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
|
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
O60902
|
SHOX2_HUMAN
|
MEELTAFVSKSFDQKVKEKKEAITYREVLESGPLRGAKEPTGCTEAGRDDRSSPAVRAAGGGGGGGGGGGGGGGGGGVGGGGAGGGAGGGRSPVRELDMGAAERSREPGSPRLTEVSPELKDRKEDAKGMEDEGQTKIKQRRSRTNFTLEQLNELERLFDETHYPDAFMREELSQRLGLSEARVQVWFQNRRAKCRKQENQLHKGVLIGAASQFEACRVAPYVNVGALRMPFQQDSHCNVTPLSFQVQAQLQLDSAVAHAHHHLHPHLAAHAPYMMFPAPPFGLPLATLAADSASAASVVAAAAAAKTTSKNSSIADLRLKAKKHAAALGL
| null | null |
cardiac pacemaker cell differentiation [GO:0060920]; cardiac right atrium morphogenesis [GO:0003213]; cartilage development involved in endochondral bone morphogenesis [GO:0060351]; chondrocyte development [GO:0002063]; embryonic digestive tract morphogenesis [GO:0048557]; embryonic forelimb morphogenesis [GO:0035115]; embryonic skeletal joint morphogenesis [GO:0060272]; mesenchymal cell proliferation [GO:0010463]; muscle tissue morphogenesis [GO:0060415]; negative regulation of transcription by RNA polymerase II [GO:0000122]; nervous system development [GO:0007399]; osteoblast differentiation [GO:0001649]; positive regulation of axonogenesis [GO:0050772]; positive regulation of mesenchymal cell proliferation [GO:0002053]; positive regulation of skeletal muscle fiber development [GO:0048743]; positive regulation of smoothened signaling pathway [GO:0045880]; positive regulation of stem cell proliferation [GO:2000648]; regulation of branching morphogenesis of a nerve [GO:2000172]; regulation of chondrocyte differentiation [GO:0032330]; regulation of heart rate [GO:0002027]; regulation of transcription by RNA polymerase II [GO:0006357]; sinoatrial node cell development [GO:0060931]; sinoatrial node development [GO:0003163]; sinoatrial valve development [GO:0003172]; skeletal system development [GO:0001501]; smoothened signaling pathway [GO:0007224]; stem cell proliferation [GO:0072089]
|
chromatin [GO:0000785]; nucleus [GO:0005634]
|
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; sequence-specific double-stranded DNA binding [GO:1990837]
|
PF00046;PF03826;
|
1.10.10.60;
|
Paired homeobox family, Bicoid subfamily
| null |
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: May be a growth regulator and have a role in specifying neural systems involved in processing somatosensory information, as well as in face and body structure formation.
|
Homo sapiens (Human)
|
O60906
|
NSMA_HUMAN
|
MKPNFSLRLRIFNLNCWGIPYLSKHRADRMRRLGDFLNQESFDLALLEEVWSEQDFQYLRQKLSPTYPAAHHFRSGIIGSGLCVFSKHPIQELTQHIYTLNGYPYMIHHGDWFSGKAVGLLVLHLSGMVLNAYVTHLHAEYNRQKDIYLAHRVAQAWELAQFIHHTSKKADVVLLCGDLNMHPEDLGCCLLKEWTGLHDAYLETRDFKGSEEGNTMVPKNCYVSQQELKPFPFGVRIDYVLYKAVSGFYISCKSFETTTGFDPHRGTPLSDHEALMATLFVRHSPPQQNPSSTHGPAERSPLMCVLKEAWTELGLGMAQARWWATFASYVIGLGLLLLALLCVLAAGGGAGEAAILLWTPSVGLVLWAGAFYLFHVQEVNGLYRAQAELQHVLGRAREAQDLGPEPQPALLLGQQEGDRTKEQ
|
3.1.4.12
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:10608884};
|
ceramide biosynthetic process [GO:0046513]; 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]; phosphoric diester hydrolase activity [GO:0008081]; sphingomyelin phosphodiesterase activity [GO:0004767]
|
PF03372;
|
3.60.10.10;
|
Neutral sphingomyelinase family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O70572}; 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:10608884, ECO:0000269|PubMed:14741383}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19254; Evidence={ECO:0000305|PubMed:10608884}; 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:0000269|PubMed:14741383}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45301; Evidence={ECO:0000305|PubMed:14741383}; 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:0000269|PubMed:10608884, ECO:0000269|PubMed:14741383}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39924; Evidence={ECO:0000305|PubMed:14741383}; 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:0000269|PubMed:10608884}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36088; Evidence={ECO:0000305|PubMed:10608884}; 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:0000269|PubMed:14741383}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41120; Evidence={ECO:0000305|PubMed:14741383}; 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:0000269|PubMed:14741383}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45297; Evidence={ECO:0000305|PubMed:14741383};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=26.2 uM for sphingomyelin (at pH 7.4 and 37 degrees Celsius in the presence of 0.05% Triton X-100) {ECO:0000269|PubMed:10608884}; KM=26.9 uM for 1-O-octadecyl-sn-glycero-3-phosphocholine (at pH 7.4 and 37 degrees Celsius) {ECO:0000269|PubMed:10608884}; KM=27.1 uM for 1-O-hexadecyl-sn-glycero-3-phosphocholine (at pH 7.4 and 37 degrees Celsius) {ECO:0000269|PubMed:10608884}; Vmax=367 nmol/h/mg enzyme with sphingomyelin as substrate (at pH 7.5 and 37 degrees Celsius in presence of 0.1% Triton X-100) {ECO:0000269|PubMed:14741383}; Vmax=434 nmol/h/mg enzyme with sphingosylphosphocholine as substrate (at pH 7.5 and 37 degrees Celsius) {ECO:0000269|PubMed:14741383}; Vmax=349 nmol/h/mg enzyme with 1-O-octadecyl-sn-glycero-3-phosphocholine as substrate (at pH 7.5 and 37 degrees Celsius) {ECO:0000269|PubMed:14741383}; Vmax=611 nmol/h/mg enzyme with 1-hexadecanoyl-sn-glycero-3-phosphocholine as substrate (at pH 7.5 and 37 degrees Celsius) {ECO:0000269|PubMed:14741383};
|
PATHWAY: Lipid metabolism; sphingolipid metabolism. {ECO:0000269|PubMed:10608884, ECO:0000269|PubMed:14741383}.
| null | null |
FUNCTION: Catalyzes, at least in vitro, the hydrolysis of sphingomyelin to form ceramide and phosphocholine (PubMed:10608884). Also hydrolyzes 1-O-alkyl-2-lyso-sn-glycero-3-phosphocholine (lyso-platelet-activating factor) in vivo (PubMed:10608884). Also acts on 1-acyl-2-lyso-sn-glycero-3-phosphocholine (lyso-PC) and sphingosylphosphocholine (PubMed:10608884, PubMed:14741383). {ECO:0000269|PubMed:10608884, ECO:0000269|PubMed:14741383}.
|
Homo sapiens (Human)
|
O60907
|
TBL1X_HUMAN
|
MTELAGASSSCCHRPAGRGAMQSVLHHFQRLRGREGGSHFINTSSPRGEAKMSITSDEVNFLVYRYLQESGFSHSAFTFGIESHISQSNINGTLVPPAALISILQKGLQYVEAEISINEDGTVFDGRPIESLSLIDAVMPDVVQTRQQAFREKLAQQQASAAAAAAAATAAATAATTTSAGVSHQNPSKNREATVNGEENRAHSVNNHAKPMEIDGEVEIPSSKATVLRGHESEVFICAWNPVSDLLASGSGDSTARIWNLNENSNGGSTQLVLRHCIREGGHDVPSNKDVTSLDWNTNGTLLATGSYDGFARIWTEDGNLASTLGQHKGPIFALKWNRKGNYILSAGVDKTTIIWDAHTGEAKQQFPFHSAPALDVDWQNNTTFASCSTDMCIHVCRLGCDRPVKTFQGHTNEVNAIKWDPSGMLLASCSDDMTLKIWSMKQEVCIHDLQAHNKEIYTIKWSPTGPATSNPNSNIMLASASFDSTVRLWDIERGVCTHTLTKHQEPVYSVAFSPDGKYLASGSFDKCVHIWNTQSGNLVHSYRGTGGIFEVCWNARGDKVGASASDGSVCVLDLRK
| null | null |
negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription by RNA polymerase II [GO:0045944]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein stabilization [GO:0050821]; proteolysis [GO:0006508]; regulation of transcription by RNA polymerase II [GO:0006357]; sensory perception of sound [GO:0007605]
|
histone deacetylase complex [GO:0000118]; mitotic spindle [GO:0072686]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription repressor complex [GO:0017053]
|
histone binding [GO:0042393]; identical protein binding [GO:0042802]; transcription cis-regulatory region binding [GO:0000976]; transcription corepressor activity [GO:0003714]
|
PF08513;PF00400;
|
1.20.960.30;2.130.10.10;
|
WD repeat EBI family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Colocalized with MECP2 to the heterochromatin foci. {ECO:0000250|UniProtKB:Q9QXE7}.
| null | null | null | null | null |
FUNCTION: F-box-like protein involved in the recruitment of the ubiquitin/19S proteasome complex to nuclear receptor-regulated transcription units (PubMed:14980219). Plays an essential role in transcription activation mediated by nuclear receptors. Probably acts as integral component of corepressor complexes that mediates the recruitment of the 19S proteasome complex, leading to the subsequent proteasomal degradation of transcription repressor complexes, thereby allowing cofactor exchange (PubMed:21240272). {ECO:0000269|PubMed:14980219, ECO:0000269|PubMed:21240272}.
|
Homo sapiens (Human)
|
O60909
|
B4GT2_HUMAN
|
MSRLLGGTLERVCKAVLLLCLLHFLVAVILYFDVYAQHLAFFSRFSARGPAHALHPAASSSSSSSNCSRPNATASSSGLPEVPSALPGPTAPTLPPCPDSPPGLVGRLLIEFTSPMPLERVQRENPGVLMGGRYTPPDCTPAQTVAVIIPFRHREHHLRYWLHYLHPILRRQRLRYGVYVINQHGEDTFNRAKLLNVGFLEALKEDAAYDCFIFSDVDLVPMDDRNLYRCGDQPRHFAIAMDKFGFRLPYAGYFGGVSGLSKAQFLRINGFPNEYWGWGGEDDDIFNRISLTGMKISRPDIRIGRYRMIKHDRDKHNEPNPQRFTKIQNTKLTMKRDGIGSVRYQVLEVSRQPLFTNITVDIGRPPSWPPRG
|
2.4.1.-; 2.4.1.22; 2.4.1.38; 2.4.1.90
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
|
carbohydrate metabolic process [GO:0005975]; cerebellar Purkinje cell layer development [GO:0021680]; glycosylation [GO:0070085]; locomotory behavior [GO:0007626]; memory [GO:0007613]; protein glycosylation [GO:0006486]; visual learning [GO:0008542]
|
Golgi apparatus [GO:0005794]; Golgi cisterna membrane [GO:0032580]; Golgi membrane [GO:0000139]; intracellular membrane-bounded organelle [GO:0043231]; nucleoplasm [GO:0005654]
|
beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase activity [GO:0003831]; galactosyltransferase activity [GO:0008378]; lactose synthase activity [GO:0004461]; metal ion binding [GO:0046872]; N-acetyllactosamine synthase activity [GO:0003945]
|
PF02709;PF13733;
| null |
Glycosyltransferase 7 family
| null |
SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein. Note=Trans cisternae of Golgi stack.
|
CATALYTIC ACTIVITY: Reaction=D-glucose + UDP-alpha-D-galactose = H(+) + lactose + UDP; Xref=Rhea:RHEA:12404, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378, ChEBI:CHEBI:17716, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914; EC=2.4.1.22; Evidence={ECO:0000269|PubMed:9405390}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12405; Evidence={ECO:0000269|PubMed:9405390}; CATALYTIC ACTIVITY: Reaction=an N-acetyl-beta-D-glucosaminyl derivative + UDP-alpha-D-galactose = a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + H(+) + UDP; Xref=Rhea:RHEA:22932, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:61631, ChEBI:CHEBI:66914, ChEBI:CHEBI:133507; EC=2.4.1.38; Evidence={ECO:0000269|PubMed:9405390}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22933; Evidence={ECO:0000269|PubMed:9405390}; CATALYTIC ACTIVITY: Reaction=N-acetyl-D-glucosamine + UDP-alpha-D-galactose = beta-D-galactosyl-(1->4)-N-acetyl-D-glucosamine + H(+) + UDP; Xref=Rhea:RHEA:17745, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:60152, ChEBI:CHEBI:66914, ChEBI:CHEBI:506227; EC=2.4.1.90; Evidence={ECO:0000269|PubMed:11588157, ECO:0000269|PubMed:9405390}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17746; Evidence={ECO:0000269|PubMed:9405390};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=71 uM for GlcNAc-B-S-pNP {ECO:0000269|PubMed:11588157}; KM=0.011 mM for UDP-galactose {ECO:0000269|PubMed:9405390}; KM=0.16 mM for benzyl-beta-D-GlcNAc {ECO:0000269|PubMed:9405390}; KM=2.65 mM for D-GlcNAc {ECO:0000269|PubMed:9405390}; Vmax=207.6 pmol/min/mg enzyme towards UDP-galactose {ECO:0000269|PubMed:9405390}; Vmax=352 pmol/min/mg enzyme towards for benzyl-beta-D-GlcNAc {ECO:0000269|PubMed:9405390}; Vmax=237.6 pmol/min/mg enzyme towards D-GlcNAc {ECO:0000269|PubMed:9405390};
|
PATHWAY: Protein modification; protein glycosylation.
| null | null |
FUNCTION: Responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids (PubMed:9405390). Can produce lactose (PubMed:9405390). {ECO:0000269|PubMed:9405390}.
|
Homo sapiens (Human)
|
O60911
|
CATL2_HUMAN
|
MNLSLVLAAFCLGIASAVPKFDQNLDTKWYQWKATHRRLYGANEEGWRRAVWEKNMKMIELHNGEYSQGKHGFTMAMNAFGDMTNEEFRQMMGCFRNQKFRKGKVFREPLFLDLPKSVDWRKKGYVTPVKNQKQCGSCWAFSATGALEGQMFRKTGKLVSLSEQNLVDCSRPQGNQGCNGGFMARAFQYVKENGGLDSEESYPYVAVDEICKYRPENSVANDTGFTVVAPGKEKALMKAVATVGPISVAMDAGHSSFQFYKSGIYFEPDCSSKNLDHGVLVVGYGFEGANSNNSKYWLVKNSWGPEWGSNGYVKIAKDKNNHCGIATAASYPNV
|
3.4.22.43
| null |
antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; extracellular matrix disassembly [GO:0022617]; immune response [GO:0006955]; positive regulation of apoptotic signaling pathway [GO:2001235]; proteolysis involved in protein catabolic process [GO:0051603]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]; lysosomal lumen [GO:0043202]
|
cysteine-type endopeptidase activator activity involved in apoptotic process [GO:0008656]; cysteine-type endopeptidase activity [GO:0004197]; cysteine-type peptidase activity [GO:0008234]; serine-type endopeptidase activity [GO:0004252]
|
PF08246;PF00112;
|
3.90.70.10;
|
Peptidase C1 family
| null |
SUBCELLULAR LOCATION: Lysosome {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=The recombinant enzyme hydrolyzes proteins (serum albumin, collagen) and synthetic substrates (Z-Phe-Arg-NHMec > Z-Leu-Arg-NHMec > Z-Val-Arg-NHMec).; EC=3.4.22.43; Evidence={ECO:0000269|PubMed:10029531};
| null | null | null | null |
FUNCTION: Cysteine protease. May have an important role in corneal physiology. {ECO:0000269|PubMed:10029531, ECO:0000269|PubMed:9727401}.
|
Homo sapiens (Human)
|
O60921
|
HUS1_HUMAN
|
MKFRAKIVDGACLNHFTRISNMIAKLAKTCTLRISPDKLNFILCDKLANGGVSMWCELEQENFFNEFQMEGVSAENNEIYLELTSENLSRALKTAQNARALKIKLTNKHFPCLTVSVELLSMSSSSRIVTHDIPIKVIPRKLWKDLQEPVVPDPDVSIYLPVLKTMKSVVEKMKNISNHLVIEANLDGELNLKIETELVCVTTHFKDLGNPPLASESTHEDRNVEHMAEVHIDIRKLLQFLAGQQVNPTKALCNIVNNKMVHFDLLHEDVSLQYFIPALS
| null | null |
cellular response to ionizing radiation [GO:0071479]; DNA damage checkpoint signaling [GO:0000077]; DNA damage response [GO:0006974]; DNA repair [GO:0006281]; double-strand break repair via homologous recombination [GO:0000724]; embryo development ending in birth or egg hatching [GO:0009792]; meiotic DNA integrity checkpoint signaling [GO:0044778]; mitotic DNA replication checkpoint signaling [GO:0033314]; mitotic intra-S DNA damage checkpoint signaling [GO:0031573]; nucleotide-excision repair [GO:0006289]; regulation of protein phosphorylation [GO:0001932]; response to UV [GO:0009411]; telomere maintenance [GO:0000723]
|
checkpoint clamp complex [GO:0030896]; cytosol [GO:0005829]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; site of double-strand break [GO:0035861]
| null |
PF04005;
|
3.70.10.10;
|
HUS1 family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10846170, ECO:0000269|PubMed:11077446}. Cytoplasm, cytosol {ECO:0000269|PubMed:11077446}. Note=In discrete nuclear foci upon DNA damage (PubMed:11077446). According to PubMed:11077446, localized also in the cytoplasm (PubMed:11077446). DNA damage induces its nuclear translocation (PubMed:11077446). Shuttles between the nucleus and the cytoplasm (PubMed:11077446). {ECO:0000269|PubMed:11077446}.
| null | null | null | null | null |
FUNCTION: Component of the 9-1-1 cell-cycle checkpoint response complex that plays a major role in DNA repair (PubMed:21659603). The 9-1-1 complex is recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex (PubMed:21659603). Acts then as a sliding clamp platform on DNA for several proteins involved in long-patch base excision repair (LP-BER) (PubMed:21659603). The 9-1-1 complex stimulates DNA polymerase beta (POLB) activity by increasing its affinity for the 3'-OH end of the primer-template and stabilizes POLB to those sites where LP-BER proceeds; endonuclease FEN1 cleavage activity on substrates with double, nick, or gap flaps of distinct sequences and lengths; and DNA ligase I (LIG1) on long-patch base excision repair substrates (PubMed:21659603). The 9-1-1 complex is necessary for the recruitment of RHNO1 to sites of double-stranded breaks (DSB) occurring during the S phase (PubMed:21659603). {ECO:0000269|PubMed:21659603}.
|
Homo sapiens (Human)
|
O60927
|
PP1RB_HUMAN
|
MAEAGAGLSETVTETTVTVTTEPENRSLTIKLRKRKPEKKVEWTSDTVDNEHMGRRSSKCCCIYEKPRAFGESSTESDEEEEEGCGHTHCVRGHRKGRRRATLGPTPTTPPQPPDPSQPPPGPMQH
|
2.3.2.27
| null |
defense response to Gram-positive bacterium [GO:0050830]; negative regulation of cytokine production [GO:0001818]; protein ubiquitination [GO:0016567]; ubiquitin-dependent protein catabolic process [GO:0006511]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
phosphatase binding [GO:0019902]; protein phosphatase 1 binding [GO:0008157]; protein phosphatase inhibitor activity [GO:0004864]; protein serine/threonine phosphatase inhibitor activity [GO:0004865]; ubiquitin protein ligase activity [GO:0061630]
|
PF07491;
| null | null |
PTM: Auto-ubiquitinated. {ECO:0000269|PubMed:27805901}.
| null |
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27;
| null |
PATHWAY: Protein modification; protein ubiquitination.
| null | null |
FUNCTION: Atypical E3 ubiquitin-protein ligase which ubiquitinates TLR2 at 'Lys-754' leading to its degradation by the proteasome. Plays a role in regulating inflammatory cytokine release and gram-positive bacterial clearance by functioning, in part, through the ubiquitination and degradation of TLR2 (PubMed:27805901). Inhibitor of protein phosphatase 1 (PubMed:9843442). {ECO:0000269|PubMed:27805901, ECO:0000269|PubMed:9843442}.
|
Homo sapiens (Human)
|
O60928
|
KCJ13_HUMAN
|
MDSSNCKVIAPLLSQRYRRMVTKDGHSTLQMDGAQRGLAYLRDAWGILMDMRWRWMMLVFSASFVVHWLVFAVLWYVLAEMNGDLELDHDAPPENHTICVKYITSFTAAFSFSLETQLTIGYGTMFPSGDCPSAIALLAIQMLLGLMLEAFITGAFVAKIARPKNRAFSIRFTDTAVVAHMDGKPNLIFQVANTRPSPLTSVRVSAVLYQERENGKLYQTSVDFHLDGISSDECPFFIFPLTYYHSITPSSPLATLLQHENPSHFELVVFLSAMQEGTGEICQRRTSYLPSEIMLHHCFASLLTRGSKGEYQIKMENFDKTVPEFPTPLVSKSPNRTDLDIHINGQSIDNFQISETGLTE
| null | null |
potassium ion import across plasma membrane [GO:1990573]; potassium ion transport [GO:0006813]; regulation of monoatomic ion transmembrane transport [GO:0034765]
|
monoatomic ion channel complex [GO:0034702]; plasma membrane [GO:0005886]
|
inward rectifier potassium channel activity [GO:0005242]
|
PF01007;PF17655;
|
1.10.287.70;2.60.40.1400;
|
Inward rectifier-type potassium channel (TC 1.A.2.1) family, KCNJ13 subfamily
|
PTM: Phosphorylation at Ser-201 by PKC strongly inhibits ionic currents, while phosphorylation at Ser-287 by PKA increases them. {ECO:0000269|PubMed:18976636}.
|
SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
| null | null | null | null | null |
FUNCTION: Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. KCNJ13 has a very low single channel conductance, low sensitivity to block by external barium and cesium, and no dependence of its inward rectification properties on the internal blocking particle magnesium.
|
Homo sapiens (Human)
|
O60930
|
RNH1_HUMAN
|
MSWLLFLAHRVALAALPCRRGSRGFGMFYAVRRGRKTGVFLTWNECRAQVDRFPAARFKKFATEDEAWAFVRKSASPEVSEGHENQHGQESEAKASKRLREPLDGDGHESAEPYAKHMKPSVEPAPPVSRDTFSYMGDFVVVYTDGCCSSNGRRRPRAGIGVYWGPGHPLNVGIRLPGRQTNQRAEIHAACKAIEQAKTQNINKLVLYTDSMFTINGITNWVQGWKKNGWKTSAGKEVINKEDFVALERLTQGMDIQWMHVPGHSGFIGNEEADRLAREGAKQSED
|
3.1.26.4
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Binds 1 Mg(2+) ion per subunit. May bind a second metal ion at a regulatory site, or after substrate binding.;
|
DNA replication, removal of RNA primer [GO:0043137]; RNA catabolic process [GO:0006401]
|
cytoplasm [GO:0005737]
|
magnesium ion binding [GO:0000287]; nucleic acid binding [GO:0003676]; RNA binding [GO:0003723]; RNA nuclease activity [GO:0004540]; RNA-DNA hybrid ribonuclease activity [GO:0004523]
|
PF01693;PF00075;
|
3.30.420.10;3.40.970.10;
|
RNase H family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU00408};
| null | null | null | null |
FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids (PubMed:10497183). Plays a role in RNA polymerase II (RNAp II) transcription termination by degrading R-loop RNA-DNA hybrid formation at G-rich pause sites located downstream of the poly(A) site and behind the elongating RNAp II (PubMed:21700224). {ECO:0000269|PubMed:10497183, ECO:0000269|PubMed:21700224}.
|
Homo sapiens (Human)
|
O60931
|
CTNS_HUMAN
|
MIRNWLTIFILFPLKLVEKCESSVSLTVPPVVKLENGSSTNVSLTLRPPLNATLVITFEITFRSKNITILELPDEVVVPPGVTNSSFQVTSQNVGQLTVYLHGNHSNQTGPRIRFLVIRSSAISIINQVIGWIYFVAWSISFYPQVIMNWRRKSVIGLSFDFVALNLTGFVAYSVFNIGLLWVPYIKEQFLLKYPNGVNPVNSNDVFFSLHAVVLTLIIIVQCCLYERGGQRVSWPAIGFLVLAWLFAFVTMIVAAVGVTTWLQFLFCFSYIKLAVTLVKYFPQAYMNFYYKSTEGWSIGNVLLDFTGGSFSLLQMFLQSYNNDQWTLIFGDPTKFGLGVFSIVFDVVFFIQHFCLYRKRPGYDQLN
| null | null |
adult walking behavior [GO:0007628]; amino acid metabolic process [GO:0006520]; ATP metabolic process [GO:0046034]; brain development [GO:0007420]; brush border assembly [GO:1904970]; cognition [GO:0050890]; glutathione metabolic process [GO:0006749]; grooming behavior [GO:0007625]; L-cystine transport [GO:0015811]; lens development in camera-type eye [GO:0002088]; long-term memory [GO:0007616]; melanin biosynthetic process [GO:0042438]; monoatomic ion transport [GO:0006811]; negative regulation of apoptotic process [GO:0043066]; negative regulation of hydrogen peroxide biosynthetic process [GO:0010730]; positive regulation of mitochondrial membrane potential [GO:0010918]; positive regulation of thyroid hormone generation [GO:2000611]; positive regulation of TORC1 signaling [GO:1904263]; protein transport [GO:0015031]; proximal tubule morphogenesis [GO:0072158]; regulation of melanin biosynthetic process [GO:0048021]; regulation of TORC1 signaling [GO:1903432]; renal albumin absorption [GO:0097018]; renal glucose absorption [GO:0035623]; renal phosphate ion absorption [GO:0097291]; renal water absorption [GO:0070295]; thyroid gland development [GO:0030878]; transmembrane transport [GO:0055085]; visual learning [GO:0008542]
|
extracellular exosome [GO:0070062]; intracellular membrane-bounded organelle [GO:0043231]; late endosome [GO:0005770]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; melanosome [GO:0042470]; melanosome membrane [GO:0033162]; plasma membrane [GO:0005886]
|
L-cystine transmembrane transporter activity [GO:0015184]; solute:proton symporter activity [GO:0015295]
|
PF04193;
|
1.20.1280.290;
|
Cystinosin family
| null |
SUBCELLULAR LOCATION: [Isoform 1]: Lysosome membrane {ECO:0000269|PubMed:11150305, ECO:0000269|PubMed:11689434, ECO:0000269|PubMed:15128704, ECO:0000269|PubMed:17897319, ECO:0000269|PubMed:25753619, ECO:0000269|PubMed:28082515}; Multi-pass membrane protein {ECO:0000269|PubMed:36113465}. Melanosome membrane {ECO:0000269|PubMed:22649030}; Multi-pass membrane protein {ECO:0000269|PubMed:36113465}. Note=AP-3 complex is required for localization to the lysosome. {ECO:0000269|PubMed:25753619}.; SUBCELLULAR LOCATION: [Isoform 2]: Lysosome membrane {ECO:0000269|PubMed:18337546, ECO:0000269|PubMed:27148969}; Multi-pass membrane protein {ECO:0000269|PubMed:36113465}. Cell membrane {ECO:0000269|PubMed:18337546, ECO:0000269|PubMed:27148969}; Multi-pass membrane protein {ECO:0000269|PubMed:36113465}.
|
CATALYTIC ACTIVITY: Reaction=H(+)(out) + L-cystine(out) = H(+)(in) + L-cystine(in); Xref=Rhea:RHEA:66172, ChEBI:CHEBI:15378, ChEBI:CHEBI:35491; Evidence={ECO:0000269|PubMed:11689434, ECO:0000269|PubMed:22232659, ECO:0000269|PubMed:36113465}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66173; Evidence={ECO:0000269|PubMed:11689434, ECO:0000269|PubMed:22232659, ECO:0000269|PubMed:36113465}; CATALYTIC ACTIVITY: [Isoform 1]: Reaction=H(+)(out) + L-cystine(out) = H(+)(in) + L-cystine(in); Xref=Rhea:RHEA:66172, ChEBI:CHEBI:15378, ChEBI:CHEBI:35491; Evidence={ECO:0000269|PubMed:18337546}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66173; Evidence={ECO:0000269|PubMed:18337546}; CATALYTIC ACTIVITY: [Isoform 2]: Reaction=H(+)(out) + L-cystine(out) = H(+)(in) + L-cystine(in); Xref=Rhea:RHEA:66172, ChEBI:CHEBI:15378, ChEBI:CHEBI:35491; Evidence={ECO:0000269|PubMed:18337546}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66173; Evidence={ECO:0000269|PubMed:18337546};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=75 uM for cystine (at pH 5.0) {ECO:0000269|PubMed:22232659}; KM=278 uM for cystine {ECO:0000269|PubMed:11689434};
| null | null | null |
FUNCTION: Cystine/H(+) symporter that mediates export of cystine, the oxidized dimer of cysteine, from lysosomes (PubMed:11689434, PubMed:15128704, PubMed:18337546, PubMed:22232659, PubMed:29467429, PubMed:33208952, PubMed:36113465). Plays an important role in melanin synthesis by catalyzing cystine export from melanosomes, possibly by inhibiting pheomelanin synthesis (PubMed:22649030). In addition to cystine export, also acts as a positive regulator of mTORC1 signaling in kidney proximal tubular cells, via interactions with components of the v-ATPase and Ragulator complexes (PubMed:36113465). Also involved in small GTPase-regulated vesicle trafficking and lysosomal localization of LAMP2A, independently of cystine transporter activity (By similarity). {ECO:0000250|UniProtKB:P57757, ECO:0000269|PubMed:11689434, ECO:0000269|PubMed:15128704, ECO:0000269|PubMed:18337546, ECO:0000269|PubMed:22232659, ECO:0000269|PubMed:22649030, ECO:0000269|PubMed:29467429, ECO:0000269|PubMed:33208952, ECO:0000269|PubMed:36113465}.
|
Homo sapiens (Human)
|
O60934
|
NBN_HUMAN
|
MWKLLPAAGPAGGEPYRLLTGVEYVVGRKNCAILIENDQSISRNHAVLTANFSVTNLSQTDEIPVLTLKDNSKYGTFVNEEKMQNGFSRTLKSGDGITFGVFGSKFRIEYEPLVACSSCLDVSGKTALNQAILQLGGFTVNNWTEECTHLVMVSVKVTIKTICALICGRPIVKPEYFTEFLKAVESKKQPPQIESFYPPLDEPSIGSKNVDLSGRQERKQIFKGKTFIFLNAKQHKKLSSAVVFGGGEARLITEENEEEHNFFLAPGTCVVDTGITNSQTLIPDCQKKWIQSIMDMLQRQGLRPIPEAEIGLAVIFMTTKNYCDPQGHPSTGLKTTTPGPSLSQGVSVDEKLMPSAPVNTTTYVADTESEQADTWDLSERPKEIKVSKMEQKFRMLSQDAPTVKESCKTSSNNNSMVSNTLAKMRIPNYQLSPTKLPSINKSKDRASQQQQTNSIRNYFQPSTKKRERDEENQEMSSCKSARIETSCSLLEQTQPATPSLWKNKEQHLSENEPVDTNSDNNLFTDTDLKSIVKNSASKSHAAEKLRSNKKREMDDVAIEDEVLEQLFKDTKPELEIDVKVQKQEEDVNVRKRPRMDIETNDTFSDEAVPESSKISQENEIGKKRELKEDSLWSAKEISNNDKLQDDSEMLPKKLLLTEFRSLVIKNSTSRNPSGINDDYGQLKNFKKFKKVTYPGAGKLPHIIGGSDLIAHHARKNTELEEWLRQEMEVQNQHAKEESLADDLFRYNPYLKRRR
| null | null |
blastocyst growth [GO:0001832]; DNA damage checkpoint signaling [GO:0000077]; DNA damage response, signal transduction by p53 class mediator [GO:0030330]; DNA double-strand break processing [GO:0000729]; DNA duplex unwinding [GO:0032508]; DNA strand resection involved in replication fork processing [GO:0110025]; double-strand break repair [GO:0006302]; double-strand break repair via alternative nonhomologous end joining [GO:0097681]; double-strand break repair via homologous recombination [GO:0000724]; homologous recombination [GO:0035825]; intrinsic apoptotic signaling pathway [GO:0097193]; isotype switching [GO:0045190]; meiotic cell cycle [GO:0051321]; mitotic G2 DNA damage checkpoint signaling [GO:0007095]; mitotic G2/M transition checkpoint [GO:0044818]; negative regulation of telomere capping [GO:1904354]; neuroblast proliferation [GO:0007405]; neuromuscular process controlling balance [GO:0050885]; positive regulation of double-strand break repair via homologous recombination [GO:1905168]; positive regulation of kinase activity [GO:0033674]; positive regulation of protein autophosphorylation [GO:0031954]; positive regulation of telomere maintenance [GO:0032206]; protection from non-homologous end joining at telomere [GO:0031848]; protein K63-linked ubiquitination [GO:0070534]; protein localization to site of double-strand break [GO:1990166]; R-loop processing [GO:0062176]; regulation of cell cycle [GO:0051726]; regulation of DNA-templated DNA replication initiation [GO:0030174]; t-circle formation [GO:0090656]; telomere maintenance [GO:0000723]; telomere maintenance in response to DNA damage [GO:0043247]; telomere maintenance via telomere trimming [GO:0090737]; telomeric 3' overhang formation [GO:0031860]
|
BRCA1-C complex [GO:0070533]; chromosomal region [GO:0098687]; chromosome, telomeric region [GO:0000781]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; Mre11 complex [GO:0030870]; nuclear inclusion body [GO:0042405]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PML body [GO:0016605]; replication fork [GO:0005657]; site of double-strand break [GO:0035861]
|
chromatin-protein adaptor activity [GO:0140463]; damaged DNA binding [GO:0003684]; DNA-binding transcription factor binding [GO:0140297]; histone binding [GO:0042393]; phosphorylation-dependent protein binding [GO:0140031]; protein serine/threonine kinase activator activity [GO:0043539]
|
PF00533;PF00498;PF08599;PF16508;
|
2.60.200.20;3.40.50.10190;3.40.50.10980;
|
Nibrin family
|
PTM: Phosphorylated by ATM in response of ionizing radiation, and such phosphorylation is responsible intra-S phase checkpoint control and telomere maintenance (PubMed:10766245, PubMed:10802669, PubMed:10839544, PubMed:10839545). Phosphorylated at Ser-432 by CDK2 in S/G2 phases abolishes interaction with TERF2, enabling DCLRE1B/Apollo recruitment to telomeres (PubMed:28216226). Phosphorylation at Ser-432 in response to dysfunctional telomeres promotes non-homologous end joining repair at telomeres, while dephosphorylation by PPP1CA promotes microhomology-mediated end-joining (MMEJ) repair (PubMed:28216226). {ECO:0000269|PubMed:10766245, ECO:0000269|PubMed:10802669, ECO:0000269|PubMed:10839544, ECO:0000269|PubMed:10839545, ECO:0000269|PubMed:28216226}.; PTM: Ubiquitinated at Lys-435 via 'Lys-6'-linked ubiquitin chains by RNF8, promoting NBN recruitment to DNA double-strand breaks (DSBs) (PubMed:23115235). Ubiquitinated at Lys-686 and Lys-689 via 'Lys-63'-linked ubiquitin chains by PELI1: ubiquitination takes place following PELI1 phosphorylation and promotes ATM activation and DNA repair (PubMed:30952868). Ubiquitinated at Lys-735 via 'Lys-63'-linked ubiquitin chains by the SCF(SKP2) complex: ubiquitination takes place following SKP2 phosphorylation and promotes ATM activation and DNA repair (PubMed:22464731). {ECO:0000269|PubMed:22464731, ECO:0000269|PubMed:23115235, ECO:0000269|PubMed:30952868}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10783165, ECO:0000269|PubMed:26215093}. Chromosome {ECO:0000269|PubMed:12419185, ECO:0000269|PubMed:18411307, ECO:0000269|PubMed:18582474, ECO:0000269|PubMed:18583988, ECO:0000269|PubMed:18678890, ECO:0000269|PubMed:19338747, ECO:0000269|PubMed:23115235, ECO:0000269|PubMed:24534091, ECO:0000269|PubMed:26215093, ECO:0000269|PubMed:26438602}. Nucleus, PML body {ECO:0000269|PubMed:12470659, ECO:0000269|PubMed:15916964}. Chromosome, telomere {ECO:0000269|PubMed:10888888, ECO:0000269|PubMed:28216226}. Note=Localizes to discrete nuclear foci after treatment with genotoxic agents (PubMed:10783165, PubMed:26215093, PubMed:26438602). Localizes to DNA double-strand breaks (DSBs); recruited to DNA damage sites via association with phosphorylated proteins, such as phosphorylated H2AX, phosphorylated MDC1 and phosphorylated RAD17 (PubMed:12419185, PubMed:18411307, PubMed:18582474, PubMed:18583988, PubMed:18678890, PubMed:19338747, PubMed:23115235, PubMed:24534091, PubMed:26438602). Acetylation of 'Lys-5' of histone H2AX (H2AXK5ac) promotes NBN/NBS1 assembly at the sites of DNA damage (PubMed:26438602). {ECO:0000269|PubMed:10783165, ECO:0000269|PubMed:12419185, ECO:0000269|PubMed:18411307, ECO:0000269|PubMed:18582474, ECO:0000269|PubMed:18583988, ECO:0000269|PubMed:18678890, ECO:0000269|PubMed:23115235, ECO:0000269|PubMed:24534091, ECO:0000269|PubMed:26215093, ECO:0000269|PubMed:26438602}.
| null | null | null | null | null |
FUNCTION: Component of the MRN complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis (PubMed:10888888, PubMed:15616588, PubMed:18411307, PubMed:18583988, PubMed:18678890, PubMed:19759395, PubMed:23115235, PubMed:28216226, PubMed:28867292, PubMed:9705271). The MRN complex is involved in the repair of DNA double-strand breaks (DSBs) via homologous recombination (HR), an error-free mechanism which primarily occurs during S and G2 phases (PubMed:19759395, PubMed:28867292, PubMed:9705271). The complex (1) mediates the end resection of damaged DNA, which generates proper single-stranded DNA, a key initial steps in HR, and is (2) required for the recruitment of other repair factors and efficient activation of ATM and ATR upon DNA damage (PubMed:19759395, PubMed:9705271). The MRN complex possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity, which are provided by MRE11, to initiate end resection, which is required for single-strand invasion and recombination (PubMed:19759395, PubMed:28867292, PubMed:9705271). Within the MRN complex, NBN acts as a protein-protein adapter, which specifically recognizes and binds phosphorylated proteins, promoting their recruitment to DNA damage sites (PubMed:12419185, PubMed:15616588, PubMed:18411307, PubMed:18582474, PubMed:18583988, PubMed:18678890, PubMed:19759395, PubMed:19804756, PubMed:23762398, PubMed:24534091, PubMed:27814491, PubMed:27889449, PubMed:33836577). Recruits MRE11 and RAD50 components of the MRN complex to DSBs in response to DNA damage (PubMed:12419185, PubMed:18411307, PubMed:18583988, PubMed:18678890, PubMed:24534091, PubMed:26438602). Promotes the recruitment of PI3/PI4-kinase family members ATM, ATR, and probably DNA-PKcs to the DNA damage sites, activating their functions (PubMed:15064416, PubMed:15616588, PubMed:15790808, PubMed:16622404, PubMed:22464731, PubMed:30952868, PubMed:35076389). Mediates the recruitment of phosphorylated RBBP8/CtIP to DSBs, leading to cooperation between the MRN complex and RBBP8/CtIP to initiate end resection (PubMed:19759395, PubMed:27814491, PubMed:27889449, PubMed:33836577). RBBP8/CtIP specifically promotes the endonuclease activity of the MRN complex to clear DNA ends containing protein adducts (PubMed:27814491, PubMed:27889449, PubMed:30787182, PubMed:33836577). The MRN complex is also required for the processing of R-loops (PubMed:31537797). NBN also functions in telomere length maintenance via its interaction with TERF2: interaction with TERF2 during G1 phase preventing recruitment of DCLRE1B/Apollo to telomeres (PubMed:10888888, PubMed:28216226). NBN also promotes DNA repair choice at dysfunctional telomeres: NBN phosphorylation by CK2 promotes non-homologous end joining repair at telomeres, while unphosphorylated NBN promotes microhomology-mediated end-joining (MMEJ) repair (PubMed:28216226). Enhances AKT1 phosphorylation possibly by association with the mTORC2 complex (PubMed:23762398). {ECO:0000269|PubMed:10888888, ECO:0000269|PubMed:12419185, ECO:0000269|PubMed:15064416, ECO:0000269|PubMed:15616588, ECO:0000269|PubMed:15790808, ECO:0000269|PubMed:16622404, ECO:0000269|PubMed:18411307, ECO:0000269|PubMed:18582474, ECO:0000269|PubMed:18583988, ECO:0000269|PubMed:18678890, ECO:0000269|PubMed:19759395, ECO:0000269|PubMed:19804756, ECO:0000269|PubMed:22464731, ECO:0000269|PubMed:23115235, ECO:0000269|PubMed:23762398, ECO:0000269|PubMed:24534091, ECO:0000269|PubMed:26438602, ECO:0000269|PubMed:27814491, ECO:0000269|PubMed:27889449, ECO:0000269|PubMed:28216226, ECO:0000269|PubMed:28867292, ECO:0000269|PubMed:30787182, ECO:0000269|PubMed:30952868, ECO:0000269|PubMed:31537797, ECO:0000269|PubMed:33836577, ECO:0000269|PubMed:35076389, ECO:0000269|PubMed:9705271}.
|
Homo sapiens (Human)
|
O60936
|
NOL3_HUMAN
|
MGNAQERPSETIDRERKRLVETLQADSGLLLDALLARGVLTGPEYEALDALPDAERRVRRLLLLVQGKGEAACQELLRCAQRTAGAPDPAWDWQHVGPGYRDRSYDPPCPGHWTPEAPGSGTTCPGLPRASDPDEAGGPEGSEAVQSGTPEEPEPELEAEASKEAEPEPEPEPELEPEAEAEPEPELEPEPDPEPEPDFEERDESEDS
| null | null |
blood vessel remodeling [GO:0001974]; cardiac muscle cell apoptotic process [GO:0010659]; inhibition of cysteine-type endopeptidase activity involved in apoptotic process [GO:1990001]; intrinsic apoptotic signaling pathway [GO:0097193]; mRNA splice site recognition [GO:0006376]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cardiac muscle cell apoptotic process [GO:0010667]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; negative regulation of hypoxia-induced intrinsic apoptotic signaling pathway [GO:1903298]; negative regulation of intrinsic apoptotic signaling pathway [GO:2001243]; negative regulation of mitochondrial membrane permeability involved in apoptotic process [GO:1902109]; negative regulation of muscle atrophy [GO:0014736]; negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway [GO:1902176]; negative regulation of programmed necrotic cell death [GO:0062099]; negative regulation of release of cytochrome c from mitochondria [GO:0090201]; negative regulation of tumor necrosis factor-mediated signaling pathway [GO:0010804]; protein complex oligomerization [GO:0051259]; regulation of non-canonical NF-kappaB signal transduction [GO:1901222]; release of sequestered calcium ion into cytosol by sarcoplasmic reticulum [GO:0014808]; response to hypoxia [GO:0001666]; response to injury involved in regulation of muscle adaptation [GO:0014876]; response to ischemia [GO:0002931]; RNA splicing [GO:0008380]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]; sarcoplasmic reticulum [GO:0016529]
|
calcium ion binding [GO:0005509]; caspase binding [GO:0089720]; cysteine-type endopeptidase inhibitor activity involved in apoptotic process [GO:0043027]; death effector domain binding [GO:0035877]; death receptor binding [GO:0005123]; identical protein binding [GO:0042802]; RNA binding [GO:0003723]
|
PF00619;
|
1.10.533.10;
| null |
PTM: Phosphorylation at Thr-149 is required for its antiapoptotic effect by blocking death-inducing signaling complex death-inducing signaling complex (DISC) activity through the control of interaction with CASP8. Phosphorylation at Thr-149 results in translocation to mitochondria and this translocation enables the binding to CASP8. Dephosphorylated at Thr-149 by calcineurin; doesn't inhibit the association between FADD and CASP8 and the consequent apoptosis. {ECO:0000250|UniProtKB:Q62881}.; PTM: Polyubiquitinated by MDM2; promoting proteasomal-dependent degradation in response to apoptotic stimuli. {ECO:0000250|UniProtKB:Q62881, ECO:0000269|PubMed:17142452}.
|
SUBCELLULAR LOCATION: [Isoform 1]: Nucleus, nucleolus {ECO:0000269|PubMed:10196175}. Note=The SR-rich C-terminus mediates nuclear localization. {ECO:0000269|PubMed:10196175}.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:10196175}. Mitochondrion {ECO:0000250|UniProtKB:Q62881}. Sarcoplasmic reticulum {ECO:0000250|UniProtKB:Q62881}. Membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Note=Phosphorylation at Thr-149 results in translocation to mitochondria. Colocalized with mitochondria in response to oxidative stress. {ECO:0000250|UniProtKB:Q62881}.
| null | null | null | null | null |
FUNCTION: [Isoform 1]: May be involved in RNA splicing. {ECO:0000269|PubMed:10196175}.; FUNCTION: [Isoform 2]: Functions as an apoptosis repressor that blocks multiple modes of cell death. Inhibits extrinsic apoptotic pathways through two different ways. Firstly by interacting with FAS and FADD upon FAS activation blocking death-inducing signaling complex (DISC) assembly (By similarity). Secondly by interacting with CASP8 in a mitochondria localization- and phosphorylation-dependent manner, limiting the amount of soluble CASP8 available for DISC-mediated activation (By similarity). Inhibits intrinsic apoptotic pathway in response to a wide range of stresses, through its interaction with BAX resulting in BAX inactivation, preventing mitochondrial dysfunction and release of pro-apoptotic factors (PubMed:15004034). Inhibits calcium-mediated cell death by functioning as a cytosolic calcium buffer, dissociating its interaction with CASP8 and maintaining calcium homeostasis (PubMed:15509781). Negatively regulates oxidative stress-induced apoptosis by phosphorylation-dependent suppression of the mitochondria-mediated intrinsic pathway, by blocking CASP2 activation and BAX translocation (By similarity). Negatively regulates hypoxia-induced apoptosis in part by inhibiting the release of cytochrome c from mitochondria in a caspase-independent manner (By similarity). Also inhibits TNF-induced necrosis by preventing TNF-signaling pathway through TNFRSF1A interaction abrogating the recruitment of RIPK1 to complex I (By similarity). Finally through its role as apoptosis repressor, promotes vascular remodeling through inhibition of apoptosis and stimulation of proliferation, in response to hypoxia (By similarity). Inhibits too myoblast differentiation through caspase inhibition (By similarity). {ECO:0000250|UniProtKB:Q62881, ECO:0000250|UniProtKB:Q9D1X0, ECO:0000269|PubMed:15004034, ECO:0000269|PubMed:15509781}.
|
Homo sapiens (Human)
|
O60938
|
KERA_HUMAN
|
MAGTICFIMWVLFITDTVWSRSVRQVYEVHDSDDWTIHDFECPMECFCPPSFPTALYCENRGLKEIPAIPSRIWYLYLQNNLIETIPEKPFENATQLRWINLNKNKITNYGIEKGALSQLKKLLFLFLEDNELEEVPSPLPRSLEQLQLARNKVSRIPQGTFSNLENLTLLDLQNNKLVDNAFQRDTFKGLKNLMQLNMAKNALRNMPPRLPANTMQLFLDNNSIEGIPENYFNVIPKVAFLRLNHNKLSDEGLPSRGFDVSSILDLQLSHNQLTKVPRISAHLQHLHLDHNKIKSVNVSVICPSPSMLPAERDSFSYGPHLRYLRLDGNEIKPPIPMALMTCFRLLQAVII
| null | null |
cornea development in camera-type eye [GO:0061303]; response to stimulus [GO:0050896]; visual perception [GO:0007601]
|
extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi lumen [GO:0005796]; lysosomal lumen [GO:0043202]
| null |
PF13516;PF13855;PF01462;
|
3.80.10.10;
|
Small leucine-rich proteoglycan (SLRP) family, SLRP class II subfamily
|
PTM: Binds keratan sulfate chains. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: May be important in developing and maintaining corneal transparency and for the structure of the stromal matrix. {ECO:0000305|PubMed:10802664, ECO:0000305|PubMed:11726611}.
|
Homo sapiens (Human)
|
O60939
|
SCN2B_HUMAN
|
MHRDAWLPRPAFSLTGLSLFFSLVPPGRSMEVTVPATLNVLNGSDARLPCTFNSCYTVNHKQFSLNWTYQECNNCSEEMFLQFRMKIINLKLERFQDRVEFSGNPSKYDVSVMLRNVQPEDEGIYNCYIMNPPDRHRGHGKIHLQVLMEEPPERDSTVAVIVGASVGGFLAVVILVLMVVKCVRRKKEQKLSTDDLKTEEEGKTDGEGNPDDGAK
| null | null |
cardiac muscle cell action potential involved in contraction [GO:0086002]; cardiac muscle contraction [GO:0060048]; chemical synaptic transmission [GO:0007268]; gene expression [GO:0010467]; membrane depolarization during cardiac muscle cell action potential [GO:0086012]; nervous system development [GO:0007399]; regulation of atrial cardiac muscle cell membrane depolarization [GO:0060371]; regulation of heart rate by cardiac conduction [GO:0086091]; regulation of sodium ion transmembrane transporter activity [GO:2000649]; response to heat [GO:0009408]; response to pyrethroid [GO:0046684]; sodium ion transmembrane transport [GO:0035725]
|
plasma membrane [GO:0005886]; synapse [GO:0045202]; T-tubule [GO:0030315]; voltage-gated sodium channel complex [GO:0001518]
|
sodium channel regulator activity [GO:0017080]; voltage-gated potassium channel activity involved in ventricular cardiac muscle cell action potential repolarization [GO:1902282]; voltage-gated sodium channel activity involved in cardiac muscle cell action potential [GO:0086006]
|
PF07686;
|
2.60.40.10;
|
Sodium channel auxiliary subunit SCN2B (TC 8.A.17) family
| null |
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
| null | null | null | null | null |
FUNCTION: Crucial in the assembly, expression, and functional modulation of the heterotrimeric complex of the sodium channel. The subunit beta-2 causes an increase in the plasma membrane surface area and in its folding into microvilli. Interacts with TNR may play a crucial role in clustering and regulation of activity of sodium channels at nodes of Ranvier (By similarity). {ECO:0000250}.
|
Homo sapiens (Human)
|
O60941
|
DTNB_HUMAN
|
MIEESGNKRKTMAEKRQLFIEMRAQNFDVIRLSTYRTACKLRFVQKRCNLHLVDIWNMIEAFRDNGLNTLDHTTEISVSRLETVISSIYYQLNKRLPSTHQISVEQSISLLLNFMIAAYDSEGRGKLTVFSVKAMLATMCGGKMLDKLRYVFSQMSDSNGLMIFSKFDQFLKEVLKLPTAVFEGPSFGYTEHSVRTCFPQQRKIMLNMFLDTMMADPPPQCLVWLPLMHRLAHVENVFHPVECSYCRCESMMGFRYRCQQCHNYQLCQNCFWRGHAGGPHSNQHQMKEHSSWKSPAKKLSHAISKSLGCVPTREPPHPVFPEQPEKPLDLAHIVPPRPLTNMNDTMVSHMSSGVPTPTKRLQYSQDIPSHLADEHALIASYVARLQHCARVLDSPSRLDEEHRLIARYAARLAAEAGNVTRPPTDLSFNFDANKQQRQLIAELENKNREILQEIQRLRLEHEQASQPTPEKAQQNPTLLAELRLLRQRKDELEQRMSALQESRRELMVQLEELMKLLKEEEQKQAAQATGSPHTSPTHGGGRPMPMPVRSTSAGSTPTHCPQDSLSGVGGDVQEAFAQGTRRNLRNDLLVAADSITNTMSSLVKELHSAEEGAEEEEEKMQNGKDRG
| null | null |
neuron differentiation [GO:0030182]; 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]
|
zinc ion binding [GO:0008270]
|
PF09068;PF09069;PF00569;
|
3.30.60.90;1.10.238.10;
|
Dystrophin family, Dystrobrevin subfamily
|
PTM: Phosphorylated by PKA. Phosphorylation at Thr-11 alters the interaction with KIF5A. {ECO:0000250|UniProtKB:O70585}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27223470}. Postsynaptic density {ECO:0000250|UniProtKB:P84060}. Cell projection, dendrite {ECO:0000250|UniProtKB:O70585}. Basal cell membrane {ECO:0000250|UniProtKB:O70585}. Postsynapse {ECO:0000250|UniProtKB:O70585}. Nucleus {ECO:0000269|PubMed:27223470}. Note=Localized at inhibitory synapses on the dendrites of cerebellar Purkinje cells. {ECO:0000250|UniProtKB:O70585}.
| null | null | null | null | null |
FUNCTION: Scaffolding protein that assembles DMD and SNTA1 molecules to the basal membrane of kidney cells and liver sinusoids (By similarity). 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:27223470). May be required for proper maturation and function of a subset of inhibitory synapses (By similarity). {ECO:0000250|UniProtKB:O70585, ECO:0000269|PubMed:27223470}.
|
Homo sapiens (Human)
|
O60942
|
MCE1_HUMAN
|
MAHNKIPPRWLNCPRRGQPVAGRFLPLKTMLGPRYDSQVAEENRFHPSMLSNYLKSLKVKMGLLVDLTNTSRFYDRNDIEKEGIKYIKLQCKGHGECPTTENTETFIRLCERFNERNPPELIGVHCTHGFNRTGFLICAFLVEKMDWSIEAAVATFAQARPPGIYKGDYLKELFRRYGDIEEAPPPPLLPDWCFEDDEDEDEDEDGKKESEPGSSASFGKRRKERLKLGAIFLEGVTVKGVTQVTTQPKLGEVQQKCHQFCGWEGSGFPGAQPVSMDKQNIKLLDLKPYKVSWKADGTRYMMLIDGTNEVFMIDRDNSVFHVSNLEFPFRKDLRMHLSNTLLDGEMIIDRVNGQAVPRYLIYDIIKFNSQPVGDCDFNVRLQCIEREIISPRHEKMKTGLIDKTQEPFSVRNKPFFDICTSRKLLEGNFAKEVSHEMDGLIFQPTGKYKPGRCDDILKWKPPSLNSVDFRLKITRMGGEGLLPQNVGLLYVGGYERPFAQIKVTKELKQYDNKIIECKFENNSWVFMRQRTDKSFPNAYNTAMAVCNSISNPVTKEMLFEFIDRCTAASQGQKRKHHLDPDTELMPPPPPKRPRPLT
|
2.7.7.50; 3.6.1.74
| null |
7-methylguanosine mRNA capping [GO:0006370]; dephosphorylation [GO:0016311]; RNA processing [GO:0006396]
|
nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; GTP binding [GO:0005525]; inorganic triphosphate phosphatase activity [GO:0050355]; mRNA 5'-phosphatase activity [GO:0140818]; mRNA guanylyltransferase activity [GO:0004484]; polynucleotide 5'-phosphatase activity [GO:0004651]; protein tyrosine/serine/threonine phosphatase activity [GO:0008138]; RNA guanylyltransferase activity [GO:0008192]
|
PF00782;PF03919;PF01331;
|
3.30.1490.430;3.30.470.30;2.40.50.140;3.90.190.10;
|
Non-receptor class of the protein-tyrosine phosphatase family; Eukaryotic GTase family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=a 5'-end triphospho-ribonucleoside in mRNA + H2O = a 5'-end diphospho-ribonucleoside in mRNA + H(+) + phosphate; Xref=Rhea:RHEA:67004, Rhea:RHEA-COMP:17164, Rhea:RHEA-COMP:17165, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:167616, ChEBI:CHEBI:167618; EC=3.6.1.74; Evidence={ECO:0000269|PubMed:9473487}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67005; Evidence={ECO:0000305|PubMed:9473487}; CATALYTIC ACTIVITY: Reaction=a 5'-end diphospho-ribonucleoside in mRNA + GTP + H(+) = a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + diphosphate; Xref=Rhea:RHEA:67012, Rhea:RHEA-COMP:17165, Rhea:RHEA-COMP:17166, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:167616, ChEBI:CHEBI:167617; EC=2.7.7.50; Evidence={ECO:0000269|PubMed:9473487}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67013; Evidence={ECO:0000305|PubMed:9473487};
| null | null | null | null |
FUNCTION: Bifunctional mRNA-capping enzyme exhibiting RNA 5'-triphosphate monophosphatase activity in the N-terminal part and mRNA guanylyltransferase activity in the C-terminal part. Catalyzes the first two steps of cap formation: by removing the gamma-phosphate from the 5'-triphosphate end of nascent mRNA to yield a diphosphate end, and by transferring the GMP moiety of GTP to the 5'-diphosphate terminus of RNA via a covalent enzyme-GMP reaction intermediate. {ECO:0000269|PubMed:21636784, ECO:0000269|PubMed:9473487, ECO:0000269|PubMed:9512541}.
|
Homo sapiens (Human)
|
O60952
|
LIME_DICDI
|
MSASVKCGACAKTAYPLESVVANNNSYHKGCFKCSTCNSTLNVKTFKSFEGKLYCPVHTPKVSATAVTDSVALKNALNAPKKVAEGLGNAHRGLDEKPNIGLDSMATANALNAPKKVVEGLGNVQKGIGGKPTYAVFGADGQPTGEQQEQQQYTEEQYEQPQEEQQYQEEQQQYQEEEQQYQEEEQQYQEEEQQYEEEQ
| null | null |
actin filament bundle assembly [GO:0051017]; cell cycle [GO:0007049]
|
actin cytoskeleton [GO:0015629]; cortical actin cytoskeleton [GO:0030864]; extracellular matrix [GO:0031012]; filopodium [GO:0030175]; lamellipodium [GO:0030027]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; pseudopodium [GO:0031143]
|
actin filament binding [GO:0051015]; metal ion binding [GO:0046872]
|
PF00412;
|
2.10.110.10;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cell cortex. Nucleus. Cell projection, lamellipodium. Cell projection, filopodium. Cytoplasm, cytoskeleton. Note=Weakly expressed in cytoplasm. Found in actin-rich protrusions, and lamellipodia and filopodia during motility.
| null | null | null | null | null |
FUNCTION: Associates with the actin cytoskeleton and may regulate actin polymerization in lamellipodia, through a rac1-dependent signaling pathway. May play a role in cell motility. Involved in cytokinesis by regulating the microtubule system and linking it to the cortical actin network. {ECO:0000269|PubMed:14506710}.
|
Dictyostelium discoideum (Social amoeba)
|
O60999
|
CUL1_DICDI
|
MSMMTSTPTKRSVKLDDIWPELEEGIYKIITDLNKGFPKQKWIALYTHVYDYCAASQSKSSAKVGMPKQQASGANYVGEDLYNRLNLFLKKHMSQLLKLTETKMDEPLLNYYYTEWDRYTSAMKYINNIFQYMNRYWIKREIDDGKKEVYEIFILSLVIWRDCLFTPLKQRLTNSLLDIIESERNGYQINTHLIKGVINGYVSLGLNREKPKETILQVYKSGFEELFLTATENYYTNESAKFISENSVADYMKKVETRLNEEVKRVQQYLHQNTESELIAKCEKVLIEKHVEVIWNEFQTLLEKDKIPDLTRMYSLLSRIPRGLEPLRTTLEKHVQNVGLQAVSSIATNGVIEPKVYIETLLKVFKKYNELVTGAFRSDTGFVASLDKACRRFINENAVTIAAKSSSKSPELLARFTDFLLKKSPNNPEESEMEQLLNDVMIVFKYIEDKDVFQDFYSKMLAKRLIHGTSTSEDLEGTMIGKLKSTCGYEYTSKLQRMFTDMSLSRELLDRFNNHIEQVERSSLNIDFSVLVLATGSWPLQPPSTNFSIPKELQACEQLFQKFYQNQHSGRKLNWLHHLSKGELKTKYLQTSKSGYTLQCSTYQIGVLLQFNQYETLTSEEIQESTQLIDSVLKGTLTSLAKSKILLADPPLDDEEIAKTTKFSLNKQFKNKKTKIFINVPVLTQVKEEIDSIHKTVEEDRKLQIQAAIVRIMKMRKQLAHSGLMTEVISQLQTRFNPKVNIIKKCIDILIEKEYLMRVEGKKDHYSYVA
| null | null |
cell differentiation [GO:0030154]; chemotaxis [GO:0006935]; G1/S transition of mitotic cell cycle [GO:0000082]; protein ubiquitination [GO:0016567]; sorocarp development [GO:0030587]; ubiquitin-dependent protein catabolic process [GO:0006511]
|
cullin-RING ubiquitin ligase complex [GO:0031461]; SCF ubiquitin ligase complex [GO:0019005]
|
ubiquitin protein ligase binding [GO:0031625]; ubiquitin-protein transferase activity [GO:0004842]
|
PF00888;PF10557;
|
1.20.1310.10;1.10.10.10;
|
Cullin family
|
PTM: Neddylated; which enhances the ubiquitination activity of SCF. {ECO:0000250|UniProtKB:Q13616}.
| null | null | null |
PATHWAY: Protein modification; protein ubiquitination.
| null | null |
FUNCTION: Probable core component of cullin-based SCF-like E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit (By similarity). Required at several stages during development. CulA and fbxA regulate multicellular development by targeting regA for degradation via a pathway that requires erkB function, leading to an increase in cAMP and PKA activity. {ECO:0000250, ECO:0000269|PubMed:11390363}.
|
Dictyostelium discoideum (Social amoeba)
|
O61122
|
SVKA_DICDI
|
MASKKGDPEELYVRQEKIGKGSFGEVFKGINKKTNETIAIKTIDLEDAEDEIEDIQQEINVLSQCESPFVTKYFGSFLKGSKLWIIMEYLAGGSVLDLMKPGPFDEGYIAIILRELLKGLEYLHSEGKIHRDIKAANVLLSASGDVKLADFGVSGQLTDQMTKRNTFVGTPFWMAPEVIKQTGYDSKADIWSMGITALEMAKGEPPRADLHPMRALFLIPKDPPPTLEGNFSKGFKEFCALCLNKDPNQRPTAKDLLKHKFIKAAKKTSSLTDLIERRQKWLQLNGNNADDENDDLDRDAKSNEEDFGWEFPTIKQKSPVAVQEQQQTPQKPTVVSTPIKEQQQQQQPTPVTTPQQPVTTTTTTPTTETKVRSLSNSSQTTPVKTTVAATTAPATTPASNAPTSTTPNGAAVTQQQAPRASALTSVIYPVLSKLLKNTSDENVINALAQLKMAFDNAEKAKPGITHSLIAQIIETLKR
|
2.7.11.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:9582328}; COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:9582328};
|
cell cycle [GO:0007049]; cell division [GO:0051301]; hippo signaling [GO:0035329]; hyperosmotic response [GO:0006972]; positive regulation of cell division [GO:0051781]; positive regulation of mitotic cytokinetic process [GO:1903438]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of sorocarp development [GO:0031156]
|
actin cytoskeleton [GO:0015629]; centrosome [GO:0005813]; cleavage furrow [GO:0032154]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitotic spindle [GO:0072686]; nucleus [GO:0005634]
|
actin binding [GO:0003779]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF20929;PF00069;
|
1.10.12.70;1.10.510.10;
|
Protein kinase superfamily, STE Ser/Thr protein kinase family, STE20 subfamily
|
PTM: Autophosphorylated.
|
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:18042625}. Nucleus {ECO:0000269|PubMed:18042625}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:18042625}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:18042625}. Cleavage furrow {ECO:0000269|PubMed:18042625}. Note=Shows overall localization in the cytosol and, to a lesser extent, in the nucleus. Enriched around the centrosome. In dividing cells, forms a cloud around the spindle and nuclei. Enriched in the cleavage furrow during late cytokinesis.
|
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 |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:9582328};
| null |
FUNCTION: Involved in regulation of actin cytoskeleton organization during cell motility; F-actin fragmenting and capping protein allowing dynamic rearrangements of the actin cytoskeleton. Also part of a regulatory pathway from the centrosome to the midzone, thus regulating the completion of cell division. {ECO:0000269|PubMed:18042625, ECO:0000269|PubMed:9582328}.
|
Dictyostelium discoideum (Social amoeba)
|
O61125
|
STK4_DICDI
|
MSTLNVPKETMSRKDPEKFFTIVEKLGEGSYGSVYKAINISTGIVVAIKKVSVDNDLEDMEKEISFMKQCKSPYIVTYYASFRKENEVWIVMEHCGAGSVCDAMKITDKTLSEDQIAVVSRDVLQGLAYLHSVRKIHRDIKAGNILMNHKGESKLADFGVSGQLSDTMAKRQTVIGTPFWMAPEVIQEIGYDYKADIWSYGITCIEMAESKPPLFNVHPMRVIFMIPNPSRPPPKLTEPEKWSPEFNDFLAKCLTRKPELRPSAEELLKHPFITKAKSHSLLVPLIDEQDIIINEKGREVALGIEQRDEEEEDEDEDSEDSDDNRGTMVRAKPRSMQNSGGEDNDEEYDTGTMVITDNKNSYDTVVFNNDDEDSGTMKLKNTMPSNKKNFVPDYMNQFKKSDDDVTNVPLSDKYSSYSLEELKKMLAELEIEREKEVQKTLEKFSINRQALLAVIDEKKSK
|
2.7.11.1
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:16842885};
|
aggregation involved in sorocarp development [GO:0031152]; hyperosmotic response [GO:0006972]; intracellular signal transduction [GO:0035556]; protein autophosphorylation [GO:0046777]; protein tetramerization [GO:0051262]; regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0106070]; regulation of MAPK cascade [GO:0043408]; signal transduction [GO:0007165]
|
cell cortex [GO:0005938]; cytoplasm [GO:0005737]; cytosol [GO:0005829]
|
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00069;
|
4.10.170.10;1.10.510.10;
|
Protein kinase superfamily, STE Ser/Thr protein kinase family, STE20 subfamily
|
PTM: Undergoes autophosphorylation in the catalytic domain.
|
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:16842885}.
|
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: Regulates both cAMP signaling during early development and the stress response. Functions as an activator of adenylylcyclase. {ECO:0000269|PubMed:16842885, ECO:0000269|PubMed:17362909}.
|
Dictyostelium discoideum (Social amoeba)
|
O61142
|
SUB1_PLAFA
|
MMLNKKVVALCTLTLHLFCIFLCLGKEVRSEENGKIQDDAKKIVSELRFLEKVEDVIEKSNIGGNEVDADENSFNPDTEVPIEEIEEIKMRELKDVKEEKNKNDNHNNNNNNNNISSSSSSSSNTFGEEKEEVSKKKKKLRLIVSENHATTPSFFQESLLEPDVLSFLESKGNLSNLKNINSMIIELKEDTTDDELISYIKILEEKGALIESDKLVSADNIDISGIKDAIRRGEENIDVNDYKSMLEVENDAEDYDKMFGMFNESHAATSKRKRHSTNERGYDTFSSPSYKTYSKSDYLYDDDNNNNNYYYSHSSNGHNSSSRNSSSSRSRPGKYHFNDEFRNLQWGLDLSRLDETQELINEHQVMSTRICVIDSGIDYNHPDLKDNIELNLKELHGRKGFDDDNNGIVDDIYGANFVNNSGNPMDDNYHGTHVSGIISAIGNNNIGVVGVDVNSKLIICKALDEHKLGRLGDMFKCLDYCISRNAHMINGSFSFDEYSGIFNSSVEYLQRKGILFFVSASNCSHPKSSTPDIRKCDLSINAKYPPILSTVYDNVISVANLKKNDNNNHYSLSINSFYSNKYCQLAAPGTNIYSTAPHNSYRKLNGTSMAAPHVAAIASLIFSINPDLSYKKVIQILKDSIVYLPSLKNMVAWAGYADINKAVNLAIKSKKTYINSNISNKWKKKSRYLH
|
3.4.21.62
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:24785947}; Note=Binds 3 Ca(2+) ions per subunit. {ECO:0000269|PubMed:24785947};
|
peptide hormone processing [GO:0016486]
|
extracellular space [GO:0005615]; membrane [GO:0016020]; neuron projection [GO:0043005]; trans-Golgi network [GO:0005802]
|
metal ion binding [GO:0046872]; serine-type endopeptidase activity [GO:0004252]
|
PF00082;PF18213;
|
3.30.70.2380;3.40.50.200;
|
Peptidase S8 family
|
PTM: The propeptide (p31) is cleaved, probably by autocatalysis, during the transport to or in the Golgi apparatus, and remains non-covalently associated with the p54 form as an inhibitor (PubMed:10617661, PubMed:12764150, PubMed:9722575). p54 is further cleaved into the p45 form (PubMed:10617661, PubMed:9722575). This cleavage is likely occurring in the exoneme prior to egress and is mediated by PMX/plasmepsin X (By similarity). {ECO:0000250|UniProtKB:W7K9M0, ECO:0000269|PubMed:10617661, ECO:0000269|PubMed:12764150, ECO:0000269|PubMed:9722575}.; PTM: The disulfide bond between Cys-523 and Cys-536 acts as a redox-sensitive disulfide switch (PubMed:24785947). The oxidized form is required for catalytic activity (PubMed:24785947). {ECO:0000269|PubMed:24785947}.; PTM: The relevance of N-glycosylation is not clear. In an insect expression system, SUB1 glycosylation appears to affect its processing into the active mature form suggesting that SUB1 may not be N-glycosylated in parasites. {ECO:0000269|PubMed:10617661}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9722575}. Parasitophorous vacuole lumen {ECO:0000250|UniProtKB:Q8I0V0}. Note=At the schizont stage, in merozoites, localizes to dense secretory granules called exonemes (PubMed:9722575). Just prior to egress secreted into the parasitophorous vacuole (By similarity). {ECO:0000250|UniProtKB:Q8I0V0, ECO:0000269|PubMed:9722575}.
|
CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides.; EC=3.4.21.62; Evidence={ECO:0000269|PubMed:10617661, ECO:0000269|PubMed:12764150, ECO:0000269|PubMed:24785947};
| null | null | null | null |
FUNCTION: Serine protease which plays an essential role in merozoite invasion of and egress from host erythrocytes by processing and activating various merozoite surface and parasitophorous vacuole proteins. Mediates the proteolytic maturation of serine proteases SERA4, SERA5 and SERA6 just prior to merozoite egress. Prior to merozoite egress, cleaves merozoite surface proteins MSP1, MSP6 and MSP7, which form the MSP1/6/7 complex, and thereby may prime the parasite cell surface for invasion of fresh erythrocytes. Prior to merozoite egress, cleaves MSRP2 converting it to MSRP2 p25 form, and RAP1 converting it to RAP1 p67 form. {ECO:0000250|UniProtKB:Q8I0V0}.
|
Plasmodium falciparum
|
O61213
|
DUOX1_CAEEL
|
MRSKHVLYIAILFSSIFGGKGIQQNEEFQRYDGWYNNLANSEWGSAGSRLHRDARSYYSDGVYSVNNSLPSARELSDILFKGESGIPNTRGCTTLLAFFSQVVAYEIMQSNGVSCPLETLKIQVPLCDNVFDKECEGKTEIPFTRAKYDKATGNGLNSPREQINERTSWIDGSFIYGTTQPWVSSLRSFKQGRLAEGVPGYPPLNNPHIPLNNPAPPQVHRLMSPDRLFMLGDSRVNENPGLLSFGLILFRWHNYNANQIHREHPDWTDEQIFQAARRLVIASMQKIIAYDFVPGLLGEDVRLSNYTKYMPHVPPGISHAFGAAAFRFPHSIVPPAMLLRKRGNKCEFRTEVGGYPALRLCQNWWNAQDIVKEYSVDEIILGMASQIAERDDNIVVEDLRDYIFGPMHFSRLDVVASSIMRGRDNGVPPYNELRRTFGLAPKTWETMNEDFYKKHTAKVEKLKELYGGNILYLDAYVGGMLEGGENGPGELFKEIIKDQFTRIRDGDRFWFENKLNGLFTDEEVQMIHSITLRDIIKATTDIDETMLQKDVFFFKEGDPCPQPFQVNTTGLEPCVPFMQSTYWTDNDTTYVFTLIGLACVPLICYGIGRYLVNRRIAIGHNSACDSLTTDFANDDCGAKGDIYGVNALEWLQEEYIRQVRIEIENTTLAVKKPRGGILRKIRFETGQKIELFHSMPNPSAMHGPFVLLSQKNNHHLVIRLSSDRDLSKFLDQIRQAASGINAEVIIKDEENSILLSQAITKERRQDRLDLFFREAYAKAFNDSELQDSETSFDSSNDDILNETISREELASAMGMKANNEFVKRMFAMTAKHNEDSLSFNEFLTVLREFVNAPQKQKLQTLFKMCDLEGKNKVLRKDLAELVKSLNQTAGVHITESVQLRLFNEVLHYAGVSNDAKYLTYDDFNALFSDIPDKQPVGLPFNRKNYQPSIGETSSLNSFAVVDRSINSSAPLTLIHKVSAFLETYRQHVFIVFCFVAINLVLFFERFWHYRYMAENRDLRRVMGAGIAITRGAAGALSFCMALILLTVCRNIITLLRETVIAQYIPFDSAIAFHKIVALFAAFWATLHTVGHCVNFYHVGTQSQEGLACLFQEAFFGSNFLPSISYWFFSTITGLTGIALVAVMCIIYVFALPCFIKRAYHAFRLTHLLNIAFYALTLLHGLPKLLDSPKFGYYVVGPIVLFVIDRIIGLMQYYKKLEIVNAEILPSDIIYIEYRRPREFKYKSGQWVTVSSPSISCTFNESHAFSIASSPQDENMKLYIKAVGPWTWKLRSELIRSLNTGSPFPLIHMKGPYGDGNQEWMDYEVAIMVGAGIGVTPYASTLVDLVQRTSSDSFHRVRCRKVYFLWVCSTHKNYEWFVDVLKNVEDQARSGILETHIFVTQTFHKFDLRTTMLYICEKHFRATNSGISMFTGLHAKNHFGRPNFKAFFQFIQSEHKEQSKIGVFSCGPVNLNESIAEGCADANRQRDAPSFAHRFETF
|
1.11.1.-; 1.6.3.1
| null |
collagen and cuticulin-based cuticle development [GO:0040002]; cuticle development involved in collagen and cuticulin-based cuticle molting cycle [GO:0042338]; defense response [GO:0006952]; defense response to fungus [GO:0050832]; defense response to Gram-positive bacterium [GO:0050830]; hydrogen peroxide catabolic process [GO:0042744]; nematode larval development [GO:0002119]; post-embryonic body morphogenesis [GO:0040032]; response to oxidative stress [GO:0006979]; superoxide anion generation [GO:0042554]
|
NADPH oxidase complex [GO:0043020]; oxidoreductase complex [GO:1990204]; plasma membrane [GO:0005886]
|
calcium ion binding [GO:0005509]; heme binding [GO:0020037]; NAD(P)H oxidase H2O2-forming activity [GO:0016174]; NADH oxidase H202-forming activity [GO:0106293]; NADPH oxidase H202-forming activity [GO:0106294]; peroxidase activity [GO:0004601]; superoxide-generating NAD(P)H oxidase activity [GO:0016175]
|
PF03098;PF08022;PF01794;PF08030;
|
1.10.238.10;1.10.640.10;3.40.50.80;2.40.30.10;
|
Peroxidase family
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=H(+) + NADH + O2 = H2O2 + NAD(+); Xref=Rhea:RHEA:11264, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.6.3.1; Evidence={ECO:0000269|PubMed:11514595}; CATALYTIC ACTIVITY: Reaction=H(+) + NADPH + O2 = H2O2 + NADP(+); Xref=Rhea:RHEA:11260, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.6.3.1; Evidence={ECO:0000269|PubMed:11514595};
| null | null | null | null |
FUNCTION: Plays a role in cuticle biogenesis (PubMed:11514595, PubMed:18460651, PubMed:19406744, PubMed:23028364, PubMed:25480962). In complex with doxa-1 and tsp-15, produces reactive oxygen species (ROS), which are probably used by mlt-7 for tyrosine cross-linking, thus stabilizing cuticular extracellular matrix (PubMed:11514595, PubMed:19406744, PubMed:23028364). May regulate the production of ROS by playing a role in modulating proline catabolism (PubMed:27974198). Required in combination with mlt-7 for correct formation of cross-links in cuticle collagens (PubMed:19406744). Association with the GTPase rho-1 promotes ROS production and this interaction may be modulated by memo-1, in order to control the oxidative stress response and longevity (PubMed:28085666). {ECO:0000269|PubMed:11514595, ECO:0000269|PubMed:18460651, ECO:0000269|PubMed:19406744, ECO:0000269|PubMed:23028364, ECO:0000269|PubMed:25480962, ECO:0000269|PubMed:27974198, ECO:0000269|PubMed:28085666}.
|
Caenorhabditis elegans
|
O61219
|
DAF31_CAEEL
|
MNIRCARVDDLMSMQNANLMCLPENYQMKYYFYHALSWPQLSYIAEDHKGNVVGYVLAKMEEDPGEEPHGHITSLAVKRSYRRLGLANKMMDQTARAMVETYNAKYVSLHVRVSNRAALNLYKNTLKFEIVDTEPKYYADGEDAYAMRRDLAKWAEERNIEPADREAYTTAKTTDDKKKNRS
|
2.3.1.255
| null |
dauer exit [GO:0043054]; dauer larval development [GO:0040024]; determination of adult lifespan [GO:0008340]; multicellular organism reproduction [GO:0032504]; nematode larval development [GO:0002119]
|
NatA complex [GO:0031415]
|
peptide alpha-N-acetyltransferase activity [GO:0004596]; peptide-glutamate-alpha-N-acetyltransferase activity [GO:1990190]; peptide-serine-alpha-N-acetyltransferase activity [GO:1990189]
|
PF00583;
|
3.40.630.30;
|
Acetyltransferase family, ARD1 subfamily
| null | null |
CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N-terminal glycyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetylglycyl-[protein]; Xref=Rhea:RHEA:50496, Rhea:RHEA-COMP:12666, Rhea:RHEA-COMP:12700, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64723, ChEBI:CHEBI:133369; EC=2.3.1.255; Evidence={ECO:0000250|UniProtKB:P41227}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N-terminal L-alanyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-alanyl-[protein]; Xref=Rhea:RHEA:50500, Rhea:RHEA-COMP:12701, Rhea:RHEA-COMP:12702, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64718, ChEBI:CHEBI:83683; EC=2.3.1.255; Evidence={ECO:0000250|UniProtKB:P41227}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N-terminal L-seryl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-seryl-[protein]; Xref=Rhea:RHEA:50504, Rhea:RHEA-COMP:12703, Rhea:RHEA-COMP:12704, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64738, ChEBI:CHEBI:83690; EC=2.3.1.255; Evidence={ECO:0000250|UniProtKB:P41227}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N-terminal L-valyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-valyl-[protein]; Xref=Rhea:RHEA:50508, Rhea:RHEA-COMP:12705, Rhea:RHEA-COMP:12706, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64741, ChEBI:CHEBI:133371; EC=2.3.1.255; Evidence={ECO:0000250|UniProtKB:P41227}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N-terminal L-cysteinyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:50512, Rhea:RHEA-COMP:12707, Rhea:RHEA-COMP:12708, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:65250, ChEBI:CHEBI:133372; EC=2.3.1.255; Evidence={ECO:0000250|UniProtKB:P41227}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + N-terminal L-threonyl-[protein] = CoA + H(+) + N-terminal N(alpha)-acetyl-L-threonyl-[protein]; Xref=Rhea:RHEA:50516, Rhea:RHEA-COMP:12709, Rhea:RHEA-COMP:12710, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:64739, ChEBI:CHEBI:133375; EC=2.3.1.255; Evidence={ECO:0000250|UniProtKB:P41227};
| null | null | null | null |
FUNCTION: Catalytic subunit of the N-terminal acetyltransferase A (NatA) complex which displays alpha (N-terminal) acetyltransferase activity (By similarity). Plays a role in regulating larval development, metabolism and longevity. Functions downstream or alongside daf-3, daf-12 and daf-16 in the dauer formation pathway. Functions upstream of daf-15 to enable animal development. {ECO:0000250|UniProtKB:P41227, ECO:0000269|PubMed:25330189}.
|
Caenorhabditis elegans
|
O61267
|
LOK_DROME
|
MARDTQGTQGTQSQASNIWTQVESQPMEKIVWGRLYGKNIKIKSLGTSSKYRIIYTHSSFSVDLNNDEFTAGRGEANDLILTLNDLPEKILTRISKVHFIIKRANCELTNPVYIQDLSRNGTFVNNEKIGTNRMRILKNDDVISLSHPTYKAFVFKDLSPNESIGLPEEINKTYYVNRKLGSGAYGLVRLVYDTRTCQQFAMKIVKKNMLSGARPSTNFSDPDRVLNEAKIMKNLSHPCVVRMHDIVDKPDSVYMVLEFMRGGDLLNRIISNKLLSEDISKLYFYQMCHAVKYLHDRGITHRDLKPDNVLLETNDEETLLKVSDFGLSKFVQKDSVMRTLCGTPLYVAPEVLITGGREAYTKKVDIWSLGVVLFTCLSGTLPFSDEYGTPAAQQIKKGRFAYGHPSWKSVSQRAKLLINQMLIVDPERRPSIDDVLQSSWLRDAPMLQKAKRLMKLDGMEIEEENFLEPPTKRSRR
|
2.7.11.1
| null |
apoptotic process [GO:0006915]; cellular response to gamma radiation [GO:0071480]; cellular response to X-ray [GO:0071481]; DNA damage checkpoint signaling [GO:0000077]; DNA damage response [GO:0006974]; ectopic germ cell programmed cell death [GO:0035234]; germ cell development [GO:0007281]; intrinsic apoptotic signaling pathway by p53 class mediator [GO:0072332]; intrinsic apoptotic signaling pathway in response to DNA damage [GO:0008630]; meiotic recombination checkpoint signaling [GO:0051598]; mitotic DNA damage checkpoint signaling [GO:0044773]; oocyte karyosome formation [GO:0030717]; positive regulation of DNA-binding transcription factor activity [GO:0051091]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein phosphorylation [GO:0006468]; regulation of DNA repair [GO:0006282]
|
cytoplasm [GO:0005737]; nuclear speck [GO:0016607]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; cysteine-type endopeptidase activator activity involved in apoptotic process [GO:0008656]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; tau-protein kinase activity [GO:0050321]
|
PF00498;PF00069;
|
2.60.200.20;1.10.510.10;
|
Protein kinase superfamily, CAMK Ser/Thr protein kinase family, CDS1 subfamily
| null |
SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:9507063}. Note=Speckled subnuclear compartment.
|
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: May have a role in germline establishment. {ECO:0000269|PubMed:9507063}.
|
Drosophila melanogaster (Fruit fly)
|
O61307
|
TENM_DROME
|
MNPYEYESTLDCRDVGGGPTPAHAHPHAQGRTLPMSGHGRPTTDLGPVHGSQTLQHQNQQNLQAAQAAAQSSHYDYEYQHLAHRPPDTANNTAQRTHGRQGFLLEGVTPTAPPDVPPRNPTMSRMQNGRLTVNNPNDADFEPSCLVRTPSGNVYIPSGNLNINKGSPIDFKSGSACSTPTKDTLKGYERSTQGCMGPVLPQRSVMNGLPAHHYSAPMNFRKDLVARCSSPWFGIGSISVLFAFVVMLILLTTTGVIKWNQSPPCSVLVGNEASEVTAAKSTNTDLSKLHNSSVRAKNGQGIGLAQGQSGLGAAGVGSGGGSSAATVTTATSNSGTAQGLQSTSASAEATSSAATSSSQSSLTPSLSSSLANANNGGARTFPARSFPPDGTTFGQITLGQKLTKEIQPYSYWNMQFYQSEPAYVKFDYTIPRGASIGVYGRRNALPTHTQYHFKEVLSGFSASTRTARAAHLSITREVTRYMEPGHWFVSLYNDDGDVQELTFYAAVAEDMTQNCPNGCSGNGQCLLGHCQCNPGFGGDDCSESVCPVLCSQHGEYTNGECICNPGWKGKECSLRHDECEVADCSGHGHCVSGKCQCMRGYKGKFCEEVDCPHPNCSGHGFCADGTCICKKGWKGPDCATMDQDALQCLPDCSGHGTFDLDTQTCTCEAKWSGDDCSKELCDLDCGQHGRCEGDACACDPEWGGEYCNTRLCDVRCNEHGQCKNGTCLCVTGWNGKHCTIEGCPNSCAGHGQCRVSGEGQWECRCYEGWDGPDCGIALELNCGDSKDNDKDGLVDCEDPECCASHVCKTSQLCVSAPKPIDVLLRKQPPAITASFFERMKFLIDESSLQNYAKLETFNESRSAVIRGRVVTSLGMGLVGVRVSTTTLLEGFTLTRDDGWFDLMVNGGGAVTLQFGRAPFRPQSRIVQVPWNEVVIIDLVVMSMSEEKGLAVTTTHTCFAHDYDLMKPVVLASWKHGFQGACPDRSAILAESQVIQESLQIPGTGLNLVYHSSRAAGYLSTIKLQLTPDVIPTSLHLIHLRITIEGILFERIFEADPGIKFTYAWNRLNIYRQRVYGVTTAVVKVGYQYTDCTDIVWDIQTTKLSGHDMSISEVGGWNLDIHHRYNFHEGILQKGDGSNIYLRNKPRIILTTMGDGHQRPLECPDCDGQATKQRLLAPVALAAAPDGSLFVGDFNYIRRIMTDGSIRTVVKLNATRVSYRYHMALSPLDGTLYVSDPESHQIIRVRDTNDYSQPELNWEAVVGSGERCLPGDEAHCGDGALAKDAKLAYPKGIAISSDNILYFADGTNIRMVDRDGIVSTLIGNHMHKSHWKPIPCEGTLKLEEMHLRWPTELAVSPMDNTLHIIDDHMILRMTPDGRVRVISGRPLHCATASTAYDTDLATHATLVMPQSIAFGPLGELYVAESDSQRINRVRVIGTDGRIAPFAGAESKCNCLERGCDCFEAEHYLATSAKFNTIAALAVTPDSHVHIADQANYRIRSVMSSIPEASPSREYEIYAPDMQEIYIFNRFGQHVSTRNILTGETTYVFTYNVNTSNGKLSTVTDAAGNKVFLLRDYTSQVNSIENTKGQKCRLRMTRMKMLHELSTPDNYNVTYEYHGPTGLLRTKLDSTGRSYVYNYDEFGRLTSAVTPTGRVIELSFDLSVKGAQVKVSENAQKEMSLLIQGATVIVRNGAAESRTTVDMDGSTTSITPWGHNLQMEVAPYTILAEQSPLLGESYPVPAKQRTEIAGDLANRFEWRYFVRRQQPLQAGKQSKGPPRPVTEVGRKLRVNGDNVLTLEYDRETQSVVVMVDDKQELLNVTYDRTSRPISFRPQSGDYADVDLEYDRFGRLVSWKWGVLQEAYSFDRNGRLNEIKYGDGSTMVYAFKDMFGSLPLKVTTPRRSDYLLQYDDAGALQSLTTPRGHIHAFSLQTSLGFFKYQYYSPINRHPFEILYNDEGQILAKIHPHQSGKVAFVHDTAGRLETILAGLSSTHYTYQDTTSLVKSVEVQEPGFELRREFKYHAGILKDEKLRFGSKNSLASARYKYAYDGNARLSGIEMAIDDKELPTTRYKYSQNLGQLEVVQDLKITRNAFNRTVIQDSAKQFFAIVDYDQHGRVKSVLMNVKNIDVFRLELDYDLRNRIKSQKTTFGRSTAFDKINYNADGHVVEVLGTNNWKYLFDENGNTVGVVDQGEKFNLGYDIGDRVIKVGDVEFNNYDARGFVVKRGEQKYRYNNRGQLIHSFERERFQSWYYYDDRSRLVAWHDNKGNTTQYYYANPRTPHLVTHVHFPKISRTMKLFYDDRDMLIALEHEDQRYYVATDQNGSPLAFFDQNGSIVKEMKRTPFGRIIKDTKPEFFVPIDFHGGLIDPHTKLVYTEQRQYDPHVGQWMTPLWETLATEMSHPTDVFIYRYHNNDPINPNKPQNYMIDLDSWLQLFGYDLNNMQSSRYTKLAQYTPQASIKSNTLAPDFGVISGLECIVEKTSEKFSDFDFVPKPLLKMEPKMRNLLPRVSYRRGVFGEGVLLSRIGGRALVSVVDGSNSVVQDVVSSVFNNSYFLDLHFSIHDQDVFYFVKDNVLKLRDDNEELRRLGGMFNISTHEISDHGGSAAKELRLHGPDAVVIIKYGVDPEQERHRILKHAHKRAVERAWELEKQLVAAGFQGRGDWTEEEKEELVQHGDVDGWNGIDIHSIHKYPQLADDPGNVAFQRDAKRKRRKTGSSHRSASNRRQLKFGELSA
| null | null |
chaeta development [GO:0022416]; compound eye corneal lens development [GO:0048058]; compound eye morphogenesis [GO:0001745]; compound eye photoreceptor development [GO:0042051]; cytoplasmic microtubule organization [GO:0031122]; heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0007157]; maintenance of alignment of postsynaptic density and presynaptic active zone [GO:0099559]; maintenance of presynaptic active zone structure [GO:0048790]; motor neuron axon guidance [GO:0008045]; neuromuscular synaptic transmission [GO:0007274]; positive regulation of heterotypic cell-cell adhesion [GO:0034116]; positive regulation of locomotion [GO:0040017]; postsynaptic membrane organization [GO:0001941]; postsynaptic spectrin-associated cytoskeleton organization [GO:0099190]; presynaptic membrane organization [GO:0097090]; R7 cell development [GO:0045467]; regulation of homotypic cell-cell adhesion [GO:0034110]; regulation of terminal button organization [GO:2000331]; synapse organization [GO:0050808]; synaptic assembly at neuromuscular junction [GO:0051124]; synaptic target attraction [GO:0016200]; synaptic target recognition [GO:0008039]; synaptic vesicle membrane organization [GO:0048499]
|
cytoplasm [GO:0005737]; extracellular matrix [GO:0031012]; neuromuscular junction [GO:0031594]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]
|
cell adhesion molecule binding [GO:0050839]; filamin binding [GO:0031005]; identical protein binding [GO:0042802]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]
|
PF05593;PF15636;
|
2.60.120.260;2.10.25.10;2.180.10.10;2.120.10.30;2.130.10.10;
|
Tenascin family, Teneurin subfamily
|
PTM: Phosphorylated. Phosphorylation occurs at tyrosine residues. {ECO:0000269|PubMed:7514504}.; PTM: Proteolytically cleaved. {ECO:0000269|PubMed:7514504}.
|
SUBCELLULAR LOCATION: Cytoplasm. Postsynaptic cell membrane. Synapse, synaptosome. Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Note=Localizes at neuromuscular junction. Localizes in neuron cell bodies. Colocalizes with alpha-Spec at the membranous subsynaptic reticulum (SSR).
| null | null | null | null | null |
FUNCTION: Involved in neural development, regulating the establishment of proper connectivity within the nervous system. Acts as a homophilic and heterophilic synaptic cell adhesion molecule that drives synapse assembly. Promotes bi-directional trans-synaptic signaling with Ten-a to organize neuromuscular synapses. Functions in olfactory synaptic partner matching by promoting homophilic cell adhesion between pre-synaptic olfactory receptor neurons (ORN) axons and post-synaptic projection neurons (PN) dendrites partner in the developing antennal lobe to form stable connections. Also required for peripheral axon growth cone guidance and target recognition of motor neurons. {ECO:0000269|PubMed:21857973, ECO:0000269|PubMed:22425994, ECO:0000269|PubMed:22426000, ECO:0000269|PubMed:7514504}.
|
Drosophila melanogaster (Fruit fly)
|
O61365
|
NACH_DROME
|
MGHQEELKPEQVDLKVTPFVGYLRRTWSDFCATSSIHGLKYTRDEDTNKIVHLVWLLISVVMFICAVVMARTFYMDYRSSPTRMNVESDNTPVNRLYFPPVTICPDVLFNMQKSEAFLNTLRLPKGAELRGILRKLHIFYGFMLDDERYSAEDIEQMEALLFLNNLTIPEFVEHLRWNCDEILYRCRFNGEIMDCSKIFQLSKTFFGHCCSFNLRQKGWVNNKLNNLESFKVFHLNSLNFTAQRAIGGLRYGLSVVVRYKDDNYDPLQSYSYGVKLLIQEADAFPSAHSAAKFIAFNSETFAAVRPQETFCSSAVKALIIEERNCVFQNEFPMRYFSDYVYPNCELNCRVTNMVKFCGCHTYFFDFNRTSDRICTFRDIPCLVDNFANIITRKKSTQCYCPLTCEHIDYDVQLTNFPLELNMPVADKFYSGLAKNDGVLHVFINSFSYRRLRRDLLSNMVTLVSNLGSAFSLFVGMSMLSVVEIIYYFSVILRKNYKLECETRSQMLHKKPKFAWPKANDTHSKEQKSVFIIHKS
| null | null |
intestinal stem cell homeostasis [GO:0036335]; intracellular water homeostasis [GO:0009992]; liquid clearance, open tracheal system [GO:0035002]; sodium ion transmembrane transport [GO:0035725]; sodium ion transport [GO:0006814]
|
membrane [GO:0016020]
|
ligand-gated sodium channel activity [GO:0015280]; sodium channel activity [GO:0005272]; sodium ion transmembrane transporter activity [GO:0015081]
|
PF00858;
|
2.60.470.10;1.10.287.770;
|
Amiloride-sensitive sodium channel (TC 1.A.6) family
| null |
SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
| null | null | null | null | null |
FUNCTION: Part of a complex that plays a role in tracheal liquid clearance. Probable role in sodium transport. {ECO:0000269|PubMed:12571352, ECO:0000303|PubMed:12571352}.
|
Drosophila melanogaster (Fruit fly)
|
O61394
|
GALT6_CAEEL
|
MIASLIRSRRRSRRCVVYSVFLFGFLALWGSFALALVFLSDMYIGEDQISTQKAIKPIARSNYHVVVGHYNGNLPEDKKRNLTSEELNANLYAPHDDWGEGGAGVSHLTPEQQKLADSTFAVNQFNLLVSDGISVRRSLPEIRKPSCRNMTYPDNLPTTSVIIVYHNEAYSTLLRTVWSVIDRSPKELLKEIILVDDFSDREFLRYPTLDTTLKPLPTDIKIIRSKERVGLIRARMMGAQEAQGDVLTFLDSHCECTKGWLEPLLTRIKLNRKAVPCPVIDIINDNTFQYQKGIEMFRGGFNWNLQFRWYGMPTAMAKQHLLDPTGPIESPTMAGGLFSINRNYFEELGEYDPGMDIWGGENLEMSFRIWQCGGRVEILPCSHVGHVFRKSSPHDFPGKSSGKVLNTNLLRVAEVWMDDWKHYFYKIAPQAHRMRSSIDVSERVELRKKLNCKSFKWYLQNVFQDHFLPTPLDRFGRMTSSSNSSVCLAWTLRSSGIKTASTADCLKIFHKTQLWLYTGDRRIRTDEHLCLSVVQLLHTTSDWKIQLKECAGFDTEYWDFKPKIGRFQNRKTGLCLASPDIFDPTKDEFNPPIVQKCRSSNDRQNWTITEMSWLPEHP
|
2.4.1.-
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
|
protein O-linked glycosylation [GO:0006493]
|
Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]
|
carbohydrate binding [GO:0030246]; metal ion binding [GO:0046872]; polypeptide N-acetylgalactosaminyltransferase activity [GO:0004653]
|
PF00535;PF00652;
|
2.80.10.50;
|
Glycosyltransferase 2 family, GalNAc-T subfamily
| null |
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
| null | null |
PATHWAY: Protein modification; protein glycosylation.
| null | null |
FUNCTION: Probable glycopeptide transferase involved in O-linked oligosaccharide biosynthesis. Glycopeptide transferases catalyze the transfer of an N-acetyl-D-galactosamine residue to an already glycosylated peptide (By similarity). In contrast to other members of the family, it does not act as a peptide transferase that transfers GalNAc onto serine or threonine residue on peptides that have been tested. Some peptide transferase activity is however not excluded, considering that its appropriate peptide substrate may remain unidentified. {ECO:0000250}.
|
Caenorhabditis elegans
|
O61443
|
MK38B_DROME
|
MSRKMAKFYKLDINRTEWEIPETYQNLQPVGQGAYGQVCKAVVRGTSTKVAIKKLARPFQSAVHAKRTYRELRLLKHMDHENVIGLLDVFHPGQPADSLDQFQQVYMVTHLMDADLNNIIRTQKLSDDHVQFLVYQILRGLKYIHSAGVIHRDLKPSNIAVNEDCELRILDFGLARPAESEMTGYVATRWYRAPEIMLNWMHYNQTADIWSVGCIMAELLTGRTLFPGTDHIHQLNLIMEVLGTPADEFMSRISSESARNYIRSLPVMPRRNFRDIFRGANPLAIDLLEKMLELDADKRITAEQALAHPYMEKYHDPTDEQTAALYDQSFEENELPVEKWREMVFSEVTAFKPTAAFAELLPKEQ
|
2.7.11.24
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
|
cellular response to arsenic-containing substance [GO:0071243]; cellular response to cadmium ion [GO:0071276]; cellular response to reactive oxygen species [GO:0034614]; circadian rhythm [GO:0007623]; defense response to bacterium [GO:0042742]; defense response to fungus [GO:0050832]; determination of adult lifespan [GO:0008340]; heart morphogenesis [GO:0003007]; imaginal disc-derived wing morphogenesis [GO:0007476]; immune response [GO:0006955]; intracellular signal transduction [GO:0035556]; MAPK cascade [GO:0000165]; negative regulation of hippo signaling [GO:0035331]; osmosensory signaling pathway [GO:0007231]; p38MAPK cascade [GO:0038066]; paracrine signaling [GO:0038001]; positive regulation of actin filament polymerization [GO:0030838]; positive regulation of cell size [GO:0045793]; positive regulation of multicellular organism growth [GO:0040018]; positive regulation of protein phosphorylation [GO:0001934]; protein phosphorylation [GO:0006468]; regulation of adult chitin-containing cuticle pigmentation [GO:0048082]; regulation of BMP signaling pathway [GO:0030510]; regulation of cellular response to oxidative stress [GO:1900407]; regulation of innate immune response [GO:0045088]; regulation of terminal button organization [GO:2000331]; response to bacterium [GO:0009617]; response to heat [GO:0009408]; response to hydrogen peroxide [GO:0042542]; response to salt stress [GO:0009651]; response to starvation [GO:0042594]; stress-activated MAPK cascade [GO:0051403]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; MAP kinase activity [GO:0004707]; 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, MAP kinase subfamily
|
PTM: Dually phosphorylated on Thr-183 and Tyr-185, which activates the enzyme. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus.
|
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=2.7.11.24; 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=2.7.11.24;
| null | null | null | null |
FUNCTION: Kinase involved in dpp signal transduction pathway in the process of wing morphogenesis when the levels of dpp are enhanced or inhibited. May down-regulate insect immunity gene expression after prolonged infection. {ECO:0000269|PubMed:10022918, ECO:0000269|PubMed:9584193}.
|
Drosophila melanogaster (Fruit fly)
|
O61460
|
VAB1_CAEEL
|
MRLYNSRILNPHQSIFILVLQCLITIVTSHQEVLFDLSKVGSDLKWDQVSLRHDRDDVWMEETWRNPAATDEKHANQRAYVTCNYDMINPSNWLFSHFIEVKTARRIYIELLFNTRDCDAYLNPKSCKETFSVYLKQFKTSRPGSTKIEKERFSEDIDNWKNIGRLARSNSNMTTETLGMEIDSDTKTIRIAFEEQGICLSLLNVKIYYRICDEFTDQLVYFRPQVTGPKETDMVRMNGSCIPNASKKIPGVDLIGLCMSTGSGIKTSGECVCDSGYSQIADSNGARCESCPTNTYKPKGQSLCKSCPSNSISSEAASSCRCLNGYFRAEDELISMPCTQPPSRPIKLVANAITATSTRLSWNEPSSLGGRPEIWYEVKCSGRGECGTVVMTPGDKKLSTRSVQINGLRPSSDYTFLVFAKNKVSAQFPEFSEKNAVIDIRTRSEEEDVPPVSHLRVDASQSDGITIAWSVSDSDVSDFEVEVRPAIVKKRTFETRHVNMTYTTFIGLNPETVYQFRVRIRDDLRWSQPISYQLGRGLMSSPSSNEVEESQFLNQTGSALLIIIALILIVIAVALCMIVVQKKSKNRKQMSDLDVLDTYKQDSMTPDYHTTSRHHHHQGNLPATLHEQLRSTTKLNAPLIPSFGSPISQPPPYYGGVHPNSGKYKTYVDPTTYEDPYQALIEFTFDISPNDVFITQVIGGGEFGDVCLGGLSKNSPAAAKWSVSNTTMGRGGGGGGYESEPYETVAIKTLKSGSSAKAKAEFLTEATIMGQFSHPNVIRLIGVVTSAEPVMIVAEYMANGSLDQFLRNTDQRGEKVHWEKITEMLYGIASGMKYLTDMGYVHRVSFLRDLAARNVLLDMELRCKIADFGLSRGVRSEGSSVEPEYTTNGGKIPVRWTAPEAITHRKFTPSSDVWSFGVVIWEVCSFGERPYWDWTNQKVISEVMIGYRLPPPMDCPMGLYRIAQWCWKMERHERPTFTQLLATFHKYILQPTLIEHDPGELPRRVQSQSALNTYGSVNVGVVPTPPSSAAPMPSLDDFLRQIGLNHVYGQLVSNNIHSVSDLANTSHLDLLAYGLMSAECSTVRDGLNGRISGSPPGSSGTIHATTRGTRTTRPPREEGFFV
|
2.7.10.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
|
axon guidance [GO:0007411]; axonogenesis [GO:0007409]; embryo development ending in birth or egg hatching [GO:0009792]; embryonic body morphogenesis [GO:0010172]; morphogenesis of embryonic epithelium [GO:0016331]; oocyte maturation [GO:0001556]; phosphorylation [GO:0016310]; regulation of axon guidance [GO:1902667]
|
axon [GO:0030424]; dendrite [GO:0030425]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]
|
ATP binding [GO:0005524]; ephrin receptor activity [GO:0005003]; protein domain specific binding [GO:0019904]; protein tyrosine kinase activity [GO:0004713]; transmembrane receptor protein tyrosine kinase activity [GO:0004714]; transmembrane-ephrin receptor activity [GO:0005005]
|
PF14575;PF01404;PF00041;PF07714;
|
2.60.40.1770;2.60.120.260;2.60.40.10;1.10.510.10;2.10.50.10;
|
Protein kinase superfamily, Tyr protein kinase family, Ephrin receptor subfamily
|
PTM: Autophosphorylated. {ECO:0000269|PubMed:19853560}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12533508, ECO:0000269|PubMed:19853560}; Single-pass type I membrane protein {ECO:0000305}.
|
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:0000269|PubMed:19853560};
| null | null | null | null |
FUNCTION: Receptor for members of the ephrin family (By similarity). Receptor for major sperm proteins (MSPs), that functions as a sperm-sensing checkpoint which inhibits oocyte meiotic maturation and ovulation when sperm are not available for fertilization (PubMed:12533508). Specifically, functions to negatively regulates oocyte maturation and MAPK activation in the absence of MSPs (PubMed:12533508, PubMed:19853560). Required for the MSP-mediated increase in the basal sheath cell contraction rate in somatic cells (PubMed:12533508). Phosphorylates phosphatase daf-18/PTEN which probably promotes daf-18 degradation (PubMed:19853560). By inactivating daf-18, positively regulates insulin-like daf-2 signaling cascade (PubMed:9506518). Involved in interactions between neuronal substrate cells and a migrating epithelial sheet in head epidermis morphogenesis (PubMed:9506518). Also required for cell movements following gastrulation and during ventral closure of the epidermis (PubMed:9506518). Might play a role in spermatheca morphogenesis (PubMed:25529479). Involved in axon guidance of SDQL neurons during neurogenesis (PubMed:26903502). {ECO:0000250|UniProtKB:Q62413, ECO:0000269|PubMed:12533508, ECO:0000269|PubMed:19853560, ECO:0000269|PubMed:25529479, ECO:0000269|PubMed:26903502, ECO:0000269|PubMed:9506518}.
|
Caenorhabditis elegans
|
O61577
|
KTNA1_STRPU
|
MSVDEICENTKMGREYALLGNYETSLVYYQGVLQQIQKLLTSVHEPQRKHQWQTIRQELSQEYEHVKNITKTLNGFKSEPAAPEPAPNHRAAPFSHHQHAAKPAAAEPARDPDVWPPPTPVDHRPSPPYQRAARKDPPRRSEPSKPANRAPGNDRGGRGPSDRRGDARSGGGGRGGARGSDKDKNRGGKSDKDKKAPSGEEGDEKKFDPAGYDKDLVENLERDIVQRNPNVHWADIAGLTEAKRLLEEAVVLPLWMPDYFKGIRRPWKGVLMVGPPGTGKTMLAKAVATECGTTFFNVSSASLTSKYHGESEKLVRLLFEMARFYAPSTIFIDEIDSICSKRGTGSEHEASRRVKSELLIQMDGVSGPSAGEESSKMVMVLAATNFPWDIDEALRRRLEKRIYIPLPEIDGREQLLRINLKEVPLADDIDLKSIAEKMDGYSGADITNVCRDASMMAMRRRIQGLRPEEIRHIPKEELNQPSTPADFLLALQKVSKSVGKEDLVKYMAWMEEFGSV
|
5.6.1.1
| null |
cell cycle [GO:0007049]; cell division [GO:0051301]; microtubule severing [GO:0051013]
|
centrosome [GO:0005813]; cytoplasm [GO:0005737]; microtubule [GO:0005874]; microtubule cytoskeleton [GO:0015630]; midbody [GO:0030496]; mitotic spindle pole [GO:0097431]; spindle [GO:0005819]; spindle pole [GO:0000922]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; isomerase activity [GO:0016853]; microtubule binding [GO:0008017]; microtubule severing ATPase activity [GO:0008568]
|
PF00004;PF17862;PF21126;PF09336;
|
1.10.8.60;3.40.50.300;1.20.58.80;
|
AAA ATPase family, Katanin p60 subunit A1 subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03023}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03023, ECO:0000269|PubMed:8907702}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000255|HAMAP-Rule:MF_03023, ECO:0000269|PubMed:8907702}. Note=Predominantly cytoplasmic (By similarity). Also localized to the interphase centrosome and the mitotic spindle poles (PubMed:8907702). Enhanced recruitment to the mitotic spindle poles requires microtubules and interaction with KATNB1 (By similarity). {ECO:0000255|HAMAP-Rule:MF_03023, ECO:0000269|PubMed:8907702}.
|
CATALYTIC ACTIVITY: Reaction=n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers.; EC=5.6.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_03023};
| null | null | null | null |
FUNCTION: Catalytic subunit of a complex which severs microtubules in an ATP-dependent manner. Microtubule severing may promote rapid reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. In mitotic spindles this could allow depolymerization of the microtubule end proximal to the centrosome, and subsequent poleward microtubule flux. {ECO:0000255|HAMAP-Rule:MF_03023, ECO:0000269|PubMed:10531065, ECO:0000269|PubMed:8221885}.
|
Strongylocentrotus purpuratus (Purple sea urchin)
|
O61643
|
INHB_DROME
|
MRFAFDSNHSQSGAPFKGSRCFFNCQCICCRQGCCVVVVKCCCCFNLNCCNSLGSRKSFPQPAAMRKKVADLEVLRVSRFVAVILVLARWVTAVATLLTSCILLDIFSVPGQSGVADRSQASSRTVHVSVPTTPNETPSSTSETKLKLLYGYTSYDINNDQQVKSNNLCRVLCKSRNRKRQRRRRRRRNHRRRRHRYTKRLHHLMQDNMSGFEQRLNFSDAKCQSLETNYGTNYDLVQGGKLFSQSERSLLVSPLREIEAPWPAIHGSMRNCSKIKRNRANLIWLLIGLVWFEVKLINCNGISSSNYYASNLESHKGCTLCHESGKPNIYTDKDNPHTDYNIYNKYHSNNNFNKKTNQPHNNIAPSDEVRLESIKRQILTKLGLSHKPNVSHPLPKQFIWETIYRVDGGRMIPNNAFGSSGKNLDQKTIKLRAFASPGSHLFNGRGGRTDQRSERDPSHHKYRSPFDFTFNISKNNVYGKVLRNRSLERIDKKNSFLNGWTENRQLKINSQIASMPIELKSHHNSSPKELKSGAVRKVNGINGTQMNENALKKSTYPIDINHSIDNKTHTGKNGEMSHNDYEYFNDYSVQTHDKNRYHEGRSSIGYQPAIHNIEYENQKGHHESFADDHENIDHEDFFGNTQEIITFAEEGTQYRQYRILEFSAQNRRVPSQKLSIRSAQIHIRIDKPHSLWIEKAKSLPEKHLLNTKRKWGANKPHHRIKIWVFQLSTSINITEKGIDKAIIFRASFQVDPKNLGWQKFDLTDTIREWYGHTSHEKLRLLIDCTGCGGRYSLHLFQTSKLRGNSSDYLSTNPNRPFLVLHTESSRTRRVRRRAVDCGGALNGQCCKESFYVSFKALGWDDWIIAPRGYFANYCRGDCTGSFRTPDTFQTFHAHFIEEYRKMGLMNGMRPCCAPIKFSSMSLIYYGDDGIIKRDLPKMVVDECGCP
| null | null |
activin receptor signaling pathway [GO:0032924]; glucose homeostasis [GO:0042593]; mushroom body development [GO:0016319]; positive regulation of glycogen catabolic process [GO:0045819]; positive regulation of imaginal disc growth [GO:0045572]; positive regulation of neuroblast proliferation [GO:0002052]; R8 cell fate specification [GO:0045464]; regulation of imaginal disc-derived wing size [GO:0044719]; regulation of synapse structure or activity [GO:0050803]; response to glucose [GO:0009749]
|
extracellular space [GO:0005615]
|
cytokine activity [GO:0005125]; growth factor activity [GO:0008083]
|
PF00019;
|
2.60.120.970;2.10.90.10;
|
TGF-beta family
|
PTM: Cleaved in vitro by metalloproteases tok and tld to produce a 30 kDa product. {ECO:0000269|PubMed:17119021}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Controls several aspects of neuronal morphogenesis; essential for optic lobe development, EcR-B1 expression in larval brains, mushroom body remodeling, dorsal neuron morphogenesis and motoneuron axon guidance. Ligands Actbeta and daw act redundantly through the Activin receptor Babo and its transcriptional mediator Smad2 (Smox), to regulate neuroblast numbers and proliferation rates in the developing larval brain. {ECO:0000269|PubMed:12581521, ECO:0000269|PubMed:18171686}.
|
Drosophila melanogaster (Fruit fly)
|
O61661
|
CHK1_DROME
|
MAATLTEAGTGPAATREFVEGWTLAQTLGEGAYGEVKLLINRQTGEAVAMKMVDLKKHPDAANSVRKEVCIQKMLQDKHILRFFGKRSQGSVEYIFLEYAAGGELFDRIEPDVGMPQHEAQRYFTQLLSGLNYLHQRGIAHRDLKPENLLLDEHDNVKISDFGMATMFRCKGKERLLDKRCGTLPYVAPEVLQKAYHAQPADLWSCGVILVTMLAGELPWDQPSTNCTEFTNWRDNDHWQLQTPWSKLDTLAISLLRKLLATSPGTRLTLEKTLDHKWCNMQFADNERSYDLVDSAAALEICSPKAKRQRLQSSAHLSNGLDDSISRNYCSQPMPTMRSDDDFNVRLGSGRSKEDGGDRQTLAQEARLSYSFSQPALLDDLLLATQMNQTQNASQNYFQRLVRRMTRFFVTTRWDDTIKRLVGTIERLGGYTCKFGDDGVVTVSTVDRNKLRLVFKAHIIEMDGKILVDCRLSKGCGLEFKRRFIKIKNALEDIVLKGPTTWPIAIATNSVP
|
2.7.11.1
| null |
centrosome separation [GO:0051299]; DNA damage checkpoint signaling [GO:0000077]; mitotic DNA replication checkpoint signaling [GO:0033314]; protein phosphorylation [GO:0006468]; regulation of cell cycle [GO:0051726]; regulation of syncytial blastoderm mitotic cell cycle [GO:0007348]; spindle assembly [GO:0051225]; wound healing [GO:0042060]
|
cytosol [GO:0005829]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; histone H3T11 kinase activity [GO:0035402]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00069;
|
3.30.310.80;1.10.510.10;
|
Protein kinase superfamily, CAMK Ser/Thr protein kinase family, NIM1 subfamily
|
PTM: Phosphorylated in a MEI-41/ATR dependent manner in response to DNA damage or the presence of unreplicated DNA. {ECO:0000269|PubMed:15860729}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10980701, ECO:0000269|PubMed:16079276}.
|
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:O14757}; 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:0000250|UniProtKB:O14757};
| null | null | null | null |
FUNCTION: Serine/threonine-protein kinase which is required for checkpoint-mediated cell cycle arrest and activation of DNA repair in response to the presence of DNA damage or unreplicated DNA. May also negatively regulate cell cycle progression during unperturbed cell cycles. May phosphorylate the CDC25 phosphatase stg, which promotes its degradation. This results in increased inhibitory tyrosine phosphorylation of Cdk1-cyclin complexes and consequent inhibition of cell cycle progression. {ECO:0000269|PubMed:10209095, ECO:0000269|PubMed:10469601, ECO:0000269|PubMed:10980701, ECO:0000269|PubMed:12919679, ECO:0000269|PubMed:14711410, ECO:0000269|PubMed:15723794, ECO:0000269|PubMed:15860729, ECO:0000269|PubMed:16079276, ECO:0000269|PubMed:7925016, ECO:0000269|PubMed:9197245, ECO:0000269|PubMed:9214509}.
|
Drosophila melanogaster (Fruit fly)
|
O61667
|
EGL1_CAEEL
|
MLMLTFASTSSDLLPMSNVFDVQSSVFYNEKNMFYSSSQDFSSCEDSSQFADDSGFFDDSEISSIGYEIGSKLAAMCDDFDAQMMSYSAHASDRSLFHRLLDFFAF
| null | null |
actin filament depolymerization [GO:0030042]; apoptotic mitochondrial changes [GO:0008637]; apoptotic process [GO:0006915]; apoptotic process involved in development [GO:1902742]; defense response to Gram-negative bacterium [GO:0050829]; positive regulation of apoptotic process [GO:0043065]; positive regulation of apoptotic process involved in development [GO:1904747]; positive regulation of programmed cell death [GO:0043068]; positive regulation of protein-containing complex assembly [GO:0031334]; positive regulation of synapse pruning [GO:1905808]; regulation of development, heterochronic [GO:0040034]
|
cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; mitochondrion [GO:0005739]; presynapse [GO:0098793]
| null |
PF11430;
| null | null | null |
SUBCELLULAR LOCATION: Synapse {ECO:0000269|PubMed:26074078}. Note=Localizes to RMED/V synaptic regions in L1 larvae. {ECO:0000269|PubMed:26074078}.
| null | null | null | null | null |
FUNCTION: Plays a major role in programmed cell death (PCD or apoptosis) by negatively regulating ced-9 (PubMed:10688797, PubMed:15383288, PubMed:9604928). Binds to and directly inhibits the activity of ced-9, releasing the cell death activator ced-4 from a ced-9/ced-4 containing protein complex and allowing ced-4 to activate the cell-killing caspase ced-3 (PubMed:10688797, PubMed:15383288, PubMed:9604928). Required to activate programmed cell death in the sister cells of the serotonergic neurosecretory motor (NSM) neurons during embryogenesis (PubMed:12874127). Required to activate programmed cell death in the sister cells of the M4 motor neuron and I1 pharyngeal neuron during embryogenesis (PubMed:20713707). During larval development, required for the elimination of transient presynaptic components upstream of ced-9, ced-4 and ced-3 apoptotic pathway (PubMed:26074078). Together with ain-1, a component of the miRNA-induced-silencing complex (miRISC), and probably upstream of ced-3 and ced-4, regulates temporal cell fate patterning during larval development (PubMed:25432023). Has been shown in two studies to be dispensable in mitochondrial dynamics and morphology during early embryonic development (PubMed:19327994, PubMed:21949250). However, one study shows that during larval development, egl-1 is involved in modulating mitochondrial dynamics, perhaps acting by stabilizing the interaction between ced-9 and drp-1 in order to promote mitochondrial fission (PubMed:21949250). Involved in inducing mitochondrial fragmentation during apoptosis, probably acting via ced-9 and dynamin-related protein drp-1 (PubMed:15716954). {ECO:0000269|PubMed:10688797, ECO:0000269|PubMed:12874127, ECO:0000269|PubMed:15383288, ECO:0000269|PubMed:20713707, ECO:0000269|PubMed:25432023, ECO:0000269|PubMed:26074078, ECO:0000269|PubMed:9604928}.
|
Caenorhabditis elegans
|
O61668
|
SIX1_MESMA
|
MKFFLIFLVIFPIMGVLGKKNGYAVDSSGKVSECLLNNYCNNICTKVYYATSGYCCLLSCYCFGLDDDKAVLKIKDATKSYCDVQIIG
| null | null |
defense response [GO:0006952]
|
extracellular region [GO:0005576]
|
sodium channel inhibitor activity [GO:0019871]; toxin activity [GO:0090729]
|
PF00537;
|
3.30.30.10;
|
Long (4 C-C) scorpion toxin superfamily, Sodium channel inhibitor family, Beta subfamily
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8068186}.
| null | null | null | null | null |
FUNCTION: Excitatory insect beta-toxins induce a spastic paralysis. They bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing. This toxin is active only on insects. {ECO:0000269|PubMed:11042276}.
|
Mesobuthus martensii (Manchurian scorpion) (Buthus martensii)
|
O61705
|
SCXA_MESMA
|
MNYLVMISFALLLMKGVESVRDAYIAKPENCVYECGITQDCNKLCTENGAESGYCQWGGKYGNACWCIKLPDSVPIRVPGKCQR
| null | null |
defense response [GO:0006952]; negative regulation of voltage-gated sodium channel activity in another organism [GO:0044489]
|
extracellular region [GO:0005576]
|
potassium channel inhibitor activity [GO:0019870]; sodium channel inhibitor activity [GO:0019871]; toxin activity [GO:0090729]
|
PF00537;
|
3.30.30.10;
|
Long (4 C-C) scorpion toxin superfamily, Sodium channel inhibitor family, Alpha subfamily
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15200476}.
| null | null | null | null | null |
FUNCTION: Binds to voltage-dependent sodium channels (Nav) and voltage-dependent delayed rectifier potassium channels and inhibits the inactivation of the activated channels, thereby blocking neuronal transmission. Administration to mice at a dosage of 0.8 mg/kg produces an analgesic effect. {ECO:0000269|PubMed:15200476}.
|
Mesobuthus martensii (Manchurian scorpion) (Buthus martensii)
|
O61707
|
TAF4_CAEEL
|
MSLPRFRLVQGKAIGERSTPGVSTPEPAPPQIKQEVDYQDAHQMAPEPVEAPQAQNHQMQPPRQPIQQQMQHFQSPSPMAPQGPPGTPQNSAAAAAAASDDKNVTKCVRFLKTLINLSNNDDPEMPDKAARVKELIRGVIYLETTAEEFTRNLQQVLKSQAQPHLLPFLQNTLPALRNAVRNGTASVEGVNPPPGYVFNNGRTPGPPQPPPPQQQSQQQPPLEMRQIPNPNQIPPQMVQGGPHMVSVGARPMIRPMGPGGPSPMGLQGPVRGPMGHQMVQMHPPPPPQQIQQQHPAPPVEMEVEENLQPTAAATATRQYPEGSLKSSILKPDEVLNRITKRMMSSCSVEEEALVAISDAVESHLRELITLMAGVAEHRVESLRIPENYVAIDDVKRQLRFLEDLDRQEEELRESREKESLIRMSKNKNSGKETIEKAKEMQRQDAEAKRNRDANAAAIAALSSNKTVKNKWENTGAATTAPRPRTVRVTTRDLHLLVNQDSRFTGTFIREKMSYGGPAVDTTI
| null | null |
determination of adult lifespan [GO:0008340]; embryo development ending in birth or egg hatching [GO:0009792]; regulation of mitotic cell cycle, embryonic [GO:0009794]; transcription initiation at RNA polymerase II promoter [GO:0006367]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]; transcription factor TFIID complex [GO:0005669]
|
DNA binding [GO:0003677]; RNA polymerase II general transcription initiation factor activity [GO:0016251]
|
PF05236;PF07531;
|
1.20.120.1110;
|
TAF4 family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00440, ECO:0000269|PubMed:11566890, ECO:0000269|PubMed:18854162}. Cytoplasm {ECO:0000269|PubMed:18854162}. Note=Localization is ubiquitous in one-cell and early two-cell embryos, then enriched in nucleus in all subsequent embryo stages (PubMed:18854162). Localization to the nucleus is prevented by interaction with oma-1 and is sequestered in the cytoplasm, following fertilization, and thus allows for transcriptional suppression in early embryos, but not in oocytes (PubMed:18854162). Localized to the nucleus in a taf-12-dependent manner (PubMed:18854162). {ECO:0000269|PubMed:18854162}.
| null | null | null | null | null |
FUNCTION: The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription (By similarity). TFIID recognizes and binds promoters via its subunit tbp-1, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC) (By similarity). The TFIID complex consists of tbp-1 and TBP-associated factors (TAFs), including taf-4 (By similarity). Essential for early embryonic development, probably acting via activating transcription initiation by RNA polymerase II, as part of the TFIID complex (PubMed:11566890, PubMed:18854162). In early embryos, but not oocytes, remains, presumably inactive, in the cytoplasm as a result of binding to oma-1 (PubMed:18854162). Upon degradation of oma-1, taf-4 is released and bound by taf-12, and the taf-4/12 heterodimer translocates to the nucleus and transcriptional repression is relieved (PubMed:18854162). Involved in lifespan extension in a manner dependent upon mitochondrial function (PubMed:24107417). Plays a role in modulating polyribosome formation (PubMed:30198021). {ECO:0000250|UniProtKB:O00268, ECO:0000269|PubMed:11566890, ECO:0000269|PubMed:18854162, ECO:0000269|PubMed:24107417, ECO:0000269|PubMed:30198021}.
|
Caenorhabditis elegans
|
O61715
|
INX19_CAEEL
|
MWRTPASTGPLRQDRQMFFHATLARSFINALSVRGDDDAVDRLNYYYTPLILAVCCLVISAKQYGGTPIECWVNPHSRESMEEYIESYCWIQNTYWIPMYENVPDDHTAREEKQIGYYQWVPFILIAEALMFSLPCIFWRLCSFQSGLNIQTLINAACDGQALLDASDRQKAVEAITTNFVDNLDLQSPNGRIRARGWIARIKFSRFLSGQCLSILHSFTKLLYSMNVVAQFLILNACLKSSDFLFFGFQVLNDIWAGRPWTETGHFPRVTLCDFEVRYLANLNRYTVQCALLINIINEKVFAFLWCWYMILAIITTCSFIYWIANSFIHSEKVDYVMKFIQIAESSEFKKLQKFEKDATVERLYTVIAFAPHLLDTFVSDFLKSDGVLMLRMISNHAGDMIVVQLVRNLWQEFRERNWREFEEHEEMKDVEMRRIHGGERIVISNPGQTKSFL
| null | null |
cell differentiation [GO:0030154]; determination of left/right asymmetry in nervous system [GO:0035545]; intercellular transport [GO:0010496]; monoatomic ion transmembrane transport [GO:0034220]
|
gap junction [GO:0005921]; neuronal cell body membrane [GO:0032809]; plasma membrane [GO:0005886]
|
calcium channel inhibitor activity [GO:0019855]; gap junction channel activity [GO:0005243]; gap junction hemi-channel activity [GO:0055077]; protein kinase inhibitor activity [GO:0004860]
|
PF00876;
| null |
Pannexin family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17512411}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00351, ECO:0000269|PubMed:17512411}. Cell junction, gap junction {ECO:0000269|PubMed:17512411}. Note=Specifically present at the transient gap junctions formed between the cell bodies of embryonic neurons. Excluded from axons and dendrites.
| null | null | null | null | null |
FUNCTION: Structural component of the gap junctions that specifically coordinates left-right asymmetry in the developing nervous system. Acts by forming gap junction network linking embryonic neurons and providing electrical coupling between cells, leading to promote or inhibit AWC signaling. Required for the left and right AWC olfactory neurons to establish asymmetric patterns of gene expression during embryogenesis. Acts autonomously. {ECO:0000269|PubMed:17512411}.
|
Caenorhabditis elegans
|
O61722
|
PRL1_DROME
|
MSITMRQKDLRPAPALIEYKGMKFLITDRPSDITINHYIMELKKNNVNTVVRVCEPSYNTDELETQGITVKDLAFEDGTFPPQQVVDEWFEVLKDKYQQNPEACVAVHCVAGLGRAPVLVALALIELGLKYEAAVEMIRDKRRGAINAKQLSFLEKYKPKARLKHKNGHKNSCSVQ
|
3.1.3.48
| null |
cellular response to carbon dioxide [GO:0071244]; endothelial cell migration [GO:0043542]; negative regulation of BMP signaling pathway [GO:0030514]; peptidyl-tyrosine dephosphorylation [GO:0035335]
|
apicolateral plasma membrane [GO:0016327]; axon [GO:0030424]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
protein tyrosine phosphatase activity [GO:0004725]
|
PF00102;
|
3.90.190.10;
|
Protein-tyrosine phosphatase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23577193}. Cell membrane {ECO:0000269|PubMed:23577193, ECO:0000269|PubMed:31404830}; Lipid-anchor {ECO:0000250|UniProtKB:Q93096}. Apicolateral cell membrane {ECO:0000269|PubMed:23577193}. Cell projection, axon {ECO:0000269|PubMed:31048465}. Note=During embryogenesis localizes to cytoplasmic compartments from 1 to 14 hours after egg laying, thereafter becomes associated with the plasma membrane (PubMed:23577193). Localizes to contralateral axon collaterals of dorsocentral neurons (PubMed:31048465). {ECO:0000269|PubMed:23577193, ECO:0000269|PubMed:31048465}.
|
CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000250|UniProtKB:Q93096};
| null | null | null | null |
FUNCTION: Probable phosphatase (Probable). Inhibits growth possibly by negatively regulating Src64B-induced growth (PubMed:23577193). Regulates central nervous system circuit formation and stabilization of synapse-dense terminal arbors (PubMed:31048465). In dorsocentral neurons, regulates synaptogenesis in terminal arbors via modulation of the insulin receptor pathway, likely upstream of Akt1, and via reduction of PtdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) levels (PubMed:31048465). In the nervous system, plays a protective role together with uex in response to olfactory carbon dioxide stimulation (PubMed:31404830). {ECO:0000269|PubMed:23577193, ECO:0000269|PubMed:31048465, ECO:0000269|PubMed:31404830, ECO:0000305|PubMed:31048465}.
|
Drosophila melanogaster (Fruit fly)
|
O61734
|
CYCL_DROME
|
MEVQEFCENMEEIEDENYDEEKSARTSDENRKQNHSEIEKRRRDKMNTYINELSSMIPMCFAMQRKLDKLTVLRMAVQHLRGIRGSGSLHPFNGSDYRPSFLSDQELKMIILQASEGFLFVVGCDRGRILYVSDSVSSVLNSTQADLLGQSWFDVLHPKDIGKVKEQLSSLEQCPRERLIDAKTMLPVKTDVPQSLCRLCPGARRSFFCRMKLRTASNNQIKEESDTSSSSRSSTKRKSRLTTGHKYRVIQCTGYLKSWTPIKDEDQDADSDEQTTNLSCLVAIGRIPPNVRNSTVPASLDNHPNIRHVLFISRHSGEGKFLFIDQRATLVIGFLPQEILGTSFYEYFHNEDIAALMESHKMVMQVPEKVTTQVYRFRCKDNSYIQLQSEWRAFKNPWTSEIDYIIAKNSVFL
| null | null |
behavioral response to cocaine [GO:0048148]; circadian regulation of gene expression [GO:0032922]; circadian regulation of heart rate [GO:0003053]; circadian rhythm [GO:0007623]; eclosion rhythm [GO:0008062]; locomotor rhythm [GO:0045475]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of circadian sleep/wake cycle, sleep [GO:0045187]; regulation of transcription by RNA polymerase II [GO:0006357]; response to starvation [GO:0042594]; rhythmic behavior [GO:0007622]
|
aryl hydrocarbon receptor complex [GO:0034751]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667]
|
DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; protein heterodimerization activity [GO:0046982]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF00010;PF00989;PF14598;
|
4.10.280.10;3.30.450.20;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
| null | null | null | null | null |
FUNCTION: Putative transcription factor involved in the generation of biological rhythms. Activates cycling transcription of Period (PER) and Timeless (TIM) by binding to the E-box (5'-CACGTG-3') present in their promoters.
|
Drosophila melanogaster (Fruit fly)
|
O61735
|
CLOCK_DROME
|
MDDESDDKDDTKSFLCRKSRNLSEKKRRDQFNSLVNDLSALISTSSRKMDKSTVLKSTIAFLKNHNEATDRSKVFEIQQDWKPAFLSNDEYTHLMLESLDGFMMVFSSMGSIFYASESITSQLGYLPQDLYNMTIYDLAYEMDHEALLNIFMNPTPVIEPRQTDISSSNQITFYTHLRRGGMEKVDANAYELVKFVGYFRNDTNTSTGSSSEVSNGSNGQPAVLPRIFQQNPNAEVDKKLVFVGTGRVQNPQLIREMSIIDPTSNEFTSKHSMEWKFLFLDHRAPPIIGYMPFEVLGTSGYDYYHFDDLDSIVACHEELRQTGEGKSCYYRFLTKGQQWIWLQTDYYVSYHQFNSKPDYVVCTHKVVSYAEVLKDSRKEGQKSGNSNSITNNGSSKVIASTGTSSKSASATTTLRDFELSSQNLDSTLLGNSLASLGTETAATSPAVDSSPMWSASAVQPSGSCQINPLKTSRPASSYGNISSTGISPKAKRKCYFYNNRGNDSDSTSMSTDSVTSRQSMMTHVSSQSQRQRSHHREHHRENHHNQSHHHMQQQQQHQNQQQQHQQHQQLQQQLQHTVGTPKMVPLLPIASTQIMAGNACQFPQPAYPLASPQLVAPTFLEPPQYLTAIPMQPVIAPFPVAPVLSPLPVQSQTDMLPDTVVMTPTQSQLQDQLQRKHDELQKLILQQQNELRIVSEQLLLSRYTYLQPMMSMGFAPGNMTAAAVGNLGASGQRGLNFTGSNAVQPQFNQYGFALNSEQMLNQQDQQMMMQQQQNLHTQHQHNLQQQHQSHSQLQQHTQQQHQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQLQLQQQNDILLREDIDDIDAFLNLSPLHSLGSQSTINPFNSSSNNNNQSYNGGSNLNNGNQNNNNRSSNPPQNNNEDSLLSCMQMATESSPSINFHMGISDDGSETQSEDNKMMHTSGSNLVQQQQQQQQQQQILQQHQQQSNSFFSSNPFLNSQNQNQNQLPNDLEILPYQMSQEQSQNLFNSPHTAPGSSQ
| null | null |
behavioral response to cocaine [GO:0048148]; circadian regulation of gene expression [GO:0032922]; circadian regulation of heart rate [GO:0003053]; circadian rhythm [GO:0007623]; eclosion rhythm [GO:0008062]; entrainment of circadian clock [GO:0009649]; locomotor rhythm [GO:0045475]; negative regulation of apoptotic process [GO:0043066]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of circadian sleep/wake cycle, sleep [GO:0045187]; regulation of transcription by RNA polymerase II [GO:0006357]; response to light stimulus [GO:0009416]; response to temperature stimulus [GO:0009266]; rhythmic behavior [GO:0007622]
|
CLOCK-BMAL transcription complex [GO:1990513]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; protein heterodimerization activity [GO:0046982]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF00010;PF14598;
|
4.10.280.10;3.30.450.20;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
| null | null | null | null | null |
FUNCTION: Circadian regulator that acts as a transcription factor and generates a rhythmic output with a period of about 24 hours. Oscillates in antiphase to the cycling observed for period (PER) and timeless (TIM). According to PubMed:9742131, reaches peak abundance within several hours of the dark-light transition at ZT0 (zeitgeber 0), whereas PubMed:9616122 describes bimodal oscillating expression with maximum at ZT5 and ZT23. Clock-cycle heterodimers activate cycling transcription of PER and TIM by binding to the E-box (5'-CACGTG-3') present in their promoters. Once induced, Period and Timeless block Clock's ability to transactivate their promoters. {ECO:0000269|PubMed:9630223}.
|
Drosophila melanogaster (Fruit fly)
|
O61789
|
EGG5_CAEEL
|
MALNSEVMFREQINAMRSQAGRKRATSLQSFCSGNTDDSSADSTDNMDMMVDYPQQKGVSCMRARFNSESTLSKSFRKKVKKLAQKDRRSKERLNGNSEEDAIEVPRGAPSTYAAPSKLRKSKALDCLVSEKPKDEGRSEDSGHGADIEMAKGHFNDVRMKVFAARTAMQVEPALVMKTRKALEMKNAVLENHQSPGAFSLHAAYKIAASAESRVGSITPCNKKVTKEAMANLIRSSYDDTEITQELLFSSKFDSKWKGRYTDIYMRRDENGKKPKRPVNGQGWVMPLKSICEKFGINSTFFTNHRIDLKSARDQVLLMRLLSHDQTSTWISDIHPEAVKNETLAEYLLRELDASTMQKRVQAFKANVLADRDRVRVAGQFYNNIRIGKRMFGAARKAKYLSTIIGGMERRFEILENSVNHIPFTHSASDNNQEKCRNPRVHCRDSTRIALQFPRGQYLGDFIHANRISGKPLFNEFIMTQAPMKNTVDDFWRMVWQEEVPYIVMLTSRKEPERCEYYWPKSPSDPAVTVPGGLRIENFGVYQAPDPLFRVTHLRLIGPDREERHVEHWQGDVNNSSNMYSPLNILRLLRNASKPVVIHDHLGVSRAACLVAAEIAICSLLRGPTYKYPVQRAVQFLRQRRPFSIETPMQYIFVHRLVAFFFRDVIGSAKELDVDYERWLQERSERMFLDDLAAPIPGYRLLSPRADPDIVRMVGRPERPNYRREAPDCVGEMPNKVAAVDGILSPAKSVFEF
| null | null |
cortical actin cytoskeleton organization [GO:0030866]; dephosphorylation [GO:0016311]; eggshell formation [GO:0030703]; motor neuron axon guidance [GO:0008045]; oocyte maturation [GO:0001556]; polar body extrusion after meiotic divisions [GO:0040038]; positive regulation of protein localization to cell cortex [GO:1904778]
|
cell cortex [GO:0005938]; nucleus [GO:0005634]
|
protein kinase binding [GO:0019901]; protein tyrosine phosphatase activity [GO:0004725]
|
PF00102;
|
3.90.190.10;
|
Protein-tyrosine phosphatase family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000269|PubMed:19879147}. Note=Localizes to the cell cortex in developing oocytes and in newly fertilized embryos. {ECO:0000269|PubMed:19879147}.
| null | null | null | null | null |
FUNCTION: Inactive phosphatase which acts redundantly with egg-4 in the oocyte-to-zygote transition (PubMed:19879147, PubMed:19879842). Required for polarized cortical actin cytoskeleton rearrangement in the oocyte before and after fertilization (PubMed:19879147). Together with egg-4, required for the cortical localization of kinase mbk-2 in maturing oocyte until the end of meiosis I (PubMed:19879842). Also required for kinase mbk-2, pseudophosphatase egg-3 and chitin synthase chs-1 localization to cytoplasmic foci after fertilization (PubMed:19879147). {ECO:0000269|PubMed:19879147, ECO:0000269|PubMed:19879842}.
|
Caenorhabditis elegans
|
O61847
|
CDK2_CAEEL
|
MSREIRSLESIISDARENTHEKMLIRKQRDMTTDIAPERDLQGRFCSLRRIGEGTYGVVFKAIHVRDNVKCALKMIRTDRDEEGIPSTCLREISCIKDLQHDNIVTLFDIIYANSKLYMVFEFIDRDLKNLLEMLEPTNSVLPPNYVKSFMWQLLSALSYCHLRRIVHRDLKPQNILVSDSGVIKIADFGLARNFSFPSRNYTHEVVTLWYRPPEILLGSQRYSTSLDMWSLGCIFSEIASNKPLFPGECEISQLFKIFEIVGTPNIKSWPGVDSFPHYKAVFPQWPVNLKKLEETSCLTGNGLDVLREILRYPPERRLTAKGALSHRYFLQNGFTQNRPSVTDLMKDIRAQNRTPPLLNNHQEKSIF
|
2.7.11.22
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P24941}; Note=Binds 2 Mg(2+) ions. {ECO:0000250|UniProtKB:P24941};
|
cell division [GO:0051301]; embryo development ending in birth or egg hatching [GO:0009792]; G1/S transition of mitotic cell cycle [GO:0000082]; germline cell cycle switching, mitotic to meiotic cell cycle [GO:0051729]; meiotic cell cycle [GO:0051321]; nematode larval development [GO:0002119]; nuclear membrane disassembly [GO:0051081]; phosphorylation [GO:0016310]; positive regulation of G1/S transition of mitotic cell cycle [GO:1900087]; positive regulation of protein localization to centrosome [GO:1904781]; post-transcriptional regulation of gene expression [GO:0010608]; protein localization [GO:0008104]; pseudocleavage [GO:0030588]; regulation of G2/M transition of mitotic cell cycle [GO:0010389]; regulation of gene expression [GO:0010468]; regulation of meiotic cell cycle [GO:0051445]; regulation of protein localization to cell cortex [GO:1904776]; response to organic substance [GO:0010033]; signal transduction [GO:0007165]
|
chromatin [GO:0000785]; cyclin E1-CDK2 complex [GO:0097134]; cyclin-dependent protein kinase holoenzyme complex [GO:0000307]; cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; cyclin binding [GO:0030332]; cyclin-dependent protein serine/threonine kinase activity [GO:0004693]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, CMGC Ser/Thr protein kinase family, CDC2/CDKX 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=2.7.11.22; Evidence={ECO:0000250|UniProtKB:P24941}; 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=2.7.11.22; Evidence={ECO:0000250|UniProtKB:P24941};
| null | null | null | null |
FUNCTION: Serine/threonine-protein kinase which, in association with cye-1, regulates proliferation, quiescent state and cell fate during the development of several cell lineages (PubMed:17115027, PubMed:17476329). In the embryo, initiates the establishment of cell polarity through the recruitment of the centrosomal proteins spd-2 and spd-5 during prophase (PubMed:17115027). Phosphorylation and inhibition of the translational repressor gld-1 by the cdk-2/cye-1 complex regulates the pool of germline stem cells and the size of the mitotic zone in the gonads by preventing entry into meiosis (PubMed:21455289). {ECO:0000269|PubMed:17115027, ECO:0000269|PubMed:17476329, ECO:0000269|PubMed:21455289}.
|
Caenorhabditis elegans
|
O61866
|
LIPL5_CAEEL
|
MWRFAVFLAAFFVQDVVGSHGDPELHMTTPQIIERWGYPAMIYTVATDDGYILEMHRIPFGKTNVTWPNGKRPVVFMQHGLLCASSDWVVNLPDQSAGFLFADAGFDVWLGNMRGNTYSMKHKDLKPSHSAFWDWSWDEMATYDLNAMINHVLEVTGQDSVYYMGHSQGTLTMFSHLSKDDGSFAKKIKKFFALAPIGSVKHIKGFLSFFANYFSLEFDGWFDIFGAGEFLPNNWAMKLAAKDICGGLKVEADLCDNVLFLIAGPESDQWNQTRVPVYATHDPAGTSTQNIVHWMQMVHHGGVPAYDWGTKTNKKKYGQANPPEYDFTAIKGTKIYLYWSDADWLADTPDVPDYLLTRLNPAIVAQNNHLPDYNHLDFTWGLRAPDDIYRPAIKLCTDDYLGK
|
3.1.1.-
| null |
defense response to Gram-negative bacterium [GO:0050829]; lipid homeostasis [GO:0055088]; lipid metabolic process [GO:0006629]; triglyceride catabolic process [GO:0019433]
|
extracellular region [GO:0005576]; lysosomal lumen [GO:0043202]; lysosome [GO:0005764]
|
hydrolase activity, acting on ester bonds [GO:0016788]
|
PF04083;
|
3.40.50.1820;
|
AB hydrolase superfamily, Lipase family
| null |
SUBCELLULAR LOCATION: Lysosome lumen {ECO:0000269|PubMed:31340142}. Secreted {ECO:0000269|PubMed:31340142}. Note=Localizes to lysosomes in coelomocytes. {ECO:0000269|PubMed:31340142}.
| null | null | null | null | null |
FUNCTION: Lipase involved in lipid homeostasis (PubMed:31676440). Regulates mitochondrial lipid composition, in particular cardiolipins and coenzyme Q-9 levels, in response to nutrient availability (PubMed:31676440). Does not affect global triglyceride levels in response to nutrient availability (PubMed:31676440). However, in coelomocytes, specifically promotes triglyceride catabolism and lifespan extension in response to nutrient deprivation (PubMed:31340142). {ECO:0000269|PubMed:31340142, ECO:0000269|PubMed:31676440}.
|
Caenorhabditis elegans
|
O61931
|
ERGO1_CAEEL
|
MSYNNGGGGGGGGYRNDRDDRYHNNDRQNYRSSDQGRSGYNDDRRDNRYDDRRGSNNDRGCYDQHDRRGSSNDDRRGYRGYNQGGGGYQQQYSQDARYGSNQRNDNYGNNRGSHGGANMYSQNGGNRGGGGGRVGGGRTAAGMSNPGDLVGGADQPIHSVSKKSLRHNAQEFAVRPKTMVQDKGLGQKTTLLTNHTLVQLPQEPITLHVFNIEVFINGKSSNKRELCGPRFWEILKENKPTFGMPNQYIFNDVNMMWSTNKLRQSEGRTNNRRMNFVWKYVKQIKFGGNIEDEETMQLLSTLIDAIATQRARLPLAPPKYTVFKRLTYLICEEAYEPELPDVSLCHKLRIGTDARVGVSIAIRTNLRAGITACFDLGHTLFTRPAYPLVRLLCDIIEHSVVLDEAFEMKYDAALRACNVSDENLRVMTQILTKMTLQLSTETGDYVGEDGEVIVRPAPTIRNPGRNFKFVGLGAPADRYYFTSDGVELTVADYYLQKYNIRLRYPNLPCVLKKAPEQCGNKHSAMPLELVSYIVVPTRYGGFTMPDMRADMINKTTYTAQQRGKLLQHIIAQKSLSGIEPPVSNNDDYMKKHKLVMKREPIRVKATILPPPTLVYGDSVFHDEHHIGEWEAVTHDPPRQVLDGAVFRRKLYKSSEQPLMKRLMGSILLIQSPRQCRDFDYNQQGYHAIMRAIEDSGQPVLWADENKHSAVIQGELQFNQNQHGIEVIEQFLQNIKSTIGEYERDGEVIVPIVFAVFQARATVYSGNNNEYNDYNVLKYLADNKYGIHTQGILEKSLGVVGPSPKNCALTRLMVEKVLGKVGTTHRKLERGGAHKTWTIFTDPAKPTLVLGIDVSHPSTRDRETGNVLQKMSAATVVGNIDLDVTEFRASSRIQDTGVECLIDFSKEIDERIGEFIDHTGKRPAHIVVYRDGLSEGDFQKYLFEERVCIEERCLKIDTSFQPSITYIVVTKRHHTQFFLEDPSQGYESQGYNVLPGTLIEDAVTTNKYYDFFLSTQIGNEGCFRPTHYYVLHDTWTGKPDSFWPTVTHALTYNFCRSTTTVALPAPVLYAHLAAKRAKETLDGINTYKSVNNIYCDLESFGDLCEVNKDMNVNEKLEGMTFV
| null | null |
regulation of translation [GO:0006417]; regulatory ncRNA-mediated post-transcriptional gene silencing [GO:0035194]; siRNA processing [GO:0030422]
|
cytoplasm [GO:0005737]; cytoplasmic ribonucleoprotein granule [GO:0036464]; nucleus [GO:0005634]; RISC complex [GO:0016442]
|
DEAD/H-box RNA helicase binding [GO:0017151]; miRNA binding [GO:0035198]; RNA endonuclease activity [GO:0004521]; single-stranded RNA binding [GO:0003727]; siRNA binding [GO:0035197]
|
PF02170;PF02171;
|
2.170.260.10;3.30.420.10;
|
Argonaute family, Piwi subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22548001}.
| null | null | null | null | null |
FUNCTION: Argonaute protein required for gene silencing in the endogenous RNA interference (RNAi) pathway (PubMed:17110334, PubMed:20133583). Involved in the 26G RNAi pathway and associates with both unmethylated and methylated 26G small interfering RNAs (26G-siRNAs), which are a class of 26 nucleotide siRNAs that possess a guanine residue at the 5'-end (PubMed:22102828, PubMed:22548001). Associated 26G-siRNAs are methylated by the methyltransferase henn-1, which stabilizes the siRNAs (PubMed:22548001). Association with 26G-siRNAs is required for the biogenesis of secondary 22G-siRNAs (a class of 22 nucleotide siRNAs that possess a triphosphorylated guanine residue at the 5'-end) (PubMed:22102828). May be involved in passenger strand cleavage of target 26G-siRNAs (PubMed:22102828). {ECO:0000269|PubMed:17110334, ECO:0000269|PubMed:20133583, ECO:0000269|PubMed:22102828, ECO:0000269|PubMed:22548001}.
|
Caenorhabditis elegans
|
O61955
|
IF4E3_CAEEL
|
MSTSVAENKALSASGDVNASDASVPPELLTRHPLQNRWALWYLKADRNKEWEDCLKMVSLFDTVEDFWSLYNHIQSAGGLNWGSDYYLFKEGIKPMWEDVNNVQGGRWLVVVDKQKLQRRTQLLDHYWLELLMAIVGEQFDEYGDYICGAVVNVRQKGDKVSLWTRDATRDDVNLRIGQVLKQKLSIPDTEILRYEVHKDSSARTSSTVKPRICLPAKDPAPVKEKGPAATTSPSNPGTEATGTSPATPTP
| null | null |
21U-RNA metabolic process [GO:0034585]; embryo development ending in birth or egg hatching [GO:0009792]; piRNA processing [GO:0034587]; translational initiation [GO:0006413]
|
eukaryotic translation initiation factor 4F complex [GO:0016281]; perinuclear region of cytoplasm [GO:0048471]; RNA cap binding complex [GO:0034518]; translation initiation complex [GO:0070992]
|
RNA 7-methylguanosine cap binding [GO:0000340]; translation initiation factor activity [GO:0003743]
|
PF01652;
|
3.30.760.10;
|
Eukaryotic initiation factor 4E family
| null |
SUBCELLULAR LOCATION: Cytoplasmic granule {ECO:0000269|PubMed:31147388}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:31147388, ECO:0000269|PubMed:31216475}. Note=Localizes to cytoplasmic granules in early embryos (PubMed:31147388). Localizes to puncta in the perinuclear region in the germline syncytium (PubMed:31147388, PubMed:31216475). {ECO:0000269|PubMed:31147388, ECO:0000269|PubMed:31216475}.
| null | null | null | null | null |
FUNCTION: Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures. All 5 eIF4E proteins bind monomethyl cap structures. Only ife-1, ife-2 and ife-5 bind trimethyl cap structures which result from trans-splicing. Translation of trimethyl cap structure mRNAs may be regulated by intracellular redox state; disulfide bonds change the width and depth of the cap-binding cavity determining selectivity to mRNA caps. Ife-3 is essential for viability. Component of the pid-1 and tost-1 variants of the PETISCO complexes, which have roles in the biogenesis of a class of 21 nucleotide PIWI-interacting RNAs (piRNAs) that possess a uracil residue at the 5'-end (also called 21U-RNAs) and embryogenesis, respectively (PubMed:31147388, PubMed:31216475). Within the pid-1 variant of the PETISCO complex binds to capped 21U-RNA precursor molecules, possibly playing a role in the processing of the 5' end of the molecules to promote binding of other complex components such as pid-3 (PubMed:31147388). However, it is not essential for the biogenesis of 21U-RNAs by itself (PubMed:31147388). Within the tost-1 variant of the PETISCO complex binds to splice leader SL1 RNA fragments to possibly play a role in their processing (PubMed:31147388). {ECO:0000269|PubMed:10744754, ECO:0000269|PubMed:12422237, ECO:0000269|PubMed:31147388, ECO:0000269|PubMed:9553113, ECO:0000305|PubMed:31216475}.
|
Caenorhabditis elegans
|
O61967
|
LAP1_CAEEL
|
MPAFFCLPMACQRQVDSIDRSQSNLQAIPSDIFRFRKLEDLNLTMNNIKELDHRLFSLRHLRILDVSDNELAVLPAEIGNLTQLIELNLNRNSIAKLPDTMQNCKLLTTLNLSSNPFTRLPETICECSSITILSLNETSLTLLPSNIGSLTNLRVLEARDNLLRTIPLSIVELRKLEELDLGQNELEALPAEIGKLTSLREFYVDINSLTSLPDSISGCRMLDQLDVSENQIIRLPENLGRMPNLTDLNISINEIIELPSSFGELKRLQMLKADRNSLHNLTSEIGKCQSLTELYLGQNFLTDLPDTIGDLRQLTTLNVDCNNLSDIPDTIGNCKSLTVLSLRQNILTELPMTIGKCENLTVLDVASNKLPHLPFTVKVLYKLQALWLSENQTQSILKLSETRDDRKGIKVVTCYLLPQVDAIDGEGRSGSAQHNTDRGAFLGGPKVHFHDQADTTFEENKEAEIHLGNFERHNTPHPKTPKHKKGSIDGHMLPHEIDQPRQLSLVSNHRTSTSSFGESSNSINRDLADIRAQNGVREATLSPEREERMATSLSSLSNLAAGTQNMHTIRIQKDDTGKLGLSFAGGTSNDPAPNSNGDSGLFVTKVTPGSAAYRCGLREGDKLIRANDVNMINASQDNAMEAIKKRETVELVVLRRSPSPVSRTSEPSLNGSSHQLNHFDAGSPDSTMFVTSSTPVYAS
| null | null |
actin filament-based process [GO:0030029]; adherens junction assembly [GO:0034333]; cell-cell adhesion [GO:0098609]; cell-cell junction assembly [GO:0007043]; chemical synaptic transmission [GO:0007268]; embryo development ending in birth or egg hatching [GO:0009792]; embryonic digestive tract morphogenesis [GO:0048557]; establishment or maintenance of cell polarity [GO:0007163]; maintenance of epithelial cell apical/basal polarity [GO:0045199]; protein transport [GO:0015031]; receptor clustering [GO:0043113]; receptor localization to synapse [GO:0097120]; regulation of intermediate filament polymerization or depolymerization [GO:0045108]
|
basolateral plasma membrane [GO:0016323]; neuromuscular junction [GO:0031594]; neuron projection [GO:0043005]; postsynaptic density membrane [GO:0098839]
| null |
PF13855;PF00595;
|
2.30.42.10;3.80.10.10;
|
LAP (LRR and PDZ) protein family
| null |
SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000269|PubMed:10878806, ECO:0000269|PubMed:14578922, ECO:0000269|PubMed:27506200}; Peripheral membrane protein {ECO:0000269|PubMed:10878806, ECO:0000269|PubMed:14578922}. Note=Basolateral membrane of epithelial cells. {ECO:0000269|PubMed:10878806, ECO:0000269|PubMed:14578922}.
| null | null | null | null | null |
FUNCTION: Critical role in assembling adherens junctions; adapter protein involved in polarizing protein trafficking in epithelial cells. Necessary to maintain, not establish, the entire terminal web (organelle-depleted, intermediate filament-rich layer of cytoplasm that underlies the apical microvilli of polarized epithelial cells) or brush border assembly at the apical surface gut cells. Required for correct localization of ifb-2 intermediate filaments in the terminal web. Required for dlg-1 lateral localization (PubMed:18411252). With dlg-1, cooperatively regulates ajm-1 localization to apical junctions (PubMed:11715019). {ECO:0000269|PubMed:10878806, ECO:0000269|PubMed:11715019, ECO:0000269|PubMed:15063180, ECO:0000269|PubMed:18411252}.
|
Caenorhabditis elegans
|
O62090
|
PRY1_CAEEL
|
METHLGWARSLEAVLSDRSALDAFQEWLIEYSSPQYLDLFFAIRAYERMALEGKPEKSQLSKSIYSKFLSSRTGNCEAIPKHFRAPIGEKLRHGTELEDRVFSHCSNFVQEFLRRQHEEFVGSEEFIEAFNKMSSTTADQLPGGSAHHSSHQNTMRRSSGTTSRKSAAQIATQLTAEALLKSKHDRHSKLGETKLEKMYPPTRQPYVCNATTSHNDSAVSSTFSGDTPEAHRMHSNRLRHIRDEQARENHGTMTLPRVEKASVDGQQWDHSSESGRRNFAMEITRKLLRHIDKVKLNDEMEKRIDDIEECRYTTIDMVNGTEPNDDLGKIDEDEELDDYLKMKMTDDSQKGSTNRSPKGPAGEPNKSGEGSKNTTLSPTNRAPAQLHNTIRVPRRKDYPRDTSASLKSHRHHQIDTNRMMSQSMCAPSYSSASSSYSRDSFAPAPTTRVNFAPGSSKSSQFYDSSGIGSMAPSAFSATSSLDYKDRRQHRKAPTPKKHSKIGKNLSNLITISYLGTDKIPVVTHVPNDGPMTLAEFKRHFALPNGAHQLFFKTECEDGSAPFQLLLIKDEHHLLPVFEGRIAAELR
| null | null |
anterior/posterior axis specification [GO:0009948]; anterior/posterior pattern specification [GO:0009952]; axon guidance [GO:0007411]; canonical Wnt signaling pathway [GO:0060070]; cell development [GO:0048468]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of vulval development [GO:0040027]; negative regulation of Wnt signaling pathway [GO:0030178]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; regulation of cell fate specification [GO:0042659]; regulation of protein localization [GO:0032880]
|
beta-catenin destruction complex [GO:0030877]; cell cortex [GO:0005938]; cytoplasm [GO:0005737]; membrane [GO:0016020]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
beta-catenin binding [GO:0008013]; I-SMAD binding [GO:0070411]; molecular adaptor activity [GO:0060090]; protein kinase binding [GO:0019901]; ubiquitin protein ligase binding [GO:0031625]
|
PF00778;PF00615;
|
2.40.240.130;1.10.167.10;
| null | null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12023307, ECO:0000269|PubMed:16077004}. Nucleus {ECO:0000269|PubMed:12023307, ECO:0000269|PubMed:16077004}. Cytoplasm, cell cortex {ECO:0000269|PubMed:12023307, ECO:0000269|PubMed:16077004}. Note=Subcellular location was measured using a GFP reporter gene. Location of the pry-1:GFP fusion protein ranges from plasma membrane and cytoplasmic dots to diffuse cytoplasmic and nuclear staining. This difference may be due to variations in expression levels of the fusion protein in different transgenic lines. {ECO:0000269|PubMed:12023307, ECO:0000269|PubMed:16077004}.
| null | null | null | null | null |
FUNCTION: Works in parallel with axl-1 in negatively regulating bar-1 signaling in vulval precursor cells and Q neuroblasts. Inhibits Wnt signaling, which affects tissue specific expression of Hox genes, egl-5, lin-39 and mab-5. This in turn affects QR (postembryonic neuroblast) cell migration, vulval cell fate specification, and the development of sensory structures by the seam cell lineage. Has a role in alae V cell patterning, ray formation in the male tail and axon guidance. Does not affect B cell polarity. {ECO:0000269|PubMed:12023307, ECO:0000269|PubMed:16077004, ECO:0000269|PubMed:16631156, ECO:0000269|PubMed:17213328, ECO:0000269|PubMed:17276345, ECO:0000269|PubMed:17601533, ECO:0000269|PubMed:9834184}.
|
Caenorhabditis elegans
|
O62137
|
ACX12_CAEEL
|
MANRSIRDGDNPELLEERRMATFDTDKMAAVIYGSEEFARRRREITDAVSKIPELADIKPYPFLTREEKVTEGTRKISILTKYLNQLIDRDNEEESLHLHREVIGYEGHPFALHDALFIPTLQSQASDEQQEKWLERARRREIIGCYAQTELGHGSNLRNLETTAVYDIASQEFVLHTPTTTALKWWPGALGKSCNYALVVAELIIKRNNYGPHFFMVQLRDEKTHIPLKGVTVGDIGPKMNFNAADNGYLGLNNLRVPRTNLLMRHCKVEADGTYVKPPHAKIGYSGMVKIRSQMAMEQGLFLAHALTIAARYSAVRRQGHLDDKQVEVKVLDYQTQQHRLFPSLARAYAFIFTGFETIHLYSQLLKDVDMGNTSGMADLHALTSGLKSVVAHETGEGIEQARMACGGHGYSMASYISVVYGIAIGGCTYEGENMVMLLQLARYLVKSVELIKAGKAKKLGPVASYLADKSDETDLTSLNGYVKMFENMARRQAWKATEKFLKLMESGESREVAWNKSAVELTRASRLHTRLFIIEAFMRRVSRIEDIPVKEVLTDLLHLHVNYELLDVATYALEFMSFTQLDYVRDQLYLYLEKIRPNAVSLVDSFQISDMQLRSVLGRRDGHVYENLFKWAKSSPLNNADVLPSVEKYLKPMMEKAKL
|
1.3.3.-
|
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:27551084};
|
ascaroside biosynthetic process [GO:1904070]; fatty acid beta-oxidation using acyl-CoA oxidase [GO:0033540]; lipid homeostasis [GO:0055088]; long-chain fatty acid metabolic process [GO:0001676]; very long-chain fatty acid metabolic process [GO:0000038]
|
peroxisome [GO:0005777]
|
acyl-CoA oxidase activity [GO:0003997]; ATP binding [GO:0005524]; FAD binding [GO:0071949]; fatty acid binding [GO:0005504]; flavin adenine dinucleotide binding [GO:0050660]; palmitoyl-CoA oxidase activity [GO:0016401]
|
PF01756;PF14749;
|
1.10.540.10;2.40.110.10;1.20.140.10;
|
Acyl-CoA oxidase family
| null |
SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:O62140}.
|
CATALYTIC ACTIVITY: Reaction=asc-omegaC5-CoA + O2 = asc-omegaDeltaC5-CoA + H2O2; Xref=Rhea:RHEA:66212, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:140060, ChEBI:CHEBI:166969; Evidence={ECO:0000269|PubMed:25775534, ECO:0000269|PubMed:27551084};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=175 uM for asc-omega-C5-CoA (at 30 degrees Celsius and pH 7.4) {ECO:0000269|PubMed:25775534}; KM=152 uM for asc-omega-C5-CoA (at 30 degrees Celsius, pH 7.4 and in complex with acox-1.1) {ECO:0000269|PubMed:25775534}; Note=kcat is 364 sec(-1) with asc-omega-C5-CoA (at 30 degrees Celsius and pH 7.4) (PubMed:25775534). kcat is 478 sec(-1) with asc-omega-C5-CoA (at 30 degrees Celsius, pH 7.4 and in complex with acox-1.1) (PubMed:25775534). {ECO:0000269|PubMed:25775534};
|
PATHWAY: Lipid metabolism; peroxisomal fatty acid beta-oxidation. {ECO:0000269|PubMed:25775534, ECO:0000269|PubMed:27551084}.
| null | null |
FUNCTION: Involved in the first step of peroxisomal beta-oxidation by catalyzing the desaturation of fatty acid-derived side chains of ascaroside pheromones, which regulates development and behavior (PubMed:25775534, PubMed:27551084). Specifically, shortens ascarosides with 5-carbon omega side chain (asc-omega-C5) (PubMed:25775534, PubMed:27551084). Does not shorten indol-3-carbonyl(IC)-ascaroside with 7-carbon or 9-carbon side chains (PubMed:29863473). Does not catalyze the desaturation of fatty acids or hydroxylated fatty acids (PubMed:25775534, PubMed:27551084). {ECO:0000269|PubMed:25775534, ECO:0000269|PubMed:27551084, ECO:0000269|PubMed:29863473}.
|
Caenorhabditis elegans
|
O62138
|
ACX13_CAEEL
|
MSSICKGDNSDLTEERKNATFDTDKMAAVIYGREEIASRRRQLTESISRIHELAESKPLVFMTREEKIAESCRKLEVLSRHWNQTPFNRDNEEDALHIYREVLGMEGHPLALHDTMFIPTLVAQASQEQQEKWLGRARRKEIIGCYAQTEMGHGTNLRKLETTATYSPDTQEFILNTPTITALKWWPGALGKSSNNAIVVANLLIKDQNYGPHPFMVQLRDEKTHIPLKGIVVGDIGPKMAFNGADNGYLGFNNHRIPRTNLLMRHTKVEANGTYIKPSHAKIGYSSMVKVRSRMAMDQGLFLASALVIAVRYSAVRRQGFLEDKTQKVKVLDYQTQQHRLFPSLARAYAFIFTGFETIHLYSQLLKDVDMGNTSGMADLHALTSGLKSVVTHQTGEGIEQARMACGEHGYSMASYISEIYGVAIGGCTYEGENMVMLLQLARYLVKSVELIKSGEEKKLGPMVSYLAAKGGHPDLSSLNGYVTAFEHMARRQAWKATEKFLKLMETGESREVAWNKSAVELTRASRLHTRLFIIEAFMRRVSRIEDIPVKEVLTDLLHLHVNYELLDVATYALEFMSSTQLDYIRDQLYLYLEKIRPSAVSLVDSFQISDMQLRSVLGRRDGNVYENLFKWAKSSPLNKSDVLPSVDKYLKPMMEKAKL
|
1.3.3.-
|
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:O62137};
|
ascaroside biosynthetic process [GO:1904070]; fatty acid beta-oxidation using acyl-CoA oxidase [GO:0033540]; lipid homeostasis [GO:0055088]; long-chain fatty acid metabolic process [GO:0001676]; pheromone biosynthetic process [GO:0042811]; very long-chain fatty acid metabolic process [GO:0000038]
|
peroxisome [GO:0005777]
|
acyl-CoA oxidase activity [GO:0003997]; ATP binding [GO:0005524]; FAD binding [GO:0071949]; fatty acid binding [GO:0005504]; flavin adenine dinucleotide binding [GO:0050660]; palmitoyl-CoA oxidase activity [GO:0016401]
|
PF01756;PF14749;
|
1.10.540.10;2.40.110.10;1.20.140.10;
|
Acyl-CoA oxidase family
| null |
SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:O62140}.
|
CATALYTIC ACTIVITY: Reaction=asc-C7-CoA + O2 = asc-DeltaC7-CoA + H2O2; Xref=Rhea:RHEA:66216, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:139646, ChEBI:CHEBI:139712; Evidence={ECO:0000269|PubMed:25775534};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=60 uM for asc-C7-CoA (at 30 degrees Celsius, pH 7.4 and in complex with acox-1.1) {ECO:0000269|PubMed:25775534}; Note=kcat is 144 sec(-1) with asc-C7-CoA (at 30 degrees Celsius, pH 7.4 and in complex with acox-1.1). {ECO:0000269|PubMed:25775534};
|
PATHWAY: Lipid metabolism; peroxisomal fatty acid beta-oxidation. {ECO:0000269|PubMed:25775534}.
| null | null |
FUNCTION: Involved in the first step of peroxisomal beta-oxidation by catalyzing the desaturation of fatty acid-derived side chains of ascaroside pheromones, which regulates development and behavior (PubMed:20610393, PubMed:25775534, PubMed:29537254). Specifically, shortens ascarosides with a 7-carbon side chain (asc-C7) (PubMed:25775534, PubMed:29537254). Does not catalyze the desaturation of fatty acids or hydroxylated fatty acids (PubMed:25775534, PubMed:29537254). Involved in the biosynthesis of asc-C6-MK (daumone 2) and asc-delta-C9 (daumone 3) but not asc-C7 (daumone 1); daumones are pheromones produced during unfavourable growth conditions which promote entry into the dauer stage (PubMed:20610393). {ECO:0000269|PubMed:20610393, ECO:0000269|PubMed:25775534, ECO:0000269|PubMed:29537254}.
|
Caenorhabditis elegans
|
O62139
|
ACX14_CAEEL
|
MHLNTSICEVDNPDLTEEREKGTFDTDKMAAVIYGSEKLARRRREISEAVSKIPELADTQPFPFMDRLEKITEGSRKLEVLNNNIRDIIDYDDNGERLHIYQEVTGMEGHPLALHEVMFIPALVSQASKEQQEKWLGRARRREIIGCYAQTEMGHGTNLRKLETTATYFPDTQEFVLNTPTTTALKWWPGALGKSSNYAVVVVDMIIKGKSYGPHPFMVQLRDEKTHIPLKGIVVGDIGPKMSFNGGDNGFLGFDKFRVPRTNLLMRHVRVEADGTYVKPPHAKVNHSAMVHVRSHMATGQGALLAQALIIAVRYSAVRRQGFLENKTQEVKVLDYQTQQHRLFPSLARAYAFIFTGFETIHLYSQLLKDVDMGNTSGMADLHALTSGLKSVVTHQTGEGIEQARMACGGHGYSMASYISEIYGIAIGGCTYEGENMVMLLQLARYLVKSVELIKSGEAKKLGPMVSYLAAKGGHPDLSSLNGYVTAFEHMARRQAWKATEKFLKLMESGESREIAWNKSTVELTRASRLHTRLFIIEAFMRRVSRIEDIPVKEVLTDLLHLHVNYELLDVATYALEFMSSTQLDYIRDQLYLYLEKIRPSAVSLVDSFQISDMQLRSVLGRRDGNVYENLFKWAKSSPLNKSDVLPSVDKYLMPMMEKAKL
|
1.3.3.-
|
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:O62140};
|
ascaroside biosynthetic process [GO:1904070]; fatty acid beta-oxidation using acyl-CoA oxidase [GO:0033540]; lipid homeostasis [GO:0055088]; long-chain fatty acid metabolic process [GO:0001676]; pheromone biosynthetic process [GO:0042811]; very long-chain fatty acid metabolic process [GO:0000038]
|
peroxisome [GO:0005777]
|
acyl-CoA oxidase activity [GO:0003997]; ATP binding [GO:0005524]; FAD binding [GO:0071949]; fatty acid binding [GO:0005504]; flavin adenine dinucleotide binding [GO:0050660]; palmitoyl-CoA oxidase activity [GO:0016401]
|
PF01756;PF14749;
|
1.10.540.10;2.40.110.10;1.20.140.10;
|
Acyl-CoA oxidase family
| null |
SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:O62140}.
|
CATALYTIC ACTIVITY: Reaction=asc-C9-CoA + O2 = asc-DeltaC9-CoA + H2O2; Xref=Rhea:RHEA:66224, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:139617, ChEBI:CHEBI:139706; Evidence={ECO:0000305|PubMed:29537254, ECO:0000305|PubMed:29863473};
| null |
PATHWAY: Lipid metabolism; peroxisomal fatty acid beta-oxidation. {ECO:0000269|PubMed:29537254}.
| null | null |
FUNCTION: Involved in the first step of peroxisomal beta-oxidation by catalyzing the desaturation of fatty acid-derived side chains of ascaroside pheromones, which regulates development and behavior (PubMed:29537254, PubMed:29863473). Specifically, shortens ascarosides with a 9-carbon side chain (asc-C9) and, in association with acox-1.1, may contribute to the shortening of ascarosides with a 11-carbon side chain (asc-C11) (PubMed:29537254, PubMed:29863473). May contribute to the production of indol-3-carbonyl(IC)-ascarosides in association with acox-1.1 and acox-3 (PubMed:29863473). {ECO:0000269|PubMed:29537254, ECO:0000269|PubMed:29863473}.
|
Caenorhabditis elegans
|
O62140
|
ACX11_CAEEL
|
MVHLNKTIQEGDNPDLTAERLTATFDTHAMAAQIYGGEMRARRRREITAKLAEIPELHDSMPLPYMTREEKIMESARKLTVLTQRMSEIIDPTDAGELYHLNNEVLGIEGNPMALHGVMFIPALNAQASDEQQAKWLIRALRREIIGTYAQTEMGHGTNLQNLETTATYDIGTQEFVLHTPKITALKWWPGNLGKSSNYAVVVAHMYIKGKNFGPHTFMVPLRDEKTHKPLPGITIGDIGPKMAYNIVDNGFLGFNNYRIPRTNLLMRHTKVEADGTYIKPPHAKINYSAMVHVRSYMLTGQAIMLSYALNIATRYSAVRRQGQIDKNEPEVKVLEYQTQQHRLFPFIARAYAFQFAGAETVKLYERVLKEMKSGNVSLMADLHALTSGLKSVVTHQTGEGIEQARMACGGHGYSMASYISEIYGVAIGGCTYEGENMVMLLQLARYLVKSAALVKSGKASQLGPLVAYLGARSEPTSLIDRVPNGGITEYIKTFQHIAKRQTLKAANKFFGLMENGEKREIAWNKSSVELNRASRLHTRLFIVEAFARRVNEIGDITIKEALSDLLHLHVNYELLDVATYALEDGFMSSTQLDYVRDQLYFYLQKIRPNAVSLLDSWEFSDRELRSVLGRRDGHVYENLFKWAKESPLNKTDVLPSVDTYLKPMMEKARQSKL
|
1.3.3.-; 1.3.3.6
|
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:27551084};
|
ascaroside biosynthetic process [GO:1904070]; fatty acid beta-oxidation using acyl-CoA oxidase [GO:0033540]; lipid homeostasis [GO:0055088]; pheromone biosynthetic process [GO:0042811]
|
peroxisomal matrix [GO:0005782]; peroxisome [GO:0005777]
|
acyl-CoA oxidase activity [GO:0003997]; ATP binding [GO:0005524]; FAD binding [GO:0071949]; fatty acid binding [GO:0005504]; flavin adenine dinucleotide binding [GO:0050660]
|
PF01756;PF14749;
|
1.10.540.10;2.40.110.10;1.20.140.10;
|
Acyl-CoA oxidase family
| null |
SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:20610393, ECO:0000269|PubMed:29537254, ECO:0000269|PubMed:29863473}.
|
CATALYTIC ACTIVITY: Reaction=nonanoyl-CoA + O2 = (2E)-nonenoyl-CoA + H2O2; Xref=Rhea:RHEA:38987, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:76291, ChEBI:CHEBI:76292; Evidence={ECO:0000269|PubMed:25775534, ECO:0000269|PubMed:29537254, ECO:0000269|PubMed:29863473}; CATALYTIC ACTIVITY: Reaction=dodecanoyl-CoA + O2 = (2E)-dodecenoyl-CoA + H2O2; Xref=Rhea:RHEA:40171, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:57330, ChEBI:CHEBI:57375; Evidence={ECO:0000269|PubMed:27551084, ECO:0000269|PubMed:29537254, ECO:0000269|PubMed:29863473}; CATALYTIC ACTIVITY: Reaction=a 2,3-saturated acyl-CoA + O2 = a (2E)-enoyl-CoA + H2O2; Xref=Rhea:RHEA:38959, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:58856, ChEBI:CHEBI:65111; EC=1.3.3.6; Evidence={ECO:0000269|PubMed:25775534, ECO:0000269|PubMed:27551084, ECO:0000269|PubMed:29537254, ECO:0000269|PubMed:29863473}; CATALYTIC ACTIVITY: Reaction=heptanoyl-CoA + O2 = (2E)-heptenoyl-CoA + H2O2; Xref=Rhea:RHEA:66204, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:78811, ChEBI:CHEBI:166980; Evidence={ECO:0000269|PubMed:25775534, ECO:0000269|PubMed:27551084}; CATALYTIC ACTIVITY: Reaction=(8R)-8-hydroxynonanoyl-CoA + O2 = (2E,8R)-8-hydroxynonenoyl-CoA + H2O2; Xref=Rhea:RHEA:66208, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:166978, ChEBI:CHEBI:166979; Evidence={ECO:0000269|PubMed:25775534}; CATALYTIC ACTIVITY: Reaction=O2 + pentanoyl-CoA = (2E)-pentenoyl-CoA + H2O2; Xref=Rhea:RHEA:66200, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:57389, ChEBI:CHEBI:86160; Evidence={ECO:0000269|PubMed:25775534, ECO:0000269|PubMed:27551084}; CATALYTIC ACTIVITY: Reaction=hexadecanoyl-CoA + O2 = (2E)-hexadecenoyl-CoA + H2O2; Xref=Rhea:RHEA:40167, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:57379, ChEBI:CHEBI:61526; Evidence={ECO:0000269|PubMed:27551084}; CATALYTIC ACTIVITY: Reaction=IC-asc-C7-CoA + O2 = H2O2 + IC-asc-DeltaC7-CoA; Xref=Rhea:RHEA:66232, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:166976, ChEBI:CHEBI:166977; Evidence={ECO:0000269|PubMed:29863473}; CATALYTIC ACTIVITY: Reaction=IC-asc-C9-CoA + O2 = H2O2 + IC-asc-DeltaC9-CoA; Xref=Rhea:RHEA:66236, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:166973, ChEBI:CHEBI:166974; Evidence={ECO:0000269|PubMed:29863473}; CATALYTIC ACTIVITY: Reaction=asc-omegaC5-CoA + O2 = asc-omegaDeltaC5-CoA + H2O2; Xref=Rhea:RHEA:66212, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:140060, ChEBI:CHEBI:166969; Evidence={ECO:0000269|PubMed:25775534}; CATALYTIC ACTIVITY: Reaction=asc-C7-CoA + O2 = asc-DeltaC7-CoA + H2O2; Xref=Rhea:RHEA:66216, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:139646, ChEBI:CHEBI:139712; Evidence={ECO:0000269|PubMed:25775534, ECO:0000269|PubMed:27551084}; CATALYTIC ACTIVITY: Reaction=asc-omegaC7-CoA + O2 = asc-omegaDeltaC7-CoA + H2O2; Xref=Rhea:RHEA:66220, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:139994, ChEBI:CHEBI:140057; Evidence={ECO:0000269|PubMed:27551084}; CATALYTIC ACTIVITY: Reaction=asc-C9-CoA + O2 = asc-DeltaC9-CoA + H2O2; Xref=Rhea:RHEA:66224, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:139617, ChEBI:CHEBI:139706; Evidence={ECO:0000269|PubMed:25775534, ECO:0000269|PubMed:27551084, ECO:0000269|PubMed:29863473}; CATALYTIC ACTIVITY: Reaction=asc-C13-CoA + O2 = asc-DeltaC13-CoA + H2O2; Xref=Rhea:RHEA:66228, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:139652, ChEBI:CHEBI:139655; Evidence={ECO:0000269|PubMed:29863473};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=42.7 uM for asc-C9-CoA (at 30 degrees Celsius and pH 7.4) {ECO:0000269|PubMed:25775534}; KM=60 uM for asc-C7-CoA (at 30 degrees Celsius, pH 7.4 and in complex with acox-1.3) {ECO:0000269|PubMed:25775534}; KM=152 uM for asc-omega-C5-CoA (at 30 degrees Celsius, pH 7.4 and in complex with acox-1.2) {ECO:0000269|PubMed:25775534}; Note=kcat is 252 sec(-1) with asc-C9-CoA (at 30 degrees Celsius and pH 7.4) (PubMed:25775534). kcat is 144 sec(-1) with asc-C7-CoA (at 30 degrees Celsius, pH 7.4 and in complex with acox-1.3) (PubMed:25775534). kcat is 478 sec(-1) with asc-omega-C5-CoA (at 30 degrees Celsius, pH 7.4 and in complex with acox-1.2) (PubMed:25775534). {ECO:0000269|PubMed:25775534};
|
PATHWAY: Lipid metabolism; peroxisomal fatty acid beta-oxidation. {ECO:0000269|PubMed:25775534, ECO:0000269|PubMed:27551084, ECO:0000269|PubMed:29537254}.
| null | null |
FUNCTION: Involved in the first step of peroxisomal beta-oxidation by catalyzing the desaturation of fatty acid-derived side chains (PubMed:25775534, PubMed:27551084, PubMed:29537254). Specifically, catalyzes the desaturation of fatty acids heptanoyl-CoA (C7), nonanoyl-CoA (C9), dodecanoyl-CoA (C12) and to a lesser extent pentanoyl-CoA (C5) and hexadecanoyl-CoA (C16), and hydroxylated fatty acid hydroxynonanoyl-CoA (PubMed:25775534, PubMed:27551084, PubMed:29537254). Also, catalyzes the desaturation fatty acid-derived side chains of ascaroside pheromones, which regulates development and behavior (PubMed:20610393, PubMed:25775534, PubMed:27551084, PubMed:29537254, PubMed:29863473). Specifically, shortens ascaroside with 5-carbon omega side chain (asc-omega-C5), 7-carbon side chain (asc-C7), 9-carbon side chain (asc-C9), 11-carbon side chain (asc-C11), 13-carbon side chain (asc-C13), 15-carbon side chain (asc-C15) and to a lesser extent ascarosides with 7-omega-carbon side chain (asc-omega-C7) (PubMed:25775534, PubMed:27551084, PubMed:29537254). Also shortens indol-3-carbonyl(IC)-ascarosides with 7-carbon side chain (IC-asc-C7) and to a lesser extent (IC)-ascarosides with 9-carbon side chain (IC-asc-C9) (PubMed:29863473). May associate and regulate the folding and/or the catalytic activity of other acyl-coenzyme A oxidases including acox-1.2, acox-1.3, acox-1.4 and acox-3 modulating the type of ascarosides produced (PubMed:25775534, PubMed:29537254, PubMed:29863473). In association with acox-1.3, catalyzes the desaturation of asc-C7-CoA but not of fatty acids or hydroxylated fatty acids (PubMed:25775534). Involved in the biosynthesis of asc-C6-MK (daumone 2) and asc-delta-C9 (daumone 3) but not asc-C7 (daumone 1); daumones are pheromones produced during unfavourable growth conditions which promote entry into the dauer stage (PubMed:20610393). {ECO:0000269|PubMed:20610393, ECO:0000269|PubMed:25775534, ECO:0000269|PubMed:27551084, ECO:0000269|PubMed:29537254, ECO:0000269|PubMed:29863473}.
|
Caenorhabditis elegans
|
O62238
|
SYP3_CAEEL
|
MNFEKLVSQAVNGDRFKIFCGQLTEFTNSLAGEREAIEKGMRQIETQQLEAETSFTERIAEDRVKCAAQRESLERQLQDLTATDNKLSEQKRDWEERQEKAYDELMSYLENEDVDSAGTQFGDHFNSLIKSMNNLSHDSMNGQFNSLKNNLDELNIEKKQLEVAIADQSSTISEMIPSLRPTCGATYKERNTLRIIFHYQVAKLRSEYQKCRLQEEALKARLST
| null | null |
chiasma assembly [GO:0051026]; embryo development ending in birth or egg hatching [GO:0009792]; homologous chromosome pairing at meiosis [GO:0007129]; meiotic chromosome segregation [GO:0045132]; reciprocal meiotic recombination [GO:0007131]; synaptonemal complex assembly [GO:0007130]
|
central element [GO:0000801]; chromosome [GO:0005694]; lateral element [GO:0000800]; synaptonemal complex [GO:0000795]
| null | null | null | null | null |
SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:17565948}. Note=Upon entrance into pachytene, localizes continuously at the interface between paired and aligned homologous chromosomes (PubMed:17565948). As nuclei progress through late prophase, chromosomal association is progressively reduced (PubMed:17565948). {ECO:0000269|PubMed:17565948}.
| null | null | null | null | null |
FUNCTION: Plays a role in early meiotic events; during prophase I contributes to synaptonemal complex (SC) assembly, synapsis and chiasmata formation and stabilization of homologous chromosomes pairing (PubMed:17565948). Required for restricting SC assembly to bridge paired chromosome axes (PubMed:17565963). Required for the timely progression of meiotic crossover recombination (PubMed:17565963). Required for the synapsis checkpoint (PubMed:27605049). {ECO:0000269|PubMed:17565948, ECO:0000269|PubMed:17565963, ECO:0000269|PubMed:27605049}.
|
Caenorhabditis elegans
|
O62247
|
BLI5_CAEEL
|
MVSIHNSFILLMLMISICFCEKCLTNEECDLKWPDAICVRGRCRCSENTIRKKSASREWVCLATNDATGNSGPPLTCPTPEGAGYQVMYRKDGEPVKCSSKKKPDTCPEGFECIQGLSILGALDGVCCPDRAKTCVHPIFDHPDDGYLSRWGFDGEQCIEFKWNPERPSSANNFKTRAHCEDYCIGSINGITNYHQSNFHLF
| null | null |
cuticle development involved in collagen and cuticulin-based cuticle molting cycle [GO:0042338]; protein catabolic process [GO:0030163]; vulval development [GO:0040025]
| null |
serine-type endopeptidase activity [GO:0004252]; serine-type endopeptidase inhibitor activity [GO:0004867]; structural constituent of collagen and cuticulin-based cuticle [GO:0042329]
|
PF00014;PF14625;
|
4.10.410.10;
| null | null | null | null | null | null | null | null |
FUNCTION: Appears to lack serine protease inhibitor activity in vitro when tested with bovine pancreatic alpha-chymotrypsin and elastase (PubMed:19716386). Involved in cuticle biosynthesis (PubMed:16500660, PubMed:19716386). {ECO:0000269|PubMed:16500660, ECO:0000269|PubMed:19716386}.
|
Caenorhabditis elegans
|
O62255
|
DCP2_CAEEL
|
MEISTENWCKKPKNRSIFSKNISFQKQNKSTEEPPSSVQKLLASLQQAQNKSDLSEQPSTSKPKKNEKRKKAVAQAPASAPAPGPEEKKKQPKRASVGARMQQQAENARISQTKRPRQVSTSKGSSRNTTAPEQQNYQQQQQQYKGPRIPTDILDELEFRFISNMVECEINDNIRVCFHLELAHWYYIDHMVEDDKISGCPNVGSRDFNFQMCQHCRVLRKYAHRADEVLAKFREYKSTVPTYGAILVDPEMDHVVLVQSYFAKGKNWGFPKGKINQAEPPRDAAIRETFEETGFDFGIYSEKEKKFQRFINDGMVRLYLVKNVPKDFNFQPQTRKEIRKIEWFKIDDLPTDKTDELPAYLQGNKFYMVMPFVKDIQIYVQKEKEKLRRRKAEAVQSTPSSSIFSQLFPAQPPPPVPEDATPTRPMYKRLTSEELFSAFKNPPAGEVARPTLPDMSPAVNGLDTLAVLGICTPLKPGASLNEFSGAPQNCPMISEEAGSPADPSAEIGFAMPMDLKQPVVTSDHPWQHHKISDSSAPPQTLESHQGWLDTQLVNTIMHSPNHPLPPTSNSPATPTAVLGHLIGKPIQPQAILPQAATPTALGSAEKPKSSRISLSDNSAFKAISSTQKQSIPKATAAPPSTEKTRSASLSGSSQVVGKPARNLFNSVVSPVSSGIQSIQGDGGAWEDVWFREQLAATTTAGTSISSLAASNQELAMINREETPIEDPYFKQQAYQKAQKAQSLIPACSQWTNSIKLDIDYVVGPLSFWMQQFSTKSPVSGTGPQLP
|
3.6.1.62
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q8IU60}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q8IU60};
|
deadenylation-dependent decapping of nuclear-transcribed mRNA [GO:0000290]; determination of adult lifespan [GO:0008340]; mRNA processing [GO:0006397]; nematode larval development [GO:0002119]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; regulation of locomotion [GO:0040012]; reproduction [GO:0000003]; response to heat [GO:0009408]; response to oxidative stress [GO:0006979]; response to UV [GO:0009411]
|
cytoplasm [GO:0005737]; P granule [GO:0043186]; P-body [GO:0000932]; perinuclear region of cytoplasm [GO:0048471]
|
5'-(N(7)-methyl 5'-triphosphoguanosine)-[mRNA] diphosphatase activity [GO:0140932]; 5'-(N(7)-methylguanosine 5'-triphospho)-[mRNA] hydrolase activity [GO:0140933]; manganese ion binding [GO:0030145]; mRNA 5'-diphosphatase activity [GO:0034353]; RNA binding [GO:0003723]
|
PF05026;PF00293;
|
1.10.10.1050;3.90.79.10;
|
Nudix hydrolase family, DCP2 subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasmic granule {ECO:0000269|PubMed:18439994}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:18439994}. Note=Localizes to perinuclear puncta in pachytene-stage germ cells (PubMed:18439994). Diffusely localized to cytoplasmic puncta in maturing oocytes (PubMed:18439994). {ECO:0000269|PubMed:18439994}.
|
CATALYTIC ACTIVITY: Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + H2O = a 5'-end phospho-ribonucleoside in mRNA + 2 H(+) + N(7)-methyl-GDP; Xref=Rhea:RHEA:67484, Rhea:RHEA-COMP:15692, Rhea:RHEA-COMP:17167, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:63714, ChEBI:CHEBI:138282, ChEBI:CHEBI:156461; EC=3.6.1.62; Evidence={ECO:0000269|PubMed:16199859}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67485; Evidence={ECO:0000269|PubMed:16199859}; CATALYTIC ACTIVITY: Reaction=a 5'-end (N(2),N(2),N(7)-trimethyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + H2O = a 5'-end phospho-ribonucleoside in mRNA + 2 H(+) + N(2),N(2),N(7)-trimethyl-GDP; Xref=Rhea:RHEA:67612, Rhea:RHEA-COMP:15692, Rhea:RHEA-COMP:17171, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:138282, ChEBI:CHEBI:156463, ChEBI:CHEBI:167623; Evidence={ECO:0000269|PubMed:16199859}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67613; Evidence={ECO:0000269|PubMed:16199859};
| null | null | null | null |
FUNCTION: Decapping metalloenzyme that catalyzes the cleavage of the cap structure on mRNAs (PubMed:16199859). Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP (PubMed:16199859). RNA-decapping enzyme although it does not bind the RNA cap (PubMed:16199859). May contribute to gene regulation in multiple RNA pathways including monomethylguanosine- and trimethylguanosine-capped RNAs (PubMed:16199859). In oocytes, may play a role in the response to stress induced by heat shock, osmotic stress and anoxia (PubMed:18439994). Required for the developmental axon guidance and regrowth of PLM touch receptor neurons (PubMed:31983639). Early in embryogenesis, plays a role in ciliary shape formation in sensory neurons (PubMed:28887031). Promotes survival at high temperatures (PubMed:25061667). {ECO:0000269|PubMed:16199859, ECO:0000269|PubMed:18439994, ECO:0000269|PubMed:25061667, ECO:0000269|PubMed:28887031, ECO:0000269|PubMed:31983639}.
|
Caenorhabditis elegans
|
O62275
|
WAGO4_CAEEL
|
MPALPPVYTPSGAPSSVHAPPAVPPVPVPTQPLRSEYQTSNDACIKRLEELNIAPAAKLYPTPTEPGKCGVEAEIQTNVFGIEMHQDSLFYQYSVNITTELKNGKEVTFTKKGKDDFVVTERHDKCCAILFRALGDYEEFFKTSDSCLIYDGQSILFSNVDLFQGFREGAVKTKYMQLDGGEMDHKDLKSLPCIKLEVFPTKNPAVKFTREAVARRATDSNLDSVSLAYQQILELALTQPCLRNTARYVVFDHGKMFFIDPLGEGFEKCDVVDVGDGKQVVPGLKKTINFIEGPYGRGRSNPSVVIDGMKVAFHKNQPILDKLKEITTQPVEHGLKGLEKDRCAAVIKGLDCYSTYGGRERHHKIEGIHHEGARNARFELNDGGSCTVAQYFEDVYNITLRYPDTNLIVSKERGNINFYPMELLKISSHQRVQIPQLTSAQSQKTTKESAVLPDVRQRLILTGKNAAQISSDNEVLGKMGVSVCEDPLMVKGRSIPAVKLANAEIGANPINVKDNKWRANRFTRPATAPNVWAMYVVGTASTRITLDTLKKFADEFAAMCKSKGVNMPAPADISLIHMDAIESRLYDATKANCTFVFIITDDSITTLHQRYKMIEKDTKMIVQDMKLSKALSVINAGKRLTLENVINKTNVKLGGSNYVFVDAKKQLDSHLIIGVGISAPPAGTKYAMENKGVLNPNVIGYAYNAQHNQEFSGDFVLNSASQDTLAPIEDIVMHSLNEYQKFHDGGLPRRVIVYRTGTSEGNHGSIMAYEIPLARAAMRDFSPDIQLVYIVVSKDHSFRFFKPDLASLASRPQATSSTASRHSAMPAAPKAWDLNIAPGILVDSIVTNPACKQFFLNSHITLQGTAKTPLYTVLADDAKVSMTALEDITYKLCHLHQIVGLPTSLPTPLYVANEYAKRGRNLWNEAVALNNVPTVSGPEADRLKELTKSICYKASGDLTGRRVNA
| null | null |
regulation of gene silencing by regulatory ncRNA [GO:0060966]; regulatory ncRNA-mediated heterochromatin formation [GO:0031048]; regulatory ncRNA-mediated post-transcriptional gene silencing [GO:0035194]
|
cytoplasm [GO:0005737]; cytoplasmic ribonucleoprotein granule [GO:0036464]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; RISC complex [GO:0016442]
|
miRNA binding [GO:0035198]; RNA endonuclease activity [GO:0004521]; single-stranded RNA binding [GO:0003727]
|
PF02170;PF02171;
|
3.40.50.2300;2.170.260.10;3.30.420.10;
|
Argonaute family, WAGO subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:29769721, ECO:0000269|PubMed:29791857, ECO:0000269|PubMed:30728462}. Cytoplasmic granule {ECO:0000269|PubMed:29769721}. Cytoplasm {ECO:0000269|PubMed:29791857}. Note=Co-localizes with znfx-1 in P-granules in germline blastomeres until the 100-cell stage (PubMed:29769721). During oocyte maturation, co-localizes with znfx-1 in liquid-like condensates in the cytoplasm called Z granules (PubMed:29769721). Localizes to cytoplasmic P-granules in germline blastomeres. {ECO:0000269|PubMed:29769721}.
| null | null | null | null | null |
FUNCTION: Argonaute protein which is involved in the endogenous small interfering RNA (endo-siRNA) pathway and is required for RNA-mediated gene silencing (RNAi) in the germline (PubMed:17110334, PubMed:29791857, PubMed:30728462). Interacts with secondary 22G-RNAs, which are RNA-dependent RNA polymerase-derived endo-siRNAs, typically 22 nucleotides in length with a 5'guanosine residue (PubMed:29791857). Also interacts with the mRNA targets of 22G-RNAs (PubMed:29791857). Associates with znfx-1 to mediate small RNA-directed transgenerational epigenetic inheritance of both germline- and soma-expressed genes (PubMed:29769721, PubMed:29791857). {ECO:0000269|PubMed:17110334, ECO:0000269|PubMed:29769721, ECO:0000269|PubMed:29791857, ECO:0000269|PubMed:30728462}.
|
Caenorhabditis elegans
|
O62305
|
KCC2D_CAEEL
|
MMNASTKFSDNYDVKEELGKGAFSVVRRCVHKTTGLEFAAKIINTKKLSARDFQKLEREARICRKLQHPNIVRLHDSIQEESFHYLVFDLVTGGELFEDIVAREFYSEADASHCIQQILESIAYCHSNGIVHRDLKPENLLLASKAKGAAVKLADFGLAIEVNDSEAWHGFAGTPGYLSPEVLKKDPYSKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQIKAGAYDYPSPEWDTVTPEAKSLIDSMLTVNPKKRITADQALKVPWICNRERVASAIHRQDTVDCLKKFNARRKLKAAISAVKMVTRMSGVLRTSDSTGSVASNGSTTHDASQVAGTSSQPTSPAAEVYPNVLLFNPQKFPRNCVHPFTTHPYYSPKESSKKKLFFTLLFEVCPHTSRSHILLRDNTKNIYHPYHCFTNKMSNYERAAPSSHGSSTTKKIANAIADLVIRRSSPSIRRKTEADVHNSNRNRKVSAPANLQHALVPVIDVVVATGALASSSVDNLSASTSSDLGRNLLNKKEQGPPSTIKESSESSQTIDDNDSEKGGGQLKHENTVVRADGATGIVSSSNSSTASKSSSTNLSAQKQDIVRVTQTLLDAISCKDFETYTRLCDTSMTCFEPEALGNLIEGIEFHRFYFDGNRKNQVHTTMLNPNVHIIGEDAACVAYVKLTQFLDRNGEAHTRQSQESRVWSKKQGRWVCVHVHRSTQPSTNTTVSEF
|
2.7.11.17
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:16079277};
|
MAPK cascade [GO:0000165]; medium-term memory [GO:0072375]; phosphorylation [GO:0016310]; positive regulation of gene expression [GO:0010628]; serotonin biosynthetic process [GO:0042427]
|
axon cytoplasm [GO:1904115]; cytoplasm [GO:0005737]; neuron projection [GO:0043005]; perikaryon [GO:0043204]
|
ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; calmodulin-dependent protein kinase activity [GO:0004683]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; transmembrane transporter binding [GO:0044325]
|
PF08332;PF00069;
|
3.10.450.50;6.10.140.620;1.10.510.10;
|
Protein kinase superfamily, CAMK Ser/Thr protein kinase family, CaMK subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16079277}. Cell projection, axon {ECO:0000269|PubMed:15625192}. Perikaryon {ECO:0000269|PubMed:15625192, ECO:0000269|PubMed:16079277}. Note=Localizes at or near the Golgi apparatus (PubMed:16079277). Localizes to post-synaptic regions and is enriched in punctate structures in axons of AWC neurons where it co-localizes with tir-1. Localization is regulated by tir-1 (PubMed:15625192). {ECO:0000269|PubMed:15625192, ECO:0000269|PubMed:16079277}.
|
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=2.7.11.17; Evidence={ECO:0000269|PubMed:16079277}; 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=2.7.11.17; Evidence={ECO:0000269|PubMed:16079277};
| null | null | null | null |
FUNCTION: Acts in the signaling of a variety of pathways and processes. Phosphorylates 'Ser-319' of daf-16 in response to stress signals, such as heat, starvation and oxidation, which plays a role in prolonging lifespan. Required for viability under chronic osmotic stress in which it acts downstream of osr-1. Has roles in locomotion, oocyte maturation, brood size, egg laying, defecation, meiotic maturation and neuronal cell fate specification. Required for the regulation of synaptic density and neuromuscular junction morphology. Regulates the synaptic trafficking of glr-1. Bidirectional modulator of neurotransmitter release with negative modulatory effects mainly mediated via slo-1 activation. Involved in activation of ADF neurons and increased tph-1 transcription following exposure to pathogenic bacteria which leads to learned olfactory aversion to the bacteria (PubMed:23325232, PubMed:23505381). Implicated in the muscle regulation of spicule protraction. In conjunction with egl-2 has a role in the suppression of mating behavior under food deprivation to encourage foraging. Involved in restricting str-2 expression to only one of the two AWC neurons. May suppress the functional response to an internal pacemaker, perhaps by modulating the activity of the IP3 receptor. {ECO:0000269|PubMed:10571181, ECO:0000269|PubMed:12221132, ECO:0000269|PubMed:15166144, ECO:0000269|PubMed:16079277, ECO:0000269|PubMed:16267094, ECO:0000269|PubMed:17898212, ECO:0000269|PubMed:17941711, ECO:0000269|PubMed:17942636, ECO:0000269|PubMed:21145946, ECO:0000269|PubMed:21771813, ECO:0000269|PubMed:22629462, ECO:0000269|PubMed:23325232, ECO:0000269|PubMed:23505381, ECO:0000269|PubMed:23663262, ECO:0000269|PubMed:23805378}.
|
Caenorhabditis elegans
|
O62415
|
LYS1_CAEEL
|
MLKLAFVTFLFALASARPQDVDSNRVVALPQDNFEVTDIGFEKIKAEPAPEVVNNDASYAYAVDISVPTTVSQMNCLKTSRYAAVFIRGFTPFGSGAFDTTSVTSIRNAYSAGLGIEVYMTPQPLSSLQGYQQLDALYNGLNGNGITIRSVWIQVTSPANWQKSATTNVNFLNSIISRAKQYGLTVGIYTNQYDWSQITGNWATLSSDVLLWYWHVLGGGVTGETPATFDDFRAFGSFKKASVKQFAQVESVCSLTVNRDVYVVGIPAAASSKNTDFFTQEDISSNNKKIVVGGVIGV
| null | null |
cell wall macromolecule catabolic process [GO:0016998]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; innate immune response [GO:0045087]; peptidoglycan catabolic process [GO:0009253]; signal transduction [GO:0007165]
|
apical part of cell [GO:0045177]; cytoplasmic vesicle [GO:0031410]; cytoplasmic vesicle lumen [GO:0060205]
|
lysozyme activity [GO:0003796]
| null |
3.20.20.80;
|
Glycosyl hydrolase 25 family
| null |
SUBCELLULAR LOCATION: Cytoplasmic vesicle lumen {ECO:0000269|PubMed:12176330}. Note=Localizes in vesicles in the apical region of intestinal cells. {ECO:0000269|PubMed:12176330}.
| null | null | null | null | null |
FUNCTION: Involved in resistance to Gram-negative bacterium S.marcescens and to bacterium Gram-positive S.aureus infection. {ECO:0000269|PubMed:12176330, ECO:0000269|PubMed:21209831}.
|
Caenorhabditis elegans
|
O62471
|
QUI1_CAEEL
|
MFRGKGQQQVSSTDNIKAMMTAAIGNKLEKRLPLVSTIFVVGNDEEEFNIERRTLWQDVLPDLQNLAFQSNFDLEFCDVPLENGELTNSVAEHVLQMWKDNPRSWIVLLLGNRYGNVSVPTSLRKEEYESIRSSIFEENGNVRVFEKAYTINRNGAVEEYRLVPSAIKDKKQLAEIIKALQAGAKAAHEEGSINQVHEQRQNRFFSSPLETFVRSILQVSPCRCLFLLRKFDQLVADPNSPNAFLETNDQNSRKIEDLKNEITLKMNDRVMTHVLRPESTDINYFFNSRDGDKYREKIARQFNEKLKNHLADINPPVRPEPPKSPMVLAANEARTHQEFLENQLALGNLKRDYDKRLDELASVKVNRGVFLIQGTDLCGKTQALCRLYHKISDKDAYKVIFFTNLTYSSNFAHEAWRTICLNICSISNIDPKEVLEHFKLGGILKSLEELVQKADKPVCIFIDDVHLLKFGHLLSQIGRRTETAPDNLSLFMTSSNVAPVNAVFAVTQTVNVDVISENEVVGMVQKMAEKVDKKLTNEQISAIRPLMAAKDGILIAKSFTHEILFNGNSSMKGGMDGRMTRIEKEFGKLAVGNAVKFIAASSHGLTRLEIHDAISADREVLEEMNMSIVYSLLTLDGIIEALGPILRKVIIDDRQIIGIAHSGLISWLRNRYLTSSQDIRSAHLQLSDLFADLLIDNEQSPRHEIAYQSFSQGIKRDNGSPNFRRLRLLWYHCLHSGNLDRLKELSLCHFEYVDYVTRYFGISHLLSLYEECATQILHHDLQVISEQVLVPALVTMARDSEQLAAEVIGRLRFTRHENSHFLNSLVDQAMSWVDLYNRQPLLVPLTCWISPPATKVCRSFTLKDWKPGNTVLTLSANHQYILISGNQSDPGVIYAYHIASEQLIGTFKGHTAAVTCLCSSNDSSLFVSTSFDKTVNVWVFSQSTPTMSLTHHTAKVTCAILTSDDQYLITASADSSAKMIKLETGEVMRSFNDHTGSVVSLQLTSNNQFLITGSGDFVVQMWDVTNGKCISRMGGLMAPVSTLAITSNDAFVVVACEDETLKVFSTVGGQELHELMGHEGKVNSLVCAQDDCQLFAATKSKVFCYDIHNGQMIDVLDTAQPFPICSLKISSDNYFLISPCGPKVTIWNVTKRNHDAHDVHADKEGFLTAVALSNDDKYAACGTNNGIVALWDLEVCQCVFTTIQNKGDPITCIRYSVDSQYCISGNQAGCILILDAQNGGVVRELFMHSSEVLSIMSLVHNKMISCDIQGKMVIWELFGDDDTPEMVATGVKPPIFVPPTGRIMVGHCSLSNKEMKIWAFPEEGPPVTRAKLSHSDEITCFATSPKGGNFIATGSRDMSLKIWQIDKGFLTQVLVGHENVVTCCCISFDERLVVSGARDEKIIVWNVQSGDMVCTVNTTAAITSLSMTGDSTVVFSTTEDGWVETWSTTKGRLLSTFNAHRPIKKLINSYESHRMLLLLENCAQLPILCLHNTPAVGVEATRRRSARAQSVSSASNEPVASTSAGEIKKDPILSSNNGGNAQSAPRATAPKPTFDMLERSKSRTSLIEKDRTTTLTQSNAPPPQKSNMCTLL
| null | null |
response to alkaloid [GO:0043279]
|
axon [GO:0030424]; cytosol [GO:0005829]; dendrite [GO:0030425]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; perikaryon [GO:0043204]
| null |
PF00400;
|
3.40.50.300;2.130.10.10;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:14988722, ECO:0000269|PubMed:26976437}. Perikaryon {ECO:0000269|PubMed:14988722}. Nucleus {ECO:0000269|PubMed:14988722}. Cell projection, dendrite {ECO:0000269|PubMed:14988722}. Cell projection, axon {ECO:0000269|PubMed:14988722}.
| null | null | null | null | null |
FUNCTION: Involved in the avoidance response to the noxious chemicals and repellents such as quinine in ASH and ADL sensory neurons (PubMed:14988722). In response to the noxious chemical quinine, promotes dauer formation induced by pheromones such as the ascaroside ascr#3 in ASH nociceptive neurons (PubMed:26976437). {ECO:0000269|PubMed:14988722, ECO:0000269|PubMed:26976437}.
|
Caenorhabditis elegans
|
O62479
|
SAS6_CAEEL
|
MTSKIALFDQTLIASLLQPLSLNQPDFKAYKTKVKLKISEQRNETSGEKELKFEISRSDDFEFLFSETLNNEKYQILARDHDLTVDFDAFPKVIIQHLLCKNIVKNLEEDGEVDARKKAGYHSIADPGKPTEINIILDAEKNFCSFELFSKTPISKGKIFSIKLHAVRGDHLISHLLKICSSQAVKLSTFYKSADELASLRQKCGDLEKQVEKLSGVKEEFEEMSEKFKELEDEVELVKEERENIRLLVEDKEDEVADLKQDTESLQKQLEENQEELEIVGNMLREEQGKVDQLQKRNVAHQKEIGKLRAELGTAQRNLEKADQLLKRNSQQQNQQSLDMRKLGELEADLKEKDSMVESLTETIGILRKELENEKLKAAENMDSFEKLSMENENLKEKIAHYRAQRFSPAPSGLPGLQTGLTNRLTPSFKPVLGPHTPYGANLNSRTPFRDNTTLNFQNSTIATPHAFRFNSQLIADETTGSSVTNTPPAQR
| null | null |
centriole assembly [GO:0098534]; centriole replication [GO:0007099]; centrosome duplication [GO:0051298]; protein localization [GO:0008104]; regulation of cell cycle [GO:0051726]
|
centriole [GO:0005814]; centrosome [GO:0005813]; cytoplasm [GO:0005737]
|
identical protein binding [GO:0042802]; protein domain specific binding [GO:0019904]
|
PF21503;PF16531;
|
6.10.140.2140;2.170.210.20;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Note=Localizes to centrioles, zyg-1 and sas-5 are required for centriole localization.
| null | null | null | null | null |
FUNCTION: Central scaffolding component of the centrioles ensuring their 9-fold symmetry (PubMed:15572125). Required for centrosome biogenesis and duplication (PubMed:15665853, PubMed:19081077). {ECO:0000269|PubMed:15572125, ECO:0000269|PubMed:15665853, ECO:0000269|PubMed:19081077}.
|
Caenorhabditis elegans
|
O62589
|
GD_DROME
|
MRLHLAAILILCIEHVTKAVAQGMPISPCPKVFQYRFDGSEWFGLMAVRSPDGHQPLHIRVTLSMRGKPTTYTQNYLGEIELLTRGKFTHNAPVLYKIRFPKHHFPPKLLLMSANNHVICFGSGEHSIFMTQIQLEHIRKLSFIPDKKSSLLLDPEEEEVRKTDDKPPSTPHIQFKKKPFAQAPKEICGRIDRDLDFHLSQRTESLHVAIGEPKSSDGITSPVFVDDDEDDVLEHQFVDESEAEAIESDSADSLPSITRGSWPWLAAIYVNNLTSLDFQCGGSLVSARVVISSAHCFKLFNKRYTSNEVLVFLGRHNLKNWNEEGSLAAPVDGIYIHPDFNSQLSSYDADIAVIILKDEVRFNTFIRPACLWSGSSKTEYIVGERGIVIGWSFDRTNRTRDQKLSSELPGKKSTDASAPKVVKAPIVGNAECFRANAHFRSLSSNRTFCAGIQAEERDTHQSGASIYTGISGAGLFIRRNNRWMLRGTVSAALPAVETPDAESSHKLCCKNQYIIYADVAKFLDWITAFVI
|
3.4.21.-
| null |
dorsal/ventral axis specification [GO:0009950]; dorsal/ventral pattern formation [GO:0009953]; proteolysis [GO:0006508]; Toll receptor ligand protein activation cascade [GO:0160032]; ventral furrow formation [GO:0007370]; zymogen activation [GO:0031638]
|
extracellular region [GO:0005576]; perivitelline space [GO:0098595]
|
serine-type endopeptidase activity [GO:0004252]
|
PF16030;PF00089;
|
2.40.10.10;
|
Peptidase S1 family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9477324}.
| null | null | null | null | null |
FUNCTION: Component of the extracellular signaling pathway that establishes the dorsal-ventral pathway of the embryo (PubMed:12493753, PubMed:9477324, PubMed:9618496). Three proteases; ndl, gd and snk process easter to create active easter (PubMed:9477324). Active easter defines cell identities along the dorsal-ventral continuum by activating the spz ligand for the Tl receptor in the ventral region of the embryo (PubMed:9477324). {ECO:0000269|PubMed:12493753, ECO:0000269|PubMed:9477324, ECO:0000269|PubMed:9618496}.
|
Drosophila melanogaster (Fruit fly)
|
O62618
|
MK38A_DROME
|
MSVSITKKFYKLDINRTEWEIPDIYQDLQPVGSGAYGQVSKAVVRGTNMHVAIKKLARPFQSAVHAKRTYRELRLLKHMDHENVIGLLDIFHPHPANGSLENFQQVYLVTHLMDADLNNIIRMQHLSDDHVQFLVYQILRGLKYIHSAGVIHRDLKPSNIAVNEDCELRILDFGLARPTENEMTGYVATRWYRAPEIMLNWMHYDQTVDIWSVGCIMAELITRRTLFPGTDHIHQLNLIMEMLGTPPAEFLKKISSESARSYIQSLPPMKGRSFKNVFKNANPLAIDLLEKMLELDAEKRITAEEALSHPYLEKYAEPSVEQTSPPYDHSFEDMDLPVDKWKELIYKEVTNFKPPPSYAQVLKDVK
|
2.7.11.24
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
|
cellular response to arsenic-containing substance [GO:0071243]; cellular response to cadmium ion [GO:0071276]; cellular response to reactive oxygen species [GO:0034614]; defense response to bacterium [GO:0042742]; defense response to fungus [GO:0050832]; determination of adult lifespan [GO:0008340]; heart morphogenesis [GO:0003007]; immune response [GO:0006955]; intracellular signal transduction [GO:0035556]; MAPK cascade [GO:0000165]; mucosal immune response [GO:0002385]; negative regulation of antimicrobial humoral response [GO:0008348]; osmosensory signaling pathway [GO:0007231]; p38MAPK cascade [GO:0038066]; paracrine signaling [GO:0038001]; phosphorylation [GO:0016310]; positive regulation of cell size [GO:0045793]; regulation of adult chitin-containing cuticle pigmentation [GO:0048082]; regulation of cellular response to oxidative stress [GO:1900407]; response to heat [GO:0009408]; response to hydrogen peroxide [GO:0042542]; response to osmotic stress [GO:0006970]; response to oxidative stress [GO:0006979]; response to starvation [GO:0042594]; stress-activated MAPK cascade [GO:0051403]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; MAP kinase activity [GO:0004707]; 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, MAP kinase subfamily
|
PTM: Dually phosphorylated on Thr-184 and Tyr-186, which activates the enzyme. {ECO:0000269|PubMed:9417090}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9417090}.
|
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=2.7.11.24; 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=2.7.11.24;
| null | null | null | null |
FUNCTION: Kinase involved in a signal transduction pathway. May down-regulate insect immunity gene expression after prolonged infection. {ECO:0000269|PubMed:9417090, ECO:0000269|PubMed:9584193}.
|
Drosophila melanogaster (Fruit fly)
|
O62619
|
KPYK_DROME
|
MVNVTIYDEAPQLKPNEVPQNMAAGADTQLEHMCRLQFDSPVPHVRLSGIVCTIGPASSSVEMLEKMMATGMNIARMNFSHGSHEYHAATVANVRQAVKNYSAKLGYEHPVAIALDTKGPEIRTGLIGGSGTAEIELKKGEKIKLTTNKEFLEKGSLEIVYVDYENIVNVVKPGNRVFVDDGLISLIVREVGKDSLTCEVENGGSLGSRKGVNLPGVPVDLPAVSEKDKSDLLFGVEQEVDMIFASFIRNAAALTEIRKVLGEKGKNIKIISKIENQQGMHNLDEIIEAGDGIMVARGDLGIEIPAEKVFLAQKAMIARCNKAGKPVICATQMLESMVKKPRPTRAEISDVANAVLDGADCVMLSGETAKGEYPLECVLTMAKTCKEAEAALWHQNLFNDLVRGAGTIDASHAAAIAAVEAATKAKASAIVVITTSGKSAFQVSKYRPRCPIIAVTRFAQTARQAHLYRGLVPLIYKEPGLGDWLKDVDVRVQFGLQVGKKNGFIKTGDSVVVVTGWKQGSGFTNTIRIVTVE
|
2.7.1.40
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; COFACTOR: Name=K(+); Xref=ChEBI:CHEBI:29103;
|
canonical glycolysis [GO:0061621]; cellular response to insulin stimulus [GO:0032869]; glucose homeostasis [GO:0042593]; glycolytic process [GO:0006096]; phosphorylation [GO:0016310]; pyruvate biosynthetic process [GO:0042866]; pyruvate metabolic process [GO:0006090]; response to sucrose [GO:0009744]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; P granule [GO:0043186]
|
ATP binding [GO:0005524]; kinase activity [GO:0016301]; magnesium ion binding [GO:0000287]; potassium ion binding [GO:0030955]; pyruvate kinase activity [GO:0004743]
|
PF00224;PF02887;
|
3.20.20.60;2.40.33.10;3.40.1380.20;
|
Pyruvate kinase family
| null | null |
CATALYTIC ACTIVITY: Reaction=ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate; Xref=Rhea:RHEA:18157, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58702, ChEBI:CHEBI:456216; EC=2.7.1.40;
| null |
PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5.
| null | null | null |
Drosophila melanogaster (Fruit fly)
|
O62643
|
THY1_MACMU
|
MNLAISIALLLTVLQVSRGQKVTSLTACLVDQSLRLDCRHENTTSSPIQYEFSLTRETKKHVLFGTVGVPEHTYRSRTNFTSKYNMKVLYLSAFTXKDEGTYTCXLHHSGHSPPISSQNVTVLRDKLVKCEGISLLAQNTSWLXLLLLSLSLLQATDFMSL
| null | null |
angiogenesis [GO:0001525]; cell-cell adhesion [GO:0098609]; cytoskeleton organization [GO:0007010]; focal adhesion assembly [GO:0048041]; integrin-mediated signaling pathway [GO:0007229]; negative regulation of axonogenesis [GO:0050771]; negative regulation of cell migration [GO:0030336]; negative regulation of neuron projection regeneration [GO:0070571]; negative regulation of protein kinase activity [GO:0006469]; negative regulation of T cell receptor signaling pathway [GO:0050860]; positive regulation of focal adhesion assembly [GO:0051894]; positive regulation of GTPase activity [GO:0043547]; positive regulation of release of sequestered calcium ion into cytosol [GO:0051281]; positive regulation of T cell activation [GO:0050870]; retinal cone cell development [GO:0046549]; T cell receptor signaling pathway [GO:0050852]
|
dendrite [GO:0030425]; external side of plasma membrane [GO:0009897]; focal adhesion [GO:0005925]; growth cone [GO:0030426]; membrane raft [GO:0045121]; myelin sheath [GO:0043209]; plasma membrane [GO:0005886]
|
GPI anchor binding [GO:0034235]; GTPase activator activity [GO:0005096]; integrin binding [GO:0005178]
|
PF00047;
|
2.60.40.10;
| null | null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: May play a role in cell-cell or cell-ligand interactions during synaptogenesis and other events in the brain.
|
Macaca mulatta (Rhesus macaque)
|
O62651
|
WT1_PIG
|
MGSDVRDLNALLPAVPSLGGGGGCALPVSGAAEWAPVLDFAPPGASAYGSLGGPAPPPAPPPPPPPPPHSFIKQEPSWGGAEPHEEQCLSAFTVHFSGQFTGTAGACRYEPFGPPPPSQASSGQARMFPNAPYLPSCLESQPAIRNQGYSTVTFDGTPSYGHTPSHHAAQFPNHSFKHEDPMGQQGSLGEQQYSVPPPVYGCHTSTDSCTGSQALLLRTPYSSDNLYQMTSQLECMTWNQMNLGATLKGVAAGTSSSMKWTEGQSNHGAGYESDSHATPILCGAQYRIHTHGVFRGIQDVRRVPGVAPTLVRSASETSEKRPFMCAYPGCNKRYFKLSHLQMHSRKHTGEKPYQCDFKDCERRFSRSDQLKRHQRRHTGVKPFQCKTCQRKFSRSDHLKTHTRTHTGKTSEKPFSCRWPSCQKKFARSDELVRHHNMHQRNMSKLQLAL
| null | null |
adrenal cortex formation [GO:0035802]; adrenal gland development [GO:0030325]; branching involved in ureteric bud morphogenesis [GO:0001658]; camera-type eye development [GO:0043010]; cellular response to gonadotropin stimulus [GO:0071371]; diaphragm development [GO:0060539]; epithelial cell differentiation [GO:0030855]; germ cell development [GO:0007281]; glomerular basement membrane development [GO:0032836]; glomerulus development [GO:0032835]; gonad development [GO:0008406]; heart development [GO:0007507]; male genitalia development [GO:0030539]; male gonad development [GO:0008584]; mesenchymal to epithelial transition [GO:0060231]; metanephric mesenchyme development [GO:0072075]; metanephric S-shaped body morphogenesis [GO:0072284]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell growth [GO:0030308]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of female gonad development [GO:2000195]; negative regulation of metanephric glomerular mesangial cell proliferation [GO:0072302]; negative regulation of translation [GO:0017148]; podocyte differentiation [GO:0072112]; positive regulation of apoptotic process [GO:0043065]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of heart growth [GO:0060421]; positive regulation of male gonad development [GO:2000020]; positive regulation of metanephric ureteric bud development [GO:2001076]; posterior mesonephric tubule development [GO:0072166]; regulation of animal organ formation [GO:0003156]; regulation of DNA-templated transcription [GO:0006355]; regulation of transcription by RNA polymerase II [GO:0006357]; RNA splicing [GO:0008380]; sex determination [GO:0007530]; thorax and anterior abdomen determination [GO:0007356]; tissue development [GO:0009888]; ureteric bud development [GO:0001657]; vasculogenesis [GO:0001570]; visceral serous pericardium development [GO:0061032]
|
cytoplasm [GO:0005737]; nuclear speck [GO:0016607]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
C2H2 zinc finger domain binding [GO:0070742]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; double-stranded methylated DNA binding [GO:0010385]; hemi-methylated DNA-binding [GO:0044729]; RNA binding [GO:0003723]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]; transcription cis-regulatory region binding [GO:0000976]; zinc ion binding [GO:0008270]
|
PF02165;PF00096;
|
3.30.160.60;
|
EGR C2H2-type zinc-finger protein family
| null |
SUBCELLULAR LOCATION: [Isoform 1]: Nucleus speckle {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform 4]: Nucleus, nucleoplasm {ECO:0000250}.; SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Cytoplasm {ECO:0000250}. Nucleus speckle {ECO:0000250}. Note=Shuttles between nucleus and cytoplasm. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Transcription factor that plays an important role in cellular development and cell survival. Recognizes and binds to the DNA sequence 5'-GCG(T/G)GGGCG-3'. Regulates the expression of numerous target genes, including EPO. Plays an essential role for development of the urogenital system. It has a tumor suppressor as well as an oncogenic role in tumor formation. Function may be isoform-specific: isoforms lacking the KTS motif may act as transcription factors. Isoforms containing the KTS motif may bind mRNA and play a role in mRNA metabolism or splicing. Isoform 1 has lower affinity for DNA, and can bind RNA. {ECO:0000250|UniProtKB:P19544}.
|
Sus scrofa (Pig)
|
O62653
|
SUIS_SUNMU
|
MARKKSSGLKITLIVLLAIVTIIAIALVAILPTKTPAVELVSTIPGKCPSAENDRLDEKINCIPDQFPTQALCAMQGCCWNPRNESPTPWCSFANNHGYEFEKISNPNINFEPNLKKNSPPTLFGDNITNLLLTTQSQTANRFRFKITDPNNQRYEVPHQFVNKDFSGPPASNPLYDVKITENPFSIKVIRKSNNKILFDTSIGPLVYSNQYLQISTKLPSKYIYGLGEHVHKRFRHDLYWKTWPIFTRDQLPGDNNNNLYGHQTFFMSIEDTSGKSFGVFLMNSNAMEVFIQPTPIVTYRVIGGILDFYIFLGDTPGQVVQQYQELTGRPAMPSYWSLGFQLSRWNYGSLDAVKEVVKRNRDARIPFDAQVTDIDYMEDKKDFTYNNKTFYGLPEFVKDLHDHGQKYIIILDPAISITSLANGNHYKTYERGNEQKVWVYQSDGTTPLIGEVWPGLTVYPDFTNPKCLDWWTNECSIFHEEIKYDGLWIDMNEVSSFVHGSTKGCSDNKLNYPPFIPDILDKLMYAKTICMDAIQHWGKQYDVHSLYGYSMAIATEKAIEKVFPNKRSFILTRSTFAGTGKHATHWLGDNTPSWEHMEWSITPMLEFGLFGMPFIGADICGFVVDTTEELCRRWMQIGAFYPYFRDHNAGGYMPQDPAYFGQDSLLVNTSRHYLDIWYTLLPYLYNLLYKAYVYGETVARPFLYEFYEDTNSWIEDLQFLWGSALLITPVLRQGADRMSAYIPDATWYDYETGGKRTWRKQRVEMYLPGDKIGLHVRGGYIIPTQQPAVNTTASRKNPLGLIIALDNNAAKGDFFWDDGESKDSIEKGKYILYTFSVLNNELDIICTHSSYQEGTTLAFETIKILGLANTVTQVQVAENNQQTIIHNSFTYHASNQSLIIDNLKLNLGKNFTVQWNQVSLDSEKIDCFPDNNPENKQNCEERGCLWEPNSAAEGPRCYFPKQYNPYLVKSTQYSSMGITVDLELNTATARIKMPSNPISVLRLEVKYHKNDMLQFKIYDPQNKRYEVPIPMDIPTTPTSTYENRLYDVNIKGNPFGIQIRRRSTGRIFWDSCLPWGLLLMNQFIQISTRLPSEYVYGFGGVGHRQFKQDLNWHKWGMFNRDQPSGYKISSYGFQPYIYMALGDGGNAHGVFLLNSNAMDVTFQPNPALTYRTIGGILDFYMFLGPNPEVATKQYHEVIGRPVKPPYWALGFHLCRYGYENTSEIRQLYEDMVSAQIPYDVQYTDIDYMERQLDFTIGKGFQDLPEFVDKIRDEGMKYIIILDPAISGNETQDYLAFQRGIEKDVFVKWPNTQDICWAKVWPDLPNITIDDSLTEDEAVNASRAHVAFPDFLKTSTAEWWATEIEDFYNTYMKFDGLWIDMNEPSSFVHGSVDNKCRNEILNYPPYMPALTKRNEGLHFRTMCMETQQTLSNGSSVLHYDVHNLYGWSQAKPTYDALQKTTGKRGIVISRSTYPSAGRWAGHWLGDNYANWDKIGKSIIGMMEFSLFGISFTGADICGFFNNSDYELCARWMQVGAFYPYSRNHNITDTRRQDPVSWNETFASMSTDILNIRYNLLPYFYTQMHDIHANGGTVIRPLLHEFFSETGTWDIYKQFLWGPAFMVTPVVEPYSESVTGYVPDGRWLDYHTGQDIGLRKRLHTLDAPLYKINLHVCGGHILPCQEPAQNTYFSRQNYMKLIVAADDNQTAQGYLFWDDGESIDTYEKGQYLLVQFNLNKATLTSTILKNGYINTREMRLGFINVWGKGNTVVQEVNITYKGNKESVKFSQEANKQILNIDLTANNIVLDEPIEISWT
|
3.2.1.10; 3.2.1.48
| null |
carbohydrate metabolic process [GO:0005975]
|
apical plasma membrane [GO:0016324]
|
alpha-1,4-glucosidase activity [GO:0004558]; carbohydrate binding [GO:0030246]; oligo-1,6-glucosidase activity [GO:0004574]; sucrose alpha-glucosidase activity [GO:0004575]
|
PF13802;PF01055;PF21365;PF00088;
|
3.20.20.80;2.60.40.1760;2.60.40.1180;4.10.110.10;
|
Glycosyl hydrolase 31 family
|
PTM: The precursor is proteolytically cleaved when exposed to pancreatic proteases in the intestinal lumen. {ECO:0000250}.; PTM: Sulfated. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Apical cell membrane; Single-pass type II membrane protein. Note=Brush border.
|
CATALYTIC ACTIVITY: Reaction=Hydrolysis of sucrose and maltose by an alpha-D-glucosidase-type action.; EC=3.2.1.48; CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by alpha-amylase, and in isomaltose.; EC=3.2.1.10;
| null | null | null | null |
FUNCTION: Plays an important role in the final stage of carbohydrate digestion. Isomaltase activity is specific for both alpha-1,4- and alpha-1,6-oligosaccharides (By similarity). {ECO:0000250}.
|
Suncus murinus (Asian house shrew) (Musk shrew)
|
O62654
|
DESM_BOVIN
|
MSQAYSSSQRVSSYRRTFGGAPSFPLGSPLSSPVFPRAGFGTKGSSSSVTSRVYQVSRTSGGAGGLGALRASRLGSTRVPSSYGAGELLDFSLADAVNQEFLTTRTNEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRLKGREPTRVAEIYEEELRELRRQVEVLTNQRARVDVERDNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHEEEIRELQAQLQEQQVQVEMDMSKPDLTAALRDIRAQYETIAAKNISEAEEWYKSKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYTCEIDALKGTNDSLMRQMRELEDRFASEASGYQDNIARLEEEIRHLKDEMARHLREYQDLLNVKMALDVEIATYRKLLEGEESRINLPIQTFSALNFRETSPEQRGSEVHTKKTVMIKTIETRDGEVVSEATQQQHEVL
| null | null |
intermediate filament organization [GO:0045109]; nuclear envelope organization [GO:0006998]; skeletal muscle organ development [GO:0060538]
|
cell tip [GO:0051286]; cell-cell junction [GO:0005911]; cytoplasm [GO:0005737]; intercalated disc [GO:0014704]; intermediate filament [GO:0005882]; nuclear envelope [GO:0005635]; nucleus [GO:0005634]; sarcolemma [GO:0042383]; Z disc [GO:0030018]
|
structural constituent of cytoskeleton [GO:0005200]
|
PF00038;PF04732;
|
1.20.5.170;1.20.5.500;1.20.5.1160;
|
Intermediate filament family
|
PTM: ADP-ribosylation prevents ability to form intermediate filaments. {ECO:0000250|UniProtKB:P48675}.; PTM: Phosphorylation at Ser-7, Ser-28 and Ser-32 by CDK1 and phosphorylation at Ser-60 by AURKB contribute to efficient separation of desmin intermediate filaments during mitosis. {ECO:0000250|UniProtKB:P31001}.; PTM: Ubiquitination by a SCF-like complex containing ASB2 leads to proteasomal degradation. {ECO:0000250|UniProtKB:P31001}.
|
SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:P17661}. Cytoplasm {ECO:0000250|UniProtKB:P17661}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P17661}. Nucleus {ECO:0000250|UniProtKB:P31001}. Cell tip {ECO:0000250|UniProtKB:P31001}. Nucleus envelope {ECO:0000250|UniProtKB:P31001}. Note=Localizes in the intercalated disks which occur at the Z line of cardiomyocytes. Localizes in the nucleus exclusively in differentiating cardiac progenitor cells and premature cardiomyocytes. PKP2 is required for correct anchoring of DES at the cell tip and nuclear envelope (By similarity). {ECO:0000250|UniProtKB:P17661, ECO:0000250|UniProtKB:P31001}.
| null | null | null | null | null |
FUNCTION: Muscle-specific type III intermediate filament essential for proper muscular structure and function. Plays a crucial role in maintaining the structure of sarcomeres, inter-connecting the Z-disks and forming the myofibrils, linking them not only to the sarcolemmal cytoskeleton, but also to the nucleus and mitochondria, thus providing strength for the muscle fiber during activity. In adult striated muscle they form a fibrous network connecting myofibrils to each other and to the plasma membrane from the periphery of the Z-line structures. May act as a sarcomeric microtubule-anchoring protein: specifically associates with detyrosinated tubulin-alpha chains, leading to buckled microtubules and mechanical resistance to contraction. Required for nuclear membrane integrity, via anchoring at the cell tip and nuclear envelope, resulting in maintenance of microtubule-derived intracellular mechanical forces (By similarity). Contributes to the transcriptional regulation of the NKX2-5 gene in cardiac progenitor cells during a short period of cardiomyogenesis and in cardiac side population stem cells in the adult. Plays a role in maintaining an optimal conformation of nebulette (NEB) on heart muscle sarcomeres to bind and recruit cardiac alpha-actin. {ECO:0000250|UniProtKB:P17661, ECO:0000250|UniProtKB:P31001}.
|
Bos taurus (Bovine)
|
O62664
|
PGH1_BOVIN
|
MSRQGISLRFPLLLLLLSPSPVLPADPGAPAPVNPCCYYPCQHQGICVRFGLDRYQCDCTRTGYYGPNCTIPEIWTWLRTTLRPSPSFVHFLLTHGRWLWDFVNATFIRDKLMRLVLTVRSNLIPSPPTYNVAHDYISWESFSNVSYYTRILPSVPRDCPTPMGTKGKKQLPDAEFLSRRFLLRRKFIPDPQGTNLMFAFFAQHFTHQFFKTSGKMGPGFTKALGHGVDLGHIYGDNLERQYQLRLFKDGKLKYQMLNGEVYPPSVEEAPVLMHYPRGIPPQSQMAVGQEVFGLLPGLMVYATIWLREHNRVCDLLKAEHPTWGDEQLFQTARLILIGETIKIVIEEYVQQLSGYFLQLKFDPELLFGAQFQYRNRIAMEFNQLYHWHPLMPDSFRVGPQDYSYEQFLFNTSMLVDYGVEALVDAFSRQPAGRIGGGRNIDHHILHVAVDVIKESRELRLQPFNEYRKRFGMKPYTSFQELTGEKEMAAELEELYGDIDALEFYPGLLLEKCHPNSIFGESMIEMGAPFSLKGLLGNPICSPEYWKASTFGGDVGFNLVKTATLKKLVCLNTKTCPYVSFHVPDPHREDRPGVERPPTEL
|
1.14.99.1
|
COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250}; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit. {ECO:0000250};
|
cyclooxygenase pathway [GO:0019371]; response to oxidative stress [GO:0006979]
|
cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; neuron projection [GO:0043005]
|
heme binding [GO:0020037]; metal ion binding [GO:0046872]; oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen [GO:0016702]; peroxidase activity [GO:0004601]; prostaglandin-endoperoxide synthase activity [GO:0004666]
|
PF03098;
|
1.10.640.10;2.10.25.10;
|
Prostaglandin G/H synthase family
| null |
SUBCELLULAR LOCATION: Microsome membrane; Peripheral membrane protein. Endoplasmic reticulum membrane; Peripheral membrane protein.
|
CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + AH2 + 2 O2 = A + H2O + prostaglandin H2; Xref=Rhea:RHEA:23728, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:32395, ChEBI:CHEBI:57405; EC=1.14.99.1; Evidence={ECO:0000250|UniProtKB:P23219}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23729; Evidence={ECO:0000250|UniProtKB:P23219}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + 2 O2 = prostaglandin G2; Xref=Rhea:RHEA:42596, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:82629; Evidence={ECO:0000250|UniProtKB:P23219}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42597; Evidence={ECO:0000250|UniProtKB:P23219}; CATALYTIC ACTIVITY: Reaction=AH2 + prostaglandin G2 = A + H2O + prostaglandin H2; Xref=Rhea:RHEA:42600, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:57405, ChEBI:CHEBI:82629; Evidence={ECO:0000250|UniProtKB:P23219}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42601; Evidence={ECO:0000250|UniProtKB:P23219}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = (9R)-hydroxy-(10E,12Z)-octadecadienoate + A + H2O; Xref=Rhea:RHEA:75447, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:30245, ChEBI:CHEBI:77895; Evidence={ECO:0000250|UniProtKB:P05979}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75448; Evidence={ECO:0000250|UniProtKB:P05979}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = (9S)-hydroxy-(10E,12Z)-octadecadienoate + A + H2O; Xref=Rhea:RHEA:75459, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:30245, ChEBI:CHEBI:77852; Evidence={ECO:0000250|UniProtKB:P05979}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75460; Evidence={ECO:0000250|UniProtKB:P05979}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = (13S)-hydroxy-(9Z,11E)-octadecadienoate + A + H2O; Xref=Rhea:RHEA:75451, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:30245, ChEBI:CHEBI:90850; Evidence={ECO:0000250|UniProtKB:P05979}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75452; Evidence={ECO:0000250|UniProtKB:P05979}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = (13R)-hydroxy-(9Z,11E)-octadecadienoate + A + H2O; Xref=Rhea:RHEA:75455, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:30245, ChEBI:CHEBI:136655; Evidence={ECO:0000250|UniProtKB:P05979}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75456; Evidence={ECO:0000250|UniProtKB:P05979};
| null |
PATHWAY: Lipid metabolism; prostaglandin biosynthesis. {ECO:0000250|UniProtKB:P23219}.
| null | null |
FUNCTION: Dual cyclooxygenase and peroxidase that plays an important role in the biosynthesis pathway of prostanoids, a class of C20 oxylipins mainly derived from arachidonate ((5Z,8Z,11Z,14Z)-eicosatetraenoate, AA, C20:4(n-6)), with a particular role in the inflammatory response. The cyclooxygenase activity oxygenates AA to the hydroperoxy endoperoxide prostaglandin G2 (PGG2), and the peroxidase activity reduces PGG2 to the hydroxy endoperoxide prostaglandin H2 (PGH2), the precursor of all 2-series prostaglandins and thromboxanes. This complex transformation is initiated by abstraction of hydrogen at carbon 13 (with S-stereochemistry), followed by insertion of molecular O2 to form the endoperoxide bridge between carbon 9 and 11 that defines prostaglandins. The insertion of a second molecule of O2 (bis-oxygenase activity) yields a hydroperoxy group in PGG2 that is then reduced to PGH2 by two electrons. Involved in the constitutive production of prostanoids in particular in the stomach and platelets. In gastric epithelial cells, it is a key step in the generation of prostaglandins, such as prostaglandin E2 (PGE2), which plays an important role in cytoprotection. In platelets, it is involved in the generation of thromboxane A2 (TXA2), which promotes platelet activation and aggregation, vasoconstriction and proliferation of vascular smooth muscle cells. Can also use linoleate (LA, (9Z,12Z)-octadecadienoate, C18:2(n-6)) as substrate and produce hydroxyoctadecadienoates (HODEs) in a regio- and stereospecific manner, being (9R)-HODE ((9R)-hydroxy-(10E,12Z)-octadecadienoate) and (13S)-HODE ((13S)-hydroxy-(9Z,11E)-octadecadienoate) its major products. {ECO:0000250|UniProtKB:P05979}.
|
Bos taurus (Bovine)
|
O62667
|
S28A1_PIG
|
MEDNTPRQRDPISLTSVANGLENMGAELLESLEEGRAPGSDSSPAEVGGGWSKAGPEHLGRRSLQPALRVRRFCREHTQLFRWICTGLLCTAFAAFLLIACLLDFQRALALFVLFCVVLFFLAHSLLKRLLGPKLLRCVKPLRHPCLNLWFKRGLALAAFLGLVLWLVLDTAQRPEQLVSFGGICVFILLLFAGSKHHRAVSWRAVSWGLGLQFALGLFVIRTEPGFIAFQWLGDQIQIFLSYTEAGSSFVFGEALVKDVFAFQVLPIIVFFSCAMSVLYYVGLMQWVILKISWLMQATMGTTATETLSVAGNIFVSQTEAPLLIRPYLADMTLSEIHVVMTGGYATIAGSLLGAYISFGIDAASLIAASVMAAPCALALSKLVYPEVEESKFKREEGVKLTYGDAQNLLEAASSGAAMSVRVVTNIAANLIAFLAVLAFINAALSWLGDMVDVQGLSFQLICSYVLRPVAFLMGVAWEDCPVVAELLGMKLFLNEFVAYQELSGYKQRRLAGAEEWVGSRKQWISVRAEILTTYALCGFANFSSIGIMLGGLTSMVPQRKGDFSQIVLRALCTGACVSLVNACVAGILYVPRGAEVDCVSFLNTTLSSSSFEVYQCCRQFFQSTSLEFSPEALDNCCRFYNHTICV
| null | null |
cytidine transport [GO:0015861]; nucleoside import across plasma membrane [GO:0180015]; nucleoside transmembrane transport [GO:1901642]; pyrimidine nucleobase transport [GO:0015855]; uridine transport [GO:0015862]
|
apical plasma membrane [GO:0016324]; plasma membrane [GO:0005886]
|
pyrimidine- and adenosine-specific:sodium symporter activity [GO:0015389]
|
PF07670;PF07662;PF01773;
| null |
Concentrative nucleoside transporter (CNT) (TC 2.A.41) family
|
PTM: N-glycosylated. N-glycosylation is required for localization to the plasma membrane and the transporter activity. {ECO:0000250|UniProtKB:O00337}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9858747}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q62674}. Apical cell membrane {ECO:0000250|UniProtKB:O00337}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q62674}.
|
CATALYTIC ACTIVITY: Reaction=Na(+)(out) + uridine(out) = Na(+)(in) + uridine(in); Xref=Rhea:RHEA:69887, ChEBI:CHEBI:16704, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:9858747}; CATALYTIC ACTIVITY: Reaction=Na(+)(out) + thymidine(out) = Na(+)(in) + thymidine(in); Xref=Rhea:RHEA:69891, ChEBI:CHEBI:17748, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:9858747}; CATALYTIC ACTIVITY: Reaction=cytidine(out) + Na(+)(out) = cytidine(in) + Na(+)(in); Xref=Rhea:RHEA:69895, ChEBI:CHEBI:17562, ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:O00337}; CATALYTIC ACTIVITY: Reaction=adenosine(out) + Na(+)(out) = adenosine(in) + Na(+)(in); Xref=Rhea:RHEA:69927, ChEBI:CHEBI:16335, ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:O00337};
| null | null | null | null |
FUNCTION: Sodium and pyrimidine nucleoside symporter of the plasma membrane that imports uridine, thymidine and cytidine into cells by coupling their transport to the transmembrane sodium electrochemical gradient. Also transports adenosine, an atypical substrate transported with high apparent affinity, but low maximum velocity. Therefore, exhibits the transport characteristics of the nucleoside transport system cit or N2 subtype (N2/cit). Involved in renal nucleoside (re)absorption. {ECO:0000250|UniProtKB:O00337}.
|
Sus scrofa (Pig)
|
O62683
|
ZO3_CANLF
|
MEELTIWEQHTATLCRDPRRGFGIAISGGRDRASGSVVVSDVVPGGPADGRLQTGDHVVMVNGVSMESVTSTFAIQILKTCTKLANITVKRPRKIQLPATKAGTSGRGRQGLEEEADCGQGYDGDTSSGSGRSWDKRSRRARTGRRNQAGSRGRRSPGGNSEANGLALVSGFKRLPRQDVHMRPVKSVLVRRTESEEFGVTLGSQIFIKHITDSGLAARNRGLQEGDLILQINGVSSENLSLSDTRRLIEKSEGKLTLLVLRDRGQFLVNIPPAVSDSDSDSSFLDDISALGSELSQAVPSHVPPPPPHAQRSLDSDGTDSPRDSPPLRRENSLDSRTISEPDAPRHSSYDIYRVPSSQSAEDRGYSPDSRVVRFHKGTTIGLRLAGGNDVGIFVSGVQEGSPADGQGIQEGDQILQVNDVPFRNLTREEAVQFLVALPPGEEVELVTQRNEDIFRKMVQSRVGDSFYIRTHFELEASPPSGLGFTRGDVFHVLDTLCPGPGPSGARGTHWLAVRMGRDLREQERGIIPNQSRAEQLASLESAQRAVGAGPGASVGSSARAEFWRLRGLRRGAKKSTQRSREDLSALTRQGHYPPYERVVLREASFKRPVVILGPVADIAMQKLTAEMPDQFGIADSVLRTDSPSKIIKLDTVRVIAEKNKHALLDVTPSAVERLNYVQYYPIVVFCAPESRAALKALRQWLAPASRRSARRLYAQAQKLRKHSEHLFTATIPLRGTSDTWYQELKAVVREQQTRPIWTAEDQLDNSSEDNLELPHRGLADSSADLSCDSRVNSDYETDGEGYTDGEGYTDVDEGPPAPALARSSEPVLEEEPRSPRDHGRASGARGAQVDRHPYHSQGRQDSMRTYGQEALKKKFTRARDVESSDEDGYDWGPATDL
| null | null |
cell-cell adhesion [GO:0098609]; cell-cell junction organization [GO:0045216]; establishment of endothelial intestinal barrier [GO:0090557]; positive regulation of blood-brain barrier permeability [GO:1905605]; protein localization to cell-cell junction [GO:0150105]
|
bicellular tight junction [GO:0005923]; cell surface [GO:0009986]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; tight junction [GO:0070160]
|
cell adhesion molecule binding [GO:0050839]
|
PF00625;PF00595;PF07653;
|
2.30.42.10;3.40.50.300;2.30.30.40;
|
MAGUK family
|
PTM: Phosphorylated (PubMed:8408213). {ECO:0000269|PubMed:8408213}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12021270}; Peripheral membrane protein {ECO:0000269|PubMed:12021270}; Cytoplasmic side {ECO:0000269|PubMed:12021270}. Cell junction, tight junction {ECO:0000269|PubMed:12021270, ECO:0000269|PubMed:9531559}. Nucleus {ECO:0000250|UniProtKB:O95049}. Note=Exhibits predominant nuclear expression in proliferating cells but is exclusively junctionally expressed after confluence is reached (By similarity). Shows an epithelial-specific tight junction localization in a TJP1/TJP2-dependent fashion (By similarity). {ECO:0000250|UniProtKB:O95049, ECO:0000250|UniProtKB:Q9QXY1}.
| null | null | null | null | null |
FUNCTION: TJP1, TJP2, and TJP3 are closely related scaffolding proteins that link tight junction (TJ) transmembrane proteins such as claudins, junctional adhesion molecules, and occludin to the actin cytoskeleton (PubMed:12021270). The tight junction acts to limit movement of substances through the paracellular space and as a boundary between the compositionally distinct apical and basolateral plasma membrane domains of epithelial and endothelial cells. Binds and recruits PATJ to tight junctions where it connects and stabilizes apical and lateral components of tight junctions (PubMed:12021270). Promotes cell-cycle progression through the sequestration of cyclin D1 (CCND1) at tight junctions during mitosis which prevents CCND1 degradation during M-phase and enables S-phase transition (By similarity). With TJP1 and TJP2, participates in the junctional retention and stability of the transcription factor DBPA, but is not involved in its shuttling to the nucleus (PubMed:24986862). Contrary to TJP2, TJP3 is dispensable for individual viability, embryonic development, epithelial differentiation, and the establishment of TJs, at least in the laboratory environment (By similarity). {ECO:0000250|UniProtKB:O95049, ECO:0000250|UniProtKB:Q9QXY1, ECO:0000269|PubMed:12021270, ECO:0000269|PubMed:24986862}.
|
Canis lupus familiaris (Dog) (Canis familiaris)
|
O62698
|
PGH2_BOVIN
|
MLARALLLCAAVALSGAANPCCSHPCQNRGVCMSVGFDQYKCDCTRTGFYGENCTTPEFLTRIKLLLKPTPNTVHYILTHFKGVWNIVNKISFLRNMIMRYVLTSRSHLIESPPTYNVHYSYKSWEAFSNLSYYTRALPPVPDDCPTPMGVKGRKELPDSKEVVKKVLLRRKFIPDPQGTNLMFAFFAQHFTHQFFKTDFERGPAFTKGKNHGVDLSHIYGESLERQHKLRLFKDGKMKYQMINGEMYPPTVKDTQVEMIYPPHVPEHLKFAVGQEVFGLVPGLMMYATIWLREHNRVCDVLKQEHPEWGDEQLFQTSRLILIGETIKIVIEDYVQHLSGYHFKLKFDPELLFNQQFQYQNRIAAEFNTLYHWHPLLPDVFQIDGQEYNYQQFIYNNSVLLEHGLTQFVESFTRQRAGRVAGGRNLPVAVEKVSKASIDQSREMKYQSFNEYRKRFLVKPYESFEELTGEKEMAAELEALYGDIDAMEFYPALLVEKPRPDAIFGETMVEAGAPFSLKGLMGNPICSPEYWKPSTFGGEVGFKIINTASIQSLICSNVKGCPFTSFSVQDTHLTKTVTINASSSHSGLDDINPTVLLKERSTEL
|
1.14.99.1
|
COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250|UniProtKB:Q05769}; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit. {ECO:0000250|UniProtKB:Q05769};
|
cellular response to interleukin-1 [GO:0071347]; cyclooxygenase pathway [GO:0019371]; meiotic spindle organization [GO:0000212]; ovarian cumulus expansion [GO:0001550]; positive regulation of embryonic development [GO:0040019]; positive regulation of meiotic cell cycle process involved in oocyte maturation [GO:1904146]; positive regulation of oocyte maturation [GO:1900195]; positive regulation of protein phosphorylation [GO:0001934]; prostaglandin biosynthetic process [GO:0001516]; regulation of neuroinflammatory response [GO:0150077]; response to oxidative stress [GO:0006979]
|
cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; neuron projection [GO:0043005]; nuclear inner membrane [GO:0005637]; nuclear outer membrane [GO:0005640]
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heme binding [GO:0020037]; metal ion binding [GO:0046872]; oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen [GO:0016702]; peroxidase activity [GO:0004601]; prostaglandin-endoperoxide synthase activity [GO:0004666]
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PF03098;
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1.10.640.10;2.10.25.10;
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Prostaglandin G/H synthase family
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PTM: S-nitrosylation by NOS2 (iNOS) activates enzyme activity. S-nitrosylation may take place on different Cys residues in addition to Cys-526. {ECO:0000250|UniProtKB:P35354}.; PTM: Acetylated at Ser-565 by SPHK1. During neuroinflammation, acetylation by SPHK1 promotes neuronal secretion of specialized preresolving mediators (SPMs), especially 15-R-lipoxin A4, which results in an increase of phagocytic microglia. {ECO:0000250|UniProtKB:Q05769}.
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SUBCELLULAR LOCATION: Microsome membrane {ECO:0000250|UniProtKB:P35354}; Peripheral membrane protein {ECO:0000250|UniProtKB:P35354}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P35354}; Peripheral membrane protein {ECO:0000250|UniProtKB:P35354}. Nucleus inner membrane {ECO:0000250|UniProtKB:P35354}; Peripheral membrane protein {ECO:0000250|UniProtKB:P35354}. Nucleus outer membrane {ECO:0000250|UniProtKB:P35354}; Peripheral membrane protein {ECO:0000250|UniProtKB:P35354}. Note=Detected on the lumenal side of the endoplasmic reticulum and nuclear envelope. {ECO:0000250|UniProtKB:P35354}.
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CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + AH2 + 2 O2 = A + H2O + prostaglandin H2; Xref=Rhea:RHEA:23728, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:32395, ChEBI:CHEBI:57405; EC=1.14.99.1; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23729; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + 2 O2 = prostaglandin G2; Xref=Rhea:RHEA:42596, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:82629; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42597; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=AH2 + prostaglandin G2 = A + H2O + prostaglandin H2; Xref=Rhea:RHEA:42600, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:57405, ChEBI:CHEBI:82629; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42601; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + 2 O2 = prostaglandin G3; Xref=Rhea:RHEA:50444, ChEBI:CHEBI:15379, ChEBI:CHEBI:58562, ChEBI:CHEBI:133133; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50445; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=AH2 + prostaglandin G3 = A + H2O + prostaglandin H3; Xref=Rhea:RHEA:50448, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:133133, ChEBI:CHEBI:133134; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50449; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(8Z,11Z,14Z)-eicosatrienoate + 2 O2 = prostaglandin G1; Xref=Rhea:RHEA:50424, ChEBI:CHEBI:15379, ChEBI:CHEBI:71589, ChEBI:CHEBI:133084; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50425; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=AH2 + prostaglandin G1 = A + H2O + prostaglandin H1; Xref=Rhea:RHEA:50432, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:90793, ChEBI:CHEBI:133084; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50433; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphoethanolamine + 2 O2 = 2-(prostaglandin G2)-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:54204, ChEBI:CHEBI:15379, ChEBI:CHEBI:76091, ChEBI:CHEBI:138098; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54205; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=2-(prostaglandin G2)-sn-glycero-3-phosphoethanolamine + AH2 = 2-(prostaglandin H2)-sn-glycero-3-phosphoethanolamine + A + H2O; Xref=Rhea:RHEA:54208, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:138098, ChEBI:CHEBI:138099; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54209; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphocholine + 2 O2 = 2-(prostaglandin G2)-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:54212, ChEBI:CHEBI:15379, ChEBI:CHEBI:76079, ChEBI:CHEBI:138100; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54213; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=2-(prostaglandin G2)-sn-glycero-3-phosphocholine + AH2 = 2-(prostaglandin H2)-sn-glycero-3-phosphocholine + A + H2O; Xref=Rhea:RHEA:54216, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:138100, ChEBI:CHEBI:138101; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54217; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + AH2 = (15S)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + A + H2O; Xref=Rhea:RHEA:48856, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:57409, ChEBI:CHEBI:57446; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48857; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphocholine + AH2 + O2 = 2-[(15S)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl]-sn-glycero-3-phosphocholine + A + H2O; Xref=Rhea:RHEA:53684, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:76079, ChEBI:CHEBI:137584; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53685; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphocholine + AH2 + O2 = 2-[(15R)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl]-sn-glycero-3-phosphocholine + A + H2O; Xref=Rhea:RHEA:53680, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:76079, ChEBI:CHEBI:137583; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53681; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphocholine + AH2 + O2 = 2-[(11R)-hydroxy-(5Z,8Z,12E,14Z)-eicosatetraenoyl]-sn-glycero-3-phosphocholine + A + H2O; Xref=Rhea:RHEA:53676, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:76079, ChEBI:CHEBI:137582; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53677; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = 9-hydroxy-(10E,12Z)-octadecadienoate + A + H2O; Xref=Rhea:RHEA:50864, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:30245, ChEBI:CHEBI:133820; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50865; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = 13-hydroxy-(9Z,11E)-octadecadienoate + A + H2O; Xref=Rhea:RHEA:50860, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:30245, ChEBI:CHEBI:133819; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50861; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + AH2 + O2 = (15R)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + A + H2O; Xref=Rhea:RHEA:50856, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:32395, ChEBI:CHEBI:78837; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50857; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + AH2 + O2 = (11R)-hydroxy-(5Z,8Z,12E,14Z)-eicosatetraenoate + A + H2O; Xref=Rhea:RHEA:50852, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:32395, ChEBI:CHEBI:78836; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50853; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + AH2 + O2 = (11R)-hydroxy-(5Z,8Z,12E,14Z,17Z)-eicosapentaenoate + A + H2O; Xref=Rhea:RHEA:50848, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:58562, ChEBI:CHEBI:90820; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50849; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + AH2 + O2 = (18S)-hydroxy-(5Z,8Z,11Z,14Z,16E)-eicosapentaenoate + A + H2O; Xref=Rhea:RHEA:50200, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:58562, ChEBI:CHEBI:132083; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50201; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + AH2 + O2 = (18R)-hydroxy-(5Z,8Z,11Z,14Z,16E)-eicosapentaenoate + A + H2O; Xref=Rhea:RHEA:48836, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:58562, ChEBI:CHEBI:90818; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48837; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + AH2 + O2 = (15R)-hydroxy-(5Z,8Z,11Z,13E,17Z)-eicosapentaenoate + A + H2O; Xref=Rhea:RHEA:48840, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:58562, ChEBI:CHEBI:90819; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48841; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + AH2 + O2 = (15S)-hydroxy-(5Z,8Z,11Z,13E,17Z)-eicosapentaenoate + A + H2O; Xref=Rhea:RHEA:50196, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:58562, ChEBI:CHEBI:132087; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50197; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(7Z,10Z,13Z,16Z,19Z)-docosapentaenoate + AH2 + O2 = 13R-hydroxy-(7Z,10Z,14E,16Z,19Z)-docosapentaenoate + A + H2O; Xref=Rhea:RHEA:48852, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:77224, ChEBI:CHEBI:90824; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48853; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + AH2 + O2 = 13-hydroxy-(4Z,7Z,10Z,14E,16Z,19Z)-docosahexaenoate + A + H2O; Xref=Rhea:RHEA:48820, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:77016, ChEBI:CHEBI:90815; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48821; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(5S)-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + AH2 + O2 = (5S,15R)-dihydroxy-(6E,8Z,11Z,13E)-eicosatetraenoate + A + H2O; Xref=Rhea:RHEA:48812, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:90632, ChEBI:CHEBI:90812; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48813; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + AH2 + O2 = 17R-hydroxy-(4Z,7Z,10Z,13Z,15E,19Z)-docosahexaenoate + A + H2O; Xref=Rhea:RHEA:48816, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:77016, ChEBI:CHEBI:90814; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48817; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(5S)-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + AH2 + O2 = (5S,15S)-dihydroxy-(6E,8Z,11Z,13E)-eicosatetraenoate + A + H2O; Xref=Rhea:RHEA:48808, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:90632, ChEBI:CHEBI:90813; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48809; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(5S)-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + AH2 + O2 = (5S,11R)-dihydroxy-(6E,8Z,12E,14Z)-eicosatetraenoate + A + H2O; Xref=Rhea:RHEA:48804, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:90632, ChEBI:CHEBI:90810; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48805; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + 2 O2 = 2-glyceryl-prostaglandin G2; Xref=Rhea:RHEA:45288, ChEBI:CHEBI:15379, ChEBI:CHEBI:52392, ChEBI:CHEBI:85165; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45289; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=2-glyceryl-prostaglandin G2 + AH2 = 2-glyceryl-prostaglandin H2 + A + H2O; Xref=Rhea:RHEA:45292, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:85165, ChEBI:CHEBI:85166; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45293; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = (15R)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate; Xref=Rhea:RHEA:42284, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:82626; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42285; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = 11R-hydroperoxy-(5Z,8Z,12E,14Z)-eicosatetraenoate; Xref=Rhea:RHEA:42280, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:82628; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42281; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = (9R)-hydroxy-(10E,12Z)-octadecadienoate + A + H2O; Xref=Rhea:RHEA:75447, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:30245, ChEBI:CHEBI:77895; Evidence={ECO:0000250|UniProtKB:P79208}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75448; Evidence={ECO:0000250|UniProtKB:P79208}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = (9S)-hydroxy-(10E,12Z)-octadecadienoate + A + H2O; Xref=Rhea:RHEA:75459, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:30245, ChEBI:CHEBI:77852; Evidence={ECO:0000250|UniProtKB:P79208}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75460; Evidence={ECO:0000250|UniProtKB:P79208}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = (13S)-hydroxy-(9Z,11E)-octadecadienoate + A + H2O; Xref=Rhea:RHEA:75451, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:30245, ChEBI:CHEBI:90850; Evidence={ECO:0000250|UniProtKB:P79208}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75452; Evidence={ECO:0000250|UniProtKB:P79208}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = (13R)-hydroxy-(9Z,11E)-octadecadienoate + A + H2O; Xref=Rhea:RHEA:75455, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:30245, ChEBI:CHEBI:136655; Evidence={ECO:0000250|UniProtKB:P79208}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75456; Evidence={ECO:0000250|UniProtKB:P79208};
| null |
PATHWAY: Lipid metabolism; prostaglandin biosynthesis. {ECO:0000250|UniProtKB:P35354}.
| null | null |
FUNCTION: Dual cyclooxygenase and peroxidase in the biosynthesis pathway of prostanoids, a class of C20 oxylipins mainly derived from arachidonate ((5Z,8Z,11Z,14Z)-eicosatetraenoate, AA, C20:4(n-6)), with a particular role in the inflammatory response. The cyclooxygenase activity oxygenates AA to the hydroperoxy endoperoxide prostaglandin G2 (PGG2), and the peroxidase activity reduces PGG2 to the hydroxy endoperoxide prostaglandin H2 (PGH2), the precursor of all 2-series prostaglandins and thromboxanes. This complex transformation is initiated by abstraction of hydrogen at carbon 13 (with S-stereochemistry), followed by insertion of molecular O2 to form the endoperoxide bridge between carbon 9 and 11 that defines prostaglandins. The insertion of a second molecule of O2 (bis-oxygenase activity) yields a hydroperoxy group in PGG2 that is then reduced to PGH2 by two electrons. Similarly catalyzes successive cyclooxygenation and peroxidation of dihomo-gamma-linoleate (DGLA, C20:3(n-6)) and eicosapentaenoate (EPA, C20:5(n-3)) to corresponding PGH1 and PGH3, the precursors of 1- and 3-series prostaglandins. In an alternative pathway of prostanoid biosynthesis, converts 2-arachidonoyl lysophopholipids to prostanoid lysophopholipids, which are then hydrolyzed by intracellular phospholipases to release free prostanoids. Metabolizes 2-arachidonoyl glycerol yielding the glyceryl ester of PGH2, a process that can contribute to pain response. Generates lipid mediators from n-3 and n-6 polyunsaturated fatty acids (PUFAs) via a lipoxygenase-type mechanism. Oxygenates PUFAs to hydroperoxy compounds and then reduces them to corresponding alcohols. Plays a role in the generation of resolution phase interaction products (resolvins) during both sterile and infectious inflammation. Metabolizes docosahexaenoate (DHA, C22:6(n-3)) to 17R-HDHA, a precursor of the D-series resolvins (RvDs). As a component of the biosynthetic pathway of E-series resolvins (RvEs), converts eicosapentaenoate (EPA, C20:5(n-3)) primarily to 18S-HEPE that is further metabolized by ALOX5 and LTA4H to generate 18S-RvE1 and 18S-RvE2. In vascular endothelial cells, converts docosapentaenoate (DPA, C22:5(n-3)) to 13R-HDPA, a precursor for 13-series resolvins (RvTs) shown to activate macrophage phagocytosis during bacterial infection. In activated leukocytes, contributes to oxygenation of hydroxyeicosatetraenoates (HETE) to diHETES (5,15-diHETE and 5,11-diHETE). Can also use linoleate (LA, (9Z,12Z)-octadecadienoate, C18:2(n-6)) as substrate and produce hydroxyoctadecadienoates (HODEs) in a regio- and stereospecific manner, being (9R)-HODE ((9R)-hydroxy-(10E,12Z)-octadecadienoate) and (13S)-HODE ((13S)-hydroxy-(9Z,11E)-octadecadienoate) its major products (By similarity). During neuroinflammation, plays a role in neuronal secretion of specialized preresolving mediators (SPMs) 15R-lipoxin A4 that regulates phagocytic microglia (By similarity). {ECO:0000250|UniProtKB:P35354, ECO:0000250|UniProtKB:P79208, ECO:0000250|UniProtKB:Q05769}.
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Bos taurus (Bovine)
|
O62699
|
NOS2_CANLF
|
MACPWKFLFRAKFHQYGMKEEKDINNNVEKPPGATPSPSTQDDLKNHKHHNDSPQPLTETVQKLPESLDKLHATPLSRPQHVRIKNWGNGMTFQDTLHHKAKGDLACKSKSCLGAIMNPKSLTREPRDKPTPPDELLPQAIEFVNQYYSSFKEAKIEEHLARVEAVTKEIETTGTYQLTGDELIFATKQAWRNAPRCIGRIQWSNLQVFDARSCSTAKEMFEHICRHLRYASNNGNIRSAITVFPQRTDGKHDFRVWNAQLIRYAGYQMPDGTILGDPASVEFTQLCIDLGWKPKYGRFDVVPLVLQADGQDPEFFEIPPDLVLEVPMEHPKYEWFRELELKWYALPAVANMLLEVGGLEFPGCPFNGWYMGTEIGVRDFCDVQRYNILEEVGRRMGLETHKLASLWKDRAVIEINVAVLHSFQKQNVTIMDHHSAAESFMKYMQSEYRSRGGCPADWIWLVPPISGSITPVFHQEMLNYVLSPFYYYQVEAWKTHVWQDEKRRPQRRKIQLKVLVKAVLFASMLMRKTMASRVRVTILFATETGKSETLARDLGALFSCAFHPKVLCMDEYKLSHLEEEQLLLVVTSTFGNGDSPGNGEKLKKSLFMLKELTNKFRYAVFGLGSSMYPQFCAFAHDIDHKLSHLGASQLTPGGEGDELNGKEEAFRCWAVQTFKAACDTSDVRGKHCIQIPRLYTSNVTWDPHHYRLLQDSQPLDLNKALSKMHAKNVFTLRLKSQRNLQSPISNRTTLQVELSCEDSQELSYLPGEHLGVFPGNQLALVQGILERVVYSPAPLQPVHLETLSERGSYWVRNNRLPPCSLSQALTYFLDITTPPTHLLLRKLAQLAHQYAERHRLEILCHPSEYNKWKLTNSPTFLEVLEEFPSLRVSAGFLLSQLPILKPRYYSISSSRDCTPMEVHLTVAVLVYPTRDGQGPLHHGVCSTWLSNLKPQDPVPCFVRSAGNFKLPEDPSRPCILIGPGTGIAPFRSFWQQRLHDIKHKGLRGSRMTLVFGCRRPDEDHLYREEMLEMAQSGVLHEVHTAYSRLPGQPKVYVQDILRQQLASQVLRMLHEEQGHLYVCGDVRMARDVAHTLKHLVAAKLSLSEEQVEDYFFQLKSQKRYHEDIFGAVFPYEVKKDGAAKQPSDPRVPAAHGRS
|
1.14.13.39
|
COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250|UniProtKB:P35228}; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:P29476}; Note=Binds 1 FAD. {ECO:0000250|UniProtKB:P29476}; COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250|UniProtKB:P35228}; Note=Binds 1 FMN. {ECO:0000250|UniProtKB:P35228}; COFACTOR: Name=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin; Xref=ChEBI:CHEBI:59560; Evidence={ECO:0000250|UniProtKB:P35228}; Note=Tetrahydrobiopterin (BH4). May stabilize the dimeric form of the enzyme. {ECO:0000250|UniProtKB:P35228};
|
arginine catabolic process [GO:0006527]; defense response to bacterium [GO:0042742]; inflammatory response [GO:0006954]; negative regulation of blood pressure [GO:0045776]; nitric oxide biosynthetic process [GO:0006809]; nitric oxide mediated signal transduction [GO:0007263]; peptidyl-cysteine S-nitrosylation [GO:0018119]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of interleukin-8 production [GO:0032757]; prostaglandin secretion [GO:0032310]; regulation of cytokine production involved in inflammatory response [GO:1900015]; response to hormone [GO:0009725]; response to lipopolysaccharide [GO:0032496]; superoxide metabolic process [GO:0006801]
|
cytosol [GO:0005829]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
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calmodulin binding [GO:0005516]; flavin adenine dinucleotide binding [GO:0050660]; FMN binding [GO:0010181]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; NADP binding [GO:0050661]; nitric-oxide synthase activity [GO:0004517]
|
PF00667;PF00258;PF00175;PF02898;
|
3.40.50.360;6.10.250.410;3.90.440.10;3.40.50.80;2.40.30.10;
|
NOS family
|
PTM: Polyubiquitinated; mediated by SPSB1, SPSB2 and SPSB4, leading to proteasomal degradation. {ECO:0000250|UniProtKB:P35228}.
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SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P35228}. Note=Localizes as discrete foci scattered throughout the cytosol and in the presence of SPSB1 and SPSB4, exhibits a more diffuse cytosolic localization. {ECO:0000250|UniProtKB:P35228}.
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CATALYTIC ACTIVITY: Reaction=H(+) + 2 L-arginine + 3 NADPH + 4 O2 = 4 H2O + 2 L-citrulline + 3 NADP(+) + 2 nitric oxide; Xref=Rhea:RHEA:19897, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16480, ChEBI:CHEBI:32682, ChEBI:CHEBI:57743, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.14.13.39; Evidence={ECO:0000250|UniProtKB:P35228}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19898; Evidence={ECO:0000250|UniProtKB:P35228};
| null | null | null | null |
FUNCTION: Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In macrophages, NO mediates tumoricidal and bactericidal actions. Also has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such PTGS2/COX2. As component of the iNOS-S100A8/9 transnitrosylase complex involved in the selective inflammatory stimulus-dependent S-nitrosylation of GAPDH implicated in regulation of the GAIT complex activity and probably multiple targets including ANXA5, EZR, MSN and VIM. Involved in inflammation, enhances the synthesis of pro-inflammatory mediators such as IL6 and IL8. {ECO:0000250|UniProtKB:P35228, ECO:0000250|UniProtKB:P79290}.
|
Canis lupus familiaris (Dog) (Canis familiaris)
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O62714
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CASR_PIG
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MAFSSCCWILLALTWCTSAYGPDQRAQKKGDIILGGLFPIHFGVAAKDQNLESRPESVECIRYNFRGFRWLQAMIFAIEEINSSPALLPNMTLGYRIFDTCNTVSKALEATLSFVAQNKIDSLNLDEFCNCSEHIPSTIAVVGATGSGISTAVANLLGLFYIPQVSYASSSRLLSNKNQFKSFLRTIPNDEHQATAMADIIEYFRWNWVGTIAADDDYGRPGIEKFREEAEERDICIDFSELISQYSDEEEIQQVVEVIQNSTAKVIVVFSSGPDLEPLIKEIVRRNITGKIWLASEAWASSSLIAMPEYFHVVGGTIGFALKAGQIPGFREFLQKVHPSKSVHNGFAKEFWEETFNCHLQEGAKGPLTTDTFLRGHEEGGGRISNSSTAFRPLCTGDENISSVETPYMDYTHLRISYNVYLAVYSIAHALQDIYTCIPGRGLFTNGSCADIKKVEAWQVLKHLRHLNFTSNMGEQVTFDEYGDLAGNYSIINWHLSPEDGSIVFKEVGYYNVYAKKGERLFINEEKILWSGFSREVPFSNCSRDCLAGTRKGIIEGEPTCCFECVECPDGEYSDETDASACDKCPDDFWSNENHTSCIAKEIEFLSWTEPFGIALTLFAVLGIFLTAFVLGVFIKFRNTPIVKATNRELSYLLLFSLLCCFSSSLFFIGEPQDWTCRLRQPAFGISFVLCISCILVKTNRVLLVFEAKIPTSFHRKWWGLNLQFLLVFLCTFMQIVICAIWLYTAPPSSYRNHELEDEIIFITCHEGSLMALGFLIGYTCLLAAICFFFAFKSRKLPENFNEAKFITFSMLIFFIVWISFIPAYASTYGKFVSAVEVIAILAASFGLLACIFFNKVYIILFKPSRNTIEEVRCSTAAHAFKVAARATLRRSNVSRQRSSSLGGSTGSTPSSSISSKSNSEDPFPQPERQKKQQPLALTQHVPQPQAPSTPQPQPQLQQQPRCKQKVIFGSGTVTFSLSFDEPQKSATAHRNSTHQNSLEAQKNNDALTRHQALLPLQCGEADAELTAQETGLQGSVGGDHHPEMEDPEEMSPALVMSNSRSFVISGGGSTVTENMLHS
| null | null |
detection of calcium ion [GO:0005513]; G protein-coupled receptor signaling pathway [GO:0007186]; intracellular calcium ion homeostasis [GO:0006874]; regulation of calcium ion transport [GO:0051924]
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plasma membrane [GO:0005886]
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amino acid binding [GO:0016597]; calcium ion binding [GO:0005509]; G protein-coupled receptor activity [GO:0004930]; protein homodimerization activity [GO:0042803]
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PF00003;PF01094;PF07562;
|
3.40.50.2300;2.10.50.30;
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G-protein coupled receptor 3 family
|
PTM: N-glycosylated. {ECO:0000250|UniProtKB:P41180}.; PTM: Ubiquitinated by RNF19A; which induces proteasomal degradation. {ECO:0000250|UniProtKB:P41180}.
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SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P41180}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P41180}.
| null | null | null | null | null |
FUNCTION: G-protein-coupled receptor that senses changes in the extracellular concentration of calcium ions and plays a key role in maintaining calcium homeostasis. Senses fluctuations in the circulating calcium concentration and modulates the production of parathyroid hormone (PTH) in parathyroid glands (By similarity). The activity of this receptor is mediated by a G-protein that activates a phosphatidylinositol-calcium second messenger system. The G-protein-coupled receptor activity is activated by a co-agonist mechanism: aromatic amino acids, such as Trp or Phe, act concertedly with divalent cations, such as calcium or magnesium, to achieve full receptor activation (By similarity). {ECO:0000250|UniProtKB:P41180, ECO:0000250|UniProtKB:Q9QY96}.
|
Sus scrofa (Pig)
|
O62725
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PGH2_NEOVI
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MLARAGLLCASLSPPHAANPCCSNPCQNQGVCMSIGFDQYMCDCSRTGFYGENCSTPEFLTRVKLLLKPTPNTVHYILTHFKGVWNIVNKIPFLADVIMKYVRTSRSHCIEPPPTYNVHYAYKSWEAFSNLSYYTRALPPVADDCPTPMGVKGKKELPDSKEIVEKFLLRRKFIPDPQGTNMMFAFFAQHFTHQFFKTDHKRGPGFTKGLGHGVDLSHVYGETLDRQHKLRLFKDGKMKYQVIDGEVYPPTVKDTQVEMIYPPHVPEHLRFAVGQEVFGLVPGLMMYATIWLREHNRVCDVLKQEQGEWDDERLFRRSRLILIGETIKIVIEDYVRHLSGYHFSLKFDPELLFNQQFQYQNRIAAEFNTLYHWHPLLPDTLQIDDQEYNFQQFVYNNSILLEHGLTQFGESFSRQIAGRVAGGRNVPAAVQQEQRASIDQSRQMKYQSLNEYRKRFSVKPYASFEELTGEKEMAGELKALYQDIDAMELYPALLVEKPRPDAIFGETMVEIGAPFSLKGLMGNPICSPDYWKPSHFGGEVGFKIINTASIQSLICNNVKGCPFTAFSVQDPQLTKTVTINGSSSHSGLDDINPTVLLKERSTEL
|
1.14.99.1
|
COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250|UniProtKB:Q05769}; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit. {ECO:0000250|UniProtKB:Q05769};
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cyclooxygenase pathway [GO:0019371]; prostaglandin biosynthetic process [GO:0001516]; regulation of neuroinflammatory response [GO:0150077]; response to oxidative stress [GO:0006979]
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endoplasmic reticulum membrane [GO:0005789]; neuron projection [GO:0043005]; nuclear inner membrane [GO:0005637]; nuclear outer membrane [GO:0005640]
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heme binding [GO:0020037]; metal ion binding [GO:0046872]; oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen [GO:0016702]; peroxidase activity [GO:0004601]; prostaglandin-endoperoxide synthase activity [GO:0004666]
|
PF03098;PF00008;
|
1.10.640.10;2.10.25.10;
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Prostaglandin G/H synthase family
|
PTM: S-nitrosylation by NOS2 (iNOS) activates enzyme activity. S-nitrosylation may take place on different Cys residues in addition to Cys-526. {ECO:0000250|UniProtKB:P35354}.
|
SUBCELLULAR LOCATION: Microsome membrane {ECO:0000250|UniProtKB:P35354}; Peripheral membrane protein {ECO:0000250|UniProtKB:P35354}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P35354}; Peripheral membrane protein {ECO:0000250|UniProtKB:P35354}. Nucleus inner membrane {ECO:0000250|UniProtKB:P35354}; Peripheral membrane protein {ECO:0000250|UniProtKB:P35354}. Nucleus outer membrane {ECO:0000250|UniProtKB:P35354}; Peripheral membrane protein {ECO:0000250|UniProtKB:P35354}. Note=Detected on the lumenal side of the endoplasmic reticulum and nuclear envelope. {ECO:0000250|UniProtKB:P35354}.
|
CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + AH2 + 2 O2 = A + H2O + prostaglandin H2; Xref=Rhea:RHEA:23728, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:32395, ChEBI:CHEBI:57405; EC=1.14.99.1; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23729; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + 2 O2 = prostaglandin G2; Xref=Rhea:RHEA:42596, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:82629; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42597; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=AH2 + prostaglandin G2 = A + H2O + prostaglandin H2; Xref=Rhea:RHEA:42600, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:57405, ChEBI:CHEBI:82629; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42601; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + 2 O2 = prostaglandin G3; Xref=Rhea:RHEA:50444, ChEBI:CHEBI:15379, ChEBI:CHEBI:58562, ChEBI:CHEBI:133133; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50445; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=AH2 + prostaglandin G3 = A + H2O + prostaglandin H3; Xref=Rhea:RHEA:50448, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:133133, ChEBI:CHEBI:133134; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50449; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(8Z,11Z,14Z)-eicosatrienoate + 2 O2 = prostaglandin G1; Xref=Rhea:RHEA:50424, ChEBI:CHEBI:15379, ChEBI:CHEBI:71589, ChEBI:CHEBI:133084; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50425; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=AH2 + prostaglandin G1 = A + H2O + prostaglandin H1; Xref=Rhea:RHEA:50432, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:90793, ChEBI:CHEBI:133084; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50433; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphoethanolamine + 2 O2 = 2-(prostaglandin G2)-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:54204, ChEBI:CHEBI:15379, ChEBI:CHEBI:76091, ChEBI:CHEBI:138098; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54205; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=2-(prostaglandin G2)-sn-glycero-3-phosphoethanolamine + AH2 = 2-(prostaglandin H2)-sn-glycero-3-phosphoethanolamine + A + H2O; Xref=Rhea:RHEA:54208, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:138098, ChEBI:CHEBI:138099; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54209; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphocholine + 2 O2 = 2-(prostaglandin G2)-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:54212, ChEBI:CHEBI:15379, ChEBI:CHEBI:76079, ChEBI:CHEBI:138100; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54213; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=2-(prostaglandin G2)-sn-glycero-3-phosphocholine + AH2 = 2-(prostaglandin H2)-sn-glycero-3-phosphocholine + A + H2O; Xref=Rhea:RHEA:54216, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:138100, ChEBI:CHEBI:138101; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54217; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + AH2 = (15S)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + A + H2O; Xref=Rhea:RHEA:48856, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:57409, ChEBI:CHEBI:57446; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48857; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphocholine + AH2 + O2 = 2-[(15S)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl]-sn-glycero-3-phosphocholine + A + H2O; Xref=Rhea:RHEA:53684, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:76079, ChEBI:CHEBI:137584; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53685; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphocholine + AH2 + O2 = 2-[(15R)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl]-sn-glycero-3-phosphocholine + A + H2O; Xref=Rhea:RHEA:53680, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:76079, ChEBI:CHEBI:137583; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53681; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphocholine + AH2 + O2 = 2-[(11R)-hydroxy-(5Z,8Z,12E,14Z)-eicosatetraenoyl]-sn-glycero-3-phosphocholine + A + H2O; Xref=Rhea:RHEA:53676, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:76079, ChEBI:CHEBI:137582; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53677; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = 9-hydroxy-(10E,12Z)-octadecadienoate + A + H2O; Xref=Rhea:RHEA:50864, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:30245, ChEBI:CHEBI:133820; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50865; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = 13-hydroxy-(9Z,11E)-octadecadienoate + A + H2O; Xref=Rhea:RHEA:50860, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:30245, ChEBI:CHEBI:133819; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50861; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + AH2 + O2 = (15R)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + A + H2O; Xref=Rhea:RHEA:50856, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:32395, ChEBI:CHEBI:78837; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50857; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + AH2 + O2 = (11R)-hydroxy-(5Z,8Z,12E,14Z)-eicosatetraenoate + A + H2O; Xref=Rhea:RHEA:50852, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:32395, ChEBI:CHEBI:78836; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50853; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + AH2 + O2 = (11R)-hydroxy-(5Z,8Z,12E,14Z,17Z)-eicosapentaenoate + A + H2O; Xref=Rhea:RHEA:50848, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:58562, ChEBI:CHEBI:90820; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50849; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + AH2 + O2 = (18S)-hydroxy-(5Z,8Z,11Z,14Z,16E)-eicosapentaenoate + A + H2O; Xref=Rhea:RHEA:50200, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:58562, ChEBI:CHEBI:132083; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50201; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + AH2 + O2 = (18R)-hydroxy-(5Z,8Z,11Z,14Z,16E)-eicosapentaenoate + A + H2O; Xref=Rhea:RHEA:48836, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:58562, ChEBI:CHEBI:90818; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48837; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + AH2 + O2 = (15R)-hydroxy-(5Z,8Z,11Z,13E,17Z)-eicosapentaenoate + A + H2O; Xref=Rhea:RHEA:48840, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:58562, ChEBI:CHEBI:90819; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48841; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + AH2 + O2 = (15S)-hydroxy-(5Z,8Z,11Z,13E,17Z)-eicosapentaenoate + A + H2O; Xref=Rhea:RHEA:50196, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:58562, ChEBI:CHEBI:132087; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50197; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(7Z,10Z,13Z,16Z,19Z)-docosapentaenoate + AH2 + O2 = 13R-hydroxy-(7Z,10Z,14E,16Z,19Z)-docosapentaenoate + A + H2O; Xref=Rhea:RHEA:48852, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:77224, ChEBI:CHEBI:90824; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48853; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + AH2 + O2 = 13-hydroxy-(4Z,7Z,10Z,14E,16Z,19Z)-docosahexaenoate + A + H2O; Xref=Rhea:RHEA:48820, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:77016, ChEBI:CHEBI:90815; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48821; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(5S)-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + AH2 + O2 = (5S,15R)-dihydroxy-(6E,8Z,11Z,13E)-eicosatetraenoate + A + H2O; Xref=Rhea:RHEA:48812, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:90632, ChEBI:CHEBI:90812; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48813; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + AH2 + O2 = 17R-hydroxy-(4Z,7Z,10Z,13Z,15E,19Z)-docosahexaenoate + A + H2O; Xref=Rhea:RHEA:48816, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:77016, ChEBI:CHEBI:90814; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48817; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(5S)-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + AH2 + O2 = (5S,15S)-dihydroxy-(6E,8Z,11Z,13E)-eicosatetraenoate + A + H2O; Xref=Rhea:RHEA:48808, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:90632, ChEBI:CHEBI:90813; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48809; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(5S)-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + AH2 + O2 = (5S,11R)-dihydroxy-(6E,8Z,12E,14Z)-eicosatetraenoate + A + H2O; Xref=Rhea:RHEA:48804, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:90632, ChEBI:CHEBI:90810; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48805; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + 2 O2 = 2-glyceryl-prostaglandin G2; Xref=Rhea:RHEA:45288, ChEBI:CHEBI:15379, ChEBI:CHEBI:52392, ChEBI:CHEBI:85165; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45289; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=2-glyceryl-prostaglandin G2 + AH2 = 2-glyceryl-prostaglandin H2 + A + H2O; Xref=Rhea:RHEA:45292, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:85165, ChEBI:CHEBI:85166; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45293; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = (15R)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate; Xref=Rhea:RHEA:42284, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:82626; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42285; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = 11R-hydroperoxy-(5Z,8Z,12E,14Z)-eicosatetraenoate; Xref=Rhea:RHEA:42280, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:82628; Evidence={ECO:0000250|UniProtKB:P35354}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42281; Evidence={ECO:0000250|UniProtKB:P35354}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = (9R)-hydroxy-(10E,12Z)-octadecadienoate + A + H2O; Xref=Rhea:RHEA:75447, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:30245, ChEBI:CHEBI:77895; Evidence={ECO:0000250|UniProtKB:P79208}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75448; Evidence={ECO:0000250|UniProtKB:P79208}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = (9S)-hydroxy-(10E,12Z)-octadecadienoate + A + H2O; Xref=Rhea:RHEA:75459, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:30245, ChEBI:CHEBI:77852; Evidence={ECO:0000250|UniProtKB:P79208}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75460; Evidence={ECO:0000250|UniProtKB:P79208}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = (13S)-hydroxy-(9Z,11E)-octadecadienoate + A + H2O; Xref=Rhea:RHEA:75451, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:30245, ChEBI:CHEBI:90850; Evidence={ECO:0000250|UniProtKB:P79208}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75452; Evidence={ECO:0000250|UniProtKB:P79208}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + AH2 + O2 = (13R)-hydroxy-(9Z,11E)-octadecadienoate + A + H2O; Xref=Rhea:RHEA:75455, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499, ChEBI:CHEBI:30245, ChEBI:CHEBI:136655; Evidence={ECO:0000250|UniProtKB:P79208}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75456; Evidence={ECO:0000250|UniProtKB:P79208};
| null |
PATHWAY: Lipid metabolism; prostaglandin biosynthesis. {ECO:0000250|UniProtKB:P35354}.
| null | null |
FUNCTION: Dual cyclooxygenase and peroxidase in the biosynthesis pathway of prostanoids, a class of C20 oxylipins mainly derived from arachidonate ((5Z,8Z,11Z,14Z)-eicosatetraenoate, AA, C20:4(n-6)), with a particular role in the inflammatory response. The cyclooxygenase activity oxygenates AA to the hydroperoxy endoperoxide prostaglandin G2 (PGG2), and the peroxidase activity reduces PGG2 to the hydroxy endoperoxide prostaglandin H2 (PGH2), the precursor of all 2-series prostaglandins and thromboxanes. This complex transformation is initiated by abstraction of hydrogen at carbon 13 (with S-stereochemistry), followed by insertion of molecular O2 to form the endoperoxide bridge between carbon 9 and 11 that defines prostaglandins. The insertion of a second molecule of O2 (bis-oxygenase activity) yields a hydroperoxy group in PGG2 that is then reduced to PGH2 by two electrons. Similarly catalyzes successive cyclooxygenation and peroxidation of dihomo-gamma-linoleate (DGLA, C20:3(n-6)) and eicosapentaenoate (EPA, C20:5(n-3)) to corresponding PGH1 and PGH3, the precursors of 1- and 3-series prostaglandins. In an alternative pathway of prostanoid biosynthesis, converts 2-arachidonoyl lysophopholipids to prostanoid lysophopholipids, which are then hydrolyzed by intracellular phospholipases to release free prostanoids. Metabolizes 2-arachidonoyl glycerol yielding the glyceryl ester of PGH2, a process that can contribute to pain response. Generates lipid mediators from n-3 and n-6 polyunsaturated fatty acids (PUFAs) via a lipoxygenase-type mechanism. Oxygenates PUFAs to hydroperoxy compounds and then reduces them to corresponding alcohols. Plays a role in the generation of resolution phase interaction products (resolvins) during both sterile and infectious inflammation. Metabolizes docosahexaenoate (DHA, C22:6(n-3)) to 17R-HDHA, a precursor of the D-series resolvins (RvDs). As a component of the biosynthetic pathway of E-series resolvins (RvEs), converts eicosapentaenoate (EPA, C20:5(n-3)) primarily to 18S-HEPE that is further metabolized by ALOX5 and LTA4H to generate 18S-RvE1 and 18S-RvE2. In vascular endothelial cells, converts docosapentaenoate (DPA, C22:5(n-3)) to 13R-HDPA, a precursor for 13-series resolvins (RvTs) shown to activate macrophage phagocytosis during bacterial infection. In activated leukocytes, contributes to oxygenation of hydroxyeicosatetraenoates (HETE) to diHETES (5,15-diHETE and 5,11-diHETE). Can also use linoleate (LA, (9Z,12Z)-octadecadienoate, C18:2(n-6)) as substrate and produce hydroxyoctadecadienoates (HODEs) in a regio- and stereospecific manner, being (9R)-HODE ((9R)-hydroxy-(10E,12Z)-octadecadienoate) and (13S)-HODE ((13S)-hydroxy-(9Z,11E)-octadecadienoate) its major products (By similarity). During neuroinflammation, plays a role in neuronal secretion of specialized preresolving mediators (SPMs) 15R-lipoxin A4 that regulates phagocytic microglia (By similarity). {ECO:0000250|UniProtKB:P35354, ECO:0000250|UniProtKB:P79208, ECO:0000250|UniProtKB:Q05769}.
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Neovison vison (American mink) (Mustela vison)
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O62742
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SCP2_RABIT
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MSSSARKLAPLPRVFVVGVGMTKFVKPGTEDARDYPDMAKEAGQKALADAQIPYSAVEQACIGYVYGDSTCGQRAVYHSLGLTGIPIINVNNNCSTGSTALFMGRQLIQGGMAECVLALGFEKMERGSLGAKFPDRTNPMDKHLDVLINKYGLSAHPVAPQMFGSAGKEHMEKYGTKIEHFAKIGWKNHKHSVNNPYSQFQKEYSLDEVMSSRPIFDFLTVLQCCPTSDGAAAAILASEEFVKKYGLQSKAVEILAQEMVTDFPSSFEEKSIIKMVGFDMSKEAARRCYEKSGLRPSDIDVIELHDCFSANELLTYEALGLCPEGKGGALVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVPGAKVALQHNLGLGGAAVVTLYKMGFPEAASSFRTHQIEAAPTSSAGDGFKANLVFKEIEKKLEEEGEQFVKKIGGIFAFKVKDGPGGKEATWVVDVKNGKGSVLPNSDKKADCTITIADSDLLALMTGKMNPQSAFFQGKLKITGNMGLAMKLQNLQLQPGKAKL
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2.3.1.155; 2.3.1.16; 2.3.1.176
| null |
bile acid metabolic process [GO:0008206]; fatty acid beta-oxidation [GO:0006635]; intracellular cholesterol transport [GO:0032367]; lipid transport [GO:0006869]; regulation of phospholipid biosynthetic process [GO:0071071]
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cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; mitochondrion [GO:0005739]; peroxisomal matrix [GO:0005782]; peroxisome [GO:0005777]
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acetyl-CoA C-acyltransferase activity [GO:0003988]; acetyl-CoA C-myristoyltransferase activity [GO:0050633]; cholesterol transfer activity [GO:0120020]; lipid binding [GO:0008289]; phosphatidylcholine transfer activity [GO:0120019]; propanoyl-CoA C-acyltransferase activity [GO:0033814]; propionyl-CoA C2-trimethyltridecanoyltransferase activity [GO:0050632]
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PF02036;PF02803;PF00108;
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3.40.47.10;3.30.1050.10;
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Thiolase-like superfamily, Thiolase family
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PTM: [Isoform SCP2]: preSCP2, a protein with a molecular mass of about 15 kDa, is processed into its mature form (SCP2) by proteolytic cleavage of a 20 residue leader sequence after translocation into peroxisomes. {ECO:0000269|PubMed:9711242}.
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SUBCELLULAR LOCATION: [Isoform SCP2]: Peroxisome {ECO:0000250|UniProtKB:P32020}. Cytoplasm {ECO:0000250|UniProtKB:P22307}. Mitochondrion {ECO:0000250|UniProtKB:P22307}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P32020}. Mitochondrion {ECO:0000250|UniProtKB:P32020}.; SUBCELLULAR LOCATION: [Isoform SCPx]: Peroxisome {ECO:0000250|UniProtKB:P11915}.
|
CATALYTIC ACTIVITY: [Isoform SCPx]: Reaction=choloyl-CoA + propanoyl-CoA = 3alpha,7alpha,12alpha-trihydroxy-24-oxo-5beta-cholestan-26-oyl-CoA + CoA; Xref=Rhea:RHEA:16865, ChEBI:CHEBI:57287, ChEBI:CHEBI:57373, ChEBI:CHEBI:57392, ChEBI:CHEBI:58507; EC=2.3.1.176; Evidence={ECO:0000250|UniProtKB:P22307}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:16867; Evidence={ECO:0000250|UniProtKB:P22307}; CATALYTIC ACTIVITY: [Isoform SCPx]: Reaction=acetyl-CoA + an acyl-CoA = a 3-oxoacyl-CoA + CoA; Xref=Rhea:RHEA:21564, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:58342, ChEBI:CHEBI:90726; EC=2.3.1.16; Evidence={ECO:0000250|UniProtKB:P11915}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:21566; Evidence={ECO:0000250|UniProtKB:P11915}; CATALYTIC ACTIVITY: [Isoform SCPx]: Reaction=acetyl-CoA + hexanoyl-CoA = 3-oxooctanoyl-CoA + CoA; Xref=Rhea:RHEA:31203, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:62619, ChEBI:CHEBI:62620; Evidence={ECO:0000250|UniProtKB:P11915}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31205; Evidence={ECO:0000250|UniProtKB:P11915}; CATALYTIC ACTIVITY: [Isoform SCPx]: Reaction=acetyl-CoA + tetradecanoyl-CoA = 3-oxohexadecanoyl-CoA + CoA; Xref=Rhea:RHEA:18161, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57349, ChEBI:CHEBI:57385; EC=2.3.1.155; Evidence={ECO:0000250|UniProtKB:P11915}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18163; Evidence={ECO:0000250|UniProtKB:P11915}; CATALYTIC ACTIVITY: [Isoform SCPx]: Reaction=3-oxohexadecanedioyl-CoA + CoA = acetyl-CoA + tetradecanedioyl-CoA; Xref=Rhea:RHEA:40343, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:77081, ChEBI:CHEBI:77084; Evidence={ECO:0000250|UniProtKB:P11915}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40344; Evidence={ECO:0000250|UniProtKB:P11915}; CATALYTIC ACTIVITY: [Isoform SCPx]: Reaction=propanoyl-CoA + tetradecanoyl-CoA = 3-oxo-2-methylhexadecanoyl-CoA + CoA; Xref=Rhea:RHEA:46344, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:57392, ChEBI:CHEBI:86042; Evidence={ECO:0000250|UniProtKB:P11915}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:46346; Evidence={ECO:0000250|UniProtKB:P11915}; CATALYTIC ACTIVITY: [Isoform SCPx]: Reaction=acetyl-CoA + butanoyl-CoA = 3-oxohexanoyl-CoA + CoA; Xref=Rhea:RHEA:31111, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57371, ChEBI:CHEBI:62418; Evidence={ECO:0000250|UniProtKB:P11915}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31113; Evidence={ECO:0000250|UniProtKB:P11915}; CATALYTIC ACTIVITY: [Isoform SCPx]: Reaction=acetyl-CoA + octanoyl-CoA = 3-oxodecanoyl-CoA + CoA; Xref=Rhea:RHEA:31087, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57386, ChEBI:CHEBI:62548; Evidence={ECO:0000250|UniProtKB:P11915}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31089; Evidence={ECO:0000250|UniProtKB:P11915}; CATALYTIC ACTIVITY: [Isoform SCPx]: Reaction=acetyl-CoA + decanoyl-CoA = 3-oxododecanoyl-CoA + CoA; Xref=Rhea:RHEA:31183, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61430, ChEBI:CHEBI:62615; Evidence={ECO:0000250|UniProtKB:P11915}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31185; Evidence={ECO:0000250|UniProtKB:P11915}; CATALYTIC ACTIVITY: [Isoform SCPx]: Reaction=acetyl-CoA + dodecanoyl-CoA = 3-oxotetradecanoyl-CoA + CoA; Xref=Rhea:RHEA:31091, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57375, ChEBI:CHEBI:62543; Evidence={ECO:0000250|UniProtKB:P11915}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:31093; Evidence={ECO:0000250|UniProtKB:P11915}; CATALYTIC ACTIVITY: [Isoform SCPx]: Reaction=acetyl-CoA + hexadecanoyl-CoA = 3-oxooctadecanoyl-CoA + CoA; Xref=Rhea:RHEA:35279, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57379, ChEBI:CHEBI:71407; Evidence={ECO:0000250|UniProtKB:P11915}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:35281; Evidence={ECO:0000250|UniProtKB:P11915}; CATALYTIC ACTIVITY: [Isoform SCPx]: Reaction=3-oxo-(9Z-octadecenoyl)-CoA + CoA = (7Z)-hexadecenoyl-CoA + acetyl-CoA; Xref=Rhea:RHEA:47400, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:87695, ChEBI:CHEBI:87698; Evidence={ECO:0000250|UniProtKB:P11915}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47401; Evidence={ECO:0000250|UniProtKB:P11915}; CATALYTIC ACTIVITY: [Isoform SCPx]: Reaction=7-dehydrocholesterol(in) = 7-dehydrocholesterol(out); Xref=Rhea:RHEA:62960, ChEBI:CHEBI:17759; Evidence={ECO:0000250|UniProtKB:P11915}; CATALYTIC ACTIVITY: [Isoform SCP2]: Reaction=7-dehydrocholesterol(in) = 7-dehydrocholesterol(out); Xref=Rhea:RHEA:62960, ChEBI:CHEBI:17759; Evidence={ECO:0000305|PubMed:9711242}; CATALYTIC ACTIVITY: [Isoform SCPx]: Reaction=4,8,12-trimethyltridecanoyl-CoA + propanoyl-CoA = 3-oxopristanoyl-CoA + CoA; Xref=Rhea:RHEA:10408, ChEBI:CHEBI:57287, ChEBI:CHEBI:57291, ChEBI:CHEBI:57351, ChEBI:CHEBI:57392; EC=2.3.1.176; Evidence={ECO:0000250|UniProtKB:P11915}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10410; Evidence={ECO:0000250|UniProtKB:P11915};
| null | null | null | null |
FUNCTION: [Isoform SCPx]: Plays a crucial role in the peroxisomal oxidation of branched-chain fatty acids. Catalyzes the last step of the peroxisomal beta-oxidation of branched chain fatty acids and the side chain of the bile acid intermediates di- and trihydroxycoprostanic acids (DHCA and THCA) (By similarity). Also active with medium and long straight chain 3-oxoacyl-CoAs. Stimulates the microsomal conversion of 7-dehydrocholesterol to cholesterol and transfers phosphatidylcholine and 7-dehydrocholesterol between membrances, in vitro (By similarity). Isoforms SCP2 and SCPx cooperate in peroxisomal oxidation of certain naturally occurring tetramethyl-branched fatty acyl-CoAs (By similarity). {ECO:0000250|UniProtKB:P11915, ECO:0000250|UniProtKB:P22307, ECO:0000250|UniProtKB:P32020}.; FUNCTION: [Isoform SCP2]: Mediates the transfer of all common phospholipids, cholesterol and gangliosides from the endoplasmic reticulum to the plasma membrane (PubMed:9711242). May play a role in regulating steroidogenesis (By similarity). Stimulates the microsomal conversion of 7-dehydrocholesterol to cholesterol (By similarity). Also binds fatty acids and fatty acyl Coenzyme A (CoA) such as phytanoyl-CoA. Involved in the regulation phospholipid synthesis in endoplasmic reticulum enhancing the incorporation of exogenous fatty acid into glycerides. Seems to stimulate the rate-limiting step in phosphatidic acid formation mediated by GPAT3. Isoforms SCP2 and SCPx cooperate in peroxisomal oxidation of certain naturally occurring tetramethyl-branched fatty acyl-CoAs (By similarity). {ECO:0000250|UniProtKB:P11915, ECO:0000250|UniProtKB:P22307, ECO:0000250|UniProtKB:P32020, ECO:0000269|PubMed:9711242}.
|
Oryctolagus cuniculus (Rabbit)
|
O62743
|
CCR5_CERAT
|
MDYQVSSPTYDIDYYTSEPCQKINVKQIAARLLPPLYSLVFIFGFVGNILVVLILINCKRLKSMTDIYLLNLAISDLLFLLTVPFWAHYAAAQWDFGNTMCQLLTGLYFIGFFSGIFFIILLTIDRYLAIVHAVFALKARTVTFGVVTSVITWVVAVFASLPGIIFTRSQREGLHYTCSPHFPYSQYQFWKNFQTLKIVILGLVLPLLVMVICYSGILKTLLRCRNEKKRHRAVRLIFTIMIVYFLFWAPYNIVLLLNTFQEFFGLNNCSSSNRLDQAMQVTETLGMTHCCINPIIYAFVGEKFRNYLLVFFQKHIAKRFCKCCSIFQQEASERASSVYTRSTGEQEISVGL
| null | null |
calcium-mediated signaling [GO:0019722]; cell chemotaxis [GO:0060326]; immune response [GO:0006955]; inflammatory response [GO:0006954]; positive regulation of cytosolic calcium ion concentration [GO:0007204]
|
external side of plasma membrane [GO:0009897]
|
C-C chemokine receptor activity [GO:0016493]; chemokine (C-C motif) ligand 5 binding [GO:0071791]
|
PF00001;
|
1.20.1070.10;
|
G-protein coupled receptor 1 family
|
PTM: Sulfated on at least 2 of the N-terminal tyrosines. Sulfation is required for efficient binding of the chemokines, CCL3 and CCL4 (By similarity). {ECO:0000250|UniProtKB:P51681}.; PTM: Palmitoylation in the C-terminal is important for cell surface expression. {ECO:0000250|UniProtKB:P51681}.; PTM: Phosphorylation on serine residues in the C-terminal is stimulated by binding CC chemokines especially by APO-RANTES. {ECO:0000250|UniProtKB:P51681}.; PTM: O-glycosylated, but not N-glycosylated. Ser-6 appears to be the major site even if Ser-7 may be also O-glycosylated. Also sialylated glycans present which contribute to chemokine binding. Thr-16 and Ser-17 may also be glycosylated and, if so, with small moieties such as a T-antigen. {ECO:0000250|UniProtKB:P51681}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9XT76}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9XT76}.
| null | null | null | null | null |
FUNCTION: Receptor for a number of inflammatory CC-chemokines including CCL3/MIP-1-alpha, CCL4/MIP-1-beta and RANTES and subsequently transduces a signal by increasing the intracellular calcium ion level. May play a role in the control of granulocytic lineage proliferation or differentiation. Participates in T-lymphocyte migration to the infection site by acting as a chemotactic receptor. {ECO:0000250|UniProtKB:P51681}.
|
Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys)
|
O62747
|
CXCR4_CERAT
|
MEGISIYTSDNYTEEMGSGDYDSIKEPCFREKNAHFNRIFLPTIYSIIFLTGIVGNGLVILVMGYQKKLRSMTDKYRLHLSVADLLFVITLPFWAVDAVANWYFGNFLCKAVHVIYTVNLYSSVLILAFISLDRYLAIVHATNSQKPRKLLAEKVVYVGVWIPALLLTIPGFIFASVSEADDRFICDRFYPNDLWVVVFQFQHIMVGLILPGIVILSCYCIIISKLSHSKGHQKRKALKTTVILILAFFACWLPYYIGISIDSFILLEIIKQGCEFENTVHKWISITEALAFFHCCLNPILYAFLGAKFKTSAQHALTSVSRGSSLKILSKGKRGGHSSVSTESESSSFHSS
| null | null |
brain development [GO:0007420]; calcium-mediated signaling [GO:0019722]; cell chemotaxis [GO:0060326]; cellular response to cytokine stimulus [GO:0071345]; CXCL12-activated CXCR4 signaling pathway [GO:0038160]; immune response [GO:0006955]; neurogenesis [GO:0022008]; positive regulation of cytosolic calcium ion concentration [GO:0007204]
|
anchoring junction [GO:0070161]; early endosome [GO:0005769]; external side of plasma membrane [GO:0009897]; late endosome [GO:0005770]; lysosome [GO:0005764]; plasma membrane [GO:0005886]
|
C-C chemokine binding [GO:0019957]; C-C chemokine receptor activity [GO:0016493]; C-X-C motif chemokine 12 receptor activity [GO:0038147]
|
PF00001;PF12109;
|
1.20.1070.10;
|
G-protein coupled receptor 1 family
|
PTM: Phosphorylated on agonist stimulation. Rapidly phosphorylated on serine and threonine residues in the C-terminal. Phosphorylation at Ser-324 and Ser-325 leads to recruitment of ITCH, ubiquitination and protein degradation. {ECO:0000250|UniProtKB:P61073}.; PTM: Ubiquitinated after ligand binding, leading to its degradation. Ubiquitinated by ITCH at the cell membrane on agonist stimulation. The ubiquitin-dependent mechanism, endosomal sorting complex required for transport (ESCRT), then targets CXCR4 for lysosomal degradation. This process is dependent also on prior Ser-/Thr-phosphorylation in the C-terminal of CXCR4. Also binding of ARRB1 to STAM negatively regulates CXCR4 sorting to lysosomes though modulating ubiquitination of SFR5S. {ECO:0000250|UniProtKB:P61073}.; PTM: Sulfation is required for efficient binding of CXCL12/SDF-1alpha and promotes its dimerization. {ECO:0000250|UniProtKB:P61073}.; PTM: O- and N-glycosylated. N-glycosylation can mask coreceptor function. The O-glycosylation chondroitin sulfate attachment does not affect interaction with CXCL12/SDF-1alpha nor its coreceptor activity. {ECO:0000250|UniProtKB:P61073}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P61073}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P61073}. Cell junction {ECO:0000250}. Early endosome {ECO:0000250}. Late endosome {ECO:0000250}. Lysosome {ECO:0000250}. Note=In unstimulated cells, diffuse pattern on plasma membrane. On agonist stimulation, colocalizes with ITCH at the plasma membrane where it becomes ubiquitinated (By similarity). In the presence of antigen, distributes to the immunological synapse forming at the T-cell-APC contact area, where it localizes at the peripheral and distal supramolecular activation cluster (SMAC) (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Receptor for the C-X-C chemokine CXCL12/SDF-1 that transduces a signal by increasing intracellular calcium ion levels and enhancing MAPK1/MAPK3 activation. Involved in the AKT signaling cascade (By similarity). Plays a role in regulation of cell migration, e.g. during wound healing. Acts as a receptor for extracellular ubiquitin; leading to enhanced intracellular calcium ions and reduced cellular cAMP levels. Binds bacterial lipopolysaccharide (LPS) et mediates LPS-induced inflammatory response, including TNF secretion by monocytes (By similarity). Involved in hematopoiesis and in cardiac ventricular septum formation. Also plays an essential role in vascularization of the gastrointestinal tract, probably by regulating vascular branching and/or remodeling processes in endothelial cells. Involved in cerebellar development. In the CNS, could mediate hippocampal-neuron survival (By similarity). {ECO:0000250|UniProtKB:P61073, ECO:0000250|UniProtKB:P70658}.
|
Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys)
|
O62768
|
TRXR1_BOVIN
|
MNGSKDLPEPYDYDLIIIGGGSGGLAAAKEAAKYDKKVMVLDFVTPTPLGTRWGLGGTCVNVGCIPKKLMHQAALLGQALRDSRNYGWNVEETVKHDWERMTEAVQNHIGSLNWGYRVALREKKVTYENAYGEFVGPHRIKATNNKGKEKIYSAERFLIATGERPRYLGIPGDKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDMANKIGEHMQEHGIKFIRQFVPIKVEQIEAGTPGRLRVIAKSTDSDQTIEGEYNTVLLAIGRDACTRKIGLENVGVKINEKTGKIPVTEEEQTNVPYIYAIGDILEGKLELTPVAIQAGRLLAQRLYGGSTVKCDYENVPTTVFTPLEYGSCGLSEEKAVEKFGEENVEVYHSYFWPLEWTIPSRDNNKCYAKVVCNIKDNERVVGFHVLGPNAGEVTQGFAAALKCGLTKDQLDSTIGIHPVCAEVFTTLSVTKRSGGNILQTGCUG
|
1.11.1.2; 1.8.1.9
|
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:Q16881}; Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:Q16881};
|
cell redox homeostasis [GO:0045454]; cellular response to oxidative stress [GO:0034599]; glutathione metabolic process [GO:0006749]; response to inorganic substance [GO:0010035]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]
|
FAD binding [GO:0071949]; glutathione-disulfide reductase (NADP) activity [GO:0004362]; identical protein binding [GO:0042802]; NADPH peroxidase activity [GO:0050137]; thioredoxin-disulfide reductase (NADP) activity [GO:0004791]
|
PF07992;PF02852;
|
3.30.390.30;3.50.50.60;
|
Class-I pyridine nucleotide-disulfide oxidoreductase family
|
PTM: ISGylated. {ECO:0000250|UniProtKB:Q16881}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q16881}.
|
CATALYTIC ACTIVITY: Reaction=[thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide + H(+) + NADPH; Xref=Rhea:RHEA:20345, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.9; Evidence={ECO:0000250|UniProtKB:Q16881}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:20347; Evidence={ECO:0000250|UniProtKB:Q16881}; CATALYTIC ACTIVITY: Reaction=H(+) + H2O2 + NADPH = 2 H2O + NADP(+); Xref=Rhea:RHEA:15173, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.11.1.2; Evidence={ECO:0000250|UniProtKB:Q16881}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15174; Evidence={ECO:0000250|UniProtKB:Q16881};
| null | null | null | null |
FUNCTION: Reduces disulfideprotein thioredoxin (Trx) to its dithiol-containing form. Homodimeric flavoprotein involved in the regulation of cellular redox reactions, growth and differentiation. Contains a selenocysteine residue at the C-terminal active site that is essential for catalysis. Also has reductase activity on hydrogen peroxide (H2O2). {ECO:0000250|UniProtKB:Q16881}.
|
Bos taurus (Bovine)
|
O62772
|
CRFR1_SHEEP
|
MGRRPQLRLVKALLLLGLNSISASLQDQHCESLSLASNVSGLQCNASVDLNGTCWPQSPAGQLVVRPCLVFFYGVRYNTTSNGYRVCLANGTWAARVNHSECQEILSEGEKSKAHYHIAVIINYLGHCISLAALLVAFVLFLRLRSIRCVRNIIHWNLISAFILRNATWFVVQLTMSPEVHQSNVGWCRLVTAAYNYFHVTNFFWMFGEGCYLHTAVVLTYSTDRLRKWMFICIGWGVPFPIIVAWAIGKLYYDNEKCWFGKRPGVYTDYIYQGPMILVLLINFIFLFNIVRILMTKLRASTTSETIQYRKAVKATLVLLPLLGITYMLFFVNPGEDEVSRVVFIYFNSFLESFQGFFVSVFYCFLNSEVRSAIRKRWHRWQDKHSIRARVARAMSIPTSPTRVSFHSIKQSTAV
| null | null |
adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; cell surface receptor signaling pathway [GO:0007166]; cellular response to corticotropin-releasing hormone stimulus [GO:0071376]; corticotropin secretion [GO:0051458]; regulation of corticosterone secretion [GO:2000852]
|
endosome [GO:0005768]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]
|
corticotrophin-releasing factor receptor activity [GO:0015056]; corticotropin-releasing hormone binding [GO:0051424]; corticotropin-releasing hormone receptor activity [GO:0043404]; G protein-coupled peptide receptor activity [GO:0008528]
|
PF00002;PF02793;
|
4.10.1240.10;1.20.1070.10;
|
G-protein coupled receptor 2 family
|
PTM: C-terminal Ser or Thr residues may be phosphorylated.; PTM: Phosphorylation at Ser-301 by PKA prevents maximal coupling to Gq-protein, and thereby negatively regulates downstream signaling. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9863624}; Multi-pass membrane protein {ECO:0000269|PubMed:9863624}. Endosome {ECO:0000250}. Note=Agonist-binding promotes endocytosis.
| null | null | null | null | null |
FUNCTION: G-protein coupled receptor for CRH (corticotropin-releasing factor) and UCN (urocortin). Has high affinity for CRH and UCN. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and down-stream effectors, such as adenylate cyclase. Promotes the activation of adenylate cyclase, leading to increased intracellular cAMP levels. Inhibits the activity of the calcium channel CACNA1H. Required for normal embryonic development of the adrenal gland and for normal hormonal responses to stress. Plays a role in the response to anxiogenic stimuli. {ECO:0000269|PubMed:9863624}.
|
Ovis aries (Sheep)
|
O62786
|
GTR2_PIG
|
MTEDKITGTLVFAVLTAVLGSFQFGYDIGVINAPQQVIITHYRHVLGVPLDDRKAINSYAINSTEELPTGPYPGDPTPTSWAEEETTASASLIIMLWSLSVSIFAIGGMIASFFGGMLGDRLGRIKAMLVANILSLVGALLMWFSKLGPSHILIISGRGISGLYCGLISGLVPMYIGEIAPTKFRGAIGALHQLAIVTGILVSQIIGLDFLLGNHELWHILLGLSAVPAVLQSLMLFFCPESPRYLYIKLDEEAKARKSLKKLRGSDDVTKDITEMRKEREEASSEKKVSIIQLFTNSSYRQPILVALMLHMAQQFSGINGIFYYSTSIFQTAGISQPVYATIGVGAINTIFTALSVFLVEKAGRRSLFLIGMSGMFVCAIFMSVGLVLLDKLPWMSYVSMTAIFLFVSFFEIGPGPIPWFMVAEFFSQGPRPAALAMAAFSNWTCNFIIALCFQYIADFCGPYVFFLFAGVVLVFTLFTFFKVPETKGKSFEEIAAEFQKKSGSAQSPKAAVEMEFLGATETV
| null | null |
dehydroascorbic acid transport [GO:0070837]; fructose transmembrane transport [GO:0015755]; galactose transmembrane transport [GO:0015757]; glucose import [GO:0046323]; glucose transmembrane transport [GO:1904659]
|
brush border [GO:0005903]; membrane [GO:0016020]; plasma membrane [GO:0005886]
|
D-glucose transmembrane transporter activity [GO:0055056]; dehydroascorbic acid transmembrane transporter activity [GO:0033300]; fructose transmembrane transporter activity [GO:0005353]; galactose transmembrane transporter activity [GO:0005354]; glucose transmembrane transporter activity [GO:0005355]
|
PF00083;
|
1.20.1250.20;
|
Major facilitator superfamily, Sugar transporter (TC 2.A.1.1) family, Glucose transporter subfamily
|
PTM: N-glycosylated; required for stability and retention at the cell surface of pancreatic beta cells. {ECO:0000250|UniProtKB:P14246}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P11168}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=D-glucose(out) = D-glucose(in); Xref=Rhea:RHEA:60376, ChEBI:CHEBI:4167; Evidence={ECO:0000250|UniProtKB:P11168}; CATALYTIC ACTIVITY: Reaction=D-fructose(out) = D-fructose(in); Xref=Rhea:RHEA:60372, ChEBI:CHEBI:37721; Evidence={ECO:0000250|UniProtKB:P11168}; CATALYTIC ACTIVITY: Reaction=L-dehydroascorbate(out) = L-dehydroascorbate(in); Xref=Rhea:RHEA:60380, ChEBI:CHEBI:58539; Evidence={ECO:0000250|UniProtKB:P11168}; CATALYTIC ACTIVITY: Reaction=D-galactose(in) = D-galactose(out); Xref=Rhea:RHEA:34915, ChEBI:CHEBI:4139; Evidence={ECO:0000250|UniProtKB:P11168};
| null | null | null | null |
FUNCTION: Facilitative hexose transporter that mediates the transport of glucose, fructose and galactose. Likely mediates the bidirectional transfer of glucose across the plasma membrane of hepatocytes and is responsible for uptake of glucose by the beta cells; may comprise part of the glucose-sensing mechanism of the beta cell. May also participate with the Na(+)/glucose cotransporter in the transcellular transport of glucose in the small intestine and kidney. Also able to mediate the transport of dehydroascorbate. {ECO:0000250|UniProtKB:P11168}.
|
Sus scrofa (Pig)
|
O62806
|
MMP13_RABIT
|
MQPGVLAACLLLSWTHCWSLPLLNSNEDDDLSEEDFQFAESYLRSYYHPLNPAGILKKNAAGSMVDRLREMQSFFGLEVTGKLDDNTLAIMKQPRCGVPDVGEYNVFPRTLKWSQTNLTYRIVNYTPDLTHSEVEKAFKKAFKVWSDVTPLNFTRIHNGTADIMISFGTKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDDDETWTSSSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYTGKSHFMLPDDDVQGIQSLYGPGDEDPNPKHPKTPDKCDPSLSLDAITSLRGETMIFKDRFFWRLHPQQVDAELFLTKSFWPELPNRIDAAYEHPARDLIFIFRGKKFWAPNGYDILEGYPQKLSELGFPREVKKISAAVHFEDTGKTLFFSGNQVWSYDDTNHTMDQDYPRLIEEEFPGIGGKVDAVYEKNGYIYFFNGPIQFEYSIWSKRIVRVMPTNSLLWC
|
3.4.24.-
|
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Can bind about 5 Ca(2+) ions per subunit. {ECO:0000250}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
|
bone morphogenesis [GO:0060349]; collagen catabolic process [GO:0030574]; extracellular matrix disassembly [GO:0022617]; proteolysis [GO:0006508]
|
extracellular matrix [GO:0031012]; extracellular space [GO:0005615]
|
calcium ion binding [GO:0005509]; collagen binding [GO:0005518]; endopeptidase activity [GO:0004175]; metalloendopeptidase activity [GO:0004222]; zinc ion binding [GO:0008270]
|
PF00045;PF00413;PF01471;
|
3.40.390.10;2.110.10.10;
|
Peptidase M10A family
|
PTM: The proenzyme is activated by removal of the propeptide; this cleavage can be effected by other matrix metalloproteinases, such as MMP2, MMP3 and MMP14 and may involve several cleavage steps. Cleavage can also be autocatalytic, after partial maturation by another protease or after treatment with 4-aminophenylmercuric acetate (APMA) (in vitro) (By similarity). {ECO:0000250}.; PTM: N-glycosylated. {ECO:0000250}.; PTM: Tyrosine phosphorylated by PKDCC/VLK. {ECO:0000250|UniProtKB:P45452}.
|
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000305}. Secreted {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Plays a role in the degradation of extracellular matrix proteins including fibrillar collagen, fibronectin, TNC and ACAN. Cleaves triple helical collagens, including type I, type II and type III collagen, but has the highest activity with soluble type II collagen. Can also degrade collagen type IV, type XIV and type X. May also function by activating or degrading key regulatory proteins, such as TGFB1 and CCN2. Plays a role in wound healing, tissue remodeling, cartilage degradation, bone development, bone mineralization and ossification. Required for normal embryonic bone development and ossification. Plays a role in the healing of bone fractures via endochondral ossification. Plays a role in wound healing, probably by a mechanism that involves proteolytic activation of TGFB1 and degradation of CCN2. Plays a role in keratinocyte migration during wound healing. May play a role in cell migration and in tumor cell invasion (By similarity). {ECO:0000250}.
|
Oryctolagus cuniculus (Rabbit)
|
O62807
|
PPARG_PIG
|
MGETLGDSLIDPESDAFDTLSANISQEVTMVDTEMPFWPTNFGISSVDLSVMDDHSHSFDIKPFTTVDFSSISTPHYEDIPFPRADPMVADYKYDLKLQDYQSAIKVEPVSPPYYSEKTQLYNKPHEEPSNSLMAIECRVCGDKASGFHYGVHACEGCKGFFRRTIRLKLIYDRCDLNCRIHKKSRNKCQYCRFQKCLAVGMSHNAIRFGRMPQAEKEKLLAEISSDIDQLNPESADLRALAKHLYDSYIKSFPLTKAKARAILTGKTTDKSPFVIYDMNSLMMGEDKIKFKHITPLQEQSKEVAIRIFQGCQFRSVEAVQEITEYAKNIPGFVNLDLNDQVTLLKYGVHEIIYTMLASLMNKDGVLISEGQGFMTREFLKSLRKPFGDFMEPKFEFAVKFNALELDDSDLAIFIAVIILSGDRPGLLNVKPIEDIQDNLLQALELQLKLNHPESSQLFAKLLQKMTDLRQIVTEHVQLLQVIKKTETDMSLHPLLQEIYKDLY
| null | null |
cell differentiation [GO:0030154]; cellular response to insulin stimulus [GO:0032869]; fatty acid metabolic process [GO:0006631]; hormone-mediated signaling pathway [GO:0009755]; macrophage derived foam cell differentiation [GO:0010742]; negative regulation of cholesterol storage [GO:0010887]; negative regulation of gene expression [GO:0010629]; negative regulation of inflammatory response [GO:0050728]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of cholesterol efflux [GO:0010875]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of fatty acid metabolic process [GO:0045923]; positive regulation of intracellular cholesterol transport [GO:0032385]; positive regulation of prostaglandin biosynthetic process [GO:0031394]; positive regulation of protein secretion [GO:0050714]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of circadian rhythm [GO:0042752]; regulation of protein localization to plasma membrane [GO:1903076]; regulation of transcription by RNA polymerase II [GO:0006357]; retinoic acid receptor signaling pathway [GO:0048384]; rhythmic process [GO:0048511]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
chromatin binding [GO:0003682]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; E-box binding [GO:0070888]; nuclear receptor activity [GO:0004879]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; transcription cis-regulatory region binding [GO:0000976]; zinc ion binding [GO:0008270]
|
PF00104;PF12577;PF00105;
|
3.30.50.10;1.10.565.10;
|
Nuclear hormone receptor family, NR1 subfamily
|
PTM: Phosphorylated at basal conditions and dephosphorylated when treated with the ligand. May be dephosphorylated by PPP5C. The phosphorylated form may be inactive and dephosphorylation induces adipogenic activity (By similarity). {ECO:0000250|UniProtKB:P37231}.; PTM: Ubiquitinated by E3 ubiquitin-protein ligase complex containing FBXO9; leading to proteasomal degradation (By similarity). Ubiquitinated at Lys-251 by TRIM55 leading to proteasomal degradation (By similarity). {ECO:0000250|UniProtKB:P37231, ECO:0000250|UniProtKB:P37238}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}. Cytoplasm {ECO:0000250}. Note=Redistributed from the nucleus to the cytosol through a MAP2K1/MEK1-dependent manner. NOCT enhances its nuclear translocation (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Nuclear receptor that binds peroxisome proliferators such as hypolipidemic drugs and fatty acids. Once activated by a ligand, the nuclear receptor binds to DNA specific PPAR response elements (PPRE) and modulates the transcription of its target genes, such as acyl-CoA oxidase. It therefore controls the peroxisomal beta-oxidation pathway of fatty acids. Key regulator of adipocyte differentiation and glucose homeostasis. ARF6 acts as a key regulator of the tissue-specific adipocyte P2 (aP2) enhancer. Acts as a critical regulator of gut homeostasis by suppressing NF-kappa-B-mediated pro-inflammatory responses. Plays a role in the regulation of cardiovascular circadian rhythms by regulating the transcription of BMAL1 in the blood vessels. {ECO:0000250|UniProtKB:P37231, ECO:0000250|UniProtKB:P37238}.
|
Sus scrofa (Pig)
|
O62829
|
PPM1A_BOVIN
|
MGAFLDKPKMEKHNAQGQGNGLRYGLSSMQGWRVEMEDAHTAVIGLPSGLETWSFFAVYDGHAGSQVAKYCCEHLLDHITNNQDFKGSAGAPSVENVKNGIRTGFLEIDEHMRVMSEKKHGADRSGSTAVGVLISPQHTYFINCGDSRGLLCRNRKVYFFTQDHKPSNPLEKERIQNAGGSVMIQRVNGSLAVSRALGDFDYKCVHGKGPTEQLVSPEPEVHDIERSEEDDQFIILACDGIWDVMGNEELCDFVRSRLEVTDDLEKVCNEVVDTCLYKGSRDNMSVILICFPNAPKVSPEAVKKEEELDKYLESRVEEIIKKQGEGVPDLVHVMRTLASENIPSLPPGGELASKRNVIEAVYNRLNPYKNDDTDSTSTDDMW
|
3.1.3.16
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Note=Binds 2 magnesium or manganese ions per subunit.;
|
N-terminal protein myristoylation [GO:0006499]; negative regulation of canonical NF-kappaB signal transduction [GO:0043124]; negative regulation of non-canonical NF-kappaB signal transduction [GO:1901223]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; protein dephosphorylation [GO:0006470]
|
cytosol [GO:0005829]; membrane [GO:0016020]; nucleus [GO:0005634]
|
magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030145]; myosin phosphatase activity [GO:0017018]; phosphoprotein phosphatase activity [GO:0004721]; protein serine/threonine phosphatase activity [GO:0004722]; R-SMAD binding [GO:0070412]
|
PF00481;PF07830;
|
1.10.10.430;3.60.40.10;
|
PP2C family
|
PTM: N-myristoylation is essential for the recognition of its substrates for dephosphorylation. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P35813}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P35813}. Membrane {ECO:0000250|UniProtKB:P35813}; Lipid-anchor {ECO:0000250|UniProtKB:P35813}. Note=Weakly associates at the membrane and N-myristoylation mediates the membrane localization. {ECO:0000250|UniProtKB:P49443}.
|
CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16;
| null | null | null | null |
FUNCTION: Enzyme with a broad specificity. Negatively regulates TGF-beta signaling through dephosphorylating SMAD2 and SMAD3, resulting in their dissociation from SMAD4, nuclear export of the SMADs and termination of the TGF-beta-mediated signaling (By similarity). Dephosphorylates PRKAA1 and PRKAA2. Plays an important role in the termination of TNF-alpha-mediated NF-kappa-B activation through dephosphorylating and inactivating IKBKB/IKKB (By similarity). {ECO:0000250}.
|
Bos taurus (Bovine)
|
O62830
|
PPM1B_BOVIN
|
MGAFLDKPKTEKHNAHGAGNGLRYGLSSMQGWRVEMEDAHTAVVGIPHGLEDWSFFAVYDGHAGSRVANYCSTHLLEHITNNEDFRAAGKSGSALEPSVENVKNGIRTGFLKIDEYMRNFSDLRNGMDRSGSTAVGVMISPKHIYFINCGDSRAVLYRSGQVCFSTQDHKPCNPREKERIQNAGGSVMIQRVNGSLAVSRALGDYDYKCVDGKGPTEQLVSPEPEVYEILRAEEDEFIILACDGIWDVMSNEELCEFVKSRLEVSDDLENVCNWVVDTCLHKGSRDNMSIVLVCFSNAPKVSDEAMRKDSELDKYLESRVEEIMEKSGEEGMPDLAHVMRILSAENIPNLPPGGGLAGNIIFFRRHVIEAVYSRLNPHRESDGASDEAEESGSQGKLVEALRQMRINHRGNYRQLLEEMLTSYRLAKVEGEENPAEQAATAASSNSDAGNTVAMQESHTESKSDLAELDSCTEDAGTKMSGEKL
|
3.1.3.16
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000250};
|
N-terminal protein myristoylation [GO:0006499]; negative regulation of canonical NF-kappaB signal transduction [GO:0043124]; negative regulation of defense response to virus [GO:0050687]; negative regulation of interferon-beta production [GO:0032688]; negative regulation of non-canonical NF-kappaB signal transduction [GO:1901223]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; protein dephosphorylation [GO:0006470]
|
cytosol [GO:0005829]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleus [GO:0005634]
|
magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030145]; myosin phosphatase activity [GO:0017018]; protein serine/threonine phosphatase activity [GO:0004722]
|
PF00481;PF07830;
|
1.10.10.430;3.60.40.10;
|
PP2C family
|
PTM: Isgylation negatively regulates its activity. {ECO:0000250}.; PTM: N-myristoylation is essential for the recognition of its substrates for dephosphorylation. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P36993}. Membrane {ECO:0000250|UniProtKB:P36993}; Lipid-anchor {ECO:0000250|UniProtKB:P36993}. Note=Weakly associates at the membrane and N-myristoylation mediates the membrane localization. {ECO:0000250|UniProtKB:P36993}.
|
CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16;
| null | null | null | null |
FUNCTION: Enzyme with a broad specificity. Dephosphorylates PRKAA1 and PRKAA2. Inhibits TBK1-mediated antiviral signaling by dephosphorylating it at 'Ser-172'. Plays an important role in the termination of TNF-alpha-mediated NF-kappa-B activation through dephosphorylating and inactivating IKBKB/IKKB (By similarity). {ECO:0000250}.
|
Bos taurus (Bovine)
|
O62846
|
KAPCG_MACMU
|
MGNAAAKKDTEQETVNEFLAKARGDFLYRWGNPAQNTASSDQFERLKTLGTGSYGRVMLVRHRETGNHYAMKILDKQKVVRLKQVEHTLNEKRILQAINFPFLVKLQFSFKDNSNLYLVMEYVPGGEMFSHLRRVGRFSEPQACFYAAQVVLAFQYLHSLDLIHRDLKPENLLIDQQGYLQVTDFGFAKRVKGRTWTLCGTPEYLAPEI
|
2.7.11.11
| null |
phosphorylation [GO:0016310]; protein kinase A signaling [GO:0010737]
|
cAMP-dependent protein kinase complex [GO:0005952]; cytosol [GO:0005829]; nucleus [GO:0005634]
|
AMP-activated protein kinase activity [GO:0004679]; ATP binding [GO:0005524]; cAMP-dependent protein kinase activity [GO:0004691]; protein kinase A regulatory subunit binding [GO:0034237]; protein serine kinase activity [GO:0106310]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, AGC Ser/Thr protein kinase family, cAMP 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=2.7.11.11; 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=2.7.11.11;
| null | null | null | null |
FUNCTION: Phosphorylates a large number of substrates in the cytoplasm and the nucleus.
|
Macaca mulatta (Rhesus macaque)
|
O64390
|
HXK1_SOLTU
|
MKKVTVGAAVVGAAAVCAVAALIVNHRMRKSSKWGRAMAILREFEEKCKTQDAKLKQVADAMTVEMHAGLASEGGQSSRCLSPMSIISQLVMKLGVFYALDLGGTNFRVLRVQLGGKDGGIIHQEFAEASIPPSLMVGTSDALFDYIAAELAKFVAAEEEKFHQPPGKQRELGFHLLIPSNADFNNSGTIMRWTKGFSIDDAVGQDVVGELTKAMKEKVLDMRVSALVNDTVGTLAGGKYTQKDVAVAVILGTGTNAAYVERVQAIPKWHGPVPKSGEMVINMEWGNFRSSHLPLTEYDHALDNESLNPAEQIFEKMTSGMYLGEILRRVLTRVAEEVLAFLAMRSLQSLKDSFVLRTPDMSAMHHDTSPDLKVVGEKLKDILEISNTSLKTRKLVLSLCNIVATRGARLDAAGVLGILKKMGRDTPKQGGSERTVIAMDGGLYEHYTEYRMCLENSLKDLLGEELATSIVFVHSNDGSGIGAALLRASHSMYLEDQA
|
2.7.1.1
| null |
carbohydrate phosphorylation [GO:0046835]; glucose 6-phosphate metabolic process [GO:0051156]; glucose metabolic process [GO:0006006]; glycolytic process [GO:0006096]; intracellular glucose homeostasis [GO:0001678]; mannose metabolic process [GO:0006013]
|
chloroplast outer membrane [GO:0009707]; cytosol [GO:0005829]; mitochondrion [GO:0005739]
|
ATP binding [GO:0005524]; fructokinase activity [GO:0008865]; glucokinase activity [GO:0004340]; glucose binding [GO:0005536]; mannokinase activity [GO:0019158]
|
PF00349;PF03727;
|
3.30.420.40;3.40.367.20;
|
Hexokinase family
| null |
SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=a D-hexose + ATP = a D-hexose 6-phosphate + ADP + H(+); Xref=Rhea:RHEA:22740, ChEBI:CHEBI:4194, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:229467, ChEBI:CHEBI:456216; EC=2.7.1.1; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22741; Evidence={ECO:0000269|PubMed:10482667}; CATALYTIC ACTIVITY: Reaction=ATP + D-fructose = ADP + D-fructose 6-phosphate + H(+); Xref=Rhea:RHEA:16125, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:37721, ChEBI:CHEBI:61527, ChEBI:CHEBI:456216; EC=2.7.1.1; Evidence={ECO:0000269|PubMed:10482667}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16126; Evidence={ECO:0000269|PubMed:10482667}; CATALYTIC ACTIVITY: Reaction=ATP + D-glucose = ADP + D-glucose 6-phosphate + H(+); Xref=Rhea:RHEA:17825, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:61548, ChEBI:CHEBI:456216; EC=2.7.1.1; Evidence={ECO:0000269|PubMed:10482667}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17826; Evidence={ECO:0000269|PubMed:10482667};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.033 mM for glucose {ECO:0000269|PubMed:10482667}; KM=1.47 mM for fructose {ECO:0000269|PubMed:10482667}; KM=0.029 mM for mannose {ECO:0000269|PubMed:10482667}; Vmax=349 nmol/min/mg enzyme with glucose as substrate {ECO:0000269|PubMed:10482667}; Vmax=523 nmol/min/mg enzyme with fructose as substrate {ECO:0000269|PubMed:10482667}; Vmax=221 nmol/min/mg enzyme with mannose as substrate {ECO:0000269|PubMed:10482667}; Note=Measured in yeast lacking glucose and hexose kinase activity.;
|
PATHWAY: Carbohydrate metabolism; hexose metabolism. {ECO:0000305|PubMed:10482667}.; PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 1/4. {ECO:0000305|PubMed:10482667}.
| null | null |
FUNCTION: Fructose and glucose phosphorylating enzyme. May be involved in the phosphorylation of glucose during the export from plastids to cytosol. Seems neither to be involved in cell sugar sensing nor in carbohydrate metabolism in tuber. {ECO:0000269|PubMed:10482667}.
|
Solanum tuberosum (Potato)
|
O64392
|
WHW1_WHEAT
|
MAARPMLVVALLCAAAAAATAQQATNVRATYHYYRPAQNNWDLGAPAVSAYCATWDASKPLSWRSKYGWTAFCGPAGAHGQASCGKCLQVTNPATGAQITARIVDQCANGGLDLDWDTVFTKIDTNGIGYQQGHLNVNYQFVDCRD
|
3.1.-.-
| null |
defense response to bacterium [GO:0042742]; defense response to fungus [GO:0050832]; killing of cells of another organism [GO:0031640]; plant-type hypersensitive response [GO:0009626]
| null |
RNA nuclease activity [GO:0004540]
|
PF00967;
|
2.40.40.10;
| null | null | null | null | null | null | null | null |
FUNCTION: Shows antifungal activity towards B.cinerea and towards the wheat-specific pathogenic fungi F.culmorum and F.graminearum (groups 1 and 2). Has ribonuclease activity. {ECO:0000269|PubMed:15388335, ECO:0000269|PubMed:19647737}.
|
Triticum aestivum (Wheat)
|
O64399
|
MYB34_ARATH
|
MVRTPCCKEEGIKKGAWTPEEDQKLIAYLHLHGEGGWRTLPEKAGLKRCGKSCRLRWANYLRPDIKRGEFSPEEDDTIIKLHALKGNKWAAIATSLAGRTDNEIKNYWNTNLKKRLKQKGIDAITHKPINSTGQTGFEPKVNKPVYSSGSARLLNRVASKYAVELNRDLLTGIISGNSTVAEDSQNSGDVDSPTSTLLNKMAATSVLINTTTTYSGFSDNCSFTDEFNEFFNNEEISDIYTTVDNFGFMEELKSILSYGDASAGVIENSPEVNVADAMEFIDSWNEDDNMVGVFV
| null | null |
cellular response to sulfur starvation [GO:0010438]; defense response to insect [GO:0002213]; indole glucosinolate biosynthetic process [GO:0009759]; positive regulation of DNA-templated transcription [GO:0045893]; tryptophan biosynthetic process [GO:0000162]
|
nucleus [GO:0005634]
|
DNA-binding transcription factor activity [GO:0003700]; transcription cis-regulatory region binding [GO:0000976]
|
PF00249;
|
1.10.10.60;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Transcription factor involved in tryptophan gene activation and in indole-3-acetic acid (IAA) and indolic glucosinolates (IG) biosynthesis. Acts as a direct transcriptional activator of both Trp synthesis genes and Trp secondary metabolism genes. {ECO:0000269|PubMed:15579661, ECO:0000269|PubMed:23580754, ECO:0000269|PubMed:23943862, ECO:0000269|PubMed:9576939}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O64411
|
PAO1_MAIZE
|
MSSSPSFGLLAVAALLLALSLAQHGSLAATVGPRVIVVGAGMSGISAAKRLSEAGITDLLILEATDHIGGRMHKTNFAGINVELGANWVEGVNGGKMNPIWPIVNSTLKLRNFRSDFDYLAQNVYKEDGGVYDEDYVQKRIELADSVEEMGEKLSATLHASGRDDMSILAMQRLNEHQPNGPATPVDMVVDYYKFDYEFAEPPRVTSLQNTVPLATFSDFGDDVYFVADQRGYEAVVYYLAGQYLKTDDKSGKIVDPRLQLNKVVREIKYSPGGVTVKTEDNSVYSADYVMVSASLGVLQSDLIQFKPKLPTWKVRAIYQFDMAVYTKIFLKFPRKFWPEGKGREFFLYASSRRGYYGVWQEFEKQYPDANVLLVTVTDEESRRIEQQSDEQTKAEIMQVLRKMFPGKDVPDATDILVPRWWSDRFYKGTFSNWPVGVNRYEYDQLRAPVGRVYFTGEHTSEHYNGYVHGAYLSGIDSAEILINCAQKKMCKYHVQGKYD
|
1.5.3.14; 1.5.3.15
|
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:16331971, ECO:0000269|Ref.3}; Note=Binds 1 FAD per subunit. {ECO:0000305|Ref.3};
|
polyamine catabolic process [GO:0006598]; spermine catabolic process [GO:0046208]
|
apoplast [GO:0048046]; peroxisome [GO:0005777]; plant-type cell wall [GO:0009505]
|
flavin adenine dinucleotide binding [GO:0050660]; N1-acetylspermine:oxygen oxidoreductase (propane-1,3-diamine-forming) activity [GO:0052893]; N8-acetylspermidine:oxygen oxidoreductase (propane-1,3-diamine-forming) activity [GO:0052897]; oxidoreductase activity [GO:0016491]; polyamine oxidase activity [GO:0046592]; spermidine oxidase (propane-1,3-diamine-forming) activity [GO:0052896]; spermine oxidase (propane-1,3-diamine-forming) activity [GO:0052900]
|
PF01593;
|
3.90.660.10;3.50.50.60;
|
Flavin monoamine oxidase family
| null |
SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast {ECO:0000269|PubMed:12586904}. Secreted, cell wall {ECO:0000269|PubMed:12586904}.
|
CATALYTIC ACTIVITY: Reaction=H2O + O2 + spermidine = 4-aminobutanal + H2O2 + propane-1,3-diamine; Xref=Rhea:RHEA:25820, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:57484, ChEBI:CHEBI:57834, ChEBI:CHEBI:58264; EC=1.5.3.14; Evidence={ECO:0000269|Ref.4}; CATALYTIC ACTIVITY: Reaction=H2O + N(8)-acetylspermidine + O2 = 4-acetamidobutanal + H2O2 + propane-1,3-diamine; Xref=Rhea:RHEA:25972, ChEBI:CHEBI:7386, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:57484, ChEBI:CHEBI:58535; EC=1.5.3.15; Evidence={ECO:0000269|Ref.4}; CATALYTIC ACTIVITY: Reaction=H2O + O2 + spermine = H2O2 + N-(3-aminopropyl)-4-aminobutanal + propane-1,3-diamine; Xref=Rhea:RHEA:25824, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:45725, ChEBI:CHEBI:57484, ChEBI:CHEBI:58869; EC=1.5.3.14; Evidence={ECO:0000269|Ref.4}; CATALYTIC ACTIVITY: Reaction=H2O + N(1)-acetylspermine + O2 = H2O2 + N-(3-acetamidopropyl)-4-aminobutanal + propane-1,3-diamine; Xref=Rhea:RHEA:25996, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:57484, ChEBI:CHEBI:58101, ChEBI:CHEBI:58858; EC=1.5.3.14; Evidence={ECO:0000269|Ref.4};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=38 uM for spermine {ECO:0000269|Ref.4}; KM=40 uM for spermidine {ECO:0000269|Ref.4}; KM=62 uM for N(1)-acetylspermine {ECO:0000269|Ref.4}; KM=274 uM for N(1)-acetylspermidine {ECO:0000269|Ref.4}; KM=100 uM for dioxygen {ECO:0000269|Ref.4}; Vmax=6 umol/min/ug enzyme with spermine as substrate {ECO:0000269|Ref.4}; Vmax=70 umol/min/ug enzyme with spermidine as substrate {ECO:0000269|Ref.4}; Vmax=21 umol/min/ug enzyme with N(1)-acetylspermine as substrate {ECO:0000269|Ref.4}; Vmax=2.5 umol/min/ug enzyme with N(1)-acetylspermidine as substrate {ECO:0000269|Ref.4};
|
PATHWAY: Amine and polyamine degradation; spermine degradation. {ECO:0000305}.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5. {ECO:0000269|PubMed:16331971, ECO:0000269|Ref.4};
| null |
FUNCTION: Flavoenzyme involved in polyamine back-conversion (PubMed:16331971, Ref.4). Catalyzes the oxidation of the secondary amino group of polyamines, such as spermine, spermidine and their acetyl derivatives (PubMed:16331971, Ref.4). Plays an important role in the regulation of polyamine intracellular concentration (Probable). {ECO:0000269|PubMed:16331971, ECO:0000269|Ref.4, ECO:0000305|Ref.4}.
|
Zea mays (Maize)
|
O64425
|
RMA1_ARATH
|
MALDQSFEDAALLGELYGEGAFCFKSKKPEPITVSVPSDDTDDSNFDCNICLDSVQEPVVTLCGHLFCWPCIHKWLDVQSFSTSDEYQRHRQCPVCKSKVSHSTLVPLYGRGRCTTQEEGKNSVPKRPVGPVYRLEMPNSPYASTDLRLSQRVHFNSPQEGYYPVSGVMSSNSLSYSAVLDPVMVMVGEMVATRLFGTRVMDRFAYPDTYNLAGTSGPRMRRRIMQADKSLGRIFFFFMCCVVLCLLLF
|
2.3.2.27
| null |
protein exit from endoplasmic reticulum [GO:0032527]; protein ubiquitination [GO:0016567]; ubiquitin-dependent protein catabolic process [GO:0006511]
|
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]
|
metal ion binding [GO:0046872]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-like protein conjugating enzyme binding [GO:0044390]; ubiquitin-protein transferase activity [GO:0004842]
|
PF00097;
|
3.30.40.10;
| null | null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11329381, ECO:0000269|PubMed:19224217, ECO:0000269|PubMed:19234086}; Single-pass type IV membrane protein {ECO:0000269|PubMed:11329381, ECO:0000269|PubMed:19224217, ECO:0000269|PubMed:19234086}.
|
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 |
PATHWAY: Protein modification; protein ubiquitination.
| null | null |
FUNCTION: E3 ubiquitin-protein ligase that promotes the ubiquitination and proteasomal degradation of aquaporin PIP2-1. Forms a ubiquitin ligase complex in cooperation with the E2 enzymes UCB8/UCB10. {ECO:0000269|PubMed:11329381, ECO:0000269|PubMed:19224217, ECO:0000269|PubMed:19234086}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O64470
|
SHT_ARATH
|
MAPITFRKSYTIVPAEPTWSGRFPLAEWDQVGTITHIPTLYFYDKPSESFQGNVVEILKTSLSRVLVHFYPMAGRLRWLPRGRFELNCNAEGVEFIEAESEGKLSDFKDFSPTPEFENLMPQVNYKNPIETIPLFLAQVTKFKCGGISLSVNVSHAIVDGQSALHLISEWGRLARGEPLETVPFLDRKILWAGEPLPPFVSPPKFDHKEFDQPPFLIGETDNVEERKKKTIVVMLPLSTSQLQKLRSKANGSKHSDPAKGFTRYETVTGHVWRCACKARGHSPEQPTALGICIDTRSRMEPPLPRGYFGNATLDVVAASTSGELISNELGFAASLISKAIKNVTNEYVMIGIEYLKNQKDLKKFQDLHALGSTEGPFYGNPNLGVVSWLTLPMYGLDFGWGKEFYTGPGTHDFDGDSLILPDQNEDGSVILATCLQVAHMEAFKKHFYEDI
|
2.3.1.-
| null |
pollen development [GO:0009555]; pollen exine formation [GO:0010584]; spermidine hydroxycinnamate conjugate biosynthetic process [GO:0080088]
| null |
N-acyltransferase activity [GO:0016410]; spermidine:caffeoyl CoA N-acyltransferase activity [GO:0080074]; spermidine:coumaroyl CoA N-acyltransferase activity [GO:0080073]; spermidine:feruloyl CoA N-acyltransferase activity [GO:0080075]; spermidine:sinapoyl CoA N-acyltransferase activity [GO:0080072]
|
PF02458;
|
3.30.559.10;
|
Plant acyltransferase family
| null | null | null | null | null | null | null |
FUNCTION: Hydroxycinnamoyl transferase involved in the conjugation of feruloyl CoA to spermidine (PubMed:19077165, PubMed:19762055, PubMed:33519864). Catalyzes the three conjugating steps required for the biosynthesis of N(1),N(4),N(8)-triferuloyl-spermidine (PubMed:19077165, PubMed:33519864). Spermidine is the only acceptor substrate while feruloyl CoA > caffeoyl CoA > coumaroyl CoA > cinnamoyl CoA >> sinapoyl CoA are efficient acyl donors. No activity with hydroxyferuloyl CoA (PubMed:19077165). Required for the biosynthesis of these conjugated spermidine derivatives, specifically in anther tapetum (PubMed:22912643). {ECO:0000269|PubMed:19077165, ECO:0000269|PubMed:19762055, ECO:0000269|PubMed:22912643, ECO:0000269|PubMed:33519864}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O64471
|
MTX_ARATH
|
MEGDQETNVYTLVARKPSFDLPTACPNCLPAYIYLKLAQLPFELAFNSTFPDSDELPYFESDTYVAYNNEDGGVIEKLKKDGIVNLDSQLQSLSDYLSLKALIVSWLEEALTYEIWVGTEGISTSKIYYSDLPWVISKVLFYKQTYLAKNRLGITKENAEQREKQIYKRASEAYEALSTRLGEQKFLFEDRPSSLDAFLLSHILFIIQALPVTSVLRCKLLEHSNLVRYAEKLKSEFLEASSSSPSPPLHSFPSSFPRKSSKPKSKPKVEKTEEEKKFKKRARFFLAAQFLAVVIYVSVMGGGSSDELEYEDEDD
| null | null |
mitochondrion organization [GO:0007005]; protein targeting to mitochondrion [GO:0006626]
|
mitochondrial inner membrane [GO:0005743]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; SAM complex [GO:0001401]
| null |
PF17171;PF17172;
| null |
Metaxin family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Mitochondrion outer membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=The inner membrane localization is based on mass spectrometry identification and may be the result of sample contamination. {ECO:0000269|PubMed:14730085, ECO:0000269|PubMed:17981999}.
| null | null | null | null | null |
FUNCTION: Involved in transport of proteins into the mitochondrion. {ECO:0000269|PubMed:17981999}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O64474
|
HMA4_ARATH
|
MALQNKEEEKKKVKKLQKSYFDVLGICCTSEVPIIENILKSLDGVKEYSVIVPSRTVIVVHDSLLISPFQIAKALNEARLEANVRVNGETSFKNKWPSPFAVVSGLLLLLSFLKFVYSPLRWLAVAAVAAGIYPILAKAFASIKRPRIDINILVIITVIATLAMQDFMEAAAVVFLFTISDWLETRASYKATSVMQSLMSLAPQKAIIAETGEEVEVDEVKVDTVVAVKAGETIPIDGIVVDGNCEVDEKTLTGEAFPVPKQRDSTVWAGTINLNGYICVKTTSLAGDCVVAKMAKLVEEAQSSKTKSQRLIDKCSQYYTPAIILVSACVAIVPVIMKVHNLKHWFHLALVVLVSGCPCGLILSTPVATFCALTKAATSGLLIKSADYLDTLSKIKIVAFDKTGTITRGEFIVIDFKSLSRDINLRSLLYWVSSVESKSSHPMAATIVDYAKSVSVEPRPEEVEDYQNFPGEGIYGKIDGNDIFIGNKKIASRAGCSTVPEIEVDTKGGKTVGYVYVGERLAGFFNLSDACRSGVSQAMAELKSLGIKTAMLTGDNQAAAMHAQEQLGNVLDVVHGDLLPEDKSRIIQEFKKEGPTAMVGDGVNDAPALATADIGISMGISGSALATQTGNIILMSNDIRRIPQAVKLARRARRKVVENVCLSIILKAGILALAFAGHPLIWAAVLVDVGTCLLVIFNSMLLLREKKKIGNKKCYRASTSKLNGRKLEGDDDYVVDLEAGLLTKSGNGQCKSSCCGDKKNQENVVMMKPSSKTSSDHSHPGCCGDKKEEKVKPLVKDGCCSEKTRKSEGDMVSLSSCKKSSHVKHDLKMKGGSGCCASKNEKGKEVVAKSCCEKPKQQVESVGDCKSGHCEKKKQAEDIVVPVQIIGHALTHVEIELQTKETCKTSCCDSKEKVKETGLLLSSENTPYLEKGVLIKDEGNCKSGSENMGTVKQSCHEKGCSDEKQTGEITLASEEETDDQDCSSGCCVNEGTVKQSFDEKKHSVLVEKEGLDMETGFCCDAKLVCCGNTEGEVKEQCRLEIKKEEHCKSGCCGEEIQTGEITLVSEEETESTNCSTGCCVDKEEVTQTCHEKPASLVVSGLEVKKDEHCESSHRAVKVETCCKVKIPEACASKCRDRAKRHSGKSCCRSYAKELCSHRHHHHHHHHHHHVSA
|
7.2.2.12; 7.2.2.21
| null |
cadmium ion transport [GO:0015691]; metal ion transport [GO:0030001]; response to cadmium ion [GO:0046686]; response to cobalt ion [GO:0032025]; response to metal ion [GO:0010038]; response to zinc ion [GO:0010043]; zinc ion transport [GO:0006829]
|
plasma membrane [GO:0005886]; plasmodesma [GO:0009506]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; metal ion binding [GO:0046872]; P-type cadmium transporter activity [GO:0008551]; P-type zinc transporter activity [GO:0016463]
|
PF00122;PF00702;
|
3.30.70.100;3.40.1110.10;2.70.150.10;3.40.50.1000;
|
Cation transport ATPase (P-type) (TC 3.A.3) family, Type IB subfamily
| null |
SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O + Zn(2+)(in) = ADP + H(+) + phosphate + Zn(2+)(out); Xref=Rhea:RHEA:20621, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29105, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.12; CATALYTIC ACTIVITY: Reaction=ATP + Cd(2+)(in) + H2O = ADP + Cd(2+)(out) + H(+) + phosphate; Xref=Rhea:RHEA:12132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:48775, ChEBI:CHEBI:456216; EC=7.2.2.21;
| null | null | null | null |
FUNCTION: Involved in cadmium/zinc transport. {ECO:0000305}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O64483
|
SIRK_ARATH
|
MAMLKSLSSILFTSFALLFFLVHAQDQSGFISIDCGIPDDSSYNDETTGIKYVSDSAFVDSGTTKRIAAQFQSSGFDRHLLNVRSFPQSKRSCYDVPTPRGKGFKYLIRTRFMYGNYDDLGRVPEFDLYLGVNFWDSVKLDDATTILNKEIITIPLLDNVQVCVVDKNAGTPFLSVLEIRLLLNTTYETPYDALTLLRRLDYSKTGKLPSRYKDDIYDRIWTPRIVSSEYKILNTSLTVDQFLNNGYQPASTVMSTAETARNESLYLTLSFRPPDPNAKFYVYMHFAEIEVLKSNQTREFSIWLNEDVISPSFKLRYLLTDTFVTPDPVSGITINFSLLQPPGEFVLPPIINALEVYQVNEFLQIPTHPQDVDAMRKIKATYRVKKNWQGDPCVPVDYSWEGIDCIQSDNTTNPRVVSLNISFSELRGQIDPAFSNLTSIRKLDLSGNTLTGEIPAFLANLPNLTELNVEGNKLTGIVPQRLHERSKNGSLSLRFGRNPDLCLSDSCSNTKKKNKNGYIIPLVVVGIIVVLLTALALFRRFKKKQQRGTLGERNGPLKTAKRYFKYSEVVNITNNFERVIGKGGFGKVYHGVINGEQVAVKVLSEESAQGYKEFRAEVDLLMRVHHTNLTSLVGYCNEINHMVLIYEYMANENLGDYLAGKRSFILSWEERLKISLDAAQGLEYLHNGCKPPIVHRDVKPTNILLNEKLQAKMADFGLSRSFSVEGSGQISTVVAGSIGYLDPEYYSTRQMNEKSDVYSLGVVLLEVITGQPAIASSKTEKVHISDHVRSILANGDIRGIVDQRLRERYDVGSAWKMSEIALACTEHTSAQRPTMSQVVMELKQIVYGIVTDQENYDDSTKMLTVNLDTEMVPRAR
| null | null |
defense response to bacterium [GO:0042742]; phosphorylation [GO:0016310]
|
membrane [GO:0016020]
|
ATP binding [GO:0005524]; protein serine/threonine kinase activity [GO:0004674]
|
PF13855;PF12819;PF00069;
|
3.80.10.10;1.10.510.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family
| null |
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
| null | null | null | null | null |
FUNCTION: Involved in innate immune response of plants. {ECO:0000269|PubMed:11875555}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O64495
|
SBT12_ARATH
|
MEPKPFFLCIIFLLFCSSSSEILQKQTYIVQLHPNSETAKTFASKFDWHLSFLQEAVLGVEEEEEEPSSRLLYSYGSAIEGFAAQLTESEAEILRYSPEVVAVRPDHVLQVQTTYSYKFLGLDGFGNSGVWSKSRFGQGTIIGVLDTGVWPESPSFDDTGMPSIPRKWKGICQEGESFSSSSCNRKLIGARFFIRGHRVANSPEESPNMPREYISARDSTGHGTHTASTVGGSSVSMANVLGNGAGVARGMAPGAHIAVYKVCWFNGCYSSDILAAIDVAIQDKVDVLSLSLGGFPIPLYDDTIAIGTFRAMERGISVICAAGNNGPIESSVANTAPWVSTIGAGTLDRRFPAVVRLANGKLLYGESLYPGKGIKNAGREVEVIYVTGGDKGSEFCLRGSLPREEIRGKMVICDRGVNGRSEKGEAVKEAGGVAMILANTEINQEEDSIDVHLLPATLIGYTESVLLKAYVNATVKPKARIIFGGTVIGRSRAPEVAQFSARGPSLANPSILKPDMIAPGVNIIAAWPQNLGPTGLPYDSRRVNFTVMSGTSMSCPHVSGITALIRSAYPNWSPAAIKSALMTTADLYDRQGKAIKDGNKPAGVFAIGAGHVNPQKAINPGLVYNIQPVDYITYLCTLGFTRSDILAITHKNVSCNGILRKNPGFSLNYPSIAVIFKRGKTTEMITRRVTNVGSPNSIYSVNVKAPEGIKVIVNPKRLVFKHVDQTLSYRVWFVLKKKNRGGKVASFAQGQLTWVNSHNLMQRVRSPISVTLKTN
|
3.4.21.-
| null |
proteolysis [GO:0006508]; regulation of cell population proliferation [GO:0042127]; stomatal complex morphogenesis [GO:0010103]
|
apoplast [GO:0048046]; external side of plasma membrane [GO:0009897]
|
serine-type endopeptidase activity [GO:0004252]
|
PF17766;PF05922;PF02225;PF00082;
|
2.60.40.2310;3.50.30.30;3.30.70.80;3.40.50.200;
|
Peptidase S8 family
| null |
SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast {ECO:0000305}. Cell membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Serine protease involved in the negative regulation of stomatal density and distribution. Not active on EPFL6 (AC Q1PEY6) (PubMed:20056678). Positive regulator of water use efficiency (WUE). {ECO:0000269|PubMed:10809670, ECO:0000269|PubMed:12119372, ECO:0000269|PubMed:20056678, ECO:0000269|PubMed:21169508}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O64517
|
MCA4_ARATH
|
MTKKAVLIGINYPGTKAELRGCVNDVRRMYKCLVERYGFSEENITVLIDTDESSTQPTGKNIRRALADLVESADSGDVLVVHYSGHGTRLPAETGEDDDTGFDECIVPCDMNLITDDDFRDLVDKVPPGCRMTIISDSCHSGGLIDEAKEQIGESTKKEAEDEDESEESSSRFGFRKFLRSKVEGAIESRGFHIGGNKKDEDEAEEIETKEIELEDGETIHAKDKSLPLQTLIDILKQQTGNDNIEVGKIRPSLFDAFGDDSSPKVKKFMKVILGKLQAGNGEEGGLMGMLGKLASGFLEGKLNDEDYVKPAMQTHVGSKEEVYAGGSRGSVPLPDSGILISGCQTDQTSADATPAGKPTEAYGAMSNSIQTILEETDGEISNREMVTRARKALKKQGFTQQPGLYCHDGYANAPFIC
|
3.4.22.-
| null |
defense response [GO:0006952]; positive regulation of programmed cell death [GO:0043068]; protein autoprocessing [GO:0016540]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]; plasmodesma [GO:0009506]
|
cysteine-type endopeptidase activity [GO:0004197]; cysteine-type peptidase activity [GO:0008234]; identical protein binding [GO:0042802]
|
PF00656;
|
3.40.50.12660;
|
Peptidase C14B family
|
PTM: The two subunits are derived from the precursor sequence by an autocatalytic mechanism.
|
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:21395887}.
| null |
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=312 uM for t-butoxycarbonyl-GRR-aminomethylcoumarin (in the presence of 2 mM Ca(2+)) {ECO:0000269|PubMed:21209078}; KM=292 uM for t-butoxycarbonyl-GRR-aminomethylcoumarin (in the presence of 10 mM Ca(2+)) {ECO:0000269|PubMed:21209078}; KM=283 uM for t-butoxycarbonyl-GRR-aminomethylcoumarin (in the presence of 50 mM Ca(2+)) {ECO:0000269|PubMed:21209078}; Vmax=0.53 nmol/min/mg enzyme toward t-butoxycarbonyl-GRR-aminomethylcoumarin (in the presence of 2 mM Ca(2+)) {ECO:0000269|PubMed:21209078}; Vmax=2.28 nmol/min/mg enzyme toward t-butoxycarbonyl-GRR-aminomethylcoumarin (in the presence of 10 mM Ca(2+)) {ECO:0000269|PubMed:21209078}; Vmax=4.37 nmol/min/mg enzyme toward t-butoxycarbonyl-GRR-aminomethylcoumarin (in the presence of 50 mM Ca(2+)) {ECO:0000269|PubMed:21209078};
| null | null | null |
FUNCTION: Cysteine protease that cleaves specifically after arginine or lysine residues. Does not cleave caspase-specific substrates. Plays a positive regulatory role in biotic and abiotic stress-induced programmed cell death. {ECO:0000269|PubMed:15326173, ECO:0000269|PubMed:21209078, ECO:0000269|PubMed:21395887}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O64530
|
STR1_ARATH
|
MASTLFSRTFLAASHRLITPSLPQKIFNPATFLSRSLHSQLGSASTAYKSTTWARRAMASTGVETKAGYSTSSVSTSEPVVSVDWLHANLREPDLKILDASWYMPDEQRNPIQEYQVAHIPRALFFDLDGISDRKTSLPHMLPTEEAFAAGCSALGIDNKDEVVVYDGKGIFSAARVWWMFRVFGHEKVWVLDGGLPRWRASGYDVESSASGDAILKASAASEAIEKIYQGQTVSPITFQTKFQPHLVWTLDQVKNNMEDPTYQHIDARSKARFDGTAPEPRKGIRSGHIPGSKCIPFPQMFDSCNTLLPAEELKKRFDQEDISLDKPIMASCGTGVTACILAMGLHRLGKTDVPIYDGSWTEWATQPDLPIESVESSS
|
2.8.1.1; 2.8.1.2
| null |
embryo development ending in seed dormancy [GO:0009793]
|
chloroplast [GO:0009507]; cytosol [GO:0005829]; mitochondrion [GO:0005739]
|
3-mercaptopyruvate sulfurtransferase activity [GO:0016784]; sulfurtransferase activity [GO:0016783]; thiosulfate sulfurtransferase activity [GO:0004792]
|
PF00581;
|
3.40.250.10;
| null | null |
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:10601861, ECO:0000269|PubMed:10734224, ECO:0000269|PubMed:10951223, ECO:0000269|PubMed:15181206}.
|
CATALYTIC ACTIVITY: Reaction=hydrogen cyanide + thiosulfate = 2 H(+) + sulfite + thiocyanate; Xref=Rhea:RHEA:16881, ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:18022, ChEBI:CHEBI:18407, ChEBI:CHEBI:33542; EC=2.8.1.1; Evidence={ECO:0000269|PubMed:10601861, ECO:0000269|PubMed:10951223, ECO:0000269|PubMed:12437129, ECO:0000269|PubMed:12482606}; CATALYTIC ACTIVITY: Reaction=2-oxo-3-sulfanylpropanoate + [thioredoxin]-dithiol = [thioredoxin]-disulfide + H(+) + hydrogen sulfide + pyruvate; Xref=Rhea:RHEA:21740, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:29919, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57678; EC=2.8.1.2; Evidence={ECO:0000269|PubMed:10601861, ECO:0000269|PubMed:10951223, ECO:0000269|PubMed:12437129, ECO:0000269|PubMed:12482606};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.25 mM for thiosulfate {ECO:0000269|PubMed:10951223, ECO:0000269|PubMed:12437129, ECO:0000269|PubMed:12482606}; KM=0.7 mM for thiosulfate {ECO:0000269|PubMed:10951223, ECO:0000269|PubMed:12437129, ECO:0000269|PubMed:12482606}; KM=1.7 mM for thiosulfate {ECO:0000269|PubMed:10951223, ECO:0000269|PubMed:12437129, ECO:0000269|PubMed:12482606}; KM=3.4 mM for 3-mercaptopyruvate {ECO:0000269|PubMed:10951223, ECO:0000269|PubMed:12437129, ECO:0000269|PubMed:12482606}; KM=3.7 mM for 3-mercaptopyruvate {ECO:0000269|PubMed:10951223, ECO:0000269|PubMed:12437129, ECO:0000269|PubMed:12482606}; KM=11 mM for sodium mercaptopyruvate {ECO:0000269|PubMed:10951223, ECO:0000269|PubMed:12437129, ECO:0000269|PubMed:12482606};
| null | null | null |
FUNCTION: Catalyzes the transfer of a sulfur ion from a donor to cyanide or to other thiol compounds. Substrate preference is 3-mercaptopyruvate > thiosulfate. Involved in embryo and seed development. {ECO:0000269|PubMed:10601861, ECO:0000269|PubMed:10951223, ECO:0000269|PubMed:12437129, ECO:0000269|PubMed:12482606, ECO:0000269|PubMed:21189252}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O64587
|
ACD11_ARATH
|
MADSEADKPLRKISAAFKKLAIIVNSPNPEVPVTQFSHACSLVSPLFGCLGIAFKFAEMDYVAKVDDLVRASSSISTLVVMMDKDIEADCVRKAGSHTRNLLRVKRGLDMVKVLFEQIIASEGDNSLKDPATKSYAQVFAPHHGWAIRKAVSLGMYALPTRAHLLNMLKEDEAAAKIHMQSYVNSSAPLITYLDNLFLSKQLGIDW
| null | null |
cell death [GO:0008219]; defense response to bacterium [GO:0042742]; ER to Golgi ceramide transport [GO:0035621]; response to salicylic acid [GO:0009751]
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cytosol [GO:0005829]; membrane [GO:0016020]
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ceramide 1-phosphate binding [GO:1902387]; ceramide 1-phosphate transfer activity [GO:1902388]; sphingomyelin transfer activity [GO:0140338]
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PF08718;
|
1.10.3520.10;
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GLTP family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18845362}.
| null | null | null | null | null |
FUNCTION: Exhibits selective intermembrane transfer of ceramide-1-phosphate (C1P) and phytoceramide-1-phosphate (PubMed:24412362, PubMed:28011644). Does not transport ceramide (Cer) or GalCer, suggesting a requirement for phosphate in the headgroup for functionality (PubMed:24412362). Transports in vitro sphingosine, but not glycosphingolipids (PubMed:11850411). Has also some in vitro activity with sphingomyelin, a lipid not detected in plant tissues (PubMed:18657186). The transport function may be not directly involved in regulating cell death. Rather, perturbations in the function of ACD11 or related components could be monitored by R-proteins, which then mediate defense and programmed cell death (PCD), as proposed in the guard hypothesis (Probable). C1P transfer is stimulated by phosphatidylserine in C1P source vesicles (PubMed:28011644). Regulates autophagy, inflammasome mediated IL1B and IL18 processing, and pyroptosis, but not apoptosis (PubMed:28011644). {ECO:0000269|PubMed:11850411, ECO:0000269|PubMed:18657186, ECO:0000269|PubMed:24412362, ECO:0000269|PubMed:28011644, ECO:0000305|PubMed:18845362}.
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Arabidopsis thaliana (Mouse-ear cress)
|
O64614
|
YIP4A_ARATH
|
MSQGDTVPLHPSSQSDIDEIENLINESVQSGPGTVLAARPPSPTRPSIPVSSSSSSSPFMQSNLPPLHPSSSAQKVTHVPVPPPLPAVSNSSNFQGASAFGSPPNTLTEPVWDTVKRDLSRIVSNLKLVVFPNPYREDPGKALRDWDLWGPFFFIVFLGLTLSWSASVKKSEVFAVAFALLAAGAVILTLNVLLLGGHIIFFQSLSLLGYCLFPLDVGAVICMLKDNVILKMVVVSVTLAWSSWAAYPFMSSAVNPRRKALALYPVFLMYVSVGFLIIAIN
| null | null |
endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; pectin biosynthetic process [GO:0045489]; plant organ development [GO:0099402]; plant-type cell wall cellulose biosynthetic process [GO:0052324]; polysaccharide transport [GO:0015774]; protein transport [GO:0015031]; regulation of protein transport [GO:0051223]; root development [GO:0048364]; root hair initiation [GO:0048766]; unidimensional cell growth [GO:0009826]
|
Golgi apparatus [GO:0005794]; trans-Golgi network [GO:0005802]; trans-Golgi network membrane [GO:0032588]
|
protein homodimerization activity [GO:0042803]
|
PF04893;
| null |
YIP1 family
| null |
SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:23832588}; Multi-pass membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Together with YIP4B, involved in the regulation of cell elongation during root and hypocotyl growth (PubMed:23832588). YIP4A and YIP4B are central trafficking components in Rho-of-plant (ROPs, e.g. ARAC4/ROP2, ARAC5/ROP4 and ARAC3/ROP6) small GTPases-dependent root hair formation, thus contributing to activation and plasma membrane accumulation of ROPs during hair initiation (PubMed:30770391). The ECH/YIP4 complex is involved in the modulation of the trans-Golgi network (TGN)-mediated trafficking of some proteins and cell wall components (e.g. pectin and hemicellulose) to the cell wall in dark-grown hypocotyls and in secretory cells of the seed coat (PubMed:23832588). {ECO:0000269|PubMed:23832588, ECO:0000269|PubMed:30770391}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O64629
|
AUR3_ARATH
|
MSKKSTESDAGNTEKQWSLADFEIGRPLGKGKFGRVYLAREAKSKYIVALKVIFKEQIEKYKIHHQLRREMEIQTSLRHPNILRLFGWFHDNERIFLILEYAHGGELYGVLKQNGHLTEQQAATYIASLSQALAYCHGKCVIHRDIKPENLLLDHEGRLKIADFGWSVQSSNKRKTMCGTLDYLAPEMVENRDHDYAVDNWTLGILCYEFLYGNPPFEAESQKDTFKRILKIDLSFPLTPNVSEEAKNLISQLLVKDPSKRLSIEKIMQHPWIVKNADPKGVCASIDI
|
2.7.11.1
| null |
mitotic spindle organization [GO:0007052]; phosphorylation [GO:0016310]; regulation of cytokinesis [GO:0032465]
|
chromosome passenger complex [GO:0032133]; chromosome, centromeric region [GO:0000775]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; spindle [GO:0005819]; spindle microtubule [GO:0005876]; spindle midzone [GO:0051233]
|
ATP binding [GO:0005524]; histone H3S10 kinase activity [GO:0035175]; histone H3S28 kinase activity [GO:0044022]; protein serine kinase activity [GO:0106310]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family, Aurora subfamily
|
PTM: Phosphorylation at Thr-176 may regulate activity and degradation of AUR3 in a cell cycle dependent manner. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Nucleus. Chromosome. Chromosome, centromere. Note=Cytoplasmic perinuclear region or in dots around the nucleolus and at the nuclear periphery in interphase cells, associated to centromeric regions of condensed chromosomes at metaphase and dispersed along the entire length of the chromosomes during anaphase (PubMed:16028112). Nucleus (PubMed:15722465). {ECO:0000269|PubMed:15722465, ECO:0000269|PubMed:16028112}.
|
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: Phosphorylates in vitro histone H3 at 'Ser-10' (H3S10ph) and 'Ser-28' (H3S28ph), but not at 'Thr-3' (H3T3ph) or 'Thr-11' (H3T11ph). Colocalizes with phosphorylated histone H3 during mitosis. Associates with cytoskeletal structures that are necessary for cytokinesis and with the microtubule spindle. {ECO:0000269|PubMed:16028112, ECO:0000269|PubMed:17087760}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
O64642
|
URT1_ARATH
|
MADGGAEPPAPPSSINAGEFLLSILHGSPSPSSQGPQHHQSFALDPAIAAIGPTVNNPFPPSNWQSNGHRPSNHNPPSWPLAFSPPHNLSPNFLGFPQFPPSPFTTNQFDGNQRVSPEDAYRLGFPGTTNPAIQSMVQQQQQQQLPPPQSETRKLVFGSFSGDATQSLNGLHNGNLKYDSNQHEQLMRHPQSTLSNSNMDPNLSHHRNHDLHEQRGGHSGRGNWGHIGNNGRGLKSTPPPPPPGFSSNQRGWDMSLGSKDDDRGMGRNHDQAMGEHSKVWNQSVDFSAEANRLRGLSIQNESKFNLSQQIDHPGPPKGASLHSVSAADAADSFSMLNKEARRGGERREELGQLSKAKREGNANSDEIEDFGEDIVKSLLLEDETGEKDANDGKKDSKTSREKESRVDNRGQRLLGQKARMVKMYMACRNDIHRYDATFIAIYKSLIPAEEELEKQRQLMAHLENLVAKEWPHAKLYLYGSCANSFGFPKSDIDVCLAIEGDDINKSEMLLKLAEILESDNLQNVQALTRARVPIVKLMDPVTGISCDICINNVLAVVNTKLLRDYAQIDVRLRQLAFIVKHWAKSRRVNETYQGTLSSYAYVLMCIHFLQQRRPPILPCLQEMEPTYSVRVDNIRCTYFDNVDRLRNFGSNNRETIAELVWGFFNYWAYAHDYAYNVVSVRTGSILGKREKDWTRRVGNDRHLICIEDPFETSHDLGRVVDKFSIRVLREEFERAARIMHQDPNPCAKLLEPYIPEDNNGQGHN
|
2.7.7.52
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9NVV4}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q9NVV4};
|
miRNA catabolic process [GO:0010587]; mRNA polyadenylation [GO:0006378]; mRNA processing [GO:0006397]; negative regulation of post-transcriptional gene silencing by regulatory ncRNA [GO:1900369]; nuclear-transcribed mRNA poly(A) tail shortening [GO:0000289]; RNA 3' uridylation [GO:0071076]
|
P-body [GO:0000932]
|
metal ion binding [GO:0046872]; mRNA binding [GO:0003729]; RNA uridylyltransferase activity [GO:0050265]
|
PF03828;PF19088;
|
1.10.1410.10;3.30.460.10;
|
DNA polymerase type-B-like family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23748567}. Cytoplasm, P-body {ECO:0000269|PubMed:23748567, ECO:0000269|PubMed:25928341}. Note=The P618L single amino acid substitutiontarget URT1 to the nucleoplasm. {ECO:0000269|PubMed:25928341}.
|
CATALYTIC ACTIVITY: Reaction=RNA(n) + UTP = diphosphate + RNA(n)-3'-uridine ribonucleotide; Xref=Rhea:RHEA:14785, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17348, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:140395, ChEBI:CHEBI:173116; EC=2.7.7.52; Evidence={ECO:0000269|PubMed:23748567, ECO:0000269|PubMed:25928405};
| null | null | null | null |
FUNCTION: UTP:RNA uridylyltransferase with a marked preference for uridine polymerization and a distributive activity for the first added nucleotides (PubMed:23748567, PubMed:25928405). Uridylates oligo(A)-tailed mRNAs to prevent 3' to 5' ribonucleotytic attacks (PubMed:23748567). Reduces the accumulation of oligo(A)-tailed mRNAs (PubMed:33637717). Prevents the accumulation of excessively deadenylated mRNAs to avoid siRNA biogenesis (PubMed:26972004, PubMed:33637717). Uridylation repairs deadenylated extremities to restore the size distribution observed for non-uridylated oligo(A) tails (PubMed:26972004). Can prevent the 3' trimming of mRNAs still engaged on polysomes (PubMed:23748567). Acts synergistically with HESO1 in unmethylated miRNA uridylation, leading to their degradation (PubMed:25928341). URT1 and HESO1 prefer substrates with different 3' end nucleotides and act cooperatively to tail different forms of the same miRNAs (PubMed:25928405). URT1 and HESO1 act sequentially, with URT1 mono-uridylating the miRNAs followed by their further uridylation by HESO1 (PubMed:25928405). URT1 and HESO1 are involved in the uridylation and clearance of RISC-generated 5' mRNA fragments (PubMed:30364210). Has no effect on uridylation of heterochromatic siRNAs (PubMed:25928341). Able to act on AGO1-bound miRNAs and the uridylated species stay associated with AGO1 (PubMed:25928405). Acts as post-transcriptional gene silencing (PTGS) suppressor (PubMed:31076735). {ECO:0000269|PubMed:23748567, ECO:0000269|PubMed:25928341, ECO:0000269|PubMed:25928405, ECO:0000269|PubMed:26972004, ECO:0000269|PubMed:30364210, ECO:0000269|PubMed:31076735, ECO:0000269|PubMed:33637717}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
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