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
|
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
O70494
|
SP3_MOUSE
|
MTAPEKPVKQEEMAALDVDGGGGGGGHGEYLQQQQQQQQQHGNGAAAAAAQDTQPSPLALLAATCSKIGPPSPGDDDEEAAVAAAAGVPAAAAGATGDLASAQLGGAPNRWEVLSATPTTIKDEAGNLVQIPGAATSSGQYVLPLQNLQNQQIFSVAPGSDSSNGTVSNVQYQVIPQIQSTDAQQVQIGFTGSSDNGGINQENSQIQIIPGSNQTLLASGTPPANIQNLIPQTGQVQVQGVAIGGSSFPGQTQVVANVPLGLPGNITFVPINSVDLDSLGLSGSSQTMTAGINADGHLINTGQAMDSSDNSERTGERVSPDVNETNADTDLFVPTSSSSQLPVTIDSTGILQQNTNSLTTTSGQVHSSDLQGNYIQSPVSEETQAQNIQVSTAQPVVQHLQLQDSQQPTSQAQIVQGITPQTIHGVQASGQNISQQALQNLQLQLNPGTFLIQAQTVTPSGQITWQTFQVQGVQNLQNLQIQNTAAQQITLTPVQTLTLGQVAAGGALTSTPVSLSTGQLPNLQTVTVNSIDSTGIQLHPGENADSPADIRIKEEEPDPEEWQLSGDSTLNTNDLTHLRVQVVDEEGDQQHQEGKRLRRVACTCPNCKEGGGRGTNLGKKKQHICHIPGCGKVYGKTSHLRAHLRWHSGERPFICNWMFCGKRFTRSDELQRHRRTHTGEKKFVCPECSKRFMRSDHLAKHIKTHQNKKVIHSSSTVLASVEAGRDDALITAGGTTLILANIQQGSVSGIGTVNTSATSNQDILTNTEIPLQLVTVSGNETME
| null | null |
B cell differentiation [GO:0030183]; definitive hemopoiesis [GO:0060216]; embryonic camera-type eye morphogenesis [GO:0048596]; embryonic placenta development [GO:0001892]; embryonic process involved in female pregnancy [GO:0060136]; embryonic skeletal system development [GO:0048706]; enucleate erythrocyte differentiation [GO:0043353]; erythrocyte differentiation [GO:0030218]; granulocyte differentiation [GO:0030851]; in utero embryonic development [GO:0001701]; liver development [GO:0001889]; lung development [GO:0030324]; megakaryocyte differentiation [GO:0030219]; monocyte differentiation [GO:0030224]; myeloid progenitor cell differentiation [GO:0002318]; natural killer cell differentiation [GO:0001779]; negative regulation of DNA-templated transcription [GO:0045892]; ossification [GO:0001503]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of DNA-templated transcription [GO:0006355]; regulation of transcription by RNA polymerase II [GO:0006357]; T cell differentiation [GO:0030217]; trophectodermal cell differentiation [GO:0001829]
|
cytosol [GO:0005829]; nucleus [GO:0005634]; PML body [GO:0016605]; protein-DNA complex [GO:0032993]; transcription repressor complex [GO:0017053]
|
chromatin binding [GO:0003682]; cis-regulatory region sequence-specific DNA binding [GO:0000987]; DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; double-stranded DNA binding [GO:0003690]; 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]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]
|
PF00096;
|
3.30.160.60;
|
Sp1 C2H2-type zinc-finger protein family
|
PTM: Acetylated by histone acetyltransferase p300, deacetylated by HDACs. Acetylation/deacetylation states regulate transcriptional activity. Acetylation appears to activate transcription. Alternate sumoylation and acetylation at Lys-553 also control transcriptional activity (By similarity). {ECO:0000250}.; PTM: Sumoylated on all isoforms. Sumoylated on 2 sites in longer isoforms with Lys-553 being the major site. Sumoylation at this site promotes nuclear localization to the nuclear periphery, nuclear dots and PML nuclear bodies. Sumoylation on Lys-553 represses the transactivation activity, except for the largest isoform which has little effect on transactivation. Alternate sumoylation and acetylation at Lys-553 also control transcriptional activity (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus. Nucleus, PML body {ECO:0000250}. Note=Localizes to the nuclear periphery and in nuclear dots when sumoylated. Some localization in PML nuclear bodies (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Transcriptional factor that can act as an activator or repressor depending on isoform and/or post-translational modifications. Binds to GT and GC boxes promoter elements. Competes with SP1 for the GC-box promoters. Weak activator of transcription but can activate a number of genes involved in different processes such as cell-cycle regulation, hormone-induction and house-keeping (By similarity). {ECO:0000250, ECO:0000269|PubMed:15554904}.
|
Mus musculus (Mouse)
|
O70496
|
CLCN7_MOUSE
|
MANVSKKVSWSGRDRDDEEGAPLLRRTGQPDEETPLLNGAGPGARQSHSALFRIGQMNNVELDDELLDPEVDPPHTFPKEIPHNEKLLSLKYESLDYDNSENQLFLEEERRINHTAFRTVEIKRWVICALIGILTGLVACFIDIVVENLAGLKYRVIKDNIDKFTEKGGLSFSLLLWATLNSAFVLVGSVIVAFIEPVAAGSGIPQIKCFLNGVKIPHVVRLKTLVIKVSGVILSVVGGLAVGKEGPMIHSGSVIAAGISQGRSTSLKRDFKIFEYFRRDTEKRDFVSAGAAAGVSAAFGAPVGGVLFSLEEGASFWNQFLTWRIFFASMISTFTLNFVLSIYHGNMWDLSSPGLINFGRFDSEKMAYTIHEIPVFIAMGVVGGILGAVFNALNYWLTMFRIRYIHRPCLQVIEAMLVAAVTATVAFVLIYSSRDCQPLQGSSMSYPLQLFCADGEYNSMAAAFFNTPEKSVVSLFHDPPGSYNPMTLGLFTLVYFFLACWTYGLTVSAGVFIPSLLIGAAWGRLFGISLSYLTGAAIWADPGKYALMGAAAQLGGIVRMTLSLTVIMMEATSNVTYGFPIMLVLMTAKIVGDVFIEGLYDMHIQLQSVPFLHWEAPVTSHSLTAREVMSTPVTCLRRREKVGIIVDVLSDTASNHNGFPVVEDVGDTQPARLQGLILRSQLIVLLKHKVFVERSNMGLVQRRLRLKDFRDAYPRFPPIQSIHVSQDERECTMDLSEFMNPSPYTVPQEASLPRVFKLFRALGLRHLVVVDNHNQVVGLVTRKDLARYRLGKGGLEELSLAQT
| null | null |
response to pH [GO:0009268]
|
intracellular membrane-bounded organelle [GO:0043231]; lysosomal membrane [GO:0005765]
|
antiporter activity [GO:0015297]; ATP binding [GO:0005524]; chloride transmembrane transporter activity [GO:0015108]; voltage-gated chloride channel activity [GO:0005247]
|
PF00571;PF00654;
|
3.10.580.10;1.10.3080.10;
|
Chloride channel (TC 2.A.49) family, ClC-7/CLCN7 subfamily
| null |
SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:16525474, ECO:0000269|PubMed:31155284}; Multi-pass membrane protein {ECO:0000269|PubMed:16525474}.
|
CATALYTIC ACTIVITY: Reaction=2 chloride(in) + H(+)(out) = 2 chloride(out) + H(+)(in); Xref=Rhea:RHEA:29567, ChEBI:CHEBI:15378, ChEBI:CHEBI:17996; Evidence={ECO:0000250|UniProtKB:P51798};
| null | null | null | null |
FUNCTION: Slowly voltage-gated channel mediating the exchange of chloride ions against protons (PubMed:16525474, PubMed:19661288). Functions as antiporter and contributes to the acidification of the lysosome lumen and may be involved in maintaining lysosomal pH (PubMed:16525474, PubMed:19661288). The CLC channel family contains both chloride channels and proton-coupled anion transporters that exchange chloride or another anion for protons (By similarity). The presence of conserved gating glutamate residues is typical for family members that function as antiporters (By similarity). {ECO:0000250|UniProtKB:P35523, ECO:0000269|PubMed:16525474, ECO:0000269|PubMed:19661288}.
|
Mus musculus (Mouse)
|
O70497
|
FCN2_MOUSE
|
MALGSAALFVLTLTVHAAGTCPELKVLDLEGYKQLTILQGCPGLPGAAGPKGEAGAKGDRGESGLPGIPGKEGPTGPKGNQGEKGIRGEKGDSGPSQSCATGPRTCKELLTQGHFLTGWYTIYLPDCRPLTVLCDMDTDGGGWTVFQRRLDGSVDFFRDWTSYKRGFGSQLGEFWLGNDNIHALTTQGTSELRVDLSDFEGKHDFAKYSSFQIQGEAEKYKLILGNFLGGGAGDSLTPHNNRLFSTKDQDNDGSTSSCAMGYHGAWWYSQCHTSNLNGLYLRGPHKSYANGVNWKSWRGYNYSCKVSEMKVRLI
| null | null |
cell surface pattern recognition receptor signaling pathway [GO:0002752]; complement activation, lectin pathway [GO:0001867]; G protein-coupled receptor signaling pathway [GO:0007186]; negative regulation of viral entry into host cell [GO:0046597]; positive regulation of interleukin-8 production [GO:0032757]; positive regulation of opsonization [GO:1903028]; protein localization to cell surface [GO:0034394]; proteolysis [GO:0006508]; recognition of apoptotic cell [GO:0043654]
|
collagen trimer [GO:0005581]; collagen-containing extracellular matrix [GO:0062023]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]; serine-type endopeptidase complex [GO:1905370]
|
antigen binding [GO:0003823]; carbohydrate binding [GO:0030246]; carbohydrate derivative binding [GO:0097367]; G protein-coupled receptor binding [GO:0001664]; metal ion binding [GO:0046872]; pattern recognition receptor activity [GO:0038187]; sialic acid binding [GO:0033691]; signaling receptor binding [GO:0005102]
|
PF01391;PF00147;
|
3.90.215.10;
|
Ficolin lectin family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: May function in innate immunity through activation of the lectin complement pathway. Calcium-dependent and GlcNAc-binding lectin (By similarity). {ECO:0000250|UniProtKB:Q15485}.
|
Mus musculus (Mouse)
|
O70503
|
DHB12_MOUSE
|
MECAPPAAGFLYWVGASTIAYLALRASYSLFRAFQVWCVGNEALVGPRLGEWAVVTGGTDGIGKAYAEELAKRGMKIVLISRSQDKLNQVSNNIKEKFNVETRTIAVDFSLDDIYDKIKTGLSGLEIGVLVNNVGMSYEYPEYFLEIPDLDNTIKKLININVLSVCKVTRLVLPGMVERSKGVILNISSASGMLPVPLLTIYSATKAFVDFFSQCLHEEYKSKGIFVQSVMPYLVATKLAKIQKPTLDKPSAETFVKSAIKTVGLQTRTTGYVIHSLMGSINSIMPRWMYFKIIMGFSKSLRNRYLKKRKKN
|
1.1.1.330; 1.1.1.62
| null |
estrogen biosynthetic process [GO:0006703]; extracellular matrix organization [GO:0030198]; fatty acid elongation, saturated fatty acid [GO:0019367]; positive regulation of cell-substrate adhesion [GO:0010811]
|
endoplasmic reticulum [GO:0005783]; extracellular matrix [GO:0031012]; fatty acid elongase complex [GO:0009923]
|
collagen binding [GO:0005518]; estradiol 17-beta-dehydrogenase [NAD(P)] activity [GO:0004303]; fibronectin binding [GO:0001968]; heparin binding [GO:0008201]; oxidoreductase activity [GO:0016491]; very-long-chain 3-oxoacyl-CoA reductase activity [GO:0141040]
|
PF00106;
|
3.40.50.720;
|
Short-chain dehydrogenases/reductases (SDR) family, 17-beta-HSD 3 subfamily
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q53GQ0}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q53GQ0}.
|
CATALYTIC ACTIVITY: Reaction=a very-long-chain (3R)-3-hydroxyacyl-CoA + NADP(+) = a very-long-chain 3-oxoacyl-CoA + H(+) + NADPH; Xref=Rhea:RHEA:48680, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:85440, ChEBI:CHEBI:90725; EC=1.1.1.330; Evidence={ECO:0000250|UniProtKB:Q53GQ0}; 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:0000250|UniProtKB:Q53GQ0}; CATALYTIC ACTIVITY: Reaction=17beta-estradiol + NADP(+) = estrone + H(+) + NADPH; Xref=Rhea:RHEA:24616, ChEBI:CHEBI:15378, ChEBI:CHEBI:16469, ChEBI:CHEBI:17263, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.62; Evidence={ECO:0000250|UniProtKB:Q53GQ0}; CATALYTIC ACTIVITY: Reaction=3-oxooctadecanoyl-CoA + H(+) + NADPH = (3R)-hydroxyoctadecanoyl-CoA + NADP(+); Xref=Rhea:RHEA:39151, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:71407, ChEBI:CHEBI:76374; Evidence={ECO:0000269|PubMed:12482854}; CATALYTIC ACTIVITY: Reaction=(7Z,10Z,13Z,16Z)-3-oxodocosatetraenoyl-CoA + H(+) + NADPH = (3R)-hydroxy-(7Z,10Z,13Z,16Z)-docosatetraenoyl-CoA + NADP(+); Xref=Rhea:RHEA:39323, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:73852, ChEBI:CHEBI:76415; Evidence={ECO:0000250|UniProtKB:Q53GQ0}; CATALYTIC ACTIVITY: Reaction=(7Z,10Z,13Z,16Z,19Z)-3-oxodocosapentaenoyl-CoA + H(+) + NADPH = (3R)-hydroxy-(7Z,10Z,13Z,16Z,19Z)-docosapentaenoyl-CoA + NADP(+); Xref=Rhea:RHEA:39459, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:73863, ChEBI:CHEBI:76460; Evidence={ECO:0000250|UniProtKB:Q53GQ0}; CATALYTIC ACTIVITY: Reaction=(8Z,11Z,14Z)-3-oxoeicosatrienoyl-CoA + H(+) + NADPH = (3R)-hydroxy-(8Z,11Z,14Z)-eicosatrienoyl-CoA + NADP(+); Xref=Rhea:RHEA:39311, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:71481, ChEBI:CHEBI:76411; Evidence={ECO:0000250|UniProtKB:Q53GQ0};
| null |
PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000250|UniProtKB:Q53GQ0}.; PATHWAY: Steroid biosynthesis; estrogen biosynthesis. {ECO:0000250|UniProtKB:Q53GQ0}.
| null | null |
FUNCTION: Catalyzes the second of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme has a 3-ketoacyl-CoA reductase activity, reducing 3-ketoacyl-CoA to 3-hydroxyacyl-CoA, within each cycle of fatty acid elongation. Thereby, it may participate in the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators. May also catalyze the transformation of estrone (E1) into estradiol (E2) and play a role in estrogen formation. {ECO:0000250|UniProtKB:Q53GQ0}.
|
Mus musculus (Mouse)
|
O70507
|
HCN4_MOUSE
|
MDKLPPSMRKRLYSLPQQVGAKAWIMDEEEDGEEEGAGGRQDPSRRSIRLRPLPSPSPSVAAGCSESRGAALGATESEGPGRSAGKSSTNGDCRRFRGSLASLGSRGGGSGGAGGGSSLGHLHDSAEERRLIAAEGDASPGEDRTPPGLATEPERPATAAQPAASPPPQQPPQPASASCEQPSADTAIKVEGGAAAIDHILPEAEVRLGQSGFMQRQFGAMLQPGVNKFSLRMFGSQKAVEREQERVKSAGFWIIHPYSDFRFYWDLTMLLLMVGNLIIIPVGITFFKDENTTPWIVFNVVSDTFFLIDLVLNFRTGIVVEDNTEIILDPQRIKMKYLKSWFVVDFISSIPVEYIFLIVETRIDSEVYKTARAVRIVRFTKILSLLRLLRLSRLIRYIHQWEEIFHMTYDLASAVVRIVNLIGMMLLLCHWDGCLQFLVPMLQDFPHDCWVSINGMVNNSWGKQYSYALFKAMSHMLCIGYGRQAPVGMSDVWLTMLSMIVGATCYAMFIGHATALIQSLDSSRRQYQEKYKQVEQYMSFHKLPPDTRQRIHDYYEHRYQGKMFDEESILGELSEPLREEIINFNCRKLVASMPLFANADPNFVTSMLTKLRFEVFQPGDYIIREGTIGKKMYFIQHGVVSVLTKGNKETRLADGSYFGEICLLTRGRRTASVRADTYCRLYSLSVDNFNEVLEEYPMMRKKNSILLHKVQHDLNSGVFNYQENEIIQQIVRHDREMAHCAHRVQAAASATPTPTPVIWTPLIQAPLQAAAATTSVAIALTHHPRLPAAIFRPPPGPGLGNLGAGQTPRHPRRLQSLIPSALGSASPASSPSQVDTPSSSSFHIQQLAGFSAPPGLSPLLPSSSSSPPPGACGSPPAPTPSTSTAAAASTTGFGHFHKALGGSLSSSDSPLLTPLQPGARSPQAAQPPPPLPGARGGLGLLEHFLPPPPSSRSPSSSPGQLGQPPGELSLGLAAGPSSTPETPPRPERPSFMAGASGGASPVAFTPRGGLSPPGHSPGPPRTFPSAPPRASGSHGSLLLPPASSPPPPQVPQRRGTPPLTPGRLTQDLKLISASQPALPQDGAQTLRRASPHSSGESVAAFSLYPRAGGGSGSSGGLGPPGRPYGAIPGQHVTLPRKTSSGSLPPPLSLFGARAASSGGPPLTTAAPQREPGARSEPVRSKLPSNL
| null | null |
cellular response to cAMP [GO:0071320]; in utero embryonic development [GO:0001701]; monoatomic cation transport [GO:0006812]; potassium ion transmembrane transport [GO:0071805]; regulation of heart contraction [GO:0008016]; regulation of heart rate [GO:0002027]; regulation of membrane depolarization [GO:0003254]; sodium ion transmembrane transport [GO:0035725]
|
axon [GO:0030424]; basolateral plasma membrane [GO:0016323]; dendrite [GO:0030425]; HCN channel complex [GO:0098855]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; terminal bouton [GO:0043195]
|
cAMP binding [GO:0030552]; intracellularly cAMP-activated cation channel activity [GO:0005222]; sodium channel activity [GO:0005272]; voltage-gated potassium channel activity [GO:0005249]
|
PF00027;PF00520;PF08412;
|
1.10.287.70;1.10.287.630;2.60.120.10;
|
Potassium channel HCN family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11675786}; Multi-pass membrane protein {ECO:0000269|PubMed:11675786}.
| null | null | null | null | null |
FUNCTION: Hyperpolarization-activated ion channel with very slow activation and inactivation exhibiting weak selectivity for potassium over sodium ions. Contributes to the native pacemaker currents in heart (If) that regulate the rhythm of heart beat. May contribute to the native pacemaker currents in neurons (Ih) (By similarity). May mediate responses to sour stimuli. {ECO:0000250, ECO:0000269|PubMed:11675786}.
|
Mus musculus (Mouse)
|
O70511
|
ANK3_RAT
|
MAHAASQLKKNRDLEINAEEETEKKKKHRKRSRDRKKKSDANASYLRAARAGHLEKALDYIKNGVDVNICNQNGLNALHLASKEGHVEVVSELLQREANVDAATKKGNTALHIASLAGQAEVVKVLVTNGANVNAQSQNGFTPLYMAAQENHLEVVRFLLDNGASQSLATEDGFTPLAVALQQGHDQVVSLLLENDTKGKVRLPALHIAARKDDTKAAALLLQNDTNADIESKMVVNRATESGFTPLHIAAHYGNINVATLLLNRAAAVDFTARNDITPLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQVVEMLLDRAAPILSKTKNGLSPLHMATQGDHLNCVQLLLQHNVPVDDVTNDYLTALHVAAHCGHYKVAKVLLDKKANPNAKALNGFTPLHIACKKNRIRVMELLLKHGASIQAVTESGLTPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETALHMAARSGQAEVVRYLVQDGAQVEAKAKDDQTPLHISARLGKADIVQQLLQQGASPNAATTSGYTPLHLSAREGHEDVAAFLLDHGASLSITTKKGFTPLHVAAKYGKLEVASLLLQKSASPDAAGKSGLTPLHVAAHYDNQKVALLLLDQGASPHAAAKNGYTPLHIAAKKNQMDIATSLLEYGADANAVTRQGIASVHLAAQEGHVDMVSLLLSRNANVNLSNKSGLTPLHLAAQEDRVNVAEVLVNQGAHVDAQTKMGYTPLHVGCHYGNIKIVNFLLQHSAKVNAKTKNGYTPLHQAAQQGHTHIINVLLQNNASPNELTVNGNTALAIARRLGYISVVDTLKVVTEEIMTTTTITEKHKMNVPETMNEVLDMSDDEVGKASAPEKLSDGEYISDGEEGEDAITGDTDKYLGPQDLKELGDDSLPAEGYVGFSLGARSASLRSFSSDRSYTLNRSSYARDSMMIEELLVPSKEQHLPFTREFDSDSLRHYSWAADTLDNVNLVSSPVHSGFLVSFMVDARGGSMRGSRHHGMRIIIPPRKCTAPTRITCRLVKRHKLANPPPMVEGEGLASRLVEMGPAGAQFLGPVIVEIPHFGSMRGKERELIVLRSENGETWKEHQFDSKNEDLSELLNGMDEELDSPEELGTKRICRIITKDFPQYFAVVSRIKQESNQIGPEGGILSSTTVPLVQASFPEGALTKRIRVGLQAQPVPEETVKKILGNKATFSPIVTVEPRRRKFHKPITMTIPVPPPSGEGVSNGYKGDTTPSLRLLCSITGGTSPAQWEDITGTTPLTFIKDCVSFTTNVSARFWLADCHQVLETVGLASQLYRELICVPYMAKFVVFAKTNDPVESSLRCFCMTDDRVDKTLEQQENFEEVARSKDIEVLEGKPIYVDCYGNLAPLTKGGQQLVFNFYSFKENRLPFSIKVRDTSQEPCGRLSFLKEPKTTKGLPQTAVCNLNITLPAHKKAEKADRRQSFTSLALRKRYSYLTEPSMKTVERSSGTARSLPTTYSHKPFFSTRPYQSWTTTPITVPGPAKSGSLSSSPSNTPSASPLKSIWSVSTPSPIKSTLGASTTSSVKSISDVASPIRSFRTISSPIRTVASPSPYNTQVASGTLGRVPTITEATPIKGVAPNSTLSSRTSPVTTAGSLLEKSSITMTPPASPKANITMYSSSLPFKSIITSAAPLISSPLKSVVSPTKSAADVISTAKAAMASTLSSPLKQMSGHAEVALVNGSVSPLKYPSSSALINGCKATATLQDKISTATNAVSSVVSAAPDTVEKALSTTTAMPFSPLRSYVSAAAPSAFQSLRAPSASALYNSLGPSVGVTTSSVTSSIITVPVYSVGNVLAEPALKKLPDSNSLTKSAAALLSPIKTLTTETRPQPHFNRTSSPVKSSLFLASSALKPSVPSSLSSSQEILKDVAEMKEDLMRMTAILQTDVPEEKPFQTDLPREGRIDDEEPFKIVEKVKEDLVKVSEILKKDVCVESKGPPKSPKSDKGHSPEDDWTEFSSEEIREARQAAASHAPSLPERVHGKANLTRVIDYLTNDIGSSSLTNLKYKFEEAKKEGEERQKRILKPAMALQEHKLKMPPASMRPSTSEKELCKMADSFFGTDAILESPDDFSQHDQDKSPLSDSGFETRSEKTPSAPQSAESTGPKPLFHEVPIPPVITETRTEVVHVIRSYEPSTGEIPQSQPEDPVSPKPPPTFMELEPKPTALSIKEKVKAFQMKASSEEEDHSRVLSKGMRVKEETHITTTTRMVYHSPPGSECASERIEETMSVHDIMKAFQSGRDPSKELAGLFEHKSAMSPDVAKSAAETSAQHAEKDNQMKPKLERIIEVHIEKGPQSPCERTDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLISQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIVTLLEGPIFDYGNISGTRSFADENNVFHDPVDGWQNETPSGSLESPAQARRITGGLLDRLDDSSDQVRDPITSYLTGEAGKFEANGNHAEVIPEAKAKAYFPESQNDIGKQSIKENLKPKTHGCGRAEEPVSPLTAYQKSLEETSKLVIEDAPKPCVPVGMKKMTRTPADGKARLNLQEEEGSARSEPKQGEGYKVKTKKEIRNVEKKAH
| null | null |
anterograde axonal transport [GO:0008089]; axon development [GO:0061564]; axon guidance [GO:0007411]; axonogenesis [GO:0007409]; cellular response to magnesium ion [GO:0071286]; clustering of voltage-gated sodium channels [GO:0045162]; establishment of protein localization [GO:0045184]; establishment or maintenance of microtubule cytoskeleton polarity [GO:0030951]; Golgi to plasma membrane protein transport [GO:0043001]; magnesium ion homeostasis [GO:0010960]; maintenance of protein location in cell [GO:0032507]; maintenance of protein location in plasma membrane [GO:0072660]; membrane assembly [GO:0071709]; mitotic cytokinesis [GO:0000281]; negative regulation of delayed rectifier potassium channel activity [GO:1902260]; negative regulation of endocytosis [GO:0045806]; neuromuscular junction development [GO:0007528]; neuronal action potential [GO:0019228]; plasma membrane organization [GO:0007009]; positive regulation of cation channel activity [GO:2001259]; positive regulation of cell communication by electrical coupling [GO:0010650]; positive regulation of gene expression [GO:0010628]; positive regulation of homotypic cell-cell adhesion [GO:0034112]; positive regulation of membrane depolarization during cardiac muscle cell action potential [GO:1900827]; positive regulation of membrane potential [GO:0045838]; positive regulation of non-canonical NF-kappaB signal transduction [GO:1901224]; positive regulation of protein targeting to membrane [GO:0090314]; positive regulation of sodium ion import across plasma membrane [GO:1903784]; positive regulation of sodium ion transmembrane transporter activity [GO:2000651]; positive regulation of sodium ion transport [GO:0010765]; protein localization to axon [GO:0099612]; protein localization to plasma membrane [GO:0072659]; regulation of potassium ion transport [GO:0043266]; regulation of protein targeting [GO:1903533]; regulation of transcription by RNA polymerase II [GO:0006357]; response to immobilization stress [GO:0035902]; signal transduction [GO:0007165]; synapse organization [GO:0050808]
|
axon [GO:0030424]; axon cytoplasm [GO:1904115]; axon initial segment [GO:0043194]; basal plasma membrane [GO:0009925]; basolateral plasma membrane [GO:0016323]; cell surface [GO:0009986]; costamere [GO:0043034]; cytoskeleton [GO:0005856]; dendrite [GO:0030425]; intercalated disc [GO:0014704]; lateral plasma membrane [GO:0016328]; lysosome [GO:0005764]; membrane [GO:0016020]; neuromuscular junction [GO:0031594]; neuron projection [GO:0043005]; node of Ranvier [GO:0033268]; nucleus [GO:0005634]; paranode region of axon [GO:0033270]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; sarcolemma [GO:0042383]; sarcoplasmic reticulum [GO:0016529]; spectrin-associated cytoskeleton [GO:0014731]; synapse [GO:0045202]; T-tubule [GO:0030315]; Z disc [GO:0030018]
|
cadherin binding [GO:0045296]; cytoskeletal protein binding [GO:0008092]; phosphorylation-dependent protein binding [GO:0140031]; protein-macromolecule adaptor activity [GO:0030674]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; spectrin binding [GO:0030507]; structural constituent of cytoskeleton [GO:0005200]; transmembrane transporter binding [GO:0044325]
|
PF00023;PF12796;PF13637;PF00531;PF17809;PF00791;
|
2.60.220.30;2.60.40.2660;1.25.40.20;1.10.533.10;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q12955}. Cell projection, axon {ECO:0000269|PubMed:9744885}. Cell membrane {ECO:0000269|PubMed:21223964}. Cell membrane, sarcolemma {ECO:0000269|PubMed:15953600, ECO:0000269|PubMed:21223964}. Postsynaptic cell membrane {ECO:0000269|PubMed:11796721}. Lysosome {ECO:0000250|UniProtKB:G5E8K5}. Cell membrane, sarcolemma, T-tubule {ECO:0000269|PubMed:15579534}. Note=When transfected in root dorsal ganglia, predominantly located in the axolemma of the axon proximal segments (PubMed:9744885). Also associated with the plasma membrane in neuron cell bodies, although at a lower level than in the axon proximal segment (PubMed:9744885). Isoform 1 is restricted to the axolemma of the axon proximal segment. Isoforms containing the muscle-specific 76 amino-acid insertion localize to the sarcolemma and on the postsynaptic membrane of neuromuscular junctions (PubMed:11796721).
| null | null | null | null | null |
FUNCTION: Membrane-cytoskeleton linker. May participate in the maintenance/targeting of ion channels and cell adhesion molecules at the nodes of Ranvier and axonal initial segments (By similarity). In skeletal muscle, required for costamere localization of DMD and betaDAG1 (By similarity). Regulates KCNA1 channel activity in function of dietary Mg(2+) levels, and thereby contributes to the regulation of renal Mg(2+) reabsorption (By similarity). Required for intracellular adhesion and junctional conductance in myocytes, potentially via stabilization of GJA1/CX43 protein abundance and promotion of PKP2, GJA1/CX43, and SCN5A/Nav1.5 localization to cell-cell junctions (PubMed:21617128). {ECO:0000250|UniProtKB:G5E8K5, ECO:0000250|UniProtKB:Q12955, ECO:0000269|PubMed:21617128}.
|
Rattus norvegicus (Rat)
|
O70514
|
FGFP1_MOUSE
|
MRLHSLILLSFLLLATQAFSEKVRKRAKNAPHSTAEEGVEGSAPSLGKAQNKQRSRTSKSLTHGKFVTKDQATCRWAVTEEEQGISLKVQCTQADQEFSCVFAGDPTDCLKHDKDQIYWKQVARTLRKQKNICRNAKSVLKTRVCRKRFPESNLKLVNPNARGNTKPRKEKAEVSAREHNKVQEAVSTEPNRVKEDITLNPAATQTMAIRDPECLEDPDVLNQRKTALEFCGESWSSICTFFLNMLQATSC
| null | null |
cell-cell signaling [GO:0007267]; fibroblast growth factor receptor signaling pathway [GO:0008543]; myoblast proliferation [GO:0051450]; positive regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis [GO:1903589]; positive regulation of cell migration involved in sprouting angiogenesis [GO:0090050]; positive regulation of fibroblast growth factor receptor signaling pathway [GO:0045743]; positive regulation of myoblast proliferation [GO:2000288]
|
cell surface [GO:0009986]; extracellular region [GO:0005576]; plasma membrane [GO:0005886]
|
fibroblast growth factor binding [GO:0017134]; growth factor binding [GO:0019838]
|
PF06473;
| null |
Fibroblast growth factor-binding protein family
| null |
SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250|UniProtKB:Q14512}. Cell membrane {ECO:0000250|UniProtKB:Q14512}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q14512}. Note=Extracellular and plasma membrane-associated. {ECO:0000250|UniProtKB:Q14512}.
| null | null | null | null | null |
FUNCTION: Acts as a carrier protein that releases fibroblast-binding factors (FGFs) from the extracellular matrix (EM) storage and thus enhances the mitogenic activity of FGFs. Enhances FGF2 signaling during tissue repair, angiogenesis and in tumor growth (By similarity). {ECO:0000250}.
|
Mus musculus (Mouse)
|
O70521
|
RGS19_RAT
|
MPTPHEAEKQHTGPEEADRPPSMSSHDAAPSGPPSRNPCCLCWCCCCSCSWNQERQRAWQVSRESKLQPLPSCEVCTPPSPEEVQSWAQSFDKLMHSPTGRSVFRAFLRTEYSEENMLFWLACEELKTEADRHVVDEKARLIYEDYVSILSPKEVSLDSRVREGINRKMQEPSPHTFDDAQLQIYTLMHRDSYPRFLTSPTYRSLLLQGAPQSSEA
| null | null |
negative regulation of signal transduction [GO:0009968]; regulation of G protein-coupled receptor signaling pathway [GO:0008277]; response to ethanol [GO:0045471]
|
brush border [GO:0005903]; clathrin-coated vesicle [GO:0030136]; Golgi membrane [GO:0000139]
|
G-protein alpha-subunit binding [GO:0001965]; GTPase activator activity [GO:0005096]
|
PF00615;
|
1.10.196.10;1.10.167.10;
| null |
PTM: Fatty acylated. Heavily palmitoylated in the cysteine string motif (By similarity). {ECO:0000250}.; PTM: Phosphorylated, mainly on serine residues. {ECO:0000269|PubMed:10760275}.
|
SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Binds to G-alpha subfamily 1 members, predominantly to G(i)-alpha-3. Activity on G(z)-alpha is inhibited by phosphorylation and palmitoylation of the G-protein (By similarity). {ECO:0000250}.
|
Rattus norvegicus (Rat)
|
O70523
|
FXR1_CRIGR
|
MADVTVEVRGSNGAFYKGFIKDVHEDSLTVVFENNWQPERQVPFNEVRLPPPPDIKKEISEGDEVEVYSRANDQEPCGWWLAKVRMMKGEFYVIEYAACDATYNEIVTFERLRPVNQNKTVKKNTFFKCTVDVPEDLREACANENAHKDFKKAVGACRIFYHPETTQLMILSASEATVKRVNILSDMHLRSIRTKLMLMSRNEEATKHLECTKQLAAAFHEEFVVREDLMGLAIGTHGSNIQQARKVPGVTAIELDEDTGTFRIYGESAEAVKKARGFMEFVEDFIQVPRNLVGKVIGKNGKVIQEIVDKSGVVRVRIEGDNENKLPREDGMVPFVFVGTKESIGNVQVLLEYHIAYLKEVEQLRMERLQIDEQLRQIGSRSYSGRGRGRRGPNYTSGYGTNSELSNPSETESERKDELSDWSLAGEDDRETRHQRDSRRRPGGRGRSVSGGRGRGGPRGGKSSISSVLKDPDSNPYSLLDNTESDQTADTDASESHHSTNRRRRSRRRRTDEDAVLMDGMTESDTASVNENGLVTVADYISRAESQSRQRNLPRETLAKNKKEMAKDVIEEHGPSEKAINGPTSASGDEIPNVPRTPGEEKTKNLKEESTQEAAVLNGVS
| null | null |
dentate gyrus development [GO:0021542]; mRNA destabilization [GO:0061157]; muscle organ development [GO:0007517]; negative regulation of inflammatory response [GO:0050728]; negative regulation of long-term synaptic potentiation [GO:1900272]; negative regulation of translation [GO:0017148]; negative regulation of tumor necrosis factor production [GO:0032720]; non-membrane-bounded organelle assembly [GO:0140694]; nuclear pore complex assembly [GO:0051292]; nuclear pore localization [GO:0051664]; positive regulation of miRNA-mediated gene silencing [GO:2000637]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of translation [GO:0045727]; post-transcriptional regulation of gene expression [GO:0010608]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; regulation of circadian sleep/wake cycle, sleep [GO:0045187]; regulation of filopodium assembly [GO:0051489]; regulation of neurogenesis [GO:0050767]; regulation of synaptic transmission, glutamatergic [GO:0051966]; spermatid development [GO:0007286]
|
cytoplasmic ribonucleoprotein granule [GO:0036464]; cytoplasmic stress granule [GO:0010494]; dendritic filopodium [GO:1902737]; dendritic spine neck [GO:0044326]; growth cone [GO:0030426]; intracellular non-membrane-bounded organelle [GO:0043232]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; nuclear envelope [GO:0005635]; postsynaptic density [GO:0014069]; presynapse [GO:0098793]
|
molecular condensate scaffold activity [GO:0140693]; mRNA 3'-UTR AU-rich region binding [GO:0035925]; mRNA binding [GO:0003729]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; RNA strand annealing activity [GO:0033592]; translation regulator activity [GO:0045182]
|
PF05641;PF12235;PF16096;PF16097;PF00013;PF17904;PF18336;
|
2.30.30.140;3.30.1370.10;
|
FMR1 family
|
PTM: Phosphorylation at Ser-420 by PAK1 promotes its relocalization to stress granules and activity (By similarity). Phosphorylated by MAPK1/ERK2, promoting subsequent phosphorylation by GSK3B. Phosphorylated by GSK3B, promoting ubiquitination and degradation by the proteasome (By similarity). {ECO:0000250|UniProtKB:P51114, ECO:0000250|UniProtKB:Q61584}.; PTM: Ubiquitinated by the SCF(FBXO4) complex, leading to its degradation by the proteasome: ubiquitination by the SCF(FBXO4) complex takes place following phosphorylation by GSK3B. Ubiquitinated and degraded in a GSK3B-dependent manner in during both scaling and sleep deprivation (By similarity). Ubiquitinated via 'Lys-63'-linked ubiquitin, leading to its degradation: interaction with CEP63 inhibits 'Lys-63'-linked ubiquitination (By similarity). {ECO:0000250|UniProtKB:P51114, ECO:0000250|UniProtKB:Q61584}.
|
SUBCELLULAR LOCATION: Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000250|UniProtKB:Q61584}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:P51114}. Cytoplasm {ECO:0000250|UniProtKB:Q61584}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q61584}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:Q61584}. Cell projection, axon {ECO:0000250|UniProtKB:Q61584}. Nucleus envelope {ECO:0000250|UniProtKB:P51114}. Postsynapse {ECO:0000250|UniProtKB:Q61584}. Note=Specifically localizes to cytoplasmic ribonucleoprotein membraneless compartments (By similarity). Localizes to stress granules following phosphorylation at Ser-420 by PAK1 (By similarity). Adjacent to Z-lines in muscles (By similarity). {ECO:0000250|UniProtKB:P51114, ECO:0000250|UniProtKB:Q61584}.
| null | null | null | null | null |
FUNCTION: mRNA-binding protein that acts as a regulator of mRNAs translation and/or stability, and which is required for various processes, such as neurogenesis, muscle development and spermatogenesis. Specifically binds to AU-rich elements (AREs) in the 3'-UTR of target mRNAs. Promotes formation of some phase-separated membraneless compartment by undergoing liquid-liquid phase separation upon binding to AREs-containing mRNAs, leading to assemble mRNAs into cytoplasmic ribonucleoprotein granules that concentrate mRNAs with associated regulatory factors. Required to activate translation of stored mRNAs during late spermatogenesis: acts by undergoing liquid-liquid phase separation to assemble target mRNAs into cytoplasmic ribonucleoprotein granules that recruit translation initiation factor EIF4G3 to activate translation of stored mRNAs in late spermatids (By similarity). Promotes translation of MYC transcripts by recruiting the eIF4F complex to the translation start site. Acts as a negative regulator of inflammation in response to IL19 by promoting destabilization of pro-inflammatory transcripts (By similarity). Also acts as an inhibitor of inflammation by binding to TNF mRNA, decreasing TNF protein production. Acts as a negative regulator of AMPA receptor GRIA2/GluA2 synthesis during long-lasting synaptic potentiation of hippocampal neurons by binding to GRIA2/GluA2 mRNA, thereby inhibiting its translation. Regulates proliferation of adult neural stem cells by binding to CDKN1A mRNA and promoting its expression. Acts as a regulator of sleep and synaptic homeostasis by regulating translation of transcripts in neurons. Required for embryonic and postnatal development of muscle tissue by undergoing liquid-liquid phase separation to assemble target mRNAs into cytoplasmic ribonucleoprotein granules (By similarity). Involved in the nuclear pore complex localization to the nuclear envelope by preventing cytoplasmic aggregation of nucleoporins: acts by preventing ectopic phase separation of nucleoporins in the cytoplasm via a microtubule-dependent mechanism (By similarity). {ECO:0000250|UniProtKB:P51114, ECO:0000250|UniProtKB:Q61584}.
|
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
|
O70525
|
PEX5_CAVPO
|
MAMRELVEGECGGANPLMKLAGHFTQDKALRQEGLRPGPWPPGAPASETVSKPLGVASEDELVAEFLQDQNAPLVSRAPQTFKMDDLLAEMQEIEQSNFRQAPQRAPGVADLALSENWAQEFLAAGDAVDVTQDYNETDWSQEFIAEVTDPLSVSPARWAEEYLEQSEEKLWLGEPEGAATTDRWYDEYHPEEDLQHTASDFVAKVDDPKLANSEFLKFVRQIGEGQVSLESVAGSGRAQAEQWAAEFIQQQGTSDAWVDQFTRPVNTSALDMEFERAKSAIESDVDFWDKLQAELEEMAKRDAEAHPWLSDYDDLTSASYDKGYQFEEENPLRDHPQPFEEGLLRLEEGDLPNAVLLFEAAVQQDPKHMEAWQYLGTTQAENEQELLAISALRRCLELKPDNRTALMALAVSFTNESLQRQACETLRDWLRCTPAYAHLVTPAEEGAGGAGLGSSKRILGSLLSDSLFLEVKELFLAAVRLDPTSIDPDVQCGLGVLFNLSGEYDKAVDCFTAALSVRPNDYLLWNKLGATLANGNQSEEAVAAYRRALELQPGYIRSRYNLGISCINLGAHREAVEHFLEALNMQRKSRGPRGEGGAMSENIWSTLRLALSMLGQSDAYRAADARDLSALLALFGLSQ
| null | null |
pexophagy [GO:0000425]; protein import into peroxisome matrix [GO:0016558]; protein import into peroxisome matrix, docking [GO:0016560]; protein import into peroxisome matrix, receptor recycling [GO:0016562]; protein import into peroxisome matrix, substrate release [GO:0044721]; protein import into peroxisome matrix, translocation [GO:0016561]; protein targeting to peroxisome [GO:0006625]; protein tetramerization [GO:0051262]
|
cytosol [GO:0005829]; peroxisomal matrix [GO:0005782]; peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777]
|
peroxisome matrix targeting signal-1 binding [GO:0005052]; protein carrier chaperone [GO:0140597]
|
PF13432;PF13181;
|
1.25.40.10;
|
Peroxisomal targeting signal receptor family
|
PTM: Monoubiquitinated at Cys-11 by PEX2 during PEX5 passage through the retrotranslocation channel (By similarity). Cys-11 monoubiquitination acts as a recognition signal for the PEX1-PEX6 complex and is required for PEX5 extraction and export from peroxisomes. Monoubiquitination at Cys-11 is removed by USP9X in the cytosol, resetting PEX5 for a subsequent import cycle (By similarity). When PEX5 recycling is compromised, polyubiquitinated by PEX10 during its passage through the retrotranslocation channel, leading to its degradation (By similarity). Monoubiquitination at Lys-473 by TRIM37 promotes its stability by preventing its polyubiquitination and degradation by the proteasome. Ubiquitination at Lys-528 is not mediated by the PEX2-PEX10-PEX12 ligase complex and is not related to PEX5 recycling. Monoubiquitinated at Lys-210 by PEX2 following phosphorylation by ATM in response to starvation or reactive oxygen species (ROS), leading to PEX5 recognition by p62/SQSTM1 and induction of pexophagy (By similarity). {ECO:0000250|UniProtKB:P35056, ECO:0000250|UniProtKB:P50542}.; PTM: Phosphorylated at Ser-141 by ATM in response to reactive oxygen species (ROS), promoting monoubiquitination at Lys-210 and induction of pexophagy. {ECO:0000250|UniProtKB:P50542}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P50542}. Peroxisome matrix {ECO:0000250|UniProtKB:P50542}. Note=Cycles between the cytosol and the peroxisome matrix (By similarity). Following binding to cargo proteins containing a PTS1 peroxisomal targeting signal in the cytosol, recruited to the docking complex, composed of PEX13 and PEX14, leading to translocation into the peroxisome matrix along with cargo proteins. Export and recycling to the cytosol is initiated by binding to the PEX2-PEX10-PEX12 ligase complex via its unstructured N-terminus that inserts into the ligase pore and emerges in the cytosol (By similarity). Cys-11 of PEX5 is then monoubiquitinated, promoting its extraction from peroxisomal membrane by the PEX1-PEX6 AAA ATPase complex (By similarity). Extraction is accompanied by unfolding of the TPR repeats and release of bound cargo in the peroxisome matrix. The TPR repeats refold in the cytosol and ubiquitination is removed by deubiquitinating enzymes, resetting PEX5 for a subsequent import cycle (By similarity). {ECO:0000250|UniProtKB:A0A1L8FDW4, ECO:0000250|UniProtKB:P50542}.
| null | null | null | null | null |
FUNCTION: Receptor that mediates peroxisomal import of proteins containing a C-terminal PTS1-type tripeptide peroxisomal targeting signal (SKL-type) (PubMed:11085934). Binds to cargo proteins containing a PTS1 peroxisomal targeting signal in the cytosol, and translocates them into the peroxisome matrix by passing through the PEX13-PEX14 docking complex along with cargo proteins (PubMed:11085934). PEX5 receptor is then retrotranslocated into the cytosol, leading to release of bound cargo in the peroxisome matrix, and reset for a subsequent peroxisome import cycle (By similarity). {ECO:0000250|UniProtKB:P50542, ECO:0000269|PubMed:11085934}.; FUNCTION: [Isoform 1]: In addition to promoting peroxisomal translocation of proteins containing a PTS1 peroxisomal targeting signal, mediates peroxisomal import of proteins containing a C-terminal PTS2-type peroxisomal targeting signal via its interaction with PEX7. Interaction with PEX7 only takes place when PEX7 is associated with cargo proteins containing a PTS2 peroxisomal targeting signal. PEX7 along with PTS2-containing cargo proteins are then translocated through the PEX13-PEX14 docking complex together with PEX5. {ECO:0000250|UniProtKB:P50542}.; FUNCTION: [Isoform 2]: Does not mediate translocation of peroxisomal import of proteins containing a C-terminal PTS2-type peroxisomal targeting signal. {ECO:0000250|UniProtKB:P50542}.
|
Cavia porcellus (Guinea pig)
|
O70531
|
S26A2_RAT
|
MSSENKEQHNLSPRDLPEEAYGFPPELPLGAQRGSSTDLRQFEPSDRRRAFRRIHMELHEKPDTNIRQLVMRKLQKSCQCNATKIRNRIFDFFPVLRWLPKYDLKKNILGDMMSGLIVGILLVPQSIAYSLLAGQEPIYGLYTSFFASIIYFLFGTSRHISVGIFGILCLMIGEVVDRELHKACPDIDTTSSSIAMFSNGCVVVNHTLDGLCDKSCYAIKIGSTVTFMAGVYQVAMGFFQVGFVSVYLSDALLSGFVTGASFTILTSQAKYLLGLSLPRSNGVGSVITTWIHIFRNIHKTNICDLITSLLCLLVLVPTKELNEYFKSKLPAPIPTELIVVVAATLASHFGKLNENYNSSIAGQIPTGFMPPQAPDWSLIPNVAVDAIAISIIGFAITVSLSEMFAKKHGYTVKANQEMYAIGFCNIIPSFFHCITTSAALAKTLVKESTGCQTQLSAIVTSLVLLLVLLLIAPLFYSLQKCVLGVITIVNLRGALLKFRDLPKMWRLSRMDTVIWFVTMLSSALLSTEIGLLVGVCFSMFCVILRTQMPKISLLGLEEESEIFESISTYKNLRSKSGIKVFRFIAPLYYINKECFKSALYKKTLNPVLVKAAWKKAAKRKLKEETVTFHGDPDEVSMQLSHDPLELHTVVIDCSAIQFLDTAGIHTLKEVRRDYEAIGIQVLLAQCNPSVRDSLAKGEYCKKEEENLLFYSLSEAVAFAEESQKEKGVCVVNGLSLSGD
| null | null |
chondrocyte differentiation [GO:0002062]; chondrocyte proliferation [GO:0035988]; ossification [GO:0001503]; sulfate transmembrane transport [GO:1902358]; sulfate transport [GO:0008272]
|
apical plasma membrane [GO:0016324]; microvillus membrane [GO:0031528]; plasma membrane [GO:0005886]
|
bicarbonate transmembrane transporter activity [GO:0015106]; chloride transmembrane transporter activity [GO:0015108]; oxalate transmembrane transporter activity [GO:0019531]; secondary active sulfate transmembrane transporter activity [GO:0008271]; solute:inorganic anion antiporter activity [GO:0005452]; sulfate transmembrane transporter activity [GO:0015116]
|
PF01740;PF00916;
|
3.30.750.24;
|
SLC26A/SulP transporter (TC 2.A.53) family
|
PTM: N-glycosylated. {ECO:0000250|UniProtKB:P50443}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9575183}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:20369363}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=oxalate(in) + sulfate(out) = oxalate(out) + sulfate(in); Xref=Rhea:RHEA:72275, ChEBI:CHEBI:16189, ChEBI:CHEBI:30623; Evidence={ECO:0000250|UniProtKB:Q62273}; CATALYTIC ACTIVITY: Reaction=2 chloride(in) + sulfate(out) = 2 chloride(out) + sulfate(in); Xref=Rhea:RHEA:75091, ChEBI:CHEBI:16189, ChEBI:CHEBI:17996; Evidence={ECO:0000250|UniProtKB:Q62273}; CATALYTIC ACTIVITY: Reaction=2 chloride(in) + oxalate(out) = 2 chloride(out) + oxalate(in); Xref=Rhea:RHEA:75095, ChEBI:CHEBI:17996, ChEBI:CHEBI:30623; Evidence={ECO:0000250|UniProtKB:Q62273}; CATALYTIC ACTIVITY: Reaction=bromide(in) + chloride(out) = bromide(out) + chloride(in); Xref=Rhea:RHEA:75335, ChEBI:CHEBI:15858, ChEBI:CHEBI:17996; Evidence={ECO:0000250|UniProtKB:Q62273}; CATALYTIC ACTIVITY: Reaction=chloride(out) + nitrate(in) = chloride(in) + nitrate(out); Xref=Rhea:RHEA:75339, ChEBI:CHEBI:17632, ChEBI:CHEBI:17996; Evidence={ECO:0000250|UniProtKB:Q62273}; CATALYTIC ACTIVITY: Reaction=chloride(out) + iodide(in) = chloride(in) + iodide(out); Xref=Rhea:RHEA:72379, ChEBI:CHEBI:16382, ChEBI:CHEBI:17996; Evidence={ECO:0000250|UniProtKB:Q62273};
| null | null | null | null |
FUNCTION: Sulfate transporter which mediates sulfate uptake into chondrocytes in order to maintain adequate sulfation of proteoglycans which is needed for cartilage development (PubMed:9575183). Mediates electroneutral anion exchange of sulfate ions for oxalate ions, sulfate and oxalate ions for chloride and/or hydroxyl ions and chloride ions for bromide, iodide and nitrate ions (By similarity). The coupling of sulfate transport to both hydroxyl and chloride ions likely serves to ensure transport at both acidic pH when most sulfate uptake is mediated by sulfate-hydroxide exchange and alkaline pH when most sulfate uptake is mediated by sulfate-chloride exchange (By similarity). Essential for chondrocyte proliferation, differentiation and cell size expansion (By similarity). {ECO:0000250|UniProtKB:Q62273, ECO:0000269|PubMed:9575183}.
|
Rattus norvegicus (Rat)
|
O70534
|
DLK1_RAT
|
MIATGALLRVLLLLLAFGHSTYGAECDPACDPQHGFCEADNVCRCEPGWEGPLCEKCVTSPGCVNGLCEEPWQCVCKEGWDGKFCEIDIRACTSTPCANNGTCVDLEKGQYECSCTPGFSGKDCQHKAGPCVINGSPCQHGGACVDDEGRASHASCLCPPGFSGNFCEIVTNSCTPNPCENDGVCTDIGGDFRCRCPAGFVDKTCSRPVSNCASGPCLNGGTCLQHTQVSFECLCKPPFMGPTCAKKRGTSPVQVTHLPSGYGLTYRLTPGVHELPVQQPEHHILKVSMKELNKSAPLLTEGQAICFTILGVLTSLVVLGTVAIVFLNKCEAWVSNLRYNHMLRKKKNLLLQYNSGEELAVNIIFPEKIDMTTFNKEAGDEDI
| null | null |
bone mineralization [GO:0030282]; cell differentiation [GO:0030154]; embryonic skeletal system development [GO:0048706]; multicellular organism growth [GO:0035264]; negative regulation of fat cell differentiation [GO:0045599]; negative regulation of Notch signaling pathway [GO:0045746]; negative regulation of vascular endothelial cell proliferation [GO:1905563]; ossification [GO:0001503]; osteoblast differentiation [GO:0001649]; positive regulation of bone resorption [GO:0045780]; positive regulation of cytokine production [GO:0001819]; post-embryonic development [GO:0009791]; regulation of gene expression [GO:0010468]
|
cytoplasm [GO:0005737]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; membrane [GO:0016020]
|
calcium ion binding [GO:0005509]
|
PF21700;PF00008;PF12661;
|
2.10.25.10;
| null |
PTM: Glycosylated. {ECO:0000250|UniProtKB:Q09163}.
|
SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I membrane protein. Cytoplasm {ECO:0000269|PubMed:9645708}.
| null | null | null | null | null |
FUNCTION: May have a role in neuroendocrine differentiation. Inhibits adipocyte differentiation. {ECO:0000250|UniProtKB:Q09163}.
|
Rattus norvegicus (Rat)
|
O70535
|
LIFR_RAT
|
MGAFSWWRQPSWMADNKRGRMTPSLPWLLSALTLLHLMMHVNGLKRGVQQDLKCTTNNMRVWDCSWPAPLGVSPGTVKDICIKDRPHSCHRLETTNVKIPALSPGDHEVTINYQNGFQSKFTLNEKDVSLVPDTPEILSLSADFSTSTLQLKWNDKGSALPYPSNATWEVKVLQNPRTEPVALVSLNTVLSGKDKGHHWNWTSELPLQCATHSVSIRWHIDYPRFSGYKEWSEWSPLKNISWTRNTETNVFPQDKVVLAGSNMTICCISTTKVLSGQIGNTFRPLIHLYGETVAINILNIPVSENSGSNVIFSTVDDVYGTVVFAGYPPDVPQKLSCETHDLKEIICSWNPGRITGLVGPRNTEYTLFESISGKSAVFHRFEELANETYWLTLKMAPDQEIHNFTLTARNPLGQTESAIVINATERVALHVPISLKVKDVNSTVVTLSWYLPGNFTKINLVCQIEICKANSKKEVRNVTMRGAEDSTYHVAVDKLNPYTIYTFRVRCSSETFWKWSKWSNEKRYLTTEATPSKGPDTWREWSSDGKNLIIYWKPLPINEANGKILSYNVSCSSSEETQSLSEILDPQHKAEIKVNKNDYIISVVARNSAGSSPPSKIASMEIPNDDITVEQAVGIGNRIFLSWQHNPNMTCDYVIKWCNSSWSEPCLLDWIKVPSNSTGTVIESDQFQPGVRYNFYLYGCTNQGYQLLRSTIGYIEELAPIVAPNFTVEDTSADSILVKWDDIPVEELRGFLRGYLFYFQKGERDTPKTRSLETSHSDIKLKNITDISQKTLRIADLQGKTSYHLVLRAYTHGGLGPEKSMFVVTKENSVGLIIAILIPVAVAVIVGVVTSILCYRKREWIKETFYPDIPNPENCKALQFQKSVCEGSNALKTLEMNPCTPNHVEVLESRSIPPKIEDTEITSPVSERPGESSETDPENQAAVSYCPPIIEEEITNPAADEAGGASQVVYIDVQSMYQPQAKAEDEQDTDPVMVAGYKPQMRLPINPTAEDTTAEDEADKTAGYRPQANVNTWNLVSPDSPRSTDSNSEVVSFGSPCSINSRQFLIPPKDEDSPKSNGGGWSFTNFFQNKPND
| null | null |
animal organ regeneration [GO:0031100]; ciliary neurotrophic factor-mediated signaling pathway [GO:0070120]; cytokine-mediated signaling pathway [GO:0019221]; leukemia inhibitory factor signaling pathway [GO:0048861]; negative regulation of muscle cell apoptotic process [GO:0010656]; neuron projection morphogenesis [GO:0048812]; oncostatin-M-mediated signaling pathway [GO:0038165]; positive regulation of cell population proliferation [GO:0008284]; response to cytokine [GO:0034097]; response to organic cyclic compound [GO:0014070]
|
external side of plasma membrane [GO:0009897]; receptor complex [GO:0043235]
|
ciliary neurotrophic factor receptor binding [GO:0005127]; cytokine binding [GO:0019955]; cytokine receptor activity [GO:0004896]; growth factor binding [GO:0019838]; leukemia inhibitory factor receptor activity [GO:0004923]; oncostatin-M receptor activity [GO:0004924]
|
PF00041;PF21177;PF17971;PF18207;
|
2.60.40.10;
|
Type I cytokine receptor family, Type 2 subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Signal-transducing molecule. May have a common pathway with IL6ST. The soluble form inhibits the biological activity of LIF by blocking its binding to receptors on target cells (By similarity). {ECO:0000250}.
|
Rattus norvegicus (Rat)
|
O70536
|
SOAT1_RAT
|
MVGEETSLRNRLSRSAENPEQDEAQKNLLDTHRNGHITMKQLIAKKRQLAAEAEELKPLFLKEVGCHFDDFVTNLIDKSASLDNGGCALTTFSILEEMKNNHRAKDLRAPPEQGKIFISRRSLLDELFEVDHIRTIYHMFIALLIIFILSTLVVDYIDEGRLVLEFSLLAYAFGQFPIVIWTWWAMFLSTLAIPYFLFQRWAHGYSKSSHPLIYSLIHGAFFLVFQLGILGFIPTYVVLAYTLPPASRFILILEQIRLVMKAHSYVRENVPRVLSAAKEKSSTVPVPTVNQYLYFLFAPTLIYRDSYPRTPTVRWGYVAMQFLQVFGCLFYVYYIFERLCAPLFRNIKQEPFSARVLVLCVFNSILPGVLMLFLSFFAFLHCWLNAFAEMLRFGDRMFYKDWWNSTSYSNYYRTWNVVVHDWLYYYVYKDLLWFFSKRFRPAAMLAVFALSAVVHEYALAVCLSYFYPVLFVLFMFFGMAFNFIVNDSRKRPVWNIMVRASLFLGHGVILCFYSQEWYARQRCPLKNPTFLDYVRPRTWTCRYVF
|
2.3.1.26
| null |
cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; cholesterol storage [GO:0010878]; macrophage derived foam cell differentiation [GO:0010742]; positive regulation of amyloid precursor protein biosynthetic process [GO:0042986]; very-low-density lipoprotein particle assembly [GO:0034379]
|
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]
|
cholesterol binding [GO:0015485]; cholesterol O-acyltransferase activity [GO:0034736]; fatty-acyl-CoA binding [GO:0000062]; sterol O-acyltransferase activity [GO:0004772]
|
PF03062;
| null |
Membrane-bound acyltransferase family, Sterol o-acyltransferase subfamily
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P35610}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P35610}.
|
CATALYTIC ACTIVITY: Reaction=a long-chain fatty acyl-CoA + a sterol = a sterol ester + CoA; Xref=Rhea:RHEA:59816, ChEBI:CHEBI:15889, ChEBI:CHEBI:35915, ChEBI:CHEBI:57287, ChEBI:CHEBI:83139; EC=2.3.1.26; Evidence={ECO:0000250|UniProtKB:P35610}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59817; Evidence={ECO:0000250|UniProtKB:P35610}; CATALYTIC ACTIVITY: Reaction=an acyl-CoA + cholesterol = a cholesterol ester + CoA; Xref=Rhea:RHEA:17729, ChEBI:CHEBI:16113, ChEBI:CHEBI:17002, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342; Evidence={ECO:0000250|UniProtKB:P35610}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17730; Evidence={ECO:0000250|UniProtKB:P35610}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + cholesterol = cholesteryl (9Z-octadecenoate) + CoA; Xref=Rhea:RHEA:41436, ChEBI:CHEBI:16113, ChEBI:CHEBI:46898, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387; Evidence={ECO:0000250|UniProtKB:P35610}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41437; Evidence={ECO:0000250|UniProtKB:P35610}; CATALYTIC ACTIVITY: Reaction=cholesterol + hexadecanoyl-CoA = cholesteryl hexadecanoate + CoA; Xref=Rhea:RHEA:42792, ChEBI:CHEBI:3663, ChEBI:CHEBI:16113, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; Evidence={ECO:0000250|UniProtKB:P35610}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42793; Evidence={ECO:0000250|UniProtKB:P35610}; CATALYTIC ACTIVITY: Reaction=cholesterol + octadecanoyl-CoA = cholesteryl octadecanoate + CoA; Xref=Rhea:RHEA:42812, ChEBI:CHEBI:16113, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, ChEBI:CHEBI:82750; Evidence={ECO:0000250|UniProtKB:P35610}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42813; Evidence={ECO:0000250|UniProtKB:P35610}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoyl-CoA + cholesterol = cholesteryl (9Z,12Z)-octadecadienoate + CoA; Xref=Rhea:RHEA:42796, ChEBI:CHEBI:16113, ChEBI:CHEBI:41509, ChEBI:CHEBI:57287, ChEBI:CHEBI:57383; Evidence={ECO:0000250|UniProtKB:P35610}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42797; Evidence={ECO:0000250|UniProtKB:P35610}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + cholesterol = cholesteryl (5Z,8Z,11Z,14Z)-eicosatetraenoate + CoA; Xref=Rhea:RHEA:42816, ChEBI:CHEBI:16113, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:82751; Evidence={ECO:0000250|UniProtKB:P35610}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42817; Evidence={ECO:0000250|UniProtKB:P35610}; CATALYTIC ACTIVITY: Reaction=(9Z)-hexadecenoyl-CoA + cholesterol = cholesteryl (9Z)-hexadecenoate + CoA; Xref=Rhea:RHEA:64320, ChEBI:CHEBI:16113, ChEBI:CHEBI:57287, ChEBI:CHEBI:61540, ChEBI:CHEBI:84323; Evidence={ECO:0000250|UniProtKB:P35610}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64321; Evidence={ECO:0000250|UniProtKB:P35610}; CATALYTIC ACTIVITY: Reaction=(11Z)-octadecenoyl-CoA + cholesterol = cholesteryl (11Z)-octadecenoate + CoA; Xref=Rhea:RHEA:64324, ChEBI:CHEBI:16113, ChEBI:CHEBI:57287, ChEBI:CHEBI:75121, ChEBI:CHEBI:88768; Evidence={ECO:0000250|UniProtKB:P35610}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64325; Evidence={ECO:0000250|UniProtKB:P35610}; CATALYTIC ACTIVITY: Reaction=(7Z)-octadecenoyl-CoA + cholesterol = cholesteryl (7Z)-octadecenoate + CoA; Xref=Rhea:RHEA:64328, ChEBI:CHEBI:16113, ChEBI:CHEBI:57287, ChEBI:CHEBI:152049, ChEBI:CHEBI:152050; Evidence={ECO:0000250|UniProtKB:P35610}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64329; Evidence={ECO:0000250|UniProtKB:P35610};
| null | null | null | null |
FUNCTION: Catalyzes the formation of fatty acid-cholesterol esters, which are less soluble in membranes than cholesterol. Plays a role in lipoprotein assembly and dietary cholesterol absorption. Utilizes oleoyl-CoA ((9Z)-octadecenoyl-CoA) preferentially as susbstrateb a higher activity towards an acyl-CoA substrate with a double bond at the delta-9 position (9Z) than towards saturated acyl-CoA or an unsaturated acyl-CoA with a double bond at the delta-7 (7Z) or delta-11 (11Z) positions. {ECO:0000250|UniProtKB:P35610}.
|
Rattus norvegicus (Rat)
|
O70546
|
KDM6A_MOUSE
|
MKSCGVSLATAAAAAAAAAFGDEEKKMAAGKASGESEEASPSLTAEEREALGGLDSRLFGFVRFHEDGARMKALLGKAVRCYESLILKAEGKVESDFFCQLGHFNLLLEDYPKALSAYQRYYSLQSDYWKNAAFLYGLGLVYFHYNAFQWAIKAFQEVLYVDPSFCRAKEIHLRLGLMFKVNTDYESSLKHFQLALVDCNPCTLSNAEIQFHIAHLYETQRKYHSAKEAYEQLLQTENLSAQVKATILQQLGWMHHTVDLLGDKATKESYAIQYLQKSLEADPNSGQSWYFLGRCYSSIGKVQDAFISYRQSIDKSEASADTWCSIGVLYQQQNQPMDALQAYICAVQLDHGHAAAWMDLGTLYESCNQPQDAIKCYLNATRSKNCSNTSGLAARIKYLQAQLCNLPQGSLQNKTKLLPSIEEAWSLPIPAELTSRQGAMNTAQQNTSDNWSGGNAPPPVEQQTHSWCLTPQKLQHLEQLRANRNNLNPAQKLMLEQLESQFVLMQQHQMRQTGVAQVRPTGILNGPTVDSSLPTNSVSGQQPQLPLTRMPSVSQPGVHTACPRQTLANGPFSAGHVPCSTSRTLGSTDTVLIGNNHVTGSGSNGNVPYLQRNAPTLPHNRTNLTSSTEEPWKNQLSNSTQGLHKGPSSHLAGPNGERPLSSTGPSQHLQAAGSGIQNQNGHPTLPSNSVTQGAALNHLSSHTATSGGQQGITLTKESKPSGNTLTVPETSRQTGETPNSTASVEGLPNHVHQVMADAVCSPSHGDSKSPGLLSSDNPQLSALLMGKANNNVGPGTCDKVNNIHPTVHTKTDNSVASSPSSAISTATPSPKSTEQTTTNSVTSLNSPHSGLHTINGEGMEESQSPIKTDLLLVSHRPSPQIIPSMSVSIYPSSAEVLKACRNLGKNGLSNSSILLDKCPPPRPPSSPYPPLPKDKLNPPTPSIYLENKRDAFFPPLHQFCTNPNNPVTVIRGLAGALKLDLGLFSTKTLVEANNEHMVEVRTQLLQPADENWDPTGTKKIWHCESNRSHTTIAKYAQYQASSFQESLREENEKRSHHKDHSDSESTSSDNSGKRRKGPFKTIKFGTNIDLSDDKKWKLQLHELTKLPAFVRVVSAGNLLSHVGHTILGMNTVQLYMKVPGSRTPGHQENNNFCSVNINIGPGDCEWFVVPEGYWGVLNDFCEKNNLNFLMGSWWPNLEDLYEANVPVYRFIQRPGDLVWINAGTVHWVQAIGWCNNIAWNVGPLTACQYKLAVERYEWNKLQNVKSIVPMVHLSWNMARNIKVSDPKLFEMIKYCLLRTLKQCQTLREALIAAGKEIIWHGRTKEEPAHYCSICEVEVFDLLFVTNESNSRKTYIVHCQDCARKTSGNLENFVVLEQYKMEDLMQVYDQFTLAPPLPSASS
|
1.14.11.68
|
COFACTOR: Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250}; COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
|
cellular response to angiotensin [GO:1904385]; cellular response to endothelin [GO:1990859]; cellular response to hypoxia [GO:0071456]; cellular response to transforming growth factor beta stimulus [GO:0071560]; cellular response to vitamin D [GO:0071305]; chromatin remodeling [GO:0006338]; circulatory system development [GO:0072359]; embryonic organ development [GO:0048568]; heart development [GO:0007507]; heart morphogenesis [GO:0003007]; in utero embryonic development [GO:0001701]; mesodermal cell differentiation [GO:0048333]; multicellular organism growth [GO:0035264]; negative regulation of hypoxia-induced intrinsic apoptotic signaling pathway [GO:1903298]; neural tube closure [GO:0001843]; neural tube development [GO:0021915]; notochord morphogenesis [GO:0048570]; positive regulation of cell size [GO:0045793]; positive regulation of gene expression [GO:0010628]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein modification process [GO:0036211]; regulation of gene expression [GO:0010468]; respiratory system process [GO:0003016]; somite rostral/caudal axis specification [GO:0032525]
|
histone methyltransferase complex [GO:0035097]; MLL3/4 complex [GO:0044666]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
chromatin DNA binding [GO:0031490]; histone H3K27me2/H3K27me3 demethylase activity [GO:0071558]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF02373;PF21322;PF21326;PF13432;PF13181;
|
1.20.58.1370;2.10.110.20;2.60.120.650;1.25.40.10;
|
UTX family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=2 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(27)-[histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N(6)-methyl-L-lysyl(27)-[histone H3] + 2 succinate; Xref=Rhea:RHEA:60224, Rhea:RHEA-COMP:15535, Rhea:RHEA-COMP:15544, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:61929, ChEBI:CHEBI:61961; EC=1.14.11.68; Evidence={ECO:0000250|UniProtKB:O15550};
| null | null | null | null |
FUNCTION: Histone demethylase that specifically demethylates 'Lys-27' of histone H3, thereby playing a central role in histone code. Demethylates trimethylated and dimethylated but not monomethylated H3 'Lys-27'. Plays a central role in regulation of posterior development, by regulating HOX gene expression. Demethylation of 'Lys-27' of histone H3 is concomitant with methylation of 'Lys-4' of histone H3, and regulates the recruitment of the PRC1 complex and monoubiquitination of histone H2A (By similarity). Plays a demethylase-independent role in chromatin remodeling to regulate T-box family member-dependent gene expression (PubMed:21095589). {ECO:0000250|UniProtKB:O15550, ECO:0000269|PubMed:21095589}.
|
Mus musculus (Mouse)
|
O70551
|
SRPK1_MOUSE
|
MERKVLALQARKKRTKAKKDKAQRKPETQHRGSAPHSESDIPEQEEEILGSDDDEQEDPNDYCKGGYHLVKIGDLFNGRYHVIRKLGWGHFSTVWLSWDIQGKKFVAMKVVKSAEHYTETALDEIRLLKSVRNSDPNDPNGEMVVQLLDDFKISGVNGTHICMVFEVLGHHLLKWIIKSNYQGLPLPCVKKIIQQVLQGLDYLHTKCRIIHTDIKPENILLSVNEQYIRRLAAEATEWQRSGAPPPSGSAVSTAPQPKPADKMSKNKKKKLKKKQKRQAELLEKRMQEIEEMEKESGPGQKRPNKQEESESPVDRPLTENPPNKMTQEKLEESNSIGQDQTLTERGGEGGAPEINCNGVIGVVNYPENSNNETLRHKEDLHNANDCDVHTLKQEPSFLNSSNGDSSPSQDTDSCTPTASETMVCQSSAEQSLTRQDITQLEESIRADTPSGDEQEPNGALDSKGKFSAGNFLINPLEPKNAEKLQVKIADLGNACWVHKHFTEDIQTRQYRSLEVLIGSGYNTPADIWSTACMAFELATGDYLFEPHSGEDYTRDEDHIALIIELLGKVPRKLIVAGKYSKEFFTKKGDLKHITKLKPWGLLEVLVEKYEWPQEEAAGFTDFLLPMLELMPEKRATAAECLRHPWLNS
|
2.7.11.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:10390541, ECO:0000269|PubMed:9446799};
|
cell differentiation [GO:0030154]; chromosome segregation [GO:0007059]; intracellular signal transduction [GO:0035556]; negative regulation of viral genome replication [GO:0045071]; positive regulation of viral genome replication [GO:0045070]; protein phosphorylation [GO:0006468]; regulation of mRNA processing [GO:0050684]; spliceosomal complex assembly [GO:0000245]
|
chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; nuclear matrix [GO:0016363]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, CMGC Ser/Thr protein kinase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96SB4}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q96SB4}. Nucleus matrix {ECO:0000250|UniProtKB:Q96SB4}. Microsome {ECO:0000250|UniProtKB:Q96SB4}. Nucleus speckle {ECO:0000250|UniProtKB:Q96SB4}. Chromosome {ECO:0000250|UniProtKB:Q96SB4}. Note=Shuttles between the nucleus and the cytoplasm (By similarity). Inhibition of the Hsp90 ATPase activity, osmotic stress and interaction with HHV-1 ICP27 protein can induce its translocation to the nucleus (By similarity). KAT5/TIP60 inhibits its nuclear translocation (By similarity). Preferentially localizes to the promoter of gene coding regions (By similarity). {ECO:0000250|UniProtKB:Q96SB4}.
|
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; Evidence={ECO:0000269|PubMed:10390541, ECO:0000269|PubMed:9446799}; 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; Evidence={ECO:0000269|PubMed:10390541, ECO:0000269|PubMed:9446799};
| null | null | null | null |
FUNCTION: Serine/arginine-rich protein-specific kinase which specifically phosphorylates its substrates at serine residues located in regions rich in arginine/serine dipeptides, known as RS domains and is involved in the phosphorylation of SR splicing factors and the regulation of splicing. Plays a central role in the regulatory network for splicing, controlling the intranuclear distribution of splicing factors in interphase cells and the reorganization of nuclear speckles during mitosis. Can influence additional steps of mRNA maturation, as well as other cellular activities, such as chromatin reorganization in somatic and sperm cells and cell cycle progression. Phosphorylates SFRS2, ZRSR2, LBR and PRM1. Phosphorylates SRSF1 using a directional (C-terminal to N-terminal) and a dual-track mechanism incorporating both processive phosphorylation (in which the kinase stays attached to the substrate after each round of phosphorylation) and distributive phosphorylation steps (in which the kinase and substrate dissociate after each phosphorylation event). The RS domain of SRSF1 binds first to a docking groove in the large lobe of the kinase domain of SRPK1. This induces certain structural changes in SRPK1 and/or RRM2 domain of SRSF1, allowing RRM2 to bind the kinase and initiate phosphorylation. The cycles continue for several phosphorylation steps in a processive manner (steps 1-8) until the last few phosphorylation steps (approximately steps 9-12). During that time, a mechanical stress induces the unfolding of the beta-4 motif in RRM2, which then docks at the docking groove of SRPK1. This also signals RRM2 to begin to dissociate, which facilitates SRSF1 dissociation after phosphorylation is completed. Can mediate hepatitis B virus (HBV) core protein phosphorylation. It plays a negative role in the regulation of HBV replication through a mechanism not involving the phosphorylation of the core protein but by reducing the packaging efficiency of the pregenomic RNA (pgRNA) without affecting the formation of the viral core particles. Can induce splicing of exon 10 in MAPT/TAU (By similarity). {ECO:0000250, ECO:0000269|PubMed:10390541, ECO:0000269|PubMed:9446799}.
|
Mus musculus (Mouse)
|
O70552
|
BTG4_MOUSE
|
MRDEIATAVFFVTRLVKKHEKLSTQQIETFALKLMTILFEKYRGHWHPDCPSKGQAFRCIRINNNENKDPVLERACAESNVNFFHLGLPKEMTIWVDPYEVCCRYGEKKHPFTIASFKGRWENWELAQHVSCAVNRATGDCSSGTSSDEESCSREAQIIPKVNNPKSVYQVENFKQSLQPWFCLPRRKHLADGRGFLPGAACHPVPKSSKWCRPASRRVDRYHWVNAQLFSGQTAPGEPGEEALSSLKQK
| null | null |
maternal-to-zygotic transition of gene expression [GO:0160021]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of mitotic cell cycle [GO:0045930]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]
|
mRNA 3'-UTR binding [GO:0003730]
|
PF07742;
|
3.90.640.90;
|
BTG family
| null | null | null | null | null | null | null |
FUNCTION: Adapter protein that bridges CNOT7, a catalytic subunit of the CCR4-NOT complex, to EIF4E, and facilitates maternal mRNAs decay during the maturation of oocytes and in the fertilized egg (PubMed:27065194). It is therefore required for the maternal-zygotic transition (MZT), zygotic cleavage and initiation of embryonic development (PubMed:27065194). {ECO:0000269|PubMed:27065194}.
|
Mus musculus (Mouse)
|
O70566
|
DIAP2_MOUSE
|
MEELGAAASGAGGGGGGGEEHGGGRSNKRGAGNRAANEEETRNKPKLRDRITSFRKSATKREKPVIQHSIDYQTAVVEIPPALIVHDDRSLILSEKEVLDLFEKMMEDMNLNEEKKAPLRKKDFSIKREMVVQYISATSKSIVGSKVLGGLKNSKHEFTLSSQEYVHELRSGISDEKLLNCLESLRVSLTSHPVSWVNNFGYEGLGVLLDVLEKLLDKKQQENIDKKNQYKVIQCLKAFMNNKFGLQRILGDERSLLLLARAIDPKQQNMMTEIVKILSAICIVGEENILDKLLGGITAAAELNNRERFSPIVEGLENNEALHLQVACMQFINALVTSPYDLDFRIHLRNEFLRCGLKAMLPTLKEIENEGLDIQLRVFEENKEDDLSELSHRLNDIRAEMDDINEVYHLLYNMLKDTAAEPYLLSILQHFLLIRNDYYIRPQYYKIIEECVSQIVLHCSGMDPDFKYRQRIDFDFTHLLDACVNKAKVEENEQKAMEFSKKFDEEFTARQEAQAELQKRDEKIKELETEIQQLRGQGVPSAIPGPPPPPPLPGAGPCPPPPPPPPPPPPLPGVVPPPPPPLPGMPGIPPPPPPPLSGVPPPPPPPGGVFPLLSGPIELPYGMKQKKLYKPDIPMKRINWSKIEPKELSENCVWLKLKEEKYENADLFAKLALTFPSQMKGQRNTEAAEENRSGPPKKKVKELRILDTKTAQNLSIFLGSYRMPYEEIKNIILEVNEEMLSEALIQNLVKYLPDQNALRELAQLKSEYDDLCEPEQFGVVMSTVKMLRPRLTSILFKLTFEEHVNNIKPSIIAVTLACEELKKSESFKRLLELILLVGNYMNSGSRNAQSLGFKINFLCKIKDTKSADQKSTLLHFLAEICDEKYRDILKFPDELEHVESAGKVSAQILKSNLVAMEQSILHLEKNIKNFPPAESHHDKFVEKMMSFTQNAREQYDKLSTMHSNMLKLYESLGEYFIFDPNTVNMEEFFGDLNTFRTLFLEALKENHKRKEMEEKSRRAKLAKEKAEQEKLERQKKKKQLIDINKEGDETGVMDNLLEALQSGAAFRDRRKRIPRNPDNRRPPLERSRSRHNGAMSSK
| null | null |
actin filament polymerization [GO:0030041]; axon midline choice point recognition [GO:0016199]; ephrin receptor signaling pathway [GO:0048013]; multicellular organismal locomotion [GO:0071965]; negative regulation of neuron projection regeneration [GO:0070571]; neuron projection retraction [GO:0106028]; oogenesis [GO:0048477]; protein localization [GO:0008104]
|
actin filament [GO:0005884]
|
actin binding [GO:0003779]; small GTPase binding [GO:0031267]
|
PF06367;PF06371;PF02181;
|
1.20.58.630;6.10.30.30;1.10.20.40;1.20.58.2220;1.10.238.150;1.25.10.10;
|
Formin homology family, Diaphanous subfamily
| null | null | null | null | null | null | null |
FUNCTION: May be involved in oogenesis.
|
Mus musculus (Mouse)
|
O70571
|
PDK4_MOUSE
|
MKAARFVMRSASSLSSASLVPREVELFSRYSPSPLSMKQLLDFGSENACERTSFAFLRQELPVRLANILKEIDILPDRLVNTPSVQLVKSWYIQSLMDLVEFHEKSPEDQKALSEFVDTLVKVRNRHHNVVPTMAQGILEYKDTCTVDPVTNQNLQYFLDRFYMNRISTRMLMNQHILIFSDSKTGNPSHIGSIDPNCDVVAVVQDAFECAKMLCDQYYLTSPELNLTQVNGKFPGQPIHIVYVPSHLHHMLFELFKNAMRATVEHQENRPSLTPVEATVVLGKEDLTIKISDRGGGVPLRITDRLFSYTYSTAPTPVMDNSRNAPLAGFGYGLPISRLYAKYFQGDLNLYSMSGYGTDAIIYLKALSSESVEKLPVFNKSAFKHYQMSSEADDWCIPSREPKNLAKEKLAV
|
2.7.11.2
| null |
cellular response to fatty acid [GO:0071398]; cellular response to starvation [GO:0009267]; glucose homeostasis [GO:0042593]; insulin receptor signaling pathway [GO:0008286]; negative regulation of anoikis [GO:2000811]; phosphorylation [GO:0016310]; reactive oxygen species metabolic process [GO:0072593]; regulation of acetyl-CoA biosynthetic process from pyruvate [GO:0010510]; regulation of bone resorption [GO:0045124]; regulation of cellular ketone metabolic process [GO:0010565]; regulation of fatty acid biosynthetic process [GO:0042304]; regulation of fatty acid oxidation [GO:0046320]; regulation of glucose metabolic process [GO:0010906]; regulation of pH [GO:0006885]; response to starvation [GO:0042594]
|
mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]
|
ATP binding [GO:0005524]; protein serine/threonine/tyrosine kinase activity [GO:0004712]; pyruvate dehydrogenase (acetyl-transferring) kinase activity [GO:0004740]
|
PF10436;PF02518;
|
1.20.140.20;3.30.565.10;
|
PDK/BCKDK protein kinase family
| null |
SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[pyruvate dehydrogenase E1 alpha subunit] = ADP + H(+) + O-phospho-L-seryl-[pyruvate dehydrogenase E1 alpha subunit]; Xref=Rhea:RHEA:23052, Rhea:RHEA-COMP:13689, Rhea:RHEA-COMP:13690, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.2;
| null | null | null | null |
FUNCTION: Kinase that plays a key role in regulation of glucose and fatty acid metabolism and homeostasis via phosphorylation of the pyruvate dehydrogenase subunits PDHA1 and PDHA2. This inhibits pyruvate dehydrogenase activity, and thereby regulates metabolite flux through the tricarboxylic acid cycle, down-regulates aerobic respiration and inhibits the formation of acetyl-coenzyme A from pyruvate. Inhibition of pyruvate dehydrogenase decreases glucose utilization and increases fat metabolism in response to prolonged fasting and starvation. Plays an important role in maintaining normal blood glucose levels under starvation, and is involved in the insulin signaling cascade. Via its regulation of pyruvate dehydrogenase activity, plays an important role in maintaining normal blood pH and in preventing the accumulation of ketone bodies under starvation. In the fed state, mediates cellular responses to glucose levels and to a high-fat diet. Regulates both fatty acid oxidation and de novo fatty acid biosynthesis. Plays a role in the generation of reactive oxygen species. Protects detached epithelial cells against anoikis. Plays a role in cell proliferation via its role in regulating carbohydrate and fatty acid metabolism. {ECO:0000269|PubMed:16606348, ECO:0000269|PubMed:18083902, ECO:0000269|PubMed:18430968, ECO:0000269|PubMed:19627255, ECO:0000269|PubMed:21321124, ECO:0000269|PubMed:22360721}.
|
Mus musculus (Mouse)
|
O70572
|
NSMA_MOUSE
|
MKLNFSLRLRVFNLNCWDIPYLSKHRADRMKRLGDFLNLENFDLALLEEVWSEQDFQYLRQRLSLTYPDAHYFRSGMIGSGLCVFSKHPIQEIFQHVYSLNGYPYMFHHGDWFCGKSVGLLVLRLSGLVLNAYVTHLHAEYSRQKDIYFAHRVAQAWELAQFIHHTSKNADVVLLCGDLNMHPKDLGCCLLKEWTGLHDAFVETEDFKGSDDGCTMVPKNCYVSQQDLGPFPSGIRIDYVLYKAVSEFHVCCETLKTTTGCDPHSDKPFSDHEALMATLYVKHSPPQEDPCTACGPLERSDLISVLREARTELGLGIAKARWWAAFSGYVIVWGLSLLVLLCVLAAGEEAREVAIILCIPSVGLVLVAGAVYLFHKQEAKGLCRAQAEMLHVLTRETETQDRGSEPHLAYCLQQEGDRA
|
3.1.4.12
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:9520418};
|
ceramide biosynthetic process [GO:0046513]; ceramide metabolic process [GO:0006672]; intracellular signal transduction [GO:0035556]; positive regulation of apoptotic process [GO:0043065]; response to mechanical stimulus [GO:0009612]; sphingolipid catabolic process [GO:0030149]; sphingomyelin catabolic process [GO:0006685]; sphingomyelin metabolic process [GO:0006684]
|
caveola [GO:0005901]; cell periphery [GO:0071944]; endoplasmic reticulum [GO:0005783]; plasma membrane [GO:0005886]
|
metal ion binding [GO:0046872]; sphingomyelin phosphodiesterase activity [GO:0004767]
|
PF03372;
|
3.60.10.10;
|
Neutral sphingomyelinase family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9520418}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=a sphingomyelin + H2O = an N-acylsphing-4-enine + H(+) + phosphocholine; Xref=Rhea:RHEA:19253, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17636, ChEBI:CHEBI:52639, ChEBI:CHEBI:295975; EC=3.1.4.12; Evidence={ECO:0000269|PubMed:15764706, ECO:0000269|PubMed:9520418}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19254; Evidence={ECO:0000305|PubMed:15764706}; CATALYTIC ACTIVITY: Reaction=an N-(acyl)-sphingosylphosphocholine + H2O = an N-acyl-sphingoid base + H(+) + phosphocholine; Xref=Rhea:RHEA:45300, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:64583, ChEBI:CHEBI:83273, ChEBI:CHEBI:295975; Evidence={ECO:0000250|UniProtKB:O60906}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45301; Evidence={ECO:0000250|UniProtKB:O60906}; CATALYTIC ACTIVITY: Reaction=1-O-octadecyl-sn-glycero-3-phosphocholine + H2O = 1-O-octadecyl-sn-glycerol + H(+) + phosphocholine; Xref=Rhea:RHEA:39923, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:74001, ChEBI:CHEBI:75216, ChEBI:CHEBI:295975; Evidence={ECO:0000250|UniProtKB:O60906}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39924; Evidence={ECO:0000250|UniProtKB:O60906}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycerol + H(+) + phosphocholine; Xref=Rhea:RHEA:41119, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:75542, ChEBI:CHEBI:295975; Evidence={ECO:0000250|UniProtKB:O60906}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41120; Evidence={ECO:0000250|UniProtKB:O60906}; CATALYTIC ACTIVITY: Reaction=a sphingosylphosphocholine + H2O = a sphingoid base + H(+) + phosphocholine; Xref=Rhea:RHEA:45296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:84410, ChEBI:CHEBI:85171, ChEBI:CHEBI:295975; Evidence={ECO:0000250|UniProtKB:O60906}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45297; Evidence={ECO:0000250|UniProtKB:O60906}; CATALYTIC ACTIVITY: Reaction=1-O-hexadecyl-sn-glycero-3-phosphocholine + H2O = 1-O-hexadecyl-sn-glycerol + H(+) + phosphocholine; Xref=Rhea:RHEA:36087, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:34115, ChEBI:CHEBI:64496, ChEBI:CHEBI:295975; Evidence={ECO:0000250|UniProtKB:O60906}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36088; Evidence={ECO:0000250|UniProtKB:O60906};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=15 uM for sphingomyelin (at pH 7.4 and 37 degrees Celsius) {ECO:0000269|PubMed:9520418}; Vmax=10 umol/h/mg enzyme with sphingomyelin as substrate (at pH 7.4 and 37 degrees Celsius) {ECO:0000269|PubMed:9520418};
|
PATHWAY: Lipid metabolism; sphingolipid metabolism. {ECO:0000269|PubMed:9520418}.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5-7.5. {ECO:0000269|PubMed:9520418};
| null |
FUNCTION: Catalyzes, at least in vitro, the hydrolysis of sphingomyelin to form ceramide and phosphocholine (PubMed:9520418). Also hydrolyzes 1-O-alkyl-2-lyso-sn-glycero-3-phosphocholine (lyso-platelet-activating factor) in vivo (By similarity). Also acts on 1-acyl-2-lyso-sn-glycero-3-phosphocholine (lyso-PC) and sphingosylphosphocholine (By similarity). {ECO:0000250|UniProtKB:O60906, ECO:0000269|PubMed:9520418}.
|
Mus musculus (Mouse)
|
O70576
|
STAG3_MOUSE
|
MPTLWSPSTQHHGSSSGSESSPLQKSVRRAQMALSPCSSSILPCDDRDSQGTAEWDSPSTNEDSDFEDSLRRNVKKRAAKQPPKAVPAAKHRKKQSRIVSSGNGKNESVPSTNYLFDAVKAARSCMQSLVDEWLDNYKQDENAGFLELINFFIRACGCKSTVTPEMFKTMSNSEIIQHLTEEFNEDSGDYPLTAPGPSWKKFQGSFCEFVKTLVYQCQYSLLYDGFPMDDLISLLIGLSDSQVRAFRHTSTLAAMKLMTSLVKVALQLSLHKDNNQRQYEAERNKGPEQRAPERLESLLEKRKEFQENQEDIEGMMNAIFRGVFVHRYRDILPEIRAICIEEIGYWMQSYSTSFLNDSYLKYIGWTLHDKHKEVRLKCVKALAGLYSNQELSLRMELFTNRFKDRMVSMVMDRECEVAVEAIRLLTLILKNMEGVLTSADCEKIYSIVYISNRAMASSAGEFVYWKIFHPECGAKAVSDRERRRSPQAQKTFIYLLLAFFMESEHHNHAAYLVDSLWDCAGSYLKDWESLTNLLLQKDQNLGDMQERMLIEILVSSARQAAEGHPPVGRITGKKSLTAKERKLQAYDKMKLAEHLIPLLPQLLAKFSADAENVAPLLQLLSYFDLSIYCTQRLEKHLELLLQQLQEVVVKHVEPEVLEAAAHALYLLCKPEFTFFSRVDFARSQLVDFLTDRFQQELDDLMQSSFLDEDEVYSLTATLKRLSAFYNAHDLTRWEISEPCSRLLRKAVDTGEVPHQVILPALTLVYFSILWTVTHISESTSHKQLMSLKKRMVAFCELCQSCLSDVDPEIQEQAFVLLSDLLLIFSPQMIVGGRDFLRPLVFFPEATLQSELASFLMDHVFLQPGELGNGQSQEDHVQIELLHQRRRLLAGFCKLLLYGVLELDAASDVFKHYNKFYEDYGDIIKETLTRARQIDRCQCSRILLLSLKQLYTELIQEQGPQGLTELPAFIEMRDLARRFALSFGPQQLHNRDLVVMLHKEGIKFSLSELPPAGSSHEPPNLAFLELLSEFSPRLFHQDKRLLLSYLEKCLQRVSKAPNHPWGPVTTYCHSLHPLEITAEASPRGPPHSKKRCVEGPCRPQEEESSSQEESLQLNSGPTTPTLTSTAVKRKQSLRTVGKKQKGRPGPGPGPGPELICSQQLLGTQRLKMSSAPCFQIRCDPSGSGLGKQLTRLSLMEEDEEEELRLLDEEWQRGDKMLHSPSSPSEHGLDLLDTTELNMEDF
| null | null |
establishment of meiotic sister chromatid cohesion [GO:0034089]; female meiosis sister chromatid cohesion [GO:0007066]; homologous chromosome pairing at meiosis [GO:0007129]; male meiosis sister chromatid cohesion [GO:0007065]; protein localization to chromosome [GO:0034502]; sister chromatid cohesion [GO:0007062]
|
chromatin [GO:0000785]; chromosome, centromeric region [GO:0000775]; condensed nuclear chromosome [GO:0000794]; lateral element [GO:0000800]; male germ cell nucleus [GO:0001673]; meiotic cohesin complex [GO:0030893]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; synaptonemal complex [GO:0000795]; transverse filament [GO:0000802]
|
chromatin binding [GO:0003682]
|
PF21581;PF08514;
| null |
SCC3 family
|
PTM: Phosphorylated. {ECO:0000269|PubMed:22346761}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00750, ECO:0000269|PubMed:22346761}. Chromosome {ECO:0000269|PubMed:22346761}. Chromosome, centromere {ECO:0000269|PubMed:22346761}. Note=Associates with chromatin. In prophase I stage of meiosis, it is found along the axial elements of synaptonemal complexes. In late-pachytene-diplotene, the bulk of protein dissociates from the chromosome arms probably because of phosphorylation by PLK1, except at centromeres, where cohesin complexes remain. It however remains chromatin associated at the centromeres up to metaphase I. During anaphase I, it probably dissociates from centromeres, allowing chromosomes segregation.
| null | null | null | null | null |
FUNCTION: Meiosis specific component of cohesin complex. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The meiosis-specific cohesin complex probably replaces mitosis specific cohesin complex when it dissociates from chromatin during prophase I. {ECO:0000269|PubMed:11483963, ECO:0000269|PubMed:24597867}.
|
Mus musculus (Mouse)
|
O70577
|
S22A2_MOUSE
|
MPTVDDILEHIGEFHLFQKQTFFLLALLSGAFTPIYVGIVFLGFTPNHHCRSPGVAELSQRCGWSPAEELNYTVPGLGSAGEVSFLSQCMRYEVDWNQSTLDCVDPLSSLAANRSHLPLSPCEHGWVYDTPGSSIVTEFNLVCAHSWMLDLFQSLVNVGFFIGAVGIGYLADRFGRKFCLLVTILINAISGVLMAISPNYAWMLVFRFLQGLVSKAGWLIGYILITEFVGLGYRRTVGICYQIAFTVGLLILAGVAYALPNWRWLQFAVTLPNFCFLLYFWCIPESPRWLISQNKNAKAMKIIKHIAKKNGKSVPVSLQSLTADEDTGMKLNPSFLDLVRTPQIRKHTLILMYNWFTSSVLYQGLIMHMGLAGDNIYLDFFYSALVEFPAAFIIILTIDRIGRRYPWAVSNMVAGAACLASVFIPDDLQWLKITVACLGRMGITIAYEMVCLVNAELYPTYIRNLAVLVCSSMCDIGGIVTPFLVYRLTDIWLEFPLVVFAVVGLVAGGLVLLLPETKGKALPETIEDAEKMQRPRKKKEKRIYLQVKKAELS
| null | null |
acetylcholine transport [GO:0015870]; cellular detoxification [GO:1990748]; dopamine transport [GO:0015872]; dopamine uptake [GO:0090494]; epinephrine transport [GO:0048241]; export across plasma membrane [GO:0140115]; histamine transport [GO:0051608]; histamine uptake [GO:0051615]; L-arginine import across plasma membrane [GO:0097638]; monoatomic cation transport [GO:0006812]; norepinephrine transport [GO:0015874]; norepinephrine uptake [GO:0051620]; organic cation transport [GO:0015695]; positive regulation of gene expression [GO:0010628]; prostaglandin transport [GO:0015732]; putrescine transport [GO:0015847]; quaternary ammonium group transport [GO:0015697]; serotonin transport [GO:0006837]; serotonin uptake [GO:0051610]; thiamine transmembrane transport [GO:0071934]; toxin transport [GO:1901998]; xenobiotic transport [GO:0042908]; xenobiotic transport across blood-brain barrier [GO:1990962]
|
apical plasma membrane [GO:0016324]; basal plasma membrane [GO:0009925]; basolateral plasma membrane [GO:0016323]; cholinergic synapse [GO:0098981]; plasma membrane [GO:0005886]; presynaptic membrane [GO:0042734]; synaptic vesicle membrane [GO:0030672]
|
acetylcholine transmembrane transporter activity [GO:0005277]; amine transmembrane transporter activity [GO:0005275]; choline transmembrane transporter activity [GO:0015220]; efflux transmembrane transporter activity [GO:0015562]; L-arginine transmembrane transporter activity [GO:0061459]; monoamine transmembrane transporter activity [GO:0008504]; neurotransmitter transmembrane transporter activity [GO:0005326]; organic anion transmembrane transporter activity [GO:0008514]; organic cation transmembrane transporter activity [GO:0015101]; prostaglandin transmembrane transporter activity [GO:0015132]; putrescine transmembrane transporter activity [GO:0015489]; pyrimidine nucleoside transmembrane transporter activity [GO:0015214]; quaternary ammonium group transmembrane transporter activity [GO:0015651]; steroid binding [GO:0005496]; thiamine transmembrane transporter activity [GO:0015234]; toxin transmembrane transporter activity [GO:0019534]; xenobiotic transmembrane transporter activity [GO:0042910]
|
PF00083;
|
1.20.1250.20;
|
Major facilitator (TC 2.A.1) superfamily, Organic cation transporter (TC 2.A.1.19) family
|
PTM: Tyrosine phosphorylated by tyrosine-protein kinase YES1. {ECO:0000269|PubMed:26979622}.
|
SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000250|UniProtKB:Q9R0W2}; Multi-pass membrane protein {ECO:0000305}. Basal cell membrane {ECO:0000250|UniProtKB:O15244}; Multi-pass membrane protein {ECO:0000305}. Apical cell membrane {ECO:0000250|UniProtKB:O15244}; Multi-pass membrane protein {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=(R)-noradrenaline(out) = (R)-noradrenaline(in); Xref=Rhea:RHEA:73871, ChEBI:CHEBI:72587; Evidence={ECO:0000250|UniProtKB:O15244}; CATALYTIC ACTIVITY: Reaction=(R)-adrenaline(out) = (R)-adrenaline(in); Xref=Rhea:RHEA:73875, ChEBI:CHEBI:71406; Evidence={ECO:0000250|UniProtKB:Q9R0W2}; CATALYTIC ACTIVITY: Reaction=serotonin(out) = serotonin(in); Xref=Rhea:RHEA:73867, ChEBI:CHEBI:350546; Evidence={ECO:0000250|UniProtKB:O15244}; CATALYTIC ACTIVITY: Reaction=dopamine(out) = dopamine(in); Xref=Rhea:RHEA:73863, ChEBI:CHEBI:59905; Evidence={ECO:0000250|UniProtKB:O15244}; CATALYTIC ACTIVITY: Reaction=histamine(out) = histamine(in); Xref=Rhea:RHEA:73879, ChEBI:CHEBI:58432; Evidence={ECO:0000250|UniProtKB:O15244}; CATALYTIC ACTIVITY: Reaction=thiamine(in) = thiamine(out); Xref=Rhea:RHEA:34919, ChEBI:CHEBI:18385; Evidence={ECO:0000250|UniProtKB:O15244}; CATALYTIC ACTIVITY: Reaction=creatinine(in) = creatinine(out); Xref=Rhea:RHEA:74539, ChEBI:CHEBI:16737; Evidence={ECO:0000250|UniProtKB:O15244}; CATALYTIC ACTIVITY: Reaction=1-methylnicotinamide(out) = 1-methylnicotinamide(in); Xref=Rhea:RHEA:73859, ChEBI:CHEBI:16797; Evidence={ECO:0000250|UniProtKB:O15244}; CATALYTIC ACTIVITY: Reaction=guanidine(out) = guanidine(in); Xref=Rhea:RHEA:73883, ChEBI:CHEBI:30087; Evidence={ECO:0000250|UniProtKB:O15244}; CATALYTIC ACTIVITY: Reaction=choline(out) = choline(in); Xref=Rhea:RHEA:32751, ChEBI:CHEBI:15354; Evidence={ECO:0000250|UniProtKB:O15244}; CATALYTIC ACTIVITY: Reaction=agmatine(out) = agmatine(in); Xref=Rhea:RHEA:72131, ChEBI:CHEBI:58145; Evidence={ECO:0000250|UniProtKB:O15244}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72132; Evidence={ECO:0000250|UniProtKB:O15244}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:72133; Evidence={ECO:0000250|UniProtKB:O15244}; CATALYTIC ACTIVITY: Reaction=putrescine(out) = putrescine(in); Xref=Rhea:RHEA:72135, ChEBI:CHEBI:326268; Evidence={ECO:0000250|UniProtKB:O15244}; CATALYTIC ACTIVITY: Reaction=spermidine(in) = spermidine(out); Xref=Rhea:RHEA:35039, ChEBI:CHEBI:57834; Evidence={ECO:0000305|PubMed:23458604}; CATALYTIC ACTIVITY: Reaction=tyramine(in) = tyramine(out); Xref=Rhea:RHEA:74783, ChEBI:CHEBI:327995; Evidence={ECO:0000250|UniProtKB:O15244}; CATALYTIC ACTIVITY: Reaction=L-histidyl-L-proline diketopiperazine(in) = L-histidyl-L-proline diketopiperazine(out); Xref=Rhea:RHEA:74787, ChEBI:CHEBI:90039; Evidence={ECO:0000250|UniProtKB:O15244}; CATALYTIC ACTIVITY: Reaction=(R)-salsolinol(in) = (R)-salsolinol(out); Xref=Rhea:RHEA:74791, ChEBI:CHEBI:194082; Evidence={ECO:0000250|UniProtKB:O15244}; CATALYTIC ACTIVITY: Reaction=N-methyl-(R)-salsolinol(in) = N-methyl-(R)-salsolinol(out); Xref=Rhea:RHEA:74795, ChEBI:CHEBI:194083; Evidence={ECO:0000250|UniProtKB:O15244}; CATALYTIC ACTIVITY: Reaction=acetylcholine(in) = acetylcholine(out); Xref=Rhea:RHEA:74663, ChEBI:CHEBI:15355; Evidence={ECO:0000250|UniProtKB:O15244}; CATALYTIC ACTIVITY: Reaction=prostaglandin F2alpha(out) = prostaglandin F2alpha(in); Xref=Rhea:RHEA:50988, ChEBI:CHEBI:57404; Evidence={ECO:0000250|UniProtKB:O15244}; CATALYTIC ACTIVITY: Reaction=prostaglandin E2(out) = prostaglandin E2(in); Xref=Rhea:RHEA:50984, ChEBI:CHEBI:606564; Evidence={ECO:0000250|UniProtKB:O15244};
| null | null | null | null |
FUNCTION: Electrogenic voltage-dependent transporter that mediates the transport of a variety of organic cations such as endogenous bioactive amines, cationic drugs and xenobiotics (PubMed:23458604). Functions as a Na(+)-independent, bidirectional uniporter (By similarity). Cation cellular uptake or release is driven by the electrochemical potential, i.e. membrane potential and concentration gradient (By similarity). However, may also engage electroneutral cation exchange when saturating concentrations of cation substrates are reached (By similarity). Predominantly expressed at the basolateral membrane of hepatocytes and proximal tubules and involved in the uptake and disposition of cationic compounds by hepatic and renal clearance from the blood flow. Implicated in monoamine neurotransmitters uptake such as histamine, dopamine, adrenaline/epinephrine, noradrenaline/norepinephrine, serotonin and tyramine, thereby supporting a physiological role in the central nervous system by regulating interstitial concentrations of neurotransmitters. Also capable of transporting dopaminergic neuromodulators cyclo(his-pro), salsolinol and N-methyl-salsolinol, thereby involved in the maintenance of dopaminergic cell integrity in the central nervous system. Mediates the bidirectional transport of acetylcholine (ACh) at the apical membrane of ciliated cell in airway epithelium, thereby playing a role in luminal release of ACh from bronchial epithelium. Also transports guanidine and endogenous monoamines such as vitamin B1/thiamine, creatinine and N-1-methylnicotinamide (NMN). Mediates the uptake and efflux of quaternary ammonium compound choline (By similarity). Mediates the bidirectional transport of polyamine agmatine and the uptake of polyamines putrescine and spermidine (PubMed:23458604). Able to transport non-amine endogenous compounds such as prostaglandin E2 (PGE2) and prostaglandin F2-alpha (PGF2-alpha). Also involved in the uptake of xenobiotic 4-(4-(dimethylamino)styryl)-N-methylpyridinium (ASP). May contribute to regulate the transport of organic compounds in testis across the blood-testis-barrier (By similarity). {ECO:0000250|UniProtKB:O15244, ECO:0000250|UniProtKB:Q9R0W2, ECO:0000269|PubMed:23458604}.
|
Mus musculus (Mouse)
|
O70578
|
CCG1_MOUSE
|
MSQTKTAKVRVTLFFILVGGVLAMVAVVTDHWAVLSPHLEHHNETCEAAHFGLWRICTARVAVHNKDKSCEHVTPSGEKNCSYFRHFNPGESSEIFEFTTQKEYSISAAAIAIFSLGFIIVGSICAFLSFGNKRDYLLRPASMFYAFAGLCLIVSVEVMRQSVKRMIDSEDTVWIEHYYSWSFACACAAFILLFLGGLFLLLFSLPRMPQNPWESCMDAEPEH
| null | null |
calcium ion transmembrane transport [GO:0070588]; establishment of localization in cell [GO:0051649]; positive regulation of muscle contraction [GO:0045933]; regulation of calcium ion transmembrane transport via high voltage-gated calcium channel [GO:1902514]; sarcoplasmic reticulum calcium ion transport [GO:0070296]
|
L-type voltage-gated calcium channel complex [GO:1990454]; plasma membrane [GO:0005886]; sarcolemma [GO:0042383]; T-tubule [GO:0030315]
|
calcium channel regulator activity [GO:0005246]; voltage-gated calcium channel activity [GO:0005245]
|
PF13903;
|
1.20.140.150;
|
PMP-22/EMP/MP20 family, CACNG subfamily
|
PTM: N-glycosylated. {ECO:0000250|UniProtKB:P19518}.
|
SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000305|PubMed:10799530, ECO:0000305|PubMed:9504716}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P19518}.
| null | null | null | null | null |
FUNCTION: Regulatory subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents in skeletal muscle. Regulates channel inactivation kinetics. {ECO:0000269|PubMed:10799530, ECO:0000269|PubMed:12409298}.
|
Mus musculus (Mouse)
|
O70579
|
PM34_MOUSE
|
MASVLSYESLVHAVAGAVGSVTAMTVFFPLDTARLRLQVDEKRKSKTTHAVLLEIIKEEGLLAPYRGWFPVISSLCCSNFVYFYTFNSLKAVWVKGQRSSTGKDLVVGFVAGVVNVLLTTPLWVVNTRLKLQGAKFRNEDIIPTNYKGIIDAFHQIIRDEGILALWNGTFPSLLLVFNPAIQFMFYEGLKRQLLKKRMKLSSLDVFIIGAIAKAIATTVTYPMQTVQSILRFGRHRLNPENRTLGSLRNVLSLLHQRVKRFGIMGLYKGLEAKLLQTVLTAALMFLVYEKLTAATFTVMGLKSTHKH
| null | null |
ADP transport [GO:0015866]; AMP transport [GO:0080121]; coenzyme A transmembrane transport [GO:0035349]; FAD transmembrane transport [GO:0035350]; fatty acid beta-oxidation [GO:0006635]; fatty acid transport [GO:0015908]; NAD transport [GO:0043132]
|
membrane [GO:0016020]; mitochondrion [GO:0005739]; peroxisomal membrane [GO:0005778]
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ADP transmembrane transporter activity [GO:0015217]; AMP transmembrane transporter activity [GO:0080122]; antiporter activity [GO:0015297]; ATP transmembrane transporter activity [GO:0005347]; coenzyme A transmembrane transporter activity [GO:0015228]; FAD transmembrane transporter activity [GO:0015230]; FMN transmembrane transporter activity [GO:0044610]; NAD transmembrane transporter activity [GO:0051724]; protein-folding chaperone binding [GO:0051087]
|
PF00153;
|
1.50.40.10;
|
Mitochondrial carrier (TC 2.A.29) family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O43808}. Peroxisome membrane {ECO:0000250|UniProtKB:O43808}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=AMP(out) + CoA(in) = AMP(in) + CoA(out); Xref=Rhea:RHEA:73095, ChEBI:CHEBI:57287, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:O43808}; CATALYTIC ACTIVITY: Reaction=3'-dephospho-CoA(in) + AMP(out) = 3'-dephospho-CoA(out) + AMP(in); Xref=Rhea:RHEA:73099, ChEBI:CHEBI:57328, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:O43808}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA(in) + AMP(out) = acetyl-CoA(out) + AMP(in); Xref=Rhea:RHEA:73447, ChEBI:CHEBI:57288, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:O43808}; CATALYTIC ACTIVITY: Reaction=AMP(in) + NAD(+)(out) = AMP(out) + NAD(+)(in); Xref=Rhea:RHEA:65424, ChEBI:CHEBI:57540, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:O43808}; CATALYTIC ACTIVITY: Reaction=AMP(out) + FAD(in) = AMP(in) + FAD(out); Xref=Rhea:RHEA:73087, ChEBI:CHEBI:57692, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:O43808}; CATALYTIC ACTIVITY: Reaction=AMP(out) + FMN(in) = AMP(in) + FMN(out); Xref=Rhea:RHEA:73091, ChEBI:CHEBI:58210, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:O43808}; CATALYTIC ACTIVITY: Reaction=ADP(out) + AMP(in) = ADP(in) + AMP(out); Xref=Rhea:RHEA:72851, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O43808}; CATALYTIC ACTIVITY: Reaction=adenosine 3',5'-bisphosphate(in) + AMP(out) = adenosine 3',5'-bisphosphate(out) + AMP(in); Xref=Rhea:RHEA:73451, ChEBI:CHEBI:58343, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:O43808}; CATALYTIC ACTIVITY: Reaction=CoA(out) + FAD(in) = CoA(in) + FAD(out); Xref=Rhea:RHEA:73143, ChEBI:CHEBI:57287, ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:O43808}; CATALYTIC ACTIVITY: Reaction=adenosine 3',5'-bisphosphate(out) + FAD(in) = adenosine 3',5'-bisphosphate(in) + FAD(out); Xref=Rhea:RHEA:73147, ChEBI:CHEBI:57692, ChEBI:CHEBI:58343; Evidence={ECO:0000250|UniProtKB:O43808}; CATALYTIC ACTIVITY: Reaction=CoA(out) + FMN(in) = CoA(in) + FMN(out); Xref=Rhea:RHEA:73151, ChEBI:CHEBI:57287, ChEBI:CHEBI:58210; Evidence={ECO:0000250|UniProtKB:O43808}; CATALYTIC ACTIVITY: Reaction=adenosine 3',5'-bisphosphate(out) + FMN(in) = adenosine 3',5'-bisphosphate(in) + FMN(out); Xref=Rhea:RHEA:73155, ChEBI:CHEBI:58210, ChEBI:CHEBI:58343; Evidence={ECO:0000250|UniProtKB:O43808}; CATALYTIC ACTIVITY: Reaction=FAD(out) + NAD(+)(in) = FAD(in) + NAD(+)(out); Xref=Rhea:RHEA:73163, ChEBI:CHEBI:57540, ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:O43808}; CATALYTIC ACTIVITY: Reaction=FMN(out) + NAD(+)(in) = FMN(in) + NAD(+)(out); Xref=Rhea:RHEA:73159, ChEBI:CHEBI:57540, ChEBI:CHEBI:58210; Evidence={ECO:0000250|UniProtKB:O43808}; CATALYTIC ACTIVITY: Reaction=CoA(out) + NAD(+)(in) = CoA(in) + NAD(+)(out); Xref=Rhea:RHEA:73167, ChEBI:CHEBI:57287, ChEBI:CHEBI:57540; Evidence={ECO:0000250|UniProtKB:O43808}; CATALYTIC ACTIVITY: Reaction=adenosine 3',5'-bisphosphate(out) + NAD(+)(in) = adenosine 3',5'-bisphosphate(in) + NAD(+)(out); Xref=Rhea:RHEA:73171, ChEBI:CHEBI:57540, ChEBI:CHEBI:58343; Evidence={ECO:0000250|UniProtKB:O43808}; CATALYTIC ACTIVITY: Reaction=ADP(in) + FMN(out) = ADP(out) + FMN(in); Xref=Rhea:RHEA:73175, ChEBI:CHEBI:58210, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O43808}; CATALYTIC ACTIVITY: Reaction=ADP(in) + FAD(out) = ADP(out) + FAD(in); Xref=Rhea:RHEA:73183, ChEBI:CHEBI:57692, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O43808}; CATALYTIC ACTIVITY: Reaction=ADP(out) + CoA(in) = ADP(in) + CoA(out); Xref=Rhea:RHEA:72839, ChEBI:CHEBI:57287, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O43808}; CATALYTIC ACTIVITY: Reaction=adenosine 3',5'-bisphosphate(in) + ADP(out) = adenosine 3',5'-bisphosphate(out) + ADP(in); Xref=Rhea:RHEA:72847, ChEBI:CHEBI:58343, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O43808};
| null | null | null | null |
FUNCTION: Peroxisomal transporter for multiple cofactors like coenzyme A (CoA), flavin adenine dinucleotide (FAD), flavin mononucleotide (FMN) and nucleotide adenosine monophosphate (AMP), and to a lesser extent for nicotinamide adenine dinucleotide (NAD(+)), adenosine diphosphate (ADP) and adenosine 3',5'-diphosphate (PAP). May catalyze the transport of free CoA, FAD and NAD(+) from the cytosol into the peroxisomal matrix by a counter-exchange mechanism. {ECO:0000250|UniProtKB:O43808}.
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Mus musculus (Mouse)
|
O70582
|
LX12B_MOUSE
|
MATYKVKVATGTDFFSGTLDSISLTIVGTQGESHKQRLNHFGRDFATGAVDDYTVQCQQDLGELIIIRLHKEPHSFLAKDPWYCNYVQICAPDCRVYHFPAYQWMDGYETLALREATGKITADDTLPILLEHRQEEIRAKKDFYHWRVFVPGLPNYVDIPSYHPPPRRCRNPNRPEWDGYIPGFPILINIKATRFLNSNLRFSFVKTASFFYRLGPMALAFKLRGLVDRKRSWKRLKDIKNIFPATKSVVSEYVAEHWTEDSFFGYQYLNGINPGLIRRCTQIPDKFPVTDEMVAPFLGEGTCLQAELERGNIYLADYRILDGIPTVELNGQQQHHCAPMCLLHFGPDGNMMPIAIQLSQTPGPDCPIFLPNDSEWDWLLAKTWVRYAEFYSHEAVAHLLESHLIGEAFCLALLRNLPMCHPLYKLLIPHTRYNVQINSIGRALLLNKGGLSARAMSLGLEGFAQVMVRGLSELTYKSLCIPNDFVERGVQDLPGYYFRDDSLAVWYAMERYVTEIITYYYPNDAAVEGDPELQCWVQEIFKECLLGRESSGFPTCLRTIPELIEYVTMVMYTCSARHAAVNSGQLEYTSWMPNFPSSMRNPPMQTKGLTTLQTYMDTLPDVKTTCIVLLVLWTLCREPDDRRPLGHFPDIHFVEEGPRRSIEAFRQNLNQISHNIRQRNKCLTLPYYYLDPVLIENSISI
|
1.13.11.-
|
COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000255|PROSITE-ProRule:PRU00726}; Note=Binds 1 Fe cation per subunit. {ECO:0000255|PROSITE-ProRule:PRU00726};
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arachidonic acid metabolic process [GO:0019369]; ceramide biosynthetic process [GO:0046513]; establishment of skin barrier [GO:0061436]; hepoxilin biosynthetic process [GO:0051122]; linoleic acid metabolic process [GO:0043651]; lipid oxidation [GO:0034440]; lipoxygenase pathway [GO:0019372]; positive regulation of gene expression [GO:0010628]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of mucus secretion [GO:0070257]; protein lipidation [GO:0006497]; sphingolipid metabolic process [GO:0006665]
|
cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; perinuclear region of cytoplasm [GO:0048471]
|
arachidonate 12(R)-lipoxygenase activity [GO:0106237]; arachidonate 12(S)-lipoxygenase activity [GO:0004052]; arachidonate 8(R)-lipoxygenase activity [GO:0047677]; catalytic activity [GO:0003824]; iron ion binding [GO:0005506]; linoleate 9S-lipoxygenase activity [GO:1990136]
|
PF00305;PF01477;
|
3.10.450.60;2.60.60.20;
|
Lipoxygenase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00726}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:9837935}.
|
CATALYTIC ACTIVITY: Reaction=1-O-methyl-(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = 1-O-methyl (5Z,8Z,10E,12R,14Z)-hydroperoxyiecosatetraenoate; Xref=Rhea:RHEA:41311, ChEBI:CHEBI:15379, ChEBI:CHEBI:78033, ChEBI:CHEBI:78034; Evidence={ECO:0000269|PubMed:10100631, ECO:0000269|PubMed:11256953, ECO:0000269|PubMed:16129665}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41312; Evidence={ECO:0000269|PubMed:10100631, ECO:0000269|PubMed:11256953}; CATALYTIC ACTIVITY: Reaction=1-O-methyl-(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = 1-O-methyl-8-hydroperoxy-(5Z,9E,11Z,14Z)-eicosatetraenoate; Xref=Rhea:RHEA:43480, ChEBI:CHEBI:15379, ChEBI:CHEBI:78033, ChEBI:CHEBI:83344; Evidence={ECO:0000269|PubMed:10100631}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43481; Evidence={ECO:0000269|PubMed:10100631, ECO:0000269|PubMed:11256953}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = (12R)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate; Xref=Rhea:RHEA:41336, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:75230; Evidence={ECO:0000250|UniProtKB:O75342}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41337; Evidence={ECO:0000250|UniProtKB:O75342}; CATALYTIC ACTIVITY: Reaction=N-[omega-(9Z,12Z)-octadecadienoyloxy]acyl-beta-D-glucosyl-(1<->1)-octadecasphing-4E-enine + O2 = N-[omega-(9R)-hydroperoxy-(10E,12Z)-octadecadienoyloxy]acyl-beta-D-glucosyl-(1<->1)-octadecasphing-4E-enine; Xref=Rhea:RHEA:40495, ChEBI:CHEBI:15379, ChEBI:CHEBI:134621, ChEBI:CHEBI:134624; Evidence={ECO:0000250|UniProtKB:O75342}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40496; Evidence={ECO:0000250|UniProtKB:O75342}; CATALYTIC ACTIVITY: Reaction=N-[omega-(9Z,12Z)-octadecadienoyloxy]-acylsphin-4-enine + O2 = N-acyl (9R)-hydroperoxy-(10E,12Z)-octadecadienoate octadecasphing-4E-enine; Xref=Rhea:RHEA:41239, ChEBI:CHEBI:15379, ChEBI:CHEBI:77888, ChEBI:CHEBI:77889; Evidence={ECO:0000250|UniProtKB:O75342}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41240; Evidence={ECO:0000250|UniProtKB:O75342}; CATALYTIC ACTIVITY: Reaction=(6Z,9Z,12Z)-octadecatrienoate + O2 = 10-hydroperoxy-(6Z,8E,12Z)-octadecatrienoate; Xref=Rhea:RHEA:43476, ChEBI:CHEBI:15379, ChEBI:CHEBI:32391, ChEBI:CHEBI:83342; Evidence={ECO:0000250|UniProtKB:O75342}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43477; Evidence={ECO:0000250|UniProtKB:O75342}; CATALYTIC ACTIVITY: Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 = 14-hydroperoxy-(4Z,7Z,10Z,12E,16Z,19Z)-docosahexaenoate; Xref=Rhea:RHEA:43472, ChEBI:CHEBI:15379, ChEBI:CHEBI:77016, ChEBI:CHEBI:83336; Evidence={ECO:0000250|UniProtKB:O75342}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43473; Evidence={ECO:0000250|UniProtKB:O75342}; CATALYTIC ACTIVITY: Reaction=(8Z,11Z,14Z)-eicosatrienoate + O2 = (8Z,10E,14Z)-12-hydroperoxyeicosatrienoate; Xref=Rhea:RHEA:43468, ChEBI:CHEBI:15379, ChEBI:CHEBI:71589, ChEBI:CHEBI:83334; Evidence={ECO:0000250|UniProtKB:O75342}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43469; Evidence={ECO:0000250|UniProtKB:O75342}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 = (5Z,7Z,8Z,10E,14Z,17Z)-12-hydroperoxyeicosapentaenoate; Xref=Rhea:RHEA:41344, ChEBI:CHEBI:15379, ChEBI:CHEBI:58562, ChEBI:CHEBI:78078; Evidence={ECO:0000250|UniProtKB:O75342}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41345; Evidence={ECO:0000250|UniProtKB:O75342}; CATALYTIC ACTIVITY: Reaction=(6Z,9Z,12Z)-octadecatrienoate + O2 = 10R-hydroperoxy-(6Z,8E,12Z)-octadecatrienoate; Xref=Rhea:RHEA:41340, ChEBI:CHEBI:15379, ChEBI:CHEBI:32391, ChEBI:CHEBI:78070; Evidence={ECO:0000250|UniProtKB:O75342}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41341; Evidence={ECO:0000250|UniProtKB:O75342}; CATALYTIC ACTIVITY: Reaction=1-O-methyl-(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = 1-O-methyl-(8R)-hydroperoxy-(5Z,9E,11Z,14Z)-eicosatrienoate; Xref=Rhea:RHEA:61868, ChEBI:CHEBI:15379, ChEBI:CHEBI:78033, ChEBI:CHEBI:78180; Evidence={ECO:0000269|PubMed:11256953, ECO:0000269|PubMed:16129665}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61869; Evidence={ECO:0000305|PubMed:16129665}; CATALYTIC ACTIVITY: Reaction=1-O-methyl-(9Z,12Z)-octadecadienoate + O2 = 1-O-methyl-(9R)-hydroperoxy-(10E,12Z)-octadecadienoate; Xref=Rhea:RHEA:61872, ChEBI:CHEBI:15379, ChEBI:CHEBI:69080, ChEBI:CHEBI:145036; Evidence={ECO:0000269|PubMed:11256953, ECO:0000269|PubMed:16129665}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61873; Evidence={ECO:0000305|PubMed:16129665}; CATALYTIC ACTIVITY: Reaction=1-O-methyl-20-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = 1-O-methyl-8-hydroperoxy-20-hydroxy-(5Z,9E,11Z,14Z)-eicosatetraenoate; Xref=Rhea:RHEA:61876, ChEBI:CHEBI:15379, ChEBI:CHEBI:145032, ChEBI:CHEBI:145033; Evidence={ECO:0000269|PubMed:16129665}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61877; Evidence={ECO:0000305|PubMed:16129665}; CATALYTIC ACTIVITY: Reaction=1-O-methyl-20-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = 1-O-methyl-12-hydroperoxy-20-hydroxy-(5Z,8Z,10E,14Z)-eicosatetraenoate; Xref=Rhea:RHEA:61880, ChEBI:CHEBI:15379, ChEBI:CHEBI:145032, ChEBI:CHEBI:145034; Evidence={ECO:0000269|PubMed:16129665}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61881; Evidence={ECO:0000305|PubMed:16129665}; CATALYTIC ACTIVITY: Reaction=1-O-methyl-20-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = 1-O-methyl-9-hydroperoxy-20-hydroxy-(5Z,7E,11Z,14Z)-eicosatetraenoate; Xref=Rhea:RHEA:61884, ChEBI:CHEBI:15379, ChEBI:CHEBI:145032, ChEBI:CHEBI:145035; Evidence={ECO:0000269|PubMed:16129665}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61885; Evidence={ECO:0000305|PubMed:16129665}; CATALYTIC ACTIVITY: Reaction=1-O-methyl-(9Z,12Z)-octadecadienoate + O2 = 1-O-methyl-(13S)-hydroperoxy-(9Z,11E)-octadecadienoate; Xref=Rhea:RHEA:41756, ChEBI:CHEBI:15379, ChEBI:CHEBI:69080, ChEBI:CHEBI:78040; Evidence={ECO:0000269|PubMed:16129665}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41757; Evidence={ECO:0000305|PubMed:16129665};
| null |
PATHWAY: Lipid metabolism; hydroperoxy eicosatetraenoic acid biosynthesis.; PATHWAY: Lipid metabolism; sphingolipid metabolism.
| null | null |
FUNCTION: Catalyzes the regio and stereo-specific incorporation of a single molecule of dioxygen into free and esterified polyunsaturated fatty acids generating lipid hydroperoxides that can be further reduced to the corresponding hydroxy species (PubMed:16129665). Does not convert arachidonic acid to (12R)-hydroperoxyeicosatetraenoic acid/(12R)-HPETE (PubMed:10100631, PubMed:11256953). In the skin, acts upstream of ALOXE3 on the lineolate moiety of esterified omega-hydroxyacyl-sphingosine (EOS) ceramides to produce an epoxy-ketone derivative, a crucial step in the conjugation of omega-hydroxyceramide to membrane proteins. Therefore plays a crucial role in the synthesis of corneocytes lipid envelope and the establishment of the skin barrier to water loss (PubMed:17403930, PubMed:17429434, PubMed:21558561). May also play a role in the regulation of the expression of airway mucins (By similarity). {ECO:0000250|UniProtKB:O75342, ECO:0000269|PubMed:10100631, ECO:0000269|PubMed:11256953, ECO:0000269|PubMed:16129665, ECO:0000269|PubMed:17403930, ECO:0000269|PubMed:17429434, ECO:0000269|PubMed:21558561}.
|
Mus musculus (Mouse)
|
O70583
|
TRI18_MOUSE
|
METLESELTCPICLELFEDPLLLPCAHSLCFNCAHRILVSHCATNEPVESINAFQCPTCRHVITLSQRGLDGLKRNVTLQNIIDRFQKASVSGPNSPSETRRERAFDANTMSSAEKVLCQFCDQDPAQDAVKTCVTCEVSYCDECLKATHPNKKPFTGHRLIEPIPDSHIRGLMCLEHEDEKVNMYCVTDDQLICALCKLVGRHRDHQVAALSERYDKLKQNLESNLTNLIKRNTELETLLAKLIQTCQHVEVNASRQEAKLTEECDLLIEIIQQRRQIIGTKIKEGKVIRLRKLAQQIANCKQCLERSASLISQAEHSLKENDHARFLQTAKNITERVSMATASSQVLIPEINLNDTFDTFALDFSREKKLLECLDYLTAPNPPAIREELCTASYDTITVHWTSEDEFSVVSYELQYTIFTGQANVVNVACDGTCLLGSAGLCNSADSWMIVPNIKQNHYTVHGLQSGTKYIFTVKAINQAGSRSSEPGKLKTNSQPFRLDPKSAHRKLKVSHDNLTVERDESSSKKSHAPERFAGQGSYGVAGNVFIDSGRHYWEVVTSGSTWYAIGLAYRSAPKHEWIGKNAASWALCRCHNHWAVRHDGKETPIAPAPHLRRVGVLLDYDNGSIAFYDALSSVHLHTFHAALAQPVCPTFTVWNKCLTIVTGLPIPDHLDCTEQRP
|
2.3.2.27
| null |
negative regulation of microtubule depolymerization [GO:0007026]; positive regulation of stress-activated MAPK cascade [GO:0032874]; protein localization to microtubule [GO:0035372]; regulation of microtubule cytoskeleton organization [GO:0070507]
|
centriolar satellite [GO:0034451]; cytoplasm [GO:0005737]; cytoplasmic microtubule [GO:0005881]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; microtubule cytoskeleton [GO:0015630]
|
microtubule binding [GO:0008017]; phosphoprotein binding [GO:0051219]; protein homodimerization activity [GO:0042803]; transferase activity [GO:0016740]; ubiquitin protein ligase binding [GO:0031625]; zinc ion binding [GO:0008270]
|
PF18568;PF00041;PF00622;PF00643;PF13445;
|
2.60.120.920;4.10.830.40;3.30.160.60;2.60.40.10;3.30.40.10;
|
TRIM/RBCC family
|
PTM: Phosphorylated. {ECO:0000269|PubMed:11371618}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O15344}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O15344}. Note=Microtubule-associated. {ECO:0000250|UniProtKB:O15344}.
|
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=2.3.2.27;
| null | null | null | null |
FUNCTION: Has E3 ubiquitin ligase activity towards IGBP1, promoting its monoubiquitination, which results in deprotection of the catalytic subunit of protein phosphatase PP2A, and its subsequent degradation by polyubiquitination. {ECO:0000250|UniProtKB:O15344}.
|
Mus musculus (Mouse)
|
O70584
|
NKX28_MOUSE
|
MATSGRLGFTVRSLLNLPEQDAKPRVRREQQTCVPQTAAWLESECSHYLSSDESGLETSPADSSQLASLRRESPGSDPEKRRKRRVLFSKAQTLELERRFRQQRYLSAPEREQLARLLRLTPTQVKIWFQNHRYKLKRGRAPGITEPSDMAASSDLHAAPGLLRRVVVPVLVHDRPPSNNGRGEGTSAVPQDKCSARLATACPVPGYTAFGPGSALGLFPAYQHLAPPALVSWNW
| null | null |
axonogenesis [GO:0007409]; cell differentiation [GO:0030154]; epithelial cell proliferation [GO:0050673]; lung development [GO:0030324]; negative regulation of epithelial cell proliferation [GO:0050680]; regulation of transcription by RNA polymerase II [GO:0006357]; respiratory tube development [GO:0030323]; transcription by RNA polymerase II [GO:0006366]
|
nucleus [GO:0005634]
|
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; 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]
|
PF00046;
|
1.10.10.60;
|
NK-2 homeobox family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Possible role in the specification of a distinct subset of neurons.
|
Mus musculus (Mouse)
|
O70585
|
DTNB_MOUSE
|
MIEEGGNKRKTMAEKRQLFIEMRAQNFDVIRLSTYRTACKLRFVQKRCNLHLVDIWNMIEAFRDNGLNTLDHSTEISVSRLETVISSIYYQLNKRLPSTHQISVEQSISLLLNFMVAAYDSEGRGKLTVFSVKAMLATMCGGKMLDKLRYIFSQMSDSNGLMMFGKLDQFLKEALKLPTAVFEGPSFGYTEHAVRTCFPQQKKIMLNMFLDTMMADPPPQCLVWLPLMHRLAHVENVFHPVECSYCHCESMMGFRYRCQQCHNYQLCQNCFWRGHASGAHSNQHQMKEHSSWKSPAKKLSHAISKSLGCVPSREPPHPVFPEQPEKPLDLAHLVPPRPLTNMNDTVVSHMSSGVPTPTKRLQYSQDMPNLLADEHALIASYVARLQHCTRVLDSPSRLDEEHRLIARYAARLAAEAGNMTRPPTDASFNFDANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPMLLAELRLLRQRKDELEQRMSALQESRRELMVQLEGLMKLLKAQATGSPHTSPTHGGGRPMPMPVRSTSAGSTPTHGPQDSLSGVGGDVQEAFAQGTRRNLRNDLLVAADSITNTMSSLVKELHSGAEAEEQAGTEKTREGLPPRGTFLSVFLLHTWTKLAGCQTHSTSRERSQAYGKWGGTA
| null | null |
synaptic signaling [GO:0099536]
|
basal plasma membrane [GO:0009925]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; inhibitory synapse [GO:0060077]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; synapse [GO:0045202]
|
DNA binding [GO:0003677]; phosphatase binding [GO:0019902]; zinc ion binding [GO:0008270]
|
PF09068;PF09069;PF00569;
|
3.30.60.90;1.10.238.10;
|
Dystrophin family, Dystrobrevin subfamily
|
PTM: Phosphorylated by PKA (PubMed:17610895). Phosphorylation at Thr-11 alters the interaction with KIF5A (PubMed:22978324). {ECO:0000269|PubMed:17610895, ECO:0000269|PubMed:22978324}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20530487}. Postsynaptic density {ECO:0000250|UniProtKB:P84060}. Cell projection, dendrite {ECO:0000269|PubMed:11585924, ECO:0000269|PubMed:16540561}. Basal cell membrane {ECO:0000269|PubMed:10893187}. Postsynapse {ECO:0000269|PubMed:16540561}. Nucleus {ECO:0000269|PubMed:20530487}. Note=Localized at inhibitory synapses on the dendrites of cerebellar Purkinje cells. {ECO:0000269|PubMed:16540561}.
| null | null | null | null | null |
FUNCTION: Scaffolding protein that assembles DMD and SNTA1 molecules to the basal membrane of kidney cells and liver sinusoids (PubMed:11585924). May function as a repressor of the SYN1 promoter through the binding of repressor element-1 (RE-1), in turn regulates SYN1 expression and may be involved in cell proliferation regulation during the early phase of neural differentiation (PubMed:20530487). May be required for proper maturation and function of a subset of inhibitory synapses (PubMed:16540561). {ECO:0000269|PubMed:11585924, ECO:0000269|PubMed:16540561, ECO:0000269|PubMed:20530487}.
|
Mus musculus (Mouse)
|
O70589
|
CSKP_MOUSE
|
MADDDVLFEDVYELCEVIGKGPFSVVRRCINRETGQQFAVKIVDVAKFTSSPGLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGADLCFEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSAPVKLGGFGVAIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLFEGIIKGKYKMNPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWLKERDRYAYKIHLPETVEQLRKFNARRKLKGAVLAAVSSHKFNSFYGDPPEELPDFSEDPTSSGLLAAERAVSQVLDSLEEIHALTDCSEKDLDFLHSVFQDQHLHTLLDLYDKINTKSSPQIRNPPSDAVQRAKEVLEEISCYPENNDAKELKRILTQPHFMALLQTHDVVAHEVYSDEALRVTPPPTSPYLNGDSPESANGDMDMENVTRVRLVQFQKNTDEPMGITLKMNELNHCIVARIMHGGMIHRQGTLHVGDEIREINGISVANQTVEQLQKMLREMRGSITFKIVPSYRTQSSSCERDSPSTSRQSPANGHSSTNNSVSDLPSTTQPKGRQIYVRAQFEYDPAKDDLIPCKEAGIRFRVGDIIQIISKDDHNWWQGKLENSKNGTAGLIPSPELQEWRVACIAMEKTKQEQQASCTWFGKKKKQYKDKYLAKHNAVFDQLDLVTYEEVVKLPAFKRKTLVLLGAHGVGRRHIKNTLITKHPDRFAYPIPHTTRPPKKDEENGKNYYFVSHDQMMQDISNNEYLEYGSHEDAMYGTKLETIRKIHEQGLIAILDVEPQALKVLRTAEFAPFVVFIAAPTITPGLNEDESLQRLQKESDVLQRTYAHYFDLTIINNEIDETIRHLEEAVELVCTAPQWVPVSWVY
|
2.7.11.1
|
COFACTOR: Note=Unlike other protein kinases, does not require a divalent cation such as magnesium for catalytic activity. {ECO:0000250};
|
calcium ion import [GO:0070509]; establishment of localization in cell [GO:0051649]; negative regulation of cell-matrix adhesion [GO:0001953]; negative regulation of cellular response to growth factor stimulus [GO:0090288]; negative regulation of keratinocyte proliferation [GO:0010839]; negative regulation of wound healing [GO:0061045]; phosphorylation [GO:0016310]; positive regulation of calcium ion import [GO:0090280]; positive regulation of dendritic spine morphogenesis [GO:0061003]; positive regulation of insulin secretion [GO:0032024]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein localization to plasma membrane [GO:0072659]; regulation of neurotransmitter secretion [GO:0046928]; regulation of synaptic vesicle exocytosis [GO:2000300]; regulation of transcription by RNA polymerase II [GO:0006357]
|
apical dendrite [GO:0097440]; basement membrane [GO:0005604]; basolateral plasma membrane [GO:0016323]; cell-cell junction [GO:0005911]; ciliary membrane [GO:0060170]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; nuclear lamina [GO:0005652]; nuclear matrix [GO:0016363]; nucleolus [GO:0005730]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; podocyte foot [GO:0098846]; presynaptic membrane [GO:0042734]; protein-containing complex [GO:0032991]; Schaffer collateral - CA1 synapse [GO:0098685]; synapse [GO:0045202]; synaptic membrane [GO:0097060]; vesicle [GO:0031982]
|
ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; neurexin family protein binding [GO:0042043]; PDZ domain binding [GO:0030165]; protein kinase C binding [GO:0005080]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein-containing complex binding [GO:0044877]; signaling receptor binding [GO:0005102]
|
PF00625;PF02828;PF00595;PF00069;PF07653;
|
2.30.42.10;6.10.140.620;3.30.63.10;1.10.287.650;3.40.50.300;2.30.30.40;1.10.510.10;
|
Protein kinase superfamily, CAMK Ser/Thr protein kinase family, CaMK subfamily; MAGUK family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q62915}. Cytoplasm {ECO:0000250|UniProtKB:Q62915}. Cell membrane {ECO:0000250|UniProtKB:Q62915}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q62915}.
|
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; Evidence={ECO:0000250|UniProtKB:O14936}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; Evidence={ECO:0000250|UniProtKB:O14936}; 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: Multidomain scaffolding Mg(2+)-independent protein kinase that catalyzes the phosphotransfer from ATP to proteins such as NRXN1, and plays a role in synaptic transmembrane protein anchoring and ion channel trafficking (By similarity). Contributes to neural development and regulation of gene expression via interaction with the transcription factor TBR1. Binds to cell-surface proteins, including amyloid precursor protein, neurexins, and syndecans. May mediate a link between the extracellular matrix and the actin cytoskeleton via its interaction with syndecan and with the actin/spectrin-binding protein 4.1. Component of the LIN-10-LIN-2-LIN-7 complex, which associates with the motor protein KIF17 to transport vesicles containing N-methyl-D-aspartate (NMDA) receptor subunit NR2B along microtubules (PubMed:10846156). {ECO:0000250|UniProtKB:O14936, ECO:0000269|PubMed:10749215, ECO:0000269|PubMed:10846156}.
|
Mus musculus (Mouse)
|
O70593
|
SGTA_RAT
|
MDNRKRLAYAIIQFLHGQLRHGGLSSDAQESLEVAIQCLETAFGVTLEDSDLALPQTLPEIFEAATASKEMPQDPRGPDRTPPSEEDSAEAERLKTEGNEQMKLENFEAAVHLYGKAIELNPANAVYFCNRAAAYSKLGNYVGAVQDCERAIGIDPGYSKAYGRMGLALSSLNKHAEAVAYYKKALELDPDNDTYKSNLKIAELKLREAPSPTGGVGSLDIAGLLNNPHFITMASSLMNSPQLQQLMSGMISGGHNPLGTPGSSPQHSDLASLIQAGQQFAQQMQQQNPEFVEQIRSQVVRSRTPSASHEEQQE
| null | null |
chaperone-mediated protein folding [GO:0061077]; ERAD pathway [GO:0036503]; negative regulation of ERAD pathway [GO:1904293]; negative regulation of ubiquitin-dependent protein catabolic process [GO:2000059]; positive regulation of ERAD pathway [GO:1904294]; positive regulation of ubiquitin-dependent protein catabolic process [GO:2000060]; post-translational protein targeting to endoplasmic reticulum membrane [GO:0006620]; protein heterooligomerization [GO:0051291]; protein homooligomerization [GO:0051260]; tail-anchored membrane protein insertion into ER membrane [GO:0071816]
|
cytosol [GO:0005829]; extrinsic component of synaptic vesicle membrane [GO:0098850]; membrane [GO:0016020]; nucleus [GO:0005634]; presynapse [GO:0098793]; TRC complex [GO:0072380]
|
BAT3 complex binding [GO:1904288]; identical protein binding [GO:0042802]; molecular adaptor activity [GO:0060090]; protein self-association [GO:0043621]
|
PF16546;PF00515;PF13181;
|
1.20.5.420;1.25.40.10;
|
SGT family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O43765}. Nucleus {ECO:0000250|UniProtKB:O43765}. Note=Co-localizes with HSP90AB1 in the cytoplasm. Increased nuclear accumulation seen during cell apoptosis. {ECO:0000250|UniProtKB:O43765}.
| null | null | null | null | null |
FUNCTION: Co-chaperone that binds misfolded and hydrophobic patches-containing client proteins in the cytosol. Mediates their targeting to the endoplasmic reticulum but also regulates their sorting to the proteasome when targeting fails. Functions in tail-anchored/type II transmembrane proteins membrane insertion constituting with ASNA1 and the BAG6 complex a targeting module. Functions upstream of the BAG6 complex and ASNA1, binding more rapidly the transmembrane domain of newly synthesized proteins. It is also involved in the regulation of the endoplasmic reticulum-associated misfolded protein catabolic process via its interaction with BAG6: collaborates with the BAG6 complex to maintain hydrophobic substrates in non-ubiquitinated states. Competes with RNF126 for interaction with BAG6, preventing the ubiquitination of client proteins associated with the BAG6 complex (By similarity). Binds directly to HSC70 and HSP70 and regulates their ATPase activity (PubMed:12878599). {ECO:0000250|UniProtKB:O43765, ECO:0000269|PubMed:12878599}.
|
Rattus norvegicus (Rat)
|
O70594
|
S22A5_RAT
|
MRDYDEVTAFLGEWGPFQRLIFFLLSASIIPNGFNGMSIVFLAGTPEHRCLVPHTVNLSSAWRNHSIPLETKDGRQVPQSCRRYRLATIANFSALGLEPGRDVDLEQLEQENCLDGWEYNKDVFLSTIVTEWDLVCKDDWKAPLTTSLFFVGVLMGSFISGQLSDRFGRKNVLFLTMGMQTGFSFLQLFSVNFEMFTVLFVLVGMGQISNYVAAFVLGTEILSKSIRIIFATLGVCIFYAFGFMVLPLFAYFIRDWRMLLLALTVPGVLCGALWWFIPESPRWLISQGRVKEAEVIIRKAAKFNGIVAPSTIFDPSELQDLNSKKPQSHHIYDLVRTRNIRIITIMSIILWLTISVGYFGLSLDTPNLHGDIYVNCFLLAAVEVPAYVLAWLLLQHLPRRYSISAALFLGGSVLLFIQLVPSELFYLSTALVMVGKFGITSAYSMVYVYTAELYPTVVRNMGVGVSSTASRLGSILSPYFVYLGAYDRFLPYILMGSLTILTAILTLFFPESFGAPLPDTIDQMLRVKGIKQWQIQSQTRTQKDGGESPTVLKSTAF
| null | null |
(R)-carnitine transmembrane transport [GO:1902270]; (R)-carnitine transport [GO:1900749]; adult heart development [GO:0007512]; carnitine metabolic process [GO:0009437]; carnitine transport [GO:0015879]; establishment of localization in cell [GO:0051649]; locomotory behavior [GO:0007626]; mitochondrion organization [GO:0007005]; positive regulation of intestinal epithelial structure maintenance [GO:0060731]; quaternary ammonium group transport [GO:0015697]; reproductive structure development [GO:0048608]; response to tumor necrosis factor [GO:0034612]; response to type II interferon [GO:0034341]; sodium ion transport [GO:0006814]; sodium-dependent organic cation transport [GO:0070715]; transport across blood-brain barrier [GO:0150104]
|
apical plasma membrane [GO:0016324]; basal plasma membrane [GO:0009925]; basolateral plasma membrane [GO:0016323]; brush border membrane [GO:0031526]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; plasma membrane [GO:0005886]
|
(R)-carnitine transmembrane transporter activity [GO:1901235]; amino-acid betaine transmembrane transporter activity [GO:0015199]; ATP binding [GO:0005524]; carnitine transmembrane transporter activity [GO:0015226]; PDZ domain binding [GO:0030165]; quaternary ammonium group transmembrane transporter activity [GO:0015651]; symporter activity [GO:0015293]
|
PF00083;
|
1.20.1250.20;
|
Major facilitator (TC 2.A.1) superfamily, Organic cation transporter (TC 2.A.1.19) family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O76082}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O76082}. Apical cell membrane {ECO:0000250|UniProtKB:O76082}; Multi-pass membrane protein {ECO:0000255}. Basal cell membrane {ECO:0000250|UniProtKB:O76082}; Multi-pass membrane protein {ECO:0000255}.
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CATALYTIC ACTIVITY: Reaction=(R)-carnitine(out) + Na(+)(out) = (R)-carnitine(in) + Na(+)(in); Xref=Rhea:RHEA:72091, ChEBI:CHEBI:16347, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:10454528}; CATALYTIC ACTIVITY: Reaction=Na(+)(out) + O-acetyl-(R)-carnitine(out) = Na(+)(in) + O-acetyl-(R)-carnitine(in); Xref=Rhea:RHEA:72099, ChEBI:CHEBI:29101, ChEBI:CHEBI:57589; Evidence={ECO:0000269|PubMed:10454528}; CATALYTIC ACTIVITY: Reaction=Na(+)(out) + O-propanoyl-(R)-carnitine(out) = Na(+)(in) + O-propanoyl-(R)-carnitine(in); Xref=Rhea:RHEA:72103, ChEBI:CHEBI:29101, ChEBI:CHEBI:53210; Evidence={ECO:0000269|PubMed:10454528}; CATALYTIC ACTIVITY: Reaction=glycine betaine(out) + Na(+)(out) = glycine betaine(in) + Na(+)(in); Xref=Rhea:RHEA:72115, ChEBI:CHEBI:17750, ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:O76082}; CATALYTIC ACTIVITY: Reaction=(R)-carnitine(in) + glycine betaine(out) = (R)-carnitine(out) + glycine betaine(in); Xref=Rhea:RHEA:72119, ChEBI:CHEBI:16347, ChEBI:CHEBI:17750; Evidence={ECO:0000250|UniProtKB:O76082}; CATALYTIC ACTIVITY: Reaction=Na(+)(out) + O-butanoyl-(R)-carnitine(out) = Na(+)(in) + O-butanoyl-(R)-carnitine(in); Xref=Rhea:RHEA:72123, ChEBI:CHEBI:21949, ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:O76082}; CATALYTIC ACTIVITY: Reaction=(S)-carnitine(out) + Na(+)(out) = (S)-carnitine(in) + Na(+)(in); Xref=Rhea:RHEA:72095, ChEBI:CHEBI:11060, ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:O76082}; CATALYTIC ACTIVITY: Reaction=Na(+)(out) + O-acyl-(R)-carnitine(out) = Na(+)(in) + O-acyl-(R)-carnitine(in); Xref=Rhea:RHEA:72107, ChEBI:CHEBI:29101, ChEBI:CHEBI:75659; Evidence={ECO:0000250|UniProtKB:O76082}; CATALYTIC ACTIVITY: Reaction=L-glutamyl-L-arginyl-glycyl-L-methionyl-L-threonine(out) + Na(+)(out) = L-glutamyl-L-arginyl-glycyl-L-methionyl-L-threonine(in) + Na(+)(in); Xref=Rhea:RHEA:72111, ChEBI:CHEBI:29101, ChEBI:CHEBI:191852; Evidence={ECO:0000250|UniProtKB:O76082}; CATALYTIC ACTIVITY: Reaction=N,N-dimethylglycine(out) + Na(+)(out) = N,N-dimethylglycine(in) + Na(+)(in); Xref=Rhea:RHEA:76591, ChEBI:CHEBI:29101, ChEBI:CHEBI:58251; Evidence={ECO:0000250|UniProtKB:O76082};
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BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=63 uM for tetraethylammonium (at pH 7.5) {ECO:0000269|PubMed:10454528}; KM=14.8 uM for carnitine (at pH 7.5 adn 140 mM NaCl) {ECO:0000269|PubMed:10454528};
| null | null | null |
FUNCTION: Sodium-ion dependent, high affinity carnitine transporter. Involved in the active cellular uptake of carnitine. Transports one sodium ion with one molecule of carnitine. Also transports organic cations such as tetraethylammonium (TEA) without the involvement of sodium. Also relative uptake activity ratio of carnitine to TEA is 11.3. May also contribute to regulate the transport of organic compounds in testis across the blood-testis-barrier (Probable). {ECO:0000269|PubMed:10454528, ECO:0000305|PubMed:17616214}.
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Rattus norvegicus (Rat)
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O70595
|
ABCB6_RAT
|
MVTVGNYCEAEGPAGPAWTQNGLSPCFFYTLVPSTLMTLGVLALVLVLPCRRREVPAGTEELSWAAGPRVAPYALQLSLAILQMALPLASLAGRVGTARGVRLPGYLLLASVLESLASACGLWLLVVERSQARQSLAMGVWMKFRHSLGLLLLWTVTFAAENLVLVSWNSPQWWWSRADLGQQVQFGLWVLRYMTSGGLFILGLWAPGLRPQSYTLHVNEEDQDGGRNQGRSTDPRSTWRDLGRKLRLLSGYLWPRGSPSLQLTVLLCMGLMGLDRALNVLVPIFYRDIVNLLTSKAPWSSLAWTVTTYVFLKFLQGGGTGSTGFVSNLRTFLWIRVQQFTSRGVELRLFSHLHELSLRWHLGRRTGEVLRIVDRGTSSVTGLLSYLVFNIIPTLADIIIGIIYFSMFFNAWFGLIVFLCMSLYLILTIMVTEWRAKFRRDMNTQENATRARAVDSLLNFETVKYYNAEGYELERYREAILKFQGLEWKSTASLVLLNQTQNMVIGFGLLAGSLLCAYFVSERRLQVGDFVLFGTYITQLYMPLNWFGTYYRMIQTNFIDMENMFDLLKEETEVKDVPGAGPLRFHKGRVEFENVHFSYADGRETLQDVSFTVMPGQTVALVGPSGAGKSTILRLLFRFYDISSGCIRIDGQDISQVTQISLRSHIGVVPQDTVLFNDTIANNIRYGRVTAGDSEIQAAAQAAGIHDAILSFPEGYETQVGERGLKLSGGEKQRVAIARTILKAPDIILLDEATSALDTSNERAIQASLAKVCTNRTTIVVAHRLSTVVNADQILVIKDGCIIERGRHEALLSRGGVYAEMWQLQQQGQETVPEDS
|
7.6.2.5
| null |
brain development [GO:0007420]; cellular detoxification of cadmium ion [GO:0098849]; heme metabolic process [GO:0042168]; heme transmembrane transport [GO:0035351]; heme transport [GO:0015886]; intracellular copper ion homeostasis [GO:0006878]; melanosome assembly [GO:1903232]; porphyrin-containing compound biosynthetic process [GO:0006779]; porphyrin-containing compound metabolic process [GO:0006778]; skin development [GO:0043588]; tetrapyrrole metabolic process [GO:0033013]; transmembrane transport [GO:0055085]
|
cytosol [GO:0005829]; early endosome membrane [GO:0031901]; endolysosome membrane [GO:0036020]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; melanosome membrane [GO:0033162]; mitochondrial envelope [GO:0005740]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; multivesicular body membrane [GO:0032585]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; vacuolar membrane [GO:0005774]
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ABC-type heme transporter activity [GO:0015439]; ABC-type transporter activity [GO:0140359]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; efflux transmembrane transporter activity [GO:0015562]; heme binding [GO:0020037]; tetrapyrrole binding [GO:0046906]
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PF00664;PF00005;PF16185;
|
1.20.1560.10;3.40.50.300;
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ABC transporter superfamily, ABCB family, Heavy Metal importer (TC 3.A.1.210) subfamily
|
PTM: N-glycosylated. {ECO:0000269|PubMed:18160489}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9NP58}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q9NP58}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9NP58}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9NP58}; Multi-pass membrane protein {ECO:0000255}. Endosome membrane {ECO:0000250|UniProtKB:Q9NP58}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:18160489}. Late endosome membrane {ECO:0000269|PubMed:18160489}. Early endosome membrane {ECO:0000269|PubMed:18160489}. Secreted, extracellular exosome {ECO:0000250|UniProtKB:Q9NP58}. Mitochondrion {ECO:0000250|UniProtKB:Q9NP58}. Endosome, multivesicular body membrane {ECO:0000250|UniProtKB:Q9NP58}. Melanosome membrane {ECO:0000250|UniProtKB:Q9NP58}. Note=Present in the membrane of mature erythrocytes and in exosomes released from reticulocytes during the final steps of erythroid maturation. Traffics from endoplasmic reticulum to Golgi during its glycans's maturation, therefrom is first targeted to the plasma membrane, and is rapidly internalized through endocytosis to be distributed to the limiting membrane of multivesicular bodies and lysosomes. Localized on the limiting membrane of early melanosomes of pigment cells (By similarity). Targeted to the endolysosomal compartment (PubMed:18160489). {ECO:0000250|UniProtKB:Q9NP58, ECO:0000269|PubMed:18160489}.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O + heme b(in) = ADP + H(+) + heme b(out) + phosphate; Xref=Rhea:RHEA:19261, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:60344, ChEBI:CHEBI:456216; EC=7.6.2.5; Evidence={ECO:0000250|UniProtKB:Q9NP58}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19262; Evidence={ECO:0000250|UniProtKB:Q9NP58}; CATALYTIC ACTIVITY: Reaction=ATP + coproporphyrin III(in) + H2O = ADP + coproporphyrin III(out) + H(+) + phosphate; Xref=Rhea:RHEA:66664, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:131725, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q9NP58}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66665; Evidence={ECO:0000250|UniProtKB:Q9NP58}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + pheophorbide a(in) = ADP + H(+) + pheophorbide a(out) + phosphate; Xref=Rhea:RHEA:61360, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58687, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q9NP58}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61361; Evidence={ECO:0000250|UniProtKB:Q9NP58}; CATALYTIC ACTIVITY: Reaction=ATP + coproporphyrinogen III(in) + H2O = ADP + coproporphyrinogen III(out) + H(+) + phosphate; Xref=Rhea:RHEA:66680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57309, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q9DC29}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66681; Evidence={ECO:0000250|UniProtKB:Q9DC29}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + protoporphyrin IX(in) = ADP + H(+) + phosphate + protoporphyrin IX(out); Xref=Rhea:RHEA:61336, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57306, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q9NP58}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61337; Evidence={ECO:0000250|UniProtKB:Q9NP58}; CATALYTIC ACTIVITY: Reaction=ATP + coproporphyrin I(in) + H2O = ADP + coproporphyrin I(out) + H(+) + phosphate; Xref=Rhea:RHEA:66768, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:167478, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q9DC29}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66769; Evidence={ECO:0000250|UniProtKB:Q9DC29}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + uroporphyrin I(in) = ADP + H(+) + phosphate + uroporphyrin I(out); Xref=Rhea:RHEA:66772, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:167480, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q9DC29}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66773; Evidence={ECO:0000250|UniProtKB:Q9DC29}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + uroporphyrin III(in) = ADP + H(+) + phosphate + uroporphyrin III(out); Xref=Rhea:RHEA:66776, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:167479, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q9DC29}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66777; Evidence={ECO:0000250|UniProtKB:Q9DC29};
| null | null | null | null |
FUNCTION: ATP-dependent transporter that catalyzes the transport of a broad-spectrum of porphyrins from the cytoplasm to the extracellular space through the plasma membrane or into the vesicle lumen (By similarity). May also function as an ATP-dependent importer of porphyrins from the cytoplasm into the mitochondria, in turn may participate in the de novo heme biosynthesis regulation and in the coordination of heme and iron homeostasis during phenylhydrazine stress (By similarity). May play a key role in the early steps of melanogenesis producing PMEL amyloid fibrils (By similarity). In vitro, it confers to cells a resistance to toxic metal such as arsenic and cadmium and against chemotherapeutics agent such as 5-fluorouracil, SN-38 and vincristin (By similarity). In addition may play a role in the transition metal homeostasis (PubMed:18160489). {ECO:0000250|UniProtKB:Q9NP58, ECO:0000269|PubMed:18160489}.
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Rattus norvegicus (Rat)
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O70597
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PX11A_RAT
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MDAFIRVANQSQGRDRLFRATQHACMLLRYLLESKAGKEAVVTKLKNLETSVSTGRKWFRLGNVLHAIQATEQSIQATDLVPRLCLTLANLNRVVYYICDTVLWAKSVGLTSGINREKWQMRAARHYYYFLLLSLVRDLYEVLLHMGQVARDRAKREKSSGDPPKYSVANEESEWLQSFLLLLFQSLKRNPPLFLDTVKNFCDILIPLNQLGIYKSNLGVVGFGGLVSSVAGLITVVYPQLKLKAR
| null | null |
brown fat cell differentiation [GO:0050873]; peroxisome fission [GO:0016559]; peroxisome membrane biogenesis [GO:0016557]; peroxisome organization [GO:0007031]; regulation of peroxisome size [GO:0044375]; signal transduction [GO:0007165]
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peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777]; protein-containing complex [GO:0032991]
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protein homodimerization activity [GO:0042803]
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PF05648;
| null |
Peroxin-11 family
| null |
SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000269|PubMed:9548716}; Multi-pass membrane protein {ECO:0000269|PubMed:9548716}.
| null | null | null | null | null |
FUNCTION: May be involved in peroxisomal proliferation and may regulate peroxisomes division. May mediate binding of coatomer proteins to the peroxisomal membrane (PubMed:9548716). Promotes membrane protrusion and elongation on the peroxisomal surface. {ECO:0000250|UniProtKB:O75192, ECO:0000269|PubMed:9548716}.
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Rattus norvegicus (Rat)
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O70600
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RSAD2_RAT
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MLVPTALAARLLSLFQQQLGSLWSGLAMLFCWLRIALGWPDPGKGQPRVRGEPKETQETHEDPGSAQPTTPVSVNYHFTRQCNYKCGFCFHTAKTSFVLPLEEAKRGLLLLKQAGMEKINFSGGEPFLQDRGEYLGKLVRFCKEELALPSVSIVSNGSLIRERWFKDYGDYLDILAISCDSFDEQVNVLIGRGQGKKNHVENLQKLRKWCRDYKVAFKINSVINRFNVDEDMNEHIKALSPVRWKVFQCLLIEGENSGEDALREAERFLISNEEFEAFLQRHKDVSCLVPESNQKMKDSYLILDEYMRFLNCTGGRKDPSRSILDVGVEEAIKFSGFDEKMFLKRGGKYVWSKADLKLDW
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4.2.-.-
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COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250|UniProtKB:Q8WXG1}; Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. {ECO:0000250|UniProtKB:Q8WXG1};
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CD4-positive, alpha-beta T cell activation [GO:0035710]; CD4-positive, alpha-beta T cell differentiation [GO:0043367]; defense response to virus [GO:0051607]; innate immune response [GO:0045087]; negative regulation of protein secretion [GO:0050709]; negative regulation of viral genome replication [GO:0045071]; ossification [GO:0001503]; positive regulation of immune response [GO:0050778]; positive regulation of T-helper 2 cell cytokine production [GO:2000553]; positive regulation of toll-like receptor 7 signaling pathway [GO:0034157]; positive regulation of toll-like receptor 9 signaling pathway [GO:0034165]; regulation of ossification [GO:0030278]; response to virus [GO:0009615]
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endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; lipid droplet [GO:0005811]; mitochondrial inner membrane [GO:0005743]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]
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4 iron, 4 sulfur cluster binding [GO:0051539]; lyase activity [GO:0016829]; metal ion binding [GO:0046872]; protein self-association [GO:0043621]
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PF13353;PF04055;
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3.20.20.70;
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Radical SAM superfamily, RSAD2 family
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PTM: Acetylated by HAT1. HAT1-mediated acetylation of Lys-196 in turn recruits UBE4A that stimulates RSAD2 polyubiquitination leading to proteasomal degradation. {ECO:0000250|UniProtKB:Q8WXG1}.; PTM: 'Lys-6'-linked polyubiquitination at Lys-205 leads to RSAD2 protein degradation. {ECO:0000250|UniProtKB:Q8WXG1}.
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SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8WXG1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8WXG1}; Cytoplasmic side {ECO:0000250|UniProtKB:Q8WXG1}. Golgi apparatus {ECO:0000250|UniProtKB:Q8WXG1}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q8WXG1}. Lipid droplet {ECO:0000250|UniProtKB:Q8WXG1}. Mitochondrion {ECO:0000250|UniProtKB:Q8WXG1}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q8WXG1}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q8WXG1}.
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CATALYTIC ACTIVITY: Reaction=AH2 + CTP + S-adenosyl-L-methionine = 3'-deoxy-3',4'-didehydro-CTP + 5'-deoxyadenosine + A + H(+) + H2O + L-methionine; Xref=Rhea:RHEA:65944, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17319, ChEBI:CHEBI:17499, ChEBI:CHEBI:37563, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789, ChEBI:CHEBI:166821; Evidence={ECO:0000250|UniProtKB:Q8WXG1};
| null | null | null | null |
FUNCTION: Interferon-inducible antiviral protein which plays a major role in the cell antiviral state induced by type I and type II interferon. Catalyzes the conversion of cytidine triphosphate (CTP) to 3'-deoxy-3',4'-didehydro-CTP (ddhCTP) via a SAM-dependent radical mechanism. In turn, ddhCTP acts as a chain terminator for the RNA-dependent RNA polymerases from multiple viruses and directly inhibits viral replication. Therefore, inhibits a wide range of DNA and RNA viruses. Promotes also TLR7 and TLR9-dependent production of IFN-beta production in plasmacytoid dendritic cells (pDCs) by facilitating 'Lys-63'-linked ubiquitination of IRAK1 by TRAF6. Plays a role in CD4+ T-cells activation and differentiation. Facilitates T-cell receptor (TCR)-mediated GATA3 activation and optimal T-helper 2 (Th2) cytokine production by modulating NFKB1 and JUNB activities. Can inhibit secretion of soluble proteins. {ECO:0000250|UniProtKB:Q8WXG1}.
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Rattus norvegicus (Rat)
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O70601
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LAT_RAT
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MEADALSPVELGLLLLPFVVMLLAALCVRCRELPASYDSASTESLYPRSILIKPPQITVPRTPATSYPLVTSFPPLRQPDLLPIPRSPQPLGGSHRMPSSRQNSDDANSVASYENQEPARKNVDEDEDEDDYPEGYLVVLPDSSPAAVPVVSSAPVPSNPDLGDSAFSMESCEDYVNVPESEESAEASLDGSREYVNVSQDAQPVIRAELASVTSQEVEDEEEEDVDGEEAPDYENLQELN
| null | null |
adaptive immune response [GO:0002250]; calcium-mediated signaling [GO:0019722]; gene expression [GO:0010467]; homeostasis of number of cells [GO:0048872]; immune response [GO:0006955]; inflammatory response [GO:0006954]; integrin-mediated signaling pathway [GO:0007229]; intracellular signal transduction [GO:0035556]; lymphocyte homeostasis [GO:0002260]; mast cell degranulation [GO:0043303]; Ras protein signal transduction [GO:0007265]; regulation of T cell activation [GO:0050863]; T cell receptor signaling pathway [GO:0050852]
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cell-cell junction [GO:0005911]; COP9 signalosome [GO:0008180]; immunological synapse [GO:0001772]; membrane [GO:0016020]; plasma membrane [GO:0005886]
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protein kinase binding [GO:0019901]; signaling receptor complex adaptor activity [GO:0030159]
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PF15234;
| null | null |
PTM: Phosphorylated on tyrosines by ZAP70 upon TCR activation, or by SYK upon other immunoreceptor activation; which leads to the recruitment of multiple signaling molecules. Is one of the most prominently tyrosine-phosphorylated proteins detected following TCR engagement. May be dephosphorylated by PTPRJ (By similarity). {ECO:0000250}.; PTM: Palmitoylation of Cys-27 and Cys-30 is required for raft targeting and efficient phosphorylation. {ECO:0000250}.; PTM: Phosphorylated on tyrosines by ZAP70 upon TCR activation, or by SYK upon other immunoreceptor activation; which leads to the recruitment of multiple signaling molecules. Is one of the most prominently tyrosine-phosphorylated proteins detected following TCR engagement. May be dephosphorylated by PTPRJ. Phosphorylated by ITK leading to the recruitment of VAV1 to LAT-containing complexes. {ECO:0000250|UniProtKB:O43561}.; PTM: 'Lys-63'-linked ubiquitinated by TRAF6. {ECO:0000250|UniProtKB:O43561}.
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SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Note=Present in lipid rafts. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Required for TCR (T-cell antigen receptor)- and pre-TCR-mediated signaling, both in mature T-cells and during their development. Involved in FCGR3 (low affinity immunoglobulin gamma Fc region receptor III)-mediated signaling in natural killer cells and FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Couples activation of these receptors and their associated kinases with distal intracellular events such as mobilization of intracellular calcium stores, PKC activation, MAPK activation or cytoskeletal reorganization through the recruitment of PLCG1, GRB2, GRAP2, and other signaling molecules (By similarity). {ECO:0000250}.
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Rattus norvegicus (Rat)
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O70608
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SYCP2_RAT
|
MPVRPDPQQLEKCIDDALRKNDFKPLVTLLQIDICEDVKIKCSKQFLRKLDDLICRELHKKDIQTISNILISIGRCSKNIFILGQTGLQTMIKQGLVQKMVSWFENSKEIILSQRQSKDEAVMNMIEDLFDLLMVVYDVNDEGKNQVLESFIPHICALVIDSRVNFCIQQEALKKMNLMLDRIPQDANKILCNQEILTLMSNMGERILDVGDYELQVGIVEALCRMTTEKRRQELAYEWFSMDFIANAFKKIKDCEFETDCRIFLNLVNGMLGDRRRVFTFPCLSAFLGKYELQIPSDEKLEEFWIDFNLGSHTLSFYIAGDDDDHQWEAVTVPEEKVDMYNIEVRESKKLLTLTLKNIVKISKKEGKELLLYFDAALEITNVTKKLFGGNKYKEFTRKQDISVAKTSIHVLFDASGSQILVPESQPSPVKENLIHLKEKSNLQKKLTNPLEPDNSSSQRDRKNSQDEITTPSRKKMSEASMIVPDTDRYTVRSPILLINTSTPRRSRAPLQAIHSAEKAVSKTSESGVDYAVSLKSRQSDGRNRGNNRANHNKTATVQNKGHEHHESPDQTFNEIEETLSDAYAVEKVDKPVLPGVLDISKNKAHSRWACWTPVTTIKLCNNQRSCALPGDTFTQDTGVNKKCTKQKSVSDDDSEETQRVKYSKDVIKCNKSEEAEVCERNIQEQNHPKYSQKKNTANAKKNDWHIESETTYKSVLLNKTTEESLIYKKTCVLSKDVNTTICDKSPSRKSMRSHTKSRKELMSEVTSCELDEIPVRENSKGKRFTGTAESLINLINKRYNSSDDMISTRKLKEPRDGSGFSKKPELQFNKVQRKSYRKLKTVVNVTSECPLNDVYNFSLNGADEPVIKLGIQEFQATTREASMDNSIKLVDVRNRDERDLSLKTKDERILSHERKTLFSDTETECGWDDSKTDISWLRKPKSKRLMDYSRNKNTKKCKSIKSRSSTEKGQPRSTVVLSKNIAKNDYEVIVDGRTRLPRRATKTKKNYKDLSTSGSESESEKEISYLFKDKLPTKEETVHSSAQTKKLPKKQQKVFNTEALKGQPSEEQKNSSTLRNGREDSLYLSSASVSGSSSSVEVMRCTEKITERDFTQDYDYITKSLSPYPKAASPEFLNRSNRVVGHGKSPRISETSAVCVRKSCSPASGLPFSPRHTTKNNSVMNIKNTNSVINNQRTQHCNSYSDVSSNSSEKLYMEPESPDSCENHVQSKREENHAASPFSLSSEKIEKIWFDMPNDNTHVSGPSQRGSKRRMYLEEDELSNPSEAEVQEAEEREHLVSKKLCQREHFDQHTSETSLSTPEFSVPKDWQQELQGAGMFYDNINSDYKRKTDTQHKIMDDFTTKTLKLTQQHLLAMACQARGHRDENIDKFQVTLLDELEKVEKDSQTLRDLEKEFVDIEEKIVHKMRAFHQSERERFRALKTSLDKSLLVYNSVYEENVLTSEMCLMKANMKMLQDKLLKEMHEEELLNIRRGLESLFKDHEGNNA
| null | null |
animal organ morphogenesis [GO:0009887]; apoptotic process [GO:0006915]; cell division [GO:0051301]; ectopic germ cell programmed cell death [GO:0035234]; female meiotic nuclear division [GO:0007143]; fertilization [GO:0009566]; male genitalia morphogenesis [GO:0048808]; male meiotic nuclear division [GO:0007140]; negative regulation of apoptotic process [GO:0043066]; negative regulation of developmental process [GO:0051093]; negative regulation of reproductive process [GO:2000242]
|
lateral element [GO:0000800]; synaptonemal complex [GO:0000795]
|
DNA binding [GO:0003677]
|
PF18581;PF18584;
| null |
SYCP2 family
|
PTM: Phosphorylated. {ECO:0000250|UniProtKB:Q9CUU3}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9933407}. Chromosome {ECO:0000269|PubMed:9592139, ECO:0000269|PubMed:9933407}. Note=In axial/lateral elements of the tripartite segments of synaptonemal complexes. {ECO:0000269|PubMed:9933407}.
| null | null | null | null | null |
FUNCTION: Major component of the axial/lateral elements of synaptonemal complexes (SCS) during meiotic prophase (PubMed:9592139, PubMed:9933407). Plays a role in the assembly of synaptonemal complexes. Required for normal meiotic chromosome synapsis during oocyte and spermatocyte development and for normal male and female fertility. Required for insertion of SYCP3 into synaptonemal complexes. May be involved in the organization of chromatin by temporarily binding to DNA scaffold attachment regions. Requires SYCP3, but not SYCP1, in order to be incorporated into the axial/lateral elements. {ECO:0000250|UniProtKB:Q9CUU3, ECO:0000269|PubMed:9592139, ECO:0000269|PubMed:9933407}.
|
Rattus norvegicus (Rat)
|
O70622
|
RTN2_MOUSE
|
MGQVLPVFAHCKEAPSTASSTPDSTEGGNDDSDFRELHTAREFSEDEEEETTSQDWGTPRELTFSYIAFDGVVGSGGRRDSVVRRPRPQGRSVSEPRDPPQQSGLGDSLESIPSLSQSPEPGRRGDPDPVPPAERPLEELRLRLDQLGWVVRSAGSGEDSATSSSTPLENEEPDGLEASEAGEETNLELRLAQSLHLQLEVLTPQLSPSSGTPQAHTPSPQRSQDSNSGPDDEPLLNVVEEHWRLLEQEPITAQCLDSTDQSEFMLEPLLLVADLLYWKDTRTSGAVFTGLMASLLCLLHFSIVSVAAHLALLGLCATISLRVYRKVLQAVHRGDGTNPFQAYLDMDLTLTREQTERLSQQIASHVVSTATQLRHFFLVEDLVDSLKLALLFYILTFVGAIFNGLTLVILGVVALFTVPLLYRQHQAQIDQYVGLVTNQLSHIKAKIRAKIPGTGTLAPTASVSGSKAKAE
| null | null |
gene expression [GO:0010467]; intracellular protein transmembrane transport [GO:0065002]; negative regulation of amyloid-beta formation [GO:1902430]; protein transport [GO:0015031]; regulation of glucose import [GO:0046324]
|
cell surface [GO:0009986]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; intermediate filament [GO:0005882]; sarcoplasmic reticulum membrane [GO:0033017]; T-tubule [GO:0030315]; terminal cisterna [GO:0014802]; Z disc [GO:0030018]
| null |
PF02453;
|
1.20.5.2480;
| null | null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O75298}; Multi-pass membrane protein {ECO:0000255}. Sarcoplasmic reticulum membrane {ECO:0000269|PubMed:19720795}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q6WN19}; Multi-pass membrane protein {ECO:0000255}. Cell membrane, sarcolemma {ECO:0000269|PubMed:19720795}; Multi-pass membrane protein {ECO:0000255}. Cell membrane, sarcolemma, T-tubule {ECO:0000269|PubMed:19720795}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:10672514}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10672514}. Note=Localizes to intermediate filaments in mononucleated myoblasts and to Z lines in mature myotubes. {ECO:0000269|PubMed:10672514}.
| null | null | null | null | null |
FUNCTION: Inhibits amyloid precursor protein processing, probably by blocking BACE1 activity (By similarity). Enhances trafficking of the glutamate transporter SLC1A1/EAAC1 from the endoplasmic reticulum to the cell surface (By similarity). Plays a role in the translocation of SLC2A4/GLUT4 from intracellular membranes to the cell membrane which facilitates the uptake of glucose into the cell (PubMed:19720795). {ECO:0000250|UniProtKB:O75298, ECO:0000250|UniProtKB:Q6WN19, ECO:0000269|PubMed:19720795}.
|
Mus musculus (Mouse)
|
O70624
|
MYOC_MOUSE
|
MPALHLLFLACLVWGMGARTAQFRKANDRSGRCQYTFTVASPNESSCPREDQAMSAIQDLQRDSSIQHADLESTKARVRSLESLLHQMTLGRVTGTQEAQEGLQGQLGALRRERDQLETQTRDLEAAYNNLLRDKSALEEEKRQLEQENEDLARRLESSSEEVTRLRRGQCPSTQYPSQDMLPGSREVSQWNLDTLAFQELKSELTEVPASQILKENPSGRPRSKEGDKGCGALVWVGEPVTLRTAETIAGKYGVWMRDPKPTHPYTQESTWRIDTVGTEIRQVFEYSQISQFEQGYPSKVHVLPRALESTGAVVYAGSLYFQGAESRTVVRYELDTETVKAEKEIPGAGYHGHFPYAWGGYTDIDLAVDESGLWVIYSTEEAKGAIVLSKLNPANLELERTWETNIRKQSVANAFVICGILYTVSSYSSAHATVNFAYDTKTGTSKTLTIPFTNRYKYSSMIDYNPLERKLFAWDNFNMVTYDIKLLEM
| null | null |
bone development [GO:0060348]; clustering of voltage-gated sodium channels [GO:0045162]; ERBB2-ERBB3 signaling pathway [GO:0038133]; myelination in peripheral nervous system [GO:0022011]; negative regulation of cell-matrix adhesion [GO:0001953]; negative regulation of Rho protein signal transduction [GO:0035024]; negative regulation of stress fiber assembly [GO:0051497]; neuron projection development [GO:0031175]; non-canonical Wnt signaling pathway [GO:0035567]; osteoblast differentiation [GO:0001649]; positive regulation of cell migration [GO:0030335]; positive regulation of focal adhesion assembly [GO:0051894]; positive regulation of JNK cascade [GO:0046330]; positive regulation of mitochondrial depolarization [GO:0051901]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of stress fiber assembly [GO:0051496]; positive regulation of substrate adhesion-dependent cell spreading [GO:1900026]; regulation of MAPK cascade [GO:0043408]; signal transduction [GO:0007165]; skeletal muscle hypertrophy [GO:0014734]
|
cilium [GO:0005929]; collagen-containing extracellular matrix [GO:0062023]; cytoplasmic vesicle [GO:0031410]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; mesaxon [GO:0097453]; mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space [GO:0005758]; mitochondrial outer membrane [GO:0005741]; myelin sheath abaxonal region [GO:0035748]; node of Ranvier [GO:0033268]; rough endoplasmic reticulum [GO:0005791]; Schmidt-Lanterman incisure [GO:0043220]
|
fibronectin binding [GO:0001968]; frizzled binding [GO:0005109]; metal ion binding [GO:0046872]; myosin light chain binding [GO:0032027]; receptor tyrosine kinase binding [GO:0030971]
|
PF02191;
| null | null |
PTM: Palmitoylated. {ECO:0000250|UniProtKB:Q2PT31}.; PTM: Undergoes a calcium-dependent proteolytic cleavage at Gln-212 by CAPN2 in the endoplasmic reticulum. The result is the production of two fragments, one of 35 kDa containing the C-terminal olfactomedin-like domain, and another of 20 kDa containing the N-terminal leucine zipper-like domain (By similarity). {ECO:0000250}.; PTM: Glycosylated. {ECO:0000250|UniProtKB:Q99972}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16392033}. Golgi apparatus {ECO:0000269|PubMed:23629661}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q99972}. Secreted, extracellular space {ECO:0000250|UniProtKB:Q99972}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q99972}. Secreted, extracellular exosome {ECO:0000250|UniProtKB:Q99972}. Mitochondrion {ECO:0000250|UniProtKB:Q99972}. Mitochondrion intermembrane space {ECO:0000250|UniProtKB:Q99972}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q99972}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q99972}. Rough endoplasmic reticulum {ECO:0000269|PubMed:23629661}. Cell projection {ECO:0000250|UniProtKB:Q99972}. Cell projection, cilium {ECO:0000250|UniProtKB:Q99972}. Note=Located preferentially in the ciliary rootlet and basal body of the connecting cilium of photoreceptor cells, and in the rough endoplasmic reticulum. It is only imported to mitochondria in the trabecular meshwork. Localizes to the Golgi apparatus in Schlemm's canal endothelial cells. Appears in the extracellular space of trabecular meshwork cells by an unconventional mechanism, likely associated with exosome-like vesicles. Localizes in trabecular meshwork extracellular matrix. {ECO:0000250|UniProtKB:Q99972}.; SUBCELLULAR LOCATION: [Myocilin, C-terminal fragment]: Secreted {ECO:0000250}.; SUBCELLULAR LOCATION: [Myocilin, N-terminal fragment]: Endoplasmic reticulum. Note=Remains retained in the endoplasmic reticulum. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Secreted glycoprotein regulating the activation of different signaling pathways in adjacent cells to control different processes including cell adhesion, cell-matrix adhesion, cytoskeleton organization and cell migration. Promotes substrate adhesion, spreading and formation of focal contacts. Negatively regulates cell-matrix adhesion and stress fiber assembly through Rho protein signal transduction. Modulates the organization of actin cytoskeleton by stimulating the formation of stress fibers through interactions with components of Wnt signaling pathways. Promotes cell migration through activation of PTK2 and the downstream phosphatidylinositol 3-kinase signaling (By similarity). Plays a role in bone formation and promotes osteoblast differentiation in a dose-dependent manner through mitogen-activated protein kinase signaling (PubMed:23629661). Mediates myelination in the peripheral nervous system through ERBB2/ERBB3 signaling (PubMed:23897819). Plays a role as a regulator of muscle hypertrophy through the components of dystrophin-associated protein complex (PubMed:22371502). Involved in positive regulation of mitochondrial depolarization. Plays a role in neurite outgrowth. May participate in the obstruction of fluid outflow in the trabecular meshwork (By similarity). {ECO:0000250|UniProtKB:Q99972, ECO:0000269|PubMed:22371502, ECO:0000269|PubMed:23629661, ECO:0000269|PubMed:23897819}.
|
Mus musculus (Mouse)
|
O70628
|
PDE9A_MOUSE
|
MGAGSSSYRPKAIYLDIDGRIQKVVFSKYCNSSDIMDLFCIATGLPRNTTISLLTTDDAMVSIDPTMPANSERTPYKVRPVAVKQVSEREELIQGVLAQVAEQFSRAFKINELKAEVANHLAVLEKRVELEGLKVVEIEKCKSDIKKMREELAARNSRTNCPCKYSFLDNKKLTPRRDVPTYPKYLLSPETIEALRKPTFDVWLWEPNEMLSCLEHMYHDLGLVRDFSINPITLRRWLLCVHDNYRNNPFHNFRHCFCVTQMMYSMVWLCGLQEKFSQMDILVLMTAAICHDLDHPGYNNTYQINARTELAVRYNDISPLENHHCAIAFQILARPECNIFASVPPEGFRQIRQGMITLILATDMARHAEIMDSFKEKMENFDYSNEEHLTLLKMILIKCCDISNEVRPMEVAEPWVDCLLEEYFMQSDREKSEGLPVAPFMDRDKVTKATAQIGFIKFVLIPMFETVTKLFPVVEETMLRPLWESREHYEELKQLDDAMKELQKKTESLTSGAPENTTEKNRDAKDSEGHSPPN
|
3.1.4.35
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:O76083}; Note=Binds 1 Zn(2+) ion per subunit. Binds 2 divalent metal cations per subunit: site 1 preferentially binds zinc, while site 2 has a preference for magnesium. Tightly binds zinc. {ECO:0000250|UniProtKB:O76083}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O76083}; Note=Binds 1 Mg(2+) ions per subunit. Binds 2 divalent metal cations per subunit: site 1 preferentially binds zinc, while site 2 has a preference for magnesium. Binds magnesium less tightly than zinc. {ECO:0000250|UniProtKB:O76083};
|
cAMP-mediated signaling [GO:0019933]; cGMP catabolic process [GO:0046069]; negative regulation of neural precursor cell proliferation [GO:2000178]; positive regulation of cardiac muscle hypertrophy [GO:0010613]; positive regulation of long-term synaptic potentiation [GO:1900273]
|
cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; nucleoplasm [GO:0005654]; perikaryon [GO:0043204]; perinuclear region of cytoplasm [GO:0048471]; ruffle membrane [GO:0032587]; sarcolemma [GO:0042383]
|
3',5'-cyclic-AMP phosphodiesterase activity [GO:0004115]; 3',5'-cyclic-GMP phosphodiesterase activity [GO:0047555]; metal ion binding [GO:0046872]
|
PF00233;
|
1.10.1300.10;
|
Cyclic nucleotide phosphodiesterase family, PDE9 subfamily
| null |
SUBCELLULAR LOCATION: Cell projection, ruffle membrane {ECO:0000250|UniProtKB:O76083}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O76083}. Golgi apparatus {ECO:0000250|UniProtKB:O76083}. Endoplasmic reticulum {ECO:0000250|UniProtKB:O76083}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:O76083}.
|
CATALYTIC ACTIVITY: Reaction=3',5'-cyclic GMP + H2O = GMP + H(+); Xref=Rhea:RHEA:16957, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57746, ChEBI:CHEBI:58115; EC=3.1.4.35; Evidence={ECO:0000269|PubMed:9624145};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.07 mM for cGMP {ECO:0000269|PubMed:9624145};
|
PATHWAY: Purine metabolism; 3',5'-cyclic GMP degradation; GMP from 3',5'-cyclic GMP: step 1/1.
| null | null |
FUNCTION: Specifically hydrolyzes the second messenger cGMP, which is a key regulator of many important physiological processes (PubMed:9624145). Highly specific: compared to other members of the cyclic nucleotide phosphodiesterase family, has the highest affinity and selectivity for cGMP. Specifically regulates natriuretic-peptide-dependent cGMP signaling in heart, acting as a regulator of cardiac hypertrophy in myocytes and muscle. Does not regulate nitric oxide-dependent cGMP in heart (PubMed:25799991). Additional experiments are required to confirm whether its ability to hydrolyze natriuretic-peptide-dependent cGMP is specific to heart or is a general feature of the protein (Probable). In brain, involved in cognitive function, such as learning and long-term memory (PubMed:22328573, PubMed:24746365). {ECO:0000269|PubMed:22328573, ECO:0000269|PubMed:24746365, ECO:0000269|PubMed:25799991, ECO:0000269|PubMed:9624145, ECO:0000305}.
|
Mus musculus (Mouse)
|
O70631
|
EST2C_RAT
|
MARKQPHSWLNAVLFGLLLILIHVWGQDSPESSSIRTTHTGQVRGKLDHVRDTKAGVHTFLGIPFAKAPVGPLRFAPPEDPEPWSGVRDGTSHPAMCLQNIDMLDEVGLTDMKMILSSIPMSEDCLYLNIYTPAHAHEGSNLPVMVCIHGGALVIGMASMCDGSLLAVNEDLVVVAIQYRLGVLGFFSTGDEHARGNWGYLDQVAALRWVQQNIAHFGGNPNRVTIFGVSAGGTSVSSHVISPMSQGLFHGAIMESGVALLPDLISETSETVSTTVAKLSGCEATDSETLVRCLRAKSGAEILVINKVFKMIPAVVDGEFLPRHPKELLASEDFHPVPSIIGVNTDEYCCTIPMVMGTAQIIKELSRENLQAVLKDTAAQMMLPPECGDLLMEEYMGNTDDPQTLQIQYAEMMGDFLFVIPALQVAHFQRSHAPVYFYEFQHAPSYFKNVRPPHVKADHADEVPFVFGSFFWGIKVDFTEEEKLLSRRMMKYWANFARHGNPNSEGLPYWPVLDHDEQYLQLDTQPAVDRALKARRLQFWTKTLPQKIQELNGAQKNHAEL
|
3.1.1.-; 3.1.1.28
| null |
retinoid metabolic process [GO:0001523]
|
endoplasmic reticulum [GO:0005783]; intracellular membrane-bounded organelle [GO:0043231]
|
acylcarnitine hydrolase activity [GO:0047619]; all-trans-retinyl-palmitate hydrolase, all-trans-retinol forming activity [GO:0047376]; carboxylic ester hydrolase activity [GO:0052689]; retinyl-palmitate esterase activity [GO:0050253]
|
PF00135;
|
3.40.50.1820;
|
Type-B carboxylesterase/lipase family
| null |
SUBCELLULAR LOCATION: Microsome {ECO:0000269|PubMed:12230550}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q91WG0}.
|
CATALYTIC ACTIVITY: Reaction=all-trans-retinyl hexadecanoate + H2O = all-trans-retinol + H(+) + hexadecanoate; Xref=Rhea:RHEA:13933, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17336, ChEBI:CHEBI:17616; Evidence={ECO:0000305|PubMed:12230550}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13934; Evidence={ECO:0000305|PubMed:12230550}; CATALYTIC ACTIVITY: Reaction=H2O + O-acyl-(R)-carnitine = (R)-carnitine + a fatty acid + H(+); Xref=Rhea:RHEA:17101, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16347, ChEBI:CHEBI:28868, ChEBI:CHEBI:75659; EC=3.1.1.28; Evidence={ECO:0000250|UniProtKB:Q91WG0};
| null | null | null | null |
FUNCTION: Hydrolase with high activity towards palmitoylcarnitine. Is also active with p-nitrophenylacetate and alpha-naphthylacetate (By similarity). May also hydrolyze retinyl esters (PubMed:12230550). {ECO:0000250|UniProtKB:Q91WG0, ECO:0000269|PubMed:12230550}.
|
Rattus norvegicus (Rat)
|
O70632
|
M2_I97A1
|
MSLLTEVETLTRNGWGCRCSDSSDPLVVAASIIGILHLILWILDRLFFKCIYRRFKYGLKRGPSTEGVPESMREEYRQEQQNAVDVDDGHFVNIELE
| null | null |
protein complex oligomerization [GO:0051259]; suppression by virus of host autophagy [GO:0039521]
|
host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion membrane [GO:0055036]
|
identical protein binding [GO:0042802]; monoatomic ion channel activity [GO:0005216]; proton transmembrane transporter activity [GO:0015078]
|
PF00599;
|
6.10.250.1640;
|
Influenza viruses matrix protein M2 family
| null |
SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04069}. Host apical cell membrane {ECO:0000255|HAMAP-Rule:MF_04069}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04069}. Note=Abundantly expressed at the apical plasma membrane in infected polarized epithelial cells, in close proximity to budding and assembled virions. Minor component of virions (only 16-20 molecules/virion). {ECO:0000255|HAMAP-Rule:MF_04069}.
| null | null | null | null | null |
FUNCTION: Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry. After attaching to the cell surface, the virion enters the cell by endocytosis. Acidification of the endosome triggers M2 ion channel activity. The influx of protons into virion interior is believed to disrupt interactions between the viral ribonucleoprotein (RNP), matrix protein 1 (M1), and lipid bilayers, thereby freeing the viral genome from interaction with viral proteins and enabling RNA segments to migrate to the host cell nucleus, where influenza virus RNA transcription and replication occur. Also plays a role in viral proteins secretory pathway. Elevates the intravesicular pH of normally acidic compartments, such as trans-Golgi network, preventing newly formed hemagglutinin from premature switching to the fusion-active conformation. {ECO:0000255|HAMAP-Rule:MF_04069}.
|
Influenza A virus (strain A/Hong Kong/156/1997 H5N1 genotype Gs/Gd)
|
O70889
|
TAT_HV193
|
MELVDPNLDPWNHPGSQPTTPCTRCYCKWCCFHCYWCFTTKGLGISYGRKKRRQRPRTPQSSQIHQDFVPKQPISQARGNPTGPKESKKEVESKAKTDP
| null | null |
DNA-templated transcription [GO:0006351]; modulation by virus of host chromatin organization [GO:0039525]; negative regulation of peptidyl-threonine phosphorylation [GO:0010801]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; positive regulation of viral transcription [GO:0050434]; symbiont-mediated suppression of host translation initiation [GO:0039606]; symbiont-mediated suppression of host type I interferon-mediated signaling pathway [GO:0039502]; virus-mediated perturbation of host defense response [GO:0019049]
|
extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]; host cell nucleolus [GO:0044196]
|
actinin binding [GO:0042805]; cyclin binding [GO:0030332]; metal ion binding [GO:0046872]; protein domain specific binding [GO:0019904]; protein serine/threonine phosphatase inhibitor activity [GO:0004865]; RNA-binding transcription regulator activity [GO:0001070]; trans-activation response element binding [GO:1990970]
|
PF00539;
|
4.10.20.10;
|
Lentiviruses Tat family
|
PTM: Asymmetrical arginine methylation by host PRMT6 seems to diminish the transactivation capacity of Tat and affects the interaction with host CCNT1. {ECO:0000255|HAMAP-Rule:MF_04079}.; PTM: Acetylation by EP300, CREBBP, GCN5L2/GCN5 and PCAF regulates the transactivation activity of Tat. EP300-mediated acetylation of Lys-50 promotes dissociation of Tat from the TAR RNA through the competitive binding to PCAF's bromodomain. In addition, the non-acetylated Tat's N-terminus can also interact with PCAF. PCAF-mediated acetylation of Lys-28 enhances Tat's binding to CCNT1. Lys-50 is deacetylated by SIRT1. {ECO:0000255|HAMAP-Rule:MF_04079}.; PTM: Polyubiquitination by host MDM2 does not target Tat to degradation, but activates its transactivation function and fosters interaction with CCNT1 and TAR RNA. {ECO:0000255|HAMAP-Rule:MF_04079}.; PTM: Phosphorylated by EIF2AK2 on serine and threonine residues adjacent to the basic region important for TAR RNA binding and function. Phosphorylation of Tat by EIF2AK2 is dependent on the prior activation of EIF2AK2 by dsRNA. {ECO:0000255|HAMAP-Rule:MF_04079}.
|
SUBCELLULAR LOCATION: Host nucleus, host nucleolus {ECO:0000255|HAMAP-Rule:MF_04079}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04079}. Secreted {ECO:0000255|HAMAP-Rule:MF_04079}. Note=Probably localizes to both nuclear and nucleolar compartments. Nuclear localization is mediated through the interaction of the nuclear localization signal with importin KPNB1. Secretion occurs through a Golgi-independent pathway. Tat is released from infected cells to the extracellular space where it remains associated to the cell membrane, or is secreted into the cerebrospinal fluid and sera. Extracellular Tat can be endocytosed by surrounding uninfected cells via binding to several receptors depending on the cell type. {ECO:0000255|HAMAP-Rule:MF_04079}.
| null | null | null | null | null |
FUNCTION: Transcriptional activator that increases RNA Pol II processivity, thereby increasing the level of full-length viral transcripts. Recognizes a hairpin structure at the 5'-LTR of the nascent viral mRNAs referred to as the transactivation responsive RNA element (TAR) and recruits the cyclin T1-CDK9 complex (P-TEFb complex) that will in turn hyperphosphorylate the RNA polymerase II to allow efficient elongation. The CDK9 component of P-TEFb and other Tat-activated kinases hyperphosphorylate the C-terminus of RNA Pol II that becomes stabilized and much more processive. Other factors such as HTATSF1/Tat-SF1, SUPT5H/SPT5, and HTATIP2 are also important for Tat's function. Besides its effect on RNA Pol II processivity, Tat induces chromatin remodeling of proviral genes by recruiting the histone acetyltransferases (HATs) CREBBP, EP300 and PCAF to the chromatin. This also contributes to the increase in proviral transcription rate, especially when the provirus integrates in transcriptionally silent region of the host genome. To ensure maximal activation of the LTR, Tat mediates nuclear translocation of NF-kappa-B by interacting with host RELA. Through its interaction with host TBP, Tat may also modulate transcription initiation. Tat can reactivate a latently infected cell by penetrating in it and transactivating its LTR promoter. In the cytoplasm, Tat is thought to act as a translational activator of HIV-1 mRNAs. {ECO:0000255|HAMAP-Rule:MF_04079}.; FUNCTION: Extracellular circulating Tat can be endocytosed by surrounding uninfected cells via the binding to several surface receptors such as CD26, CXCR4, heparan sulfate proteoglycans (HSPG) or LDLR. Neurons are rarely infected, but they internalize Tat via their LDLR. Through its interaction with nuclear HATs, Tat is potentially able to control the acetylation-dependent cellular gene expression. Modulates the expression of many cellular genes involved in cell survival, proliferation or in coding for cytokines or cytokine receptors. Tat plays a role in T-cell and neurons apoptosis. Tat induced neurotoxicity and apoptosis probably contribute to neuroAIDS. Circulating Tat also acts as a chemokine-like and/or growth factor-like molecule that binds to specific receptors on the surface of the cells, affecting many cellular pathways. In the vascular system, Tat binds to ITGAV/ITGB3 and ITGA5/ITGB1 integrins dimers at the surface of endothelial cells and competes with bFGF for heparin-binding sites, leading to an excess of soluble bFGF. {ECO:0000255|HAMAP-Rule:MF_04079}.
|
Human immunodeficiency virus type 1 group M subtype F1 (isolate 93BR020) (HIV-1)
|
O70899
|
TAT_HV190
|
MDPVDPKLEPWNHPGSQPQTACNNCYCKKCCYHCQMCFLKKGLGISYGRKKRSQRHRTPASLQDHQNSISKQPLSRTHGDPTGPKEQKKEVASKTETDP
| null | null |
DNA-templated transcription [GO:0006351]; modulation by virus of host chromatin organization [GO:0039525]; negative regulation of peptidyl-threonine phosphorylation [GO:0010801]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; positive regulation of viral transcription [GO:0050434]; symbiont-mediated suppression of host translation initiation [GO:0039606]; symbiont-mediated suppression of host type I interferon-mediated signaling pathway [GO:0039502]; virus-mediated perturbation of host defense response [GO:0019049]
|
extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]; host cell nucleolus [GO:0044196]
|
actinin binding [GO:0042805]; cyclin binding [GO:0030332]; metal ion binding [GO:0046872]; protein domain specific binding [GO:0019904]; protein serine/threonine phosphatase inhibitor activity [GO:0004865]; RNA-binding transcription regulator activity [GO:0001070]; trans-activation response element binding [GO:1990970]
|
PF00539;
|
4.10.20.10;
|
Lentiviruses Tat family
|
PTM: Asymmetrical arginine methylation by host PRMT6 seems to diminish the transactivation capacity of Tat and affects the interaction with host CCNT1. {ECO:0000255|HAMAP-Rule:MF_04079}.; PTM: Acetylation by EP300, CREBBP, GCN5L2/GCN5 and PCAF regulates the transactivation activity of Tat. EP300-mediated acetylation of Lys-50 promotes dissociation of Tat from the TAR RNA through the competitive binding to PCAF's bromodomain. In addition, the non-acetylated Tat's N-terminus can also interact with PCAF. PCAF-mediated acetylation of Lys-28 enhances Tat's binding to CCNT1. Lys-50 is deacetylated by SIRT1. {ECO:0000255|HAMAP-Rule:MF_04079}.; PTM: Polyubiquitination by host MDM2 does not target Tat to degradation, but activates its transactivation function and fosters interaction with CCNT1 and TAR RNA. {ECO:0000255|HAMAP-Rule:MF_04079}.; PTM: Phosphorylated by EIF2AK2 on serine and threonine residues adjacent to the basic region important for TAR RNA binding and function. Phosphorylation of Tat by EIF2AK2 is dependent on the prior activation of EIF2AK2 by dsRNA. {ECO:0000255|HAMAP-Rule:MF_04079}.
|
SUBCELLULAR LOCATION: Host nucleus, host nucleolus {ECO:0000255|HAMAP-Rule:MF_04079}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04079}. Secreted {ECO:0000255|HAMAP-Rule:MF_04079}. Note=Probably localizes to both nuclear and nucleolar compartments. Nuclear localization is mediated through the interaction of the nuclear localization signal with importin KPNB1. Secretion occurs through a Golgi-independent pathway. Tat is released from infected cells to the extracellular space where it remains associated to the cell membrane, or is secreted into the cerebrospinal fluid and sera. Extracellular Tat can be endocytosed by surrounding uninfected cells via binding to several receptors depending on the cell type. {ECO:0000255|HAMAP-Rule:MF_04079}.
| null | null | null | null | null |
FUNCTION: Transcriptional activator that increases RNA Pol II processivity, thereby increasing the level of full-length viral transcripts. Recognizes a hairpin structure at the 5'-LTR of the nascent viral mRNAs referred to as the transactivation responsive RNA element (TAR) and recruits the cyclin T1-CDK9 complex (P-TEFb complex) that will in turn hyperphosphorylate the RNA polymerase II to allow efficient elongation. The CDK9 component of P-TEFb and other Tat-activated kinases hyperphosphorylate the C-terminus of RNA Pol II that becomes stabilized and much more processive. Other factors such as HTATSF1/Tat-SF1, SUPT5H/SPT5, and HTATIP2 are also important for Tat's function. Besides its effect on RNA Pol II processivity, Tat induces chromatin remodeling of proviral genes by recruiting the histone acetyltransferases (HATs) CREBBP, EP300 and PCAF to the chromatin. This also contributes to the increase in proviral transcription rate, especially when the provirus integrates in transcriptionally silent region of the host genome. To ensure maximal activation of the LTR, Tat mediates nuclear translocation of NF-kappa-B by interacting with host RELA. Through its interaction with host TBP, Tat may also modulate transcription initiation. Tat can reactivate a latently infected cell by penetrating in it and transactivating its LTR promoter. In the cytoplasm, Tat is thought to act as a translational activator of HIV-1 mRNAs. {ECO:0000255|HAMAP-Rule:MF_04079}.; FUNCTION: Extracellular circulating Tat can be endocytosed by surrounding uninfected cells via the binding to several surface receptors such as CD26, CXCR4, heparan sulfate proteoglycans (HSPG) or LDLR. Neurons are rarely infected, but they internalize Tat via their LDLR. Through its interaction with nuclear HATs, Tat is potentially able to control the acetylation-dependent cellular gene expression. Modulates the expression of many cellular genes involved in cell survival, proliferation or in coding for cytokines or cytokine receptors. Tat plays a role in T-cell and neurons apoptosis. Tat induced neurotoxicity and apoptosis probably contribute to neuroAIDS. Circulating Tat also acts as a chemokine-like and/or growth factor-like molecule that binds to specific receptors on the surface of the cells, affecting many cellular pathways. In the vascular system, Tat binds to ITGAV/ITGB3 and ITGA5/ITGB1 integrins dimers at the surface of endothelial cells and competes with bFGF for heparin-binding sites, leading to an excess of soluble bFGF. {ECO:0000255|HAMAP-Rule:MF_04079}.
|
Human immunodeficiency virus type 1 group M subtype H (isolate 90CF056) (HIV-1)
|
O70902
|
ENV_HV190
|
METQRNYPSLWRWGTLILGMLLICSAAQNLWVTVYYGVPVWKEAKTTLFCASDAKAYETEKHNVWATHACVPTDPNPQEMVMENVTESFNMWENNMVEQMHTDIISLWDQSLKPCVKLTPLCVTLNCTNVRNNTSNSTSSMEAGGELTNCSFNVTTVLRDKQQKVHALFYRLDVVPIDNNSTQYRLINCNTSVITQACPKVSFEPIPIHYCAPAGFAILKCNNKTFNGTGLCTNVSTVQCTHGIRPVVSTQLLLNGSLAEEQIIIRTKNISDNTKNIIVQLKTPVNITCTRPNNNTRTSIHLGPGRAFYATGDIIGDIRQAHCNISRTDWNKTLHQVVTQLGIHLNNRTISFKPNSGGDMEVRTHSFNCRGEFFYCNTSGLFNSSWEMHTNYTSNDTKGNENITLPCRIKQIVNMWQRVGRAMYAPPIQGNIMCVSNITGLILTIDEGNASAENYTFRPGGGDMRDNWRSELYKYKVVKIEPLGIAPTKTRRRVVEREKRAVGMGASFLGFLGAAGSTMGAASITLTVQARQLLSGIVQQQSNLLRAIQARQHMLQLTVWGIKQLQARVLAVERYLRDQQLLGIWGCSGKLICTTNVPWNSSWSNKSQSEIWDNMTWMEWDKQISNYTEEIYRLLEVSQTQQEKNEQDLLALDKWASLWTWFDISHWLWYIKIFIMIVGGLIGLRIIFAVLSIVNRVRQGYSPLSFQTLVPNPRGPDRPEGTEEGGGEQDRDRSVRLVNGFLPVVWDDLRSLSLFSYRLLRDLLLIVVRTVELLGRRGREALKYLWNLLQYWGQELKNSAIDLLNTTAIAVAEGTDGIIVIVQRAWRAILHIPRRIRQGFERSLL
| null | null |
clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; fusion of virus membrane with host plasma membrane [GO:0019064]; positive regulation of establishment of T cell polarity [GO:1903905]; positive regulation of plasma membrane raft polarization [GO:1903908]; positive regulation of receptor clustering [GO:1903911]; viral protein processing [GO:0019082]; virion attachment to host cell [GO:0019062]; virus-mediated perturbation of host defense response [GO:0019049]
|
host cell endosome membrane [GO:0044175]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036]
|
structural molecule activity [GO:0005198]
|
PF00516;PF00517;
|
1.10.287.210;2.170.40.20;1.20.5.490;
|
HIV-1 env protein family
|
PTM: Highly glycosylated by host. The high number of glycan on the protein is reffered to as 'glycan shield' because it contributes to hide protein sequence from adaptive immune system. {ECO:0000255|HAMAP-Rule:MF_04083}.; PTM: Palmitoylation of the transmembrane protein and of Env polyprotein (prior to its proteolytic cleavage) is essential for their association with host cell membrane lipid rafts. Palmitoylation is therefore required for envelope trafficking to classical lipid rafts, but not for viral replication. {ECO:0000255|HAMAP-Rule:MF_04083}.; PTM: Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as an inactive precursor that is heavily N-glycosylated and processed likely by host cell furin in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires the minimal sequence [KR]-X-[KR]-R. About 2 of the 9 disulfide bonds of gp41 are reduced by P4HB/PDI, following binding to CD4 receptor. {ECO:0000255|HAMAP-Rule:MF_04083}.
|
SUBCELLULAR LOCATION: [Surface protein gp120]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Note=The surface protein is not anchored to the viral envelope, but associates with the extravirion surface through its binding to TM. It is probably concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag. {ECO:0000255|HAMAP-Rule:MF_04083}.; SUBCELLULAR LOCATION: [Transmembrane protein gp41]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Note=It is probably concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag. {ECO:0000255|HAMAP-Rule:MF_04083}.
| null | null | null | null | null |
FUNCTION: [Envelope glycoprotein gp160]: Oligomerizes in the host endoplasmic reticulum into predominantly trimers. In a second time, gp160 transits in the host Golgi, where glycosylation is completed. The precursor is then proteolytically cleaved in the trans-Golgi and thereby activated by cellular furin or furin-like proteases to produce gp120 and gp41. {ECO:0000255|HAMAP-Rule:MF_04083}.; FUNCTION: [Surface protein gp120]: Attaches the virus to the host lymphoid cell by binding to the primary receptor CD4. This interaction induces a structural rearrangement creating a high affinity binding site for a chemokine coreceptor like CXCR4 and/or CCR5. Acts as a ligand for CD209/DC-SIGN and CLEC4M/DC-SIGNR, which are respectively found on dendritic cells (DCs), and on endothelial cells of liver sinusoids and lymph node sinuses. These interactions allow capture of viral particles at mucosal surfaces by these cells and subsequent transmission to permissive cells. HIV subverts the migration properties of dendritic cells to gain access to CD4+ T-cells in lymph nodes. Virus transmission to permissive T-cells occurs either in trans (without DCs infection, through viral capture and transmission), or in cis (following DCs productive infection, through the usual CD4-gp120 interaction), thereby inducing a robust infection. In trans infection, bound virions remain infectious over days and it is proposed that they are not degraded, but protected in non-lysosomal acidic organelles within the DCs close to the cell membrane thus contributing to the viral infectious potential during DCs' migration from the periphery to the lymphoid tissues. On arrival at lymphoid tissues, intact virions recycle back to DCs' cell surface allowing virus transmission to CD4+ T-cells. {ECO:0000255|HAMAP-Rule:MF_04083}.; FUNCTION: [Transmembrane protein gp41]: Acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During fusion of viral and target intracellular membranes, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Complete fusion occurs in host cell endosomes and is dynamin-dependent, however some lipid transfer might occur at the plasma membrane. The virus undergoes clathrin-dependent internalization long before endosomal fusion, thus minimizing the surface exposure of conserved viral epitopes during fusion and reducing the efficacy of inhibitors targeting these epitopes. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm. {ECO:0000255|HAMAP-Rule:MF_04083}.
|
Human immunodeficiency virus type 1 group M subtype H (isolate 90CF056) (HIV-1)
|
O70903
|
NEF_HV190
|
MGGKWSKSRMGGWSTIRERMRRAEPVAEGVGAVSRDLDRRGAVTINNTASTNRDAAWLEAQEDGEEVGFPVRPQVPLRPMTYKGAFDLSHFLKEKGGLDGLIYSKQRQDILDLWVYNTQGYFPDWQNYTPGPGERFPLTFGWCFKLVPVNPQEVEQANEGENNSLLHPMSLHGMEDDGREVLMWKFDSRLALTHLARVKHPEYKDC
| null | null |
suppression by virus of host autophagy [GO:0039521]; symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class I [GO:0046776]; symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class II [GO:0039505]; virus-mediated perturbation of host defense response [GO:0019049]
|
extracellular region [GO:0005576]; host cell Golgi membrane [GO:0044178]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion component [GO:0044423]
|
GTP binding [GO:0005525]; SH3 domain binding [GO:0017124]
|
PF00469;
|
4.10.890.10;3.30.62.10;
|
Lentivirus primate group Nef protein family
|
PTM: The virion-associated Nef proteins are cleaved by the viral protease to release the soluble C-terminal core protein. Nef is probably cleaved concomitantly with viral structural proteins on maturation of virus particles. {ECO:0000255|HAMAP-Rule:MF_04078}.; PTM: Myristoylated. {ECO:0000255|HAMAP-Rule:MF_04078}.; PTM: Phosphorylated on serine residues, probably by host PKCdelta and theta. {ECO:0000255|HAMAP-Rule:MF_04078}.
|
SUBCELLULAR LOCATION: Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04078}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04078}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_04078}. Virion {ECO:0000255|HAMAP-Rule:MF_04078}. Secreted {ECO:0000255|HAMAP-Rule:MF_04078}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_04078}. Note=TGN localization requires PACS1. Associates with the inner plasma membrane through its N-terminal domain. Nef stimulates its own export via the release of exosomes. Incorporated in virions at a rate of about 10 molecules per virion, where it is cleaved. {ECO:0000255|HAMAP-Rule:MF_04078}.
| null | null | null | null | null |
FUNCTION: Factor of infectivity and pathogenicity, required for optimal virus replication. Alters numerous pathways of T-lymphocyte function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity. Alters the functionality of other immunity cells, like dendritic cells, monocytes/macrophages and NK cells. {ECO:0000255|HAMAP-Rule:MF_04078}.; FUNCTION: In infected CD4(+) T-lymphocytes, down-regulates the surface MHC-I, mature MHC-II, CD4, CD28, CCR5 and CXCR4 molecules. Mediates internalization and degradation of host CD4 through the interaction of with the cytoplasmic tail of CD4, the recruitment of AP-2 (clathrin adapter protein complex 2), internalization through clathrin coated pits, and subsequent transport to endosomes and lysosomes for degradation. Diverts host MHC-I molecules to the trans-Golgi network-associated endosomal compartments by an endocytic pathway to finally target them for degradation. MHC-I down-regulation may involve AP-1 (clathrin adapter protein complex 1) or possibly Src family kinase-ZAP70/Syk-PI3K cascade recruited by PACS2. In consequence infected cells are masked for immune recognition by cytotoxic T-lymphocytes. Decreasing the number of immune receptors also prevents reinfection by more HIV particles (superinfection). Down-regulates host SERINC3 and SERINC5 thereby excluding these proteins from the viral particles. Virion infectivity is drastically higher when SERINC3 or SERINC5 are excluded from the viral envelope, because these host antiviral proteins impair the membrane fusion event necessary for subsequent virion penetration. {ECO:0000255|HAMAP-Rule:MF_04078}.; FUNCTION: Bypasses host T-cell signaling by inducing a transcriptional program nearly identical to that of anti-CD3 cell activation. Interaction with TCR-zeta chain up-regulates the Fas ligand (FasL). Increasing surface FasL molecules and decreasing surface MHC-I molecules on infected CD4(+) cells send attacking cytotoxic CD8+ T-lymphocytes into apoptosis. {ECO:0000255|HAMAP-Rule:MF_04078}.; FUNCTION: Plays a role in optimizing the host cell environment for viral replication without causing cell death by apoptosis. Protects the infected cells from apoptosis in order to keep them alive until the next virus generation is ready to strike. Inhibits the Fas and TNFR-mediated death signals by blocking MAP3K5/ASK1. Decreases the half-life of TP53, protecting the infected cell against p53-mediated apoptosis. Inhibits the apoptotic signals regulated by the Bcl-2 family proteins through the formation of a Nef/PI3-kinase/PAK2 complex that leads to activation of PAK2 and induces phosphorylation of host BAD. {ECO:0000255|HAMAP-Rule:MF_04078}.; FUNCTION: Extracellular Nef protein targets CD4(+) T-lymphocytes for apoptosis by interacting with CXCR4 surface receptors. {ECO:0000255|HAMAP-Rule:MF_04078}.
|
Human immunodeficiency virus type 1 group M subtype H (isolate 90CF056) (HIV-1)
|
O71189
|
R1AB_GLRV3
|
MDYIRPLRVFSFPHVNNTLEYVRYNKANGDVGAFLTTMKFIGNVKLSDFTPRCAAMIYIGKLTKGVKRTFVPPPVKGFARQYAVVSGSVSALRGDGKKVLMEARTSTSATSDVSDFDVVFEAVSNALLVVHYHRVVPYAPVKREQPKPAVKQDEQKPKRQASHWAVKPTAVGVHVPLPKKQEALEPAQSVPQQSLEEKAALTFGLFFSKGGGDESDAVILRKGKLFNRALNVPIDVKNTFVWAKIWDEASRRRGYFYVKDRAVKFFPIVRGRATIEDFIVNTAPGCDVALPRIELWSMRERAFVCTTKGWCWFNNERLRGEIYRRRCFSSSFSIGFLMHLGFRSLKVIRFAGTNILHMPSLNEERTFGWKGGDVYLPNVPKTAIVAGDRTRLGGEILASVANALNQEEVYSSVVSSITNRLVLRDQSALLSHLDTKLCDMFSQRDAMIREKPSHRCDVFLKPREREKLRELFPELSIQFSDSVRSSHPFANAMRSCFNGIFSRRCGNVCFFDIGGSFTYHVKAGHVNCHVCNPVLDVKDVKRRINEILFLSTAGGDSYVSSDLLTEAASKSVSYCSRESQNCDSRADAGFMVDVYDISPQQVAEAMDKKGALVFDIALMFPVELLYGNGEVYLEELDTLVKREGDYLAYNVGQCGEMYEHSFSNVSGFFTFSYVRTSSGNVFKLEYEGYRCGYHHLTMCRAQKSPGTEVTYRSLVPSFVGKSLVFIPVVAGSSVSFKTIVLDSDFVDRIYSYALNTIGTFENRTFEYAVGAVRSQKTHVITGSRVVHSKVDISPDDMWGLVVAVMAQAIKDRAKSIRSYNFIKASEGSLAGVFKLFFQTVGDCFSNAVSVYAKAMVHDNFNVLETLMSMPRAFIRKVPGSVVVTICTSGASDRLELRGAFDISKETFGRKLKNSRLRVFSRAIVEDSIKVMKAMKTEDGKPLPITEDSVYAFIMGNVSNVHCTRAGLLGGSKATVVSSVSKGLVARGAATKAFSGITSFFSTGSLFYDRGLTEDERLDALVRTENAINSPVGILETSRVAVSKVVAGTKEFWSEVSLNDFTTFVLRNKVLIGIFVASLGAAPIAWKYRRGIAANARRYAGSSYETLSSLSSQAAGGLRGLTSSTVSGGSLVVRRGFSSAVTVTRATVAKRQVPLALLSFSTSYAISGCSMLGIWAHALPRHLMFFFGLGTLLGARASANTWKFGGFSNNWCAVPEVVWRGKSVSSLLLPITLGVSLIIRGLLNDTIPQLAYVPPVEGRNVYDETLRYYRDFDYDEGAGPSGTQHEAVPGDDNDGSTSSVSSYDVVTNVRDVGISTNGEVTGEEETHSPRSVQYTYVEEEVAPSAAVAERQGDPSGSGTADAMAFVESVKKGVDDVFHQQSSGETAREVEVDGKGLLPESVVGEAPTQERGRAADGNTAQTAVNEGDREPVQSSLVSSPQADIPKVTQSEVHAQKEVKQEVPLATVSGATPIVDEKPAPSVTTRGVKIIDKGKAVAHVAEKKQVQVEQPKQRSLTINEGKAGKQLCMFRTCSCGVQLDVYNEATIATRFSNAFTFVDNLKGRSAVFFSKLGEGYTYNGGSHVSSGWPRALEDILTAIKYPSVFDHCLVQKYKMGGGVPFHADDEECYPSDNPILTVNLVGKANFSTKCRKGGKVMVINVASGDYFLMPCGFQRTHLHSVNSIDEGRISLTFRATRRVFGVGRMLQLAGGVSDEKSPGVPNQQPQSQGATRTITPKSGGKALSEGSGREVKGRSTYSIWCEQDYVRKCEWLRADNPVMALEPDYTPMTFEVVKTGTSEDAVVEYLKYLAIGIERTYRALLMARNIAVTTAEGVLKVPNQVYESLPGFHVYKSGTDLIFHSTQDGLRVRDLPYVLIAEKGIFTKGKDVDAVVALGDNLFVCDDILVFHDAINLIGALKVARCGMVGESFKSFEYKCYNAPPGGGKTTTLVDEFVKSPNSTATITANVGSSEDINMAVKKRDPNLEGLNSATTVNSRVVNFIVRGMYKRVLVDEVHMMHQGLLQLGVFATGASEGLFFGDINQIPFINREKVFRMDCAVFVPKKESVVYTSKSYRCPLDVCYLLSSMTVRGTEKCYPEKVVSGKDKPVVRSLSKRPIGTTDDVAEINADVYLCMTQLEKSDMKRSLKGKGKETPVMTVHEAQGKTFSDVVLFRTKKADDSLFTKQPHILVGLSRHTRSLVYAALSSKLDDKVGTYISDASPQSVSDALLTRSPRLVAFEVYERMNFGPTFEGELVRKIPTSHFVAVNGFLEDLLDGCPAFDYDFFEDDFETSDQSFLIEDVRISESFSHFTSKIEDRFYSFIRSSVGLPKRNTLKCNLVTFENRNFNADRGCNVGCDDSVAHELKEIFFEEVVNKARLAEVTESHLSSNTMLLSDWLDKRAPNAYKSLKRALGSFVFHPSMLTSYTLMVKADVKPKLDNTPLSKYVTGQNIVYHDRCVTALFSCIFTACVERLKYVVDERWLFYHGMDTAELAAALRNNLGDIRQYYTYELDISKYDKSQSALMKQVEELILLTLGVDREVLSTFFCGEYDSVVRTMTKELVLSVGSQRRSGGANTWLGNSLVLCTLLSVVLRGLDYSYIVVSGDDSLIFSRQPLDIDTSVLSDNFGFDVKIFNQAAPYFCSKFLVQVEDSLFFVPDPLKLFVKFGASKTSDIDLLHEIFQSFVDLSKGFNREDVIQELAKLVTRKYKHSGWTYSALCVLHVLSANFSQFCRLYYHNSVNLDVRPIQRTESLSLLALKARILRWKASRFAFSIKRG
|
2.1.1.-; 2.7.7.48; 3.4.22.-; 3.6.4.13
|
COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000255|PROSITE-ProRule:PRU00805}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-ProRule:PRU00805};
|
DNA-templated transcription [GO:0006351]; proteolysis [GO:0006508]; RNA processing [GO:0006396]; viral RNA genome replication [GO:0039694]
| null |
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type peptidase activity [GO:0008234]; dioxygenase activity [GO:0051213]; metal ion binding [GO:0046872]; mRNA methyltransferase activity [GO:0008174]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]
|
PF03171;PF00978;PF01443;PF01660;
|
2.60.120.590;3.40.50.300;
|
SsRNA positive-strand viruses RNA-directed RNA polymerase family
| null | null |
CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; 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=3.6.4.13;
| null | null | null | null |
FUNCTION: RNA-dependent RNA polymerase replicates the viral genome. {ECO:0000305}.
|
Grapevine leafroll-associated virus 3 (isolate United States/NY1) (GLRaV-3) (Grapevine leafroll-associated closterovirus (isolate 109))
|
O71305
|
HBSAG_WMHBV
|
MGLNQSTFNPLGFFPSHQLDPLFKANAGSADWDKNPNKDPWPQAHDTAVGAFGPGLVPPHGGLLGWSSQAQGLSVTVPDTPPPPSTNRDKGRKPTPATPPLRDTHPQAMTWNTSSFQSYLQNPKVRGLYFPAGGSTSSIVNPVPTTASTTSSSFSTTGVPVSTMDITSSGFLGPLLALQAVFFLLTKILTMPQSLDSLWTSLNFLGGTPACPGLNSQSPTSSHSPTCCPPTCPGYRWMCLRRSIIFLFILLLCLIFLLVLLDYQGMLPVCPLLPTVTGTTTTTGPCRTCTPIVPGISSYPSCCCTKPTDGNCTCIPIPSSWAFAKFLWDWALARFSWLNSLLPFVQWFAGLSPTVWLLVIWMMWFWGPSLFSILSPFLPLLPLFFWLWAYI
| null | null |
caveolin-mediated endocytosis of virus by host cell [GO:0075513]; fusion of virus membrane with host endosome membrane [GO:0039654]; virion attachment to host cell [GO:0019062]
|
membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036]
| null |
PF00695;
| null |
Orthohepadnavirus major surface antigen family
|
PTM: Isoform M is N-terminally acetylated by host at a ratio of 90%, and N-glycosylated by host at the pre-S2 region. {ECO:0000250|UniProtKB:P03138, ECO:0000255|HAMAP-Rule:MF_04075}.; PTM: Myristoylated. {ECO:0000255|HAMAP-Rule:MF_04075}.
|
SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04075}.
| null | null | null | null | null |
FUNCTION: The large envelope protein exists in two topological conformations, one which is termed 'external' or Le-HBsAg and the other 'internal' or Li-HBsAg. In its external conformation the protein attaches the virus to cell receptors and thereby initiating infection. This interaction determines the species specificity and liver tropism. This attachment induces virion internalization predominantly through caveolin-mediated endocytosis. The large envelope protein also assures fusion between virion membrane and endosomal membrane. In its internal conformation the protein plays a role in virion morphogenesis and mediates the contact with the nucleocapsid like a matrix protein. {ECO:0000255|HAMAP-Rule:MF_04075}.; FUNCTION: The middle envelope protein plays an important role in the budding of the virion. It is involved in the induction of budding in a nucleocapsid independent way. In this process the majority of envelope proteins bud to form subviral lipoprotein particles of 22 nm of diameter that do not contain a nucleocapsid. {ECO:0000255|HAMAP-Rule:MF_04075}.
|
Woolly monkey hepatitis B virus (isolate Louisville) (WMHBV)
|
O72157
|
RDRP_SBMVA
|
MYHPGRSPSFLITLANVICAAILFDIHTGGYQPGSLIPIVAWMTPFVTLLWLSASFATYLYKYVRTRLLPEEKVARVYYTAQSAPYFDPALGVMMQFAPSHGGASIEVQVNPSWISLLGGSLKINGDDASNESAVLGSFYSSVKPGDEPASLVAIKSGPQTIGFGCRTKIDGDDCLFTANHVWNNSMRPTALAKRGKQVAIEDWETPLSCDHKMLDFVVVRVPKHVWSKLGVKATQLVCPSDKDAVTCYGGSSSDNLLSGTGVCSKVDFSWKLTHSCPTAAGWSGTPIYSSRGVVGMHVGFEDIGKLNRGVNAFYVSNYLLRSQETLPPELSVIEIPFEDVETRSYEFIEVEIKGRGKAKLGKREFAWIPESGKYWADDDDDSLPPPPKVVDGKMVWSSAQETVAEPLNLPAGGRVKALAALSQLAGYDFKEGEAASTRGMPLRFVGQSACKFRELCRKDTPDEVLRATRVFPELSDFSWPERGSKAELHSLLLQAGKFNPTGIPRNLEGACQNLLERYPASKSCYCLRGEAWSFDAVYEEVCKKAQSAEINEKASPGVPLSRLASTNKDLLKRHLELVALCVTERLFLLSEAEDLLDESPVDLVRRGLCDPVRLFVKQEPHASRKVREGRFRLISSVSLVDQLVERMLFGPQNQLEIAEWEHIPSKPGMGLSLRQQAKSLFDDLRVKHSRCPAAEADISGFDWSVQDWELWADVEMRIVLGGFGHKLAKAAQNRFSCFMNSVFQLSDGTLIEQQLPGIMKSGSYCTSSTNSRIRCLMAELIGSPWCIAMGDDSVEGWVDGAKDKYMRLGHTCKDYKPCATTISGRLYEVEFCSHVIREDRCWLASWPKTLFKYLSEGKWFFEDLERDVSSSPHWPRIRHYVVGNTPSPHKTNLQNQSPRYGEEVDKTTVNQGYSEHSGSPGHSIEEAQEPEAAPFCCEAASVYPGWGVHGPYCSGDYGSLT
|
2.7.7.48; 3.4.21.-
| null |
DNA-templated transcription [GO:0006351]; proteolysis [GO:0006508]; viral process [GO:0016032]
|
host cell membrane [GO:0033644]; membrane [GO:0016020]
|
nucleotide binding [GO:0000166]; RNA binding [GO:0003723]; RNA-dependent RNA polymerase activity [GO:0003968]; serine-type endopeptidase activity [GO:0004252]
|
PF02122;PF02123;
|
2.40.10.10;
| null |
PTM: The polyprotein is proteolytically cleaved into several chains by the viral protease.
|
SUBCELLULAR LOCATION: [N-terminal protein]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Replicase polyprotein P2AB]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48;
| null | null | null | null |
FUNCTION: [Serine protease]: Responsible for cleavages of polyprotein P2A and replicase polyprotein P2AB.; FUNCTION: [VPg]: Covalently attached to the 5' extremity of the genomic and subgenomic RNAs. It may serve as a primer for the replicase.; FUNCTION: [RNA-directed RNA polymerase]: Replicates the viral genome. {ECO:0000305}.
|
Southern bean mosaic virus (isolate Bean/United States/Arkansas) (SBMV)
|
O73556
|
POLG_HPE2W
|
METIKSIADMATGVTKTIDATINSVNEIITNTDNASGGDILTKVADDASNILGPNCYATTSEPENKDVVQATTTVNTTNLTQHPSAPTLPFTPDFSNVDTFHSMAYDTTTGSKNPNKLVRLTTHAWASTLQRGHQIDHVNLPVDFWDEQRKPAYGHAKYFAAVRCGFHFQVQVNVNQGTAGSALVVYEPKPVVDYDKDLEFGAFTNLPHVLMNLAETTQADLCIPYVADTNYVKTDSSDLGQLKVYVWTPLSIPSGSSNQVDVTILGSLLQLDFQNPRVYGQNVDIYDTAPSKPIPLRKTKYLTMSTKYKWTRNKVDIAEGPGSMNMANVLSTTAAQSVALVGERAFYDPRTAGSKSRFDDLVKISQLFSVMADSTTPSANHGIDQKGYFKWSANSDPQAIVHRNLVHLNLFPNLKVFENSYSYFRGSLIIRLSVYASTFNRGRLNGFFPNSSTDETSEIDNAIYTICDIGSDNSFEITIPYSFSTWMRKTHGKPIGLFQIEVLNRLTYNYSSPNEVYCIVQGKMGQDAKFFCPTGSLVTFQNSWGSQMDLTDPLCIEDSVEDCKQTITPTELGLTSAQDDGPLGNDKPNYFLNFKSMNVDIFTVSHTKVDNIFGRAWFAHVHDFTNDGLWRQGLEFPKEGHGALSLLFAYFTGELNIHVLFLSDRGFLRVGHTYDTETNRTNFLSSSGIITVPAGEQMTLSVPSYSNKPLRTVRSSNALGYLLCKPLLTGTSSGRIEIFLSLRCPNFFFPLPAPKPATRKYRGDLATWSDQSPYGRQGKKQLMKLAYLDRGFYKHYGIVVGDDVYQLDSDDIFKTALTGKAKFTKTRLTPDWVVEEECELDYFRIKYLESSVNSEHIFSVDNNCETIAKDIFGSHSLSQHQQIGLIGTILLTAGLMSTIKTPVNPTTIKEFFNHAIEGDEQGLSLLVQKCTTFFSSAATELLDNDLVKFIIKILVRILCYMVLYCHKPNILTTACLSTLLVMDVTSSSVLSPSCKALMQCLMDGDVKKLAEVVAESMSNTDDDEIKEQICDTVKYTKQILSNQGPFKGFNEISTAFRHIDWWIQTLLKIKDMVLSVFKPSVEKRAVEWLERNKEHVCSILDYASDIIVKSKDQTKMKTQEFYQRYNDCLSKFKPIMAMCFRSCHNSISNTVYRLFQELARIPNRMATQNDLIRVEPIGIWIQGEPGQGKSFLTHTLSKQLQKTCGLQGIYTNPTASEFMDGYDNQDIHLIDDLGQTRKERDIEMLCNCISSDPDIVPMAHLEEKGKFYTSKLVIATTNKPDFSSTVLLDSGALRRRFPYIMHIRAAKHYSKSGKLNVSQAMPHMSTGECWEVSKNGRDWETLKLKELIDKITVDYKERIANYNTWKKQLEDQTLDDLDDAVSYIKHNYPDAIPYIDEYLNIEMSTLIEQMEAFIEPKPSVFKCFASRVGDKIKEASREVVKWFSDKLKSMLNFVERNKAWLTVVSAVTSAIGILLLVTKIFKKEESKDERAYNPTLPVAKPKGTFPVSQREFKNEAPYDGQLEHIISQMAYITGSTTGHITHCAGYQHDEIILHGHSIKYLEQEEELTLHYKNKVFPIEQPSVTQVTLGGKPMDLAIVKCKLPFRFKKNSKYYTNKIGTESMLIWMTEQGIITKEVQRVHHSGGIKTREGTESTKTISYTVKSCKGMCGGLLISKVEGNFKILGMHIAGNGEMGVAIPFNFLKNDMSDQGIVTEVTPIQPMYINTKSQIHKSPVYGAVEVKMGPAVLSKSDTRLEEPVDCLVKKSASKYRVNKFQVNNELWQGVKACVKSKFREIFGVNGIVDMKTAILGTSHVNSMDLSTSAGYSFVKSGYKKKDLICLEPFSVSPMLEKLVQEKFHNLLKGNQITTIFNTCLKDELRKLDKIATGKTRCIEACEIDYCIVYRMIMMEIYDKIYQTPCYYSGLAVGINPYRDWHFMINALNDYNYEMDYSQYDGSLSSMLLWEAVQVLAYCHDSPDLVMQLHKPVIDSDHVVFNERWLIHGGMPSGSPCTTVLNSLCNLMMCIYTTNLISPGIDCLPIVYGDDVILSLDKEIEPERLQSIMAESFGAEVTGSRKDEPPSLKPRMEVEFLKRKPGYFPESTFIVGKLDTENMIQHLMWMKNFSTFKQQLQSYLMELCLHGKDTYQHYVKILNPYLKEWNIPVDDYEVVIGKLVPMVFD
|
2.7.7.48; 3.4.22.28; 3.6.1.15
|
COFACTOR: [RNA-directed RNA polymerase 3D-POL]: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P03300}; Note=Binds 2 magnesium ions that constitute a dinuclear catalytic metal center. The magnesium ions are not prebound but only present for catalysis. {ECO:0000250|UniProtKB:P03300};
|
DNA-templated transcription [GO:0006351]; induction by virus of host autophagy [GO:0039520]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; viral RNA genome replication [GO:0039694]; virion attachment to host cell [GO:0019062]
|
host cell cytoplasmic vesicle membrane [GO:0044162]; host cell nucleolus [GO:0044196]; membrane [GO:0016020]; T=pseudo3 icosahedral viral capsid [GO:0039618]
|
ATP binding [GO:0005524]; cysteine-type endopeptidase activity [GO:0004197]; metal ion binding [GO:0046872]; monoatomic ion channel activity [GO:0005216]; ribonucleoside triphosphate phosphatase activity [GO:0017111]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; structural molecule activity [GO:0005198]
|
PF06344;PF00548;PF06363;PF00680;PF00073;PF00910;
|
2.60.120.20;3.30.70.270;3.40.50.300;2.40.10.10;
|
Picornaviruses polyprotein family
|
PTM: VPg is uridylylated by the polymerase and is covalently linked to the 5'-end of genomic RNA. This uridylylated form acts as a nucleotide-peptide primer for the polymerase (By similarity). {ECO:0000250}.; PTM: Specific enzymatic cleavages yield mature proteins (By similarity). All cleavages are catalyzed by P3C (By similarity). {ECO:0000250|UniProtKB:Q8JV21}.
|
SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion {ECO:0000305}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion {ECO:0000250|UniProtKB:Q66578}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Protein 2A H-NC]: Host cytoplasm {ECO:0000250|UniProtKB:Q66578}. Host nucleus, host nucleolus {ECO:0000250|UniProtKB:Q66578}.; SUBCELLULAR LOCATION: [Protein 2B]: Host cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q66578}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q66578}; Cytoplasmic side {ECO:0000250|UniProtKB:Q66578}. Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum. {ECO:0000250|UniProtKB:Q66578}.; SUBCELLULAR LOCATION: [Protein 2C]: Host cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q66578}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q66578}; Cytoplasmic side {ECO:0000250|UniProtKB:Q66578}. Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum. {ECO:0000250|UniProtKB:Q66578}.; SUBCELLULAR LOCATION: [Protein 3A]: Host cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q66578}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q66578}; Cytoplasmic side {ECO:0000250|UniProtKB:Q66578}. Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum. {ECO:0000250|UniProtKB:Q66578}.; SUBCELLULAR LOCATION: [Viral protein genome-linked]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Protease 3C]: Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [RNA-directed RNA polymerase 3D-POL]: Host cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Probably localizes to the surface of intracellular membrane vesicles that are induced after virus infection as the site for viral RNA replication. These vesicles are derived from the endoplasmic reticulum (By similarity). {ECO:0000250}.
|
CATALYTIC ACTIVITY: [RNA-directed RNA polymerase 3D-POL]: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYTIC ACTIVITY: [Protein 2C]: 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; EC=3.6.1.15; Evidence={ECO:0000250|UniProtKB:P03300}; CATALYTIC ACTIVITY: [Protease 3C]: Reaction=Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.; EC=3.4.22.28; Evidence={ECO:0000255|PROSITE-ProRule:PRU01222};
| null | null | null | null |
FUNCTION: [Capsid protein VP0]: Forms an icosahedral capsid of pseudo T=3 symmetry together with capsid proteins VP1 and VP3 (By similarity). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity). Capsid proteins interact with host alpha-V/beta-3 integrin heterodimer to provide virion attachment target cell (By similarity). This attachment induces virion internalization predominantly through clathrin-mediated endocytosis (By similarity). Binds packaging signals present in the viral RNA (By similarity). {ECO:0000250|UniProtKB:Q66578, ECO:0000250|UniProtKB:Q8JV21}.; FUNCTION: [Capsid protein VP3]: Forms an icosahedral capsid of pseudo T=3 symmetry together with capsid proteins VP0 and VP1 (By similarity). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity). Capsid proteins interact with host alpha-V/beta-3 integrin heterodimer to provide virion attachment target cell (By similarity). This attachment induces virion internalization predominantly through clathrin-mediated endocytosis (By similarity). Binds packaging signals present in the viral RNA (By similarity). {ECO:0000250|UniProtKB:Q66578, ECO:0000250|UniProtKB:Q8JV21}.; FUNCTION: [Capsid protein VP1]: Forms an icosahedral capsid of pseudo T=3 symmetry together with capsid proteins VP0 and VP3 (By similarity). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity). Capsid proteins interact with host alpha-V/beta-3 integrin heterodimer to provide virion attachment target cell (By similarity). This attachment induces virion internalization predominantly through clathrin-mediated endocytosis (By similarity). Binds packaging signals present in the viral RNA (By similarity). {ECO:0000250|UniProtKB:Q66578, ECO:0000250|UniProtKB:Q8JV21}.; FUNCTION: [Protein 2A H-NC]: Is not a protease. {ECO:0000303|PubMed:34315275}.; FUNCTION: [Protein 2B]: Plays an essential role in the virus replication cycle by acting as a viroporin. Creates a pore in the host reticulum endoplasmic and as a consequence releases Ca2+ in the cytoplasm of infected cell. In turn, high levels of cytoplasmic calcium may trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication. {ECO:0000250|UniProtKB:P03300}.; FUNCTION: [Protein 2C]: Induces and associates with structural rearrangements of intracellular membranes. Displays RNA-binding, nucleotide binding and NTPase activities. May play a role in virion morphogenesis and viral RNA encapsidation by interacting with the capsid protein VP3. {ECO:0000250|UniProtKB:P03300}.; FUNCTION: [Protein 3A]: Localizes the viral replication complex to the surface of membranous vesicles (By similarity). It inhibits host cell endoplasmic reticulum-to-Golgi apparatus transport and causes the disassembly of the Golgi complex, possibly through GBF1 interaction (By similarity). This would result in depletion of MHC, trail receptors and IFN receptors at the host cell surface (By similarity). Plays an essential role in viral RNA replication by recruiting ACBD3 and PI4KB at the viral replication sites, thereby allowing the formation of the rearranged membranous structures where viral replication takes place (By similarity). {ECO:0000250|UniProtKB:P03300, ECO:0000250|UniProtKB:Q9YLG5}.; FUNCTION: [Viral protein genome-linked]: Acts as a primer for viral RNA replication and remains covalently bound to viral genomic RNA. VPg is uridylylated prior to priming replication into VPg-pUpU. The VPg-pUpU is then used as primer on the genomic RNA poly(A) by the RNA-dependent RNA polymerase to replicate the viral genome. Following genome release from the infecting virion in the cytoplasm, the VPg-RNA linkage is probably removed by host TDP2. During the late stage of the replication cycle, host TDP2 is excluded from sites of viral RNA synthesis and encapsidation, allowing for the generation of progeny virions. {ECO:0000250|UniProtKB:P03300}.; FUNCTION: [Protease 3C]: Cysteine protease that generates mature viral proteins from the precursor polyprotein (By similarity). In addition to its proteolytic activity, it binds to viral RNA, and thus influences viral genome replication. RNA and substrate bind cooperatively to the protease (By similarity). {ECO:0000250|UniProtKB:P03304, ECO:0000250|UniProtKB:P12296}.; FUNCTION: [RNA-directed RNA polymerase 3D-POL]: Replicates the viral genomic RNA on the surface of intracellular membranes. Covalently attaches UMP to a tyrosine of VPg, which is used to prime RNA synthesis. The positive stranded RNA genome is first replicated at virus induced membranous vesicles, creating a dsRNA genomic replication form. This dsRNA is then used as template to synthesize positive stranded RNA genomes. ss(+)RNA genomes are either translated, replicated or encapsidated. {ECO:0000250|UniProtKB:P03300}.
|
Human parechovirus 2 (strain Williamson) (HPeV-2) (Echovirus 23)
|
O73557
|
Z_LASSJ
|
MGNKQAKAPESKDSPRASLIPDATHLGPQFCKSCWFENKGLVECNNHYLCLNCLTLLLSVSNRCPICKMPLPTKLRPSAAPTAPPTGAADSIRPPPYSP
| null | null |
viral budding from plasma membrane [GO:0046761]; viral budding via host ESCRT complex [GO:0039702]
|
host cell perinuclear region of cytoplasm [GO:0044220]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion component [GO:0044423]
|
RNA binding [GO:0003723]; zinc ion binding [GO:0008270]
|
PF03854;
|
3.30.160.310;
|
Arenaviridae Z protein family
| null |
SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04087}. Host cytoplasm, host perinuclear region {ECO:0000255|HAMAP-Rule:MF_04087}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04087}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04087}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_04087}. Note=Mainly perinuclear. During budding, associates at the inner side of the plasma membrane of infected cells. {ECO:0000255|HAMAP-Rule:MF_04087}.
| null | null | null | null | null |
FUNCTION: Plays a crucial role in virion assembly and budding. Expressed late in the virus life cycle, it acts as an inhibitor of viral transcription and RNA synthesis by interacting with the viral polymerase L. Presumably recruits the NP encapsidated genome to cellular membranes at budding sites via direct interaction with NP. Plays critical roles in the final steps of viral release by interacting with host TSG101, a member of the vacuolar protein-sorting pathway and using other cellular host proteins involved in vesicle formation pathway. The budding of the virus progeny occurs after association of protein Z with the viral glycoprotein complex SSP-GP1-GP2 at the cell periphery, step that requires myristoylation of protein Z. Also selectively represses protein production by associating with host eIF4E. {ECO:0000255|HAMAP-Rule:MF_04087, ECO:0000269|PubMed:12970458, ECO:0000269|PubMed:14990716}.
|
Lassa virus (strain Mouse/Sierra Leone/Josiah/1976) (LASV)
|
O73673
|
GCR_PAROL
|
MDQGGLKRNCNRDDSLTFGETAVGVGSDTGDTAGSLLQPAAMHLPSPSSLPQLTVAPNGGAGTKDQGEFGGLFESPRGQCEGSEMKEGKIIRLQKRKHHLDIGMFNMEDNLSLLNQNISDLNRTSTSVISTSDTSVLGKLPLPNLFPQHIKQEGGFSLEKELGTYGGHTGGGPCDLDGNSGHLIEDTEIWQDLDLPNSLPEISDFELDSEVAHLDNILHDSSGGCGPDGSLLKETKVLVGNGGNCTDVNGTDQQHPLQHHQHQQQQHRHLLQHQQHQLHHQHQQPPSLLSSVMIKEEKDHDNSFIHIRTPGVVKQEKQENGSFCQSQCLQSSMSSLHGGGPMSSTMGAGAVPGYHYKASPSSTVGLQDQKPFGIFSNLPAVAESWTRGGRFGEPSGIQRGNDGLPSAAMSPFSVSFSSSSPRTGENSSSAVPGLSKPSGPTHKICLVCSDEASGCHYGVVTCGSCKVFFKRAVEGWRARQNTDGQHNYLCAGRNDCIIDKIRRKNCPACRFRKCLQAGMNLEARKNKKLIKMKVHRPTGSAEPISNMPVPVIPRMPQLVPTMLSVLKAIEPEIIYSGYDSTLPDTSTRLMTTLNRLGGQQVISAVKWAKSLPGFRNLHLDDQMTLLQCSWLFLMSFSLGWRSYEQCNGNMLCFAPDLVINKERMKLPFMTDQCEQMLKICNEFVRLQVSYDEYLCMKVLLLLSTVPKDGLKSQAVFDEIRMTYIKELGKAIVKREENASQNWQRFYQLTKLLDSMQEMVEGLLQICFYTFVNKTLSVEFPEMLAEIITNQIPKFKDGSVKPLLFHQK
| null | null |
cellular response to glucocorticoid stimulus [GO:0071385]; cellular response to steroid hormone stimulus [GO:0071383]; chromatin organization [GO:0006325]; positive regulation of transcription by RNA polymerase II [GO:0045944]
|
centrosome [GO:0005813]; cytoplasm [GO:0005737]; mitochondrion [GO:0005739]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; spindle [GO:0005819]
|
DNA-binding transcription factor activity [GO:0003700]; estrogen response element binding [GO:0034056]; nuclear glucocorticoid receptor activity [GO:0004883]; nuclear receptor activity [GO:0004879]; steroid binding [GO:0005496]; steroid hormone binding [GO:1990239]; zinc ion binding [GO:0008270]
|
PF02155;PF00104;PF00105;
|
3.30.50.10;1.10.565.10;
|
Nuclear hormone receptor family, NR3 subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P04150}. Nucleus {ECO:0000250|UniProtKB:P04150}. Mitochondrion {ECO:0000250|UniProtKB:P04150}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P04150}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P04150}. Note=After ligand activation, translocates from the cytoplasm to the nucleus. {ECO:0000250|UniProtKB:P04150}.
| null | null | null | null | null |
FUNCTION: Receptor for glucocorticoids (GC). Has a dual mode of action: as a transcription factor that binds to glucocorticoid response elements (GRE), both for nuclear and mitochondrial DNA, and as a modulator of other transcription factors. Affects inflammatory responses, cellular proliferation and differentiation in target tissues. Involved in chromatin remodeling. Plays a role in rapid mRNA degradation by binding to the 5' UTR of target mRNAs and interacting with PNRC2 in a ligand-dependent manner which recruits the RNA helicase UPF1 and the mRNA-decapping enzyme DCP1A, leading to RNA decay. Could act as a coactivator for STAT5-dependent transcription upon growth hormone (GH) stimulation and could reveal an essential role of hepatic GR in the control of body growth. Mediates glucocorticoid-induced apoptosis. Promotes accurate chromosome segregation during mitosis. May act as a tumor suppressor. May play a negative role in adipogenesis through the regulation of lipolytic and antilipogenic gene expression. {ECO:0000250|UniProtKB:P04150, ECO:0000250|UniProtKB:P06537}.
|
Paralichthys olivaceus (Bastard halibut) (Hippoglossus olivaceus)
|
O73682
|
VGFAA_DANRE
|
MNLVVYLIQLFLAALLHLSAVKAAHIPKEGGKSKNDVIPFMDVYKKSACKTRELLVDIIQEYPDEIEHTYIPSCVVLMRCAGCCNDEALECVPTETRNVTMEVLRVKQRVSQHNFQLSFTEHTKCECRPKAEVKAKKENHCEPCSERRKRLYVQDPLTCKCSCKFTQMQCKSRQLELNERTCRCEKPR
| null | null |
angioblast cell migration from lateral mesoderm to midline [GO:0035479]; angiogenesis [GO:0001525]; artery morphogenesis [GO:0048844]; blood vessel development [GO:0001568]; blood vessel endothelial cell proliferation involved in sprouting angiogenesis [GO:0002043]; branching involved in blood vessel morphogenesis [GO:0001569]; cardioblast migration to the midline involved in heart rudiment formation [GO:0003319]; central nervous system vasculogenesis [GO:0022009]; dorsal aorta development [GO:0035907]; endocardial progenitor cell migration to the midline involved in heart field formation [GO:0003262]; hemopoiesis [GO:0030097]; induction of positive chemotaxis [GO:0050930]; motor neuron axon guidance [GO:0008045]; phosphorylation [GO:0016310]; positive regulation of angiogenesis [GO:0045766]; positive regulation of cell division [GO:0051781]; positive regulation of endothelial cell proliferation [GO:0001938]; positive regulation of focal adhesion assembly [GO:0051894]; positive regulation of mast cell chemotaxis [GO:0060754]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of protein-containing complex assembly [GO:0031334]; pronephros development [GO:0048793]; regulation of angioblast cell migration involved in selective angioblast sprouting [GO:0035477]; regulation of heart contraction [GO:0008016]; regulation of vasculature development [GO:1901342]; response to glucose [GO:0009749]; response to hypoxia [GO:0001666]; sprouting angiogenesis [GO:0002040]; thyroid gland development [GO:0030878]; vascular endothelial growth factor receptor signaling pathway [GO:0048010]; vascular endothelial growth factor signaling pathway [GO:0038084]; vasculature development [GO:0001944]; vasculogenesis [GO:0001570]; venous blood vessel development [GO:0060841]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]; membrane [GO:0016020]
|
chemoattractant activity [GO:0042056]; growth factor activity [GO:0008083]; heparin binding [GO:0008201]; vascular endothelial growth factor receptor 1 binding [GO:0043183]; vascular endothelial growth factor receptor 2 binding [GO:0043184]; vascular endothelial growth factor receptor binding [GO:0005172]
|
PF00341;PF14554;
|
2.10.90.10;2.10.160.10;
|
PDGF/VEGF growth factor family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17698971}.
| null | null | null | null | null |
FUNCTION: Growth factor active in angiogenesis, vasculogenesis and endothelial cell growth. Induces endothelial cell proliferation, promotes cell migration, inhibits apoptosis, and induces permeabilization of blood vessels. Required for intersegmental vessel development in the tail during embryogenesis (PubMed:15305301). Acts both upstream of kdr and tie1 to stimulate endothelial cell differentiation, and upstream of gata1 to stimulate hematopoietic cell differentiation. {ECO:0000250|UniProtKB:P15692, ECO:0000269|PubMed:11578859, ECO:0000269|PubMed:15305301, ECO:0000269|PubMed:17698971}.
|
Danio rerio (Zebrafish) (Brachydanio rerio)
|
O73683
|
A4_TETFL
|
MGHSVAWLLLVAAASTLAAEVPTDVSMGLLAEPQVAMFCGKINMHINVQSGKWEPDPSGTKSCIGTKEGILQYCQEVYPELQITNVVEANQPVSIQNWCKKGRKQCRSHMHIVVPYRCLVGEFVSDALLVPDKCKFLHQERMNQCESHLHWHTVAKESCGDRAMNLHDYGMLLPCGIDRFRGVEFVCCPAEAERDMDSTEKDADDSDVWWGGADNDYSDNSMVREPEPAEQQEETRPSVVEEEEEGEVAQEDDEEEEEVLDTDQDGDGEEDHEAADDEEEEEDVDEIDAFGESDDVDADEPTTNVAMTTTTTTTTTESVEEVVRMFCWAHADTGPCTASMPSWYFDAVDGRTMYELMYGGCGGNMNNFESEEYCLSVCSSVVPTDMPSSPDAVDHYLETPADENEHAHFQKAKESLEAKHRERMSQVMREWEEAERQAKNLPRADKKIVIQRFQEKVEALEQEAASERQQLVETHMARVEALLNDRRRLALENYLTALQQDPPRPRHVFSLLKKYVRAEQKDRQHTLKHFEHVRMVDPKKAAQIRPQVLTHLRVIEERMNQSLGLLYKVPGVADDIQDQVELLQREQAEMAQQLANLQTDVRVSYGNDALMPDQELGDGQADLLPQEDTLGGVGFVHPESFNQLNTENQVEPVDSRPTFERGVPTRPVTGKSMEAVPELRMETEDRQSTEYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIATVIVITLVMLRKKQYTSIHHGIIEVDAAVTPEERHLSKMQQNGYENPTYKFFEQMQN
| null | null |
axonogenesis [GO:0007409]; central nervous system development [GO:0007417]
|
cell surface [GO:0009986]; early endosome [GO:0005769]; Golgi apparatus [GO:0005794]; Golgi-associated vesicle [GO:0005798]; membrane raft [GO:0045121]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]
|
heparin binding [GO:0008201]; serine-type endopeptidase inhibitor activity [GO:0004867]; signaling receptor activator activity [GO:0030546]; signaling receptor binding [GO:0005102]; transition metal ion binding [GO:0046914]
|
PF10515;PF12924;PF12925;PF02177;PF03494;PF00014;
|
6.10.250.1670;1.20.120.770;3.30.1490.140;3.90.570.10;4.10.410.10;2.30.29.30;
|
APP family
| null |
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
| null | null | null | null | null |
FUNCTION: Functional neuronal receptor which couples to intracellular signaling pathway through the GTP-binding protein G(O). {ECO:0000250}.
|
Tetraodon fluviatilis (Green pufferfish) (Chelonodon fluviatilis)
|
O73689
|
ZIC1_XENLA
|
MLLDAGAQYPAIGVTTFGSSRHHSAGDVTDREVALGINPFADGMGAFKLNPSSHDLASGQTAFTSQAPGYAAAALGHHHHPGHVSSYSSAAFNSTRDFLFRNRGFGEAASAQHSLFASAAGGFPGPHGPHADTTGHLIFPGLHEQAASHASPNVVNGQMRLGFSGDMYGRPDQYGQVTSPRSEHYASSQLHGYGPMNMNMAAHHGAGAFFRYMRQPIKQELICKWIEPEQLANPKKSCNKTFSTMHELVTHVTVEHVGGPEQSNHICVWEECPREGKPFKAKYKLINHIRVHTGEKPFPCPFPGCGKVFARSENLKIHKRTHTGEKPFKCEFEGCDRRFANSSDRKKHMHVHTSDKPYLCKMCDKSYTHPSSLRKHMKVHEASSQGSQPSPAASSGYESSTPPTIVSPSAENQSTSSLSPSSSAVHHTSNHSTLSSNFNEWYV
| null | null |
dorsal/ventral neural tube patterning [GO:0021904]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neural crest cell differentiation [GO:0014033]; neural crest cell fate commitment [GO:0014034]; neural crest formation [GO:0014029]; neural plate development [GO:0001840]; neurogenesis [GO:0022008]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of protein import into nucleus [GO:0042307]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of Wnt signaling pathway [GO:0030177]; Wnt signaling pathway [GO:0016055]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
DNA-binding transcription factor activity [GO:0003700]; 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]
|
PF00096;PF18366;
|
3.30.160.60;
|
GLI C2H2-type zinc-finger protein family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9655809}. Cytoplasm {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Transcriptional activator that induces expression of multiple genes including pax3, en2, snai2/slug, feb and a subset of wnt genes. Has multiple key roles in the regulation of neural induction and neurogenesis: acts as a neural competence factor, sensitizing the presumptive neuroectoderm to respond to subsequent neuralizing signals. Promotes both preplacodal cell fates and neural crest cell fates, two of the cell populations that arise from the neural plate border. Cooperates with pax3 in concert with wnt signaling to determine neural crest fate. Synergizes with the bmp-inhibitor noggin/nog and acts through the wnt pathway to induce expression of en2. May bind to the minimal GLI-consensus sequence 5'-TGGGTGGTC-3'. {ECO:0000269|PubMed:15843410, ECO:0000269|PubMed:16871635, ECO:0000269|PubMed:16892174, ECO:0000269|PubMed:17409353, ECO:0000269|PubMed:9435279, ECO:0000269|PubMed:9655809, ECO:0000269|PubMed:9739105}.
|
Xenopus laevis (African clawed frog)
|
O73693
|
EGR1_TAEGU
|
CDRRFSRSDELTRHIRIHTGQKPFQCRICMRNFSRSDHLTTHIRTHTGEKPFACDICGRKFARSDERKRHTKIHLRQKDKKVEKAAPASTASPIPAYSSSVTTSYPSSITTTYPSPVRTAYSSPAPSSYPSPVHTTFPSPSIATTYPSGTATFQTQVATSFSSPGVANNFSSQVTSALSDINSAFSPRTIEIC
| null | null |
cellular response to interleukin-8 [GO:0098759]; circadian regulation of gene expression [GO:0032922]; interleukin-1-mediated signaling pathway [GO:0070498]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of protein sumoylation [GO:0033233]; response to auditory stimulus [GO:0010996]; transcription by RNA polymerase II [GO:0006366]
|
cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; double-stranded methylated DNA binding [GO:0010385]; hemi-methylated DNA-binding [GO:0044729]; histone acetyltransferase binding [GO:0035035]; promoter-specific chromatin binding [GO:1990841]; 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]; transcription cis-regulatory region binding [GO:0000976]; zinc ion binding [GO:0008270]
|
PF11914;PF00096;
|
3.30.160.60;
|
EGR C2H2-type zinc-finger protein family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P18146}. Cytoplasm {ECO:0000250|UniProtKB:P18146}.
| null | null | null | null | null |
FUNCTION: Transcriptional regulator. Recognizes and binds to the DNA sequence 5'-GCG(T/G)GGGCG-3'(EGR-site) in the promoter region of target genes (By similarity). Binds double-stranded target DNA, irrespective of the cytosine methylation status (By similarity). Regulates the transcription of numerous target genes, and thereby plays an important role in regulating the response to growth factors, DNA damage, and ischemia. Plays a role in the regulation of cell survival, proliferation and cell death. Mediates responses to ischemia and hypoxia; regulates the expression of proteins that are involved in inflammatory processes (By similarity). Plays a role in regulating the expression of circadian clock genes (By similarity). {ECO:0000250|UniProtKB:P08046, ECO:0000250|UniProtKB:P18146}.
|
Taeniopygia guttata (Zebra finch) (Poephila guttata)
|
O73700
|
CAC1D_CHICK
|
MQHHQQQQPEQHPEEANYASSTRIPLPGDGPTTQSNSSAPSKQTVLSWQAAIDAARQAKAAQNMNTTTAQPVGSLSQRKRQQYAKSKKQGNTSNSRPPRALFCLSLNNPIRRACISLVEWKPFDIFILLSIFANCVALAVYIPFPEDDSNSTNHNLEKVEYAFLIIFTVETFLKIIAYGLLLHPNAYVRNGWNLLDFVIVVVGLFSVILEQLTKETEGGSHSGGKPGGFDVKALRAFRVLRPLRLVSGVPSLQVVLNSIIKAMVPLLHIALLVLFVIIIYAIIGLELFIGKMHKSCFLIDSDILVEEDPAPCAFSGNGRQCVMNGTECKGGWVGPNGGITNFDNFAFAMLTVFQCITMEGWTDVLYWVNDAIGCEWPWIYFVSLIILGSFFVLNLVLGVLSGEFSKEREKAKARGDFQKLREKQQLEEDLKGYLDWITQAEDIDPENDEEADEEGKRNRVTLADLMEEKKKSRLSCFGRSSNKHASMPTSETESVNTENVSGEGENPACCGSLCQTISKSKFSRRWRRWNRFNRRKCRAAVKSVTFYWLVIVLVFLNTLTISSEHYNQPDWLTQIQDIANKVLLALFTCEMLVKMYSLGLQAYFVSLFNRFDCFVVCGGIVETILVELEIMSPLGISVFRCVRLLRIFKVTRHWASLSNLVASLLNSMKSIASLLLLLFLFIIIFSLLGMQLFGGKFNFDETQTKRSTFDNFPQALLTVFQILTGEDWNAVMYDGIMAYGGPSSSGMIVCIYFIILFICGNYILLNVFLAIAVDNLADAESLNTAQKEEAEEKERKKNARKESLENKKSEKSEGDQKKPKDSKVTIAEYGEGEDEDKDPYPPCDVPVGEDEEDEEDEPEVPAGPRPRRISELNMKEKITPIPEGSAFFIFSSTNPIRVGCHRLINHHIFTNLILVFIMLSSVSLAAEDPIRSHSFRNNILGYADYVFTSMFTFEIILKMTAFGAFLHKGSFCRNYFNLLDLLVVGVSLVSFGIQSSAISVVKILRVLRVLRPLRAINRAKGLKHVVQCVFVAIRTIGNIMIVTTLLQFMFACIGVQLFKGKFYKCTDEAKQNPEECRGIYIVYKDGDVDNPMVKERVWQNSDFNFDNVLSAMMALFTVSTFEGWPALLYKAIDSNGENVGPVYNYRVEISIFFIIYIIIIAFFMMNIFVGFVIVTFQEQGEQEYKNCELDKNQRQCVEYALKARPLRRYIPKNPYQYKFWYVVNSTGFEYIMFVLIMLNTLCLAMQHYGQSKLFNDAMDIMNMVFTGVFTVEMVLKLIAFKPKIFVRKKERWLGYFSDAWNTFDSLIVIGSIVDVVLSEADPKPTETVTTDESGNSEDSARISITFFRLFRVMRLVKLLSRGEGIRTLLWTFIKSFQALPYVALLIAMLFFIYAVIGMQVFGKVAMRDNNQINRNNNFQTFPQAVLLLFRCATGEAWQEIMLACLPGKRCDPESDYNPGEEYTCGSNFAIIYFISFYMLCAFLIINLFVAVIMDNFDYLTRDWSILGPHHLDEFKRIWSEYDPEAKGRIKHLDVVTLLRRIQPPLGFGKLCPHRVACKRLVAMNMPLNSDGTVMFNATLFALVRTALKIKTEGNLEQANEELRAVIKKIWKKTSMKLLDQVVPPAGDDEVTVGKFYATFLIQDYFRKFKKRKEQGLVGKYPAKNTTIALQAGLRTLHDIGPEIRRAISCDLQDDEPEENNPDEEEEVYKRNGALFGNHINHISSDRRDSFQQINTTHRPLHVQRPSIPSASDTEKNIYPHTGNSVYHNHHNHNSVGKQVPNSTNANLNNANVSKVVHGKHANFGSHEHRSENGYHSYSRADHEKRRRPSSRRTRYYETYIRSDSGDGRRPTICREERDIRDYCNDDHYLGEQEYYSGEEYYEEDSMLSGNRHVYDYHCRHHCHDSDFERPKGYHHPHGFFEEDDSQTCYDTKRSPRRRLLPPTPASNRRSSFNFECLRRQSSQDDIPLSPNFHHRTALPLHLMQQQVMAVAGLDSSKAHKHSPSRSTRSWATPPATPPNRDHTPYYTPLIQVDRAESTEHMNGSLPSLHRSSWYTDDPDISYRTFTPANLTVPNDFRHKHSDKQRSADSLVEAVLISEGLGRYAKDPKFVSATKHEIADACDMTIDEMESAASNLLNGNISNGTNGDMFPILSRQDYELQDFGPGYSDEEPEPGRYEEDLADEMICITSL
| null | null |
calcium ion import across plasma membrane [GO:0098703]
|
voltage-gated calcium channel complex [GO:0005891]
|
high voltage-gated calcium channel activity [GO:0008331]; metal ion binding [GO:0046872]
|
PF08763;PF16885;PF16905;PF00520;
|
1.10.287.70;6.10.250.2180;6.10.250.2500;1.20.120.350;
|
Calcium channel alpha-1 subunit (TC 1.A.1.11) family, CACNA1D subfamily
| null |
SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
| null | null | null | null | null |
FUNCTION: The isoform alpha-1D gives rise to L-type calcium currents. Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group.
|
Gallus gallus (Chicken)
|
O73707
|
CAC1C_CHICK
|
ALIVVGSIVDIAITEVNNAEENSRISITFFRLFRVMRLVKLLSRGEGIRTLLWTFIKSFQALPYVALLIVMLFFIYAVIGMQVFGKIALNDTTEINRNNNFQTFPQAVLLLFRCATGEAWQEIMLACLPDKKCDPDSEPANSTEADHSCGSSFAVFYFISFYMLCAFLIIDLFVAVI
| null | null |
calcium ion import across plasma membrane [GO:0098703]; calcium ion transmembrane transport [GO:0070588]; calcium ion transmembrane transport via high voltage-gated calcium channel [GO:0061577]; calcium ion transport into cytosol [GO:0060402]; cardiac conduction [GO:0061337]; regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion [GO:0010881]
|
dendrite [GO:0030425]; L-type voltage-gated calcium channel complex [GO:1990454]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; postsynaptic density membrane [GO:0098839]; sarcolemma [GO:0042383]; T-tubule [GO:0030315]
|
calmodulin binding [GO:0005516]; high voltage-gated calcium channel activity [GO:0008331]; voltage-gated calcium channel activity [GO:0005245]
|
PF00520;
|
1.10.287.70;1.20.120.350;
|
Calcium channel alpha-1 subunit (TC 1.A.1.11) family, CACNA1C subfamily
|
PTM: Phosphorylation by PKA activates the channel. {ECO:0000250|UniProtKB:P15381}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P22002}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P22002}. Perikaryon {ECO:0000250|UniProtKB:P22002}. Postsynaptic density membrane {ECO:0000250|UniProtKB:P22002}. Cell projection, dendrite {ECO:0000250|UniProtKB:P22002}. Cell membrane, sarcolemma, T-tubule {ECO:0000250|UniProtKB:Q01815}. Note=The interaction between RRAD and CACNB2 promotes the expression of CACNA1C at the cell membrane. {ECO:0000250|UniProtKB:P15381}.
| null | null | null | null | null |
FUNCTION: Pore-forming, alpha-1C subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents. Mediates influx of calcium ions into the cytoplasm, and thereby triggers calcium release from the sarcoplasm. Plays an important role in excitation-contraction coupling in the heart. Required for normal heart development and normal regulation of heart rhythm (By similarity). Required for normal contraction of smooth muscle cells in blood vessels and in the intestine. Essential for normal blood pressure regulation via its role in the contraction of arterial smooth muscle cells (By similarity). Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group (By similarity). {ECO:0000250|UniProtKB:P15381, ECO:0000250|UniProtKB:Q01815, ECO:0000250|UniProtKB:Q13936}.
|
Gallus gallus (Chicken)
|
O73727
|
INS_DANRE
|
MAVWLQAGALLVLLVVSSVSTNPGTPQHLCGSHLVDALYLVCGPTGFFYNPKRDVEPLLGFLPPKSAQETEVADFAFKDHAELIRKRGIVEQCCHKPCSIFELQNYCN
| null | null |
glucose homeostasis [GO:0042593]; glucose metabolic process [GO:0006006]; negative regulation of feeding behavior [GO:2000252]; positive regulation of pancreatic A cell differentiation [GO:2000228]; positive regulation of protein secretion [GO:0050714]; response to glucose [GO:0009749]; response to nutrient levels [GO:0031667]; type B pancreatic cell differentiation [GO:0003309]
|
extracellular space [GO:0005615]
|
hormone activity [GO:0005179]; insulin receptor binding [GO:0005158]
|
PF00049;
|
1.10.100.10;
|
Insulin family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver.
|
Danio rerio (Zebrafish) (Brachydanio rerio)
|
O73754
|
GREM1_XENLA
|
MNCLVYALGSLFLLSGLLLPSSEGKKKVSGSQGAIPPPDKGQPNDSEQGQAQPGDRVRGKGKGQALAAEEVLESSQEALHVTERKYLKRDWCKTQPLKQTIHEDGCNSRTIINRFCYGQCNSFYIPRHIRREEGSFQSCSFCKPKKFTTMVVTLNCPELQPPTKKKRITRVKQCRCISIDLD
| null | null |
animal organ morphogenesis [GO:0009887]; determination of dorsal identity [GO:0048263]; nervous system development [GO:0007399]; neural crest cell development [GO:0014032]; neural crest formation [GO:0014029]; pronephric duct development [GO:0039022]; sequestering of BMP from receptor via BMP binding [GO:0038098]; sequestering of BMP in extracellular matrix [GO:0035582]; somite rostral/caudal axis specification [GO:0032525]
|
extracellular space [GO:0005615]
|
BMP binding [GO:0036122]; cytokine activity [GO:0005125]; morphogen activity [GO:0016015]
|
PF03045;
|
2.10.90.10;
|
DAN family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Cytokine that has an axial patterning activity. Acts like BMP antagonist in embryonic explants. Blocks the BMP2 activity. {ECO:0000269|PubMed:9660951}.
|
Xenopus laevis (African clawed frog)
|
O73755
|
GREM1_CHICK
|
MVRTLYAIGAVFLLTGFLLPTAEGRKRNRGSQGAIPPPDKDQPNDSEQMQTQQQSGSRHRERGKGTSMPAEEVLESSQEALHITERKYLKRDWCKTQPLKQTIHEEGCNSRTIINRFCYGQCNSFYIPRHVRKEEGSFQSCSFCKPKKFTTMTVTLNCPELQPPRKKKRITRVKECRCISIDLD
| null | null |
animal organ morphogenesis [GO:0009887]; cardiac muscle cell differentiation [GO:0055007]; cardiac muscle cell myoblast differentiation [GO:0060379]; cell migration involved in sprouting angiogenesis [GO:0002042]; cell morphogenesis [GO:0000902]; cell-cell signaling [GO:0007267]; collagen fibril organization [GO:0030199]; determination of dorsal identity [GO:0048263]; embryonic limb morphogenesis [GO:0030326]; limb development [GO:0060173]; mesenchymal to epithelial transition involved in metanephros morphogenesis [GO:0003337]; negative regulation of apoptotic process [GO:0043066]; negative regulation of bone mineralization involved in bone maturation [GO:1900158]; negative regulation of bone remodeling [GO:0046851]; negative regulation of bone trabecula formation [GO:1900155]; 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 osteoblast differentiation [GO:0045668]; negative regulation of osteoblast proliferation [GO:0033689]; negative regulation of osteoclast proliferation [GO:0090291]; negative regulation of SMAD protein signal transduction [GO:0060392]; positive regulation of angiogenesis [GO:0045766]; positive regulation of branching involved in ureteric bud morphogenesis [GO:0090190]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of non-canonical NF-kappaB signal transduction [GO:1901224]; positive regulation of peptidyl-tyrosine autophosphorylation [GO:1900086]; positive regulation of receptor internalization [GO:0002092]; positive regulation of transcription by RNA polymerase II [GO:0045944]; proximal/distal pattern formation [GO:0009954]; regulation of epithelial to mesenchymal transition [GO:0010717]; regulation of focal adhesion assembly [GO:0051893]; sequestering of BMP from receptor via BMP binding [GO:0038098]; ureteric bud formation [GO:0060676]
|
cell surface [GO:0009986]; extracellular space [GO:0005615]
|
BMP binding [GO:0036122]; cytokine activity [GO:0005125]; protein homodimerization activity [GO:0042803]; receptor ligand activity [GO:0048018]; transmembrane receptor protein tyrosine kinase activator activity [GO:0030297]; vascular endothelial growth factor receptor 2 binding [GO:0043184]
|
PF03045;
|
2.10.90.10;
|
DAN family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Cytokine that may play a role in the development of the medial pallium and during optic nerve and pecten development by modulating BMP signaling. {ECO:0000269|PubMed:14991724}.
|
Gallus gallus (Chicken)
|
O73790
|
SPB10_CHICK
|
MEQVSASIGNFTVDLFNKLNETNRDKNIFFSPWSISSALALTYLAAKGSTAREMAEVLHFTEAVRAESSSVARPSRGRPKRRRMDPEHEQAENIHSGFKELLTAFNKPRNNYSLRSANRIYVEKTYALLPTYLQLSKKYYKAEPQKVNFKTAPEQSRKEINTWVEKQTESKIKNLLSSDDVKATTRLILVNAIYFKAEWEVKFQAEKTSIQPFRLSKNKSKPVKMMYMRDTFPVLIMEKMNFKMIELPYVKRELSMFILLPDDIKDGTTGLEQLERELTYERLSEWADSKMMTETLVDLHLPKFSLEDRIDLRDTLRNMGMTTAFTTNADFRGMTDKKDLAISKVIHQSFVAVDEKGTEAAAATAVIISFTTSVINHVLKFKVDHPFHFFIRHNKSKTILFFGRFCCPVE
| null | null |
chromatin organization [GO:0006325]; chromosome condensation [GO:0030261]; nucleate erythrocyte maturation [GO:0043362]
|
chromatin [GO:0000785]; extracellular space [GO:0005615]; nucleoplasm [GO:0005654]
|
chromatin DNA binding [GO:0031490]; serine-type endopeptidase inhibitor activity [GO:0004867]
|
PF00079;
|
2.30.39.10;3.30.497.10;
|
Serpin family, Ov-serpin subfamily
| null |
SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Associated with chromatin.
| null | null | null | null | null |
FUNCTION: DNA-binding protein that promotes DNA condensation into transcriptionally inactive heterochromatin in terminally differentiated avian blood cells. Promotes tight packing of nucleosomes into spherical clusters by binding to linker DNA and subsequent oligomerization. Acts as a cysteine protease inhibitor towards CTSL (cathepsin L1) and CTSV (cathepsin L2), but does not inhibit serine proteases. {ECO:0000269|PubMed:10026180, ECO:0000269|PubMed:11821386, ECO:0000269|PubMed:12930828, ECO:0000269|PubMed:16810322, ECO:0000269|PubMed:9446625}.
|
Gallus gallus (Chicken)
|
O73791
|
TIE2_DANRE
|
MCLLDSCTALLLLGCWMSGSAVRISDVTLVNPDPVVSPLTAPSLLCVSSDWSSGGSVLALGQEFPRPQGSVLALGQEFPHTEPRPHPAAATVTWSSRSHAFGAFYCQIRNSTGRKIYTYKMLQEAAFLPESLTITVNQGENINISYSRRLYSPEDTVIHKNGHFEHSSPKEDISDIIHYPVTNAKAESHAGIYAIRYISAAPSSAAITRLIVRSCRAGFWGPNCTESCPRCANGGVCDDTTGECVCPPGFRGHTCDIVCGEGRFGAGCKERCVDGVCRALVFCLRDPYGCSCASGWRGLSCNDACPDGYYGAGCTQKCVCAKGRCDRFRGCVCAGRHGSRCEEADSSPVISHLRDVEINTGVELSVNCSASGRPAPLHGDITLITANRTTIAAVDTHTLNDQSTSVFRVQQVRVSSAGRWRCQVNNTHMQVEDEFTVEVKVPPRPQNPPVLQGSGPRHLLLLLNTEPYSGDGPIATTTLLYRPASAHTWSSVTAHGPLVRLDNLYPMTQYLTQVQLSRPGPGGAGQAGPAATFSTQVLELPVGVKLSAVSQTALLLSWDIAPAEQHCTYEVSCLQAGAPGTLRTFQLPSNSSAMHLSDLKPRHKYQCTVRSSCGVGQNHPSASAWTLSDQLPPPPANISIWNISDTSAVLTWAVAEGESVSRAVIRFQQVEQAQYRQQVELPVQTQQLHMRFQLLGLRPNTGYQLQLWTVNNMGESAESPPVSLMTLPQQESSALFAAHGHLLLYAILGSAGMTCCTVLLAFCIVLQLKRNTLQRRIHSILREEPAVHFSSAPPPHRRSAVVSRSLVFPALQWSDIQFQDVLGEGNFGQVLKARIRKDGLRMDAAVKRMKDYASQDDHRDFAGELEVLCRLGPHKNIIHLLGACEHRGYLYLAIEFAPHGNLLDFLRKSRVLETDPAFAIAHRTASTLSSQQLLAFSADVARGMSYLSQKQFIHRDLAARNVLVGENFVAKIADFGLSRGQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEVVSLGGTPYCGMTCAELYEKLPLGFRLEKPLNCDDEVYELMQQCWREKPFERPSFSQILLSLGRMLEERKTYVNTTLYEKFTYAGIDCSAEEAG
|
2.7.10.1
| null |
angiogenesis [GO:0001525]; endothelial cell proliferation [GO:0001935]; heart development [GO:0007507]; phosphorylation [GO:0016310]; positive regulation of angiogenesis [GO:0045766]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]
|
cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; focal adhesion [GO:0005925]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]
|
ATP binding [GO:0005524]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]
|
PF00041;PF00047;PF10430;PF07714;
|
2.60.40.10;2.170.300.10;1.10.510.10;
|
Protein kinase superfamily, Tyr protein kinase family, Tie subfamily
|
PTM: Autophosphorylated on tyrosine residues in response to ligand binding. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Autophosphorylation occurs in a sequential manner, where Tyr-984 in the kinase activation loop is phosphorylated first, followed by autophosphorylation at additional tyrosine residues. Phosphorylation is important for interaction with scaffold proteins and effectors.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q02763}; Single-pass type I membrane protein {ECO:0000255}. Cell junction {ECO:0000250|UniProtKB:Q02763}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q02763}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Recruited to cell-cell contacts in quiescent endothelial cells (By similarity). Colocalizes with the actin cytoskeleton and at actin stress fibers during cell spreading. Recruited to the lower surface of migrating cells, especially the rear end of the cell (By similarity). {ECO:0000250|UniProtKB:Q02763}.
|
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: Tyrosine-protein kinase that acts as a cell-surface receptor for angiopoietins and regulates angiogenesis, endothelial cell survival, proliferation, migration, adhesion and cell spreading, reorganization of the actin cytoskeleton, but also maintenance of vascular quiescence. Can activate or inhibit angiogenesis, depending on the context. Angiopoietin signaling triggers receptor dimerization and autophosphorylation at specific tyrosine residues that then serve as binding sites for scaffold proteins and effectors (By similarity). {ECO:0000250}.
|
Danio rerio (Zebrafish) (Brachydanio rerio)
|
O73792
|
TIE1_DANRE
|
QLLQFAADVATGMHYLSDKQFIHRDLAARNVLVGDNLVAKIADFGLSRGEEVYVKKTMGRLPVRWMAIESLNYSVYTTKSDVWSFGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRMEQPRNCDDEVYELMRQCWRDRPYERPPFSQISVQLNRMQEARKAYVNMALFENFTYAGIDATAEEA
|
2.7.10.1
| null |
angiogenesis [GO:0001525]; blood vessel development [GO:0001568]; endothelial cell-cell adhesion [GO:0071603]; heart development [GO:0007507]; phosphorylation [GO:0016310]; positive regulation of angiogenesis [GO:0045766]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]; vasculature development [GO:0001944]
|
plasma membrane [GO:0005886]; receptor complex [GO:0043235]
|
ATP binding [GO:0005524]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]
|
PF07714;
|
1.10.510.10;
|
Protein kinase superfamily, Tyr protein kinase family, Tie subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {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=2.7.10.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
| null | null | null | null |
FUNCTION: Transmembrane tyrosine-protein kinase (Probable). Required for the formation of facial lymphatic structures and brain lymphatic endothelial cells (PubMed:37097004). Also required for embryonic ventral and dorsal migration of parachordal lymphoblasts along the arterial intersegmental vessel (PubMed:37097004). Plays a role in the embryonic formation of the dorsal longitudinal anastomotic vessel (PubMed:37097004). {ECO:0000269|PubMed:37097004, ECO:0000305}.
|
Danio rerio (Zebrafish) (Brachydanio rerio)
|
O73798
|
IGF1R_XENLA
|
MKAELVPVCTAWILGLLLCLGPAAAKVCGPNMDIRNDVSELKQLRDCVVIEGYLQILLISNAKAEDFRNLRFPNLTVITDYLLLFRVSGLVSLSNLFPNLTVIRGRVLFYNYALVIFEMTDLKEIGLYNLRNITRGAVRIEKNSELCYVSTVDWSLVLDAVYNNYIVGNKPPKECVDLCPGAREKMQICEKSSINNEFADRCWSDEHCQKVCPSVCGKRACSDNNECCHPECLGSCTAPDNDTACVACHHYFYEGRCVPTCPSNTYKFEGWRCITREVCAKMHIWIHSTIPFIIHKGECVYECPSGYMLNKSQSMTCSPCEGPCPKICEEKMKTIDSVTSAQMLEGCTVLKGNLQLNIRKGQNIAAELENFLGLIETVTGYVKIRHSHALVSLSFLKSLRYILGEEQMPGNYSFYVFDNNNLQQLWDWSKHNLTIKEGKIRFAFNSKLCASEIYRMEEVTGTKGRQAEEDISLSTNGNMASCESHVLNFTSRSKIKNRIKLTWERYRPPDYRDLISFTVYYKEAPFRNVTEYDGQDACGSNSWNMVDVDLPASKESDPGILLQGLKPWTQYAIYVKAITLTMLENRHIHGAKSKIIYMRTDAAVPSIPQDMISASNSSSQLVVKWNPPSLPNGNLSYYIVRWQQQPQDRHLYQYNYCFKDKVPNRKYANGTIDTEGGTEPTKPEGSVGEKGHYCACPKTEAEEKAEKDEAEYRKVFENFLHNSIFVPRPNRRRRDVLAVGNSTVTSYEKNSTTEDFSNFSDSERDDIEYPFYETKVDYKWERTVISNLQPFTLYRIDIHSCNHEAEKLGCSASNFVFARTMPAAGADDIPGIVNTKEEDDGVIFLGWPEPLRPNGLILMYEIEYKHQGEVHRECVSRQDYRKNGGIKLVRLPPGNYSAQVQAISLYGNGSWTEMVSFCVKLKPDVRNNILQMVVAIPLALSFLLVGIISIVCFVFKKRNSNRLGNGVLYASVNPEYFSAAEMYVPDKWEVPREKITMNRELGQGSFGMVYEGIAKGVVKDEAETKVAIKTVNEAASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQGQPTLVIMELMTRGDLKSYLRSLRPDTESNSGQPTPSLKKMIQMAGEIADGMSYLNANKFVHRDLAARNCMVTEDFTVKIGDFGMTRDIYETDYYRKGGKGLLPVRWMSPESLKDGVFTTNSDVWSFGVVLWEIATLAEQPYQGMSNEQVLRFVMEGGLLEKPDNCPDMLFELMRMCWQFNPKMRPSFLEIISSIKDELDPGFKEVSFFYSEENKPPDTEELDLEAENMESIPLDPSCALQNSEHHAGHKSENGPGVVVLRASFDERQPYAHMNGGRKNERALPLPQSSAC
|
2.7.10.1
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
|
cellular response to glucose stimulus [GO:0071333]; insulin-like growth factor receptor signaling pathway [GO:0048009]; oocyte maturation [GO:0001556]; positive regulation of MAPK cascade [GO:0043410]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; protein autophosphorylation [GO:0046777]; regulation of JNK cascade [GO:0046328]
|
axon [GO:0030424]; insulin receptor complex [GO:0005899]; plasma membrane [GO:0005886]
|
ATP binding [GO:0005524]; insulin receptor activity [GO:0005009]; insulin receptor substrate binding [GO:0043560]; insulin-like growth factor binding [GO:0005520]; insulin-like growth factor receptor activity [GO:0005010]; metal ion binding [GO:0046872]; phosphatidylinositol 3-kinase binding [GO:0043548]; protein tyrosine kinase activity [GO:0004713]; structural molecule activity [GO:0005198]
|
PF00757;PF07714;PF01030;
|
2.60.40.10;3.80.20.20;1.10.510.10;
|
Protein kinase superfamily, Tyr protein kinase family, Insulin receptor subfamily
|
PTM: The cytoplasmic domain of the beta subunit is autophosphorylated on Tyr residues in response to low concentrations of insulin-like growth factor (IGF 1) and higher concentrations of insulin.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1847619}; Single-pass type I membrane protein {ECO:0000269|PubMed:1847619}. Note=Expressed at the oocyte surface.
|
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, ECO:0000269|PubMed:9492024};
| null | null | null | null |
FUNCTION: This receptor binds insulin-like growth factor 1 (IGF1) with a high affinity and IGF2 with a lower affinity. It has a tyrosine-protein kinase activity, which is necessary for the activation of the IGF1-stimulated downstream signaling cascade. Plays a role in oocyte maturation. Promotes head development by inhibiting Wnt signaling during embryogenesis. {ECO:0000269|PubMed:11944947, ECO:0000269|PubMed:1847619, ECO:0000269|PubMed:9492024}.
|
Xenopus laevis (African clawed frog)
|
O73810
|
DRD2_MELGA
|
MDPLNLSWYNTGDRNWSEPVNESSADQKPQYNYYAVLLTLLIFVIVFGNVLVCMAVSREKALQTTTNYLIVSLAVADLLVATLVMPWVVYLEVVGEWRFSRIHCDIFVTLDVMMCTASILNLCAISIDRYTAAAMPMLYNTRYSSKRRVTVMIACVWVLSFAISSPILFGLNKADERECIIANPAFVVYSSVVSFYVPFIVTLLVYVQIYMVLRRRRKRHTKRSSHGLDSDTHAPLKDKCTHPENVKLGTVIVKSNGSFQVNKRKCEAESHIKMEMEMMSSTSPPERTIVKAAAPSNHQLVVPVASSRSTLDSPGKVEKNGHAKENLHTAKVFEIQSMPNGKTRSTLLKAMNRRKLSQQKEKKATQMLAIVLGVFIICWLPFFITHILNMHCDCNIPPAMYSAFTWLGYVNSAVNPIIYTTFNIEFRKAFMKILHC
| null | null |
adenylate cyclase-activating adrenergic receptor signaling pathway [GO:0071880]; adenylate cyclase-inhibiting dopamine receptor signaling pathway [GO:0007195]; hyaloid vascular plexus regression [GO:1990384]; negative regulation of calcium ion transport into cytosol [GO:0010523]; negative regulation of peptide hormone secretion [GO:0090278]; negative regulation of synaptic transmission, glutamatergic [GO:0051967]; phospholipase C-activating dopamine receptor signaling pathway [GO:0060158]; regulation of dopamine secretion [GO:0014059]; regulation of potassium ion transport [GO:0043266]
|
glutamatergic synapse [GO:0098978]; Golgi membrane [GO:0000139]; plasma membrane [GO:0005886]
|
dopamine binding [GO:0035240]; dopamine neurotransmitter receptor activity, coupled via Gi/Go [GO:0001591]; G protein-coupled receptor activity [GO:0004930]; signaling receptor activity [GO:0038023]
|
PF00001;
|
1.20.1070.10;
|
G-protein coupled receptor 1 family
|
PTM: Palmitoylated. Palmitoylation which is required for proper localization to the plasma membrane and stability of the receptor could be carried on by ZDHHC4, ZDHHC3 and ZDHHC8. {ECO:0000250|UniProtKB:P14416}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P14416}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P14416}; Multi-pass membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Dopamine receptor whose activity is mediated by G proteins which inhibit adenylyl cyclase (By similarity). Positively regulates postnatal regression of retinal hyaloid vessels via suppression of VEGFR2/KDR activity, downstream of OPN5 (By similarity). {ECO:0000250|UniProtKB:P14416, ECO:0000250|UniProtKB:P61168}.
|
Meleagris gallopavo (Wild turkey)
|
O73864
|
WNT11_DANRE
|
MTEYRNFLLLFITSLSVIYPCTGISWLGLTINGSSVGWNQTHHCKLLDGLVPDQQQLCKRNLELMHSIVRAARLTKSACTSSFSDMRWNWSSIESAPHFTPDLAKGTREAAFVVSLAAAVVSHAIARACASGDLPSCSCAAMPSEQAAPDFRWGGCGDNLRYYGLQMGSAFSDAPMRNRRSGPQDFRLMQLHNNAVGRQVLMDSLEMKCKCHGVSGSCSVKTCWKGLQDISTISADLKSKYLSATKVIPRQIGTRRQLVPREMEVRPVGENELVYLVSSPDYCTQNAKQGSLGTTDRQCNKTASGSESCGLMCCGRGYNAYTEVLVERCQCKYHWCCYVSCKTCKRTVERYVSK
| null | null |
camera-type eye development [GO:0043010]; canonical Wnt signaling pathway [GO:0060070]; cell fate commitment [GO:0045165]; cell migration [GO:0016477]; cell migration involved in gastrulation [GO:0042074]; cell-cell adhesion [GO:0098609]; central nervous system development [GO:0007417]; convergent extension [GO:0060026]; convergent extension involved in axis elongation [GO:0060028]; convergent extension involved in gastrulation [GO:0060027]; embryonic eye morphogenesis [GO:0048048]; establishment of mitotic spindle orientation [GO:0000132]; eye field cell fate commitment involved in camera-type eye formation [GO:0060898]; gastrulation with mouth forming second [GO:0001702]; heart development [GO:0007507]; heart looping [GO:0001947]; Kupffer's vesicle development [GO:0070121]; mediolateral intercalation [GO:0060031]; mesodermal cell migration [GO:0008078]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of cell growth [GO:0030308]; negative regulation of cell migration [GO:0030336]; negative regulation of DNA-templated transcription [GO:0045892]; neural plate morphogenesis [GO:0001839]; neuroendocrine cell differentiation [GO:0061101]; neuron differentiation [GO:0030182]; non-canonical Wnt signaling pathway [GO:0035567]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of GTPase activity [GO:0043547]; positive regulation of protein kinase C signaling [GO:0090037]; positive regulation of stress fiber assembly [GO:0051496]; protein localization [GO:0008104]; protein localization to cell surface [GO:0034394]; protein phosphorylation [GO:0006468]; regulation of endocytosis [GO:0030100]; secondary palate development [GO:0062009]; signal transduction [GO:0007165]
|
cytoplasm [GO:0005737]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]
|
cytokine activity [GO:0005125]; frizzled binding [GO:0005109]; GTPase activator activity [GO:0005096]; protein heterodimerization activity [GO:0046982]; protein kinase activator activity [GO:0030295]
|
PF00110;
|
3.30.2460.20;
|
Wnt family
|
PTM: Palmitoleoylation is required for efficient binding to frizzled receptors. Depalmitoleoylation leads to Wnt signaling pathway inhibition. {ECO:0000250|UniProtKB:P27467, ECO:0000250|UniProtKB:P56704}.
|
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix.
| null | null | null | null | null |
FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors. May play a role in the formation of dermal structure in limb buds. Is likely to signal over only few cell diameters (By similarity). {ECO:0000250}.
|
Danio rerio (Zebrafish) (Brachydanio rerio)
|
O73872
|
SODC_DANRE
|
MVNKAVCVLKGTGEVTGTVYFNQEGEKKPVKVTGEITGLTPGKHGFHVHAFGDNTNGCISAGPHFNPHDKTHGGPTDSVRHVGDLGNVTADASGVAKIEIEDAMLTLSGQHSIIGRTMVIHEKEDDLGKGGNEESLKTGNAGGRLACGVIGITQ
|
1.15.1.1
|
COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250}; Note=Binds 1 copper ion per subunit. {ECO:0000250}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250};
|
neuron cellular homeostasis [GO:0070050]; removal of superoxide radicals [GO:0019430]; response to metal ion [GO:0010038]; response to methylmercury [GO:0051597]; response to xenobiotic stimulus [GO:0009410]
|
cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; peroxisome [GO:0005777]
|
copper ion binding [GO:0005507]; superoxide dismutase activity [GO:0004784]
|
PF00080;
|
2.60.40.200;
|
Cu-Zn superoxide dismutase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:18421; EC=1.15.1.1;
| null | null | null | null |
FUNCTION: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
|
Danio rerio (Zebrafish) (Brachydanio rerio)
|
O73874
|
EFNB2_DANRE
|
MGDSLWRYYFGVLVIACKVNLSRALILDSIYWNTTNTKFVPGQGLVLYPQIGDKMDIVCPRVEGGSMEGVEYYKLYMVPLEQLKSCQVTKADTPLLNCVKPDQDVKFTLKFQEFSPNLWGLEFFRGKDYYIISTSNGTMEGLDNQEGGVCKTKSMKIIMKVGQNPSDPISPKDYPTSYPPKHPDLGGKDSKSNEVLKPDASPHGEDKGDGNKSSSVIGSEVALFACIASASVIVIIIIIMLVFLLLKYRRRHRKHSPQHATTLSLSTLATPKRGGSGGNNNGSEPSDIIIPLRTADSVFCPHYEKVSGDYGHPVYIVQEMPPQSPANIYYKV
| null | null |
angioblast cell migration involved in selective angioblast sprouting [GO:0035475]; anterior/posterior pattern specification [GO:0009952]; axon guidance [GO:0007411]; axon target recognition [GO:0007412]; blood vessel development [GO:0001568]; blood vessel morphogenesis [GO:0048514]; cell adhesion [GO:0007155]; cell migration involved in sprouting angiogenesis [GO:0002042]; ephrin receptor signaling pathway [GO:0048013]; optic vesicle morphogenesis [GO:0003404]; regulation of chemotaxis [GO:0050920]; rhombomere boundary formation [GO:0021654]; somitogenesis [GO:0001756]; synaptic target recognition [GO:0008039]
|
glutamatergic synapse [GO:0098978]; plasma membrane [GO:0005886]; presynaptic membrane [GO:0042734]
|
ephrin receptor binding [GO:0046875]
|
PF00812;
|
2.60.40.420;
|
Ephrin family
|
PTM: Inducible phosphorylation of tyrosine residues in the cytoplasmic domain. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P52799}; Single-pass type I membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Cell surface transmembrane ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Together with ephb4 may play a central role in heart morphogenesis and angiogenesis through regulation of cell adhesion and cell migration (By similarity). {ECO:0000250}.
|
Danio rerio (Zebrafish) (Brachydanio rerio)
|
O73875
|
EPB4A_DANRE
|
MELFSRNVAAFWIILLEFLLGSVAEEEVLMNTKTETSDLKWTTHSRSKPEWEEVSGLDEENNSVRTYQICQADGSSSHWLRSKLIERRGASQVYVELFFTMVECSSRNTHHRSCKETFNLYYYQSDTDDATATHPAWMENPYTKVDTVAADFLLRKGGEKKVNVKTLRLGPLSKRGFYLAFQAQGACMALLSVRVFFKKCPALTRSLSVFPETVPRSLVQEAVGQCVANAAQPGPSPRPPKMFCGEDGQWVDQPTTTCTCLPGFEASHGELECRACPVGLFKMGSGTGPCSVCPENSQTGETGSAACVCRSGFYRALSDSADTPCTRPPSSPRSPVPQVNDTSLTLEWSEPLDSGGRSDLSYSVECRMCSTPGSPCTLCSDGVNYRPSQTGIQGRRVSIWGLRPHTTYSFTVMALNGVSAQSQQGPAGETINITTSPNVPVLVSGLRKSTATESSLTLYWNTPTQSHYRILQYQIRYCEKERGSEENSCHYMESNNNEVVLSDLRRATQYEVQVRARTFAGYGSFGKAILFRTLPDEDDSSSPLLVTGILIAMGMLLLIIVIGAAIYCIRKQNNYKDPELSDKNGQYLMGQGVKVYIDPFTYEDPNEAVREFAKEIDVSCVKIEEVIGAGEFGEVCRGRLRIPGKKENYVAIKTLKGGYTDKQRRDFLAEASIMGQFQHPNIIHLEGIITASCPVMILTEFMENGALDSFLRLNDGQFTPIQLVGMLRGIASGMKYLSEMSYVHRDLAARNILVNSNLVCKVSDFGLSRFLQENSSDPTYTSSLGGKIPIRWTAPEAIAFRKFTCASDVWSYGIVMWEVMSFGERPYWDMSNQDVINAIEQDYRLPPPPDCPTYLHQLMLDCWQKERTARPRFANIVSALDKLIRNPASLKITAQEGAGPSHPLLDQRSPLTPSSCGTVGDWLRAIKMERYEETFLQAGYTSMQLVTHINTEDLLRLGITLAGHQKKILSSIEALGIQNKAPGNVLY
|
2.7.10.1
| null |
angioblast cell migration involved in selective angioblast sprouting [GO:0035475]; angiogenesis [GO:0001525]; axon guidance [GO:0007411]; blood vessel development [GO:0001568]; convergent extension [GO:0060026]; ephrin receptor signaling pathway [GO:0048013]; lymph vessel development [GO:0001945]; phosphorylation [GO:0016310]; venous blood vessel morphogenesis [GO:0048845]
|
dendrite [GO:0030425]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]
|
ATP binding [GO:0005524]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]; transmembrane-ephrin receptor activity [GO:0005005]
|
PF14575;PF01404;PF00041;PF07714;PF00536;
|
2.60.40.1770;2.60.120.260;2.60.40.10;1.10.150.50;1.10.510.10;2.10.50.10;
|
Protein kinase superfamily, Tyr protein kinase family, Ephrin receptor subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P54760}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P54760}.
|
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:PRU00159};
| null | null | null | null |
FUNCTION: Receptor tyrosine kinase which binds promiscuously transmembrane ephrin-B family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Together with its cognate ligand/functional ligand EFNB2 is involved in the regulation of cell adhesion and cell migration, and plays a central role in heart morphogenesis, angiogenesis and blood vessel remodeling and permeability (PubMed:29444212). EPHB4-mediated forward signaling controls cellular repulsion and segregation from EFNB2-expressing cells (By similarity) (PubMed:29444212). Involved in somitogenesis (PubMed:9765210). {ECO:0000250|UniProtKB:P54760, ECO:0000269|PubMed:29444212, ECO:0000269|PubMed:9765210}.
|
Danio rerio (Zebrafish) (Brachydanio rerio)
|
O73878
|
EPB4B_DANRE
|
MDRVCWIMALSWFWMVSTGLVSAEEEVLMNTKLETSDLRWTIYPSGDPEWEEMSGLDEEGNSVRTFQVCPMDSSVSHWLRTRFIPRHGASQVYVEIRFTMMECSAMPASFRTCKETFNLYYYQSDEDTASATHPAWMENPYSKVDTVAADFLLRRGGERKSNVKTVRVGPLSKKGFYLAFQTQGACMALLSVRVFFKKCPAVSRAFSSFPETLPHSLVQQAEGVCVDNSAPTGQSTAPPTMFCGEDGQWVGPPSSTCACKPGYEPVDSDRCRACGLGQYKASVGGSLCRVCPDNSNTHFAGSSLCVCRPGYHRATSDLPDSACTKPPSAPRSIIYQINDTVVTLEWSEPLDRGGRSDLSYSVECMHCRGSLCVQCADSITYRPGQMGVPGRRVIIRGLLPHTTYTFTVLAQNGVSAVSHTSPASSSVNITTSRDVAVPVSGIRRIKASESSVSISWTVPPQTQHSIQDYQLRYSLKGQDDGWQYVSSRSSSVVLNDLSRASQYQVQVRARTAAGYGHFSSAVSISTLPDDEESPSRLMLTGVLVAIGLLILIAVVIVAVFCFRRSTRRRDPDPDKSGQFLMGQGIKVYIDPFTYEDPNEAVREFAKEIDVSFVKIEEVIGAGEFGEVCRGRLKVPGKKENYVAIKTLKGGYTDKQRRDFLSEASIMGQFQHPNIIHLEGVITASCPVMILTEYMENGALDSFLRLNDGQFTPIQLVGMLRGIASGMKYLSEMSFVHRDLAARNILVNSNLVCKVSDFGLSRFLTENSSDPTYTSSLGGKIPIRWTAPEAIAFRKFTSASDVWSYGIVMWEVMSFGERPYWDMSNQDVINAIEQDYRLPPPPECPASLHQLMLDCWQKERSSRPRFCAIVSALDRLIRNPASLKITGRIPDGPSHPLLDQRAPPPLSHCSSVADWLRAIKMERYEDAFMQAGFTAIQHITHISTEDLLRIGVTLAGHQKKILSSVQTLRIHGGSLRY
|
2.7.10.1
| null |
angiogenesis [GO:0001525]; axon guidance [GO:0007411]; ephrin receptor signaling pathway [GO:0048013]; Kupffer's vesicle development [GO:0070121]; phosphorylation [GO:0016310]; somitogenesis [GO:0001756]
|
dendrite [GO:0030425]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]
|
ATP binding [GO:0005524]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]; transmembrane-ephrin receptor activity [GO:0005005]
|
PF14575;PF01404;PF00041;PF07714;PF00536;
|
2.60.40.1770;2.60.120.260;2.60.40.10;1.10.150.50;1.10.510.10;2.10.50.10;
|
Protein kinase superfamily, Tyr protein kinase family, Ephrin receptor subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P54760}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P54760}.
|
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:PRU00159};
| null | null | null | null |
FUNCTION: Receptor tyrosine kinase which binds promiscuously transmembrane ephrin-B family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Together with its cognate ligand/functional ligand EFNB2 is involved in the regulation of cell adhesion and cell migration, and plays a central role in heart morphogenesis, angiogenesis and blood vessel remodeling and permeability. EPHB4-mediated forward signaling controls cellular repulsion and segregation from EFNB2-expressing cells (By similarity). Involved in somitogenesis (PubMed:9765210). {ECO:0000250|UniProtKB:P54760, ECO:0000269|PubMed:9765210}.
|
Danio rerio (Zebrafish) (Brachydanio rerio)
|
O73885
|
HSP7C_CHICK
|
MSKGPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDSVVQSDMKHWPFTVVNDAGRPKVQVEYKGETKSFYPEEISSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQGTKDAGTIAGLNVLRIINEPTAAAIAYGLDKKVGAERNLLIFDLGGGTFDVSILTIENGIFEVKSTAGDTHLGGEDFDNRLVNHFIAEFKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRARFEKLNADLFRGTLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAILSGDKSENVQDLLLLDVTPLSLGIETAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVTFDIDANGILNVSAVDKSTGKENKITITNDKGRLSKEDIERMVQEAEKYKAEDEKQRDKVSSKNSLDSYAFNMKATVEDEKLPGKILDEDHQNILDKCNEIINWLDKNQTAEKEEFEHQQKELEKVCNPIITKLYQSAGGMPGGMPGGFPGGGAPPSGGASSGPTIEEVD
| null | null |
chaperone cofactor-dependent protein refolding [GO:0051085]; chaperone-mediated autophagy translocation complex disassembly [GO:1904764]; clathrin coat disassembly [GO:0072318]; embryo development ending in birth or egg hatching [GO:0009792]; embryonic organ development [GO:0048568]; gastrulation [GO:0007369]; late endosomal microautophagy [GO:0061738]; protein refolding [GO:0042026]; protein targeting to lysosome involved in chaperone-mediated autophagy [GO:0061740]; slow axonal transport [GO:1990832]
|
autophagosome [GO:0005776]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; lysosomal membrane [GO:0005765]; nucleolus [GO:0005730]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; postsynaptic cytosol [GO:0099524]; presynaptic cytosol [GO:0099523]; ribonucleoprotein complex [GO:1990904]; terminal bouton [GO:0043195]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein folding chaperone [GO:0140662]; clathrin-uncoating ATPase activity [GO:1990833]; heat shock protein binding [GO:0031072]; phosphoprotein binding [GO:0051219]; protein folding chaperone [GO:0044183]; protein-macromolecule adaptor activity [GO:0030674]
|
PF00012;
|
1.20.1270.10;3.30.30.30;3.30.420.40;
|
Heat shock protein 70 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P11142}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P11142}. Cell membrane {ECO:0000250|UniProtKB:P11142}. Lysosome membrane {ECO:0000250|UniProtKB:P11142}; Peripheral membrane protein {ECO:0000250|UniProtKB:P11142}; Cytoplasmic side {ECO:0000250|UniProtKB:P11142}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Translocates rapidly from the cytoplasm to the nuclei, and especially to the nucleoli, upon heat shock. {ECO:0000250|UniProtKB:P11142}.
| null | null | null | null | null |
FUNCTION: Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, chaperone-mediated autophagy, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes (By similarity). Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation (By similarity). This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones (By similarity). The affinity of HSP70 for polypeptides is regulated by its nucleotide bound state (By similarity). In the ATP-bound form, it has a low affinity for substrate proteins (By similarity). However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins (By similarity). HSP70 goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release (By similarity). Substrate recognition component in chaperone-mediated autophagy (CMA), a selective protein degradation process that mediates degradation of proteins with a -KFERQ motif: HSPA8/HSC70 specifically recognizes and binds cytosolic proteins bearing a -KFERQ motif and promotes their recruitment to the surface of the lysosome where they bind to lysosomal protein LAMP2 (By similarity). KFERQ motif-containing proteins are eventually transported into the lysosomal lumen where they are degraded (By similarity). May play a role in regulating apoptosis during embryonic development (PubMed:9707581). May play a role in uncoating of clathrin-coated vesicles (By similarity). {ECO:0000250|UniProtKB:P11142, ECO:0000250|UniProtKB:P19120, ECO:0000269|PubMed:9707581}.
|
Gallus gallus (Chicken)
|
O73888
|
HPGDS_CHICK
|
MPNYKLTYFNLRGRAEICRYLFAYAGIKYEDHRLEGADWPKIKPTIPFGKVPILEVDGVIIHQSLAIARYLARESGLAGQTPVEQALADAIVDTIDDFMMLFPWAEKNQDVKEKAFNDILTNKAPELLKDLDTFLGDKKWFVGKSVTWADFYWDVCSTTLLSYKADLADKYPRLLALRDRVEALPAIAAWIQKRPKTAI
|
2.5.1.18; 5.3.99.2
|
COFACTOR: Name=glutathione; Xref=ChEBI:CHEBI:57925; Evidence={ECO:0000269|PubMed:9657971}; Note=Glutathione is required for the prostaglandin D synthase activity. {ECO:0000269|PubMed:9657971};
|
glutathione metabolic process [GO:0006749]; prostaglandin biosynthetic process [GO:0001516]; prostaglandin metabolic process [GO:0006693]
|
cytoplasm [GO:0005737]
|
calcium ion binding [GO:0005509]; glutathione transferase activity [GO:0004364]; magnesium ion binding [GO:0000287]; prostaglandin-D synthase activity [GO:0004667]
|
PF14497;PF02798;
|
1.20.1050.10;3.40.30.10;
|
GST superfamily, Sigma family
| null |
SUBCELLULAR LOCATION: Cytoplasm.
|
CATALYTIC ACTIVITY: Reaction=prostaglandin H2 = prostaglandin D2; Xref=Rhea:RHEA:10600, ChEBI:CHEBI:57405, ChEBI:CHEBI:57406; EC=5.3.99.2; Evidence={ECO:0000269|PubMed:9657971}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10601; Evidence={ECO:0000305}; CATALYTIC ACTIVITY: Reaction=glutathione + RX = a halide anion + an S-substituted glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378, ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925, ChEBI:CHEBI:90779; EC=2.5.1.18; Evidence={ECO:0000269|PubMed:9657971}; CATALYTIC ACTIVITY: Reaction=2-glyceryl-prostaglandin H2 = 2-glyceryl-prostaglandin D2; Xref=Rhea:RHEA:51232, ChEBI:CHEBI:85166, ChEBI:CHEBI:133979; Evidence={ECO:0000250|UniProtKB:O60760}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51233; Evidence={ECO:0000250|UniProtKB:O60760};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=128 umol/min/mg enzyme with 1-bromo-2,4-dinitrobenzene as substrate {ECO:0000269|PubMed:9657971}; Vmax=97 umol/min/mg enzyme with 1-chloro-2,4-dinitrobenzene as substrate {ECO:0000269|PubMed:9657971}; Vmax=410 umol/min/mg enzyme with 1-fluoro-2,4-dinitrobenzene as substrate {ECO:0000269|PubMed:9657971}; Vmax=116 umol/min/mg enzyme with 1-iodo-2,4-dinitrobenzene as substrate {ECO:0000269|PubMed:9657971}; Vmax=67 umol/min/mg enzyme with 7-chloro-4-nitrobenz-2-oxa-1,3-diazole as substrate {ECO:0000269|PubMed:9657971}; Vmax=1.4 umol/min/mg enzyme with 4-nitrobenzyl chloride as substrate {ECO:0000269|PubMed:9657971}; Vmax=0.05 umol/min/mg enzyme with 1,2-dichloro-4-nitrobenzene as substrate {ECO:0000269|PubMed:9657971}; Vmax=0.04 umol/min/mg enzyme with ethacrynic acid as substrate {ECO:0000269|PubMed:9657971}; Vmax=2.8 umol/min/mg enzyme with 4-hydroxynon-2-enal as substrate {ECO:0000269|PubMed:9657971}; Vmax=0.06 umol/min/mg enzyme with trans,trans-deca-2,4-dienal as substrate {ECO:0000269|PubMed:9657971}; Vmax=0.02 umol/min/mg enzyme with trans-non-2-enal as substrate {ECO:0000269|PubMed:9657971}; Vmax=0.5 umol/min/mg enzyme with cumene hydroperoxide as substrate {ECO:0000269|PubMed:9657971}; Vmax=0.06 umol/min/mg enzyme with t-butyl hydroperoxide as substrate {ECO:0000269|PubMed:9657971}; Vmax=12.6 umol/min/mg enzyme with allyl isothiocyanate as substrate {ECO:0000269|PubMed:9657971}; Vmax=17.6 umol/min/mg enzyme with benzyl isothiocyanate as substrate {ECO:0000269|PubMed:9657971}; Vmax=0.02 umol/min/mg enzyme with Delta5-androstene-3,17-dione as substrate {ECO:0000269|PubMed:9657971}; Vmax=0.11 umol/min/mg enzyme with 4-nitrophenyl acetate as substrate {ECO:0000269|PubMed:9657971};
| null | null | null |
FUNCTION: Bifunctional enzyme which catalyzes both the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation, and the conjugation of glutathione with a wide range of aryl halides, organic isothiocyanates and alpha,beta-unsaturated carbonyls. Also exhibits low glutathione-peroxidase activity towards cumene hydroperoxide and t-butyl hydroperoxide. {ECO:0000269|PubMed:9657971}.
|
Gallus gallus (Chicken)
|
O73916
|
SIX3_ORYLA
|
MVFRAPLDFISASRLLLPHFADAPPVLSRSRSPEHPPAGFLSLALPGLCFSATQIASVCETLEETGDIERLARFLWSLPVNTDGRDSISEHESVQRARAVVAFHTGCYRELYRILETHRFTRASHSKLQAMWLEAHYREAEKLRGRPLGPVDKYRVRKKFPLPRTIWDGEQKTHCFKERTRGLLREWYLQDPYPNPGKKRELAHATGLTPTQVGNWFKNRRQRDRAAAAKNRLQHHRICPDSACTLSGGDSSERADGDTFLSVTDSDSDLDV
| null | null |
apoptotic process involved in development [GO:1902742]; cell proliferation in forebrain [GO:0021846]; epithelial cell maturation [GO:0002070]; eye development [GO:0001654]; forebrain dorsal/ventral pattern formation [GO:0021798]; lens development in camera-type eye [GO:0002088]; lens fiber cell apoptotic process [GO:1990086]; lens fiber cell differentiation [GO:0070306]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of neuron differentiation [GO:0045665]; neuroblast differentiation [GO:0014016]; neuroblast migration [GO:0097402]; optic vesicle morphogenesis [GO:0003404]; pituitary gland development [GO:0021983]; proximal/distal axis specification [GO:0009946]; regulation of cell cycle phase transition [GO:1901987]; regulation of cell population proliferation [GO:0042127]; regulation of neural precursor cell proliferation [GO:2000177]; regulation of neural retina development [GO:0061074]; regulation of neuroblast proliferation [GO:1902692]; regulation of transcription by RNA polymerase II [GO:0006357]; telencephalon development [GO:0021537]; telencephalon regionalization [GO:0021978]
|
nucleus [GO:0005634]; transcription regulator complex [GO:0005667]
|
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; transcription corepressor binding [GO:0001222]
|
PF00046;PF16878;
|
1.10.10.60;
|
SIX/Sine oculis homeobox family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q62233, ECO:0000255|PROSITE-ProRule:PRU00108}.
| null | null | null | null | null |
FUNCTION: Transcriptional regulator which can act as both a transcriptional repressor and activator by binding a ATTA homeodomain core recognition sequence on these target genes. During forebrain development represses WNT1 expression allowing zona limitans intrathalamica formation and thereby ensuring proper anterio-posterior patterning of the diencephalon and formation of the rostral diencephalon. Acts as a direct upstream activator of SHH expression in the rostral diencephalon ventral midline and that in turn SHH maintains its expression. In addition, Six3 activity is required for the formation of the telencephalon. During postnatal stages of brain development is necessary for ependymal cell maturation by promoting the maturation of radial glia into ependymal cells through regulation of neuroblast proliferation and migration. Acts on the proliferation and differentiation of neural progenitor cells through activating transcription of CCND1 and CCND2. During early lens formation plays a role in lens induction and specification by activating directly PAX6 in the presumptive lens ectoderm. In turn PAX6 activates SIX3 resulting in activation of PDGFRA and CCND1 promoting cell proliferation. Also is required for the neuroretina development by directly suppressing WNT8B expression in the anterior neural plate territory. Its action during retina development and lens morphogenesis is AES and TLE4-dependent manner. Furthermore, during eye development regulates several genes expression. Before and during early lens development represses the CRYGF promoter by binding a SIX repressor element. Directly activates RHO transcription, or cooperates with CRX or NRL. Six3 functions also in the formation of the proximodistal axis of the optic cup, and promotes the formation of optic vesicles-like structures. During pituitary development, acts in parallel or alternatively with HESX1 to control cell proliferation through Wnt/beta-catenin pathway. Plays a role in eye development by suppressing WNT1 expression and in dorsal-ventral patterning by repressing BMP signaling pathway. {ECO:0000250|UniProtKB:O42406, ECO:0000250|UniProtKB:O95343, ECO:0000250|UniProtKB:Q62233}.
|
Oryzias latipes (Japanese rice fish) (Japanese killifish)
|
O73925
|
KCNQ1_SQUAC
|
MSSEVKSRWSGSGSQKSGTARKPTMLEMAENAASRHYEPVPLPLQRSNSPDSSTDKNPESRAADSRAEVIINPDIPPKAIALPLSRYRGRNPFFSKVNIQGRTYNFLERPTGWKCFIYHFTVFLIVLVCLIFSVMSTIEQYHYFANRALVWMEIVLVVFFGTEYIVRLWSAGCRSKYVGFWGRLRFARKPISIIDLIVVVASVIVLCVGSNGQVFATSAIRGIRFLQILRMLHVDRQGGTWRLLGSVVFIHRQELITTLYIGFLGLIFSSYFVYLAEKDAVDDSGSQQFGSYADALWWGVVTVTTIGYGDKVPQTWIGRTIASCFSVFAISFFALPAGILGSGFALKVQQKQRQKHFNRQIPAAASLIQTSWRCHAAENHESATWKMYVRQPTKFYVASPSPKTKKSVGKRKKLKTDKDNGLNSEKSLNVPNITYDHVVDKDDRKFENSNIDGYDSSVKKSLGILDVNSGALSRANSYADDLDFIEGEPVLAPITHVSQLRESHRVTVKVIRRMQYFVAKKKFQQARKPYDVRDVIEQYSQGHLNLMVRIKELQRRLDQSLGKPTMFLSVSEKSQDRGKNTIGARLNRVEEKFVHMDQKLNTITDMLHHLVAHQQGHPHPQTQPQAQGTVVQAVASTHSSLPSYEQLTVRRKDQDNQPDL
| null | null |
inner ear development [GO:0048839]; intestinal absorption [GO:0050892]; membrane repolarization [GO:0086009]; regulation of gastric acid secretion [GO:0060453]; renal absorption [GO:0070293]
|
basolateral plasma membrane [GO:0016323]; cytoplasm [GO:0005737]; cytoplasmic vesicle membrane [GO:0030659]; endoplasmic reticulum [GO:0005783]; membrane raft [GO:0045121]; monoatomic ion channel complex [GO:0034702]; plasma membrane [GO:0005886]; voltage-gated potassium channel complex [GO:0008076]
|
calmodulin binding [GO:0005516]; delayed rectifier potassium channel activity [GO:0005251]; outward rectifier potassium channel activity [GO:0015271]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; voltage-gated potassium channel activity [GO:0005249]
|
PF00520;PF03520;
|
1.10.287.70;6.10.140.1910;1.20.120.350;
|
Potassium channel family, KQT (TC 1.A.1.15) subfamily, Kv7.1/KCNQ1 sub-subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P51787}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P51787}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P51787}. Membrane raft {ECO:0000250|UniProtKB:P51787}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P51787}. Basolateral cell membrane {ECO:0000250|UniProtKB:P51787}.
| null | null | null | null | null |
FUNCTION: Potassium channel that plays an important role in a number of tissues, including heart, inner ear, stomach and colon (By similarity). Associates with KCNE beta subunits that modulates current kinetics (By similarity). Induces a voltage-dependent by rapidly activating and slowly deactivating potassium-selective outward current (By similarity). Promotes also a delayed voltage activated potassium current showing outward rectification characteristic (By similarity). During beta-adrenergic receptor stimulation participates in cardiac repolarization by associating with KCNE1 to form the I(Ks) cardiac potassium current that increases the amplitude and slows down the activation kinetics of outward potassium current I(Ks) (By similarity). When associated with KCNE3, forms the potassium channel that is important for cyclic AMP-stimulated intestinal secretion of chloride ions (By similarity). When associated with KCNE2, forms a heterooligomer complex leading to currents with an apparently instantaneous activation, a rapid deactivation process and a linear current-voltage relationship and decreases the amplitude of the outward current (By similarity). When associated with KCNE4, inhibits voltage-gated potassium channel activity (By similarity). When associated with KCNE5, this complex only conducts current upon strong and continued depolarization (By similarity). {ECO:0000250|UniProtKB:P51787, ECO:0000250|UniProtKB:P97414, ECO:0000250|UniProtKB:Q9Z0N7}.
|
Squalus acanthias (Spiny dogfish)
|
O73932
|
IF23A_XENLA
|
MNKLYIGNLSENVSPTDLESLFKESKIPFTGQFLVKSGYAFVDCPDETWAMKAIDTLSGKVELHGKVIEVEHSVPKRQRSRKLQIRNIPPHLQWEVLDSLLAQYGTVENCEQVNTESETAVVNVTYANKEHARQGLEKLNGYQLENYSLKVTYIPDEMATPQAPSQQLQQQPQQQHPQGRRGFGQRGPARQGSPGAAARPKPQTEVPLRMLVPTQFVGAIIGKEGATIRNITKQTQSKIDIHRKENAGAAEKPITIHSTPEGCSAACKIIMEIMQKEAQDTKFTEEIPLKILAHNNFVGRLIGKEGRNLKKIEQDTDTKITISPLQDLTLYNPERTITVKGSIEPCAKAEEEIMKKIRESYENDIAAMNLQAHLIPGLNLNALGLFPSSSSGMPPPSVGVPSPTSSTSYPPFGQQPESETVHLFIPALAVGAIIGKQGQHIKQLSRFAGASIKIAPAEGPDAKLRMVIITGPPEAQFKAQGRIYGKLKEENFFGPKEEVKLETHIKVPSYAAGRVIGKGGKTVNELQNLTSAEVVVPRDQTPDENDEVVVKITGHFYASQLAQRKIQEILAQVRRQQQQQQKTVQSGQPQPRRK
| null | null |
mRNA transport [GO:0051028]; nervous system development [GO:0007399]; regulation of translation [GO:0006417]
|
cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:1990904]
|
DNA binding [GO:0003677]; mRNA 3'-UTR binding [GO:0003730]
|
PF00013;PF00076;
|
3.30.310.210;3.30.70.330;3.30.1370.10;
|
RRM IMP/VICKZ family
| null |
SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Endoplasmic reticulum. Note=Accumulates along the vegetal cortex in oocytes as oogenesis progresses ('late pathway' for RNA localization). Colocalizes with Vg1 RNA along the vegetal cortex.
| null | null | null | null | null |
FUNCTION: RNA-binding protein that acts as a regulator of mRNA transport and localization. Binds to the RNA sequence motif 5'-UUCAC-3'. Preferentially binds to N6-methyladenosine (m6A)-containing mRNAs and increases their stability (By similarity). Mediates the specific association of Vg1 RNA to microtubules. Binds specifically to the vegetal localization elements (VLE or VgLE) in the 3'-UTR of Vg1 and VegT mRNAs. Binds to the Vg1 and VegT mRNAs in both the nucleus and the cytoplasm. May regulate mRNA translation (By similarity). Acts as a transcription regulator (By similarity). Binds to the 5'-[TA]GGTTACT-3' motif within element 3 of the TFIIIA gene promoter (By similarity). {ECO:0000250|UniProtKB:O00425, ECO:0000250|UniProtKB:O57526, ECO:0000269|PubMed:15096527, ECO:0000269|PubMed:9148809, ECO:0000269|PubMed:9560341, ECO:0000269|PubMed:9620847}.
|
Xenopus laevis (African clawed frog)
|
O73946
|
HELS_PYRFU
|
MRVDELRVDERIKSTLKERGIESFYPPQAEALKSGILEGKNALISIPTASGKTLIAEIAMVHRILTQGGKAVYIVPLKALAEEKFQEFQDWEKIGLRVAMATGDYDSKDEWLGKYDIIIATAEKFDSLLRHGSSWIKDVKILVADEIHLIGSRDRGATLEVILAHMLGKAQIIGLSATIGNPEELAEWLNAELIVSDWRPVKLRRGVFYQGFVTWEDGSIDRFSSWEELVYDAIRKKKGALIFVNMRRKAERVALELSKKVKSLLTKPEIRALNELADSLEENPTNEKLAKAIRGGVAFHHAGLGRDERVLVEENFRKGIIKAVVATPTLSAGINTPAFRVIIRDIWRYSDFGMERIPIIEVHQMLGRAGRPKYDEVGEGIIVSTSDDPREVMNHYIFGKPEKLFSQLSNESNLRSQVLALIATFGYSTVEEILKFISNTFYAYQRKDTYSLEEKIRNILYFLLENEFIEISLEDKIRPLSLGIRTAKLYIDPYTAKMFKDKMEEVVKDPNPIGIFHLISLTPDITPFNYSKREFERLEEEYYEFKDRLYFDDPYISGYDPYLERKFFRAFKTALVLLAWINEVPEGEIVEKYSVEPGDIYRIVETAEWLVYSLKEIAKVLGAYEIVDYLETLRVRVKYGIREELIPLMQLPLVGRRRARALYNSGFRSIEDISQARPEELLKIEGIGVKTVEAIFKFLGKNVKISEKPRKSTLDYFLKS
|
5.6.2.4
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:15677450}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:15677450}; Note=Divalent cations, Mg(2+) and Zn(2+) are best. {ECO:0000269|PubMed:15677450};
|
DNA repair [GO:0006281]
| null |
3'-5' DNA helicase activity [GO:0043138]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; isomerase activity [GO:0016853]
|
PF00270;PF00271;PF21280;PF14520;
|
1.10.3380.30;1.10.150.20;3.40.50.300;
|
Helicase family, Hel308 subfamily
| null | null |
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:0000255|HAMAP-Rule:MF_00442, ECO:0000269|PubMed:16436047}; 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=5.6.2.4; Evidence={ECO:0000255|HAMAP-Rule:MF_00442, ECO:0000269|PubMed:16436047};
| null | null | null | null |
FUNCTION: DNA-dependent ATPase and 3'-5' DNA helicase that may be involved in repair of stalled replication forks. Unwinds the lagging strand from forked DNA structures in a 3'-5' direction. PCNA, the DNA polymerase sliding clamp subunit, stimulates the helicase activity, and may alter substrate specificity. Unwinds branched DNA (Holliday junctions) in an ATP-dependent fashion; ss- and dsDNA stimulate ATPase to the greatest extent, although it preferentially binds DNA with a single-stranded region. Processes a RecA-mediated recombination intermediate between gapped circular and homologous linear dsDNA. {ECO:0000255|HAMAP-Rule:MF_00442, ECO:0000269|PubMed:15677450, ECO:0000269|PubMed:16436047}.
|
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
|
O74113
|
CDC45_SCHPO
|
MFIKRSDYASAYLKIKEASVSGGCTVQLFVALDPDALCACKLLSTLLKGDFISHKIRPVSGYRDLEQANKTLLEQNEDIKFIILLNCGTMVDLNNYLVSMEDVSIYVIDSHRPHNLNNIYIENNIFVFDDGDIEEDMNKIHDAWYAFNSHELSDEENSDSSNEREEEVEDDNRSVESYSSSDYQARSRRRFSEETTQRRAEIKEKRKKRKEFASILSEYYEKGSWYGESITNILFAVASMLGREDNDMLWLAIVGLTCLEIHCQSSKKYFNRSYSLLKDEVNRLNPSPLENQIVGRAHGKTPHDQSIRLEDEFRFMLVRHWSLYDSMLHSAYVGSRLHIWSEEGRKRLHKLLAKMGLSLVECKQTYIHMNMDLKKTLKSSLKRFAPFYGLDDVIFHSFTRTYGFKCTLSASDVSYAISALLEMGNTGVLLQSKTVARSPDMTEEEYLEKFENAQNQEWLHNFYDAYDALDDVDSLERALKLAMHLQRAIVRTGITLLEKRAIKTLRSFRFGLINEGPDLKIFMHPLALTKMSLWIAEAINEQEREFGKLRHLPLVLAAFVEEKNRYLIVGTSTSAFTSNEDDDDDDGHGHNRFGVAFQEVANMTSATLQMDCFEASVIECQKSDLGVFLESLSFKTLL
| null | null |
DNA replication initiation [GO:0006270]; double-strand break repair via break-induced replication [GO:0000727]; mitotic DNA replication initiation [GO:1902975]; mitotic DNA replication preinitiation complex assembly [GO:1902977]; mitotic intra-S DNA damage checkpoint signaling [GO:0031573]
|
chromatin [GO:0000785]; cytosol [GO:0005829]; DNA replication preinitiation complex [GO:0031261]; nuclear replication fork [GO:0043596]; nucleus [GO:0005634]
|
chromatin binding [GO:0003682]; DNA replication origin binding [GO:0003688]; single-stranded DNA binding [GO:0003697]
|
PF02724;
| null |
CDC45 family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9619628}.
| null | null | null | null | null |
FUNCTION: Required for initiation of chromosomal DNA replication. May have a role in regulating the MCM proteins nda1 and nda4. {ECO:0000269|PubMed:9619628}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74135
|
CKI3_SCHPO
|
MSTTSSHSNVVGVHYRVGKKIGEGSFGMLFQGVNLINNQPIALKFESRKSEVPQLRDEYLTYKLLMGLPGIPSVYYYGQEGMYNLLVMDLLGPSLEDLFDYCGRRFSPKTVAMIAKQMITRIQSVHERHFIYRDIKPDNFLIGFPGSKTENVIYAVDFGMAKQYRDPKTHVHRPYNEHKSLSGTARYMSINTHLGREQSRRDDLESMGHVFMYFLRGSLPWQGLKAATNKQKYEKIGEKKQVTPLKELCEGYPKEFLQYMIYARNLGYEEAPDYDYLRSLFDSLLLRINETDDGKYDWTLLNNGKGWQYSAAKQHVVQRRHTQGTNNRRQSTIPPYARTRQNLLSSPSKQTPVNNVVDASVATQKDGIPGKAASPQVQQQQQTSSAQQQQPQRVEQPAPQTTQPTQVDTQQAAKPAPSKEKSRKKFHLRLLSCCISKQE
|
2.7.11.1
| null |
endocytosis [GO:0006897]; negative regulation of establishment of bipolar cell polarity [GO:1904846]; negative regulation of protein localization to cell tip [GO:1903067]; phosphorylation [GO:0016310]; regulation of endocytosis [GO:0030100]; signal transduction [GO:0007165]
|
cell division site [GO:0032153]; cell periphery [GO:0071944]; cell tip [GO:0051286]; cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, CK1 Ser/Thr protein kinase family, Casein kinase I subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm.
|
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: Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74184
|
WAT1_SCHPO
|
MSVQYPPQHSVLLVSSGYDHTIRFWEALSGICSRTIQHADSQVNRLCISPDKKFLAAAGNPHVRLYDINTSSQMPLMTFEGHTNNVTAIAFHCDGKWLATSSEDGTVKVWDMRAPSVQRNYDHKSPVNDLLIHPNQGELLSCDQSGRVRAWDLGENSCTHELIPEEDVPMSSITVGSDGSMLIAGNNKGNCYVWRMLNHQGASLLQPVVKFQAHQRYITRCVLSPDVKHLATCSADATVNIWSTEDMSFMLERRLQGHQRWVWDCAFSADSTYLVTASSDHVARLWELSSGETIRQYSGHHKAAVCVALNDYQI
| null | null |
meiotic cell cycle [GO:0051321]; regulation of actin cytoskeleton organization [GO:0032956]; sporulation resulting in formation of a cellular spore [GO:0030435]; TOR signaling [GO:0031929]; TORC1 signaling [GO:0038202]; TORC2 signaling [GO:0038203]
|
cytosol [GO:0005829]; fungal-type vacuole membrane [GO:0000329]; nucleus [GO:0005634]; TORC1 complex [GO:0031931]; TORC2 complex [GO:0031932]
| null |
PF00400;
|
2.130.10.10;
|
WD repeat LST8 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
| null | null | null | null | null |
FUNCTION: component of both TORC1 and TORC2, which regulate multiple cellular processes to control cell growth in response to environmental signals. Nutrient limitation and environmental stress signals cause inactivation of TORC1. Active TORC1 positively controls cell growth and ribosome biogenesis by regulating ribosomal protein gene expression. TORC1 negatively controls G1 cell-cycle arrest, sexual development and amino acid uptake. Represses mating, meiosis and sporulation efficiency by interfering with the functions of the transcription factor ste11 and the meiosis-promoting RNA-binding protein mei2. TORC2 is required for cell survival under various stress conditions. TORC2 positively controls G1 cell-cycle arrest, sexual development and amino acid uptake. Positively regulates amino acid uptake through the control of expression of amino acid permeases (PubMed:17046992, PubMed:17261596, PubMed:18076573). May play a role in mRNA maturation as a coupling protein between splicing and synthesis and/or stabilization. {ECO:0000269|PubMed:11686295, ECO:0000269|PubMed:17046992, ECO:0000269|PubMed:17261596, ECO:0000269|PubMed:18076573}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74189
|
PMT1_CANAL
|
MAKKPVTPASKVAAKQAAVRSRHQEDVFTLDPLIDPIFQKGELRSYLVTEPSPSVLKKRSIHTKEYWMLSSLLLIAFYVRMYNLSNPNSVVFDEVHFGGFARKYILGTFFMDVHPPLAKMLFGAVGAIGGFKGDFEFKSIGDKFPDSTPYIFMRQFPALLGVGTVILCYLTLRQSGVRPIIAYITTFLLIIENSNVTISRYILLDSPLIFFIAAAIYAWKKFEIQIPFTFGWYRSLLATGIALGLALSSKWVGLFTVAWVGFLCIYQLWFLIGDLSVSTKKIWGHFFARGIILLGVPIALYLGFFAIHFQLLNKEGDGGAFMSSAFRAGLQGNKIPRDITEQVGLGSVVTIRHVDTQGGYLHSHEHFYQTGSKQQQITLYPHLDSNNKWLIEPYNGTIHNETFVPLINGMKIRLKHINTGRRLHSHDEKPPVSERDWQKECSCYGYDGFAGDANDDWVVEIVNYRSQKGEAQTFVKAINTIFRLRHAMTGHYLFSSEVKLPEWGFGQQEVTSASQGKRALTHWYIETNENSILPPSEAKIINYPKLSLWQKVVESHKRMWKINQGLTSHHHWQSSPSEWPLLLRGINYWNKEHKQVYLLGNAVTWWAATLSIITFGTYVLVTVFRWHLGTPLSTNKHVFNFNVQTFSYVLGWALHYLPFFIMGRQLFLHHYLPALYFGILALGHFFEIFTGYLTSRSKYFQQVAFVLVGLFSILSLVFYVNYSSLIYGTPWTKASCELTKPFSGWDYNCGTFFDTLGEYDIQEKSLASESEIPTETVVVEAKQTPKAEPKLAKQDDHIESPAAAEPVEEKEVKEEVEQLAPPLAVDFEEETPKVEDPQVADVDASSNDEKSVEEKQQQEQQQEQEQVEDESVHQVQQ
|
2.4.1.109
| null |
biological process involved in interaction with host [GO:0051701]; cell-substrate adhesion [GO:0031589]; cellular response to starvation [GO:0009267]; filamentous growth [GO:0030447]; filamentous growth of a population of unicellular organisms in response to starvation [GO:0036170]; fungal-type cell wall organization [GO:0031505]; negative regulation of proteolysis [GO:0045861]; protein O-linked glycosylation [GO:0006493]; protein O-linked mannosylation [GO:0035269]; single-species biofilm formation on inanimate substrate [GO:0044011]
|
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; plasma membrane [GO:0005886]
|
dolichyl-phosphate-mannose-protein mannosyltransferase activity [GO:0004169]; mannosyltransferase activity [GO:0000030]
|
PF02815;PF02366;PF16192;
|
2.80.10.50;
|
Glycosyltransferase 39 family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P33775}.
|
CATALYTIC ACTIVITY: Reaction=a dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-O-(alpha-D-mannosyl)-L-seryl-[protein] + a dolichyl phosphate + H(+); Xref=Rhea:RHEA:17377, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:13546, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211, ChEBI:CHEBI:137321; EC=2.4.1.109; Evidence={ECO:0000250|UniProtKB:P33775, ECO:0000303|PubMed:15659169}; CATALYTIC ACTIVITY: Reaction=a dolichyl beta-D-mannosyl phosphate + L-threonyl-[protein] = 3-O-(alpha-D-mannosyl)-L-threonyl-[protein] + a dolichyl phosphate + H(+); Xref=Rhea:RHEA:53396, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:13547, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211, ChEBI:CHEBI:137323; EC=2.4.1.109; Evidence={ECO:0000250|UniProtKB:P33775, ECO:0000303|PubMed:15659169};
| null |
PATHWAY: Protein modification; protein glycosylation. {ECO:0000305}.
| null | null |
FUNCTION: Protein mannosyltransferase (PMT) involved in hyphal growth and drug sensitivity. Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins. PMT1, PMT2 and PMT4 account for most of the protein-O-glycosylation activity, while PMT5 and PMT6 may specifically modulate a much narrower spectrum of target proteins. Accounts for the O-glycosylation of the cell wall proteins KRE9, PIR2, RHD3, and ALS1, as well as the SEC20 t-SNARE component. O-glycosylation of SEC20 is essential for its stability. Required for filamentation and early phases of biofilm formation. {ECO:0000269|PubMed:15470244, ECO:0000269|PubMed:15659169, ECO:0000269|PubMed:16040968, ECO:0000269|PubMed:17005840, ECO:0000269|PubMed:20533408, ECO:0000269|PubMed:9694829}.
|
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
|
O74198
|
ERG6_CANAL
|
MSPVQLAEKNYERDEQFTKALHGESYKKTGLSALIAKSKDAASVAAEGYFKHWDGGISKDDEEKRLNDYSQLTHHYYNLVTDFYEYGWGSSFHFSRYYKGEAFRQATARHEHFLAHKMNLNENMKVLDVGCGVGGPGREITRFTDCEIVGLNNNDYQIERANHYAKKYHLDHKLSYVKGDFMQMDFEPESFDAVYAIEATVHAPVLEGVYSEIYKVLKPGGVFGVYEWVMTDKYDETNEEHRKIAYGIEVGDGIPKMYSRKVAEQALKNVGFEIEYQKDLADVDDEIPWYYPLSGDLKFCQTFGDYLTVFRTSRIGRFITTESVGLMEKIGLAPKGSKQVTHALEDAAVNLVEGGRQKLFTPMMLYVVRKPLEKKD
|
2.1.1.41
| null |
ergosterol biosynthetic process [GO:0006696]; methylation [GO:0032259]; zymosterol biosynthetic process [GO:0036197]
|
endoplasmic reticulum [GO:0005783]; plasma membrane [GO:0005886]
|
sterol 24-C-methyltransferase activity [GO:0003838]
|
PF08241;PF08498;
|
3.40.50.150;
|
Class I-like SAM-binding methyltransferase superfamily, Erg6/SMT family
| null | null |
CATALYTIC ACTIVITY: Reaction=S-adenosyl-L-methionine + zymosterol = fecosterol + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:21128, ChEBI:CHEBI:15378, ChEBI:CHEBI:17038, ChEBI:CHEBI:18252, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.41; Evidence={ECO:0000269|PubMed:20946868}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21129; Evidence={ECO:0000269|PubMed:20946868};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=55 uM for zymosterol {ECO:0000269|PubMed:20946868};
|
PATHWAY: Steroid metabolism; ergosterol biosynthesis; ergosterol from zymosterol: step 1/5. {ECO:0000269|PubMed:20946868}.
| null | null |
FUNCTION: Sterol 24-C-methyltransferase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (PubMed:20946868, PubMed:9593144). ERG6 catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol (PubMed:20946868, PubMed:9593144). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase ERG9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, the squalene epoxidase ERG1 catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, which is considered to be a rate-limiting enzyme in steroid biosynthesis. Then, the lanosterol synthase ERG7 catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol core. In the next steps, lanosterol is transformed to zymosterol through a complex process involving various demethylation, reduction and desaturation reactions. The lanosterol 14-alpha-demethylase ERG11 (also known as CYP51) catalyzes C14-demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol, which is critical for ergosterol biosynthesis. The C-14 reductase ERG24 reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol. 4,4-dimethyl-cholesta-8,24-dienol is substrate of the C-4 demethylation complex ERG25-ERG26-ERG27 in which ERG25 catalyzes the three-step monooxygenation required for the demethylation of 4,4-dimethyl and 4alpha-methylsterols, ERG26 catalyzes the oxidative decarboxylation that results in a reduction of the 3-beta-hydroxy group at the C-3 carbon to an oxo group, and ERG27 is responsible for the reduction of the keto group on the C-3. ERG28 has a role as a scaffold to help anchor ERG25, ERG26 and ERG27 to the endoplasmic reticulum and ERG29 regulates the activity of the iron-containing C4-methylsterol oxidase ERG25. Then, the sterol 24-C-methyltransferase ERG6 catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol. The C-8 sterol isomerase ERG2 catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase ERG3 then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The C-22 sterol desaturase ERG5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductase ERG4 to produce ergosterol (Probable). {ECO:0000269|PubMed:20946868, ECO:0000269|PubMed:9593144, ECO:0000305}.
|
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
|
O74201
|
UBC2_CANAL
|
MSTPARRRLMRDFKRMQQDPPSGVSASPLPDNVMKWNAVIIGPSDTPFEDGTFRLLLSFDEQYPNKPPQVKFISEMFHPNVYASGELCLDILQNRWSPTYDVSSILTSVQSLLNDPNISSPANVEAANLYKDHRSLYVKRVRETVENSWNDDDDEEEEEEDEDEAEDEDDDDDDNIDED
|
2.3.2.23
| null |
cellular response to UV [GO:0034644]; cytoplasm protein quality control by the ubiquitin-proteasome system [GO:0071629]; DNA damage response [GO:0006974]; DNA repair [GO:0006281]; DNA-templated transcription termination [GO:0006353]; double-strand break repair via homologous recombination [GO:0000724]; ERAD pathway [GO:0036503]; error-free postreplication DNA repair [GO:0042275]; error-free translesion synthesis [GO:0070987]; error-prone translesion synthesis [GO:0042276]; filamentous growth [GO:0030447]; meiotic DNA double-strand break formation [GO:0042138]; mitotic G1 DNA damage checkpoint signaling [GO:0031571]; negative regulation of SREBP signaling pathway [GO:2000639]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein polyubiquitination [GO:0000209]; regulation of dipeptide transport [GO:0090089]; sporulation resulting in formation of a cellular spore [GO:0030435]; stress-induced homeostatically regulated protein degradation pathway [GO:0120174]; subtelomeric heterochromatin formation [GO:0031509]; telomere maintenance via recombination [GO:0000722]; transcription by RNA polymerase II [GO:0006366]; ubiquitin-dependent protein catabolic process via the N-end rule pathway [GO:0071596]
|
chromosome, telomeric region [GO:0000781]; cytoplasm [GO:0005737]; fungal biofilm matrix [GO:0062040]; HULC complex [GO:0033503]; MUB1-RAD6-UBR2 ubiquitin ligase complex [GO:1990304]; nucleus [GO:0005634]; Rad6-Rad18 complex [GO:0097505]; RAD6-UBR2 ubiquitin ligase complex [GO:1990305]; UBR1-RAD6 ubiquitin ligase complex [GO:1990303]
|
ATP binding [GO:0005524]; proteasome binding [GO:0070628]; single-stranded DNA binding [GO:0003697]; single-stranded DNA helicase activity [GO:0017116]; ubiquitin conjugating enzyme activity [GO:0061631]; ubiquitin-protein transferase activity [GO:0004842]
|
PF00179;
|
3.10.110.10;
|
Ubiquitin-conjugating enzyme family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q5VVX9}. Nucleus {ECO:0000250|UniProtKB:Q5VVX9}.
|
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.; EC=2.3.2.23; Evidence={ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133};
| null |
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000255|PROSITE-ProRule:PRU00388}.
| null | null |
FUNCTION: Catalyzes the covalent attachment of ubiquitin to other proteins. Plays a role in transcription regulation by catalyzing the monoubiquitination of histone H2B to form H2BK123ub1. H2BK123ub1 gives a specific tag for epigenetic transcriptional activation and is also a prerequisite for H3K4me and H3K79me formation. Also involved in postreplication repair of UV-damaged DNA, in N-end rule-dependent protein degradation and in sporulation. {ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000269|PubMed:10712706}.
|
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
|
O74205
|
TOXE_COCCA
|
MGTTSPNSEKRQITDINERRKLQNRVAQRKYRTRQKTRMKLAEAVLNDYTYIHPTLGTIQSKKKSPLTMECDRSSASYPDLSSYAEICSETRSETQATRARQLTSQRTCFRESVDNNQADSHAQLSRCLNRQEMFYGISGETEFSEGDTRDRVECIDPNLTRGWLDMDLRSGTPNSSTVVDCGLCTVGANSQPPTRTNVQEAIETLELFEPNDQRKTENLPREPCGSCPSSSHGYSPTSGNPSTLLLTPSESLMNSVIVTSDSPLLAADDKSPGDLVISEANTHGPKEDQFSPLMTAISLGRLDIARILLQSGAPLDIPDDSGKTALHRAVGRRELHMVEALLNLGAEMLATDHEGNSLLHIAVKTNSLSITRLLLERYKSCRELKDAQLGHGCRQHGNQVHSESWIDLRNREGMTAVHLSVIFNRPEILQLLVKYSANVN
| null | null |
negative regulation of canonical Wnt signaling pathway [GO:0090090]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of JNK cascade [GO:0046330]; protein targeting to chloroplast [GO:0045036]; regulation of DNA-templated transcription [GO:0006355]; toxin biosynthetic process [GO:0009403]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
chloroplast targeting sequence binding [GO:0030941]; DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]
|
PF00023;PF12796;
|
1.20.5.170;1.25.40.20;
|
BZIP family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:11698648}.
| null | null | null | null | null |
FUNCTION: Transcription factor, part of the diffuse TOX2 gene cluster that mediates the biosynthesis of the HC-toxin, cyclic tetrapeptide of structure cyclo(D-Pro-L-Ala-D-Ala-L-Aeo), where Aeo stands for 2-amino-9,10-epoxi-8-oxodecanoic acid (PubMed:11698648, PubMed:9894916). HC-toxin is a determinant of specificity and virulence in the interaction between the producing fungus and its host, maize (PubMed:11698648, PubMed:9894916). TOXE is a pathway-specific transcription factor which coordinates the expression of genes involved in HC-toxin biosynthesis (PubMed:9894916). Binds to the tox-box, a 10-bp motif with the consensus 5'-ATCTCNCGNA-3', which is found in the promoter of all genes involved in HC-toxin biosynthesis (PubMed:11698648). Required for pathogenicity of the fungus on maize (PubMed:9894916). {ECO:0000269|PubMed:11698648, ECO:0000269|PubMed:9894916}.
|
Cochliobolus carbonum (Maize leaf spot fungus) (Bipolaris zeicola)
|
O74208
|
PDH1_CANGA
|
MNTPDDSSVSSVDSHQPYMGFDDNVEKRIRELARSLTQQSLTSSNRSVNKEAPADGSAPLDRVSTRASSIFSADFKGVNPVFSDEEEDDYDARLDPNSDEFSSKAWVQNMAKITTGDPEFYKPYSIGCCWKDLSASGESADVSYQSTFLNLPVKLLNAVWRKARPARESDTFRILKPMDGLLKPGELLVVLGRPGSGCTTLLKSISSTTHGFQISKDSVISYNGLTPNEIKKHYRGEVVYNAEADIHLPHLTVYQTLVTVARLKTPQNRVKGVTREDFANHVTDVAMATYGLSHTRDTKVGNDLVRGVSGGERKRVSIAEVWICGSKFQCWDNATRGLDSATALEFVRALKTQAHIAKNVATVAIYQCSQDAYNLFNKVSVLYEGYQIYFGDAQHAKVYFQKMGYFCPKRQTIPDFLTSITSPAERRINKEYLDKGIKVPQTPLDMVEYWHNSEEYKQLREEIDETLAHQSEDDKEEIKEAHIAKQSKRARPSSPYVVSYMMQVKYILIRNFWRIKNSASVTLFQVFGNSAMAFILGSMFYKIQKGSSADTFYFRGAAMFFAILFNAFSSLLEIFSLYEARPITEKHRTYSLYHPSADAFASVISEIPPKIVTAILFNIIFYFLVNFRRDAGRFFFYFLINVIAVFAMSHLFRCVGSLTKTLQEAMVPASMLLLALSMYTGFAIPRTKMLGWSKWIWYINPLAYLFESLMVNEFHDRRFPCNTYIPRGGAYNDVTGTERVCASVGARPGNDYVLGDDFLKESYDYENKHKWRGFGVGMAYVIFFFFVYLILCEFNEGAKQKGEMLVFPHSVVKRMKKEGKIRDKTKMHTDKNDIENNSESITSNATNEKNMLQDTYDENADSESITSGSRGGSPQVGLSKSEAIFHWQNLCYDVPIKTEVRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERTTMGVITGDVMVNGRPRDTSFSRSIGYCQQQDLHLKTATVRESLRFSAYLRQPSSVSIEEKNEYVEAVIKILEMETYADAVVGVPGEGLNVEQRKRLTIGVELAAKPKLLVFLDEPTSGLDSQTAWATCQLMKKLANHGQAILCTIHQPSAMLMQEFDRLLFLQKGGQTVYFGDLGKGCKTMIKYFEDHGAHKCPPDANPAEWMLEVVGAAPGSHANQDYHEVWRNSEQFKQVKQELEQMEKELSQKELDNDEDANKEFATSLWYQFQLVCVRLFQQYWRTPDYLWSKYILTIFNQLFIGFTFFKADHTLQGLQNQMLSIFMYTVIFNPLLQQYLPTFVQQRDLYEARERPSRTFSWKAFILAQIVVEVPWNIVAGTLAYCIYYYSVGFYANASQAHQLHERGALFWLFSIAFYVYVGSLGLFVISFNEVAETAAHIGSLMFTMALSFCGVMATPDAMPRFWIFMYRVSPLTYLIDALLSTGVANVDIRCSNTELVTFTPPQGLTCGQYMTPYLNVAGTGYLTDPSATDECHFCQFSYTNDFLATVSSKYYRRWRNYGIFICFIVFDYVAGIFLYWLARVPKTNGKIAKNGKTAKVNFIRRLIPF
| null | null |
response to xenobiotic stimulus [GO:0009410]; xenobiotic detoxification by transmembrane export across the plasma membrane [GO:1990961]
|
plasma membrane [GO:0005886]
|
ABC-type xenobiotic transporter activity [GO:0008559]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]
|
PF01061;PF19055;PF00005;PF14510;PF06422;
|
3.40.50.300;
|
ABC transporter superfamily, ABCG family, PDR (TC 3.A.1.205) subfamily
|
PTM: Phosphorylated by PKA. Dephosphorylated on glucose depletion and independently rephosphorylated during glucose exposure or under stress. {ECO:0000269|PubMed:12244114}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12244114}; Multi-pass membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Pleiotropic ABC efflux transporter that confers resistance to structurally and functionally unrelated compounds including caspofungin or azoles such as fluconazole, itraconazole, posaconazole, voriconazole, and isavuconazole (PubMed:11257032, PubMed:12244114, PubMed:12557277, PubMed:15105134, PubMed:15388433, PubMed:16803598, PubMed:17581937, PubMed:20038613, PubMed:24273749, PubMed:24838041, PubMed:26482310, PubMed:27486188, PubMed:29371812). Does not play a role in the azole resistance in mature biofilms (PubMed:18651314). {ECO:0000269|PubMed:11257032, ECO:0000269|PubMed:12244114, ECO:0000269|PubMed:12557277, ECO:0000269|PubMed:15105134, ECO:0000269|PubMed:15388433, ECO:0000269|PubMed:16803598, ECO:0000269|PubMed:17581937, ECO:0000269|PubMed:18651314, ECO:0000269|PubMed:20038613, ECO:0000269|PubMed:24273749, ECO:0000269|PubMed:24838041, ECO:0000269|PubMed:26482310, ECO:0000269|PubMed:27486188, ECO:0000269|PubMed:29371812}.
|
Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
|
O74213
|
PGLR1_ASPAC
|
MHLNTTLLVSLALGAASVLASPAPPAITAPPTAEEIAKRATTCTFSGSNGASSASKSKTSCSTIVLSNVAVPSGTTLDLTKLNDGTHVIFSGETTFGYKEWSGPLISVSGSDLTITGASGHSINGDGSRWWDGEGGNGGKTKPKFFAAHSLTNSVISGLKIVNSPVQVFSVAGSDYLTLKDITIDNSDGDDNGGHNTDAFDIGTSTYVTISGATVYNQDDCVAVNSGENIYFSGGYCSGGHGLSIGSVGGRSDNTVKNVTFVDSTIINSDNGVRIKTNIDTTGSVSDVTYKDITLTSIAKYGIVVQQNYGDTSSTPTTGVPITDFVLDNVHGSVVSSGTNILISCGSGSCSDWTWTDVSVSGGKTSSKCTNVPSGASC
|
3.2.1.15
| null |
cell wall organization [GO:0071555]; pectin catabolic process [GO:0045490]
|
extracellular region [GO:0005576]
|
polygalacturonase activity [GO:0004650]
|
PF00295;
|
2.160.20.10;
|
Glycosyl hydrolase 28 family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=(1,4-alpha-D-galacturonosyl)n+m + H2O = (1,4-alpha-D-galacturonosyl)n + (1,4-alpha-D-galacturonosyl)m.; EC=3.2.1.15;
| null | null | null | null |
FUNCTION: Involved in maceration and soft-rotting of plant tissue. Hydrolyzes the 1,4-alpha glycosidic bonds of de-esterified pectate in the smooth region of the plant cell wall.
|
Aspergillus aculeatus
|
O74237
|
XYL1_CANTE
|
MSASIPDIKLSSGHLMPSIGFGCWKLANATAGEQVYQAIKAGYRLFDGAEDYGNEKEVGDGVKRAIDEGLVKREEIFLTSKLWNNYHDPKNVETALNKTLADLKVDYVDLFLIHFPIAFKFVPIEEKYPPGFYCGDGNNFVYEDVPILETWKALEKLVAAGKIKSIGVSNFPGALLLDLLRGATIKPAVLQVEHHPYLQQPKLIEFAQKAGVTITAYSSFGPQSFVEMNQGRALNTPTLFAHDTIKAIAAKYNKTPAEVLLRWAAQRGIAVIPKSNLPERLVQNRSFNTFDLTKEDFEEIAKLDIGLRFNDPWDWDNIPIFV
|
1.1.1.307
| null |
D-xylose catabolic process [GO:0042843]
|
cytosol [GO:0005829]
|
D-xylose:NADP reductase activity [GO:0032866]
|
PF00248;
|
3.20.20.100;
|
Aldo/keto reductase family
| null | null |
CATALYTIC ACTIVITY: Reaction=NAD(+) + xylitol = D-xylose + H(+) + NADH; Xref=Rhea:RHEA:27441, ChEBI:CHEBI:15378, ChEBI:CHEBI:17151, ChEBI:CHEBI:53455, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.307; CATALYTIC ACTIVITY: Reaction=NADP(+) + xylitol = D-xylose + H(+) + NADPH; Xref=Rhea:RHEA:27445, ChEBI:CHEBI:15378, ChEBI:CHEBI:17151, ChEBI:CHEBI:53455, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.307;
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=142 mM for xylose {ECO:0000269|PubMed:15320875, ECO:0000269|PubMed:16336198}; KM=38 uM for NADH {ECO:0000269|PubMed:15320875, ECO:0000269|PubMed:16336198}; KM=3 uM for NADPH {ECO:0000269|PubMed:15320875, ECO:0000269|PubMed:16336198};
|
PATHWAY: Carbohydrate metabolism; D-xylose degradation.
| null | null |
FUNCTION: Reduces D-xylose into xylitol. Has a preference for NADPH, but can also utilize NADH as cosubstrate.
|
Candida tenuis (Yeast) (Yamadazyma tenuis)
|
O74288
|
ABFB_EMENI
|
MTMSRSSRSSVLALALATGSLVAAGPCDIYSSGGTPCIAAHSTTRALYSSYNGPLYQVQRASDGTTTTITPLSAGGVADASAQDAFCENTTCLITIIYDQSGNGNDLTQAPPGGFNGPDVGGYDNLAGAIGAPVTLNGKKAYGVFVSPGTGYRNNEAIGTATGDEPEGMYAVLDGTHYNDGCCFDYGNAETSSLDTGNGHMEAIYYGTNTAWGYGAGNGPWIMADLENGLFSGQSSDYNAGDPSISYRFVTAILKGGPNLWALRGGNAASGSLSTYYNGIRPTDASGYNPMSKEGAIILGIGGDNSVSAQGTFYEGAMTDGYPDDATENSVQADIVAAKYATTSLISGPALTVGDTVSLKVTTSGYDTRYIAHTGSTINTQVVSSSSSSTLKQQASWTVRTGLASTAAANGCVSFESVDTPGSYIRHSNFALLLNANDGTKLFSEDATFCPQDSFNDDGTNSIRSWNYPTRYWRHYENVLYVASNGGVNTFDAATAFTDDVSWVVADGFA
|
3.2.1.55
| null |
arabinan catabolic process [GO:0031222]; arabinose metabolic process [GO:0019566]; L-arabinose metabolic process [GO:0046373]; pectin catabolic process [GO:0045490]; xylan catabolic process [GO:0045493]
|
extracellular region [GO:0005576]
|
alpha-L-arabinofuranosidase activity [GO:0046556]
|
PF05270;PF09206;
|
2.60.120.200;2.80.10.50;
|
Glycosyl hydrolase 54 family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10217508}.
|
CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides.; EC=3.2.1.55;
| null |
PATHWAY: Glycan metabolism; L-arabinan degradation.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.8. {ECO:0000269|PubMed:16844780};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 65 degrees Celsius. {ECO:0000269|PubMed:16844780};
|
FUNCTION: Alpha-L-arabinofuranosidase involved in the degradation of arabinoxylan, a major component of plant hemicellulose. Able to hydrolyze 1,5-, 1,3- and 1,2-alpha-linkages not only in L-arabinofuranosyl oligosaccharides, but also in polysaccharides containing terminal non-reducing L-arabinofuranoses in side chains, like L-arabinan, arabinogalactan and arabinoxylan. {ECO:0000269|PubMed:10217508, ECO:0000269|PubMed:16844780}.
|
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
|
O74304
|
WIN1_SCHPO
|
MENILDPSVVNSHILENGSRRSSINPILDSELRDKTFEKAHRRSLTLLSSFTSSMLELPNNGKEENHRRPSVARSSSDRSKASAKEDLFSEAFRMAEQPPAEALTISTPVDPINIDELDRAYAVSPSDTSNLLHPPTSSSSIPIPIKNAGHSNLDHPIRPSLQSSISSNRIIKSPGIKEDDYMHRGRSISSPMIDVEHINSTAVPSKTKNLPEKPKRSHKLRNSITFAKIEDHPERKSQLRRLSSSLKCFDPEYDYNDPSLSIRRDSSTYYFSNVNETYDEEDSDLDSETSTVNWVQSVLNLPSLLSDDLMANPKNKERFEWQYMLTSVLTGDIVRSEKLRLRKIASSREGRNSDYSDNLWMEIWCWLTHRSVDSYRENLKHLRTGMVDVLLAIMNFHWDESNELTPIVAVDNMLQKLDKYERLYPSRRSILQEHSLYASESFQHKLDVLTAYSNVTHALEIQVNIIRSWVGNEEMDITKNTTNSINNVSQISNGPFVERFYRETGLIRAFEQRIMTNMNSVLSKVCNTIVTYADDLKSYGLPLIADDYMRLLSFPFRLIKEFLNLRLSCAENITSISLFTIDSLLDDLRNTMKVAVHIIQQHTVLIKPFRDDSKFVDENQSLNNILVASLKFYFNLLHRKVRNGCALLHFKETEILEGEWDFLLAVCPHIEHGFQIMSKSLSSLVGEILTNINRYLKDQLQGPDTDDSALITSFYIKVLDCVRIRFRKLMSFTRILKAHLENSCEYVIKENSLSLLIQRLEESNHVLTYTASIEHEGAYVIVPGHLVDSPNILREVLSMTFNKGDNNFESVPPYAVVLAPDSSICWNGHVTDLDIPEVSISIAPNCVRLVTLATANQLSVIEDYFISIVGDTVSLVDSAKANSSKINKQMTKIKRNSLKLALSLLDVIQTIRTRYHGMNCQNLIHYSFSYAIEFAQRLMRLSILDASSIGLIRRKMIQLAISWVGFIYEDCSPTDRNTFRWTVTALEFAMIMTYGSNILMIDKKSFEELKEKVGKCVALLLLHFDVMGTKHAGRSMDQQAGDIPARLVRNNSDRSRLSDNELASFVKEEVMHRIIELESNRRDRLYKSQLIGRVLDDTTKENRLLKELASSKSNITIRWQQGGLIGSGSFGTVYRAVNLDTGDLMAVKEVALHKPRISRPMIKRIKGEMLVLELFDHPNVVSYYGIEVHREKVNIFMELCQGSSLFEFLRYGRIEDELVIQVYVLQLLEGLAYIHSCGVSHQDVKPENILFDHNGIMKFTDFGSAKMSGSASTKIFEQLTQQEEEEFEKDSEFLQHLDQNRGYSLTGTPTYMAPELILGNPSERVGAMDIWSLGCVIVEMATGSPPWPRLDNHFSLMYHIAAHNPPIIPADDQLSPLGQNFLKRCFVSDPNQRATAAELLMDPWVYPLRAGTEFDLMNSSVVESAPSTNGAPLEL
|
2.7.11.25
| null |
p38MAPK cascade [GO:0038066]; phosphorylation [GO:0016310]; stress-activated MAPK cascade [GO:0051403]
|
cytoplasm [GO:0005737]; Mcs4 RR-MAPKKK complex [GO:1990315]
|
ATP binding [GO:0005524]; MAP kinase kinase kinase activity [GO:0004709]; protein serine kinase activity [GO:0106310]
|
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: Involved in a signal transduction pathway that is activated by changes in the osmolarity of the extracellular environment. Activates the wis1 MAP kinase kinase by phosphorylation. {ECO:0000269|PubMed:9693384}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74309
|
SLM9_SCHPO
|
MHIFVPKLLENHQFSSISSSKDFVAVSAETNVYILSKDFFYPKSSEKRIIQSLNGHKTTHLSFDSPISCIRFTYDGSCLAVATEAGTFLYHSEKWDKAFQVLSGPAYEVCWSQQGHILATSWKQISIYVKDEGLRTETIVKKTEHADSNHQPAVSIEESKEAVESTSQSSEISFKLIKVIEGHHTFVGGLAFDPMGQFLASQSFDHTLKVWKLSTFGVEKSIAKPFEQMPTGNRFLRLSWSPDGAHIASVNAVNEGAYVIAIVQRDTWTYDINLVGHQGPLECATFNPYLYEDPFQKSIIASAAHDGCVSIWNTACARPMAVIHELSCSSFVDLQWSTSGFELYGVSLDGNLMLLQFEESEFGEKMDTIHYPDDLSYFNSSRSKAHVNKNAAADRTTSPTQGQPESPSKSILLRPPPSIASSPESKRRKCPKKFVARPPVPHPTSLYSQIRIGCPYLKPKLVISKSFGTLIVKNHNQLSLLKCTFSNLDGNDCSWFSYLPNAIVLANGTSVFWAVATEDSSIYIYSPAGRLLLPPVVVAATPCFLECCGDFLCCIVSTGLLYIWNIKNFEAIHSPVSTLPLFHSNFSVSKIARGPSIEQFFVTKQGHPVAIMSDGNAFAFIRDSSSWLRVSEGWWMIGSQYWGPLASESNEESPLGFLERCTDEEIIKAGRGRFLQRLVKALMLRQGYDNYEMLVSIRHLENRLMSSAKLDLEYDFRENLILYAKKIAEEGMKDKMDELCKELLGPLRIPHNGIDTVKVGNRLWSPTIAGNNKRNLLKDIIIHTAKYRDMQRITSQYSDLLRRSALL
| null | null |
chromatin remodeling [GO:0006338]; DNA repair-dependent chromatin remodeling [GO:0140861]; regulation of DNA-templated transcription [GO:0006355]; transcription elongation-coupled chromatin remodeling [GO:0140673]; transcription initiation-coupled chromatin remodeling [GO:0045815]
|
chromatin [GO:0000785]; cytosol [GO:0005829]; HIR complex [GO:0000417]; nucleus [GO:0005634]
|
ATP-dependent H3-H4 histone complex chaperone activity [GO:0140665]; nucleosome binding [GO:0031491]
|
PF07569;PF00400;
|
2.130.10.10;
|
WD repeat HIR1 family
| null |
SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
| null | null | null | null | null |
FUNCTION: Probably required for replication-independent chromatin assembly (By similarity). Required for transcriptional silencing in the outer repeat (otr) centromeric repeats and the Tf2 long terminal repeat retrotransposons. May play an indirect role in the regulation of cdc2 and/or wee1 at the G2/M stage of mitosis. {ECO:0000250, ECO:0000269|PubMed:10835386, ECO:0000269|PubMed:15121850, ECO:0000269|PubMed:16428807}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74312
|
ATG9_SCHPO
|
MFYQPAQNKKQYDDLADIEAQNNVPNTQEVLEAWQESLDSDEDESSPLEESNGFTISEHDDFVKSVPRKNNPTDLLYSGKLLDSDEPPSVHGNSSKVPSKHPSPSFPETTSLRNLQNGSKQKPALPNFNDPHFYNEDVTRSGHPNRSIYTQLPRNEFSNARVLWNRLSARDRVLWRWANVENLDSFLQQVYTYYTGKGLSCIIVHRLFQILTVSFVIGFTTFITSCIDWPAVTPHGSLAGVTKSQCIAQMSPITYLVLWLFLSFLLALWIYYLTDIPRLWQMREFYIHALKIATADMPTVSWQRVLYRLLKLKNVNALTAEDGRVVSLHNMKRLDAYAIANRIMRKDNYFIALINNGIINIELPLLHRRILTHTTEWNINWCIFNFVFDEQGQLRSAFRNPNSRKRLSEELRRRFIVAGFLNCLFAPIVAIYLVIHNFFRYFNEYHKNPGALSTRRYTPLALWTFREYNELQHFFDERINDSYAAASHYVSQFPDFNMIRLFKYISFILGSFTAILVIITVFDPELMVTFEITKDRSVLFYLGLFGSLIAVSRSIIPDETLVFAPEKALRRVITFTHYMPGWWSDNMHSKAVQQEFCSLYSYRIVNLLWEILGILLTPVLLFFTFPSCSQDIVDFFREHTINVEGVGYVCSYAVFQDNPPYESVASLVQSRKISPLIQNKPELSRISFYEQFNTEAPRRDLR
| null | null |
autophagosome assembly [GO:0000045]; macroautophagy [GO:0016236]; piecemeal microautophagy of the nucleus [GO:0034727]; protein localization to phagophore assembly site [GO:0034497]; reticulophagy [GO:0061709]
|
autophagosome [GO:0005776]; cytoplasmic vesicle membrane [GO:0030659]; endoplasmic reticulum membrane [GO:0005789]; fungal-type vacuole membrane [GO:0000329]; Golgi membrane [GO:0000139]; phagophore assembly site [GO:0000407]; phagophore assembly site membrane [GO:0034045]
|
phospholipid scramblase activity [GO:0017128]
|
PF04109;
| null |
ATG9 family
|
PTM: Phosphorylated by atg1. Atg1 phosphorylation is required for preautophagosome elongation. {ECO:0000250|UniProtKB:Q12142}.
|
SUBCELLULAR LOCATION: Preautophagosomal structure membrane {ECO:0000269|PubMed:23950735}; Multi-pass membrane protein {ECO:0000269|PubMed:23950735}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q12142}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q12142}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q12142}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q12142}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q12142}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q12142}.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(in) = a 1,2-diacyl-sn-glycero-3-phosphocholine(out); Xref=Rhea:RHEA:38571, ChEBI:CHEBI:57643; Evidence={ECO:0000250|UniProtKB:Q12142}; 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:0000250|UniProtKB:Q12142}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out); Xref=Rhea:RHEA:38895, ChEBI:CHEBI:64612; Evidence={ECO:0000250|UniProtKB:Q12142}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate)(in) = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate)(out); Xref=Rhea:RHEA:67920, ChEBI:CHEBI:58088; Evidence={ECO:0000250|UniProtKB:Q12142};
| null | null | null | null |
FUNCTION: Phospholipid scramblase involved in autophagy and cytoplasm to vacuole transport (Cvt) vesicle formation (PubMed:23950735). Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome (By similarity). Lipid scramblase activity plays a key role in preautophagosomal structure/phagophore assembly by distributing the phospholipids that arrive through atg2 from the cytoplasmic to the luminal leaflet of the bilayer, thereby driving autophagosomal membrane expansion (By similarity). Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress (By similarity). Different machineries are required for anterograde trafficking to the PAS during either the Cvt pathway or bulk autophagy and for retrograde trafficking (By similarity). Has a role in meiosis and sporulation (PubMed:19778961). {ECO:0000250|UniProtKB:Q12142, ECO:0000269|PubMed:19778961, ECO:0000269|PubMed:23950735}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74327
|
AVT5_SCHPO
|
MSGYSPLSSGPADVHIGKAGFFSSVINLANTILGAGILSLPNAFTKTGLLFGCLTIVFSAFASFLGLYFVSQCAARLPRGKASFAAVAKHTFPSLAVVFDASIAVKCFGVAVSYLVIVGDLMPQIAPSLGLSSPMFLRRQTWIVFALFVLTPLSFLKRLDSLRHTSVISLIALCYLVFIVLYHFIIGDTVKGEIRYFVPESGFGYLSVLPVFVFGFTCHQNAFSVINEVRNFSQGFVNFTMFTAIISSTLLYLLVAITGYLSFGSLASGNIIAMYDNTSIWIIGGKLAIVVLVLFSYPLQCHPCRNSVYQAIRRSYSAHDMSDGYHAVITLCILLFTHSLALLLSSLEMVLAFVGSTGSTFISFILPGSLYYFFSHKVASPGNSSPLQLRISRAFAAGLAIYGTVVMILCLNINIAKLSH
| null | null |
amino acid transmembrane import into vacuole [GO:0032975]; amino acid transmembrane transport [GO:0003333]; L-arginine transmembrane import into vacuole [GO:0090518]; L-glutamate import involved in cellular response to nitrogen starvation [GO:1901481]; L-glutamate transmembrane import into vacuole [GO:0090515]; L-histidine transmembrane import into vacuole [GO:0090513]; L-lysine import into vacuole involved in cellular response to nitrogen starvation [GO:1901482]; L-lysine transmembrane import into vacuole [GO:0090517]; L-serine transmembrane import into vacuole [GO:0090516]; L-tyrosine transmembrane import into vacuole [GO:0090514]; sporulation resulting in formation of a cellular spore [GO:0030435]
|
fungal-type vacuole membrane [GO:0000329]
|
L-arginine transmembrane transporter activity [GO:0061459]; L-glutamate transmembrane transporter activity [GO:0005313]; L-histidine transmembrane transporter activity [GO:0005290]; L-lysine transmembrane transporter activity [GO:0015189]; L-serine transmembrane transporter activity [GO:0015194]; L-tyrosine transmembrane transporter activity [GO:0005302]
|
PF01490;
| null |
Amino acid/polyamine transporter 2 family
| null |
SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:20388511}; Multi-pass membrane protein {ECO:0000269|PubMed:20388511}.
| null | null | null | null | null |
FUNCTION: Vacuolar amino acid transporter involved in the vacuolar uptake of histidine, glutamate, tyrosine, arginine, lysine, and serine. Required for sporulation. {ECO:0000269|PubMed:19778961, ECO:0000269|PubMed:20388511}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74352
|
HOB1_SCHPO
|
MSWKGFTKALARTPQTLRSKFNVGEITKDPIYEDAGRRFKSLETEAKKLAEDAKKYTDAINGLLNHQIGFADACIEIYKPISGRASDPESYEQEGNAEGIEAAEAYKEIVYDLQKNLASEMDVINTRIVNPTGELLKIVKDVDKLLLKRDHKQLDYDRHRSSFKKLQEKKDKSLKDEKKLYEAETAFEQSSQEYEYYNEMLKEELPKLFALAQSFIAPLFQGFYYMQLNVYYVLYEKMSHCEIQYFDFNTDILESYERRRGDVKDRAEALTITKFKTAKPTYKRPGMGPGGKDATASSSSSFSSKREEAAAEPSSSTATDIPPPYSTPSVAGASDYSTPSAGYQTVQTTTTTTEAAAAQYPQAAFPPPPVMPQPAAAAVTTPVAAPVAAAAAAVPVPPPAPAPAAAPAAEHVVALYDYAAQAAGDLSFHAGDRIEVVSRTDNQNEWWIGRLNGAQGQFPGNYVQLE
| null | null |
actin cortical patch localization [GO:0051666]; DNA damage response [GO:0006974]; endocytosis [GO:0006897]; establishment or maintenance of cell polarity [GO:0007163]; plasma membrane tubulation [GO:0097320]
|
actin cortical patch [GO:0030479]; mating projection tip [GO:0043332]; medial cortex [GO:0031097]; mitotic actomyosin contractile ring [GO:0110085]; Rvs161p-Rvs167p complex [GO:1990528]
|
lipid binding [GO:0008289]; protein-membrane adaptor activity [GO:0043495]
|
PF03114;PF00018;
|
1.20.1270.60;2.30.30.40;
| null | null | null | null | null | null | null | null |
FUNCTION: Has a role in DNA damage signaling as a part of stress response processes. {ECO:0000269|PubMed:12569356}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74354
|
DNT1_SCHPO
|
MRTTLRLHIIKDGEQDNQFMILFDPSSSISLLKEKVQETYKSLYPFESNINIRNIKNEESYDIPNEYLVGEIFPTNSKVIVESFSSPLKKLDGTMINFKEKNIQHDLDGVENDFATVQSASNGVHAINGKRTHPDESENPRKLPKKNFVEAIDANSPGFVYRPTSIRDRAYSISSNHDNESTLTEGIALKEIESPDKDRKADGIVNLSVTQEEDDNHQSFNSSLTPSQPTTYNRANFFSINDASSDSSSDAPLRTLSSPSRLRMKDNDRKYLVEHSPAALIKESETIDGIDDKSLRSSTREVSVESPNEDSVNDDSSSDVSDEKETEAKHEIRAPAIIVRETSSHPSTAVPSENDTTESENDTLSESSTTSISSSPSENSDTSDDLTKVDSPNKSLVNDNVSAKHDKESENGKSKFPPPSQTLVTTSTISAAGNEPSDEIGSENDSDSDSDSDSSVPLSQLQKKSQQRNSVSHEIQNRGTKGSPKEPKAKPSTERPETHRTLSYSRLSELSKTFSPEIREPSLTKKTAVSMQESKEEGRSDESSESEESGSSSDESDNSEKEDRSNPIPVEKRASTVLNTKKKRKAKRNSALAGLAALV
| null | null |
deactivation of mitotic spindle assembly checkpoint [GO:1902426]; division septum assembly [GO:0000917]; negative regulation of protein localization to mitotic spindle pole body [GO:1902543]; negative regulation of septation initiation signaling [GO:0031030]; positive regulation of G2/M transition of mitotic cell cycle [GO:0010971]; rDNA heterochromatin formation [GO:0000183]
|
cytoplasm [GO:0005737]; mitotic spindle [GO:0072686]; nucleolus [GO:0005730]
|
phosphatase activator activity [GO:0019211]; rDNA binding [GO:0000182]
|
PF10407;
| null | null |
PTM: Phosphorylated by clp1. {ECO:0000269|PubMed:17538026, ECO:0000269|PubMed:18257517}.
|
SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleolus. Cytoplasm, cytoskeleton, spindle. Note=In late anaphase, localizes to the ends of the mitotic spindle.
| null | null | null | null | null |
FUNCTION: Negatively regulates the septation initiation network (SIN) pathway, independently of the cdc14 phosphatase clp1. May also have a role in silencing rDNA transcription. Required for maintaining the exclusive nucleolus localization of nuc1. {ECO:0000269|PubMed:17538026}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74360
|
RGA4_SCHPO
|
MNSGTTLHLDRLSLETPSERTCFCIKCWESVPSTSQVWFGGKCWHSDCFKCVNCNKKLDPSSEDFSQDDQKQIFCKLCVDICNGCSTPICEFNAVSNSQANHPCCSNCRAFINSNAFGKFKGQHYCLPCLRKQDEENQKAVMESASGFIPLRNIAQTAENTSLTGQNQGFQNPHFIASDSPSSVLSGRMQNTSSPTNSLRPQLKVQTNGYETPGDINSAKSYKDIQKDFLLKPKNSFVKTSPSPLANGPSFRSANASPFDSCDSFHSGSSIPIEPVSSRQSSVVNNNSVQQPVAYHAFVQSPTENGTLPQLPKNESVVNPPPLRRSSTMNYKSVSTTTSPSKYGYVSGRIALSPIHLRGALRDVTNKCNLKVPRNRNSLSNLDEYYVNGLESDETPTKARFPRYPTVFNKLDDKRLSSEPNGLKKRLTNSSNYEASPRAKSLNLSQVSLHQACEPEYNRSSLVRASDVFTSNVFDATEESANELAIRISELQAEVGTLLLEATSLASIIEQQTPVSPEAFKQELVADLNYRLDYLRKSFQPELSTLLLRRDALSTTVSKLQNAYSTVMEETAYLNVKNTELVSLNNQLERELAYLREQQHKKRTSSSFGIFNNDKKSNRTISTPSPRESFSRLQMVASSLGFRPKDNKDKESGGYNKRNSKIDLKKSFSKRFHWKRDSPHMSSTPSISEEHLASEEQEDFVPAVGHCKLCGKYSNELRAHYQDCVSSTIDRQYQSKKSESPVWALNPDDFDQNRLTLLRVPTLIVSCINFIESYGMDFEGLYRKSGATSQMKKIVALLRNEDTVLDPSEDISAVTSVFKQYLRNLPNPIITYDQYFPFITAANCASFQDKLDGFIMVIKSLPPAHAEILQLIIRHLARVAAYSHANRMTSKNLAVVFSPTLIRDPDNSRDVIDMTVKNYSLAFLIDHVHEVFA
| null | null |
establishment or maintenance of bipolar cell polarity [GO:0061245]; negative regulation of cell wall integrity MAPK cascade [GO:1903138]; positive regulation of establishment of bipolar cell polarity [GO:0061173]; positive regulation of establishment of cell polarity regulating cell shape [GO:2000784]; regulation of actin filament bundle assembly [GO:0032231]; regulation of cell wall organization or biogenesis [GO:1903338]; signal transduction [GO:0007165]
|
cell periphery [GO:0071944]; cytoplasm [GO:0005737]; lateral cell cortex [GO:0097575]; lateral plasma membrane [GO:0016328]; medial cortex [GO:0031097]
|
GTPase activator activity [GO:0005096]; metal ion binding [GO:0046872]; small GTPase binding [GO:0031267]
|
PF00412;PF00620;
|
2.10.110.10;1.10.555.10;
| null | null | null | null | null | null | null | null |
FUNCTION: GTPase-activating protein for Rho-type proteins. {ECO:0000305}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74365
|
SOL1_SCHPO
|
MNNQGFVPASDYPTAVSYPTQGQSYNTQEEQPAYPQRFSTSQGMYAAEYGNANMMNTSENEPNNLAHSQPFRQSPSTQRNLPNQSFDFASNGAWNGSGSVKYSSPMMPSSRIPFQQEKEAAMQQQQQQQQQQQLYQRQMQSREALLSQQIPPNQIGINAHPAVRQTPQPAPSPNTPSGNANQLTPAYAASFDKFMVSLISFMEKRGTPIKSYPQINNTPINLMMLYALVMRAGGSRQVSAHNFWPKISASLGFPSPDAISLLIQYYNSYLLPYEEAWLAAQQQQKSLQQAKANHSANVQSRPKNYPQKPVQTTPEAVHANGSMHGSLHSKSPSPAFTANRFSPAAPTTVSSERNAPPYPSAPTRPTPPTVQTSSSAAPVDSAEPVAYQPIKKPIDPMLGYPLNVAATYRLDESLLRLQMPSIVDLGTVNIQALCMSLQSTLEKEITYAMNVLLILTNDQKWMFPLSECQDVVDALIDVATQCLDNLLSVLPNEDLMEIADKRPSYRQLLYNCCVEISQFSREDFSNSLSENKTKDSINAIDVHNSEQNLLAVFVIFRNLSHFEANQNVLVQNPDFFPLLIRVVKSLNFHATSLLRSSRNTLDLHKDVLIVLCQLSQNFILPNVDVARHVLLFILSFSPFNRKKSKTILNDTLPTSIPSYTPATHPYAGPAINAYAKLLAKDANNKTNFQAIFDNNPKFLDSLFLLLASVVPKFNRHCLKICERRLPLLQQSFFCLAATVSYVKQSEQAANWCNIGEGFFVSMLRLLILLSGHPSLNPPSRVASQYPTTNPFRYVIQSGISTVRRLLSLVEAGNISLSSFPKSETLLAVLLAPTTETSFLKEISNLLDRTGDSDASLENTDDKSGI
| null | null |
chromatin remodeling [GO:0006338]; regulation of transcription by RNA polymerase II [GO:0006357]; transcription initiation-coupled chromatin remodeling [GO:0045815]
|
chromatin [GO:0000785]; nucleus [GO:0005634]; SWI/SNF complex [GO:0016514]
|
transcription cis-regulatory region binding [GO:0000976]
|
PF01388;
|
1.10.150.60;
|
SWI1 family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355, ECO:0000269|PubMed:16823372}.
| null | null | null | null | null |
FUNCTION: Component of the SWI/SNF complex, an ATP-dependent chromatin remodeling complex, required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors. {ECO:0000269|PubMed:18622392}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74369
|
CSS1_SCHPO
|
MSVEKAPELRVLSFNCWGLRFVSKYRTERLKAVGEKLAKCDYDIVLLQEVWSIYDFQEIRNLVSCNLVYSRFFHSAAMGAGLAMFSKFPIIESSMNKYPLNGRPQAFWRGDWYVGKGVATASLQHPSGRIISLFNTHLHAPYGKGADTYLCHRLSQAWYISKLLRAAVQRGHIVIAAGDFNIQPLSVPHEIITSYGLVNDAWLSVYPDQVEHPPNRFSMNDKELVEIAGTTCDSRLNTWRENISSKDMDDFVAKRLDYVFHSPSTCEAKNAKVVFLERVPKLDCSYSDHFAIETVLSIKLQPIPVQETRVSYSIIDDTLGITYQYMARERLHMRLRIAHLLISIPLIIGVHVAIAWCDPAWLKVIILFFTVMLTIAAVVNGFCIGLLFGRWEFNGLLEFVAELKEQKLLCKQYLVDHPLPFAKS
|
3.1.4.-
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
|
cell wall organization [GO:0071555]; ceramide biosynthetic process [GO:0046513]; sphingoid catabolic process [GO:0046521]; sphingolipid catabolic process [GO:0030149]
|
cell periphery [GO:0071944]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; fungal-type vacuole [GO:0000324]; membrane [GO:0016020]; plasma membrane [GO:0005886]
|
inositol phosphosphingolipid phospholipase activity [GO:0052712]; mannosyl-inositol phosphorylceramide phospholipase activity [GO:0052714]; metal ion binding [GO:0046872]; sphingomyelin phosphodiesterase activity [GO:0004767]
|
PF03372;
|
3.60.10.10;
|
Neutral sphingomyelinase family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11514435}; Multi-pass membrane protein {ECO:0000269|PubMed:11514435}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:11514435}; Multi-pass membrane protein {ECO:0000269|PubMed:11514435}.
| null | null |
PATHWAY: Lipid metabolism; sphingolipid metabolism.
| null | null |
FUNCTION: Inositol phosphosphingolipids phospholipase essential for the coordination of cell wall formation. Responsible for the hydrolysis of the phosphosphingolipids (IPS), inositol phosphorylceramide (IPC), mannosylinositol phosphorylceramide (MIPC), and mannosyldiinositol phosphorylceramide (M(IP)2C). {ECO:0000269|PubMed:11514435}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74372
|
DUO1_SCHPO
|
MTSELQQELQILRSFNYTIEKLTDGLSASKEKIKSFETSINNSNRLIQLWSSVLSQTEHTQNLILNSDWKGLSFDNEELERLQHQKMLQIQAEEQRKIELQQEQERLEQERRQKEEAIALQKQQQQRLLRSKDPKVRPARRAASSYVPSRPSHVPRSSSMNVRSRVSMATTSNPNSLRTPSSSFASHRQSAIPKSATSSAPTIPTSNLPSVASSIPNNGLNSSNRKSIISKTSSRLRPPSRVSNVPSVPQHPSTRSRTSTRETTQPPFTTNPSNRSKRTTLR
| null | null |
attachment of spindle microtubules to kinetochore [GO:0008608]; cell division [GO:0051301]; mitotic sister chromatid biorientation [GO:1990758]; protein transport along microtubule to mitotic spindle pole body [GO:1990976]; spindle attachment to meiosis I kinetochore [GO:0051455]
|
cytoplasm [GO:0005737]; DASH complex [GO:0042729]; microtubule [GO:0005874]; mitotic spindle [GO:0072686]
| null |
PF08651;
| null |
DASH complex DUO1 family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P53168}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P53168}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:P53168}. Cytoplasm, cytoskeleton {ECO:0000305|PubMed:20624975}. Note=Associates with the mitotic spindle and the kinetochore (By similarity). In the cytoskeleton, localizes to cortical microtubules (Probable). {ECO:0000250|UniProtKB:P53168, ECO:0000305|PubMed:20624975}.
| null | null | null | null | null |
FUNCTION: Component of the DASH complex that connects microtubules with kinetochores and couples microtubule depolymerisation to chromosome movement; it is involved in retrieving kinetochores to the spindle poles before their re-orientation on the spindle in early mitosis and allows microtubule depolymerization to pull chromosomes apart and resist detachment during anaphase (PubMed:16079914, PubMed:20624975). Kinetochores, consisting of a centromere-associated inner segment and a microtubule-contacting outer segment, play a crucial role in chromosome segregation by mediating the physical connection between centromeric DNA and microtubules (PubMed:16079914, PubMed:20624975). Kinetochores also serve as an input point for the spindle assembly checkpoint, which delays anaphase until all chromosomes have bioriented on the mitotic spindle (PubMed:16079915). The DASH complex mediates bipolar kinetochore-microtubule attachments and facilitates the formation of additional interactions between outer kinetochore components and spindle microtubules (PubMed:16079914). During chromosome movement along the microtubule, it is required both for the sliding of kinetochores along the lateral side of the microtubule and also for microtubule end-on pulling on the kinetochore (PubMed:18256284). Modulates cytoplasmic microtubule dynamics by tracking the plus-end of shortening microtubules and slowing their depolymerization (PubMed:20624975). {ECO:0000269|PubMed:16079914, ECO:0000269|PubMed:16079915, ECO:0000269|PubMed:18256284, ECO:0000269|PubMed:20624975}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74374
|
PGM_SCHPO
|
MIETIPTKPYEGQRPGTSGLRKKVTVFEQPNYVENFVQATMDVVEPSAKGAHLVVGGDGRYFNFHAIQVIAAIAAGNGVEKIIVGTNGYLSTPAASHIIRKYKLTGGIILTASHNAGGPKNDFGIKYNLGNGGPAPESVTEKIYSITKTISEYKMVKIPPLDLTTTGVRRYGPLTVEVIDPVKDYVQLMKEIFDFDLIRSFLSKNPDFTFVFDALHGITGPYGEALFCKELGMPSSVCQNCKPLPDFGGGHPDPNLTYAKSLVARVDRDNIVMGAASDGDGDRNMIYGANAFVTPSDSVAIIAHHAELIPYFRDGGVHGFARSMPTSGAIDRVGKYKGKNVYEVPTGWKFFCNLFDAKRLSICGEESFGTGSDHIREKDGVWGILCWLNILAGLNAQNPKIKTLIDVKKDFYNIYGRTFYSRYDYEELENEAAGKVMDRMRAIADDKSKVGEAVLPGFVVSEAGDFEYHDPIDGSESKHQGLYIKFENGSRIVTRLSGTGSSGATLRLYMEKHESDSSKFDLDAQVALKPVVHAALEILALEELTGRKEPTVIT
|
5.4.2.2
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P00949}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P00949};
|
carbohydrate metabolic process [GO:0005975]; galactose catabolic process [GO:0019388]; glucose 1-phosphate metabolic process [GO:0019255]; glucose 6-phosphate metabolic process [GO:0051156]; glucose metabolic process [GO:0006006]; glycogen biosynthetic process [GO:0005978]; trehalose biosynthetic process [GO:0005992]; UDP-glucose metabolic process [GO:0006011]
|
cytosol [GO:0005829]; nucleus [GO:0005634]
|
metal ion binding [GO:0046872]; phosphoglucomutase activity [GO:0004614]
|
PF02878;PF02879;PF02880;
|
3.40.120.10;3.30.310.50;
|
Phosphohexose mutase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
|
CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate; Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601; EC=5.4.2.2; Evidence={ECO:0000250|UniProtKB:P37012}; CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 1-phosphate + O-phospho-L-seryl-[protein] = alpha-D-glucose 1,6-bisphosphate + L-seryl-[protein]; Xref=Rhea:RHEA:68748, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:29999, ChEBI:CHEBI:58392, ChEBI:CHEBI:58601, ChEBI:CHEBI:83421; Evidence={ECO:0000250|UniProtKB:P37012}; CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 1,6-bisphosphate + L-seryl-[protein] = alpha-D-glucose 6-phosphate + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:68752, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:29999, ChEBI:CHEBI:58225, ChEBI:CHEBI:58392, ChEBI:CHEBI:83421; Evidence={ECO:0000250|UniProtKB:P37012};
| null | null | null | null |
FUNCTION: Catalyzes the reversible isomerization of alpha-D-glucose 1-phosphate to alpha-D-glucose 6-phosphate (By similarity). The mechanism proceeds via the intermediate compound alpha-D-glucose 1,6-bisphosphate (By similarity). Key enzyme in hexose metabolism (By similarity). The reverse reaction is an essential step for biosynthesis because glucose 1-phosphate is the starting point for the synthesis of UDP-glucose, which acts as a precursor for the synthesis of oligosaccharides and trehalose (By similarity). {ECO:0000250|UniProtKB:P37012}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74384
|
ERFB_SCHPO
|
MSYEKHSDAKASRYAWNQPWNPFEVTLSDPTYPMNLEEKNQIPYRFQSVPDDVPEVPHIESRYKNLPGNNIYLCCGRLQMSSQYKAFLISLFALILPGVLFFIFSAFWLWHHVSPAVPITFAYLYALAVVSMFKCSTADPGILPRNAYSLTYNPAHPWSVIPEDRKVLVGSTRSDSVFVNTVYCHTCHLYRPPRASHCHLCDNCVEYLDHHCIWLNTCIGRRNYRYYFIFLLSVVLSALYLTGLGFYTSIGSFHESTDTNFAAHLRRPWAGVSFFLGIYGALGAILPGILFCYQCYLISVGQNVHEYLRAKSTETEDVHPFHDSIWLNFLVVLCRPKNVSYVRPTRKSYV
|
2.3.1.225
| null |
protein targeting to membrane [GO:0006612]; sporulation resulting in formation of a cellular spore [GO:0030435]
|
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum palmitoyltransferase complex [GO:0031211]; Golgi apparatus [GO:0005794]; Golgi cisterna membrane [GO:0032580]
|
protein-cysteine S-palmitoyltransferase activity [GO:0019706]
|
PF01529;
| null |
DHHC palmitoyltransferase family, ERF2/ZDHHC9 subfamily
|
PTM: Autopalmitoylated. {ECO:0000250|UniProtKB:Q9UIJ5}.
|
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q06551}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q06551}. Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
|
CATALYTIC ACTIVITY: Reaction=hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:36683, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:29950, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:74151; EC=2.3.1.225; Evidence={ECO:0000305|PubMed:23843742};
| null | null | null | null |
FUNCTION: The erf2-erf4 complex is a palmitoyltransferase with a major role in driving sexual development (PubMed:16303567, PubMed:23843742). Palmitoylates ras1 (PubMed:23843742). Palmitoylates isp3 (PubMed:23843742). Palmitoylates rho3 (PubMed:23843742). {ECO:0000269|PubMed:16303567, ECO:0000269|PubMed:23843742}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O74420
|
WTF13_SCHPO
|
MKNKDYPLRSSMDELSTKNDNEIDLEKGPLPEYNSEDGSTLPPYSEIWKYIKTVSEDSSTGPTEIANPNVERRQEFKDSHPNIYSLLRLLISVLAVIVVFFTAWVCVNPLEKSIFGKVAFSVTIGITCPIVFIAIFCFFETWTQAVAQCIKVTVIFLAQCVKVTAISLAQCVKVTAVFLAKCVKVTAVFLAKCVKVIAVGLYNSKKDLVVTIWLAWVVICFILFGCVKDGRLNLNKALICSTCSISAALFFILLLVCIPIWTLKHMLFGLFQVLGVQSCVVIVTKGLMYLFDKHIDATGYEIEASSLFVIGNFLFFYEMERPGALKRMPKFIGNGIASFLGGLGNAFGGIGNAFGGIGNAIGRIGNAFRGANDNNDIPLGEMDVESEV
| null | null |
meiotic drive [GO:0110134]
|
ascus epiplasm [GO:0072324]; cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; vacuolar membrane [GO:0005774]
| null |
PF03303;
| null |
WTF family
| null |
SUBCELLULAR LOCATION: [Isoform 1]: Spore membrane {ECO:0000255, ECO:0000269|PubMed:30475921, ECO:0000269|PubMed:32032353}; Multi-pass membrane protein {ECO:0000255}. Vacuole membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Note=Contained within spores expressing the isoform and localizes isoform 2 to the vacuole. {ECO:0000250|UniProtKB:A0A218N034}.; SUBCELLULAR LOCATION: [Isoform 2]: Ascus epiplasm {ECO:0000269|PubMed:30475921}. Cytoplasm {ECO:0000250|UniProtKB:A0A218N034}. Spore membrane {ECO:0000255, ECO:0000269|PubMed:30475921, ECO:0000269|PubMed:32032353}; Multi-pass membrane protein {ECO:0000255}. Vacuole membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes in trans to all spores within an ascus. Localization to the spore vacuole is dependent on isoform 1. {ECO:0000250|UniProtKB:A0A218N034}.
| null | null | null | null | null |
FUNCTION: Promotes unequal transmission of alleles from the parental zygote to progeny spores by acting as poison/antidote system where the poison and antidote proteins are produced from the same locus; the poison component is trans-acting and targets all spores within an ascus whereas the antidote component is spore-specific, leading to poisoning of all progeny that do not inherit the allele. {ECO:0000269|PubMed:30475921, ECO:0000269|PubMed:32032353, ECO:0000269|PubMed:32790622}.; FUNCTION: [Isoform 1]: Localizes isoform 2 to the vacuole thereby facilitating its degradation (By similarity). In addition to suppressing isoform 2, also suppresses S.pombe strain FY29033 wtf18 isoform 2 (PubMed:32032353). {ECO:0000250|UniProtKB:A0A218N034, ECO:0000269|PubMed:32032353}.; FUNCTION: [Isoform 2]: Forms toxic aggregates that disrupt spore maturation. {ECO:0000250|UniProtKB:A0A218N034}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
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