLLAAGSASEYDYVSFQSDIGAYQSGRFYTKPPQCVDIPADLRLCHNVGYKRMVLPNLLEHETMAEVKQQASSWVPLLNKNCHIGTQVFLCSLFAPVCLDRPIYPCRWLCEAVRDSCEPVMQFFGFYWPEMLKCDKFPEGDVCIAMTPPNATEASKPQGTTVCPPCDNELKSEAIIEHLCASEFALRMKIKEVKKENGDKKIVPKKKKPLKLGPIKKKELKKLVLYLKNGADCPCHQLDNLSHHFLIMGRKVKSQYLLTAIHKWDKKNKEFKTFMKKMKNHECPTFQSVFK
| null | null |
actin cytoskeleton organization [GO:0030036]; canonical Wnt signaling pathway [GO:0060070]; cell differentiation [GO:0030154]; non-canonical Wnt signaling pathway [GO:0035567]; positive regulation of cell-matrix adhesion [GO:0001954]; positive regulation of focal adhesion assembly [GO:0051894]; positive regulation of GTPase activity [GO:0043547]; positive regulation of stress fiber assembly [GO:0051496]; regulation of angiogenesis [GO:0045765]; substrate adhesion-dependent cell spreading [GO:0034446]
|
extracellular space [GO:0005615]; plasma membrane [GO:0005886]
|
frizzled binding [GO:0005109]; Wnt-protein binding [GO:0017147]
|
PF01392;PF01759;
|
2.40.50.120;1.10.2000.10;
|
Secreted frizzled-related protein (sFRP) family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10381896}. Note=Cell membrane or extracellular matrix-associated. Released by heparin-binding.
| null | null | null | null | null |
FUNCTION: Soluble frizzled-related proteins (sFRPS) function as modulators of Wnt signaling through direct interaction with Wnts. They have a role in regulating cell growth and differentiation in specific cell types. SFRP1 decreases intracellular beta-catenin levels (By similarity). Has antiproliferative effects on vascular cells, in vitro and in vivo, and can induce, in vivo, an angiogenic response. In vascular cell cycle, delays the G1 phase and entry into the S phase (By similarity). In kidney development, inhibits tubule formation and bud growth in metanephroi (By similarity). Inhibits WNT1/WNT4-mediated TCF-dependent transcription. {ECO:0000250}.
|
Bos taurus (Bovine)
|
O19131
|
TNR1A_BOVIN
|
MGLPTVPGLLLPLVLPALLADVYPAGVQGLVPHPGDLEKRESPCPQGKYNHPQNSTICCTKCHKGTYLYNDCPGPGRDTDCRVCAPGTYTALENHLRRCLSCSRCRDEMFQVEISPCVVDRDTVCGCRKNQYREYWGETGFRCLNCSLCPNGTVNIPCQERQDTICHCHMGFFLKGAKCISCHDCKNKECEKLCPTRPSTGKDSQDPGTTVLLPLVIVFGLCLASFASVVLACRYQRWKPKLYSIICGQSTLVKEGEPELLVPAPGFNPTTTICFSSTPSSSPVSIPPYISCDRSNFGAVASPSSETAPPHLKAGPILPGPPASTHLCTPGPPASTHLCTPGPPASTHLCTPVQKWEASAPSAPDQLADADPATLYAVVDGVPPSRWKELVRRLGLSEHEIERLELENGRHLREAQYSMLAAWRRRTPRREATLELLGRVLRDMDLLGCLENIEEALGGAARLASEPRLLW
| null | null |
apoptotic process [GO:0006915]; cell surface receptor signaling pathway [GO:0007166]; cytokine-mediated signaling pathway [GO:0019221]; defense response [GO:0006952]; inflammatory response [GO:0006954]; positive regulation of inflammatory response [GO:0050729]; positive regulation of transcription by RNA polymerase II [GO:0045944]; prostaglandin metabolic process [GO:0006693]
|
Golgi membrane [GO:0000139]; membrane raft [GO:0045121]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]
|
tumor necrosis factor binding [GO:0043120]; tumor necrosis factor receptor activity [GO:0005031]
|
PF00531;PF00020;
|
1.10.533.10;2.10.50.10;
| null | null |
SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Golgi apparatus membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Receptor for TNFSF2/TNF-alpha and homotrimeric TNFSF1/lymphotoxin-alpha. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis (By similarity). {ECO:0000250}.
|
Bos taurus (Bovine)
|
O19132
|
NOS1_RABIT
|
MEEHVFGVQQIQPNVISVRLFKRKVGGLGFLVKERVSKPPVIISDLIRGGAAEQSGLIQAGDIILAVNGRPLVDLSYDSALEVLRGVASETHVVLILRGPEGFTTNLETTFTGDGTPKTIRVTQPLGAPTKAVDLSHQPPSAGKEQPRPVDGAAGPGSWPQPTQGHGQEAGSPSRANGLAPRTSSQDPAKKSGWAGLQGSGDKNELLKEIEPVLTLLAGGSKAVDGGGPAKAETRDTGVQVDRDFDAKSHKPLPLGVENDRVFSDLWGKGSAPVVLNNPYSEKEQPPASGKQSPTKNGSPSKCPRFLKVKNWETDVVLTDTLHLKSTLETGCTEHICMGSIMFPSQHTRRPEDIRTKEQLFPLAKEFIDQYYSSIKRFGSKAHMERLEEVNKEIESTSTYQLKDTELIYGAKHAWRNASRCVGRIQWSKLQVFDARDCTTAHGMFNYICNHIKYATNKGNLRSAITIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTLGDPANVQFTEICIQQGWKPPRSRFDVLPLLLQANGNDPELFQIPPELVLEVPIRHPKFEWFKDLGLKWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGVRDYCDNSRYNILEEVAKKMNLDMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATESFIKHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEMLNYRLTPCFEYQPDPWNTHVWKGTNGTPTKRRAIGFKKLAEAVKFSAKLMGQAMAKRVKATILYATETGKSQAYAKTLCEIFKHAFDAKVMSMEEYDIVHLEHETLVLVVTSTFGNGDPPENGEKFRCALMEMRHPNSLQEERKSYKVRFNSVSSYSDSRKSSGDGPDVRDHFESAGPLANVRFSVFGLGSRAYPHFCAFGHAVDTLLEELGGERILKMREGDELCGQEEAFRTWAKKVFKAACDVFCVGDDVNIEKANNSLISNDRSWKRNKFRLTYVAEAPGLTQGLSSVHKKRVSAARLLSRQNLQSPKSSRSTIFVRLHTNGSQELQYQPGDHLGVFPGNHEDLVNALIERLEDAPPANQMVKVELLEERNTALGVISNWKDEPRLPPCTVFQAFKYYLDITTPPTPLQLQQFASLASNEKEKQRLLVLSKGLQEYEEWKWGKNPTIVEVLEEFPSIQMPATLLLTQLSLLQPRYYSISSSPDMYPDEVHLTVAIVSYHTRDGEGPIHHGVCSSWLNRIPADEVVPCFVRGAPSFRLPRNPQVPCILVGPGTAFAPFRSFWQQRQFDIQHKGMSPCPMVLVFGCRQSKIDHIYREEALQAKNKGVFRELYTAYSREPDKPKKYVQDILQEQLAEQVYRALKEQGGHIYVCGDVTMAADVLKAVQRIMAQQGKLSAEDAGVFISRLRDDNRYHEDIFGVTLRTYEVTNRLRSESIAFIEESKKDTDEVFSS
|
1.14.13.39
|
COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250|UniProtKB:P29475}; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:P29476}; Note=Binds 1 FAD. {ECO:0000250|UniProtKB:P29476}; COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250|UniProtKB:P29476}; Note=Binds 1 FMN. {ECO:0000250|UniProtKB:P29476}; COFACTOR: Name=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin; Xref=ChEBI:CHEBI:59560; Evidence={ECO:0000250|UniProtKB:P29475}; Note=Tetrahydrobiopterin (BH4). May stabilize the dimeric form of the enzyme. {ECO:0000250|UniProtKB:P29475};
|
nitric oxide biosynthetic process [GO:0006809]
|
dendritic spine [GO:0043197]; sarcolemma [GO:0042383]
|
calmodulin binding [GO:0005516]; flavin adenine dinucleotide binding [GO:0050660]; FMN binding [GO:0010181]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; NADP binding [GO:0050661]; nitric-oxide synthase activity [GO:0004517]
|
PF00667;PF00258;PF00175;PF02898;PF00595;
|
2.30.42.10;3.40.50.360;3.90.440.10;3.40.50.80;2.40.30.10;
|
NOS family
|
PTM: Ubiquitinated; mediated by STUB1/CHIP in the presence of Hsp70 and Hsp40 (in vitro). {ECO:0000250|UniProtKB:P29476}.
|
SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000250|UniProtKB:Q9Z0J4}; Peripheral membrane protein {ECO:0000255}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:P29476}. Note=In skeletal muscle, it is localized beneath the sarcolemma of fast-twitch muscle fiber by associating with the dystrophin glycoprotein complex (By similarity). In neurons, enriched in dendritic spines (By similarity). {ECO:0000250|UniProtKB:P29476, ECO:0000250|UniProtKB:Q9Z0J4}.
|
CATALYTIC ACTIVITY: Reaction=H(+) + 2 L-arginine + 3 NADPH + 4 O2 = 4 H2O + 2 L-citrulline + 3 NADP(+) + 2 nitric oxide; Xref=Rhea:RHEA:19897, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16480, ChEBI:CHEBI:32682, ChEBI:CHEBI:57743, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.14.13.39; Evidence={ECO:0000250|UniProtKB:P29476}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19898; Evidence={ECO:0000250|UniProtKB:P29476};
| null | null | null | null |
FUNCTION: Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In the brain and peripheral nervous system, NO displays many properties of a neurotransmitter. Probably has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such SRR (By similarity). {ECO:0000250|UniProtKB:P29476}.
|
Oryctolagus cuniculus (Rabbit)
|
O19179
|
GUC2D_CANLF
|
MSACALLAGGLPDPRLCAPARWARSPPGVPGAPPWPQPRLRLLLLLLLLPPSALSAVFTVGVLGPWACDPIFARARPDLAARLAAARLNRDAALEDGPRFEVTLLPEPCRTPGSLGAVSSALGRVSGLVGPVNPAACRPAELLAQEAGVALVPWSCPGTRAGGTTAPAGTPAADALYALLRAFRWARVALITAPQDLWVEAGRALSAALRARGLPVALVTTMEPSDLSGAREALRRVQDGPRVRAVIMVMHSVLLGGEEQRCLLQAAEELGLADGSLVFLPFDTLHYALSPGPEALAVLANSSQLRRAHDAVLILTRHCPPGGSVMDNLRRAQEHQELPSDLDLQQVSPFFGTIYDAVLLLAGGVARARAAAGGGWVSGATVAHHIPDAQVPGFCGTLGGAQEPPFVLLDTDAAGDRLFATYMLDPTRGSLLSAGTPVHFPRGGGTPGSDPSCWFEPGVICNGGVEPGLVFLGFLLVVGMGLTGAFLAHYLRHRLLHIQMVSGPNKIILTLDDVTFLHPHGGSTRKVVQGSRSSLAARSTSDIRSVPSQPLDNSNIGLFEGDWVWLKKFPGDQHIAIRPATKTAFSKLRELRHENVVLYLGLFLGSGGAGGSAAGEGVLAVVSEHCARGSLHDLLAQRDIKLDWMFKSSLLLDLIKGMRYLHHRGVAHGRLKSRNCVVDGRFVLKVTDHGHARLMEAQRVLLEPPSAEDQLWTAPELLRDPALERRGTLPGDVFSLGIIMQEVVCRSAPYAMLELTPEEVVERVRSPPPLCRPSVSMDQAPVECIQLMKQCWAEHPDLRPSLGHIFDQFKSINKGRKTNIIDSMLRMLEQYSSNLEDLIRERTEELELEKQKTDRLLTQMLPPSVAEALKMGTPVEPEYFEEVTLYFSDIVGFTTISAMSEPIEVVDLLNDLYTLFDAIIGSHDVYKVETIGDAYMVASGLPQRNGQRHAAEIANMALDILSAVGSFRMRHMPEVPVRIRIGLHSGPCVAGVVGLTMPRYCLFGDTVNTASRMESTGLPYRIHVNMSTVRILHALDEGFQTEVRGRTELKGKGAEDTYWLVGRRGFNKPIPKPPDLQPGASNHGISLQEIPLDRRWKLEKARPGQFSGK
|
4.6.1.2
| null |
cGMP biosynthetic process [GO:0006182]; intracellular signal transduction [GO:0035556]; receptor guanylyl cyclase signaling pathway [GO:0007168]; visual perception [GO:0007601]
|
endoplasmic reticulum membrane [GO:0005789]; photoreceptor outer segment [GO:0001750]; plasma membrane [GO:0005886]
|
adenylate cyclase activity [GO:0004016]; ATP binding [GO:0005524]; GTP binding [GO:0005525]; guanylate cyclase activity [GO:0004383]; peptide receptor activity [GO:0001653]; protein homodimerization activity [GO:0042803]; protein kinase activity [GO:0004672]
|
PF01094;PF00211;PF07701;PF07714;
|
3.40.50.2300;6.10.250.780;3.30.70.1230;1.10.510.10;
|
Adenylyl cyclase class-4/guanylyl cyclase family
|
PTM: There are 9 conserved cysteine residues in sensory guanylate cyclases, 6 in the extracellular domain, which may be involved in intra- or interchain disulfide bonds.
|
SUBCELLULAR LOCATION: Photoreceptor outer segment membrane {ECO:0000250|UniProtKB:Q02846}; Single-pass type I membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q02846}; Single-pass type I membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=GTP = 3',5'-cyclic GMP + diphosphate; Xref=Rhea:RHEA:13665, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57746; EC=4.6.1.2; Evidence={ECO:0000250|UniProtKB:P55203};
| null | null | null | null |
FUNCTION: Catalyzes the synthesis of cyclic GMP (cGMP) in rods and cones of photoreceptors. Plays an essential role in phototransduction, by mediating cGMP replenishment. May also participate in the trafficking of membrane-associated proteins to the photoreceptor outer segment membrane. {ECO:0000250|UniProtKB:P52785}.
|
Canis lupus familiaris (Dog) (Canis familiaris)
|
O19183
|
PGH2_HORSE
|
MLARALLLCVALALGHAANPCCSNPCQNRGVCMSVGFDQYQCDCTRTGFYGENCSTPEFLTRIKLFLKPTPNTVHYILTHFKGVWNIVNSFPFLRNAVMKYVLVSRSHLIESPPTYNAQYGYKSWESFSNLSYYTRALPPVADGCPTPMGVKGKKELPDSKEIVEKFLLRRKFIPDPQGTNMMFAFFAQHFTHQFFKTDPKRGPAFTKGLGHGVDLSHIYGETLDRQHKLRLFKDGKMKYQIINGEVYPPTVKDTQVEMIYPPHIPEHLRFAVGQEVFGLVPGLMMYATIWLREHNRVCDVLKQEHPEWDDERLFQTSRLILIGETIKIVIEDYVQHLSGYHFKLKFDPELLFNQQFQYQNRIAAEFNTLYHWHPLLPDTFQIDDQEYNFQQFLYNNSILLEHGLTQFVESFSRQIAGRVAGGRNVPAAAQKIAKASIDQSREMKYQSLNEYRKRFRLTPYKSFEELTGEKEMAAELEALYGDIDAMELYPALLVEKPRPDAIFGETMVELGAPFSLKGLLGNPICSPDYWKPSTFGGEVGFKIINTASIQSLICNNVKGCPFTAFSVQDPQLSKAVTINASASHSGLDDVNPTVLLKERSTEL
|
1.14.99.1
|
COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250|UniProtKB:Q05769}; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit. {ECO:0000250|UniProtKB:Q05769};
|
cyclooxygenase pathway [GO:0019371]; prostaglandin biosynthetic process [GO:0001516]; regulation of blood pressure [GO:0008217]; regulation of neuroinflammatory response [GO:0150077]; response to oxidative stress [GO:0006979]
|
cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; neuron projection [GO:0043005]; nuclear inner membrane [GO:0005637]; nuclear outer membrane [GO:0005640]
|
heme binding [GO:0020037]; metal ion binding [GO:0046872]; oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen [GO:0016702]; peroxidase activity [GO:0004601]; prostaglandin-endoperoxide synthase activity [GO:0004666]
|
PF03098;PF00008;
|
1.10.640.10;2.10.25.10;
|
Prostaglandin G/H synthase family
|
PTM: S-nitrosylation by NOS2 (iNOS) activates enzyme activity. S-nitrosylation may take place on different Cys residues in addition to Cys-526. {ECO:0000250|UniProtKB:P35354}.
|
SUBCELLULAR LOCATION: Microsome membrane {ECO:0000250|UniProtKB:P35354}; Peripheral membrane protein {ECO:0000250|UniProtKB:P35354}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P35354}; Peripheral membrane protein {ECO:0000250|UniProtKB:P35354}. Nucleus inner membrane {ECO:0000250|UniProtKB:P35354}; Peripheral membrane protein {ECO:0000250|UniProtKB:P35354}. Nucleus outer membrane {ECO:0000250|UniProtKB:P35354}; Peripheral membrane protein {ECO:0000250|UniProtKB:P35354}. Note=Detected on the lumenal side of the endoplasmic reticulum and nuclear envelope. {ECO:0000250|UniProtKB:P35354}.
|
CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + AH2 + 2 O2 = A + H2O + prostaglandin H2; Xref=Rhea:RHEA:23728, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:32395, ChEBI:CHEBI:57405; EC=1.14.99.1; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23729; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + 2 O2 = prostaglandin G2; Xref=Rhea:RHEA:42596, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:82629; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42597; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=AH2 + prostaglandin G2 = A + H2O + prostaglandin H2; Xref=Rhea:RHEA:42600, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:57405, ChEBI:CHEBI:82629; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42601; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + 2 O2 = prostaglandin G3; Xref=Rhea:RHEA:50444, ChEBI:CHEBI:15379, ChEBI:CHEBI:58562, ChEBI:CHEBI:133133; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50445; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=AH2 + prostaglandin G3 = A + H2O + prostaglandin H3; Xref=Rhea:RHEA:50448, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:133133, ChEBI:CHEBI:133134; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50449; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(8Z,11Z,14Z)-eicosatrienoate + 2 O2 = prostaglandin G1; Xref=Rhea:RHEA:50424, ChEBI:CHEBI:15379, ChEBI:CHEBI:71589, ChEBI:CHEBI:133084; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50425; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=AH2 + prostaglandin G1 = A + H2O + prostaglandin H1; Xref=Rhea:RHEA:50432, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:90793, ChEBI:CHEBI:133084; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50433; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphoethanolamine + 2 O2 = 2-(prostaglandin G2)-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:54204, ChEBI:CHEBI:15379, ChEBI:CHEBI:76091, ChEBI:CHEBI:138098; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54205; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=2-(prostaglandin G2)-sn-glycero-3-phosphoethanolamine + AH2 = 2-(prostaglandin H2)-sn-glycero-3-phosphoethanolamine + A + H2O; Xref=Rhea:RHEA:54208, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:138098, ChEBI:CHEBI:138099; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54209; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphocholine + 2 O2 = 2-(prostaglandin G2)-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:54212, ChEBI:CHEBI:15379, ChEBI:CHEBI:76079, ChEBI:CHEBI:138100; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54213; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=2-(prostaglandin G2)-sn-glycero-3-phosphocholine + AH2 = 2-(prostaglandin H2)-sn-glycero-3-phosphocholine + A + H2O; Xref=Rhea:RHEA:54216, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:138100, ChEBI:CHEBI:138101; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54217; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + AH2 = (15S)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + A + H2O; Xref=Rhea:RHEA:48856, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:57409, ChEBI:CHEBI:57446; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48857; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphocholine + AH2 + O2 = 2-[(15S)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl]-sn-glycero-3-phosphocholine + A + H2O; Xref=Rhea:RHEA:53684, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:76079, ChEBI:CHEBI:137584; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53685; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphocholine + AH2 + O2 = 2-[(15R)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl]-sn-glycero-3-phosphocholine + A + H2O; Xref=Rhea:RHEA:53680, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:76079, ChEBI:CHEBI:137583; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53681; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphocholine + AH2 + O2 = 2-[(11R)-hydroxy-(5Z,8Z,12E,14Z)-eicosatetraenoyl]-sn-glycero-3-phosphocholine + A + H2O; Xref=Rhea:RHEA:53676, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:76079, ChEBI:CHEBI:137582; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53677; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = 9-hydroxy-(10E,12Z)-octadecadienoate + A + H2O; Xref=Rhea:RHEA:50864, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:30245, ChEBI:CHEBI:133820; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50865; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = 13-hydroxy-(9Z,11E)-octadecadienoate + A + H2O; Xref=Rhea:RHEA:50860, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:30245, ChEBI:CHEBI:133819; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50861; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + AH2 + O2 = (15R)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + A + H2O; Xref=Rhea:RHEA:50856, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:32395, ChEBI:CHEBI:78837; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50857; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + AH2 + O2 = (11R)-hydroxy-(5Z,8Z,12E,14Z)-eicosatetraenoate + A + H2O; Xref=Rhea:RHEA:50852, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:32395, ChEBI:CHEBI:78836; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50853; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + AH2 + O2 = (11R)-hydroxy-(5Z,8Z,12E,14Z,17Z)-eicosapentaenoate + A + H2O; Xref=Rhea:RHEA:50848, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:58562, ChEBI:CHEBI:90820; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50849; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + AH2 + O2 = (18S)-hydroxy-(5Z,8Z,11Z,14Z,16E)-eicosapentaenoate + A + H2O; Xref=Rhea:RHEA:50200, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:58562, ChEBI:CHEBI:132083; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50201; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + AH2 + O2 = (18R)-hydroxy-(5Z,8Z,11Z,14Z,16E)-eicosapentaenoate + A + H2O; Xref=Rhea:RHEA:48836, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:58562, ChEBI:CHEBI:90818; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48837; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + AH2 + O2 = (15R)-hydroxy-(5Z,8Z,11Z,13E,17Z)-eicosapentaenoate + A + H2O; Xref=Rhea:RHEA:48840, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:58562, ChEBI:CHEBI:90819; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48841; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + AH2 + O2 = (15S)-hydroxy-(5Z,8Z,11Z,13E,17Z)-eicosapentaenoate + A + H2O; Xref=Rhea:RHEA:50196, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:58562, ChEBI:CHEBI:132087; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50197; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(7Z,10Z,13Z,16Z,19Z)-docosapentaenoate + AH2 + O2 = 13R-hydroxy-(7Z,10Z,14E,16Z,19Z)-docosapentaenoate + A + H2O; Xref=Rhea:RHEA:48852, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:77224, ChEBI:CHEBI:90824; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48853; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + AH2 + O2 = 13-hydroxy-(4Z,7Z,10Z,14E,16Z,19Z)-docosahexaenoate + A + H2O; Xref=Rhea:RHEA:48820, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:77016, ChEBI:CHEBI:90815; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48821; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(5S)-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + AH2 + O2 = (5S,15R)-dihydroxy-(6E,8Z,11Z,13E)-eicosatetraenoate + A + H2O; Xref=Rhea:RHEA:48812, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:90632, ChEBI:CHEBI:90812; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48813; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + AH2 + O2 = 17R-hydroxy-(4Z,7Z,10Z,13Z,15E,19Z)-docosahexaenoate + A + H2O; Xref=Rhea:RHEA:48816, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:77016, ChEBI:CHEBI:90814; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48817; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(5S)-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + AH2 + O2 = (5S,15S)-dihydroxy-(6E,8Z,11Z,13E)-eicosatetraenoate + A + H2O; Xref=Rhea:RHEA:48808, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:90632, ChEBI:CHEBI:90813; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48809; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(5S)-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + AH2 + O2 = (5S,11R)-dihydroxy-(6E,8Z,12E,14Z)-eicosatetraenoate + A + H2O; Xref=Rhea:RHEA:48804, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:90632, ChEBI:CHEBI:90810; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48805; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + 2 O2 = 2-glyceryl-prostaglandin G2; Xref=Rhea:RHEA:45288, ChEBI:CHEBI:15379, ChEBI:CHEBI:52392, ChEBI:CHEBI:85165; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45289; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=2-glyceryl-prostaglandin G2 + AH2 = 2-glyceryl-prostaglandin H2 + A + H2O; Xref=Rhea:RHEA:45292, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:85165, ChEBI:CHEBI:85166; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45293; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = (15R)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate; Xref=Rhea:RHEA:42284, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:82626; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42285; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = 11R-hydroperoxy-(5Z,8Z,12E,14Z)-eicosatetraenoate; Xref=Rhea:RHEA:42280, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:82628; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42281; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = (9R)-hydroxy-(10E,12Z)-octadecadienoate + A + H2O; Xref=Rhea:RHEA:75447, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:30245, ChEBI:CHEBI:77895; Evidence={ECO:0000250|UniProtKB:P79208}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75448; Evidence={ECO:0000250|UniProtKB:P79208}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = (9S)-hydroxy-(10E,12Z)-octadecadienoate + A + H2O; Xref=Rhea:RHEA:75459, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:30245, ChEBI:CHEBI:77852; Evidence={ECO:0000250|UniProtKB:P79208}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75460; Evidence={ECO:0000250|UniProtKB:P79208}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = (13S)-hydroxy-(9Z,11E)-octadecadienoate + A + H2O; Xref=Rhea:RHEA:75451, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:30245, ChEBI:CHEBI:90850; Evidence={ECO:0000250|UniProtKB:P79208}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75452; Evidence={ECO:0000250|UniProtKB:P79208}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = (13R)-hydroxy-(9Z,11E)-octadecadienoate + A + H2O; Xref=Rhea:RHEA:75455, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:30245, ChEBI:CHEBI:136655; Evidence={ECO:0000250|UniProtKB:P79208}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75456; Evidence={ECO:0000250|UniProtKB:P79208};
| null |
PATHWAY: Lipid metabolism; prostaglandin biosynthesis. {ECO:0000250|UniProtKB:P35354}.
| null | null |
FUNCTION: Dual cyclooxygenase and peroxidase in the biosynthesis pathway of prostanoids, a class of C20 oxylipins mainly derived from arachidonate ((5Z,8Z,11Z,14Z)-eicosatetraenoate, AA, C20:4(n-6)), with a particular role in the inflammatory response. The cyclooxygenase activity oxygenates AA to the hydroperoxy endoperoxide prostaglandin G2 (PGG2), and the peroxidase activity reduces PGG2 to the hydroxy endoperoxide prostaglandin H2 (PGH2), the precursor of all 2-series prostaglandins and thromboxanes. This complex transformation is initiated by abstraction of hydrogen at carbon 13 (with S-stereochemistry), followed by insertion of molecular O2 to form the endoperoxide bridge between carbon 9 and 11 that defines prostaglandins. The insertion of a second molecule of O2 (bis-oxygenase activity) yields a hydroperoxy group in PGG2 that is then reduced to PGH2 by two electrons. Similarly catalyzes successive cyclooxygenation and peroxidation of dihomo-gamma-linoleate (DGLA, C20:3(n-6)) and eicosapentaenoate (EPA, C20:5(n-3)) to corresponding PGH1 and PGH3, the precursors of 1- and 3-series prostaglandins. In an alternative pathway of prostanoid biosynthesis, converts 2-arachidonoyl lysophopholipids to prostanoid lysophopholipids, which are then hydrolyzed by intracellular phospholipases to release free prostanoids. Metabolizes 2-arachidonoyl glycerol yielding the glyceryl ester of PGH2, a process that can contribute to pain response. Generates lipid mediators from n-3 and n-6 polyunsaturated fatty acids (PUFAs) via a lipoxygenase-type mechanism. Oxygenates PUFAs to hydroperoxy compounds and then reduces them to corresponding alcohols. Plays a role in the generation of resolution phase interaction products (resolvins) during both sterile and infectious inflammation. Metabolizes docosahexaenoate (DHA, C22:6(n-3)) to 17R-HDHA, a precursor of the D-series resolvins (RvDs). As a component of the biosynthetic pathway of E-series resolvins (RvEs), converts eicosapentaenoate (EPA, C20:5(n-3)) primarily to 18S-HEPE that is further metabolized by ALOX5 and LTA4H to generate 18S-RvE1 and 18S-RvE2. In vascular endothelial cells, converts docosapentaenoate (DPA, C22:5(n-3)) to 13R-HDPA, a precursor for 13-series resolvins (RvTs) shown to activate macrophage phagocytosis during bacterial infection. In activated leukocytes, contributes to oxygenation of hydroxyeicosatetraenoates (HETE) to diHETES (5,15-diHETE and 5,11-diHETE). Can also use linoleate (LA, (9Z,12Z)-octadecadienoate, C18:2(n-6)) as substrate and produce hydroxyoctadecadienoates (HODEs) in a regio- and stereospecific manner, being (9R)-HODE ((9R)-hydroxy-(10E,12Z)-octadecadienoate) and (13S)-HODE ((13S)-hydroxy-(9Z,11E)-octadecadienoate) its major products (By similarity). During neuroinflammation, plays a role in neuronal secretion of specialized preresolving mediators (SPMs) 15R-lipoxin A4 that regulates phagocytic microglia (By similarity). {ECO:0000250|UniProtKB:P35354, ECO:0000250|UniProtKB:P79208, ECO:0000250|UniProtKB:Q05769}.
|
Equus caballus (Horse)
|
O19477
|
HMR1_RAT
|
MMFLLPFLTVFLAKQSHTRTHSLRYFRLAISDPGPGVPEFISVGYVDSHPITTYDSVTRQKEPRAPWMAENLAPDHWERYTQLLRGWQRTFQTELRHLQRHYNHSGLHTYQRMIGCELLEDGSTTGFLQYAYDGQDFIVFDKDTLSWLAMDNVAHITKRAWEANLHELQYQKNWLEEECIAWLKRFLEYGSDALERTEHPVVRTTRKETFPGITTLFCRAHGFYPPEISMIWKKNGEEIVQEVDYGGVLPSGDGTYQMWVSVDLDPQTKDIYSCHVEHCGLQMVLEAPQESGNTLLVANTISGTIILIIVLAGVGALIWRRRSREPKEVMYQPTQVNEGSSPS
| null | null |
antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent [GO:0002486]; antigen processing and presentation of endogenous peptide antigen via MHC class Ib [GO:0002476]; antigen processing and presentation of exogenous antigen [GO:0019884]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; immune response [GO:0006955]; innate immune response [GO:0045087]; positive regulation of T cell mediated cytotoxicity directed against tumor cell target [GO:0002854]; T cell differentiation in thymus [GO:0033077]
|
early endosome membrane [GO:0031901]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; Golgi membrane [GO:0000139]; late endosome membrane [GO:0031902]; MHC class I protein complex [GO:0042612]; plasma membrane [GO:0005886]
|
beta-2-microglobulin binding [GO:0030881]; T cell receptor binding [GO:0042608]
|
PF07654;PF00129;
|
2.60.40.10;3.30.500.10;
| null |
PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q95460}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q95460}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q95460}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q95460}; Single-pass type I membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q95460}; Single-pass type I membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000250|UniProtKB:Q95460}; Single-pass type I membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000250|UniProtKB:Q95460}; Single-pass type I membrane protein {ECO:0000255}. Note=In the absence of antigen remains within the endoplasmic reticulum where it acts as a metabolite sensor. Antigen binding triggers trafficking of the ternary complex to the plasma membrane. After presentation, most of these complexes are rapidly internalized and degraded via endocytosis. A small subset recycles via endosomes back to the plasma membrane and may thus acquire and present new antigens that do not efficiently reach the endoplasmic reticulum. {ECO:0000250|UniProtKB:Q95460}.
| null | null | null | null | null |
FUNCTION: Antigen-presenting molecule specialized in displaying microbial pyrimidine-based metabolites to alpha-beta T cell receptors (TCR) on innate-type mucosal-associated invariant T (MAIT) cells. In complex with B2M preferentially presents riboflavin-derived metabolites to semi-invariant TCRs on MAIT cells, guiding immune surveillance of the microbial metabolome at mucosal epithelial barriers (By similarity). Signature pyrimidine-based microbial antigens are generated via non-enzymatic condensation of metabolite intermediates of the riboflavin pathway with by-products arising from other metabolic pathways such as glycolysis. Typical potent antigenic metabolites are 5-(2-oxoethylideneamino)-6-D-ribitylaminouracil (5-OE-RU) and 5-(2-oxopropylideneamino)-6-D-ribitylaminouracil (5-OP-RU), products of condensation of 5-amino-6-D-ribityaminouracil (5-A-RU) with glyoxal or methylglyoxal by-products, respectively (By similarity). May present microbial antigens to various MAIT cell subsets, providing for unique recognition of diverse microbes, including pathogens that do not synthesize riboflavin. Upon antigen recognition, elicits rapid innate-type MAIT cell activation to eliminate pathogenic microbes by directly killing infected cells (By similarity). During T cell development, drives thymic selection and post-thymic terminal differentiation of MAIT cells in a process dependent on commensal microflora (By similarity). Acts as an immune sensor of cancer cell metabolome. May present a tumor-specific or -associated metabolite essential for cancer cell survival to a pan-cancer TCR on a non-MAIT CD8-positive T cell clone, triggering T cell-mediated killing of a wide range of cancer cell types (By similarity). {ECO:0000250|UniProtKB:Q8HWB0, ECO:0000250|UniProtKB:Q95460}.
|
Rattus norvegicus (Rat)
|
O20250
|
TKTC_SPIOL
|
MAASSSLSTLSHHQTLLSHPKTHLPTTPASSLLVPTTSSKVNGVLLKSTSSSRRLRVGSASAVVRAAAVEALESTDIDQLVEKSVNTIRFLAIDAVEKANSGHPGLPMGCAPMGHILYDEIMRYNPKNPYWFNRDRFVLSAGHGCMLQYALLHLAGYDSVLEEDLKTFRQWGSRIPGHPENFETPGVEVTTGPLGQGIANAVGLALAEKHLAARFNKPDAEIVDHYTYVILGDGCQMEGIAQEACSLAGHWGLGKLIAFYDDNHISIDGDTAIAFTESVDLRFEALGWHVIWVKNGNTGYDEIRAAIKEAKTVTDKPTLIKVTTTIGFGSPNKSNSYSVHGSALGSKEVEATRQNLGWPYEPFHVPEEVKKHWSRHTPEGASLEAEWNTKFAEYEKKYPEDATEFKSITTGEFPAGWEKALPTYTPETPGDATRNLSQQCLNALAKVIPGLLGGSADLASSNMTLLKMFGDFRRTHRKKETFRFGVREHGMGAICNGICLHSPGFVPYCATFFVFTDYMRGAMRISALSEAGVIYVMTHDSIGLGEDGPTHQPIEALSKFPAMPNILMLRPADGNETAGSYKVAVENRKTPSILALSRKKLPNLPGTSIEGVEKGGYTITDNSSGNKPDVILIGTGSELEIAAKAGDELRKEGKAVRVVSFVSWELFEKQSDEYKESVLPSDVTARVSIEAGSTFGWHKIVGSKGKAIGIDKFGASAPAGKIYQEYGITVEAVVEAAKSVC
|
2.2.1.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250}; Note=Binds 1 Mg(2+) ion per subunit. Can also utilize other divalent metal cations, such as Ca(2+), Mn(2+) and Co(2+). {ECO:0000250}; COFACTOR: Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; Evidence={ECO:0000250}; Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250};
|
pentose-phosphate shunt, oxidative branch [GO:0009051]; reductive pentose-phosphate cycle [GO:0019253]
|
chloroplast thylakoid membrane [GO:0009535]; cytosol [GO:0005829]
|
metal ion binding [GO:0046872]; transketolase activity [GO:0004802]
|
PF02779;PF02780;PF00456;
|
3.40.50.920;3.40.50.970;
|
Transketolase family
| null |
SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:9523694}.
|
CATALYTIC ACTIVITY: Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate = aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate; Xref=Rhea:RHEA:10508, ChEBI:CHEBI:57483, ChEBI:CHEBI:57737, ChEBI:CHEBI:58273, ChEBI:CHEBI:59776; EC=2.2.1.1; Evidence={ECO:0000269|PubMed:8980496};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=67 uM for xylulose 5-phosphate {ECO:0000269|PubMed:9523694}; KM=330 uM for ribose 5-phosphate {ECO:0000269|PubMed:9523694};
|
PATHWAY: Carbohydrate biosynthesis; Calvin cycle.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:9523694};
| null |
FUNCTION: Catalyzes the reversible transfer of a two-carbon ketol group from fructose-6-phosphate or sedoheptulose-7-phosphate to glyceraldehyde-3-phosphate to yield xylulose-5-phosphate and erythrose-4-phosphate or ribose-5-phosphate, respectively. {ECO:0000269|PubMed:8980496, ECO:0000303|PubMed:8980496}.
|
Spinacia oleracea (Spinach)
|
O22040
|
ANP1_ARATH
|
MQDFFGSVRRSLVFRPSSDDDNQENQPPFPGVLADKITSCIRKSKIFIKPSFSPPPPANTVDMAPPISWRKGQLIGRGAFGTVYMGMNLDSGELLAVKQVLIAANFASKEKTQAHIQELEEEVKLLKNLSHPNIVRYLGTVREDDTLNILLEFVPGGSISSLLEKFGPFPESVVRTYTRQLLLGLEYLHNHAIMHRDIKGANILVDNKGCIKLADFGASKQVAELATMTGAKSMKGTPYWMAPEVILQTGHSFSADIWSVGCTVIEMVTGKAPWSQQYKEVAAIFFIGTTKSHPPIPDTLSSDAKDFLLKCLQEVPNLRPTASELLKHPFVMGKHKESASTDLGSVLNNLSTPLPLQINNTKSTPDSTCDDVGDMCNFGSLNYSLVDPVKSIQNKNLWQQNDNGGDEDDMCLIDDENFLTFDGEMSSTLEKDCHLKKSCDDISDMSIALKSKFDESPGNGEKESTMSMECDQPSYSEDDDELTESKIKAFLDEKAADLKKLQTPLYEEFYNSLITFSPSCMESNLSNSKREDTARGFLKLPPKSRSPSRGPLGGSPSRATDATSCSKSPGSGGSRELNINNGGDEASQDGVSARVTDWRGLVVDTKQELSQCVALSEIEKKWKEELDQELERKRQEIMRQAGLGSSPRDRGMSRQREKSRFASPGK
|
2.7.11.25
| null |
protein autophosphorylation [GO:0046777]; response to oxidative stress [GO:0006979]
| null |
ATP binding [GO:0005524]; MAP kinase kinase kinase activity [GO:0004709]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, STE Ser/Thr protein kinase family, MAP kinase kinase kinase subfamily
| null | null |
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.25; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.25;
| null | null | null | null |
FUNCTION: May be involved in an oxidative stress-mediated signaling cascade that phosphorylates downstream MAP kinases MPK3 and MPK6. May suppress auxin signaling that promotes cell cycle. Functionally redundant to ANP2 and ANP3 in the positive regulation of cytokinesis. {ECO:0000269|PubMed:10717008, ECO:0000269|PubMed:12034900}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O22042
|
M3K3_ARATH
|
MQDILGSVRRSLVFRSSLAGDDGTSGGGLSGFVGKINSSIRSSRIGLFSKPPPGLPAPRKEEAPSIRWRKGELIGCGAFGRVYMGMNLDSGELLAIKQVLIAPSSASKEKTQGHIRELEEEVQLLKNLSHPNIVRYLGTVRESDSLNILMEFVPGGSISSLLEKFGSFPEPVIIMYTKQLLLGLEYLHNNGIMHRDIKGANILVDNKGCIRLADFGASKKVVELATVNGAKSMKGTPYWMAPEVILQTGHSFSADIWSVGCTVIEMATGKPPWSEQYQQFAAVLHIGRTKAHPPIPEDLSPEAKDFLMKCLHKEPSLRLSATELLQHPFVTGKRQEPYPAYRNSLTECGNPITTQGMNVRSSINSLIRRSTCSGLKDVCELGSLRSSIIYPQKSNNSGFGWRDGDSDDLCQTDMDDLCNIESVRNNVLSQSTDLNKSFNPMCDSTDNWSCKFDESPKVMKSKSNLLSYQASQLQTGVPCDEETSLTFAGGSSVAEDDYKGTELKIKSFLDEKAQDLKRLQTPLLEEFHNAMNPGIPQGALGDTNIYNLPNLPSISKTPKRLPSRRLSAISDAMPSPLKSSKRTLNTSRVMQSGTEPTQVNESTKKGVNNSRCFSEIRRKWEEELYEELERHRENLRHAGAGGKTPLSGHKG
|
2.7.11.25
| null |
cortical microtubule organization [GO:0043622]; protein autophosphorylation [GO:0046777]
|
apoplast [GO:0048046]; cytoplasm [GO:0005737]; microtubule [GO:0005874]
|
ATP binding [GO:0005524]; MAP kinase kinase kinase activity [GO:0004709]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, STE Ser/Thr protein kinase family, MAP kinase kinase kinase subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.25; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.25;
| null | null | null | null |
FUNCTION: Involved in cortical microtubules organization and stabilization by regulating the phosphorylation state of microtubule-associated proteins such as MAP65-1. {ECO:0000269|PubMed:20215588}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O22043
|
GGPP6_ARATH
|
MRPRYSLILSAMRLIRPSNRRLSSIASSDSEFISYMKNKAKSINKALDNSIPLCNNFVPLWEPVLEVHKAMRYTLLPGGKRVRPMLCLVACELVGGQESTAMPAACAVEMIHAASLILDDLPCMDDDSLRRGKPTNHKVFGEKTSILASNALRSLAVKQTLASTSLGVTSERVLRAVQEMARAVGTEGLVAGQAADLAGERMSFKNEDDELRYLELMHVHKTAVLVEAAAVVGAIMGGGSDEEIERLKSYARCVGLMFQVMDDVLDETKSSEELGKTAGKDLITGKLTYPKVMGVDNAREYAKRLNREAQEHLQGFDSDKVVPLLSLADYIVKRQN
|
2.5.1.-; 2.5.1.1; 2.5.1.10; 2.5.1.29
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P14324}; Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:P14324};
|
carotenoid biosynthetic process [GO:0016117]; farnesyl diphosphate biosynthetic process [GO:0045337]; geranyl diphosphate biosynthetic process [GO:0033384]; geranylgeranyl diphosphate biosynthetic process [GO:0033386]; isoprenoid biosynthetic process [GO:0008299]
|
mitochondrion [GO:0005739]
|
dimethylallyltranstransferase activity [GO:0004161]; farnesyltranstransferase activity [GO:0004311]; geranyltranstransferase activity [GO:0004337]; metal ion binding [GO:0046872]
|
PF00348;
|
1.10.600.10;
|
FPP/GGPP synthase family
| null |
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:10759500, ECO:0000269|PubMed:9349257}.
|
CATALYTIC ACTIVITY: Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769; EC=2.5.1.1; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate + isopentenyl diphosphate = (2E,6E)-farnesyl diphosphate + diphosphate; Xref=Rhea:RHEA:19361, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.10; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate + isopentenyl diphosphate = (2E,6E,10E)-geranylgeranyl diphosphate + diphosphate; Xref=Rhea:RHEA:17653, ChEBI:CHEBI:33019, ChEBI:CHEBI:58756, ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.29; Evidence={ECO:0000269|PubMed:9349257}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17654; Evidence={ECO:0000269|PubMed:9349257};
| null |
PATHWAY: Isoprenoid biosynthesis; farnesyl diphosphate biosynthesis; farnesyl diphosphate from geranyl diphosphate and isopentenyl diphosphate: step 1/1.; PATHWAY: Isoprenoid biosynthesis; geranyl diphosphate biosynthesis; geranyl diphosphate from dimethylallyl diphosphate and isopentenyl diphosphate: step 1/1.; PATHWAY: Isoprenoid biosynthesis; geranylgeranyl diphosphate biosynthesis; geranylgeranyl diphosphate from farnesyl diphosphate and isopentenyl diphosphate: step 1/1.
| null | null |
FUNCTION: Catalyzes the trans-addition of the three molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate. {ECO:0000269|PubMed:9349257}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O22049
|
AOX2_ARATH
|
MSQLITKAALRVLLVCGRGNCNMFVSSVSSTSVMKSPYEITAPMRIHDWCGGFGDFKIGSKHVQGNFNLRWMGMSSASAMEKKDENLTVKKGQNGGGSVAVPSYWGIETAKMKITRKDGSDWPWNCFMPWETYQANLSIDLKKHHVPKNIADKVAYRIVKLLRIPTDIFFQRRYGCRAMMLETVAAVPGMVGGMLLHLKSIRKFEHSGGWIKALLEEAENERMHLMTMMELVKPKWYERLLVMLVQGIFFNSFFVCYVISPRLAHRVVGYLEEEAIHSYTEFLKDIDNGKIENVAAPAIAIDYWRLPKDATLKDVVTVIRADEAHHRDVNHFASDIRNQGKELREAAAPIGYH
|
1.10.3.11
|
COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250|UniProtKB:Q39219}; Note=Binds 2 iron ions per subunit. {ECO:0000250|UniProtKB:Q39219};
|
alternative respiration [GO:0010230]
|
chloroplast [GO:0009507]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; respirasome [GO:0070469]
|
alternative oxidase activity [GO:0009916]; metal ion binding [GO:0046872]; superoxide-generating NADPH oxidase activity [GO:0106292]; ubiquinol:oxygen oxidoreductase activity [GO:0102721]
|
PF01786;
|
1.20.1260.140;
|
Alternative oxidase family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:11434463}; Multi-pass membrane protein {ECO:0000269|PubMed:11434463}. Note=Mitochondrial, possibly in the inner surface of the inner mitochondrial membrane.
|
CATALYTIC ACTIVITY: Reaction=2 a ubiquinol + O2 = 2 a ubiquinone + 2 H2O; Xref=Rhea:RHEA:30255, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976; EC=1.10.3.11;
| null | null | null | null |
FUNCTION: Catalyzes the cyanide-resistant oxidation of ubiquinol and the reduction of molecular oxygen to water, but does not translocate protons and consequently is not linked to oxidative phosphorylation. May increase respiration when the cytochrome respiratory pathway is restricted, or in response to low temperatures (By similarity). {ECO:0000250}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O22056
|
SIGB_ARATH
|
MSSCLLPQFKCPPDSFSIHFRTSFCAPKHNKGSVFFQPQCAVSTSPALLTSMLDVAKLRLPSFDTDSDSLISDRQWTYTRPDGPSTEAKYLEALASETLLTSDEAVVVAAAAEAVALARAAVKVAKDATLFKNSNNTNLLTSSTADKRSKWDQFTEKERAGILGHLAVSDNGIVSDKITASASNKESIGDLESEKQEEVELLEEQPSVSLAVRSTRQTERKARRAKGLEKTASGIPSVKTGSSPKKKRLVAQEVDHNDPLRYLRMTTSSSKLLTVREEHELSAGIQDLLKLERLQTELTERSGRQPTFAQWASAAGVDQKSLRQRIHHGTLCKDKMIKSNIRLVISIAKNYQGAGMNLQDLVQEGCRGLVRGAEKFDATKGFKFSTYAHWWIKQAVRKSLSDQSRMIRLPFHMVEATYRVKEARKQLYSETGKHPKNEEIAEATGLSMKRLMAVLLSPKPPRSLDQKIGMNQNLKPSEVIADPEAVTSEDILIKEFMRQDLDKVLDSLGTREKQVIRWRFGMEDGRMKTLQEIGEMMGVSRERVRQIESSAFRKLKNKKRNNHLQQYLVAQS
| null | null |
cellular response to light stimulus [GO:0071482]; chloroplast organization [GO:0009658]; DNA-templated transcription initiation [GO:0006352]; regulation of RNA biosynthetic process [GO:2001141]; response to red light [GO:0010114]; tRNA metabolic process [GO:0006399]
|
chloroplast [GO:0009507]
|
DNA binding [GO:0003677]; sigma factor activity [GO:0016987]
|
PF04542;PF04539;PF04545;
|
1.10.601.10;1.10.10.10;
|
Sigma-70 factor family
| null |
SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:10555304, ECO:0000269|PubMed:12602869}.
| null | null | null | null | null |
FUNCTION: Required for the transition of plastids into chloroplasts by coordinating nuclear and chloroplastic genomes under light conditions. Sigma factors are initiation factors that promote the attachment of plastid-encoded RNA polymerase (PEP) to specific initiation sites and are then released. Promotes the biosynthesis of plastid-encoded tRNAs (e.g. trnE-UUC and trnV-UAC). {ECO:0000269|PubMed:10734058, ECO:0000269|PubMed:11094163, ECO:0000269|PubMed:11673617, ECO:0000269|PubMed:12602869, ECO:0000269|PubMed:14654684, ECO:0000269|PubMed:14976253}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O22059
|
CPC_ARATH
|
MFRSDKAEKMDKRRRRQSKAKASCSEEVSSIEWEAVKMSEEEEDLISRMYKLVGDRWELIAGRIPGRTPEEIERYWLMKHGVVFANRRRDFFRK
| null | null |
epidermal cell differentiation [GO:0009913]; positive regulation of trichoblast fate specification [GO:0010063]; stomatal complex formation [GO:0010376]
|
nucleus [GO:0005634]
|
DNA-binding transcription factor activity [GO:0003700]; transcription cis-regulatory region binding [GO:0000976]
|
PF00249;
|
1.10.10.60;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16291794}. Note=Moves from developing non-hair cells (atrichoblasts) to developing hair cells (trichoblasts).
| null | null | null | null | null |
FUNCTION: Transcription factor. Determines the fate of epidermal cell differentiation. Represses trichome development by lateral inhibition. Together with GL3 or BHLH2, promotes the formation of hair developing cells (H position) in root epidermis, probably by inhibiting non-hair cell formation. Represses the expression of GL2 and WER in H cells. Positively regulates stomatal formation in the hypocotyl (PubMed:19513241). {ECO:0000269|PubMed:11910008, ECO:0000269|PubMed:12356720, ECO:0000269|PubMed:16291794, ECO:0000269|PubMed:19513241, ECO:0000269|PubMed:9262483}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O22130
|
AHL22_ARATH
|
MDQVSRSLPPPFLSRDLHLHPHHQFQHQQQQQQQNHGHDIDQHRIGGLKRDRDADIDPNEHSSAGKDQSTPGSGGESGGGGGGDNHITRRPRGRPAGSKNKPKPPIIITRDSANALKSHVMEVANGCDVMESVTVFARRRQRGICVLSGNGAVTNVTIRQPASVPGGGSSVVNLHGRFEILSLSGSFLPPPAPPAASGLTIYLAGGQGQVVGGSVVGPLMASGPVVIMAASFGNAAYERLPLEEDDQEEQTAGAVANNIDGNATMGGGTQTQTQTQQQQQQQLMQDPTSFIQGLPPNLMNSVQLPAEAYWGTPRPSF
| null | null |
flower development [GO:0009908]; photomorphogenesis [GO:0009640]; skotomorphogenesis [GO:0009647]; vegetative to reproductive phase transition of meristem [GO:0010228]
|
nucleus [GO:0005634]
|
DNA-binding transcription factor activity [GO:0003700]; histone deacetylase binding [GO:0042826]; minor groove of adenine-thymine-rich DNA binding [GO:0003680]; protein self-association [GO:0043621]
|
PF03479;
| null | null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19517252, ECO:0000269|PubMed:22442143}.
| null | null | null | null | null |
FUNCTION: Transcription factor that specifically binds AT-rich DNA sequences related to the nuclear matrix attachment regions (MARs). Binds an AT-rich DNA sequences in the FLOWERING LOCUS T (FT) promoter (PubMed:22442143). Acts redundantly with AHL18, AHL27 and AHL29 in the regulation of flowering and regulation of the hypocotyl elongation. Plays a role in both photo- and skotomorphogenesis (PubMed:19517252). Acts as a chromatin remodeling factor that modifies the architecture of FLOWERING LOCUS T (FT) chromatin by modulating both H3 acetylation and methylation leading to the regulation of FT expression during flowering induction (PubMed:22442143). {ECO:0000269|PubMed:19517252, ECO:0000269|PubMed:22442143}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
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