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
|
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
A2AUM9
|
CE152_MOUSE
|
MSLEFGSVALQTQNEDEEFDKEDFEREKELQQLLTDLPHDMLDDELSSPERHDSDCSMDGRAAEPHPSEHLERKWIERDILPKPHSMNCGNGWEENRSKTEDQHLGYHPGEGGDEGGSGYSPPGKREQADLYRLPEDFRPYTGGSKQAASVITFSDPQRDNFQQFGLSRGPSCGALEPYKAVYKPYRNSSVQKNSSPAQEVAASDMFEGLQQQFLGANETDSAENIHIIQLQVLNKAKERQLDSLVEKLKDSERQVRYLSHQLLIVQDEKDGLALSLRESQQLFQNGKEREMQLEAQIAALEAQVEAFRVSEEKLTKKLRTTEITLESLKQQLVELHHSESLQRAREHHESIVASLTQKHEEQVSSLQKNLDATITALQEQESICTRLKDHVQQLERNQEAVRLEKTELINRLTRSLEDSQKQCAHLLQSGSVQEVAQLQLQLQQAQKAHVLSESMNKALQEELTELKDEISLYESAAELGVLPGDSEGDLSIELTESCVDLGIKKVNWKQSKANRVTQQESPDEDPSKDELILKLKTQVQRLLTSNSVKRHLVSQLQSDLRECRETMEAFQQSKDGDSGMETKTDTSEKTTKQLWLESSEAINREDILQLKNEVQVLQKQNQELKEAEEKLRSTNQDLCNQMRQMVQEFDHDKQEAVARCERTYQQHHEAMKAQIRESLLAKHAVEKQHLLEVYEGTQSQLRSDLDKMNKEMAAVQECYLEVCREKDGLESTLRKTMEKAQEQKRQLLEAREEYVRKLKLELEEKYQETLKTERQSWLQEQAAGATQQAEKESRQKLIQQLEKEWQSKLDDSLAAWRKTTSDRGSQTEQVACPAAVSKAEAAAVLAEEQARQVQQEKELATKEALRKPEVELELKYCEIIAQKVETAVQNARSRWIQELPMLAEYKALLRAQQQEWAKQQELAVAHRLSLALSEAKEKWKSELENMKPNVMSVKELEEKVHSLQKELELKDEEVPVIVRAEVAKARTEWNKEKQEEIHKIQEQNEEDYRQFLEDHRNKINEVLAAAKEDFVKQKAELLLQKETEFQACLDQSRKEWTLQEAQQTQVEIRQYEEDTLTVLAYLLKDTQLEYGGDSQDKQLLEAMSACSSKWISVQYFEKVKACIQKALHDMLSLLTDSVASEQEKRKVVKSSADTVSWTSSEGDSAVPVPLPDSTSVRCAQSSAWLKAEAETDKKICEIKGLRCGHCFQELEKEKQECQDLRRKLEKCRRHLQHLERTHRAAVEKLGEENSRVVEELIEENHDMKNKLEALRALCRTPPRSLSAGAAESAGPSCSRQALEELRGQYIKAVRKIKRDMLRYIQESKERAAEMVKAEVLRERQETARKMRNYYLSCLQQILQDNGKEEGAEKKIMSAASKLATMAELLGTIAESDCRVRCAQAGRSVALPLASEMLTGTERSERSGVNHNIPHYVESKPNSGKTLPRSVCEQLPGRKAAPRSQRRLEESKHREMRPMASTALPSDCRCGDASCRHSGVLAKDVAPEFVPCQGEGGFDLHEKRDALGAGSEPLLYSAAHSFLGGAEKNSSPRCISESRHTTLRSPSEMPRLKALMCGSPTETDSIASEKSQGVGSQDSPVKDGVGPSSSPAWPSDSTLPCGSPAVLFLGDGSQRTQEMLGDSVQWKQFSATSCHPDAQKSNMVCRSSHTLDLPKETLHSQQGKMGATLGHPSPQSTDMLKTDFKRLSGTGPSSLCQKPLIKLTAPMPSQQDSGFDSPLE
| null | null |
cell projection organization [GO:0030030]; centriole replication [GO:0007099]; de novo centriole assembly involved in multi-ciliated epithelial cell differentiation [GO:0098535]
|
centriole [GO:0005814]; centrosome [GO:0005813]; deuterosome [GO:0098536]; nucleoplasm [GO:0005654]; pericentriolar material [GO:0000242]; procentriole [GO:0120098]; procentriole replication complex [GO:0120099]
|
protein kinase binding [GO:0019901]
| null | null |
CEP152 family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:O94986}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:O94986}. Note=Colocalizes with CDK5RAP2, WDR62 and CEP63 in a discrete ring around the proximal end of the parental centriole (By similarity). At this site, a cohesive structure is predicted to engage parental centrioles and procentrioles (By similarity). Localizes to the deuterosome (PubMed:24240477). Localizes to pericentriolar material (PCM) (By similarity). {ECO:0000250|UniProtKB:O94986, ECO:0000269|PubMed:24240477}.
| null | null | null | null | null |
FUNCTION: Necessary for centrosome duplication; the function seems also to involve CEP63, CDK5RAP2 and WDR62 through a stepwise assembled complex at the centrosome that recruits CDK2 required for centriole duplication (By similarity). Acts as a molecular scaffold facilitating the interaction of PLK4 and CENPJ, 2 molecules involved in centriole formation (By similarity). Proposed to snatch PLK4 away from PLK4:CEP92 complexes in early G1 daughter centriole and to reposition PLK4 at the outer boundary of a newly forming CEP152 ring structure (By similarity). Also plays a key role in deuterosome-mediated centriole amplification in multiciliated that can generate more than 100 centrioles (PubMed:24240477). Overexpression of cep152 can drive amplification of centrioles. {ECO:0000250|UniProtKB:O94986, ECO:0000250|UniProtKB:Q498G2, ECO:0000269|PubMed:24240477}.
|
Mus musculus (Mouse)
|
A2AUU0
|
METL8_MOUSE
|
MNVIWRSCICRLRQGKVPHRCQSGVHPVAPLGSRILTDPAKVFEHNMWDHMQWSKEEEDAARKKVEENSATRVAPEEQVKFESDANKYWDIFYQTHKNKFFKNRNWLLREFPEILPVNQNTKEKVGESSWDQVGSSISRTQGTETHCQESFVSPEPGSRGRSAPDPDLEEYSKGPGKTEPFPGSNATFRILEVGCGAGNSVFPILNTLQNIPGSFLYCCDFASEAVELVKSHESYSEAQCSAFIHDVCDDGLAYPFPDGILDVVLLVFVLSSIHPDRALFI
|
2.1.1.-
| null |
fat cell differentiation [GO:0045444]; mRNA methylation [GO:0080009]; positive regulation of mitochondrial translation [GO:0070131]; skeletal muscle tissue development [GO:0007519]; tRNA C3-cytosine methylation [GO:0106217]
|
cytoplasm [GO:0005737]; mitochondrion [GO:0005739]; nucleus [GO:0005634]
|
histone acetyltransferase activity [GO:0004402]; mRNA methyltransferase activity [GO:0008174]; tRNA (cytidine-3-)-methyltransferase activity [GO:0052735]
|
PF08242;
|
3.40.50.150;
|
Methyltransferase superfamily, METL family
| null |
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q9H825}. Cytoplasm {ECO:0000305|PubMed:15992539}. Nucleus {ECO:0000305|PubMed:15992539}. Note=Mitochondrial protein (By similarity). The cytoplasmic or nuclear localization observed by some groups is either the result of an incorrect localization caused by N-terminal tagging that interferes with mitochondrial targeting, or splice isoforms that lack the N-terminal mitochondrial transit sequence (By similarity). {ECO:0000250|UniProtKB:Q9H825}.; SUBCELLULAR LOCATION: [Isoform 5]: Nucleus {ECO:0000269|PubMed:15992539}. Note=Isoform 5 localizes to the nucleus upon cell stretch in embryonic lung progenitor cells. {ECO:0000269|PubMed:15992539}.
|
CATALYTIC ACTIVITY: Reaction=cytidine(32) in tRNA(Ser) + S-adenosyl-L-methionine = H(+) + N(3)-methylcytidine(32) in tRNA(Ser) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:50956, Rhea:RHEA-COMP:12849, Rhea:RHEA-COMP:12851, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74894, ChEBI:CHEBI:82748; Evidence={ECO:0000250|UniProtKB:Q9H825}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50957; Evidence={ECO:0000250|UniProtKB:Q9H825}; CATALYTIC ACTIVITY: Reaction=cytidine(32) in tRNA(Thr) + S-adenosyl-L-methionine = H(+) + N(3)-methylcytidine(32) in tRNA(Thr) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:50960, Rhea:RHEA-COMP:12850, Rhea:RHEA-COMP:12852, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74894, ChEBI:CHEBI:82748; Evidence={ECO:0000250|UniProtKB:Q9H825}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50961; Evidence={ECO:0000250|UniProtKB:Q9H825}; CATALYTIC ACTIVITY: Reaction=a cytidine in mRNA + S-adenosyl-L-methionine = an N(3)-methylcytidine in mRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60916, Rhea:RHEA-COMP:15145, Rhea:RHEA-COMP:15713, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74894, ChEBI:CHEBI:82748; Evidence={ECO:0000305|PubMed:28655767}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60917; Evidence={ECO:0000305|PubMed:28655767};
| null | null | null | null |
FUNCTION: Mitochondrial S-adenosyl-L-methionine-dependent methyltransferase that mediates N(3)-methylcytidine modification of residue 32 of the tRNA anticodon loop of mitochondrial tRNA(Ser)(UCN) and tRNA(Thr) (By similarity). N(3)-methylcytidine methylation modification regulates mitochondrial translation efficiency and is required for activity of the respiratory chain (By similarity). N(3)-methylcytidine methylation of mitochondrial tRNA(Ser)(UCN) requires the formation of N(6)-dimethylallyladenosine(37) (i6A37) by TRIT1 as prerequisite (By similarity). May also mediate N(3)-methylcytidine modification of mRNAs (PubMed:28655767). The existence of N(3)-methylcytidine modification on mRNAs is however unclear, and additional evidences are required to confirm the role of the N(3)-methylcytidine-specific mRNA methyltransferase activity of METTL8 in vivo (By similarity). {ECO:0000250|UniProtKB:Q9H825, ECO:0000269|PubMed:28655767}.; FUNCTION: [Isoform 5]: Overexpression in lung progenitor cells stimulates smooth muscle-specific gene expression and suppresses adipogenic gene expression. {ECO:0000269|PubMed:15992539}.; FUNCTION: [Isoform 4]: Stimulates adipogenesis. {ECO:0000269|PubMed:18710950}.; FUNCTION: [Isoform 7]: Stimulates adipogenesis. {ECO:0000269|PubMed:18710950}.
|
Mus musculus (Mouse)
|
A2AVA0
|
SVEP1_MOUSE
|
MWSRLAFCCWALALVSGWTNFQPVAPSLNFSFRLFPEASPGALGRLAVPPASSEEEAAGSKVERLGRAFRSRVRRLRELSGSLELVFLVDESSSVGQTNFLNELKFVRKLLSDFPVVSTATRVAIVTFSSKNNVVARVDYISTSRAHQHKCALLSREIPAITYRGGGTYTKGAFQQAAQILRHSRENSTKVIFLITDGYSNGGDPRPIAASLRDFGVEIFTFGIWQGNIRELNDMASTPKEEHCYLLHSFEEFEALARRALHEDLPSGSFIQEDMARCSYLCEAGKDCCDRMASCKCGTHTGQFECICEKGYYGKGLQHECTACPSGTYKPEASPGGISTCIPCPDVSHTSPPGSTSPEDCVCREGYQRSGQTCEVVHCPALKPPENGFFIQNTCKNHFNAACGVRCRPGFDLVGSSIHLCQPNGLWSGTESFCRVRTCPHLRQPKHGHISCSTAEMSYNTLCLVTCNEGYRLEGSTRLTCQGNAQWDGPEPRCVERHCATFQKPKGVIISPPSCGKQPARPGMTCQLSCRQGYILSGVREVRCATSGKWSAKVQTAVCKDVEAPQISCPNDIEAKTGEQQDSANVTWQVPTAKDNSGEKVSVHVHPAFTPPYLFPIGDVAITYTATDSSGNQASCTFYIKVIDVEPPVIDWCRSPPPIQVVEKEHPASWDEPQFSDNSGAELVITSSHTQGDMFPHGETVVWYTATDPSGNNRTCDIHIVIKGSPCEVPFTPVNGDFICAQDSAGVNCSLSCKEGYDFTEGSTEKYYCAFEDGIWRPPYSTEWPDCAIKRFANHGFKSFEMLYKTTRCDDMDLFKKFSAAFETTLGNMVPSFCNDADDIDCRLEDLTKKYCIEYNYNYENGFAIGPGGWGAGNRLDYSYDHFLDVVQETPTDVGKARSSRIKRTVPLSDPKIQLIFNITASVPLPEERNDTLELENQQRLIKTLETITNRLKSTLNKEPMYSFQLASETVVADSNSLETEKAFLFCRPGSVLRGRMCVNCPLGTSYSLEHSTCESCLMGSYQDEEGQLECKLCPPRTHTEYLHSRSVSECKAQCKQGTYSSSGLETCESCPLGTYQPEFGSRSCLLCPETTTTVKRGAVDISACGVPCPVGEFSRSGLTPCYPCPRDYYQPNAGKSFCLACPFYGTTTITGATSITDCSSFSSTFSAAEESIVPLVAPGHSQNKYEVSSQVFHECFLNPCHNSGTCQQLGRGYVCLCPPGYTGLKCETDIDECSSLPCLNGGICRDQVGGFTCECSLGYSGQICEENINECISSPCLNKGTCTDGLASYRCTCVKGYMGVHCETDVNECQSSPCLNNAVCKDQVGGFSCKCPPGFLGTRCEKNVDECLSQPCQNGATCKDGANSFRCQCPAGFTGTHCELNINECQSNPCRNQATCVDELNSYSCKCQPGFSGHRCETEQPSGFNLDFEVSGIYGYVLLDGVLPTLHAITCAFWMKSSDVINYGTPISYALEDDKDNTFLLTDYNGWVLYVNGKEKITNCPSVNDGIWHHIAITWTSTGGAWRVYIDGELSDGGTGLSIGKAIPGGGALVLGQEQDKKGEGFNPAESFVGSISQLNLWDYVLSPQQVKLLASSCPEELSRGNVLAWPDFLSGITGKVKVDSSSMFCSDCPSLEGSVPHLRPASGNRKPGSKVSLFCDPGFQMVGNPVQYCLNQGQWTQPLPHCERIRCGLPPALENGFYSAEDFHAGSTVTYQCTSGYYLLGDSRMFCTDNGSWNGISPSCLDVDECAVGSDCSEHASCLNTNGSYVCSCNPPYTGDGKNCAEPVKCKAPENPENGHSSGEIYTVGTAVTFSCDEGHELVGVSTITCLETGEWDRLRPSCEAISCGVPPVPENGGVDGSAFTYGSKVVYRCDKGYTLSGDEESACLASGSWSHSSPVCELVKCSQPEDINNGKYILSGLTYLSIASYSCENGYSLQGPSLLECTASGSWDRAPPSCQLVSCGEPPIVKDAVITGSNFTFGNTVAYTCKEGYTLAGPDTIVCQANGKWNSSNHQCLAVSCDEPPNVDHASPETAHRLFGDTAFYYCADGYSLADNSQLICNAQGNWVPPAGQAVPRCIAHFCEKPPSVSYSILESVSKAKFAAGSVVSFKCMEGFVLNTSAKIECLRGGEWSPSPLSVQCIPVRCGEPPSIANGYPSGTNYSFGAVVAYSCHKGFYIKGEKKSTCEATGQWSKPTPTCHPVSCNEPPKVENGFLEHTTGRTFESEARFQCNPGYKAAGSPVFVCQANRHWHSDAPLSCTPLNCGKPPPIQNGFLKGESFEVGSKVQFVCNEGYELVGDNSWTCQKSGKWSKKPSPKCVPTKCAEPPLLENQLVLKELASEVGVMTISCKEGHALQGPSVLKCLPSGQWNGSFPICKMVLCPSPPLIPFGVPASSGALHFGSTVKYLCVDGFFLRGSPTILCQADSTWSSPLPECVPVECPQPEEILNGIIHVQGLAYLSTTLYTCKPGFELVGNATTLCGENGQWLGGKPMCKPIECPEPKEILNGQFSSVSFQYGQTITYFCDRGFRLEGPKSLTCLETGDWDMDPPSCDAIHCSDPQPIENGFVEGADYRYGAMIIYSCFPGFQVLGHAMQTCEESGWSSSSPTCVPIDCGLPPHIDFGDCTKVRDGQGHFDQEDDMMEVPYLAHPQHLEATAKALENTKESPASHASHFLYGTMVSYSCEPGYELLGIPVLICQEDGTWNGTAPSCISIECDLPVAPENGFLHFTQTTMGSAAQYSCKPGHILEGSHLRLCLQNKQWSGTVPRCEAISCSKPNPLWNGSIKGDDYSYLGVLYYECDSGYILNGSKKRTCQENRDWDGHEPMCIPVDCGSPPVPTNGRVKGEEYTFQKEITYSCREGFILEGARSRICLTNGSWSGATPSCMPVRCPAPPQVPNGVADGLDYGFKKEVAFHCLEGYVLQGAPRLTCQSNGTWDAEVPVCKPATCGPPADLPQGFPNGFSFYHGGHIQYQCFTGYKLHGNPSRRCLPNGSWSGSSPSCLPCRCSTPIIQQGTINATDLGCGKTVQIECFKGFKLLGLSEITCDANGQWSDVPLCEHAQCGPLPTIPNAIVLEGSLSEDNVVTYSCRPGYTMQGSSDLICTEKAIWSQPYPTCEPLSCGPPPTVANAVATGEAHTYESKVKLRCLEGYVMDSDTDTFTCQQDGHWVPERITCSPKKCPVPSNMTRIRFHGDDFQVNRQVSVSCAEGFTHEGVNWSTCQPDGTWEPPFSDESCIPVVCGHPESPAHGSVVGNKHSFGSTIVYQCDPGYKLEGNRERICQENRQWSGEVAVCRENRCETPAEFPNGKAVLENTTSGPSLLFSCHRGYTLEGSPEAHCTANGTWNHLTPLCKPNPCPVPFVIPENAVLSEKEFYVDQNVSIKCREGFLLKGNGVITCSPDETWTHTNARCEKISCGPPSHVENAIARGVYYQYGDMITYSCYSGYMLEGSLRSVCLENGTWTPSPVCRAVCRFPCQNGGVCQRPNACSCPDGWMGRLCEEPICILPCLNGGRCVAPYQCDCPTGWTGSRCHTATCQSPCLNGGKCIRPNRCHCLSAWTGHDCSRKRRAGL
| null | null |
cell migration [GO:0016477]; epidermis development [GO:0008544]; epithelial cell-cell adhesion [GO:0090136]; gene expression [GO:0010467]; lymph circulation [GO:0003017]; lymph vessel development [GO:0001945]; lymph vessel morphogenesis [GO:0036303]; negative regulation of complement activation, classical pathway [GO:0045959]; negative regulation of vasoconstriction [GO:0045906]; positive regulation of platelet activation [GO:0010572]; Tie signaling pathway [GO:0048014]; tight junction organization [GO:0120193]
|
cytoplasm [GO:0005737]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; membrane [GO:0016020]; nucleus [GO:0005634]
|
calcium ion binding [GO:0005509]; chromatin binding [GO:0003682]; integrin binding [GO:0005178]; integrin binding involved in cell-matrix adhesion [GO:0098640]
|
PF00008;PF12947;PF07645;PF07699;PF12661;PF02494;PF00354;PF00084;PF00092;
|
2.60.120.200;2.10.70.10;2.60.40.10;2.10.25.10;2.10.50.10;3.40.50.410;
| null | null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22654117}. Nucleus {ECO:0000250|UniProtKB:Q4LDE5}. Cytoplasm {ECO:0000250|UniProtKB:Q4LDE5}. Membrane {ECO:0000250|UniProtKB:Q4LDE5}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q4LDE5}.
| null | null | null | null | null |
FUNCTION: Required for morphological development, cell alignment and migration of lymphatic endothelial cells during embryonic development, potentially via modulation of ANGPT2-TIE1 signaling and subsequent activation of FOXC2 transcription (PubMed:28179430). Required for embryonic lymphatic vascular development, via mediating the correct formation of the first lymphovenous contact site and tight association of the lymphatic endothelium with the venous endothelium (PubMed:28179432). Represses PRKCA-mediated L-type voltage-gated channel Ca(2+) influx and ROCK-mediated calcium sensitivity in vascular smooth muscle cells, via its interaction with integrins, thereby inhibiting vasocontraction (PubMed:35802072). Promotes platelet activation, via its interaction with PEAR1 and subsequent activation of AKT/mTOR signaling (PubMed:36792666). Plays a role in epidermal development and keratinocyte differentiation, independent of cell-cell adhesion (PubMed:27892606). May play a role in initial cell attachment of stromal osteogenic cells (PubMed:16206243). May promote myoblast cell adhesion when in the presence of integrin ITGA9:ITGB1 (PubMed:22654117). {ECO:0000269|PubMed:16206243, ECO:0000269|PubMed:22654117, ECO:0000269|PubMed:27892606, ECO:0000269|PubMed:28179430, ECO:0000269|PubMed:28179432, ECO:0000269|PubMed:35802072, ECO:0000269|PubMed:36792666}.
|
Mus musculus (Mouse)
|
A2AVJ5
|
PRR5L_MOUSE
|
MTRGLAPLLPIEFHKMGSFRRPRPRFMSSPVLSELPRFQAARQALQLSSNSAWNSVQTAVINVFKGGGLQSNELYALNESIRRLLKSELGSFITDYFQNQLLAKGLSFVEEKIKLCEGDNRIEVLAEVWDHFFTETLPTLQAIFYPVQGQELTIRQISLLGFRDLVLLKVKLGDVLLLAQSKLPSSVIQMLLILQSVHEPTGPSEGYLQLEELVKQVVSPFLSISGDRSCSGPTYSLARRHSRVRPKVTVLNYASLMTTVGRPLNEMVLTPLTEQEGEAYLEKCGSVRRHTVANAHSDIQLLAMATMMHSGLGEEAGGEDKHLLLPPSFPPPHRQCSSEPSILDSPDELELEDVASGSQEDSELNCASLS
| null | null |
cellular response to oxidative stress [GO:0034599]; negative regulation of protein phosphorylation [GO:0001933]; negative regulation of signal transduction [GO:0009968]; phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0043491]; positive regulation of intracellular protein transport [GO:0090316]; positive regulation of mRNA catabolic process [GO:0061014]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of protein phosphorylation [GO:0001934]; regulation of fibroblast migration [GO:0010762]; TORC2 signaling [GO:0038203]
|
mitochondrion [GO:0005739]; TORC2 complex [GO:0031932]
|
ubiquitin protein ligase binding [GO:0031625]
|
PF08539;
| null |
PROTOR family
|
PTM: Ubiquitinated. Ubiquitination by RFFL promotes proteasomal degradation of PRR5L thereby modifying the substrate-specific activity of the mTORC2 complex. Ubiquitination by RFFL is stimulated by LPA/lysophosphatidic acid (By similarity). {ECO:0000250}.
| null | null | null | null | null | null |
FUNCTION: Associates with the mTORC2 complex that regulates cellular processes including survival and organization of the cytoskeleton (By similarity). Regulates the activity of the mTORC2 complex in a substrate-specific manner preventing for instance the specific phosphorylation of PKCs and thereby controlling cell migration (PubMed:22609986). Plays a role in the stimulation of ZFP36-mediated mRNA decay of several ZFP36-associated mRNAs, such as TNF-alpha and GM-CSF, in response to stress. Required for ZFP36 localization to cytoplasmic stress granule (SG) and P-body (PB) in response to stress. {ECO:0000250|UniProtKB:Q6MZQ0, ECO:0000269|PubMed:22609986}.
|
Mus musculus (Mouse)
|
A2AVZ9
|
S43A3_MOUSE
|
MASKGLPLYLATLLTGLLECIGFAGVLFGWTSLLFVFKAENYFSEPCEQDCLLQSNVTGPSDLKAQDEKFSLIFTLASFMNNFMTFPTGYIFDRFKTTVARLIAIFFYTCATIIIAFTSANTAMLLFLAMPMLAVGGILFLITNLQIGNLFGKHRSTIITLYNGAFDSSSAVFLVIKLLYEQGISLRSSFIFMSVCSVWHIARTFLLMPKGHIPYPLPPNYSYGLCSRFGASKKENKAAEHETKELRSKECLPPKEENSGPEQQQQQEQQQQQQQQQEQHEQHSFRRCALSRRFILHVVWLSIIQLWHYLFIGTLNSLLTKLSGGDKVEVSAYTNAFAITQFFGVLCAPWNGLLMDRLKQKYQKAAKRTGSSSEAVALCSMVPSLALTSLLSLGFALCASIPVMQLQYATFILQVVSRSFLYGCNAAFLTLAFPSEHFGKLFGLVMALSAIVSLLQFPLFKVSPESNAVYVSMGLAIFLTLVHPFLVYRECRAEKTKSSVDA
| null | null |
hypoxanthine transport [GO:0035344]
|
basolateral plasma membrane [GO:0016323]
|
adenine transmembrane transporter activity [GO:0015207]; fatty acid transmembrane transporter activity [GO:0015245]; guanine transmembrane transporter activity [GO:0015208]; xenobiotic transmembrane transporter activity [GO:0042910]
|
PF07690;
|
1.20.1250.20;
|
SLC43A transporter (TC 2.A.1.44) family
| null |
SUBCELLULAR LOCATION: Basolateral cell membrane {ECO:0000250|UniProtKB:Q8NBI5}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=adenine(out) = adenine(in); Xref=Rhea:RHEA:71523, ChEBI:CHEBI:16708; Evidence={ECO:0000250|UniProtKB:Q8NBI5}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71524; Evidence={ECO:0000250|UniProtKB:Q8NBI5}; CATALYTIC ACTIVITY: Reaction=guanine(out) = guanine(in); Xref=Rhea:RHEA:71531, ChEBI:CHEBI:16235; Evidence={ECO:0000250|UniProtKB:Q8NBI5}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71532; Evidence={ECO:0000250|UniProtKB:Q8NBI5}; CATALYTIC ACTIVITY: Reaction=hypoxanthine(out) = hypoxanthine(in); Xref=Rhea:RHEA:71515, ChEBI:CHEBI:17368; Evidence={ECO:0000250|UniProtKB:Q8NBI5}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71516; Evidence={ECO:0000250|UniProtKB:Q8NBI5};
| null | null | null | null |
FUNCTION: Sodium-independent purine-selective nucleobase transporter which mediates the equilibrative transport of extracellular purine nucleobases such as adenine, guanine and hypoxanthine (By similarity). May regulate fatty acid (FA) transport in adipocytes, acting as a positive regulator of FA efflux and as a negative regulator of FA uptake (PubMed:32217606). {ECO:0000250|UniProtKB:Q8NBI5, ECO:0000269|PubMed:32217606}.
|
Mus musculus (Mouse)
|
A2AWL7
|
MGAP_MOUSE
|
MEEKQQIILANQDGGTVTGGAPTFFVILKQPGNGKTDQGILVTNRDARALLSRESSPGKSKEKICLPADCTVGKITVTLDNNSMWNEFHNRSTEMILTKQGRRMFPYCRYWITGLDSNLKYILVMDISPVDSHRYKWNGRWWEPSGKAEPHILGRVFIHPESPSTGHYWMHQPVSFYKLKLTNNTLDQEGHIILHSMHRYLPRLHLVPAEKATEVIQLNGPGVHTFTFPQTEFFAVTAYQNIQITQLKIDYNPFAKGFRDDGLSSKPQREGKQRNSSDQEGNSVSSSPAHRVRLTEGEGSEIHSGDFDPVLRGHEASSLSLEKAPHNVKQDFLGFMNTDSTHEVPQLKHEISESRIVNSFEDDSQISSPSNPNGNFNVVIKEEPLDDYDYELGECPEGITVKQEETDEETDVYSNSDDDPILEKQLKRHNKVDNLEADHPSYKWLPNSPGVAKAKMFKLDAGKMPVVYLEPCAVTKSTVKISELPDNMLSTSRKDKSMLAELEYLPAYIENSDGTDFCLSKDSENSLRKHSPDLRIVQKYTLLKEPNWKYPDILDNSSTERIHDSSKGSTAESFSGKEDLGKKRTTMLKMAIPSKTVTASHSASPNTPGKRGRPRKLRLSKAGRPPKNTGKSLTAAKNIPVGPGSTFPDVKPDLEDVDGVLFVSFESKEALDIHAVDGTTEEPSSLQTTTTNDSGCRTRISQLEKELIEDLKSLRHKQVIHPALQEVGLKLNSVDPTVSIDLKYLGVQLPLAPATSFPLWNVTGTNPASPDAGFPFVSRTGKTNDFTKIKGWRGKFQNASASRNEGGNSEASLKNRSAFCSDKLDEYLENEGKLMETNIGFSSNAPTSPVVYQLPTKSTSYVRTLDSVLKKQSTISPSTSHSVKPQSVTTASRKTKAQNKQTTLSGRTKSSYKSILPYPVSPKQKNSHVSQGDKITKNSLSSTSDNQVTNLVVPSVDENAFPKQISLRQAQQQHLQQQGTRPPGLSKSQVKLMDLEDCALWEGKPRTYITEERADVSLTTLLTAQASLKTKPIHTIIRKRAPPCNNDFCRLGCVCSSLALEKRQPAHCRRPDCMFGCTCLKRKVVLVKGGSKTKHFHKKAANRDPLFYDTLGEEGREGGGVREDEEQLKEKKKRKKLEYTVCEAEPEQPVRHYPLWVKVEGEVDPEPVYIPTPSVIEPIKPLVLPQPDLSSTTKGKLTPGIKPARTYTPKPNPVIREEDKDPVYLYFESMMTCARVRVYERKKEEQRQLSPPLSPSSSFQQQSSCYSSPENRVTKELDSEQTLKQLICDLEDDSDKSQEKSWKSSCNEGESSSTSYVHQRSPGGPTKLIEIISDCNWEEDRNKILSILSQHINSNMPQSLKVGSFIIELASQRKCRGEKTPPVYSSRVKISMPSSQDQDDMAEKSGSETPDGPLSPGKMDDISPVQTDALDSVRERLHGGKGLPFYAGLSPSGKLVAYKRKPSSTTSGLIQVASNAKVAASRKPRTLLPSTSNSKMASSGPATNRSGKNLKAFVPAKRPIAARPSPGGVFTQFVMSKVGALQQKIPGVRTPQPLTGPQKFSIRPSPVMVVTPVVSSEQVQVCSTVAAAVTTSPQVFLENVTAVPSLTANSDMGAKEATYSSSASTAGVVEISETNNTTLVTSTQSTATVNLTKTTGITTSPVASVSFAKPLVASPTITLPVASTASTSIVMVTTAASSSVVTTPTSSLSSVPIILSGINGSPPVSQRPENAPQIPVTTPQISSNNVKRTGPRLLHPNGQIVQLLPLHQIRGSNAQPSLQPVVFRNPGSMVGIRLPAPCKSSETPSSSASSSAFSVMSPVIQAVGSSPTVNVISQAPSLLSSGSSFVSQAGTLTLRISPPETQNLASKTGSESKITPSTGGQPVGTASLIPLQSGSFALLQLPGQKPIPSSVLQHVASLQIKKESQSTDQKDETNSIKREEETKKALPSKDKALDSEANIMKQNSGIIASENTSNNSLDDGGDLLDEETLREDARPYEYSYSTGSHTDEDKDGDEDSGNKNQNSPKEKQTVPEVRAGSKNIDIMALQSIRSIRPQKCVKVKVEPQEGSDNPENPDDFLVLSKDSKFELSGNQVKEQQSNSQAEAKKDCEDSLGKDSLRERWRKHLKGPLTQKYIGISQNFNKEANVQFFTEMKPCQENSEQDISELLGKSGTIESGGVLKTEDGSWSGISSSAAFSIIPRRATKGRRGSRHFQGHLLLPREQMKPKQQTKDGRSSAADFTVLDLEDEDEEDEKTDDSLDEIVDVVSGYQSEEVDVEKNNYVDYLEDDEQVDVETIEELSEEINFPYKKTTATHTQSFKQQCHSHISADEKASEKSRKVSLISSKLKDDCWGDKPHKETEAFAYYRRTHTANERRRRGEMRDLFEKLKITLGLLHSSKVSKSLILNRAFSEIQGLTDQADKLIGQKNLLSRKRSILIRKVSSLSGKTEEVVLKKLEYIYAKQQALEAQKRKKKLGSDEFCVSPRIGTQLEGSSASSVDLGQMLMNNRRGKPLILSRKRDQATENASPSDTPHSSANLVMTPQGQLLTLKGPLFSGPVVAVSPALLEGGLKPQVASSTMSQSENDDLFMMPRIVNVTSLAAEEDLGGMSGNKYRHEVPDGKPLDHLRDIAGSEASSLKDTERISSRGNHRDSRKALGPTQVLLANKDSGFPHVADVSTMQAAQEFIPKNMSGDVRGHRYKWKECELRGERLKSKESQFHKLKMKDLKDSSIEMELRKVASAIEEAALHPSELLTNMEDEDDTDETLTSLLNEIAFLNQQLNDDSGLAELSGSMDTEFSGDAQRAFISKLAPGNRSAFQVGHLGAGVKELPDVQEESESISPLLLHLEDDDFSENEKQLGDTASEPDVLKIVIDPEIKDSLVSHRKSSDGGQSTSGLPAEPESVSSPPILHMKTGPENSNTDTLWRPMPKLAPLGLKVANPPSDADGQSLKVMPALAPIAAKVGSIGHKMNLAGIDQEGRGSKVMPTLAPVVPKLGNSGAPSSSSGK
| null | null |
cell fate specification [GO:0001708]; cellular response to leukemia inhibitory factor [GO:1990830]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]
|
chromatin [GO:0000785]; MLL1 complex [GO:0071339]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667]
|
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]; protein dimerization activity [GO:0046983]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]
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PF00010;PF16059;PF00907;
|
4.10.280.10;2.60.40.820;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Functions as a dual-specificity transcription factor, regulating the expression of both MAX-network and T-box family target genes. Functions as a repressor or an activator. Binds to 5'-AATTTCACACCTAGGTGTGAAATT-3' core sequence and seems to regulate MYC-MAX target genes. Suppresses transcriptional activation by MYC and inhibits MYC-dependent cell transformation. Function activated by heterodimerization with MAX. This heterodimerization serves the dual function of both generating an E-box-binding heterodimer and simultaneously blocking interaction of a corepressor.
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Mus musculus (Mouse)
|
A2AWP0
|
BIRC7_MOUSE
|
MFSPADLFRAAVFSMGPESRARDSVRGPELSHREDGSGRTQEQDKPHCPCNHVLGQDCLDGQILGQLRPLSEEEESSGAAFLGEPAFPEMDSEDLRLASFYDWPSTAGIQPEPLAAAGFFHTGQQDKVRCFFCYGGLQSWERGDDPWTEHARWFPRCQFLLRSKGRDFVERIQTYTPLLGSWDQREEPEDAVSATPSAPAHGSPELLRSRRETQPEDVSEPGAKDVQEQLRQLQEERRCKVCLDRAVSIVFVPCGHFVCTECAPNLQLCPICRVPICSCVRTFLS
|
2.3.2.27
| null |
apoptotic process [GO:0006915]; lens development in camera-type eye [GO:0002088]; negative regulation of apoptotic process [GO:0043066]; negative regulation of necroptotic process [GO:0060546]; negative regulation of tumor necrosis factor-mediated signaling pathway [GO:0010804]; positive regulation of JNK cascade [GO:0046330]; positive regulation of protein ubiquitination [GO:0031398]; protein ubiquitination [GO:0016567]; regulation of cell cycle [GO:0051726]; regulation of cell population proliferation [GO:0042127]; regulation of natural killer cell apoptotic process [GO:0070247]
|
centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
cysteine-type endopeptidase inhibitor activity [GO:0004869]; cysteine-type endopeptidase inhibitor activity involved in apoptotic process [GO:0043027]; metal ion binding [GO:0046872]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]
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PF00653;PF13920;
|
3.30.40.10;
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IAP family
|
PTM: Autoubiquitinated and undergoes proteasome-mediated degradation. {ECO:0000250|UniProtKB:Q96CA5}.; PTM: The truncated protein (tLivin) not only loses its anti-apoptotic effect but also acquires a pro-apoptotic effect. {ECO:0000250|UniProtKB:Q96CA5}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96CA5}. Cytoplasm {ECO:0000250|UniProtKB:Q96CA5}. Golgi apparatus {ECO:0000250|UniProtKB:Q96CA5}. Note=Nuclear, and in a filamentous pattern throughout the cytoplasm. Full-length livin is detected exclusively cytoplasm, whereas the truncated form (tLivin) is found in the peri-nuclear region with marked localization to the Golgi apparatus; the accumulation of tLivin in the nucleus shows positive correlation with the increase in apoptosis. {ECO:0000250|UniProtKB:Q96CA5}.
|
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; Evidence={ECO:0000250|UniProtKB:Q96CA5};
| null | null | null | null |
FUNCTION: Apoptotic regulator capable of exerting proapoptotic and anti-apoptotic activities and plays crucial roles in apoptosis, cell proliferation, and cell cycle control. Its anti-apoptotic activity is mediated through the inhibition of CASP3, CASP7 and CASP9, as well as by its E3 ubiquitin-protein ligase activity. As it is a weak caspase inhibitor, its anti-apoptotic activity is thought to be due to its ability to ubiquitinate DIABLO/SMAC targeting it for degradation thereby promoting cell survival. May contribute to caspase inhibition, by blocking the ability of DIABLO/SMAC to disrupt XIAP/BIRC4-caspase interactions. Protects against apoptosis induced by TNF or by chemical agents such as adriamycin, etoposide or staurosporine. Suppression of apoptosis is mediated by activation of MAPK8/JNK1, and possibly also of MAPK9/JNK2. This activation depends on TAB1 and MAP3K7/TAK1. In vitro, inhibits CASP3 and proteolytic activation of pro-CASP9. {ECO:0000250|UniProtKB:Q96CA5}.
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Mus musculus (Mouse)
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A2AX52
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CO6A4_MOUSE
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MGTWKTFWLIISLAAGLGFVKSQRIVCREASVGDIVFLVHNSINPQHAHSVRNFLYILANSLQVGRDNIRVGLAQYSDTPTSEFLLSVYHRKGDVLKHIRGLQFKPGGNRMGQALQFILEHHFREGAGSRASQGVPQVAVVVSSGLTEDHIREPAEALRRAGILVYAIGVKDASQAELREISSSPKDNFTFFVPNFPGLPGLAQKLRPELCSTLGKAAQYTERESPACSEASPADIVFLVDSSTSIGLQNFQKVKHFLHSVVSGLDVRSDQVQVGLVQYSDNIYPAFPLKQSSLKSAVLDRIRNLPYSMGGTSTGSALEFIRANSLTEMSGSRAKDGVPQIVVLVTDGESSDEVQDVADQLKRDGVFVFVVGINIQDVQELQKIANEPFEEFLFTTENFSILQALSGTLLQALCSTVERQMKKSTKTYADVVFLIDTSQGTSQASFQWMQNFISRIIGILEVGQDKYQIGLAQYSDQGHTEFLFNTHKTRNEMVAHIHELLVFQGGSRKTGQGLRFLHRTFFQEAAGSRLLQGVPQYVVVITSGKSEDEVGEVAQILRKRGVDIVSVGLQDFDRAELEGIGPVVLVSDLQGEDRIRQLMLDVNMFIQGSPKPPRVMTDVAKDAVEECLVPVPADLVFLVEDFSSARQPNFQRVVHFLTTTVHSLNIHPDTTRVSLVFYSEKPRLEFSLDMYQSAAQVLRHLDRLTFRARRGRAKAGAALDFLRKEVFLPEKGSRPHRGVQQIAVVIIESPSLDNVSTPASYLRRAGVTIYAAGTQPASESKDLEKIVTYPPWKHAIRLESFLQLSVVGNKLKKKLCPEMLSGMPPLMSFIPESTRQSTQEGCESVEKADIYFLIDGSGSIKPNDFIEMKDFMKEVIKMFHIGPDRVRFGVVQYSDKIISQFFLTQYASMAGLSAAIDNIQQVGGGTTTGKALSKMVPVFQNTARIDVARYLIVITDGQSTDPVAEAAQGLRDIGVNIYAIGVRDANTTELEEIASKKMFFIYEFDSLKSIHQEVIRDICSSENCKSQKADIIFLIDGSESIAPKDFEKMKDFMERMVNQSNIGADEIQIGLLQFSSNPQEEFRLNRYSSKVDMCRAILSVQQMSDGTHTGKALNFTLPFFDSSRGGRPRVHQYLIVITDGVSQDNVAPPAKALRDRNIIIFAIGVGNVQRAQLLEITNDQDKVFQEENFESLQSLEKEILSEVCSSQGCNIDLSVGVDTSTSSERAQQELRRLLPELMQQLAFLSNISCEAPGQMEPRFRYVVPGSSDQPVFDSGFEKYSDETIQKFLVHQGSVNNRMDVDFLQSLGETAIHLSLAKVKVLLVFTDGLDEDLERLRRTSEFLRSRGLSGLLLIGLGGAHKLEELQELEFGRGFAYRQPLSSSLPSLPSVLLKQLDTIVERTCCNMYAKCYGDDGIRGEPGSRGEQGERGLDGLPGHPGEEGDHGQRGPRGLPGLRGEEGCPGVRGPKGARGFSGEKGNPGEEGVGGLDGEQGDRGAAGPSGEKGSSGSRGLTGLPGPAGPRGEPGLRGDPGDPGIDNLIQGPKGEKGRRGHQGSPGFHGPLGEAGSVGPRGSLGRHGLPGLKGVLGETGELGSRGEPGHPGPQGPRGRQGPPGFFGQKGDPGTQGNPGLPGPSGSKGPDGPRGLKGEVGPAGERGPRGQQGPRGQPGLFGPDGHGYPGRKGRKGEPGFPGYPGVQGEDGNPGRGGEKGAKGIRGKRGNSGFPGLAGTPGDQGPPGKMGTKGSKGLADRTPCEIVDFVRGNCPCSTGISRCPAFPTEVVFTLDMSNDVAPSDFERMRNILLSLLMKLEMCESNCPTGARVAIVSYNTRTDYLVRLSDHRGKAALLQAVRKIPLERSSGSRNLGATMRFVARHVFKRVRSGLLVRKVAVFFQAGRNYDTASVSTATLELHAADIATAVVTFTEEHNLPEAGLVDGPNEFHLFTWETEGQQDVERLASCTLCYDKCRPALGCQLRAPGPQKLDMDLVFLVDSSQGVSRDIYLGALRLVDSVLKDLEVAAQPGTSWHGARAALLTHTTPGFWPGVDQAPVLEYFHLTSHGHRTEMQRQIREAASGLLQGGPALGHALEWTLENVLLTAVLPRRSRVLYAIVASETSIWDREKLRTLSQEAKCKGIALFVLAVGPGVGAQELAELAKVASAPWEQHLLRLEGVSEAEVAYASRFTEAFLNLLNSGINQYPPPELVKECGGPNRGDTLLHFFTSAKRFSRSQSGTSAAFANDSEALKSQGIFLGERKSRVASVALQEALGSHGKDRADTEDIDQETPAKGRHLGPTHGPCPMGPEEGECLNYVLK
| null | null |
cell adhesion [GO:0007155]; extracellular matrix organization [GO:0030198]
|
collagen trimer [GO:0005581]; collagen-containing extracellular matrix [GO:0062023]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; protein-containing complex [GO:0032991]
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collagen binding [GO:0005518]
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PF01391;PF00092;
|
3.40.50.410;
|
Type VI collagen family
|
PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Collagen VI acts as a cell-binding protein. {ECO:0000250}.
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Mus musculus (Mouse)
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A2BD05
|
NEK6_PIG
|
MAGQPSHMPHGGSPNNLCHTPGPAHPPDPQRHPNALSFRCSLADFQIEKKIGRGQFSEVYKATCLLDRKTVALKKVQIFEMMDAKARQDCVKEIGLLKQLNHPNIIKYLDSFIEDNELNIVLELADAGDLSQMIKYFKKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGIVKLGDLGLGRFFSSETTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNLFSLCQKIEQCDYPPLPGEHYSEKLRELVSMCIYPDPNQRPDIGYVHQVARQMHVWTSST
|
2.7.11.34
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
|
apoptotic process [GO:0006915]; cell division [GO:0051301]; chromosome segregation [GO:0007059]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]; regulation of mitotic metaphase/anaphase transition [GO:0030071]
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centriolar satellite [GO:0034451]; cytosol [GO:0005829]; nuclear speck [GO:0016607]; protein-containing complex [GO:0032991]; spindle pole [GO:0000922]
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ATP binding [GO:0005524]; DNA-binding transcription factor binding [GO:0140297]; kinesin binding [GO:0019894]; magnesium ion binding [GO:0000287]; protein kinase binding [GO:0019901]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; transcription corepressor binding [GO:0001222]; ubiquitin protein ligase binding [GO:0031625]
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PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, NEK Ser/Thr protein kinase family, NIMA subfamily
|
PTM: Autophosphorylated. Phosphorylation at Ser-206 is required for its activation. Phosphorylated upon IR or UV-induced DNA damage. Phosphorylated by CHEK1 and CHEK2. Interaction with APBB1 down-regulates phosphorylation at Thr-210 (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Nucleus speckle {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}. Note=Colocalizes with APBB1 at the nuclear speckles. Colocalizes with PIN1 in the nucleus. Colocalizes with ATF4, CIR1, ARHGAP33, ANKRA2, CDC42, NEK9, RAD26L, RBBP6, RPS7, TRIP4, RELB and PHF1 in the centrosome. Localizes to spindle microtubules in metaphase and anaphase and to the midbody during cytokinesis (By similarity). {ECO:0000250}.
|
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=2.7.11.34; Evidence={ECO:0000250|UniProtKB:Q9HC98}; 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=2.7.11.34; Evidence={ECO:0000250|UniProtKB:Q9HC98};
| null | null | null | null |
FUNCTION: Protein kinase which plays an important role in mitotic cell cycle progression. Required for chromosome segregation at metaphase-anaphase transition, robust mitotic spindle formation and cytokinesis. Phosphorylates ATF4, CIR1, PTN, RAD26L, RBBP6, RPS7, RPS6KB1, TRIP4, STAT3 and histones H1 and H3. Phosphorylates KIF11 to promote mitotic spindle formation. Involved in G2/M phase cell cycle arrest induced by DNA damage. Inhibition of activity results in apoptosis. May contribute to tumorigenesis by suppressing p53/TP53-induced cancer cell senescence (By similarity). Phosphorylates EML4 at 'Ser-144', promoting its dissociation from microtubules during mitosis which is required for efficient chromosome congression (By similarity). {ECO:0000250|UniProtKB:Q9HC98}.
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Sus scrofa (Pig)
|
A2BDX3
|
MOCS3_MOUSE
|
MAAPEDVAALQAEITRREEELASLKRRLAAALTAEPEPERPLRVPPPPLAPRAALSRDEILRYSRQLLLPELGVRGQLRLAAAAVLVVGCGGLGCPLAQYLAAAGVGRLGLVDHDVVETSNLARQVLHGEAQAGESKARSAAAALRRLNSAVECVAYPRALAEDWALDLVRGYDVVADCCDNVPTRYLVNDACVLAGRPLVSASALRFEGQMTVYHHDGGPCYRCVFPRPPPPETVTNCADGGVLGAVPGVLGCAQALEVLKIAAGLGSSYSGSMLLFDGLGGHFRRIRLRRRRPDCVVCGQQPTVTRLQDYEAFCGSSATDKCRALKLLCPEERISVTDYKRLLDSGAPHVLLDVRPQVEVDICRLPHSLHIPLSQLERRDADSLKLLGAALRKGKQESQEGVALPVYVICKLGNDSQKAVKVLQSLTAVPELDSLTVQDIVGGLMAWAAKIDGTFPQY
|
2.7.7.80; 2.8.1.11
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_03049}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03049};
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Mo-molybdopterin cofactor biosynthetic process [GO:0006777]; molybdopterin cofactor biosynthetic process [GO:0032324]; protein urmylation [GO:0032447]; tRNA thio-modification [GO:0034227]; tRNA wobble position uridine thiolation [GO:0002143]; tRNA wobble uridine modification [GO:0002098]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]
|
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; molybdopterin-synthase adenylyltransferase activity [GO:0061605]; molybdopterin-synthase sulfurtransferase activity [GO:0061604]; nucleotidyltransferase activity [GO:0016779]; sulfotransferase activity [GO:0008146]; sulfurtransferase activity [GO:0016783]; thiosulfate sulfurtransferase activity [GO:0004792]; URM1 activating enzyme activity [GO:0042292]
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PF00581;PF00899;
|
3.40.50.720;3.40.250.10;
|
HesA/MoeB/ThiF family, UBA4 subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03049}.
|
CATALYTIC ACTIVITY: Reaction=[molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly + ATP + H(+) = [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly-AMP + diphosphate; Xref=Rhea:RHEA:43616, Rhea:RHEA-COMP:12159, Rhea:RHEA-COMP:12202, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:90618, ChEBI:CHEBI:90778; EC=2.7.7.80; Evidence={ECO:0000255|HAMAP-Rule:MF_03049}; CATALYTIC ACTIVITY: Reaction=[molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly-AMP + AH2 + S-sulfanyl-L-cysteinyl-[cysteine desulfurase] = [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-NH-CH2-C(O)SH + A + AMP + H(+) + L-cysteinyl-[cysteine desulfurase]; Xref=Rhea:RHEA:48612, Rhea:RHEA-COMP:12157, Rhea:RHEA-COMP:12158, Rhea:RHEA-COMP:12159, Rhea:RHEA-COMP:12160, ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:17499, ChEBI:CHEBI:29950, ChEBI:CHEBI:61963, ChEBI:CHEBI:90618, ChEBI:CHEBI:90619, ChEBI:CHEBI:456215; EC=2.8.1.11; Evidence={ECO:0000255|HAMAP-Rule:MF_03049};
| null |
PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03049}.; PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03049}.
| null | null |
FUNCTION: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers URM1 and MOCS2A. Its N-terminus first activates URM1 and MOCS2A as acyl-adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to URM1 and MOCS2A to form thiocarboxylation (-COSH) of their C-terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as a nucleophile towards URM1 and MOCS2A. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor; NFS1 acting as a sulfur donor for thiocarboxylation reactions. {ECO:0000255|HAMAP-Rule:MF_03049}.
|
Mus musculus (Mouse)
|
A2BGM5
|
FOXN4_DANRE
|
MTVQSKLQGRGKFKKRFFRAGQQVPRPTLELSSVWLSKIFYNPEQHHNKQKMIESGITTRMSGIHENPGQSHHTSAQDYRLLTTDPSQLKDELPGDLQSLSWLTSVDVPRLQQIGGGRPDFTSSAQSSLLERQTAQLNSMTVAGGAGSAIHLQSEMQHSPLAINSMPQFSPGFPCAASVYQTAPQQVLTFTQANQQCSPGGLYGNYNSQNLFPQPRITAHSQDLQPKCFPKPIYSYSCLIAMALKNSKTGSLPVSEIYSFMKEHFPYFKTAPDGWKNSVRHNLSLNKCFEKVENKMSGSSRKGCLWALNPAKIDKMEEEMQKWKRKDLPAIRRSMANPDELDKLITDRPESCRQKSVDPGMTRLPSCPPGQTLPLAAQMQPQPVVTLSLQCLPMHQHLQLQLQNQSRLAPSSPAPAQTPPLHTVPDMTNSSLPQHPAKQHTDFYTVHTDVNSEVDALDPSIMDFAWQGNLWEEMKDDSFNLEALGTLSNSPLRLSDCDLDTSSVTPVSSAGGLPYPDLQVTGLYSSYSAIDALSNQYMNTQGGTKPIVLL
| null | null |
amacrine cell differentiation [GO:0035881]; atrioventricular canal development [GO:0036302]; heart looping [GO:0001947]; heart valve development [GO:0003170]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of DNA-templated transcription [GO:0006355]; regulation of heart contraction [GO:0008016]; retina layer formation [GO:0010842]; ventral spinal cord interneuron fate commitment [GO:0060579]
|
nucleus [GO:0005634]
|
chromatin binding [GO:0003682]; cis-regulatory region sequence-specific DNA binding [GO:0000987]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; sequence-specific DNA binding [GO:0043565]
|
PF00250;
|
1.10.10.10;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089}.
| null | null | null | null | null |
FUNCTION: Transcription factor essential for neural and some non-neural tissues development. Binds to an 11-bp consensus sequence containing the invariant tetranucleotide 5'-ACGC-3'. During development of the central nervous system, required to specify the amacrine and horizontal cell fates from multipotent retinal progenitors while suppressing the alternative photoreceptor cell fates. Drives commitment of p2 progenitors to the V2b interneuron fates during spinal cord neurogenesis. In development of non-neural tissues, plays an essential role in the specification of the atrioventricular canal. {ECO:0000269|PubMed:18347092}.
|
Danio rerio (Zebrafish) (Brachydanio rerio)
|
A2BH40
|
ARI1A_MOUSE
|
MAAQVAPAAASSLGNPPPPPSELKKAEQQQREEAGGEAAAAAAERGEMKAAAGQESEGPAVGPPQPLGKELQDGAESNGGGGGGGAGSGGGPGAEPDLKNSNGNAGPRPALNNNLPEPPGGGGGGGSSSSDGVGAPPHSAAAALPPPAYGFGQAYGRSPSAVAAAAAAVFHQQHGGQQSPGLAALQSGGGGGLEPYAGPQQNSHDHGFPNHQYNSYYPNRSAYPPPPQAYALSSPRGGTPGSGAAAAAGSKPPPSSSASASSSSSSFAQQRFGAMGGGGPSAAGGGTPQPTATPTLNQLLTSPSSARGYQGYPGGDYGGGPQDGGAGKGPADMASQCWGAAAAAAAAAAAVSGGAQQRSHHAPMSPGSSGGGGQPLARTPQSSSPMDQMGKMRPQPYGGTNPYSQQQGPPSGPQQGHGYPGQPYGSQTPQRYPMTMQGRAQSAMGSLSYAQQIPPYGQQGPSAYGQQGQTPYYNQQSPHPQQQPPYAQQPPSQTPHAQPSYQQQPQTQQPQLQSSQPPYSQQPSQPPHQQSPTPYPSQQSTTQQHPQSQPPYSQPQAQSPYQQQQPQQPASSSLSQQAAYPQPQPQQSQQTAYSQQRFPPPQELSQDSFGSQASSAPSMTSSKGGQEDMNLSLQSRPSSLPDLSGSIDDLPMGTEGALSPGVSTSGISSSQGEQSNPAQSPFSPHTSPHLPGIRGPSPSPVGSPASVAQSRSGPLSPAAVPGNQMPPRPPSGQSDSIMHPSMNQSSIAQDRGYMQRNPQMPQYTSPQPGSALSPRQPSGGQMHSGVGSYQQNSMGSYGPQGSQYGPQGGYPRQPNYNALPNANYPNAGMAGSMNPMGAGGQMHGQPGIPPYGTLPPGRMAHASMGNRPYGPNMANMPPQVGSGMCPPPGGMNRKTQESAVAMHVAANSIQNRPPGYPNMNQGGMMGTGPPYGQGINSMAGMINPQGPPYPMGGTMANNSAGMAASPEMMGLGDVKLTPATKMNNKADGTPKTESKSKKSSSSTTTNEKITKLYELGGEPERKMWVDRYLAFTEEKAMGMTNLPAVGRKPLDLYRLYVSVKEIGGLTQVNKNKKWRELATNLNVGTSSSAASSLKKQYIQCLYAFECKIERGEDPPPDIFAAADSKKSQPKIQPPSPAGSGSMQGPQTPQSTSSSMAEGGDLKPPTPASTPHSQIPPLPGMSRSNSVGIQDAFPDGSDPTFQKRNSMTPNPGYQPSMNTSDMMGRMSYEPNKDPYGSMRKAPGSDPFMSSGQGPNGGMGDPYSRAAGPGLGSVAMGPRQHYPYGGPYDRVRTEPGIGPEGNMGTGAPQPNLMPSTPDSGMYSPSRYPPQQQQQQQQQHDSYGNQFSTQGTPSSSPFPSQQTTMYQQQQQNYKRPMDGTYGPPAKRHEGEMYSVPYSAGQGQPQQQQLPAAQSQPASQPQAAQPSPQQDVYNQYSNAYPASATAATDRRPAGGPQNQFPFQFGRDRVSAPPGSSAQQNMPPQMMGGPIQASAEVAQQGTMWQGRNDMTYNYANRQNTGSATQGPAYHGVNRTDEMLHTDQRANHEGPWPSHGTRQPPYGPSAPVPPMTRPPPSNYQPPPSMPNHIPQVSSPAPLPRPMENRTSPSKSPFLHSGMKMQKAGPPVPASHIAPTPVQPPMIRRDITFPPGSVEATQPVLKQRRRLTMKDIGTPEAWRVMMSLKSGLLAESTWALDTINILLYDDNSIMTFNLSQLPGLLELLVEYFRRCLIEIFGILKEYEVGDPGQRTLLDPGRFTKVYSPAHTEEEEEEHLDPKLEEEEEEGVGNDEEMAFLGKDKPSSENNEEKLVSKFDKLPVKIVQRNDPFVVDCSDKLGRVQEFDSGLLHWRIGGGDTTEHIQTHFESKIELLPSRPYVPCPTPPRKHLTTVEGTPGTTEQEGPPPDGLPEKRITATMDDMLSTRSSTLTDEGAKSAEATKESSKFPFGISPAQSHRNIKILEDEPHSKDETPLCTLLDWQDSLAKRCVCVSNTIRSLSFVPGNDFEMSKHPGLLLILGKLILLHHKHPERKQAPLTYEKEEEQDQGVSCDKVEWWWDCLEMLRENTLVTLANISGQLDLSPYPESICLPVLDGLLHWAVCPSAEAQDPFSTLGPNAVLSPQRLVLETLSKLSIQDNNVDLILATPPFSRLEKLYSTMVRFLSDRKNPVCREMAVVLLANLAQGDSLAARAIAVQKGSIGNLLGFLEDSLAATQFQQSQASLLHMQNPPFEPTSVDMMRRAARALLALAKVDENHSEFTLYESRLLDISVSPLMNSLVSQVICDVLFLIGQS
| null | null |
androgen receptor signaling pathway [GO:0030521]; cardiac chamber development [GO:0003205]; cardiac muscle cell differentiation [GO:0055007]; chromatin organization [GO:0006325]; chromatin remodeling [GO:0006338]; embryo implantation [GO:0007566]; forebrain development [GO:0030900]; formation of primary germ layer [GO:0001704]; gastrulation [GO:0007369]; intracellular estrogen receptor signaling pathway [GO:0030520]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neural tube closure [GO:0001843]; optic cup formation involved in camera-type eye development [GO:0003408]; placenta blood vessel development [GO:0060674]; positive regulation of cell differentiation [GO:0045597]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of double-strand break repair [GO:2000781]; positive regulation of myoblast differentiation [GO:0045663]; positive regulation of stem cell population maintenance [GO:1902459]; positive regulation of T cell differentiation [GO:0045582]; regulation of G0 to G1 transition [GO:0070316]; regulation of G1/S transition of mitotic cell cycle [GO:2000045]; regulation of mitotic metaphase/anaphase transition [GO:0030071]; regulation of nucleotide-excision repair [GO:2000819]; regulation of transcription by RNA polymerase II [GO:0006357]; stem cell population maintenance [GO:0019827]
|
bBAF complex [GO:0140092]; brahma complex [GO:0035060]; chromatin [GO:0000785]; nBAF complex [GO:0071565]; npBAF complex [GO:0071564]; nucleoplasm [GO:0005654]; SWI/SNF complex [GO:0016514]
|
ATP-dependent chromatin remodeler activity [GO:0140658]; DNA binding [GO:0003677]; nucleosome binding [GO:0031491]
|
PF01388;PF12031;
|
1.10.150.60;1.25.10.10;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355}.
| null | null | null | null | null |
FUNCTION: Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. Binds DNA non-specifically (PubMed:22952240, PubMed:26601204). Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and the neuron-specific chromatin remodeling complex (nBAF complex). During neural development a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (PubMed:17640523). {ECO:0000250|UniProtKB:O14497, ECO:0000269|PubMed:17640523, ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}.
|
Mus musculus (Mouse)
|
A2BIE7
|
TAPT1_DANRE
|
MADSVAAGLGDENETENEDKEREKRLFSGVKKMEKQAAASDVTETLGFYERKAKCKDRKTNVSDLSLVRFISAELTRGYFLEHNEAKYTERRERVYTCLRIPKELEKLMIFGYFLCLDVFLYVFTLLPLRVLLALVRLLTLPCCGLSGSRILQPAQVCDVLKGFIMVLCYFMMHYVDYSMMYHLIRGQSVIKLYIIYNMLEVADRLFSSFGQDILDALYWTATEPKERKRAHIGVIPHFFMAVLYVFLHAILIMVQATTLNVAFNSHNKSLLTIMMSNNFVEIKGSVFKKFEKNNLFQMSNSDIKERFTNYTLLLIVCLRNMEQFSWNPDHLWVLFPDVCMVIASEIAVDVVKHAFITKFNDITADVYSEYRASLAFDLVSSRQKNAYTDYSDSVSRRMGFIPLPLALLLIRVVTSSVKIQGSLSIVCVLLFYLGMITLKVLNSIVLLGKSCMYVKEANMEEKLFQNPPSAAPSRVSSRAHRTKHTREPPGDPAEEGMSASVTTQPTQQDECPAPQIPTSESDQFLTTPDESEEKSLIQDDSELKHRAPKKDLLEIDRFTICGNRID
| null | null |
cartilage development [GO:0051216]; cell projection organization [GO:0030030]; cranial skeletal system development [GO:1904888]; neural crest cell development [GO:0014032]; ossification [GO:0001503]; positive regulation of bone development [GO:1903012]; positive regulation of cartilage development [GO:0061036]; positive regulation of cilium assembly [GO:0045724]
|
centrosome [GO:0005813]; ciliary basal body [GO:0036064]; cytoplasm [GO:0005737]; membrane [GO:0016020]
| null |
PF05346;
| null |
TAPT1 family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q6NXT6}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q6NXT6}. Membrane {ECO:0000250|UniProtKB:Q6NXT6}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q6NXT6}.
| null | null | null | null | null |
FUNCTION: Plays a role in primary cilia formation (PubMed:26365339). Involved in cartilage and bone development (PubMed:26365339). May play a role in the differentiation of cranial neural crest cells (PubMed:26365339). May act as a downstream effector of hoxc8 during development (By similarity). {ECO:0000250|UniProtKB:Q4VBD2, ECO:0000269|PubMed:26365339}.
|
Danio rerio (Zebrafish) (Brachydanio rerio)
|
A2BIL7
|
BAZ1B_DANRE
|
MAPLLGRKPYPLVKPLSEPPGPGEEVYTIEHTKEAFRNKEEYEARLRRYGERIWTCKSTGSSQLTHKEAWEEEQEVTELLQEEYPVWFEKPVLEIVHHNTVPLDKLVDQVWVEILTKYAVGEKCDLMVGNDKTLSVEVVKIHPLENPPEENAEKKMEGACDSPSSDKENASQENLKKEPQSKEEESRRESLSDRARRSPRKLPTTMKEEKKKWVMPKFLPHKYDVKLVNEDKVISDVPADNLFRTERPPNKEIMRYFIRHYALRLGSGESAPWVVEDELVKKFSLPSKFSDFLLDPHKFLAENPSTKRKSLSSPEGKPRKRLKNVETGTGGEGAKGDKKKNKDSQNIPLSPTIWSHMQVKKVNGSPLKMKNSGTSKKSDEENVLGTPKSSKKQGDKKSSDPKRRRKSGLNKTPNSQRLSKKEDKSLGGAKKPRMKQMTLLDLAKSPAAAGSPKKQRRSSTTGSAKLGKPFPPMALHLLRFYKENKGKEDKKTTLSSLLSKAAKALSPEDRSRLPEELKELVQKRWELLEQKRRWALMSEEEKQSVLKQKRQEVKQKLREKAKERREKEMQVRREMSRRYEDQELEGKNLPAFRLFDMPEGLPNTIFGDVAMVVEFLHCYSGLLMPDDQYPITSIALLEALAGEKAGFLYLNRVLVVLLQTLLQDELAEGYSELDMPLSEIPLTMHSVSELVRLCLRPSDAHEEESARGSDDWQSGADFDDMVSSEFLEKLETAEVFELDPQEKVSLLLALCHRILMTYSVEDHVEAVHQKSAEMWKERVATLKEANDRKRAEKQKRKEQMETKTDGDVLIKAEKKKESTVKKETPKVLPKEEPEPEDMISTVKSRRLMSIQAKKEKEEQERLNKVRMEKEAEEERIRRQKAATEKAFQDAVTKAKLVLRRTPLGTDRNHNRYWLFSDVVPGLYIEKGWVHESIDYSFTLPPEEEPVLTEEEEEEEEVKKEEETEDGEKEDEGSIISASNDISQQGAPSHESSIETTVPKQGQNLWFVCDTPKDFDELLESLHPQGVRESELKIRLQINYQEILHSIHLTKKGNPGLKTCDGHQELLKFLRSDIIEVASRLQKGGLGYLEDTSEFEEFEERVKTLEKLPEFGECVIALQESVIKKFLQGFMAPKQKKKKKTGGEESTTAEEVDDQKKLAEEARVATAVEKWKTAVREAQTFSRMHVLLGMLDACIKWDMSAENARCKVCRRKGEDDKLILCDECNKAFHLFCLRPALYRIPAGEWLCPACQPTIARRSSRGRNYKEDSEEEEDSEEEDEEESEEEDSEEEHRNTGHSLRSRKKVKTSSKSKMQKKPAKPASRSASKTDTNPSKTSPKSSAKPKSRAAPSSPVDIDELVRQSSKPPSRKKDVELQKCEEILQKIMKFRHSWPFREPVSAEEAEDYQDVITSPMDLTTMQGKFKSSEYHSASDFIEDMKLIFSNAEEYNQPSSNVLTCMSRTEEAFVELLQKSLPGVSYLRRRTRKRAATPSDNSDDDDDDEEEDERSKKQKNGKQGKKASSKRKVEHSRTEKYQTKQK
|
2.7.10.2
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
|
chromatin remodeling [GO:0006338]; DNA damage response [GO:0006974]; phosphorylation [GO:0016310]; post-translational protein modification [GO:0043687]
|
nucleus [GO:0005634]; WICH complex [GO:0090535]
|
ATP binding [GO:0005524]; histone binding [GO:0042393]; histone H2AXY142 kinase activity [GO:0140801]; histone kinase activity [GO:0035173]; metal ion binding [GO:0046872]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]
|
PF00439;PF00628;PF10537;PF15612;PF15613;
|
1.20.920.10;3.30.40.10;
|
WAL family, BAZ1B subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00063, ECO:0000255|PROSITE-ProRule:PRU00475}. Note=Accumulates in pericentromeric heterochromatin during replication. Targeted to replication foci throughout S phase (By similarity). Localizes to sites of DNA damage (By similarity). {ECO:0000250|UniProtKB:Q9UIG0}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2;
| null | null | null | null |
FUNCTION: Atypical tyrosine-protein kinase that plays a central role in chromatin remodeling and acts as a transcription regulator. Involved in DNA damage response by phosphorylating 'Tyr-142' of histone H2AX (H2AXY142ph). H2AXY142ph plays a central role in DNA repair and acts as a mark that distinguishes between apoptotic and repair responses to genotoxic stress. Essential component of the WICH complex, a chromatin remodeling complex that mobilizes nucleosomes and reconfigures irregular chromatin to a regular nucleosomal array structure. The WICH complex regulates the transcription of various genes, has a role in RNA polymerase I and RNA polymerase III transcription, mediates the histone H2AX phosphorylation at 'Tyr-142', and is involved in the maintenance of chromatin structures during DNA replication processes. {ECO:0000250}.
|
Danio rerio (Zebrafish) (Brachydanio rerio)
|
A2BIX4
|
SPEE1_HYPBU
|
MELGMFRLNIYQPGGPIGALYPVEKILYHGRSQYQEIMILVLRGFGKTLVLDGLIQSTESDEHIYHETLVHPAMTVHPNPRRVLILGGGEGATLREVLKHNTVEKAVMVDIDGEVVRVAREYLPEWHQGAFDDPRAQVVIMDGFEYIKEAARRGEDFDVIIMDLTDPFGPKIAAKLYTKEAIGLVKSVLRSDGILVTQAGCAALFPEAFEKVYGSVKSLFAHAEEYGVWVPSFMYVNSFVFASDKYRLTDLSMEEVDRRLRERGVETRFYSGLRHYTLIGLGGIRLLEGRGS
|
2.5.1.126; 2.5.1.127; 2.5.1.79
| null |
polyamine biosynthetic process [GO:0006596]; spermidine biosynthetic process [GO:0008295]
|
cytoplasm [GO:0005737]
|
spermidine synthase activity [GO:0004766]; sym-norspermidine synthase activity [GO:0050314]; thermospermine synthase activity [GO:0010487]
|
PF17284;PF01564;
|
2.30.140.10;3.40.50.150;
|
Spermidine/spermine synthase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00198}.
|
CATALYTIC ACTIVITY: Reaction=norspermine + S-adenosyl 3-(methylsulfanyl)propylamine = caldopentamine + 2 H(+) + S-methyl-5'-thioadenosine; Xref=Rhea:RHEA:42868, ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:57443, ChEBI:CHEBI:58704, ChEBI:CHEBI:82769; EC=2.5.1.127; Evidence={ECO:0000269|PubMed:19822146}; CATALYTIC ACTIVITY: Reaction=norspermidine + S-adenosyl 3-(methylsulfanyl)propylamine = H(+) + norspermine + S-methyl-5'-thioadenosine; Xref=Rhea:RHEA:42864, ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:57443, ChEBI:CHEBI:57920, ChEBI:CHEBI:58704; EC=2.5.1.126; Evidence={ECO:0000269|PubMed:19822146}; CATALYTIC ACTIVITY: Reaction=S-adenosyl 3-(methylsulfanyl)propylamine + spermidine = H(+) + S-methyl-5'-thioadenosine + thermospermine; Xref=Rhea:RHEA:30515, ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:57443, ChEBI:CHEBI:57834, ChEBI:CHEBI:59903; EC=2.5.1.79; Evidence={ECO:0000269|PubMed:19822146};
| null | null | null | null |
FUNCTION: Involved in the biosynthesis of polyamines which are thought to support the growth of thermophilic microorganisms under high-temperature conditions. It seems that long-chain and branched-chain of polyamines effectively stabilize DNA and RNA, respectively. Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to norspermidine, spermidine and norspermine to yield norspermine, thermospermine and caldopentamine, respectively. It can also synthesize sym-norspermidine (bis(3-aminopropyl)amine) from 1,3-diaminopropane with a very low activity. The biosynthesis of caldohexamine and caldoheptamine from caldopentamine has been also observed. {ECO:0000269|PubMed:19822146}.
|
Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5)
|
A2CEH0
|
POC1B_DANRE
|
MASVMEDPTLERHFKGHKDVISCADFNPNNKQLATGSCDKSLMIWNLAPKARAFRFVGHTDVITGVNFAPSGSLVASSSRDQTVRLWTPSIKGESTVFKAHTASVRSVHFSRDGQRLVTASDDKSVKVWGVERKKFLYSLNRHTNWVRCARFSPDGRLIASCGDDRTVRLWDTSSHQCINIFTDYGGSATFVDFNSSGTCIASSGADNTIKIWDIRTNKLIQHYKVHNAGVNCFSFHPSGNYLISGSSDSTIKILDLLEGRLIYTLHGHKGPVLTVTFSRDGDLFASGGADSQVLMWKTNFDSLNYRELLSKHSKRVTPDPPPHLMDIYPRSHHRHHPQNGTVEINPVADTQSTDPQVVEVGRVVFSTTDARNYDGASSSRAQFTSGMDSGPFRTHTQAREEEDENQEERFAGGMTASPAERSGIPSSLTSTLENIVQQLDILTQTVAVLEERLTLTEDKLRTCLDNQVLLMQQNQQLDRSDEESEGPPL
| null | null |
centriole replication [GO:0007099]; cilium assembly [GO:0060271]; epithelial cilium movement involved in determination of left/right asymmetry [GO:0060287]; heart development [GO:0007507]; optokinetic behavior [GO:0007634]; renal system process [GO:0003014]; retina homeostasis [GO:0001895]; retina layer formation [GO:0010842]
|
centriole [GO:0005814]; ciliary basal body [GO:0036064]; cytoplasm [GO:0005737]; extracellular region [GO:0005576]
| null |
PF00400;
|
2.130.10.10;
|
WD repeat POC1 family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q8TC44}.
| null | null | null | null | null |
FUNCTION: Plays an important role in centriole assembly and/or stability and ciliogenesis. Involved in early steps of centriole duplication, as well as in the later steps of centriole length control. {ECO:0000250|UniProtKB:Q8TC44, ECO:0000269|PubMed:20008567}.
|
Danio rerio (Zebrafish) (Brachydanio rerio)
|
A2CEI6
|
PIWL2_DANRE
|
MDPKRPTFPSPPGVIRAPWQQSTEDQSQLLDQPSLGRARGLIMPIDEPLPGRGRAFSVPGEMPVRFGRGITQSIAAEPLVGMARGVRLPMEEGGFGRGRGFLLPTPEPTVGIGRGAAIGPVPTLDIQKAEVEEKMPELQAEVAPTVAKVGSPGTGSSLVSMFRGLGIEPGKTWGRGAAPVGRGAAGDMGADLQPKPTIIGASLTPEREEVRSEESISFLGRGFTGFGRAAMPHMTVGRGPIGPLSPSPSVAAPFSLISASSASEDAPVAPGTPPKVEVKIETVKEPLQKIGTKGSPIPIGSNYIPICCKNDAVFQYHVTFTPNVESLSMRFGMMKEHRPTTGEVVAFDGSILYLPKRLEEVVHLKAERKTDNQEIDIKIQLTKILPPSSDLCIPFYNVVLRRVMKILGLKLVGRNHYDPNAVVILGKHRLQVWPGYSTSIKHTDGGLYLVVDVSHKVLRNDSVLDVMNLIYQGSRESFQDECTKEFVGSIVITRYNNRTYRIDDIEWSKSPKDTFTLADGSVTTFVDYYRKNYGITIKELDQPLLIHRPKERSRPGGKVITGEILLLPELSFMTGIPEKMRKDFRAMKDLTMHINVGAQQHTQSLKQLLHNINSNNEALSELGRWGLSISQEILVTQGRTLPSETICLHSASFVTSPAVDWSRELVRDPSISTVPLNCWAVFYPRRATDQAEELVTTFSRVAGPMGMRVERPIRVELRDDRTETFVKSIHSQLTSEPRVQLVVCIMTGNRDDLYSAIKKLCCIQSPVPSQAINVRTISQPQKLRSVAQKILLQINCKLGGELWTVNVPLKYLMVIGVDVHHDTSKKSRSVMGFVASLNSMLTKWYSRVTFQMPNEEIINGFRVCLLAALQKYYEVNHAFPEKIVIYRDGVSDGQLKTVEHYEIPQILKCFETIPNYEPKLAFIVVQKRISTTLYSYGSDHFGTPSPGTVLDHTVTNRDWVDFYLMAHSIRQGCGLPTHYITVYNTANLTPDHLQRLTFKMCHLYWNWPGTIRVPAPCKYAHKLAFLSGQYLHSEPAIQLSEKLFFL
|
3.1.26.-
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9JMB7};
|
gamete generation [GO:0007276]; germ-line stem cell population maintenance [GO:0030718]; meiotic cell cycle [GO:0051321]; negative regulation of SMAD protein signal transduction [GO:0060392]; oogenesis [GO:0048477]; piRNA processing [GO:0034587]; positive regulation of gene expression [GO:0010628]; regulation of translation [GO:0006417]; regulatory ncRNA-mediated gene silencing [GO:0031047]; retrotransposon silencing by heterochromatin formation [GO:0141005]; rhythmic process [GO:0048511]; secondary piRNA processing [GO:0140965]; siRNA-mediated retrotransposon silencing by heterochromatin formation [GO:0141007]; spermatogenesis [GO:0007283]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]; P granule [GO:0043186]; PET complex [GO:1990923]; pi-body [GO:0071546]
|
metal ion binding [GO:0046872]; piRNA binding [GO:0034584]; RNA endonuclease activity [GO:0004521]
|
PF08699;PF02170;PF02171;
|
3.40.50.2300;2.170.260.10;3.30.420.10;
|
Argonaute family, Piwi subfamily
|
PTM: Methylated on arginine residues; required for the interaction with Tudor domain-containing protein and subsequent localization to the meiotic nuage, also named P granule. {ECO:0000250|UniProtKB:Q8CDG1}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18833190}. Nucleus {ECO:0000269|PubMed:18833190}. Note=Probable component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis (By similarity). In mitotic and early meiotic cells of ovary, it is predominantly cytoplasmic. In primary oocytes, it is found in a granular distribution around the nucleus. Later, in maturing oocytes, it localizes to the nucleus. In testis, it is present in the cytoplasm of mitotic and meiotic germ cells, where a distinct granular distribution around the nucleus is observed. {ECO:0000250|UniProtKB:Q8CDG1}.
| null | null | null | null | null |
FUNCTION: Endoribonuclease that plays a central role during spermatogenesis by repressing transposable elements and preventing their mobilization, which is essential for the germline integrity (PubMed:18833190). Plays an essential role in germ cell differentiation and meiosis, independently of the function in transposable elements repression (PubMed:18833190). Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and govern the methylation and subsequent repression of transposons (PubMed:18833190). During piRNA biosynthesis, plays a key role in the piRNA amplification loop, also named ping-pong amplification cycle, by acting as a 'slicer-competent' piRNA endoribonuclease that cleaves primary piRNAs, which are then loaded onto 'slicer-incompetent' piwil4 (By similarity). Piwil2 slicing produces a pre-miRNA intermediate, which is then processed in mature piRNAs, and as well as a 16 nucleotide by-product that is degraded (By similarity). Required for piwil4/miwi2 nuclear localization and association with secondary piRNAs antisense (By similarity). Represses circadian rhythms by promoting the stability and activity of core clock components BMAL1 and CLOCK (By similarity). {ECO:0000250|UniProtKB:Q8CDG1, ECO:0000269|PubMed:18833190}.
|
Danio rerio (Zebrafish) (Brachydanio rerio)
|
A2CG49
|
KALRN_MOUSE
|
MVLSGSFRNDGLKASDVLPILKEKVAFVSGGRDKRGGPILTFPARSNHDRIRQEDLRKLVTYLASVPSEDVCKRGFTVIIDMRGSKWDLIKPLLKTLQEAFPAEIHVALIIKPDNFWQKQKTNFGSSKFIFETSMVSVEGLTKLVDPSQLTEEFDGSLDYNHEEWIELRLSLEEFFNSAVHLLSRLEDLQEMLARKEFPVDVEGSRRLIDEHTQLKKKVLKAPVEELDREGQRLLQCIRCSDGFSGRNCIPGSADFQSLVPKITSLLDKLHSTRQHLHQMWHVRKLKLDQCFQLRLFEQDAEKMFDWISHNKELFLQSHTEIGVSYQHALDLQTQHNHFAMNSMNAYVNINRIMSVASRLSEAGHYASQQIKQISTQLDQEWKSFAAALDERSTILAMSAVFHQKAEQFLSGVDAWCKMCSEGGLPSEMQDLELAIHHHQSLYEQVTQAYTEVSQDGKALLDVLQRPLSPGNSESLTATANYSKAVHQVLDVVHEVLHHQRRLESIWQHRKVRLHQRLQLCVFQQDVQQVLDWIENHGEAFLSKHTGVGKSLHRARALQKRHDDFEEVAQNTYTNADKLLEAAEQLAQTGECDPEEIYKAARHLEVRIQDFVRRVEQRKLLLDMSVSFHTHTKELWTWMEDLQKEVLEDVCADSVDAVQELIKQFQQQQTATLDATLNVIKEGEDLIQQLRSAPPSLGEPTEARDSAMSNNKTPHSSSISHIESVLQQLDDAQVQMEELFHERKIKLDIFLQLRIFEQYTIEVTAELDAWNEDLLRQMNDFNTEDLTLAEQRLQRHTERKLAMNNMTFEVIQQGQDLHQYIMEVQASGIELICEKDLDLAAQVQELLEFLHEKQHELELNAEQTHKRLEQCLQLRHLQAEVKQVLGWIRNGESMLNASLVNASSLSEAEQLQREHEQFQLAIEKTHQSALQVQQKAEALLQAGHYDADAIRECAEKVALHWQQLMLKMEDRLKLVNASVAFYKTSEQVCSVLESLEQEYRRDEDWCGGRDKLGPAAEMDHVIPLLSKHLEQKEAFLKACTLARRNAEVFLKYIHRNNVSMPSVASHTRGPEQQVKAILSELLQRENRVLHFWTLKKRRLDQCQQYVVFERSAKQALDWIQETGEYYLSTHTSTGETTEETQELLKEYGEFRVPAKQTKEKVKLLIQLADSFVEKGHIHATEIRKWVTTVDKHYRDFSLRMGKYRYSLEKALGVNTEDNKDLELDIIPASLSDREVKLRDANHEINEEKRKSARKKEFIMAELLQTEKAYVRDLHECLETYLWEMTSGVEEIPPGILNKEHIIFGNIQEIYDFHNNIFLKELEKYEQLPEDVGHCFVTWADKFQMYVTYCKNKPDSNQLILEHAGTFFDEIQQRHGLANSISSYLIKPVQRVTKYQLLLKELLTCCEEGKGELKDGLEVMLSVPKKANDAMHVSMLEGFDENLDVQGELILQDAFQVWDPKSLIRKGRERHLFLFEISLVFSKEIKDSSGHTKYVYKNKLLTSELGVTEHVEGDPCKFALWSGRTPSSDNKTVLKASNIETKQEWIKNIREVIQERIIHLKGALKEPIQLPKTPAKLRNNSKRDGVEDGDSQGDGSSQPDTISIASRTSQNTVESDKLSGGCELTVVLQDFSAGHSSELSIQVGQTVELLERPSERPGWCLVRTTERSPPQEGLVPSSALCISHSRSSVEMDCFFPLKDSYSHSSSENGGKSESVAHLQSQPSLNSIHSSPGPKRSTNTLKKWLTSPVRRLNSGKADGNIKKQKKVRDGRKSFDLGSPKPGDETTPQGDSADEKSKKGWGEDEPDEESHTPLPPPMKIFDNDPTQDEMSSLLAARQAPPDVPTAADLVSAIEKLVKNKLTLEGGSYRGSLKDPTGCLNEGMTPPTPPRNLEEEQKAKALRGRMFVLNELVQTEKDYVKDLGIVVEGFMKRIEEKGVPEDMRGKEKIVFGNIHQIYDWHKDFFLAELEKCIQEQDRLAQLFIKHERKLHIYVWYCQNKPRSEYIVAEYDAYFEEVKQEINQRLTLSDFLIKPIQRITKYQLLLKDFLRYSEKAGLECSDIEKAVELMCLVPKRCNDMMNLGRLQGFEGTLTAQGKLLQQDTFYVIELDAGMQSRTKERRVFLFEQIVIFSELLRKGSLTPGYMFKRSIKMNYLVLEDNVDGDPCKFALMNRETSERVILQAANSDIQQAWVQDINQVLETQRDFLNALQSPIEYQRKERSTAVIRSQPPRVPQASPRPYSSGPVGSEKPPKGSSYNPPLPPLKISTSNGSPGFDYHQPGDKFDASKQNDLGGCNGTSTMTVIKDYYALKENEICVSQGEVVQVLAVNQQNMCLVYQPASDHSPAAEGWVPGSILAPLAKATAAAESSDGSIKKSCSWHTLRMRKRADVENSGKNEATGPRKPKDILGNKVSVKETNSSEESECDDLDPNTSMEILNPNFIQEVAPEFLVPLVDVTCLLGDTVLLQCKACGRPKPSITWKGPDQNILDTDNSSATYTISSCDSGESTLKICNLMPQDSGIYTCIAANDHGTASTSATVKVQGVPAAPNRPIAQERSCTSVILRWLPPASTGNCTISGYTVEYREEGSQVWQQSVASTLDTYLVIEDLSPGCPYQFRVSASNPWGISLPSEPSEFVRLPEYDAAADGATISWKENFDSAYTELNEIGRGRFSIVKKCIHKATRKDVAVKFVSKKMKKKEQAAHEAALLQHLQHPQYVTLHDTYESPTSYILILELMDDGRLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVPRVKLIDLEDAVQISGHFHIHHLLGNPEFAAPEVIQGIPVSLGTDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPHEYFCGVSNAARDFINVILQEDFRRRPTAATCLQHPWLQPHNGSYSKIPLDTSRLACFIERRKHQNDVRPIPNVKSYIVNRVNQGTSLSHNP
|
2.7.11.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O60229};
|
adult locomotory behavior [GO:0008344]; axon guidance [GO:0007411]; axonogenesis [GO:0007409]; habituation [GO:0046959]; intracellular signal transduction [GO:0035556]; lactation [GO:0007595]; maternal behavior [GO:0042711]; maternal process involved in parturition [GO:0060137]; memory [GO:0007613]; modification of postsynaptic actin cytoskeleton [GO:0098885]; negative regulation of growth hormone secretion [GO:0060125]; nervous system development [GO:0007399]; neuromuscular junction development [GO:0007528]; neurotransmitter receptor localization to postsynaptic specialization membrane [GO:0099645]; NMDA selective glutamate receptor signaling pathway [GO:0098989]; phosphorylation [GO:0016310]; positive regulation of dendritic spine morphogenesis [GO:0061003]; regulation of dendrite development [GO:0050773]; regulation of modification of postsynaptic actin cytoskeleton [GO:1905274]; regulation of neurotransmitter receptor localization to postsynaptic specialization membrane [GO:0098696]; social behavior [GO:0035176]
|
cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extrinsic component of membrane [GO:0019898]; glutamatergic synapse [GO:0098978]; neuronal cell body [GO:0043025]; nucleoplasm [GO:0005654]; perinuclear region of cytoplasm [GO:0048471]; postsynaptic density [GO:0014069]; presynapse [GO:0098793]
|
ATP binding [GO:0005524]; enzyme binding [GO:0019899]; guanyl-nucleotide exchange factor activity [GO:0005085]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF13716;PF00041;PF07679;PF00169;PF00069;PF00621;PF16609;PF00018;PF00435;
|
1.20.58.60;3.40.525.10;1.20.900.10;2.60.40.10;2.30.29.30;2.30.30.40;1.10.510.10;
|
Protein kinase superfamily, CAMK Ser/Thr protein kinase family
|
PTM: Autophosphorylated. {ECO:0000250|UniProtKB:O60229}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O60229, ECO:0000250|UniProtKB:P97924}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O60229, ECO:0000250|UniProtKB:P97924}.
|
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:O60229}; 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:O60229};
| null | null | null | null |
FUNCTION: Promotes the exchange of GDP by GTP. Activates specific Rho GTPase family members, thereby inducing various signaling mechanisms that regulate neuronal shape, growth, and plasticity, through their effects on the actin cytoskeleton. Induces lamellipodia independent of its GEF activity (By similarity). {ECO:0000250|UniProtKB:P97924}.
|
Mus musculus (Mouse)
|
A2CG63
|
ARI4B_MOUSE
|
MKALDEPPYLTVGTDVSAKYRGAFCEAKIKTAKRLVKVKVTFRHDSSTVEVQDDHIKGPLKVGAIVEVKNLDGAYQEAVINKLTDASWYTVVFDDGDEKTLRRSSLCLKGERHFAESETLDQLPLTNPEHFGTPVIGKKTNRGRRSNHIPEEESSSSSSDDDEEERKQTDELLGKVVCVDYVSLEKKKAMWFPALVVCPDCSDEIAVKKDNILVRSFKDGKFTSVPRKDVHEITSDTVPKPDAVLKQAFDQALEFHKSRAIPANWKTELKEDSSSSEAEEEEEEEDDEKEKEDNSSEEEEEIEPFPEERENFLQQLYKFMEDRGTPINKRPVLGYRNLNLFKLFRLVHKLGGFDNIESGAVWKQVYQDLGIPVLNSAAGYNVKCAYKKYLYGFEEYCRSANIDFQMALPEKVLNKPCKDCENKEVKVKEESETEIKEVNVEDSKNVMPKEETPAEDESERKENIKPSLGSKKSLLECIPAQSDEEKEAHITKLEENENLEDKDGGRARTEEAFSTEVDGEEEQARSGDETNKEEDEDDEEIEEEEEEDEEEDEDEDDDDNNEEEEFECYPPGMKVQVRYGRGKNQKMYEASIKDSDVEGGEALYLVHYCGWNVRYDEWIKADKIVRPADKNVPKIKHRKKIKNKLDKEKDRDEKYSPKNCKLRRLSKSPFQSNPSPEMVSKLDLADAKNSDTAHIKSIEITSILNGLQASESSAEDSEQEDERCTQDVDNIGKDESKVEHSTHSRNELISKEEQSSPSLLEENKVHTDLVIAKTVSKSPERLRKDMEAISEDTDFEEEDEITKKRKDVKKDTTDKALKPQTKRGKRRYCSADECLQTGSPGKKEDRTKSKEPLCTENSSNSSSDEDEEEKSKAKMTPTKKYNGLEEKRKSLRTTSFYSGFSEVAEKRIKLLNNSDERLQNNRAKDRKDVWSSIQGQWPKKTLKELFSDSDTEAAASPPHPAPDEGAVEESLQTVAEEESCSPIMELEKPLPASVDNKPIEEKPLEVSDRKTEFPSSGSNSVLNTPPTTPESPSSVTITEASQQQSSVTVSVPLPPNQEEVRSIKSETDSTIEVDSVVGELQDLQSEGNSSPAGFDASVSSSSSNQPEPDNPEKACTGQKRVKDTQGVGSSSKKQKRSHKATVVNNKKKGKGTNSSDSEELSAGESVTKTQTIKSVPTGMKTHNSKSPARVQSPGKGGRNGDKDPDLKEPSNRLPKVYKWSFQTSDLENMTSAERISILQEKLQEIRKHYLSLKSEVASIDRRRKRLKKKERESAATSSSSSSPSSSSITAAVMLTLAEPSMSSASQNGMSVECR
| null | null |
chromatin organization [GO:0006325]; establishment of Sertoli cell barrier [GO:0097368]; genomic imprinting [GO:0071514]; negative regulation of cell migration [GO:0030336]; negative regulation of stem cell population maintenance [GO:1902455]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; positive regulation of stem cell population maintenance [GO:1902459]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]; spermatogenesis [GO:0007283]; transcription by RNA polymerase II [GO:0006366]
|
cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
transcription cis-regulatory region binding [GO:0000976]
|
PF01388;PF08169;PF11717;
|
2.30.30.140;1.10.150.60;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355}.
| null | null | null | null | null |
FUNCTION: Acts as a transcriptional repressor. May function in the assembly and/or enzymatic activity of the Sin3A corepressor complex or in mediating interactions between the complex and other regulatory complexes (By similarity). Plays a role in the regulation of epigenetic modifications at the PWS/AS imprinting center near the SNRPN promoter, where it might function as part of a complex with RB1 and ARID4A (PubMed:17043311). Involved in spermatogenesis, together with ARID4A, where it functions as a transcriptional coactivator for AR (androgen receptor) and enhances expression of genes required for sperm maturation. Regulates expression of the tight junction protein CLDN3 in the testis, which is important for integrity of the blood-testis barrier (PubMed:23487765). Plays a role in myeloid homeostasis where it regulates the histone methylation state of bone marrow cells and expression of various genes involved in hematopoiesis. May function as a leukemia suppressor (PubMed:18728284). {ECO:0000250|UniProtKB:Q4LE39, ECO:0000269|PubMed:17043311, ECO:0000269|PubMed:18728284, ECO:0000269|PubMed:23487765}.
|
Mus musculus (Mouse)
|
A2CI34
|
DUSTY_PIMPR
|
MENPQKAGPLLRDLTRAFSHYNKHNLLLKKNLKETIAFFREIRQNHSNTCSTSGPELDSGQLRCISFPRHDEDHLQKVVGCAPYILILGQDCSARYQLLNCMLGERLLPLGSDAGGACGVEGGACRRRKLCFTHGRQTRLSLALPGQYELVHQLAAHCGRWDTVPREDLEIQECEDPAQRLAELEITLHHALLQEAKIMVLPCRNVQPVEEALEDCRRGILPIILYAVSKATLSADQLSELQKVRETLPYPVCFVRIPTEPAPDPPGQRSALFAQLVSQELIGGAAGNCACGAPAQTPGKMQGILGEDLERLHRVLVPFARQVLQSQQVEATTLLNAVHCRCLDLFINQAFDMQRDLQITPRRLEYTREKEGELYSSLMAIANRKQEEMKEMIVETLESMKEQLLEDAANLEFTDIIMTSNSEPMSSKDIKVCISQIQDLIVIRLNQAVANKLTSSVDYLRESFVGTLERCLCSLEKSTGEPCAHNVTSNHLKQILNAAYHVEVTFHSGSSVTRLFWEQIKQIIHRISWVNPPSVTSEWKRKVAQDAIESLSAAKLAKSICSQFRTRLNSSHEAFASSLRQLEEGHTGRLERTEDLWLRVRKDHAPRLARLSLESRSLRDILLHGKPKLGRELGRGQYGVVYLCDNWAGRHPCALKSVVPPDDKHWNDLALEFHYTRSLPKHERLVNLHGSVIDHSYGGGSSIAVLLIMERLHRDLYTGLKAGLVLKERLQIALDVVEGIRFLHGQGLLHRDIKLKNVLLDKQNRAKITDLGFCKPEAMMSGSIVGTPIHMAPELFTGKYDNSVDVYAFGILFWYLCTGSVKLPEAFERCSSKDQLWTNVKKGSRPERLASFDEECWQLMEACWNGDPSQRPLLGIVQPSLQSIMDRLCNDSDQKSGNLEDSN
|
2.7.12.1
| null |
cellular response to fibroblast growth factor stimulus [GO:0044344]; embryonic organ development [GO:0048568]; negative regulation of apoptotic process [GO:0043066]; phosphorylation [GO:0016310]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of fibroblast growth factor receptor signaling pathway [GO:0045743]
|
anchoring junction [GO:0070161]; apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; cytoplasm [GO:0005737]
|
ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein serine/threonine/tyrosine kinase activity [GO:0004712]; protein tyrosine kinase activity [GO:0004713]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6XUX1}. Cell membrane {ECO:0000250|UniProtKB:Q6XUX1}. Apical cell membrane {ECO:0000250|UniProtKB:Q6XUX1}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q6XUX1}. Cell junction {ECO:0000250|UniProtKB:Q6XUX1}.
|
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=2.7.12.1; Evidence={ECO:0000250|UniProtKB:P16879}; 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=2.7.12.1; Evidence={ECO:0000250|UniProtKB:P16879}; 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=2.7.12.1; Evidence={ECO:0000250|UniProtKB:P16879};
| null | null | null | null |
FUNCTION: May act as a positive regulator of ERK phosphorylation downstream of fibroblast growth factor-receptor activation. May induce both caspase-dependent apoptosis and caspase-independent cell death. May play a role in the embryonic development. {ECO:0000250|UniProtKB:Q4VSN1, ECO:0000250|UniProtKB:Q6XUX3}.
|
Pimephales promelas (Fathead minnow)
|
A2CI35
|
DUSTY_STRPU
|
MSSRRLGSSRARGRDLAHEVKHFGGLTKHLKKIIFDSNNCLTELKTSDHFEEEVISTLVLPPVADEIVGKVTKNPPALVIFGQTYTSKATLVNKIFREDLFQIVDDSDNNKTWRAVHLKYGSQRNTRLTLTNSFELLNEEPGSPVMRNSWTGIPRVEMLVKEEHQKDACMLSATTEATLNHPLLQCKLQILVTPHNCPGISISQAYNVCTHNVLPVLLYCFDKDQLSEENLRDLQELQNCAGTLPILFVDCREPSEPLVAHRERRLVEDAHEDFDDDSAYDTDERIEGERERHNGLDARLRRRCRPTPNDRPSVIDQLSRAGFISSPEENGRMRGVLDVFTIVNQVEDLHNSAAIVQFIRRSLQYYLIRCCTAMHDLHQHCMNLFITTAFDMQRDILVTPKRIEYARQRENELFDSLKDLTNQKQEQLRSLIQSTVADMTEDLLEQAGNYRFTDLEVSQEGKIQSQKDIKRCTEQIQDLVLARLNACVVEKLIGSVELLRESFLGTLQRCLASLEKIDGDLETSTTVALRQILNAAYQVEVSVRTSSSVVRIIWERMKEFFQSIKPFKTPTRVDTEWKRKVAQTMINNLDESKLAKSICSQFRSRLNNSHESFSTSLRQLEQKHSGRLEKTEEQRMKVRKVYAPRLARLALESTSLRDMVLYGMPKLEREIGRGQYGVVYSCRSWGGVTHCAVKSVVPPDDKHWNDLAMEFHYTRSIAEHDRIVAVIGSVIDHGYGGMGCSPAVLLLMERMQRDLHTAIKANMELPERLHVALDVAEGVRYLHSLGLVHRDIKLKNVLLDKHDRGKITDLGFCKPEAMMSGSIVGTPIHMAPELFSGKYDNSVDTYAFGILLWYVCAGHVKLPQAFEQCANKDHLWTSVKKGVRPERLRPQFDDASWNLMKSSWAGEPSERPLLGEVQSKLQDIYTKALAKREAEGGGGGGAKEQQNLKSDTL
|
2.7.12.1
| null |
cellular response to fibroblast growth factor stimulus [GO:0044344]; embryonic organ development [GO:0048568]; negative regulation of apoptotic process [GO:0043066]; phosphorylation [GO:0016310]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of fibroblast growth factor receptor signaling pathway [GO:0045743]
|
anchoring junction [GO:0070161]; apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; cytoplasm [GO:0005737]
|
ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein serine/threonine/tyrosine kinase activity [GO:0004712]; protein tyrosine kinase activity [GO:0004713]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6XUX1}. Cell membrane {ECO:0000250|UniProtKB:Q6XUX1}. Apical cell membrane {ECO:0000250|UniProtKB:Q6XUX1}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q6XUX1}. Cell junction {ECO:0000250|UniProtKB:Q6XUX1}.
|
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=2.7.12.1; Evidence={ECO:0000250|UniProtKB:P16879}; 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=2.7.12.1; Evidence={ECO:0000250|UniProtKB:P16879}; 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=2.7.12.1; Evidence={ECO:0000250|UniProtKB:P16879};
| null | null | null | null |
FUNCTION: May act as a positive regulator of ERK phosphorylation downstream of fibroblast growth factor-receptor activation. May induce both caspase-dependent apoptosis and caspase-independent cell death. May play a role in the embryonic development. {ECO:0000250|UniProtKB:Q4VSN1, ECO:0000250|UniProtKB:Q6XUX3}.
|
Strongylocentrotus purpuratus (Purple sea urchin)
|
A2D4U1
|
OSTCN_ATEGE
|
MRALTLLALLALATLCITGQAGAKPSGAESSKGAAFVSKQEGSEVVKRPRRYLYQWLGAPAPYPDPLEPKREVCELNPDCDELADHIGFQEAYRRFYGPV
| null | null |
biomineral tissue development [GO:0031214]; bone development [GO:0060348]; brain development [GO:0007420]; cellular response to insulin stimulus [GO:0032869]; cognition [GO:0050890]; glucose homeostasis [GO:0042593]; learning or memory [GO:0007611]; negative regulation of bone development [GO:1903011]; osteoblast differentiation [GO:0001649]; positive regulation of neurotransmitter secretion [GO:0001956]; regulation of bone mineralization [GO:0030500]; regulation of cellular response to insulin stimulus [GO:1900076]; regulation of testosterone biosynthetic process [GO:2000224]; response to vitamin K [GO:0032571]; type B pancreatic cell proliferation [GO:0044342]
|
cytoplasm [GO:0005737]; extracellular region [GO:0005576]
|
calcium ion binding [GO:0005509]; hormone activity [GO:0005179]; hydroxyapatite binding [GO:0046848]; structural constituent of bone [GO:0008147]
| null | null |
Osteocalcin/matrix Gla protein family
|
PTM: Gamma-carboxyglutamate residues are formed by vitamin K dependent carboxylation by GGCX. These residues are essential for the binding of calcium (By similarity). Decarboxylation promotes the hormone activity (By similarity). {ECO:0000250|UniProtKB:P86546, ECO:0000255|PROSITE-ProRule:PRU00463}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P86546}.
| null | null | null | null | null |
FUNCTION: The carboxylated form is one of the main organic components of the bone matrix, which constitutes 1-2% of the total bone protein: it acts as a negative regulator of bone formation and is required to limit bone formation without impairing bone resorption or mineralization. The carboxylated form binds strongly to apatite and calcium. {ECO:0000250|UniProtKB:P86546}.; FUNCTION: The uncarboxylated form acts as a hormone secreted by osteoblasts, which regulates different cellular processes, such as energy metabolism, male fertility and brain development. Regulates of energy metabolism by acting as a hormone favoring pancreatic beta-cell proliferation, insulin secretion and sensitivity and energy expenditure. Uncarboxylated osteocalcin hormone also promotes testosterone production in the testes: acts as a ligand for G protein-coupled receptor GPRC6A at the surface of Leydig cells, initiating a signaling response that promotes the expression of enzymes required for testosterone synthesis in a CREB-dependent manner. Also acts as a regulator of brain development: osteocalcin hormone crosses the blood-brain barrier and acts as a ligand for GPR158 on neurons, initiating a signaling response that prevents neuronal apoptosis in the hippocampus, favors the synthesis of all monoamine neurotransmitters and inhibits that of gamma-aminobutyric acid (GABA). Osteocalcin also crosses the placenta during pregnancy and maternal osteocalcin is required for fetal brain development. {ECO:0000250|UniProtKB:P86546}.
|
Ateles geoffroyi (Black-handed spider monkey) (Geoffroy's spider monkey)
|
A2D5H2
|
SIX1_LAGLA
|
MSMLPSFGFTQEQVACVCEVLQQGGNLERLGRFLWSLPACDHLHKNESVLKAKAVVAFHRGNFRELYKILESHQFSPHNHPKLQQLWLKAHYVEAEKLRGRPLGAVGKYRVRRKFPLPRTIWDGEETSYCFKEKSRGVLREWYAHNPYPSPREKRELAEATGLTTTQVSNWFKNRRQRDRAAEAKERENTENNNSSSNKQNQLSPLEGGKPLMSSSEEEFSPPQSPDQNSVLLLQGNMGHARSSNYSLPGLTASQPSHGLQAHQHQLQDSLLGPLTSSLVDLGS
| null | null |
apoptotic process [GO:0006915]; branching involved in ureteric bud morphogenesis [GO:0001658]; embryonic cranial skeleton morphogenesis [GO:0048701]; embryonic skeletal system morphogenesis [GO:0048704]; epithelial cell differentiation [GO:0030855]; generation of neurons [GO:0048699]; inner ear development [GO:0048839]; inner ear morphogenesis [GO:0042472]; kidney development [GO:0001822]; mesonephric tubule formation [GO:0072172]; metanephric mesenchyme development [GO:0072075]; myoblast migration [GO:0051451]; negative regulation of neuron apoptotic process [GO:0043524]; organ induction [GO:0001759]; pattern specification process [GO:0007389]; positive regulation of branching involved in ureteric bud morphogenesis [GO:0090190]; positive regulation of brown fat cell differentiation [GO:0090336]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of ureteric bud formation [GO:0072107]; regulation of branch elongation involved in ureteric bud branching [GO:0072095]; regulation of DNA-templated transcription [GO:0006355]; regulation of neuron differentiation [GO:0045664]; regulation of skeletal muscle cell proliferation [GO:0014857]; skeletal muscle fiber development [GO:0048741]; skeletal muscle tissue development [GO:0007519]; thymus development [GO:0048538]; thyroid gland development [GO:0030878]; ureteric bud development [GO:0001657]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667]
|
DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]
|
PF05920;PF16878;
|
1.10.10.60;
|
SIX/Sine oculis homeobox family
|
PTM: Phosphorylated during interphase; becomes hyperphosphorylated during mitosis. Hyperphosphorylation impairs binding to promoter elements (By similarity). {ECO:0000250}.; PTM: Ubiquitinated by the anaphase promoting complex (APC), leading to its proteasomal degradation. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q15475}. Cytoplasm {ECO:0000250|UniProtKB:Q15475}.
| null | null | null | null | null |
FUNCTION: Transcription factor that is involved in the regulation of cell proliferation, apoptosis and embryonic development (By similarity). Plays an important role in the development of several organs, including kidney, muscle and inner ear (By similarity). Depending on context, functions as a transcriptional repressor or activator (By similarity). Lacks an activation domain, and requires interaction with EYA family members for transcription activation (By similarity). Mediates nuclear translocation of EYA1 and EYA2 (By similarity). Binds the 5'-TCA[AG][AG]TTNC-3' motif present in the MEF3 element in the MYOG promoter and CIDEA enhancer (By similarity). Regulates the expression of numerous genes, including MYC, CCNA1, CCND1 and EZR (By similarity). Acts as an activator of the IGFBP5 promoter, probably coactivated by EYA2 (By similarity). Repression of precursor cell proliferation in myoblasts is switched to activation through recruitment of EYA3 to the SIX1-DACH1 complex (By similarity). During myogenesis, seems to act together with EYA2 and DACH2 (By similarity). Regulates the expression of CCNA1 (By similarity). Promotes brown adipocyte differentiation (By similarity). {ECO:0000250|UniProtKB:Q15475, ECO:0000250|UniProtKB:Q62231}.
|
Lagothrix lagotricha (Brown woolly monkey) (Humboldt's woolly monkey)
|
A2D670
|
OSTCN_MACMU
|
MRALTLLALLALATLCITGQAGAKPSGAESSKGAAFVSKQEGSEVVKRPRRYLYQWLGAPAPYPDPLEPKREVCELNPDCDELADHIGFQEAYRRFYGPV
| null | null |
biomineral tissue development [GO:0031214]; bone development [GO:0060348]; brain development [GO:0007420]; cellular response to insulin stimulus [GO:0032869]; cognition [GO:0050890]; glucose homeostasis [GO:0042593]; learning or memory [GO:0007611]; negative regulation of bone development [GO:1903011]; osteoblast differentiation [GO:0001649]; positive regulation of neurotransmitter secretion [GO:0001956]; regulation of bone mineralization [GO:0030500]; regulation of cellular response to insulin stimulus [GO:1900076]; regulation of testosterone biosynthetic process [GO:2000224]; response to vitamin K [GO:0032571]; type B pancreatic cell proliferation [GO:0044342]
|
cytoplasm [GO:0005737]; extracellular region [GO:0005576]
|
calcium ion binding [GO:0005509]; hormone activity [GO:0005179]; hydroxyapatite binding [GO:0046848]; structural constituent of bone [GO:0008147]
| null | null |
Osteocalcin/matrix Gla protein family
|
PTM: Gamma-carboxyglutamate residues are formed by vitamin K dependent carboxylation by GGCX. These residues are essential for the binding of calcium (By similarity). Decarboxylation promotes the hormone activity (By similarity). {ECO:0000250|UniProtKB:P86546, ECO:0000255|PROSITE-ProRule:PRU00463}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P86546}.
| null | null | null | null | null |
FUNCTION: The carboxylated form is one of the main organic components of the bone matrix, which constitutes 1-2% of the total bone protein: it acts as a negative regulator of bone formation and is required to limit bone formation without impairing bone resorption or mineralization. The carboxylated form binds strongly to apatite and calcium. {ECO:0000250|UniProtKB:P86546}.; FUNCTION: The uncarboxylated form acts as a hormone secreted by osteoblasts, which regulates different cellular processes, such as energy metabolism, male fertility and brain development. Regulates of energy metabolism by acting as a hormone favoring pancreatic beta-cell proliferation, insulin secretion and sensitivity and energy expenditure. Uncarboxylated osteocalcin hormone also promotes testosterone production in the testes: acts as a ligand for G protein-coupled receptor GPRC6A at the surface of Leydig cells, initiating a signaling response that promotes the expression of enzymes required for testosterone synthesis in a CREB-dependent manner. Also acts as a regulator of brain development: osteocalcin hormone crosses the blood-brain barrier and acts as a ligand for GPR158 on neurons, initiating a signaling response that prevents neuronal apoptosis in the hippocampus, favors the synthesis of all monoamine neurotransmitters and inhibits that of gamma-aminobutyric acid (GABA). Osteocalcin also crosses the placenta during pregnancy and maternal osteocalcin is required for fetal brain development. {ECO:0000250|UniProtKB:P86546}.
|
Macaca mulatta (Rhesus macaque)
|
A2ICN5
|
MEF2A_PIG
|
MGRKKIQITRIMDERNRQVTFTKRKFGLMKKAYELSVLCDCEIALIIFNSSNKLFQYASTDMDKVLLKYTEYNEPHESGTNSDIVEALNKKEHRGCDSPDPDTSYVLTPHTEEKYKKINEEFDNMMRNHKIAPGLPPQNFSMSVTVPVTSPNALSYTNPGSSLVSPSLAASSTLADSSMLSPPQATLHRNVSPGAPQRPPSTGSAGGMLSTSDLTVPNGAGSSPVGNGFVNSRASPNLVGTTGANSLGKVMPTESPPPPGGGNLGMNSRKPDLRVVIPPSSKGMMPPLSEEEELELNTQRISSSQAPQPLATPVVSVTTPSLPQQGLVYSAMPTAYNTDYSLTSADLSALQGFNSPGMLSLGQVSAWQQHHLGQAALSSLVAGGQLSQGSNLSINTNQNINIKSEPISPPRDRMTPSGFQQQQPPPPSQAPQPQPPQPQPQPQPQARQEMGRSPVDSLSSSSSSYDGSDREDPRGDFHSPVVLGRPPNTEDRESPSVKRMRMDAWVT
| null | null |
apoptotic process [GO:0006915]; cardiac conduction [GO:0061337]; cellular response to calcium ion [GO:0071277]; dendrite morphogenesis [GO:0048813]; ERK5 cascade [GO:0070375]; MAPK cascade [GO:0000165]; mitochondrial genome maintenance [GO:0000002]; mitochondrion distribution [GO:0048311]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]; ventricular cardiac myofibril assembly [GO:0055005]
|
nucleus [GO:0005634]
|
chromatin binding [GO:0003682]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription factor binding [GO:0140297]; histone acetyltransferase binding [GO:0035035]; histone deacetylase binding [GO:0042826]; protein dimerization activity [GO:0046983]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; SMAD binding [GO:0046332]
|
PF12347;PF00319;
|
3.40.1810.10;
|
MEF2 family
|
PTM: Constitutive phosphorylation on Ser-408 promotes Lys-403 sumoylation thus preventing acetylation at this site. Dephosphorylation on Ser-408 by PPP3CA upon neuron depolarization promotes a switch from sumoylation to acetylation on residue Lys-403 leading to inhibition of dendrite claw differentiation. Phosphorylation on Thr-312 and Thr-319 are the main sites involved in p38 MAPK signaling and activate transcription. Phosphorylated on these sites by MAPK14/p38alpha and MAPK11/p38beta, but not by MAPK13/p38delta nor by MAPK12/p38gamma. Phosphorylation on Ser-408 by CDK5 induced by neurotoxicity inhibits MEF2A transcriptional activation leading to apoptosis of cortical neurons. Phosphorylation on Thr-312, Thr-319 and Ser-355 can be induced by EGF (By similarity). {ECO:0000250}.; PTM: Sumoylation on Lys-403 is enhanced by PIAS1 and represses transcriptional activity. Phosphorylation on Ser-408 is required for sumoylation. Has no effect on nuclear location nor on DNA binding. Sumoylated with SUMO1 and, to a lesser extent with SUMO2 and SUMO3. PIASx facilitates sumoylation in postsynaptic dendrites in the cerebellar cortex and promotes their morphogenesis (By similarity). {ECO:0000250}.; PTM: Acetylation on Lys-403 activates transcriptional activity. Acetylated by p300 on several sites in diffentiating myocytes. Acetylation on Lys-4 increases DNA binding and transactivation (By similarity). Hyperacetylation by p300 leads to enhanced cardiac myocyte growth and heart failure (By similarity). {ECO:0000250}.; PTM: Proteolytically cleaved on several sites by caspase 3 and caspase 7 following neurotoxicity. Preferentially cleaves the CDK5-mediated hyperphosphorylated form which leads to cortical neuron apoptosis and transcriptional inactivation (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251}.
| null | null | null | null | null |
FUNCTION: Transcriptional activator which binds specifically to the MEF2 element, 5'-YTA[AT](4)TAR-3', found in numerous muscle-specific genes. Also involved in the activation of numerous growth factor- and stress-induced genes. Mediates cellular functions not only in skeletal and cardiac muscle development, but also in neuronal differentiation and survival. Plays diverse roles in the control of cell growth, survival and apoptosis via p38 MAPK signaling in muscle-specific and/or growth factor-related transcription. In cerebellar granule neurons, phosphorylated and sumoylated MEF2A represses transcription of NUR77 promoting synaptic differentiation. Associates with chromatin to the ZNF16 promoter (By similarity). {ECO:0000250}.
|
Sus scrofa (Pig)
|
A2IDD5
|
CCD78_HUMAN
|
MEHAATTGPRPGPPSRRVENVVLRAKDWLPGAPGGTAVWATSLEAEVPPDLALNKEQQLQISKELVDIQITTHHLHEQHEAEIFQLKSEILRLESRVLELELRGDGTSQGCAVPVESDPRHPRAAAQELRHKAQVPGHSDDHRFQVQPKNTMNPENEQHRLGSGLQGEVKWALEHQEARQQALVTRVATLGRQLQGAREEARAAGQRLATQAVVLCSCQGQLRQAEAENARLQLQLKKLKDEYVLRLQHCAWQAVEHADGAGQAPATTALRTFLEATLEDIRAAHRSREQQLARAARSYHKRLVDLSRRHEELLVAYRAPGNPQAIFDIASLDLEPLPVPLVTDFSHREDQHGGPGALLSSPKKRPGGASQGGTSEPQGLDAASWAQIHQKLRDFSRSTQSWNGSGHSCWSGPRWLKSNFLSYRSTWTSTWAGTSTKS
| null | null |
cell projection organization [GO:0030030]; de novo centriole assembly involved in multi-ciliated epithelial cell differentiation [GO:0098535]; skeletal muscle contraction [GO:0003009]
|
centriole [GO:0005814]; cytoplasm [GO:0005737]; deuterosome [GO:0098536]; perinuclear region of cytoplasm [GO:0048471]; sarcolemma [GO:0042383]; sarcoplasmic reticulum [GO:0016529]
| null |
PF14739;
| null |
CCDC78 family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Cytoplasm, perinuclear region. Cell membrane, sarcolemma. Sarcoplasmic reticulum. Note=Localizes to centrioles and deuterosome. Found primarily in the perinuclear region as well as along the sarcolemmal membrane and in reticular pattern within the sarcoplasm.
| null | null | null | null | null |
FUNCTION: Component of the deuterosome, a structure that promotes de novo centriole amplification in multiciliated cells that can generate more than 100 centrioles. Deuterosome-mediated centriole amplification occurs in terminally differentiated multiciliated cells (G1/0) and not in S phase. Essential for centriole amplification and is required for CEP152 localization to the deuterosome. {ECO:0000269|PubMed:24075808}.
|
Homo sapiens (Human)
|
A2PYH4
|
HFM1_HUMAN
|
MLKSNDCLFSLENLFFEKPDEVENHPDNEKSLDWFLPPAPLISEIPDTQELEEELESHKLLGQEKRPKMLTSNLKITNEDTNYISLTQKFQFAFPSDKYEQDDLNLEGVGNNDLSHIAGKLTYASQKYKNHIGTEIAPEKSVPDDTKLVNFAEDKGESTSVFRKRLFKISDNIHGSAYSNDNELDSHIGSVKIVQTEMNKGKSRNYSNSKQKFQYSANVFTANNAFSASEIGEGMFKAPSFSVAFQPHDIQEVTENGLGSLKAVTEIPAKFRSIFKEFPYFNYIQSKAFDDLLYTDRNFVICAPTGSGKTVVFELAITRLLMEVPLPWLNIKIVYMAPIKALCSQRFDDWKEKFGPIGLNCKELTGDTVMDDLFEIQHAHIIMTTPEKWDSMTRKWRDNSLVQLVRLFLIDEVHIVKDENRGPTLEVVVSRMKTVQSVSQTLKNTSTAIPMRFVAVSATIPNAEDIAEWLSDGERPAVCLKMDESHRPVKLQKVVLGFPCSSNQTEFKFDLTLNYKIASVIQMYSDQKPTLVFCATRKGVQQAASVLVKDAKFIMTVEQKQRLQKYAYSVRDSKLRDILKDGAAYHHAGMELSDRKVVEGAFTVGDLPVLFTTSTLAMGVNLPAHLVVIKSTMHYAGGLFEEYSETDILQMIGRAGRPQFDTTATAVIMTRLSTRDKYIQMLACRDTVESSLHRHLIEHLNAEIVLHTITDVNIAVEWIRSTLLYIRALKNPSHYGFASGLNKDGIEAKLQELCLKNLNDLSSLDLIKMDEGVNFKPTEAGRLMAWYYITFETVKKFYTISGKETLSDLVTLIAGCKEFLDIQLRINEKKTLNTLNKDPNRITIRFPMEGRIKTREMKVNCLIQAQLGCIPIQDFALTQDTAKIFRHGSRITRWLSDFVAAQEKKFAVLLNSLILAKCFRCKLWENSLHVSKQLEKIGITLSNAIVNAGLTSFKKIEETDARELELILNRHPPFGTQIKETVMYLPKYELKVEQITRYSDTTAEILVTVILRNFEQLQTKRTASDSHYVTLIIGDADNQVVYLHKITDSVLLKAGSWAKKIAVKRALKSEDLSINLISSEFVGLDIQQKLTVFYLEPKRFGNQITMQRKSETQISHSKHSDISTIAGPNKGTTASKKPGNRECNHLCKSKHTCGHDCCKIGVAQKSEIKESTISSYLSDLRNRNAVSSVPPVKRLKIQMNKSQSVDLKEFGFTPKPSLPSISRSEYLNISELPIMEQWDQPEIYGKVRQEPSEYQDKEVLNVNFELGNEVWDDFDDENLEVTSFSTDTEKTKISGFGNTLSSSTRGSKLPLQESKSKFQREMSNSFVSSHEMSDISLSNSAMPKFSASSMTKLPQQAGNAVIVHFQERKPQNLSPEIEKQCFTFSEKNPNSSNYKKVDFFIRNSECKKEVDFSMYHPDDEADEMKSLLGIFDGIF
|
3.6.4.12
| null |
resolution of meiotic recombination intermediates [GO:0000712]
|
nucleus [GO:0005634]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA helicase activity [GO:0003678]; nucleic acid binding [GO:0003676]
|
PF00270;PF00271;PF02889;
|
3.40.50.300;1.10.3380.10;1.10.10.10;
|
Helicase family, SKI2 subfamily
| null | null |
CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
| null | null | null | null |
FUNCTION: Required for crossover formation and complete synapsis of homologous chromosomes during meiosis. {ECO:0000250|UniProtKB:D3Z4R1}.
|
Homo sapiens (Human)
|
A2PYL6
|
HXK2_HORSE
|
MIASHLLAYFFTELNHDQVQKVDQYLYHMRLSDETLLEISKRFRKEMEKGLAATTHPTASVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLRVRVTDNGLQKVEMENQIYAIPEDIMQGSGTQLFDHIAGCLANFMDKLQIKDKKLPLGFTFSFPCIQTKLDESFLVSWTKGFKSRGVEGRDVVTLIRKAIQRRGDFDIDIVAMVNDTVATMMTCGYDDQNCEIGLIVGMGSNACYMEEMRYIDTVEGDEGRMCINMEWGAFGDDGTLDDIRTEFDQEIDMGSLNPGQQLFEKMISGMYMGELVRLILVKMAKEELLFRGKLSPELLTTGRFETKDVSEIEGEKDGIQKAREVLVRLGMDPTQEDCVATHRICQIVSTRSASLCAATLAAVLQRIKENKGEERLRSTIGVDGSVYKKHPHFAKRLQKTVRRLVPNCDIRFLCSEDGSGKGAAMVTAVAYRLAYQHRARLKTLEPLKLSREQLLEVKRRMKVEMERGLSKETHASAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVRVRNGKRRGVEMHNKIYSIPQDIMHGTGDELFDHIVQCIADFLEYMGMKGVSLPLGFTFSFPCQQNRLDESILLKWTKGFKASGCEGEDVVTLLKEAIHRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVEGEEGRMCVNTEWGAFGDNGCLDDFCTEFDVAVDELSLNPGKQRFEKMMSGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDCLALQQVRAILQHLGLESTCDDSIIVKEVCTVVAQRAAQLCGAGMAAVVDKIRENRGLDTLKVTVGVDGTLYKLHPHFAKVMRETVKDLAPKCDVSFLESEDGSGKGAALITAVACRIREAGQR
|
2.7.1.1
| null |
carbohydrate phosphorylation [GO:0046835]; fructose 6-phosphate metabolic process [GO:0006002]; glucose 6-phosphate metabolic process [GO:0051156]; glucose metabolic process [GO:0006006]; glycolytic process [GO:0006096]; intracellular glucose homeostasis [GO:0001678]
|
cytosol [GO:0005829]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]
|
ATP binding [GO:0005524]; fructokinase activity [GO:0008865]; glucokinase activity [GO:0004340]; glucose binding [GO:0005536]; hexokinase activity [GO:0004396]
|
PF00349;PF03727;
|
3.30.420.40;3.40.367.20;
|
Hexokinase family
| null |
SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250|UniProtKB:P52789}; Peripheral membrane protein {ECO:0000250|UniProtKB:P52789}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P52789}. Note=The mitochondrial-binding peptide (MBP) region promotes association with the mitochondrial outer membrane. The interaction with the mitochondrial outer membrane via the mitochondrial-binding peptide (MBP) region promotes higher stability of the protein. Release from the mitochondrial outer membrane into the cytosol induces permeability transition pore (PTP) opening and apoptosis. {ECO:0000250|UniProtKB:P52789}.
|
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; Evidence={ECO:0000250|UniProtKB:P52789}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22741; Evidence={ECO:0000250|UniProtKB:P52789}; 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:0000250|UniProtKB:P27881}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16126; Evidence={ECO:0000250|UniProtKB:P27881}; 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:0000250|UniProtKB:P52789}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17826; Evidence={ECO:0000250|UniProtKB:P52789};
| null |
PATHWAY: Carbohydrate metabolism; hexose metabolism. {ECO:0000250|UniProtKB:P52789}.; PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 1/4. {ECO:0000250|UniProtKB:P52789}.
| null | null |
FUNCTION: Catalyzes the phosphorylation of hexose, such as D-glucose and D-fructose, to hexose 6-phosphate (D-glucose 6-phosphate and D-fructose 6-phosphate, respectively). Mediates the initial step of glycolysis by catalyzing phosphorylation of D-glucose to D-glucose 6-phosphate. Plays a key role in maintaining the integrity of the outer mitochondrial membrane by preventing the release of apoptogenic molecules from the intermembrane space and subsequent apoptosis. {ECO:0000250|UniProtKB:P52789}.
|
Equus caballus (Horse)
|
A2PZA5
|
FC1_PHOAM
|
MEFKYSEVVEPSTYYTEGLCEGIDVRKSKFTTLEDRGAIRAHEDWNKHIGPCGEYRGTLGPRFSFISVAVPECIPERLEVISYANEFAFLHDDVTDHVGHDTGEVENDEMMTVFLEAAHTGAIDTSNKVDIRRAGKKRIQSQLFLEMLAIDPECAKTTMKSWARFVEVGSSRQHETRFVELAKYIPYRIMDVGEMFWFGLVTFGLGLHIPDHELELCRELMANAWIAVGLQNDIWSWPKERDAATLHGKDHVVNAIWVLMQEHQTDVDGAMQICRKLIVEYVAKYLEVIEATKNDESISLDLRKYLDAMLYSISGNVVWSLECPRYNPDVSFNKTQLEWMRQGLPSLESCPVLARSPEIDSDESAVSPTADESDSTEDSLGSGSRQDSSLSTGLSLSPVHSNEGKDLQRVDTDHIFFEKAVLEAPYDYIASMPSKGVRDQFIDALNDWLRVPDVKVGKIKDAVRVLHNSSLLLDDFQDNSPLRRGKPSTHNIFGSAQTVNTATYSIIKAIGQIMEFSAGESVQEVMNSIMILFQGQAMDLFWTYNGHVPSEEEYYRMIDQKTGQLFSIATSLLLNAADNEIPRTKIQSCLHRLTRLLGRCFQIRDDYQNLVSADYTKQKGFCEDLDEGKWSLALIHMIHKQRSHMALLNVLSTGRKHGGMTLEQKQFVLDIIEEEKSLDYTRSVMMDLHVQLRAEIGRIEILLDSPNPAMRLLLELLRV
|
2.5.1.29; 4.2.3.43
| null |
alcohol biosynthetic process [GO:0046165]; isoprenoid biosynthetic process [GO:0008299]; ketone biosynthetic process [GO:0042181]; mycotoxin biosynthetic process [GO:0043386]
| null |
farnesyltranstransferase activity [GO:0004311]; lyase activity [GO:0016829]; metal ion binding [GO:0046872]
|
PF00348;PF19086;
|
1.10.600.10;
|
Terpene synthase family; FPP/GGPP synthase family
| null | null |
CATALYTIC ACTIVITY: Reaction=geranylgeranyl diphosphate = diphosphate + fusicocca-2,10(14)-diene; Xref=Rhea:RHEA:26245, ChEBI:CHEBI:33019, ChEBI:CHEBI:52463, ChEBI:CHEBI:57533; EC=4.2.3.43; Evidence={ECO:0000269|PubMed:17360612, ECO:0000269|PubMed:26734760}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate + isopentenyl diphosphate = (2E,6E,10E)-geranylgeranyl diphosphate + diphosphate; Xref=Rhea:RHEA:17653, ChEBI:CHEBI:33019, ChEBI:CHEBI:58756, ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.29; Evidence={ECO:0000269|PubMed:17360612, ECO:0000269|PubMed:26734760};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=9.2 uM for GPP {ECO:0000269|PubMed:26734760}; KM=0.14 uM for FPP {ECO:0000269|PubMed:26734760}; KM=0.632 uM for GGPP {ECO:0000269|PubMed:26734760};
|
PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:17360612, ECO:0000269|PubMed:26734760}.
| null | null |
FUNCTION: Multifunctional diterpene synthase; part of the 2 gene clusters that mediate the biosynthesis of fusicoccins, diterpene glucosides that display phytohormone-like activity and function as potent activators of plasma membrane H(+)-ATPases in plants by modifying 14-3-3 proteins and cause the plant disease constriction canker (PubMed:17360612, PubMed:26734760). The first step in the pathway is performed by the fusicoccadiene synthase PaFS that possesses both prenyl transferase and terpene cyclase activity, converting isopentenyl diphosphate and dimethylallyl diphosphate into geranylgeranyl diphosphate (GGDP) and successively converting GGDP into fusicocca-2,10(14)-diene, a precursor for fusicoccin H (PubMed:17360612, PubMed:26734760). Fusicoccadiene synthase is an allosteric enzyme for GGPP cyclization that generates 64% fusicoccadiene, 9% delta-araneosene, and one additional unidentified diterpene product, when incubated with GGPP (PubMed:26734760). In the absence of isopentenyl diphosphate (IPP), PaFS can also solvolyze the shorter chain geranyl diphosphate (GPP) and farnesyl diphosphate (FPP) as alternative substrates to yield predominantly acyclic products. FPP is converted to farnesol (60.5%), nerolidol (14.0%), and farnesene (14.0%), while GPP is converted to a mixture of geraniol (59.5%) and linalool (35.0%) (PubMed:26734760). The second step is the oxidation at the C-8 position by the cytochrome P450 monooxygenase PaP450-2 to yield fusicocca-2,10(14)-diene-8-beta-ol (PubMed:22870285). The cytochrome P450 monooxygenase PaP450-1 then catalyzes the hydroxylation at the C-16 position to produce fusicocca-2,10(14)-diene-8-beta,16-diol (PubMed:22870285). The dioxygenase fc-dox then catalyzes the 16-oxydation of fusicocca-2,10(14)-diene-8-beta,16-diol to yield an aldehyde (8-beta-hydroxyfusicocca-1,10(14)-dien-16-al) (PubMed:21299202, PubMed:22870285). The short-chain dehydrogenase/reductase fc-sdr catalyzes the reduction of the aldehyde to yield fusicocca-1,10(14)-diene-8-beta,16-diol (PubMed:21299202, PubMed:22870285). The next step is the hydroxylation at C-9 performed by the cytochrome P450 monooxygenase PaP450-3 that leads to fusicoccin H aglycon which is glycosylated to fusicoccin H by the O-glycosyltransferase PAGT (PubMed:22870285). Hydroxylation at C-12 by the cytochrome P450 monooxygenase PaP450-4 leads then to the production of fusicoccin Q and is followed by methylation by the O-methyltransferase PAMT to yield fusicoccin P (PubMed:22870285). Fusicoccin P is further converted to fusicoccin J via prenylation by the O-glucose prenyltransferase PaPT (PubMed:22287087). Cytochrome P450 monooxygenase PaP450-5 then performs hydroxylation at C-19 to yield dideacetyl-fusicoccin A which is acetylated to 3'-O-deacetyl-fusicoccin A by the O-acetyltransferase PaAT-2 (PubMed:22870285). Finally, a another acetylation by the O-acetyltransferase PaAT-1 yields fusicoccin A (PubMed:22870285). {ECO:0000269|PubMed:17360612, ECO:0000269|PubMed:21299202, ECO:0000269|PubMed:22287087, ECO:0000269|PubMed:22870285, ECO:0000269|PubMed:26734760}.
|
Phomopsis amygdali (Fusicoccum amygdali)
|
A2Q0Z0
|
EF1A1_HORSE
|
MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEAGISKNGQTREHALLAYTLGVKQLIVGVNKMDSTEPPYSQKRYEEIVKEVSTYIKKIGYNPDTVAFVPISGWNGDNMLEPSANMPWFKGWKVTRKDGNASGTTLLEALDCILPPTRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDVRRGNVAGDSKNDPPMEAAGFTAQVIILNHPGQISAGYAPVPDCHTAHIACKFAELKEKIDRRSGKKLEDGPKFLKSGDAAIVDMVPGKPMCVESFSDYPPLGRFAVRDMRQTVAVGVIKAVDKKAAGAGKVTKSAQKAQKAK
|
3.6.5.-
| null |
cellular response to epidermal growth factor stimulus [GO:0071364]; regulation of D-erythro-sphingosine kinase activity [GO:1900022]; translation [GO:0006412]; translational elongation [GO:0006414]
|
cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
GTP binding [GO:0005525]; GTPase activity [GO:0003924]; translation elongation factor activity [GO:0003746]
|
PF00009;PF03144;PF03143;
|
3.40.50.300;2.40.30.10;
|
TRAFAC class translation factor GTPase superfamily, Classic translation factor GTPase family, EF-Tu/EF-1A subfamily
|
PTM: ISGylated. {ECO:0000250|UniProtKB:P68104}.; PTM: Phosphorylated by TXK. Phosphorylation by PASK increases translation efficiency. Phosphorylated by ROCK2. Phosphorylation by TGFBR1 inhibits translation elongation. {ECO:0000250|UniProtKB:P68104}.; PTM: Trimethylated at Lys-79 by EEF1AKMT1. Methylated at Lys-165 by EEF1AKMT3, methylation by EEF1AKMT3 is dynamic as well as inducible by stress conditions, such as ER-stress, and plays a regulatory role on mRNA translation. Trimethylated at Lys-318 by EEF1AKMT2. Mono-, di-, and trimethylated at Lys-36 by EEF1AKMT4; trimethylated form is predominant. Methylation by EEF1AKMT4 contributes to the fine-tuning of translation rates for a subset of tRNAs. Trimethylated at Gly-2 by METTL13. Mono- and dimethylated at Lys-55 by METTL13; dimethylated form is predominant. {ECO:0000250|UniProtKB:P68104}.; PTM: Ubiquitinated at Lys-385 by RNF14 in response to ribosome collisions (ribosome stalling), leading to its degradation by the proteasome and rescue of stalled ribosomes. {ECO:0000250|UniProtKB:P68104}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P68104}. Nucleus {ECO:0000250|UniProtKB:P68104}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P68104}. Cell membrane {ECO:0000250|UniProtKB:P68104}. Note=Colocalizes with DLC1 at actin-rich regions in the cell periphery. Translocates together with ZPR1 from the cytoplasm to the nucleus and nucleolus after treatment with mitogens. Localization at the cell membrane depends on EEF1A1 phosphorylation status and the presence of PPP1R16B. {ECO:0000250|UniProtKB:P68104}.
|
CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:P68104}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:P68104};
| null | null | null | null |
FUNCTION: Translation elongation factor that catalyzes the GTP-dependent binding of aminoacyl-tRNA (aa-tRNA) to the A-site of ribosomes during the elongation phase of protein synthesis. Base pairing between the mRNA codon and the aa-tRNA anticodon promotes GTP hydrolysis, releasing the aa-tRNA from EEF1A1 and allowing its accommodation into the ribosome. The growing protein chain is subsequently transferred from the P-site peptidyl tRNA to the A-site aa-tRNA, extending it by one amino acid through ribosome-catalyzed peptide bond formation. Also plays a role in the positive regulation of IFNG transcription in T-helper 1 cells as part of an IFNG promoter-binding complex with TXK and PARP1. {ECO:0000250|UniProtKB:P68104}.
|
Equus caballus (Horse)
|
A2Q0Z1
|
HSP7C_HORSE
|
MSKGPAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRRFDDAVVQSDMKHWPFMVVNDAGRPKVQVEYKGETKSFYPEEVSSMVLTKMKEIAEAYLGKTVTNAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKVGAERNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVNHFIAEFKRKHKKDISENKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGIDFYTSITRARFEELNADLFRGTLDPVEKALRDAKLDKSQIHDIVLVGGSTRIPKIQKLLQDFFNGKELNKSINPDEAVAYGAAVQAAILSGDKSENVQDLLLLDVTPLSLGIETAGGVMTVLIKRNTTIPTKQTQTFTTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELTGIPPAPRGVPQIEVTFDIDANGILNVSAVDKSTGKENKITITNDKGRLSKEDIERMVQEAEKYKAEDEKQRDKVSSKNSLESYAFNMKATVEDEKLQGKINDEDKQKILDKCNEIINWLDKNQTAEKEEFEHQQKELEKVCNPIITKLYQSAGGMPGGMPGGFPGGGAPPSGGASSGPTIEEVD
|
3.6.4.10
| null |
chaperone cofactor-dependent protein refolding [GO:0051085]; chaperone-mediated autophagy translocation complex disassembly [GO:1904764]; clathrin coat disassembly [GO:0072318]; late endosomal microautophagy [GO:0061738]; mRNA processing [GO:0006397]; negative regulation of DNA-templated transcription [GO:0045892]; protein refolding [GO:0042026]; protein targeting to lysosome involved in chaperone-mediated autophagy [GO:0061740]; RNA splicing [GO:0008380]; slow axonal transport [GO:1990832]
|
autophagosome [GO:0005776]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; lysosomal membrane [GO:0005765]; melanosome [GO:0042470]; nucleolus [GO:0005730]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; postsynaptic cytosol [GO:0099524]; presynaptic cytosol [GO:0099523]; Prp19 complex [GO:0000974]; ribonucleoprotein complex [GO:1990904]; spliceosomal complex [GO:0005681]; terminal bouton [GO:0043195]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein folding chaperone [GO:0140662]; clathrin-uncoating ATPase activity [GO:1990833]; heat shock protein binding [GO:0031072]; protein folding chaperone [GO:0044183]; protein-macromolecule adaptor activity [GO:0030674]
|
PF00012;
|
1.20.1270.10;3.30.30.30;3.30.420.40;
|
Heat shock protein 70 family
|
PTM: Acetylated. {ECO:0000250|UniProtKB:P11142}.; PTM: ISGylated. {ECO:0000250|UniProtKB:P11142}.; PTM: Trimethylation at Lys-561 reduces fibrillar SNCA binding. {ECO:0000250|UniProtKB:P11142}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P11142}. Melanosome {ECO:0000250|UniProtKB:P11142}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P11142}. Cell membrane {ECO:0000250|UniProtKB:P11142}. Lysosome membrane {ECO:0000250|UniProtKB:P11142}; Peripheral membrane protein {ECO:0000250|UniProtKB:P11142}; Cytoplasmic side {ECO:0000250|UniProtKB:P11142}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Translocates rapidly from the cytoplasm to the nuclei, and especially to the nucleoli, upon heat shock. {ECO:0000250|UniProtKB:P11142}.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.10; Evidence={ECO:0000250|UniProtKB:P11142};
| null | null | null | null |
FUNCTION: Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, chaperone-mediated autophagy, activation of proteolysis of misfolded proteins, formation and dissociation of protein complexes, and antigen presentation. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The co-chaperones have been shown to not only regulate different steps of the ATPase cycle of HSP70, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation. The affinity of HSP70 for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. HSP70 goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The HSP70-associated co-chaperones are of three types: J-domain co-chaperones HSP40s (stimulate ATPase hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate conversion of HSP70 from the ADP-bound to the ATP-bound state thereby promoting substrate release), and the TPR domain chaperones such as HOPX and STUB1. Plays a critical role in mitochondrial import, delivers preproteins to the mitochondrial import receptor TOMM70. Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex. Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes. Substrate recognition component in chaperone-mediated autophagy (CMA), a selective protein degradation process that mediates degradation of proteins with a -KFERQ motif: HSPA8/HSC70 specifically recognizes and binds cytosolic proteins bearing a -KFERQ motif and promotes their recruitment to the surface of the lysosome where they bind to lysosomal protein LAMP2. KFERQ motif-containing proteins are eventually transported into the lysosomal lumen where they are degraded. In conjunction with LAMP2, facilitates MHC class II presentation of cytoplasmic antigens by guiding antigens to the lysosomal membrane for interaction with LAMP2 which then elicits MHC class II presentation of peptides to the cell membrane. Participates in the ER-associated degradation (ERAD) quality control pathway in conjunction with J domain-containing co-chaperones and the E3 ligase STUB1. It is recruited to clathrin-coated vesicles through its interaction with DNAJC6 leading to activation of HSPA8/HSC70 ATPase activity and therefore uncoating of clathrin-coated vesicles (By similarity). {ECO:0000250|UniProtKB:P11142, ECO:0000250|UniProtKB:P19120}.
|
Equus caballus (Horse)
|
A2Q5W1
|
ERN1_MEDTR
|
MEIQFQQPNMQNQKAGISVTNKGGKFKGRNRNSNNTNKFVGVRQRPSGRWVAEIKDTTQKIRMWLGTFETAEEAARAYDEAACLLRGSNTRTNFITHVSLDSPLASRIRNLLNNRKGDKKQEDGAVASAPSNSKTTISNTSTITSNDDNKESTLSTCATRNTELFEDAYKPDLSNCKEVFESGSQSNISCGFGPFFDHFSFTQLLDMAKNDDITDASSLELSEFERMKVERQISASLYAINGVHEYMETVQESNEALWDLPPLCSLFC
| null | null |
nodulation [GO:0009877]; positive regulation of DNA-templated transcription [GO:0045893]
|
nucleus [GO:0005634]
|
DNA-binding transcription factor activity [GO:0003700]; sequence-specific DNA binding [GO:0043565]
|
PF00847;
|
3.30.730.10;
|
AP2/ERF transcription factor family, ERF subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00366, ECO:0000269|PubMed:17827349, ECO:0000269|PubMed:23077241}.
| null | null | null | null | null |
FUNCTION: Transcription factor involved in symbiotic nodule signaling in response to rhizobial Nod factors (NFs) (PubMed:17449807, PubMed:17827349). Binds to the GCC-box (NF-responsive box) of ENOD11 promoter. Acts as a transcriptional activator of NF-responsive box-containing target gene promoters in root hairs (PubMed:17827349). Functions as a transcriptional regulator required for root infection by symbiotic rhizobia, infection thread (IT) formation and maintenance, and nodule development. Necessary for NF-induced gene expression and spontaneous nodulation activated by CCAMK. Functions downstream of CCAMK to activate nodulation gene expression (PubMed:17449807). Involved in early stages of root nodule development. Functions redundantly with ERN2. Is essential with ERN2 for the initiation of root hair infection, and nodule organogenesis and development. Required for accurate expression of the NF signaling genes ENOD11 and ENOD12 (PubMed:23077241, PubMed:27208242). {ECO:0000269|PubMed:17449807, ECO:0000269|PubMed:17827349, ECO:0000269|PubMed:23077241, ECO:0000269|PubMed:27208242}.
|
Medicago truncatula (Barrel medic) (Medicago tribuloides)
|
A2QAC0
|
LAD_ASPNC
|
MATATVLEKANIGVFTNTKHDLWVADAKPTLEEVKNGQGLQPGEVTIEVRSTGICGSDVHFWHAGCIGPMIVTGDHILGHESAGQVVAVAPDVTSLKPGDRVAVEPNIICNACEPCLTGRYNGCENVQFLSTPPVDGLLRRYVNHPAIWCHKIGDMSYEDGALLEPLSVSLAGIERSGLRLGDPCLVTGAGPIGLITLLSARAAGASPIVITDIDEGRLEFAKSLVPDVRTYKVQIGLSAEQNAEGIINVFNDGQGSGPGALRPRIAMECTGVESSVASAIWSVKFGGKVFVIGVGKNEMTVPFMRLSTWEIDLQYQYRYCNTWPRAIRLVRNGVIDLKKLVTHRFLLEDAIKAFETAANPKTGAIKVQIMSSEDDVKAASAGQKI
|
1.1.1.12
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:20414651}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:20414651};
|
L-arabinose catabolic process to xylulose 5-phosphate [GO:0019569]; sorbitol catabolic process [GO:0006062]
| null |
L-arabinitol 4-dehydrogenase activity [GO:0050019]; L-iditol 2-dehydrogenase activity [GO:0003939]; zinc ion binding [GO:0008270]
|
PF08240;PF00107;
|
3.90.180.10;3.40.50.720;
|
Zinc-containing alcohol dehydrogenase family
| null | null |
CATALYTIC ACTIVITY: Reaction=L-arabinitol + NAD(+) = H(+) + L-xylulose + NADH; Xref=Rhea:RHEA:16381, ChEBI:CHEBI:15378, ChEBI:CHEBI:17399, ChEBI:CHEBI:18403, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.12; Evidence={ECO:0000269|PubMed:16321042};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=89 mM for L-arabinitol (at pH 9.6) {ECO:0000269|PubMed:16321042, ECO:0000269|PubMed:19674460, ECO:0000269|PubMed:20414651}; KM=5 mM for L-xylulose (at pH 9.6) {ECO:0000269|PubMed:16321042, ECO:0000269|PubMed:19674460, ECO:0000269|PubMed:20414651}; KM=50 uM for NAD (at pH 9.6) {ECO:0000269|PubMed:16321042, ECO:0000269|PubMed:19674460, ECO:0000269|PubMed:20414651}; KM=8 uM for NADH (at pH 9.6) {ECO:0000269|PubMed:16321042, ECO:0000269|PubMed:19674460, ECO:0000269|PubMed:20414651}; Vmax=96 umol/min/mg enzyme for the forward reaction {ECO:0000269|PubMed:16321042, ECO:0000269|PubMed:19674460, ECO:0000269|PubMed:20414651}; Vmax=805 umol/min/mg enzyme for the reverse reaction {ECO:0000269|PubMed:16321042, ECO:0000269|PubMed:19674460, ECO:0000269|PubMed:20414651};
|
PATHWAY: Carbohydrate degradation; L-arabinose degradation via L-arabinitol; D-xylulose 5-phosphate from L-arabinose (fungal route): step 2/5. {ECO:0000269|PubMed:16321042}.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.4. Active from pH 7 to pH 11. {ECO:0000269|PubMed:16321042, ECO:0000269|PubMed:19674460, ECO:0000269|PubMed:20414651};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40-50 degrees Celsius. {ECO:0000269|PubMed:16321042, ECO:0000269|PubMed:19674460, ECO:0000269|PubMed:20414651};
|
FUNCTION: Catalyzes the NAD-dependent oxidation of L-arabinitol to L-xylulose in the fungal L-arabinose catabolic pathway. L-arabinose catabolism is important for using plant material as a carbon source. Not active with NADP as cosubstrate. {ECO:0000269|PubMed:19674460, ECO:0000269|PubMed:20414651}.
|
Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
|
A2QAN3
|
BGALA_ASPNC
|
MKLSSACAIALLAAQAAGASIKHRINGFTLTEHSDPAKRELLQKYVTWDDKSLFINGERIMIFSGEFHPFRLPVKELQLDIFQKVKALGFNCVSFYVDWALVEGKPGEYRADGIFDLEPFFDAASEAGIYLLARPGPYINAESSGGGFPGWLQRVNGTLRSSDKAYLDATDNYVSHVAATIAKYQITNGGPIILYQPENEYTSGCCGVEFPDPVYMQYVEDQARNAGVVIPLINNDASASGNNAPGTGKGAVDIYGHDSYPLGFDCANPTVWPSGDLPTNFRTLHLEQSPTTPYAIVEFQGGSYDPWGGPGFAACSELLNNEFERVFYKNDFSFQIAIMNLYMIFGGTNWGNLGYPNGYTSYDYGSAVTESRNITREKYSELKLLGNFAKVSPGYLTASPGNLTTSGYADTTDLTVTPLLGNSTGSFFVVRHSDYSSEESTSYKLRLPTSAGSVTIPQLGGTLTLNGRDSKIHVTDYNVSGTNIIYSTAEVFTWKKFADGKVLVLYGGAGEHHELAISTKSNVTVIEGSESGISSKQTSSSVVVGWDVSTTRRIIQVGDLKILLLDRNSAYNYWVPQLATDGTSPGFSTPEKVASSIIVKAGYLVRTAYLKGSGLYLTADFNATTSVEVIGVPSTAKNLFINGDKTSHTVDKNGIWSATVDYNAPDISLPSLKDLDWKYVDTLPEIQSSYDDSLWPAADLKQTKNTLRSLTTPTSLYSSDYGFHTGYLLYRGHFTATGNESTFAIDTQGGSAFGSSVWLNGTYLGSWTGLYANSDYNATYNLPQLQAGKTYVITVVIDNMGLEENWTVGEDLMKTPRGILNFLLAGRPSSAISWKLTGNLGGEDYEDKVRGPLNEGGLYAERQGFHQPEPPSQNWKSSSPLEGLSEAGIGFYSASFDLDLPKGWDVPLFLNIGNSTTPSPYRVQVYVNGYQYAKYISNIGPQTSFPVPEGILNYRGTNWLAVTLWALDSAGGKLESLELSYTTPVLTALGEVESVDQPKYKKRKGAY
|
3.2.1.23
| null |
carbohydrate metabolic process [GO:0005975]; lactose catabolic process [GO:0005990]; polysaccharide catabolic process [GO:0000272]
|
extracellular region [GO:0005576]; vacuole [GO:0005773]
|
beta-galactosidase activity [GO:0004565]; oligosaccharide binding [GO:0070492]
|
PF13364;PF10435;PF13363;PF01301;
|
2.102.20.10;2.60.390.10;2.60.120.260;3.20.20.80;
|
Glycosyl hydrolase 35 family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.; EC=3.2.1.23; Evidence={ECO:0000269|PubMed:28391618};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=92.5 mM for lactose {ECO:0000269|PubMed:28391618}; Note=kcat is 214.9 sec(-1). {ECO:0000269|PubMed:28391618};
| null | null | null |
FUNCTION: Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans. {ECO:0000269|PubMed:28391618}.
|
Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
|
A2QHE5
|
FDC1_ASPNC
|
MSAQPAHLCFRSFVEALKVDNDLVEINTPIDPNLEAAAITRRVCETNDKAPLFNNLIGMKNGLFRILGAPGSLRKSSADRYGRLARHLALPPTASMREILDKMLSASDMPPIPPTIVPTGPCKENSLDDSEFDLTELPVPLIHKSDGGKYIQTYGMHIVQSPDGTWTNWSIARAMVHDKNHLTGLVIPPQHIWQIHQMWKKEGRSDVPWALAFGVPPAAIMASSMPIPDGVTEAGYVGAMTGSSLELVKCDTNDLYVPATSEIVLEGTLSISETGPEGPFGEMHGYIFPGDTHLGAKYKVNRITYRNNAIMPMSSCGRLTDETHTMIGSLAAAEIRKLCQQNDLPITDAFAPFESQVTWVALRVDTEKLRAMKTTSEGFRKRVGDVVFNHKAGYTIHRLVLVGDDIDVYEGKDVLWAFSTRCRPGMDETLFEDVRGFPLIPYMGHGNGPAHRGGKVVSDALMPTEYTTGRNWEAADFNQSYPEDLKQKVLDNWTKMGFSN
|
4.1.1.102
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP-Rule:MF_03196, ECO:0000269|PubMed:26083754}; COFACTOR: Name=prenyl-FMN; Xref=ChEBI:CHEBI:87746; Evidence={ECO:0000255|HAMAP-Rule:MF_03196, ECO:0000269|PubMed:26083743, ECO:0000269|PubMed:26083754}; Note=Binds 1 prenylated FMN (prenyl-FMN) per subunit. {ECO:0000255|HAMAP-Rule:MF_03196, ECO:0000269|PubMed:26083754};
|
aromatic amino acid family catabolic process [GO:0009074]; cinnamic acid catabolic process [GO:0046281]; ferulate metabolic process [GO:0033494]; styrene metabolic process [GO:0018966]; ubiquinone biosynthetic process [GO:0006744]
|
cytosol [GO:0005829]
|
3-octaprenyl-4-hydroxybenzoate carboxy-lyase activity [GO:0008694]; identical protein binding [GO:0042802]; manganese ion binding [GO:0030145]
|
PF01977;PF20696;PF20695;
|
1.20.5.4570;3.40.1670.10;
|
UbiD family, UbiD-like/FDC subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03196}.
|
CATALYTIC ACTIVITY: Reaction=(E)-4-coumarate + H(+) = 4-hydroxystyrene + CO2; Xref=Rhea:RHEA:33227, ChEBI:CHEBI:1883, ChEBI:CHEBI:12876, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526; EC=4.1.1.102; Evidence={ECO:0000255|HAMAP-Rule:MF_03196}; CATALYTIC ACTIVITY: Reaction=(E)-cinnamate + H(+) = CO2 + styrene; Xref=Rhea:RHEA:46920, ChEBI:CHEBI:15378, ChEBI:CHEBI:15669, ChEBI:CHEBI:16526, ChEBI:CHEBI:27452; EC=4.1.1.102; Evidence={ECO:0000255|HAMAP-Rule:MF_03196, ECO:0000269|PubMed:26083743}; CATALYTIC ACTIVITY: Reaction=(E)-ferulate + H(+) = 2-methoxy-4-vinylphenol + CO2; Xref=Rhea:RHEA:33807, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:29749, ChEBI:CHEBI:42438; EC=4.1.1.102; Evidence={ECO:0000255|HAMAP-Rule:MF_03196};
| null | null | null | null |
FUNCTION: Catalyzes the reversible decarboxylation of aromatic carboxylic acids like ferulic acid, p-coumaric acid or cinnamic acid, producing the corresponding vinyl derivatives 4-vinylphenol, 4-vinylguaiacol, and styrene, respectively, which play the role of aroma metabolites. {ECO:0000255|HAMAP-Rule:MF_03196, ECO:0000269|PubMed:26083754}.
|
Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
|
A2QIL5
|
ATG1_ASPNC
|
MGLFHHSTLFLPLLRRSNEGPHGEMPIGHYTRLSEIGRGSFAVVYKGVHTRSRTYVAIKSVTMTKLSRKLKENLASEISILKQLHHPHIVALLDCHDTTSNIHLVMEFCALGDLSHFIKGRNTLQDSPYTRELIAKYPNPGEGAGLNEVIVRHFLKQLSSALRFLRDRDLIHRDIKPQNLLLCPAPSSYRSGAADVVPFKSSEDSFSPKTGLESLPMLKLADFGFARSLPATSLAETLCGSPLYMAPEILRYEKYDAKADLWSVGTVLYEMVVGRAPFRAVNHIELIKKIEQNKDQISFPSKNRVSEDIRELIRGLLKQHPMDRMNFDVYFAHKVLTEPIPGLVADDAPLGRSPADPTPRPGSGSRRSTPVQMKRENALSGGVRDEPATYPAAQRAMTQSPRPETPSTPMRRTGSAGTPHAAPNEPTPPASHPTRPSPVSLATAPGRQEHVDRPPTTTVVEQQRRRTASSGVPQVDKPVEKAKDEKEHAAQEVAFERDYVLVEKRAVEMNAFADELAYNPRMQGGQAGAVSRRSGAAPGTPPAGGSSPHASPSKAMQIISGRSRADSAHVRQNSYDRRYGQSPTSATSAISKALNMASGRLFGMSFSPPLTITKGGRSPPLAYNPFPAYPSAQTSLIVHADGGKPGANLDEDSKTVHDLEECATRSDVVYGFAEVKYKQLIPLAPSAATGYPGDPGSDAVDSADGGLTVDAIVTLSEEALVLYVKALSLLAKSMDIARVWWTRKSRGDTLSRADTGSTVAGNRINNVVQWVRNRFNEVLEKAEFVRLKLVEAQKRLPSDHPSHPSNLSVGSSLGSGTSADVVVSPDVTAEKLMYERALEMSRVAAINEITGEDLAGCEISYVTAIRMLEAILDDVEVSRPGQSGGADRADARRDNEDGGQNEPQAVILAKSANAWHSDIENPESPGVAPEEAGAAVESVHAPVQWTGQNAAVESGASLPCSGSHAAEIRTLTVRSMQDHAHFAPLLFSIFISSYSSSISCPSSCGHC
|
2.7.11.1
| null |
autophagosome assembly [GO:0000045]; autophagy [GO:0006914]; axon extension [GO:0048675]; cellular response to oxidative stress [GO:0034599]; negative regulation of collateral sprouting [GO:0048671]; phosphorylation [GO:0016310]; piecemeal microautophagy of the nucleus [GO:0034727]; positive regulation of autophagy [GO:0010508]; protein transport [GO:0015031]; response to starvation [GO:0042594]; reticulophagy [GO:0061709]
|
autophagosome [GO:0005776]; cytosol [GO:0005829]; phagophore assembly site membrane [GO:0034045]
|
ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF12063;PF21127;PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family, APG1/unc-51/ULK1 subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P53104}. Preautophagosomal structure membrane {ECO:0000250|UniProtKB:P53104}; Peripheral membrane protein {ECO:0000250|UniProtKB:P53104}.
|
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:P53104}; 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:P53104};
| null | null | null | null |
FUNCTION: Serine/threonine protein kinase involved in the cytoplasm to vacuole transport (Cvt) and found to be essential in autophagy, where it is required for the formation of autophagosomes. Involved in the clearance of protein aggregates which cannot be efficiently cleared by the proteasome. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Also involved in endoplasmic reticulum-specific autophagic process, in selective removal of ER-associated degradation (ERAD) substrates. Plays a key role in ATG9 and ATG23 cycling through the pre-autophagosomal structure and is necessary to promote ATG18 binding to ATG9 through phosphorylation of ATG9. Catalyzes phosphorylation of ATG4, decreasing the interaction between ATG4 and ATG8 and impairing deconjugation of PE-conjugated forms of ATG8. {ECO:0000250|UniProtKB:P53104}.
|
Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
|
A2QQ28
|
RSP5_ASPNC
|
MGSNLPAQPNLRVTIIAADGLYKRDVFRFPDPFAVATVGGEQTHTTSVIKKTLNPYWNEMFDLRVNEDSILAIQIFDQKKFKKKDQGFLGVINVRIGDVIDLQMGGDEMLTRDLKKSNDNLVVHGKLIINLSTNLSTPIPNQANGLHRSHAQSSTSSGLVPQVSSASHPSVSPGQAEPSAAASNVSLHPQRVPSTTRPTSTVGPVNGGPAPPPNGPQGSRTNLSSFEDSQGRLPAGWERREDNLGRTYYVDHNTRTTTWTRPSSNYNEQTQRTQREANMQLERRAHQSRMLPEDRTGANSPNLQESPQPQPQQAHTPPAGGSASAVSMMATGATTAGTGELPPGWEQRTTPEGRPYFVDHNTRTTTWVDPRRQQYIRMYGHNANGGNTTIQQQPVSQLGPLPSGWEMRLTNTARVYFVDHNTKTTTWDDPRLPSSLDQGVPQYKRDFRRKLIYFRSQPALRIMSGQCHVKVRRNNIFEDSYAEIMRQSASDLKKRLMIKFDGEDGLDYGGLSREFFFLLSHEMFNPFYCLFEYSAHDNYTLQINPHSGVNPEHLNYFKFIGRVVGLAIFHRRFLDSFFIGAFYKMMLRKKVSLQDMEGVDEDLHRNLAWTLENDIEGIIELTFSVDDEKFGERTTIDLKPGGRDIPVTNENKGEYVELVTEWKIVKRVEEQFNAFMSGFNELIPADLVNVFDERELELLIGGIADIDVDDWKKHTDYRGYQEQDEVIQNFWKIVRTWDAEQKSRLLQFTTGTSRIPVNGFKDLQGSDGPRRFTIEKSGDPIALPKSHTCFNRLDLPPYKTHDVLEHKLSIAVEETLGFGQE
|
2.3.2.26
| null |
chromatin organization [GO:0006325]; mitochondria-associated ubiquitin-dependent protein catabolic process [GO:0072671]; mitochondrion organization [GO:0007005]; nonfunctional rRNA decay [GO:0070651]; poly(A)+ mRNA export from nucleus [GO:0016973]; positive regulation of fatty acid biosynthetic process [GO:0045723]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; positive regulation of receptor-mediated endocytosis [GO:0048260]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein K63-linked ubiquitination [GO:0070534]; protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway [GO:0043328]; protein ubiquitination [GO:0016567]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of dolichol biosynthetic process [GO:0010794]; regulation of ergosterol biosynthetic process [GO:0032443]; regulation of mRNA export from nucleus [GO:0010793]; regulation of multivesicular body size [GO:0010796]; regulation of nitrogen utilization [GO:0006808]; regulation of phosphate metabolic process [GO:0019220]; regulation of protein localization [GO:0032880]; regulation of ribosomal large subunit export from nucleus [GO:2000203]; regulation of rRNA processing [GO:2000232]; regulation of tRNA export from nucleus [GO:2000238]; regulation of tRNA processing [GO:2000235]; regulation of ubiquinone biosynthetic process [GO:0010795]; ribophagy [GO:0034517]; ubiquitin-dependent endocytosis [GO:0070086]
|
cellular bud tip [GO:0005934]; cytosolic ribosome [GO:0022626]; endosome membrane [GO:0010008]; Golgi apparatus [GO:0005794]; nucleus [GO:0005634]; RSP5-BUL ubiquitin ligase complex [GO:1990306]; ubiquitin ligase complex [GO:0000151]
|
phosphatidylinositol binding [GO:0035091]; ubiquitin binding [GO:0043130]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]
|
PF00168;PF00632;PF00397;
|
2.20.70.10;2.60.40.150;3.30.2160.10;3.30.2410.10;3.90.1750.10;
|
RSP5/NEDD4 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P39940}.
|
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.26;
| null |
PATHWAY: Protein modification; protein ubiquitination.
| null | null |
FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Probably involved in the regulatory network controlling carbon source utilization. {ECO:0000250|UniProtKB:Q5BDP1}.
|
Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
|
A2QTW5
|
BPHA_ASPNC
|
MLALLLSPYGAYLGLALLVLYYLLPYLKRAHLRDIPAPGLAAFTNFWLLLQTRRGHRFVVVDNAHKKYGKLVRIAPRHTSIADDGAIQAVYGHGNGFLKSDFYDAFVSIHRGLFNTRDRAEHTRKRKTVSHTFSMKSIGQFEQYIHGNIELFVKQWNRMADTQRNPKTGFASLDALNWFNYLAFDIIGDLAFGAPFGMLDKGKDFAEMRKTPDSPPSYVQAVEVLNRRGEVSATLGCYPALKPFAKYLPDSFFRDGIQAVEDLAGIAVARVNERLRPEVMANNTRVDLLARLMEGKDSNGEKLGRAELTAEALTQLIAGSDTTSNTSCAILYWCMRTPGVIEKLHKVLDEAIPQDVDVPTHAMVKDIPYLQWVIWETMRIHSTSAMGLPREIPAGNPPVTISGHTFYPGDVVSVPSYTIHRSKEIWGPDAEQFVPERWDPARLTPRQKAAFIPFSTGPRACVGRNVAEMELLVICGTVFRLFEFEMQQEGPMETREGFLRKPLGLQVGMKRRQPGSA
|
1.14.14.92
|
COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P04798};
|
benzoate catabolic process [GO:0043639]
|
intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]
|
benzoate 4-monooxygenase activity [GO:0018664]; heme binding [GO:0020037]; iron ion binding [GO:0005506]
|
PF00067;
|
1.10.630.10;
|
Cytochrome P450 family
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=benzoate + O2 + reduced [NADPH--hemoprotein reductase] = 4-hydroxybenzoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:18033, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16150, ChEBI:CHEBI:17879, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210; EC=1.14.14.92; Evidence={ECO:0000269|PubMed:11594739};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.083 mM for benzoate {ECO:0000269|PubMed:11594739}; KM=0.097 mM for 2-fluorobenzoate {ECO:0000269|PubMed:11594739}; KM=0.31 mM for 2-chlorobenzoate {ECO:0000269|PubMed:11594739}; KM=0.28 mM for 2-hydroxybenzoate {ECO:0000269|PubMed:11594739}; KM=1.6 mM for 2-methylbenzoate {ECO:0000269|PubMed:11594739}; KM=0.086 mM for 3-fluorobenzoate {ECO:0000269|PubMed:11594739}; KM=0.127 mM for 3-chlorobenzoate {ECO:0000269|PubMed:11594739}; KM=0.673 mM for 3-hydroxybenzoate {ECO:0000269|PubMed:11594739}; KM=0.189 mM for 3-methylbenzoate {ECO:0000269|PubMed:11594739}; Note=kcat is 270 min(-1) for benzoate. {ECO:0000269|PubMed:11594739};
| null | null | null |
FUNCTION: Cytochrome P450 monooxygenase; part of the benzoic acid degradation pathway also known as the protocatechuic acid pathway (PubMed:11594739, Ref.5). Benzoic acid debradation begins with the conversion of benzoic acid into 4-hydroxybenzoic acid through hydroxylation by the benzoate-4-monooxygenase bphA, and its partner NADPH-cytochrome P450 reductase cprA which act as a mediator in electron donation from NADPH (PubMed:11594739). 4-Hydroxybenzoic acid is then converted into 3,4-dihydroxybenzoic acid (also called protocatechuic acid) by the p-hydroxybenzoate-m-hydroxylase phhA (Ref.5). Protocatechuic acid is converted into 3-carboxy-cis,cis-muconic acid by the intradiol ring-cleavage dioxygenase prcA, which is further metabolized through the 3-oxoadipate pathway to finally enter the tricarboxylic acid cycle (TCA) (Ref.5). {ECO:0000269|PubMed:11594739, ECO:0000269|Ref.5}.
|
Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
|
A2R2V4
|
OTASE_ASPNC
|
MVRRIASATPMVQSPMSPLGTTYCVRPNPVSLNLQRRPLVIASTDEAKVTIIYAGLLIPGDGEPLRNAALVISDKIIAFVGSEADIPKKYLRSTQSTHRVPVLMPGLWDCHMHFGGDDDYYNDYTSGLATHPASSGARLARGCWEALQNGYTSYRDLAGYGCEVAKAINDGTIVGPNVYSSGAALSQTAGHGDIFALPAGEVLGSYGVMNPRPGYWGAGPLCIADGVEEVRRAVRLQIRRGAKVIKVMASGGVMSRDDNPNFAQFSPEELKVIVEEAARQNRIVSAHVHGKAGIMAAIKAGCKSLEHVSYADEEVWELMKEKGILYVATRSVIEIFLASNGEGLVKESWAKLQALADSHLKAYQGAIKAGVTIALGTDTAPGGPTALELQFAVERGGMTPLEAIKAATANAPLSVGPQAPLTGQLREGYEADVIALEENPLEDIKVFQEPKAVTHVWKGGKLFKGPGIGPWGEDARNPFL
|
3.4.17.-
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:24947135};
|
ochratoxin A catabolic process [GO:1900817]; proteolysis [GO:0006508]
|
extracellular region [GO:0005576]
|
carboxypeptidase activity [GO:0004180]; hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds [GO:0016810]; metal ion binding [GO:0046872]; metallopeptidase activity [GO:0008237]
|
PF01979;
|
3.20.20.140;
|
Metallo-dependent hydrolases superfamily, Ochratoxinase amidase 2 family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24947135}.
|
CATALYTIC ACTIVITY: Reaction=H2O + ochratoxin A = L-phenylalanine + ochratoxin alpha; Xref=Rhea:RHEA:72751, ChEBI:CHEBI:15377, ChEBI:CHEBI:58095, ChEBI:CHEBI:166829, ChEBI:CHEBI:192527; Evidence={ECO:0000269|PubMed:24947135}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72752; Evidence={ECO:0000269|PubMed:24947135};
| null | null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6. {ECO:0000269|PubMed:24947135};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 66 degrees Celsius. {ECO:0000269|PubMed:24947135};
|
FUNCTION: Carboxypeptidase that catalyzes the release of a C-terminal amino acid with specific catalytic activity for aromatic amino acids such as phenylalanine (PubMed:24947135, PubMed:33647354). Is able to degrade ochratoxin A, one of the five major mycotoxins most harmful to humans and animals that is produced by Aspergillus and Penicillium species and occurs in a wide range of agricultural products (PubMed:24947135). {ECO:0000269|PubMed:24947135, ECO:0000269|PubMed:33647354}.
|
Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
|
A2R3H4
|
UBA4_ASPNC
|
MNGVEQTCASLRTQIAATEAKLADLKRELEIAEQAAASHKQNAADAEGGSERRWPLLDEEYRRYGRQMIVPQLGIQGQLKLRSAKVLIVGAGGLGCPAALYLAGAGVGTLGLVDGDAVESSNLHRQVLHRTRNIGKLKVDSAIEYLKELNPHSKYIAHREHLAPEAAPEIFSNYDLILDCTDNPATRYLISDTAVLLGKPLVSASALRTEGQLMVLNNPPRPAGDKTGGPCYRCVFPKPPPANTVTSCADGGIVGPVVGTMGVLQALEAIKVITADETTTPPPPSLHIFSAYSTPLFRTIKLRSRRPNCAVCSAEASVTVDTVRSGSTDYIFFCGTTGPENLLSPEERITPLEYRTRHHDKEEKEPTIIDVREKVQYDICSLENSINIPISTILASASSSMSNGDSLADGVPALPSWVPPDVASSQSTDPVYVVCRLGNDSQVAVKKLKELGLDQGGKRVVADIRGGFRAWKEQVDPEWPEY
|
2.7.7.80; 2.8.1.11
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_03049}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03049};
|
cell budding [GO:0007114]; cellular response to oxidative stress [GO:0034599]; invasive growth in response to glucose limitation [GO:0001403]; Mo-molybdopterin cofactor biosynthetic process [GO:0006777]; protein urmylation [GO:0032447]; regulation of pseudohyphal growth [GO:2000220]; tRNA wobble position uridine thiolation [GO:0002143]
|
cytosol [GO:0005829]
|
AMPylase activity [GO:0070733]; ATP binding [GO:0005524]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; molybdopterin-synthase adenylyltransferase activity [GO:0061605]; molybdopterin-synthase sulfurtransferase activity [GO:0061604]; sulfotransferase activity [GO:0008146]; thiosulfate sulfurtransferase activity [GO:0004792]; URM1 activating enzyme activity [GO:0042292]
|
PF00581;PF00899;
|
3.40.50.720;3.40.250.10;
|
HesA/MoeB/ThiF family, UBA4 subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03049}.
|
CATALYTIC ACTIVITY: Reaction=[molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly + ATP + H(+) = [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly-AMP + diphosphate; Xref=Rhea:RHEA:43616, Rhea:RHEA-COMP:12159, Rhea:RHEA-COMP:12202, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:90618, ChEBI:CHEBI:90778; EC=2.7.7.80; Evidence={ECO:0000255|HAMAP-Rule:MF_03049}; CATALYTIC ACTIVITY: Reaction=[molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly-AMP + AH2 + S-sulfanyl-L-cysteinyl-[cysteine desulfurase] = [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-NH-CH2-C(O)SH + A + AMP + H(+) + L-cysteinyl-[cysteine desulfurase]; Xref=Rhea:RHEA:48612, Rhea:RHEA-COMP:12157, Rhea:RHEA-COMP:12158, Rhea:RHEA-COMP:12159, Rhea:RHEA-COMP:12160, ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:17499, ChEBI:CHEBI:29950, ChEBI:CHEBI:61963, ChEBI:CHEBI:90618, ChEBI:CHEBI:90619, ChEBI:CHEBI:456215; EC=2.8.1.11; Evidence={ECO:0000255|HAMAP-Rule:MF_03049};
| null |
PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03049}.; PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03049}.
| null | null |
FUNCTION: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers urm1 and mocs2a. Its N-terminus first activates urm1 and mocs2a as acyl-adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to urm1 and mocs2a to form thiocarboxylation (-COSH) of their C-terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as a nucleophile towards urm1 and mocs2a. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor; nfs1 probably acting as a sulfur donor for thiocarboxylation reactions (By similarity). {ECO:0000250}.
|
Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
|
A2R6H1
|
OTAA_ASPNC
|
MSSAPIPQSEPLAIIGLACKYANGIDSPEALYEQVMAARCMHGAMPSNRMDASFYYHPTSEATGTSYSKGGYFLNCDLNAFDSPFFQLSEIDVMAMDPQQKMLLENVYHALENAGIPLKNAISSPTSVFVGCSNNDHLALANSDLLLSLKGKGTGTSPSILANRVSWFYDFQGTSQTIDTACSSSLVAFHQGCMDVRAGKSAMSIISGINLIEHPGPTLYLSSLGVLSPDGKSMSFDARANGYGRGEGVGTVIVKPLQAALRDGNRIRAIVRSTGSNQDGRTPGITVPNPSAQERLIHDVYRVADLDPRRTGYVEAHGTGTQVGDPLEVQAILAALGVARDSPLYVGSVKSVLGHLEGGAGLAGLISATLAVESKMIPPVAGLQSLNPKIPQRDDLKFAREATPWPRWDVRRASINSFGFGGTNAHAVVEDVEGFFADLFGQYIPGALPAPEVDTSLETTPMLSKPLMSGNASNQSVQSWSTSRLFVISAFDEAGIQRNTSALAEYLDSKSTTADTDGEDRLLNNLCHTLNEKRTRFDWRSYHVADSIASLRESLQHSRAIRQSSAPKPIRFVFTGQGANWAGMACDMLKYPLFRRRIQEAAAYLRELGSGWDLFERMTSKAGELDEPTFAQSSCVAVQVALVDLLASWKVVPETVVGHSSGEIAAAYCAGHISRQAAWKVAFCRGKVCARRTDGQGRMLAAAMPVHQLERVVARVNKGQPTSVKIGCYNSPRNLTLTGRYDDILRLKLELDDVGALNRMLPVKVAYHSDYMQDAAPEYLSLLGEILDGGDTIHKDASIQMISSVTGQPVPAGDVQQASYWVKNLVSPVRFCTALLASMEFPGTTGKREDTLIEIGPHSTLRSAIKESFAEVPEYQSVQYGSLLKRYETNGSTILHTLGMMFCSGHEISLAAINDRRVGTRKIPMLLTGLPGYAFDHSRSVRGTSRRIEQVKFPTYNRHELLGVPVEDSNPYEQRWRNVLRPDDLPWLRMNRMKGQIHFPGVAYILMATEALQQRVARTMTIPRVRIANMSILAPLQVPDSPSGVEIQVSIYPTNVRANGATDWATFRIISYDTAEKTWVEHCVGSVRAETGPPDLCVNTALRKQCAEPVDIAQMYHGFTAAGMDFGENLRNIQAMKVSPDRTACTATITAPSIAPQAHDQYPLHPCSFESILHALLYLCEASQSPMVTNYIEEVVIVNPNDTGAREFESFARRQRTSATTWTCDVSITTNVGDQDIQIKGLDLVQLPANNDDAVDAESFYTVNWRPDVKLLASADALHNSAPVDAAQHLPTFDEHEGYQLASAIFLQEAKEYVTRTGLPPLPTHHQAFMDWMEEEYQSINNGTTPLLDKSLLDGIRADPDRRKSLLDRVARQSARGELLVRVGTRMIDILEQKIDCLEVMFGPDNLMERTYEEGLPGQIAPAVAGYLHCLAHAQTGIKILEVGAGTGSATKVMLDSLRPTEAQDGGGLVSSVSSYDFTDISAAFFEKARARFHDWADILRPKLLNIEQDPAAQGFELGSYDLVIATHVLHATADLNVSLKNIRALLKEGGDLIVIENIQPKFMCSQLPFGLLPGWWRSVEPYRKTNPLILKEHWTEELQNAGLRPRLIINDTDDGINEMSAFVASPMPKVLDGSQPCSIIYSSTYPGQQQLALEVADRLPRSCTAAVVDLADISLDHSDTVGIVLVGCQGLDLSELTSSEYDRVKFILTSFQKLLWVTCDPTDVPKSALATGLVRSTRWEREHDNVNIILLSVSLSRPTPLTISSEIVRLCENAFISCKRVPPNSEYRIEGSNGVLLTNRLFPAAGINECIGLGSRPRSRQVPLGTVDHPIKLTSIGSQQPNGFHFIEDPQAHEPLDPDEVKIRIHAAGLDEEDADQLSRLIPGHGFGDQGSGTVVEIGHGVQGIQVGDQVMALRTGPSCALQTFFRTHSATVAKIPDGIRLSDAAALPLPWVTAYHSLVTVARLDSQEKVLIHPAIGATGQAAVQVASMLGATVYATVETDAQRQTLAEYGVEESHILDSASVEKQFGTQTSTQGVDVLLNLRRDGLEFLHLSCLSPFGRLVDISGSRAFPSQVNSPSNQSYYRVNMRELSQLKPESIRQTLRTVAQLLASPTIRPVAPFRVGYSQLQRVLSEIRRGSRGPWVIQPLPNDPIPPLGSHQFDPSASYLLIGGFGGLGRSVARWMHHRGAKHFIFFSRSGASSAAARELCADLRAAGCAVSDMICDTTDAQAVAKAMAQCEASMPPIRGCLQASMVLEDSMLSNMDHTRFLGAITPKVQGTINVASALAPIKSNLDFFVMLSSSAGIVGNRGQANYAAANTFLDAFAGQLVTQGYPATSVSLGSVLSVGWVAENQHKLRIAFAFGALSEDLLLSILEYHMDPAWGAAQSIQTCHTVVGVRSARDFQRQSIPLPGFMAHPLFSPLLAIAGRSQTAEQAAEAPVSQGLREASSMEAAVEVVTRAIVHKLARIMALSVQEIDPQRSLGSYGVDSLVTVDLKAWFQREVGVSIGSGELLGEMAMTQLAQQAADASQFLPAELRGKLRKNTDIHV
|
2.3.1.-
|
COFACTOR: Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942; Evidence={ECO:0000255}; Note=Binds 1 phosphopantetheine covalently. {ECO:0000255};
|
fatty acid biosynthetic process [GO:0006633]; methylation [GO:0032259]; ochratoxin A biosynthetic process [GO:1900818]; secondary metabolic process [GO:0019748]
| null |
3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; catalytic activity [GO:0003824]; fatty acid synthase activity [GO:0004312]; methyltransferase activity [GO:0008168]; oxidoreductase activity [GO:0016491]; phosphopantetheine binding [GO:0031177]
|
PF00698;PF08240;PF16197;PF00109;PF02801;PF08659;PF08242;PF21089;PF00550;PF14765;
|
3.40.47.10;1.10.1200.10;3.40.366.10;3.90.180.10;3.40.50.720;3.10.129.110;3.40.50.150;
| null | null | null |
CATALYTIC ACTIVITY: Reaction=acetyl-CoA + 9 H(+) + 4 malonyl-CoA + 5 NADPH = 7-methylmellein + 3 CO2 + 5 CoA + 4 H2O + 5 NADP(+); Xref=Rhea:RHEA:72767, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:192524; Evidence={ECO:0000269|PubMed:27959549}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72768; Evidence={ECO:0000269|PubMed:27959549};
| null |
PATHWAY: Mycotoxin biosynthesis. {ECO:0000269|PubMed:27959549}.
| null | null |
FUNCTION: Highly reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of ochratoxin A (OTA), a mycotoxin composed of a chlorinated type I polyketide dihydroisocoumarin moiety linked to L-phenylalanine, and demonstrated to have nephrotoxic, immunotoxic, genotoxic, neurotoxic, and teratogenic properties (PubMed:27667988, PubMed:27959549). OtaA catalyzes the condensation of one acetate and 4 malonate units to form the isocoumarin group (PubMed:27959549). The pathway begins with the highly reducing polyketide synthase otaA that catalyzes the formation of the isocoumarin group during the initial stages of biosynthesis, starting from one acetate and 4 malonate units, to originate the characteristic pentaketide skeleton 7-methylmellein (7-MM) of the OTA molecule. The newly identified cyclase otaY might be involved in the polyketide cyclization reaction during the initial steps of the OTA biosynthesis. 7-MM is then oxidized into 7-carboxymellein (also called ochratoxin beta) by the cytochrome P450 monooxygenase otaC. The NRPS encoded by the otaB gene is involved in the linking of phenylalanine to the dihydroisocoumarin ring. The reaction catalyzed by NRPS results in the production of ochratoxin B (OTB), which is the non-chlorinated analog of OTA and which subsequently serves as the substrate of the halogenase otaD for chlorination activity to form the final molecular structure of OTA, containing a chlorine atom in the C-5 position of the molecule (Probable) (PubMed:27667988, PubMed:33391201). {ECO:0000269|PubMed:27667988, ECO:0000269|PubMed:27959549, ECO:0000305|PubMed:27667988, ECO:0000305|PubMed:33391201}.
|
Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
|
A2RH77
|
ADDA_LACLM
|
MSEVKLTPEQNEAIHSSGKNILVSASAGSGKTFVMAQRIVEKVKQGIEIDRLFISTFTKKAASELRMRLERDLKKARQESSDDEEAHRLTLALQNLSNADIGTMDSFTQKLTKANFNRVNIDPNFRILADQTESDLIRQEVFEQLVESYLSADESLNISKDKFEKLIKNFSKDRNILGFQKVVYTIYRFASATENPISWLENQFLKGFETYKSLTDLSEDFTVNVKENLLTFFELLENSLTNGVIAKKGAGRDKANLILDNKNELLEAISKKDFVTCTALFLSIDTDIRVGSSKDEALSALKKDFSAQKQDLVGSKSKPGELRKFVDKIKHGQLIEKYQNQAFEIASDLQKFIIDFYKTYLERKKNENAFEYSDIAHFAIEILEENPDIRENLREHYDEIMIDEYQDTSHTQERMLELLSNGHNLFMVGDIKQSIYGFRLADPGLFLEKYKSYDQAENPNQLIRLKENFRSRGEVLNFTNDIFKHLMDEKLGEMTYGKEEALVQGNISDYPVEAEKDFYPELLLYKENTSEEEIEDSEVKISDGEIKGAAQEIKKLIEYGVEPKDIAILVRSKSNNNKIEDILLSYDIPVVLDEGRVDFLKSMEVLIMLDVLRAIDNPLYDLSLVAMLRSPLFGFNEDELTRISVQGSRDLRFWDKILLSLKKEGKNPELINLSLEQKLKAFNQKFTEWRKLVNKIPIHRLLWKIYTETYYFDYVGALKNGEMRQANLQALSVRAESYESSGYKGLFKFVRLINKFMEQNNDLASVNIKLPQNAVRVMTFHKSKGLEFDYVFLMNLQSRFNDRDLKEDVILSREHGLGMKYIADLKAEPDVITDFPYALVKMETFPYMVNKDLKQRAALSEEMRVLYVAFTRAKKKLYLVGKIKDTDKKAGLELYDAATLEGKILSDKFRNSSRGFQHWILALQNATKLPMKLNVYTKDELETEKLEFTSQPDFKKLVEESEKFDNIMSFSDEIKEAQKIMNYQYPHQAATELSSIQTPSQVKKRSYEKQLQVGEVQPVSEFVRVKNLDFSDFGPKKITAAEMGSATHSFMQYADFSQADLFSFQATLDEMGFDEKIKNQIDITKILTLFDTEFGQFLSENVDKTVKEAPFSMLRTDEFAKEQYIVRGICDGFVKLADKIILFDYKTDRFTNVSAISEIKERYKDQMNLYSEALQKAYHVNQIDKYLILLGGPRKVFVEKIDD
|
3.1.-.-; 5.6.2.4
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_01451};
|
double-strand break repair via homologous recombination [GO:0000724]
|
cytosol [GO:0005829]; DNA helicase complex [GO:0033202]
|
3'-5' DNA helicase activity [GO:0043138]; 3'-5' exonuclease activity [GO:0008408]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; double-stranded DNA binding [GO:0003690]; isomerase activity [GO:0016853]
|
PF00580;PF13361;
|
1.10.10.160;3.90.320.10;3.40.50.300;
|
Helicase family, AddA subfamily
| null | null |
CATALYTIC ACTIVITY: Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.; EC=5.6.2.4; Evidence={ECO:0000255|HAMAP-Rule:MF_01451}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=5.6.2.4; Evidence={ECO:0000255|HAMAP-Rule:MF_01451};
| null | null | null | null |
FUNCTION: The heterodimer acts both as an ATP-dependent DNA helicase and an ATP-dependent, dual-direction single-stranded exonuclease. Recognizes the L.lactis chi site (5'-GCGCGTG-3'), which stimulates homologous recombination. The RexA (AddA) nuclease domain is required for chi fragment generation; this subunit has 3'->5' exonuclease activity and probably also performs the helicase function. {ECO:0000269|PubMed:11395472, ECO:0000269|PubMed:9435243}.
|
Lactococcus lactis subsp. cremoris (strain MG1363)
|
A2RJT9
|
PYRDA_LACLM
|
MLNTTFANAKFANPFMNASGVHCMTIEDLEELKASQAGAYITKSSTLEKREGNPLPRYVDLELGSINSMGLPNLGFDYYLDYVLKNQKENAQEGPIFFSIAGMSAAENIAMLKKIQESDFSGITELNLSCPNVPGKPQLAYDFEATEKLLKEVFTFFTKPLGVKLPPYFDLVHFDIMAEILNQFPLTYVNSVNSIGNGLFIDPEAESVVIKPKDGFGGIGGAYIKPTALANVRAFYTRLKPEIQIIGTGGIETGQDAFEHLLCGATMLQIGTALHKEGPAIFDRIIKELEEIMNQKGYQSIADFHGKLKSL
|
1.3.98.1
|
COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:9032071, ECO:0000269|PubMed:9655329}; Note=Binds 1 FMN per subunit. {ECO:0000269|PubMed:9032071, ECO:0000269|PubMed:9655329};
|
'de novo' pyrimidine nucleobase biosynthetic process [GO:0006207]; 'de novo' UMP biosynthetic process [GO:0044205]
|
cytoplasm [GO:0005737]
|
dihydroorotate dehydrogenase (fumarate) activity [GO:1990663]
|
PF01180;
|
3.20.20.70;2.30.26.10;
|
Dihydroorotate dehydrogenase family, Type 1 subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=(S)-dihydroorotate + fumarate = orotate + succinate; Xref=Rhea:RHEA:30059, ChEBI:CHEBI:29806, ChEBI:CHEBI:30031, ChEBI:CHEBI:30839, ChEBI:CHEBI:30864; EC=1.3.98.1; Evidence={ECO:0000269|PubMed:8021180};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=18 uM for dihydroorotate {ECO:0000269|PubMed:12732650}; KM=250 uM for fumarate {ECO:0000269|PubMed:12732650}; Vmax=18.6 umol/min/mg enzyme {ECO:0000269|PubMed:12732650};
|
PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway.
| null | null |
FUNCTION: Catalyzes the conversion of dihydroorotate to orotate with fumarate as the electron acceptor. Molecular oxygen can replace fumarate in vitro, but cannot use NAD(+) as an electron acceptor. {ECO:0000269|PubMed:8021180}.
|
Lactococcus lactis subsp. cremoris (strain MG1363)
|
A2RRP1
|
NBAS_HUMAN
|
MAAPESGPALSPGTAEGEEETILYDLLVNTEWPPETEVQPRGNQKHGASFIITKAIRDRLLFLRQYIWYSPAPFLLPDGLVRLVNKQINWHLVLASNGKLLAAVQDQCVEIRSAKDDFTSIIGKCQVPKDPKPQWRRVAWSYDCTLLAYAESTGTVRVFDLMGSELFVISPASSFIGDLSYAIAGLIFLEYKASAQWSAELLVINYRGELRSYLVSVGTNQSYQESHCFSFSSHYPHGINTAIYHPGHRLLLVGGCETAEVGMSKASSCGLSAWRVLSGSPYYKQVTNGGDGVTAVPKTLGLLRMLSVKFYSRQGQEQDGIFKMSLSPDGMLLAAIHFSGKLSIWAIPSLKQQGEWGQNEQPGYDDLNPDWRLSTEKRKKIKDKESFYPLIDVNWWADSAVTLARCSGALTVSSVKTLKNLLGKSCEWFEPSPQVTATHDGGFLSLECEIKLAPKRSRLETRAGEEDEGEEDSDSDYEISAKARYFGYIKQGLYLVTEMERFAPPRKRPRTITKNYRLVSLRSTTPEELYQRKIESEEYEEALSLAHTYGLDTDLVYQRQWRKSAVNVASIQNYLSKIKKRSWVLHECLERVPENVDAAKELLQYGLKGTDLEALLAIGKGADDGRFTLPGEIDIDSISYEELSPPDEEPAKNKKEKELKKRQELLKLVNFSKLTLEQKELCRCRRKLLTYLDRLATYEEILGVPHASEQRYDAEFFKKFRNQNIVLSARTYAQESNVQALEILFTYHGSDLLPHRLAILSNFPETTSPHEYSVLLPEACFNGDSLMIIPWHEHKHRAKDWCEELACRMVVEPNLQDESEFLYAAQPELLRFRMTQLTVEKVMDWYQTRAEEIEHYARQVDCALSLIRLGMERNIPGLLVLCDNLVTLETLVYEARCDVTLTLKELQQMKDIEKLRLLMNSCSEDKYVTSAYQWMVPFLHRCEKQSPGVANELLKEYLVTLAKGDLKFPLKIFQHSKPDLQQKIIPDQDQLMAIALECIYTCERNDQLCLCYDLLECLPERGYGDKTEATTKLHDMVDQLEQILSVSELLEKHGLEKPISFVKNTQSSSEEARKLMVRLTRHTGRKQPPVSESHWRTLLQDMLTMQQNVYTCLDSDACYEIFTESLLCSSRLENIHLAGQMMHCSACSENPPAGIAHKGKPHYRVSYEKSIDLVLAASREYFNSSTNLTDSCMDLARCCLQLITDRPPAIQEELDLIQAVGCLEEFGVKILPLQVRLCPDRISLIKECISQSPTCYKQSTKLLGLAELLRVAGENPEERRGQVLILLVEQALRFHDYKAASMHCQELMATGYPKSWDVCSQLGQSEGYQDLATRQELMAFALTHCPPSSIELLLAASSSLQTEILYQRVNFQIHHEGGENISASPLTSKAVQEDEVGVPGSNSADLLRWTTATTMKVLSNTTTTTKAVLQAVSDGQWWKKSLTYLRPLQGQKCGGAYQIGTTANEDLEKQGCHPFYESVISNPFVAESEGTYDTYQHVPVESFAEVLLRTGKLAEAKNKGEVFPTTEVLLQLASEALPNDMTLALAYLLALPQVLDANRCFEKQSPSALSLQLAAYYYSLQIYARLAPCFRDKCHPLYRADPKELIKMVTRHVTRHEHEAWPEDLISLTKQLHCYNERLLDFTQAQILQGLRKGVDVQRFTADDQYKRETILGLAETLEESVYSIAISLAQRYSVSRWEVFMTHLEFLFTDSGLSTLEIENRAQDLHLFETLKTDPEAFHQHMVKYIYPTIGGFDHERLQYYFTLLENCGCADLGNCAIKPETHIRLLKKFKVVASGLNYKKLTDENMSPLEALEPVLSSQNILSISKLVPKIPEKDGQMLSPSSLYTIWLQKLFWTGDPHLIKQVPGSSPEWLHAYDVCMKYFDRLHPGDLITVVDAVTFSPKAVTKLSVEARKEMTRKAIKTVKHFIEKPRKRNSEDEAQEAKDSKVTYADTLNHLEKSLAHLETLSHSFILSLKNSEQETLQKYSHLYDLSRSEKEKLHDEAVAICLDGQPLAMIQQLLEVAVGPLDISPKDIVQSAIMKIISALSGGSADLGGPRDPLKVLEGVVAAVHASVDKGEELVSPEDLLEWLRPFCADDAWPVRPRIHVLQILGQSFHLTEEDSKLLVFFRTEAILKASWPQRQVDIADIENEENRYCLFMELLESSHHEAEFQHLVLLLQAWPPMKSEYVITNNPWVRLATVMLTRCTMENKEGLGNEVLKMCRSLYNTKQMLPAEGVKELCLLLLNQSLLLPSLKLLLESRDEHLHEMALEQITAVTTVNDSNCDQELLSLLLDAKLLVKCVSTPFYPRIVDHLLASLQQGRWDAEELGRHLREAGHEAEAGSLLLAVRGTHQAFRTFSTALRAAQHWV
| null | null |
negative regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:2000623]; nuclear-transcribed mRNA catabolic process [GO:0000956]; protein transport [GO:0015031]; retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum [GO:0006890]
|
cytosol [GO:0005829]; Dsl1/NZR complex [GO:0070939]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]
|
SNARE binding [GO:0000149]
|
PF15492;PF08314;
|
2.130.10.10;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20577004}. Endoplasmic reticulum {ECO:0000269|PubMed:19369418}. Endoplasmic reticulum membrane; Peripheral membrane protein {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Involved in Golgi-to-endoplasmic reticulum (ER) retrograde transport; the function is proposed to depend on its association in the NRZ complex which is believed to play a role in SNARE assembly at the ER (PubMed:19369418). Required for normal embryonic development (By similarity). May play a role in the nonsense-mediated decay pathway of mRNAs containing premature stop codons (By similarity). {ECO:0000250|UniProtKB:Q5TYW4, ECO:0000269|PubMed:19369418}.
|
Homo sapiens (Human)
|
A2RRU4
|
SCAP_RAT
|
MTLTERLREKISQAFYNHGLLCASYPIPIILFTGLCILACCYPLLKLPLPGTGPVEFSTPVKGYSPPPADSDHKQGEPSEQPEWYVGAPVAYIQQIFVKSSVSPWHRNLLAVDVFRSPLSRAFQLVEEIRNHVLRDSSGTKSLEEVCLQVTDLLPGLRKLRSLLPEHGCLLLSPGNFWQNDWERFHADPDIIGTIHQHEPKTLQTSATLKDLLFGVPGKYSGVSLYTRKRMVSYTITLVFQRYHAKFLSSLRARLMLLHPSPNCSLRAENLVHVHFKEEIGIAELIPLVTTYIILFAYIYFSTRKIDMVKSKWGLALAAVVTVLSSLLMSVGLCTLFGLTPTLNGGEIFPYLVVVIGLENVLVLTKSVVSTPVDLEVKLRIAQGLSSESWSIMKNVATELGIILIGYFTLVPAIQEFCLFAVVGLVSDFFLQMLFFTTVLSIDIRRMELADLNKRLPPESCLPSAKPVGRPARYERQLAVRPSTPHTITLQPSSFRNLRLPKRLRVIYFLARTRLAQRLIMAGTVVWIGILVYTDPAGLRTYLAAQVTEQSPLGEGSLGPMPVPSGVLPASHPDPAFSIFPPDAPKLPENQTLPGELPEHAVPAEGVQDSRAPEVTWGPEDEELWRKLSFRHWPTLFNYYNITLAKRYISLLPVIPVTLHLNPREALEGRHPQDGRTAWAPPEPLPAGLWETGPKGPGGTQTHGDITLYKVAALGLAAGIVLVLLLLCLYRVLCPRNYGQPGGGAGRRRRGELPCDDYGYAPPETEIVPLVLRGHLMDIECLASDGMLLVSCCLAGQVCVWDAQTGDCLTRIPRPGPRRDSCGGGAFEAQENWERLSDGGKASPEEPGDSPPLRRRPRGPPPPSLFGDQPDLTCLIDTNFSVQLPPEPTQPEPRHRAGCGRSRDSGYDFSRLVQRVYQEEGLAAVHMSALRPPSPGPPLPQASQEEGTAPEKGSPPLAWAPSTAGSIWSLELQGSLIVVGRSSGRLEVWDAIEGVLCCSNEEISSGITALVFLDRRIVAARLNGSLDFFSLETHTSLSPLQFRGTPGRGSSPSSPVYSSSNTVACHLTHTVPCAHQKPITALRAAAGRLVTGSQDHTLRVFRLEDSCCLFTLQGHSGAITTVYIDQTMVLASGGQDGAICLWDVLTGSRVSHTFAHRGDVTSLTCTTSCVISSGLDDFINIWDRSTGIKLYSIQQDLGCGASLGVISDNLLVTGGQGCVSFWDLNYGDLLQTVYLGKNSEAQPARQILVLDNAAIVCNFGSELSLVYVPSVLEKLD
| null | null |
cellular lipid metabolic process [GO:0044255]; cholesterol metabolic process [GO:0008203]; COPII-coated vesicle cargo loading [GO:0090110]; immune response [GO:0006955]; positive regulation of cholesterol biosynthetic process [GO:0045542]; regulation of cholesterol biosynthetic process [GO:0045540]; regulation of fatty acid biosynthetic process [GO:0042304]; regulation of fatty acid metabolic process [GO:0019217]; response to hypoxia [GO:0001666]; response to insulin [GO:0032868]; response to vitamin B3 [GO:0033552]; SREBP signaling pathway [GO:0032933]
|
endoplasmic reticulum membrane [GO:0005789]; ER to Golgi transport vesicle membrane [GO:0012507]; Golgi membrane [GO:0000139]; protein-containing complex [GO:0032991]; SREBP-SCAP complex [GO:0032936]
|
protein-containing complex binding [GO:0044877]; sterol binding [GO:0032934]
|
PF12349;PF00400;
|
2.130.10.10;
|
WD repeat SCAP family
|
PTM: Ubiquitinated at Lys-454 and Lys-466. RNF145 triggers ubiquitination of SCAP, likely inhibiting SCAP-SREBP complex transport to the Golgi apparatus and the subsequent processing/maturation of SREBF2/SREBP2. {ECO:0000250|UniProtKB:Q6GQT6}.
|
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P97260}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P97260}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250|UniProtKB:P97260}; Multi-pass membrane protein {ECO:0000255}. Note=Moves from the endoplasmic reticulum to the Golgi in the absence of sterols. Requires the presence of SPRING for proper localization to endoplasmic reticulum. {ECO:0000250|UniProtKB:P97260, ECO:0000250|UniProtKB:Q12770}.
| null | null | null | null | null |
FUNCTION: Escort protein required for cholesterol as well as lipid homeostasis. Regulates export of the SCAP-SREBP complex from the endoplasmic reticulum to the Golgi upon low cholesterol, thereby regulating the processing of sterol regulatory element-binding proteins (SREBPs) SREBF1/SREBP1 and SREBF2/SREBP2. At high sterol concentrations, formation of a ternary complex with INSIG (INSIG1 or INSIG2) leads to mask the ER export signal in SCAP, promoting retention of the complex in the endoplasmic reticulum. Low sterol concentrations trigger release of INSIG, a conformational change in the SSD domain of SCAP, unmasking of the ER export signal, promoting recruitment into COPII-coated vesicles and transport of the SCAP-SREBP to the Golgi: in the Golgi, SREBPs are then processed, releasing the transcription factor fragment of SREBPs from the membrane, its import into the nucleus and up-regulation of LDLR, INSIG1 and the mevalonate pathway. Binds cholesterol via its SSD domain. {ECO:0000250|UniProtKB:P97260}.
|
Rattus norvegicus (Rat)
|
A2RST1
|
MGST2_MOUSE
|
MAGDSSLLAAVSLLSACQQSYFAWRVGRARLKHKIAPPAVTGPLEFERIFRAQQNSLEFYPVFIVMLWMAGWYFNQVFAACLGLLYIYARHKYFWGYAEAAEKRITGFRLSLGILTLLPVLAVLGVASRFLNEYLDFHVAKKLRKPF
|
1.11.1.-; 2.5.1.18; 4.4.1.20
| null |
glutathione biosynthetic process [GO:0006750]; leukotriene biosynthetic process [GO:0019370]; lipid metabolic process [GO:0006629]; membrane lipid catabolic process [GO:0046466]; response to lipopolysaccharide [GO:0032496]; response to organonitrogen compound [GO:0010243]
|
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231]; nuclear envelope [GO:0005635]; plasma membrane [GO:0005886]
|
enzyme activator activity [GO:0008047]; glutathione binding [GO:0043295]; glutathione peroxidase activity [GO:0004602]; glutathione transferase activity [GO:0004364]; identical protein binding [GO:0042802]; leukotriene-C4 synthase activity [GO:0004464]
|
PF01124;
|
1.20.120.550;
| null | null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q99735}; Multi-pass membrane protein {ECO:0000255}. Microsome membrane {ECO:0000250|UniProtKB:Q99735}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=glutathione + RX = a halide anion + an S-substituted glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378, ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925, ChEBI:CHEBI:90779; EC=2.5.1.18; Evidence={ECO:0000250|UniProtKB:Q99735}; CATALYTIC ACTIVITY: Reaction=1-chloro-2,4-dinitrobenzene + glutathione = 2,4-dinitrophenyl-S-glutathione + chloride + H(+); Xref=Rhea:RHEA:51220, ChEBI:CHEBI:15378, ChEBI:CHEBI:17996, ChEBI:CHEBI:34718, ChEBI:CHEBI:57925, ChEBI:CHEBI:133977; EC=2.5.1.18; Evidence={ECO:0000250|UniProtKB:Q99735}; CATALYTIC ACTIVITY: Reaction=leukotriene C4 = glutathione + leukotriene A4; Xref=Rhea:RHEA:17617, ChEBI:CHEBI:57463, ChEBI:CHEBI:57925, ChEBI:CHEBI:57973; EC=4.4.1.20; Evidence={ECO:0000250|UniProtKB:Q99735}; CATALYTIC ACTIVITY: Reaction=(5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + 2 glutathione = (5S)-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + glutathione disulfide + H2O; Xref=Rhea:RHEA:48620, ChEBI:CHEBI:15377, ChEBI:CHEBI:57450, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:90632; Evidence={ECO:0000250|UniProtKB:Q99735};
| null | null | null | null |
FUNCTION: Catalyzes several different glutathione-dependent reactions. Catalyzes the glutathione-dependent reduction of lipid hydroperoxides, such as 5-HPETE. Has glutathione transferase activity, toward xenobiotic electrophiles, such as 1-chloro-2, 4-dinitrobenzene (CDNB). Catalyzes also the conjugation of leukotriene A4 with reduced glutathione to form leukotriene C4 (LTC4) (By similarity). Involved in oxidative DNA damage induced by ER stress and anticancer agents by activating LTC4 biosynthetic machinery in nonimmune cells (PubMed:26656251). {ECO:0000250|UniProtKB:Q99735, ECO:0000269|PubMed:26656251}.
|
Mus musculus (Mouse)
|
A2RSY6
|
TRM1L_MOUSE
|
MENMAEEELLPQEKEEAQVRVPTPAPDSAPVPAPAADTALDSAPTPDSDPAPALAPAPAPALSPSLASVPEEAESKRHISIQRRLADLEKLAFGTEGDVDSASSLNSDNPGTENSQTCPLCPKEKFRAYSSHKLRRHLQNLHWKISVEFEGYRMCICHLACRPVKPTIVGEQISSKLGAHYHCIICSATITRRTDMLGHVKRHVNKGETKSRYIAASTAKSSNEILKETDTDIQVFPNYSIPQKTDSYFNPKMKLNRQIIFCTLAALAKERKPLECLDAFGATGIMGLQWAKHLGNAVKVTINDLNENSVTLIQKNCHLNKLKVVVDSEEKEEGDALEDDGTLGDIQVTRMDANVLMHLRSFDFIHLDPFGTSVNYLDSAFRNVRNLGIVSVTSTDISSLYAKAQHVARRHYGCNIVRTEYYKELAARIVVAAVARAAARCNKGIEVLFAVALEHFVLVVVRVLRGPTSADETAKKIQYLIHCQWCEERIFQKDGNMVEENPYRQLPCNCHGSMPGKTAIELGPLWSSSLFNTGFLKRMLFESIHHGLDDIQPLIKTLIFESECTPQSQCSTHAPSNTNKQEENGVFVKTTDDTTIDIYSAQGKRKSNEMAINLAKKQKTDASTAHPPFYYNIHRHSIKGMNMPKLKKFLCCLSQAGFRVSRTHFDPMGIRTDAPLMQFKSILLKYSTPTYTGAQSEGQMPPAAEDTVTDRVEMSVSDKAEASGCRRW
|
2.1.1.-
| null |
adult behavior [GO:0030534]; adult locomotory behavior [GO:0008344]; tRNA N2-guanine methylation [GO:0002940]
|
nucleus [GO:0005634]
|
metal ion binding [GO:0046872]; tRNA (guanine(10)-N2)-methyltransferase activity [GO:0160102]; tRNA binding [GO:0000049]
|
PF02005;
|
3.30.56.70;3.40.50.150;
|
Class I-like SAM-binding methyltransferase superfamily, Trm1 family
| null | null | null | null | null | null | null |
FUNCTION: May play a role in motor coordination and exploratory behavior. {ECO:0000269|PubMed:17198746}.
|
Mus musculus (Mouse)
|
A2RT67
|
DEND3_MOUSE
|
MAEPAARHLSLPSGLLELCALLGASQDSLRGLEQIAQKRGVKSASSLVPEVLSVFVPPFTTKEDGQVPGASCALGKGRRRSFRKKREKPRMEPWKSHPGDSKGPDSEDVTIPGGVDLLALPQLCFPGCVCVASEPKEDYIHFLVLTDVCGNRTYGVVAQYYRPLHDEYCFYNGKSHWEPSVISARCFVPFAVCVVSRFPYYNSLKDCLSCLLTHLKLCKDFEVDNHIKDFAARLSLIPSPPPGPLHLIFNMKPLQVVFPSRADPESPIVDLDLHLPLLCFRPEKVLQILTCILTEQRIVFFSSDWALLTLMAECFVAYLHPLQWQHTFVPILSGQMLDFVMAPTSFLMGCHLDHFEEVRKEADGLVLIDIDHGSVTCSKSSDDNIDIPDVPLLLAQTFIQRVQSLQLHPDLHLAHLSASTDLNEGRARRRAWQQTLNCKIQHITLQLLVGIFREVKNHLNYEHRVFNSEEFLKTRAAGDQQFYKQVLDTYMFHSFLKARLNGRMDAFARMDLDTQSEEDRIDRMLISPRRPTVEKMASRKASPLHITHRRMVVSMPNLQDISLPELPPRNSSLRIMDTSNCRSSSPVLKVTPKSTYMFKIPDIHFPLESQCVQAYYTDFVTLLSKAMALLGPGDSLLLARYFYLRGLLHLMQGQLLSALLDFQNLYKTDIGIFPADLVKRTVESMSASERAQAERTPELRRLITEVFDKHGEAPKADDAVKNFELPKKHMQLNDFVKRVQESGIVKDAVIIHRLFDALTFGHEKQIDPETFRDFYTCWKETEAEAQEVSLPALLMEHLDKNECVYKLSSSVKTNRGVGKIAMTQKRLFLLTEGRPGYVEIATFRNIEEVKNSTVAFLLLRIPTLKIKTVAKKEVFEANLKSECDLWHLMVKEMWAGKQLADDHKDPQYVQQALTNVLLMDAVVGTLQSPSAIHAASKLAYFDNMKKKSPMAVPKTTSETLKHKINPSAGETAPQAIEVLLYTPGRLDPAEKVEDAHPKLWCALNEGKVVVFDASSWTVHQHCFKVGSSKVNCMVMAEHNQVWVGSEDSVIYIINVHSMSCNKQLTDHRSPVTGLAVHNGKKPSEIYSCSLDGTVIAWNVSTLRVISRFQLSYGDLLSISLHNDRIWCCTVHKILVVTPQGFVRQELKHPKDASFLAFQLLPEEQQLWAASTGVSELYMWSLKDLDQPPQKTYLQDCSEVTCMIRVKRQIWVGGRGLSQGKTRGKIYVMDVEKVTVEKELVAHLDTVRTLCSAEDRYVLSGAGQEEGKIAIWKVE
| null | null |
endosome to lysosome transport [GO:0008333]; protein catabolic process [GO:0030163]; regulation of Rab protein signal transduction [GO:0032483]
|
cytoplasmic vesicle [GO:0031410]
|
guanyl-nucleotide exchange factor activity [GO:0005085]
|
PF02141;
|
3.30.450.200;3.40.50.11500;2.130.10.10;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28249939}. Note=Transiently recruited to membranes to activate Rab12. {ECO:0000269|PubMed:28249939}.
| null | null | null | null | null |
FUNCTION: Guanine nucleotide exchange factor (GEF) activating Rab12. Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab12 into its active GTP-bound form. Regulates autophagy in response to starvation through Rab12 activation (PubMed:24719330, PubMed:25925668, PubMed:28249939). Starvation leads to ULK1/2-dependent phosphorylation of Ser-554 and Ser-572, which in turn allows recruitment of 14-3-3 adapter proteins and leads to up-regulation of GEF activity towards Rab12 (PubMed:25925668). Also plays a role in protein transport from recycling endosomes to lysosomes, regulating, for instance, the degradation of the transferrin receptor and of the amino acid transporter PAT4 (PubMed:21718402, PubMed:24719330). Starvation also induces phosphorylation at Tyr-940, which leads to up-regulated GEF activity and initiates autophagy (PubMed:28249939). {ECO:0000269|PubMed:21718402, ECO:0000269|PubMed:24719330, ECO:0000269|PubMed:25925668, ECO:0000269|PubMed:28249939}.
|
Mus musculus (Mouse)
|
A2RTF1
|
CTSRB_MOUSE
|
MESPLIYVMLVLLNVFVFSSGVIHNKGKERTYFSCSGEGILTGLHTIKLFLTMDNLKVRCFFRNENQSPSKEILGLFTSGGLAPNMIITNSTFYGGYYFKLTPFSNRLEWLIDIPRQNITVNTDIAAVEQWMIKITMHEGLNIYDTEGTLLDLVREPILQWNLGRVLTEMEVRDLYPEVNDIKVTKSPCANDVALIGFMMKPSSNGVFIGKTISGFWTYKECIWHDLTEIIYAELKDEHQGLTVIDLVLTNHFLVILTSLGLYVSSDLRYPTTSQIKLSRAEFCGFERVDYIRGNLWYNEKCFANRESFEVDYVTITFNRNRTLSESSSCFFSKEPFLHWLPCVFSTIKNEKSIPRVITFLIDQETDSGIYLFNVQDTKETYVTVAMLKDGKPSPRPKFPSFHFPSTFTLPLGMIFHPRSHFLYVYGSQIWVSMDGGNTFEMLCNLFSHHVTKTSNSFYTSDIVFIVEDGRILTTKAGLTTYSELGILKDAIFTLYYDQLGYIHKLTPENFDAGSKLLGHGNSGSIFGKRPDLGFEAILVPQYISTNEMYFFAHVPLTMPTNIQWKKRFKTIHLGKTIEFSKTGLANIKNVYMHKTEPVGFQTSIHTEIIVPFGIENSKDSPCLLSDLEITYSGKLYYTIKLLSKNPLHELKSTDVEKSVLIPGYSSFLIMNITDKWTASALATMPQAIKSNLKFLTGSWFLYNFGTAGGRKWSISTRQCNYWIQQDSLDFMSLNLVKYIDVGNTIDFQFKIIPKAMSTFPIPPVSMVVGNPGLVEVKTQGVFDLNENYYLDIHVSGRFFQKGSTSIALVLWEGSSKCYAITLLPTIKSSCSYLRTMHHTPGRHIPPEDWISGVHKDSQGFNMIKTLPINYRPPSHMGISIPLTDNFYHADPSKPIPRNQFHKSKETGKYKQCANVTSRAMCNCSEHQKFSHAVAFSDCKEKVHRFKFPVTQYPVVLEIFNERDKISAEPPYLVTMTEVNMRKNWQLKHNEPENVKKMKHYLEPLLKTPVYNPLGLNLTIQGSELFHFKVSVVPGVSFCELSEEFQIYVDEVPLPFPGHALIAVATSVVLGVLIFIAFVFQLRNIHPLKALKKSIRGNPGLTSSTTVSS
| null | null |
sperm capacitation [GO:0048240]
|
CatSper complex [GO:0036128]; cilium [GO:0005929]; monoatomic ion channel complex [GO:0034702]; sperm principal piece [GO:0097228]
| null |
PF15149;PF21541;PF21548;
| null | null | null |
SUBCELLULAR LOCATION: Cell projection, cilium, flagellum membrane {ECO:0000269|PubMed:17478420, ECO:0000269|PubMed:34225353}; Single-pass membrane protein {ECO:0000269|PubMed:34225353}. Note=Predominantly located in the principal piece of the sperm tail. {ECO:0000269|PubMed:17478420, ECO:0000269|PubMed:34225353}.
| null | null | null | null | null |
FUNCTION: Auxiliary component of the CatSper complex, a complex involved in sperm cell hyperactivation (PubMed:17478420, PubMed:34225353). Sperm cell hyperactivation is needed for sperm motility which is essential late in the preparation of sperm for fertilization (PubMed:17478420). {ECO:0000269|PubMed:17478420, ECO:0000269|PubMed:34225353}.
|
Mus musculus (Mouse)
|
A2RTX5
|
SYTC2_HUMAN
|
MAAEALAAEAVASRLERQEEDIRWLWSEVERLRDEQLNAPYSCQAEGPCLTREVAQLRAENCDLRHRLCSLRLCLAEERSRQATLESAELEAAQEAGAQPPPSQSQDKDMKKKKMKESEADSEVKHQPIFIKERLKLFEILKKDHQLLLAIYGKKGDTSNIITVRVADGQTVQGEVWKTTPYQVAAEISQELAESTVIAKVNGELWDLDRPLEGDSSLELLTFDNEEAQAVYWHSSAHILGEAMELYYGGHLCYGPPIENGFYYDMFIEDRAVSSTELSALENICKAIIKEKQPFERLEVSKEILLEMFKYNKFKCRILNEKVNTATTTVYRCGPLIDLCKGPHVRHTGKIKTIKIFKNSSTYWEGNPEMETLQRIYGISFPDNKMMRDWEKFQEEAKNRDHRKIGKEQELFFFHDLSPGSCFFLPRGAFIYNTLTDFIREEYHKRDFTEVLSPNMYNSKLWEASGHWQHYSENMFTFEIEKDTFALKPMNCPGHCLMFAHRPRSWREMPIRFADFGVLHRNELSGTLSGLTRVRRFQQDDAHIFCTVEQIEEEIKGCLQFLQSVYSTFGFSFQLNLSTRPENFLGEIEMWNEAEKQLQNSLMDFGEPWKMNPGDGAFYGPKIDIKIKDAIGRYHQCATIQLDFQLPIRFNLTYVSKDGDDKKRPVIIHRAILGSVERMIAILSENYGGKWPFWLSPRQVMVIPVGPTCEKYALQVSSEFFEEGFMADVDLDHSCTLNKKIRNAQLAQYNFILVVGEKEKIDNAVNVRTRDNKIHGEILVTSAIDKLKNLRKTRTLNAEEAF
|
6.1.1.3
| null |
threonyl-tRNA aminoacylation [GO:0006435]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; identical protein binding [GO:0042802]; threonine-tRNA ligase activity [GO:0004829]
|
PF03129;PF02824;PF00587;PF07973;
|
3.10.20.30;3.40.50.800;
|
Class-II aminoacyl-tRNA synthetase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8BLY2}. Nucleus {ECO:0000250|UniProtKB:Q8BLY2}. Note=Primarily cytoplasmic. Also detected at lower levels in the nucleus. {ECO:0000250|UniProtKB:Q8BLY2}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + H(+) + L-threonyl-tRNA(Thr); Xref=Rhea:RHEA:24624, Rhea:RHEA-COMP:9670, Rhea:RHEA-COMP:9704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57926, ChEBI:CHEBI:78442, ChEBI:CHEBI:78534, ChEBI:CHEBI:456215; EC=6.1.1.3; Evidence={ECO:0000250|UniProtKB:Q8BLY2};
| null | null | null | null |
FUNCTION: Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). Also edits incorrectly charged tRNA(Thr) via its editing domain, at the post-transfer stage. {ECO:0000250|UniProtKB:Q8BLY2}.
|
Homo sapiens (Human)
|
A2RU14
|
TM218_HUMAN
|
MAGTVLGVGAGVFILALLWVAVLLLCVLLSRASGAARFSVIFLFFGAVIITSVLLLFPRAGEFPAPEVEVKIVDDFFIGRYVLLAFLSAIFLGGLFLVLIHYVLEPIYAKPLHSY
| null | null | null |
cilium [GO:0005929]; membrane [GO:0016020]
| null | null | null |
TMEM218 family
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cell projection, cilium {ECO:0000250|UniProtKB:Q9CQ44}. Note=Localizes at the transition zone, a region between the basal body and the ciliary axoneme. {ECO:0000250|UniProtKB:Q9CQ44}.
| null | null | null | null | null |
FUNCTION: May be involved in ciliary biogenesis or function. {ECO:0000250|UniProtKB:Q9CQ44}.
|
Homo sapiens (Human)
|
A2RU30
|
TESP1_HUMAN
|
MEASVLSPTSWEKRRAWLRQSRNWQTQVLEEEAAAALQDVPDPEPSSLDDVFQEGNPINKIEDWLQDCGYSEEGFSEEAGQFIYNGFCSHGTSFEDDLTLGAEATLLAANGKLFSRSFLETARPCQLLDLGCSLASSSMTGGTNKTSSSISEILDKVQEDAEDVLFSLGFGQEDHKDTSRIPARFFTTPSQAKGIDFQLFLKSQVRRIEMEDPCLMLASRFKQVQTLAVTADAFFCLYSYVSKTPVQKFTPSHMFWNCNHPTDVPSIRILSREPEPQSPRDRLRKAISKMCLYTCPRDRPPPPHNTPKRNSLDQVVLEVMDKVKEEKQFLQQDSDLGQFSQEDPVPPAEGKKLPTSPYPCVFCCEEETQQRMSTVLAPSQTLDSNPKVPCCTHSLPIEDPQWSTDPAQIRRELCSLPATNTETHPAKDETFWKRKSRARKSLFQKNLMGRKVKSLDLSITQQKWKQSVDRPELRRSLSQQPQDTFDLEEVQSNSEEEQSQSRWPSRPRHPHHHQTFAGKDS
| null | null |
COP9 signalosome assembly [GO:0010387]; positive regulation of T cell differentiation in thymus [GO:0033089]; positive regulation of T cell receptor signaling pathway [GO:0050862]; protein localization [GO:0008104]; T cell differentiation in thymus [GO:0033077]; TCR signalosome assembly [GO:0036399]
|
COP9 signalosome [GO:0008180]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; TCR signalosome [GO:0036398]
|
phospholipase binding [GO:0043274]; signaling receptor binding [GO:0005102]
|
PF14722;
| null | null |
PTM: May be phosphorylated in response to store-operated Ca(+2) entry. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22561606, ECO:0000269|PubMed:23501103}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:23501103}. Note=May localize to mitochondria-associated endoplasmic reticulum membrane (MAM). {ECO:0000269|PubMed:23501103}.
| null | null | null | null | null |
FUNCTION: Required for the development and maturation of T-cells, its function being essential for the late stages of thymocyte development (By similarity). Plays a role in T-cell antigen receptor (TCR)-mediated activation of the ERK and NFAT signaling pathways, possibly by serving as a scaffolding protein that promotes the assembly of the LAT signalosome in thymocytes. May play a role in the regulation of inositol 1,4,5-trisphosphate receptor-mediated Ca(2+) release and mitochondrial Ca(2+) uptake via the mitochondria-associated endoplasmic reticulum membrane (MAM) compartment. {ECO:0000250, ECO:0000269|PubMed:22561606}.
|
Homo sapiens (Human)
|
A2RU49
|
HYKK_HUMAN
|
MSSGNYQQSEALSKPTFSEEQASALVESVFGLKVSKVRPLPSYDDQNFHVYVSKTKDGPTEYVLKISNTKASKNPDLIEVQNHIIMFLKAAGFPTASVCHTKGDNTASLVSVDSGSEIKSYLVRLLTYLPGRPIAELPVSPQLLYEIGKLAAKLDKTLQRFHHPKLSSLHRENFIWNLKNVPLLEKYLYALGQNRNREIVEHVIHLFKEEVMTKLSHFRECINHGDLNDHNILIESSKSASGNAEYQVSGILDFGDMSYGYYVFEVAITIMYMMIESKSPIQVGGHVLAGFESITPLTAVEKGALFLLVCSRFCQSLVMAAYSCQLYPENKDYLMVTAKTGWKHLQQMFDMGQKAVEEIWFETAKSYESGISM
|
2.7.1.81
| null |
lysine catabolic process [GO:0006554]; phosphorylation [GO:0016310]
|
mitochondrial matrix [GO:0005759]
|
amino acid kinase activity [GO:0019202]; hydroxylysine kinase activity [GO:0047992]
|
PF01636;
|
3.90.1200.10;
|
Aminoglycoside phosphotransferase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=(5R)-5-hydroxy-L-lysine + GTP = (5R)-5-phosphooxy-L-lysine + GDP + H(+); Xref=Rhea:RHEA:19049, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:57882, ChEBI:CHEBI:58189, ChEBI:CHEBI:58357; EC=2.7.1.81; Evidence={ECO:0000269|PubMed:22241472};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=280 uM for (5R)-5-hydroxy-L-lysine (in the presence of 2 mM ATP) {ECO:0000269|PubMed:22241472}; KM=7.6 uM for (5R)-5-hydroxy-L-lysine (in the presence of 0.2 mM GTP) {ECO:0000269|PubMed:22241472}; KM=810 uM for ATP (in the presence of 0.5 mM (5R)-5-hydroxy-L-lysine) {ECO:0000269|PubMed:22241472}; KM=3.5 uM for GTP (in the presence of 0.5 mM (5R)-5-hydroxy-L-lysine) {ECO:0000269|PubMed:22241472}; Vmax=4.95 umol/min/mg enzyme toward (5R)-5-hydroxy-L-lysine (in the presence of 2 mM ATP) {ECO:0000269|PubMed:22241472}; Vmax=0.49 umol/min/mg enzyme toward (5R)-5-hydroxy-L-lysine (in the presence of 0.2 mM GTP) {ECO:0000269|PubMed:22241472}; Vmax=5.28 umol/min/mg enzyme toward ATP (in the presence of 0.5 mM (5R)-5-hydroxy-L-lysine) {ECO:0000269|PubMed:22241472}; Vmax=0.57 umol/min/mg enzyme toward GTP (in the presence of 0.5 mM (5R)-5-hydroxy-L-lysine) {ECO:0000269|PubMed:22241472};
| null | null | null |
FUNCTION: Catalyzes the GTP-dependent phosphorylation of 5-hydroxy-L-lysine. {ECO:0000269|PubMed:22241472}.
|
Homo sapiens (Human)
|
A2RUB1
|
MEIOC_HUMAN
|
MEVRRGDTCPRPHPSGLREEGLEPKVAFPGGANRCWNLGADAGSRLTDVFGSVMLTGSASFYDCYTSQSEDNVDLRQTYTPFSSTEYSSSVDSSLFCAPWSTYGDDIKQPSNSQISIKNRIQTERNDYGSETDLYGLVSNILEEQDKSQPYFAEGTCSSNLKSVWPMNTSRFADHHDLLTETKRPIDTVISQQAFYSDESVSAMEKQYLRNSNLTPQQKIDELHHGFTGLDLEEQWMYPSRSDHSNCHNIQTNDTAKTTFQEYPLIKNCFTPQTGLSDIMKESGVDIYHYGRDRICTKGLEAPLQQKRAEMFLSQFNRYNENVDYCRYPEYVHPNKAKLNKCSNFSVQDSKKLANGTPETPTVEADTYTKLFQVKPANQKKMEETIPDQQNFTFPKTTPHLTEKQFAKEAVFTADFGLTSEYGLKPHTACPANDFANVTEKQQFAKPDPPHSEYFKSVNLLSNSATSSGGINLNRPTWMNVQTKNNTPIPYRNQGNLMKLNSHLSAASKGSNHSSDFPQLSSTNLTPNSNLFQKYCQENPSAFSSFDFSYSGAERIQSVNHIEGLTKPGEENLFKLVTDKKIKQPNGFCDNYSAQKYGIIENVNKHNFQAKPQSGHYDPEEGPKHLDGLSQNTYQDLLESQGHSNSHRTRGGDNSRVNRTQVSCFSNNYMMGDLRHNQCFQQLGSNGFPLRSTHPFGHSVVPLLDSYDLLSYDDLSHLYPYFNMMYGDNSFSGLMPTFGFQRPIKTRSGPASELHIRLEECCEQWRALEKERKKTELALAKNYPGKKVSSTNNTPVPRLTSNPSRVDRLIVDELRELARVVTLLGKMERLRSSLLHASISTALDRHLESIHIVQSRRKDEIVNASNRQRQGVPRCQDDRDVFALASAIKEMCVATRKTRTALWCALQMTLPKTASTADVVKPLQDTVNCEDKVHESINSSNPMNQRGETNKH
| null | null |
chromosome organization involved in meiotic cell cycle [GO:0070192]; double-strand break repair [GO:0006302]; female meiosis I [GO:0007144]; germline cell cycle switching, mitotic to meiotic cell cycle [GO:0051729]; male meiosis I [GO:0007141]; metaphase chromosome alignment [GO:0051310]; mRNA stabilization [GO:0048255]; oocyte development [GO:0048599]; spermatid development [GO:0007286]; synaptonemal complex assembly [GO:0007130]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
| null |
PF15189;
| null | null | null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A2AG06}. Nucleus {ECO:0000250|UniProtKB:A2AG06}. Note=at late pachytene a fraction is nuclear. {ECO:0000250|UniProtKB:A2AG06}.
| null | null | null | null | null |
FUNCTION: Is required for meiosis completion in both male and female germ cells. Confers stability to numerous meiotic mRNAs in gonads allowing proper initiation and progression into meiosis prophase I. The function may involve YTHDC2 and is independent of induction by retinoic acid (RA). Maintains an extended meiotic prophase I by properly promoting the transition from a mitotic to a meiotic cell cycle program by binding transcripts through its interaction with YTHDC2 that regulate the mitotic cell cycle. {ECO:0000250|UniProtKB:A2AG06}.
|
Homo sapiens (Human)
|
A2RUB6
|
CCD66_HUMAN
|
MNLGDGLKLETELLDGKTKLILSPYEHKSKISVKMGNKAKIAKCPLRTKTGHILKSTQDTCIGSEKLLQKKPVGSETSQAKGEKNGMTFSSTKDLCKQCIDKDCLHIQKEISPATPNMQKTRNTVNTSLVGKQKPHKKHITAENMKSSLVCLTQDQLQQILMTVNQGNRSLSLTENGKEAKSQYSLYLNSISNQPKDENIMGLFKKTEMVSSVPAENKSVLNEHQETSKQCEQKIAIENEWKPADIFSTLGERECDRSSLEAKKAQWRKELDEQVALKKKEKEVSEKWNDPWKKSESDKIIWEKHQILDQSRETVLLEHPFSAVKQELQRKWIEELNKQIEDDRQRKIEEKIIYSKGEEHDRWAMHFDSLKSYPGSQSQLFSQSTHKQPEYFCVSPDTQELADVSSVCTPTTGSQVEPSEEEHIAKPIKDVVMANSKKTNFLRSMTALLDPAQIEERDRRRQKQLEHQKAITAQVEEKRRKKQLEEEQRKKEEQEEELRLAQEREEMQKQYEEDILKQKQKEEIMTLKTNELFQTMQRAQELAQRLKQEQRIRELAQKGHDTSRLIKNLGVDTIQMEYNASNISNSRHDSDEISGKMNTYMNSTTSKKDTGVQTDDLNIGIFTNAESHCGSLMERDITNCSSPEISAELIGQFSTKKNKQELTQDKGASLEKENNRCNDQCNQFTRIEKQTKHMKKYPKRPDWNINKPPKRYIPASEKYPKQLQKQREEKKVRRQMELLHLVEKNNPGHLSQNRGISPEIFHSSHQETESKLRWHLVKKEEEPLNIHSFSKERSPSSPVPVVKNRTQQTQNTLHLPLKNSSYERENLISGSNQTELSSGISESSHFIPYVRTNEIYYLDPDAPLSGPSTQDPQYQNSQDCGQKRQLFDSDCVRDPLLNPNMVKNRDRQQAILKGLSELRQGLLQKQKELESSLLPLAENQEESFGSSF
| null | null |
cilium assembly [GO:0060271]; detection of light stimulus involved in visual perception [GO:0050908]; microtubule bundle formation [GO:0001578]; regulation of protein localization to cilium [GO:1903564]; retina homeostasis [GO:0001895]
|
cell junction [GO:0030054]; centriolar satellite [GO:0034451]; centrosome [GO:0005813]; ciliary basal body [GO:0036064]; cilium [GO:0005929]; cytosol [GO:0005829]; Flemming body [GO:0090543]; microtubule [GO:0005874]; photoreceptor inner segment [GO:0001917]; photoreceptor outer segment [GO:0001750]
|
microtubule binding [GO:0008017]; protein homodimerization activity [GO:0042803]
|
PF15236;
| null | null | null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:28235840}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000269|PubMed:28235840}. Cell projection, cilium {ECO:0000269|PubMed:28235840}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:28235840}. Photoreceptor inner segment {ECO:0000269|PubMed:19777273}. Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:19777273}. Note=Restricted to the centrosomes and the spindle microtubules during mitosis (PubMed:28235840). Enriched in the inner segment of the photoreceptor (PubMed:19777273). {ECO:0000269|PubMed:19777273, ECO:0000269|PubMed:28235840}.
| null | null | null | null | null |
FUNCTION: Microtubule-binding protein required for ciliogenesis (PubMed:28235840). May function in ciliogenesis by mediating the transport of proteins like BBS4 to the cilium, but also through the organization of the centriolar satellites (PubMed:28235840). Plays a role in retina morphogenesis and/or homeostasis (By similarity). {ECO:0000250|UniProtKB:Q6NS45, ECO:0000269|PubMed:28235840}.
|
Homo sapiens (Human)
|
A2RUC4
|
TYW5_HUMAN
|
MAGQHLPVPRLEGVSREQFMQHLYPQRKPLVLEGIDLGPCTSKWTVDYLSQVGGKKEVKIHVAAVAQMDFISKNFVYRTLPFDQLVQRAAEEKHKEFFVSEDEKYYLRSLGEDPRKDVADIRKQFPLLKGDIKFPEFFKEEQFFSSVFRISSPGLQLWTHYDVMDNLLIQVTGKKRVVLFSPRDAQYLYLKGTKSEVLNIDNPDLAKYPLFSKARRYECSLEAGDVLFIPALWFHNVISEEFGVGVNIFWKHLPSECYDKTDTYGNKDPTAASRAAQILDRALKTLAELPEEYRDFYARRMVLHIQDKAYSKNSE
|
1.14.11.42
|
COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:20972222}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000269|PubMed:20972222};
|
wybutosine biosynthetic process [GO:0031591]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
2-oxoglutarate-dependent dioxygenase activity [GO:0016706]; histone H3K36 demethylase activity [GO:0051864]; iron ion binding [GO:0005506]; protein homodimerization activity [GO:0042803]; tRNA binding [GO:0000049]; tRNA(Phe) (7-(3-amino-3-carboxypropyl)wyosine37-C2)-hydroxylase activity [GO:0102524]
|
PF13621;
|
6.10.140.1470;2.60.120.650;
|
TYW5 family
| null | null |
CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + 7-[(3S)-3-amino-3-carboxypropyl]wyosine(37) in tRNA(Phe) + O2 = 7-(2-hydroxy-3-amino-3-carboxypropyl)wyosine(37) in tRNA(Phe) + CO2 + succinate; Xref=Rhea:RHEA:37899, Rhea:RHEA-COMP:10379, Rhea:RHEA-COMP:11848, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031, ChEBI:CHEBI:73543, ChEBI:CHEBI:73603; EC=1.14.11.42; Evidence={ECO:0000269|PubMed:20739293, ECO:0000269|PubMed:20972222}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37900; Evidence={ECO:0000269|PubMed:20739293};
| null |
PATHWAY: tRNA modification; wybutosine-tRNA(Phe) biosynthesis. {ECO:0000269|PubMed:20739293, ECO:0000269|PubMed:20972222}.
| null | null |
FUNCTION: tRNA hydroxylase that acts as a component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA. Catalyzes the hydroxylation of 7-(a-amino-a-carboxypropyl)wyosine (yW-72) into undermodified hydroxywybutosine (OHyW*). OHyW* being further transformed into hydroxywybutosine (OHyW) by LCMT2/TYW4. OHyW is a derivative of wybutosine found in higher eukaryotes. {ECO:0000269|PubMed:20739293, ECO:0000269|PubMed:20972222}.
|
Homo sapiens (Human)
|
A2RUH7
|
MBPHL_HUMAN
|
MEAATAPEVAAGSKLKVKEASPADAEPPQASPGQGAGSPTPQLLPPIEEHPKIWLPRALRQTYIRKVGDTVNLLIPFQGKPKPQAIWTHDGCALDTRRVSVRNGEQDSILFIREAQRADSGRYQLRVQLGGLEATATIDILVIERPGPPQSIKLVDVWGFSATLEWTPPQDTGNTALLGYTVQKADTKSGLWFTVLEHYHRTSCIVSDLIIGNSYAFRVFAENQCGLSETAPITTDLAHIQKAATVYKTKGFAQRDFSEAPKFTQPLADCTTVTGYNTQLFCCVRASPRPKIIWLKNKMDIQGNPKYRALTHLGICSLEIRKPGPFDGGIYTCKAVNPLGEASVDCRVDVKVPN
| null | null |
in utero embryonic development [GO:0001701]
|
myofilament [GO:0036379]; sarcomere [GO:0030017]
| null |
PF00041;PF07679;
|
2.60.40.10;
|
Immunoglobulin superfamily, MyBP family
| null |
SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere {ECO:0000305|PubMed:28778945}.
| null | null | null | null | null |
FUNCTION: Myosin-binding protein which plays a role in cardiac function (PubMed:28778945). Seems to regulate conduction in the atria and ventricular conduction systems (PubMed:28778945). {ECO:0000269|PubMed:28778945}.
|
Homo sapiens (Human)
|
A2RUV0
|
NOTC1_XENTR
|
MYRIGLLVLIWSLLGLAQGLRCTQTAEMCLNGGRCEMTPGGTGVCLCSSSYFGERCQYPNPCALKNQCMNFGTCEPVLLGNAIDFTCHCPVGFTDKVCLTPVDNACVNNPCRNGGTCELLSSVSDYRCRCPPGWTGDSCQQADPCASNPCANGGKCLPFETQYICKCPSGFHGATCKQDINECSQNPCRNGGQCLNEFGSYRCNCQNRFTGRNCEEPYVPCNPSPCLNGGTCRQTDDTSYECTCLPGFSGQNCEENIDDCPSNNCRNGGTCVDGVNTYNCQCPPDWTGQYCTEDVDECQLMPNACQNGGTCHNTYGGYNCVCVNGWTGEDCSENIDDCANAACHSGATCHDRVASFFCECPHGRTGLLCHLDNACISNPCNEGSNCDTNPVNGKAICTCPPGYTGPACNNDVDECSLGANPCEHGGRCTNTLGSFQCNCPQGYAGPRCEIDVNECLSNPCQNDATCLDQIGEFQCICMPGYEGLYCETNIDECASNPCLHNGKCVDKINEFHCECPTGFNGNLCQHDVDECASTPCKNGAKCLDGPNSYTCQCTEGFTGRHCEQDINECIPDPCHYGTCKDGIATFTCLCRPGYTGRLCDNDINECLSQPCQNGGQCTDRENGYICTCPKGTTGVNCETNLDDCASNPCDYGKCIDKIDGYECTCEPGYTGKMCNINIDECASNPCRNGGTCKDKINGFTCVCPDGYHDHMCLSEVNECNSNPCIHGTCHDGINGYKCDCDAGWSGSNCDVNNNECESNPCMNGGTCKDMTGAYICTCRAGFSGPNCQTNINECASNPCLNRGTCIDDVAGYKCNCMLPYTGAICEAVLAPCSGSPCKNGGRCKESEDYETFSCECPPGWQGQTCEIDMNECVNRPCRNGAMCQNTNGSYKCNCKPGYAGRHCETDIDDCQPNPCHNGGSCSDGINMFFCNCPAGFRGPKCEEDINECASNPCKNGANCTDCVNSYTCTCQPGFSGIHCENNTPDCTESSCFNGGTCIDGINTFSCQCPPGFTGNYCQHDINECDSKPCLNGGTCQDSYGAYKCTCPQGYTGLNCQNLVRWCDSSPCKNGGKCWQTNNFYRCECKSGWTGVYCDVPSVSCEVAAKQQGVDIAHLCRNSGMCVDTGNTHFCRCQAGYTGSYCEEQVDECSPNPCQNGATCTDYLGGYSCECVAGYHGVNCSEEINECLSHPCHNGGTCIDLINTYKCSCPRGTQGVHCEINVDDCTPFYDSVSLEPKCFNNGKCFDRVGGYNCICPPGFVGERCEGDVNECLSNPCDPRGTQNCIQLVNDYRCECRQGFTGRRCDSVVDGCKGLPCRNGGTCAVASNTERGFICKCPPGFDGATCEYDARTCGNLRCQNGGTCISVLKSSKCVCSEGYTGATCQYPVVSPCASRPCYNGGTCQFSPEEPFFQCFCPTNFNGLFCHILDYGFIGGLGKNITPPDNEEICENEQCAELADNKICNANCNNHACGWDGGDCSLNFNDPWKNCTQSLQCWKYFNDGKCDSQCNNSGCLYDGFDCQKVEVQCNPLYDQYCRDHFQDGHCDQGCNNAECEWDGLDCDNMPENLAEGTLLIVVLMPPEKLKNNSVNFLRELSRVLHTNVVFKKDSKGEYKIYPYYGNEEELKKHHIKKRSAASWSDAPTAIFSTMKESVLPGRRRRELDQMEVRGSIVYLEIDNRQCYKSSSQCFTSATDVAAFLGALATHGNLNIPYKIEAVKSEIVETAKPPPPLYAMFSMLVIPLLIIFVIMVVIVNKKRRREHGQLWFPEGFIPKEPSKKKRREPLGEDSVGLKPLKNLTDGSFMDDNQNEWGDEETLENKRFRFEEQVMLPELVDDQTDHRQWTQQHLDAADLRIPSMAPTPPQGEIDADCMDVNVRGPDGFTPLMIAACSGGGLETGNSEEEEDASANMISDFIGQGAQLHNQTDRTGETALHLAARYARADAAKRLLESSADANVPDNMGRTPLHAAVAADAQGVFQILIRNRATDLDARMCDGTTPLILAARLAVEGMVEELINAHADVNAVDEFGKSALHWAAAVNNVDAAAVLLKSSANKDMQNNKEETPLFLAAREGSYETAKVLLDHYANRDITDHMDRLPRDIAQERMHHDIVHLLDEHNLVKSPTLHGGPLGAPTLSPPICSPNGYMGNMKPSVQSKKARKPSIKGNGCKEAKELKARRKKSQDGKTSLLDSGSSGVLSPVDSLESPHGYLSDVASPPLMTSPFQQSPSMPLNHLTSMQDSHLGLNHMTMANKQEMASNRMAFDGMTPRLTHLNVSSPNTIMTNGSMHFTVGGAPAMNGQCDWFARLQNGMVQNQYNPIRNGIQQGNAQQALQHGLMSSLHNGLPATTLSQMMTYQAMPNTRMANQPHLMQAQQMQQQQNLQLHQSVQQQQHQNSNATSTHIGSPFCSNDISQTDLQQMSGNNIHSVMPQDTQIFTNSLPPTLTQSMATTQFLTPPSQHSYSSPMDNTPSHQLQVPDHPFLTPSPESPDQWSSSSPHSNMSDWSEGISSPPTSMQPQRTHIPEAFK
| null | null |
angiogenesis [GO:0001525]; cell differentiation [GO:0030154]; cilium assembly [GO:0060271]; Notch signaling involved in heart development [GO:0061314]; regulation of developmental process [GO:0050793]; regulation of DNA-templated transcription [GO:0006355]
|
nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
calcium ion binding [GO:0005509]; Notch binding [GO:0005112]; signaling receptor activity [GO:0038023]
|
PF12796;PF00008;PF07645;PF12661;PF06816;PF07684;PF00066;
|
3.30.300.320;3.30.70.3310;1.25.40.20;2.10.25.10;
|
NOTCH family
|
PTM: O-glycosylated on the EGF-like domains. Contains both O-linked fucose and O-linked glucose. O-linked glycosylation by galnt11 is involved in determination of left/right symmetry: glycosylation promotes activation of notch1, possibly by promoting cleavage by adam17, modulating the balance between motile and immotile (sensory) cilia at the left-right organiser (LRO). {ECO:0000269|PubMed:24226769}.; PTM: Synthesized in the endoplasmic reticulum as an inactive form which is proteolytically cleaved by a furin-like convertase in the trans-Golgi network before it reaches the plasma membrane to yield an active, ligand-accessible form. Cleavage results in a C-terminal fragment N(TM) and a N-terminal fragment N(EC). Following ligand binding, it is cleaved by adam17 to yield a membrane-associated intermediate fragment called notch extracellular truncation (NEXT). Following endocytosis, this fragment is then cleaved by presenilin dependent gamma-secretase to release a Notch-derived peptide containing the intracellular domain (NICD) from the membrane (By similarity). {ECO:0000250|UniProtKB:Q01705}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q01705}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q01705}.; SUBCELLULAR LOCATION: [Notch 1 intracellular domain]: Nucleus {ECO:0000250|UniProtKB:Q01705}. Note=Following proteolytical processing NICD is translocated to the nucleus. {ECO:0000250|UniProtKB:Q01705}.
| null | null | null | null | null |
FUNCTION: Functions as a receptor for membrane-bound ligands Jagged-1 (JAG1), Jagged-2 (JAG2) and Delta-1 (DLL1) to regulate cell-fate determination. Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus. Affects the implementation of differentiation, proliferation and apoptotic programs. Involved in angiogenesis; negatively regulates endothelial cell proliferation and migration and angiogenic sprouting. Involved in the maturation of both CD4(+) and CD8(+) cells in the thymus. Important for follicular differentiation and possibly cell fate selection within the follicle. During cerebellar development, functions as a receptor for neuronal DNER and is involved in the differentiation of Bergmann glia. Represses neuronal and myogenic differentiation. May play an essential role in postimplantation development, probably in some aspect of cell specification and/or differentiation. May be involved in mesoderm development, somite formation and neurogenesis (By similarity). Involved in determination of left/right symmetry by modulating the balance between motile and immotile (sensory) cilia at the left-right organiser (LRO). {ECO:0000250|UniProtKB:Q01705, ECO:0000269|PubMed:24226769}.
|
Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
|
A2RUV9
|
AEBP1_RAT
|
MAAVRTASLLCGLLALLALCPEGSPQTVLTDDEIQEFLEGFLSEFETQSPPREDDVEAQPLPEPTQRARKSKAGGKPRADAEAPPEKNKDKEKKGKKDKGPKAAKHLEGSTRPTKKPKEKPPKATKKPKEKPPKATKKPKEKPPKATKKPKEKPPKATKRPSAGKRFSTVAPLETPERSLTSPSNPGTRELPEERGRTSLNTWQGQGEETQVEARQHRPEPEEETEMPTLDYNDQIEREDYEDFEYIRRQKQPRPTPSRKRIWPEPPEEKTQEPEERKEVDPPLKPLLPPDYGDGYLIPNYDDLDYYFPHPPPQKPDVGQEVDEEKEELKKPKKEGSSPKEDTEDKWAAEKNKDHKAGPRKGEELEEEWGPVEKIKCPPIGMESHRIEDNQIRASSMLRHGLGAQRGRLNMQAGANEDDYYDGAWCAEDESQTQWIEVDTRRTTRFTGVITQGRDSSIHDDFVTTFFVGFSNDSQTWVMYTNGYEEMTFHGNVDKDTPVLSELPEPVVARFIRIYPLTWNGSLCMRLEVLGCPVTPVYSYYAQNEVVTTDSLDFRHHSYKDMRQLMKVVNEECPTITRTYSLGKSSRGLKIYAMEISDNPGEHELGEPEFRYTAGMHGNEVLGRELLLLLMQYLCHEYRDGNPRVRNLVQDTRIHLVPSLNPDGYEVAAQMGSEFGNWALGLWTEEGFDIFEDFPDLNSVLWAAEEKKWVPYRVPNNNLPIPERYLSPDATVSTEVRAIISWMEKNPFVLGANLNGGERLVSYPYDMARTPSQEQLLAAALAAARGEDEDEVSEAQETPDHAIFRWLAISFASAHLTMTEPYRGGCQAQDYTSGMGIVNGAKWNPRSGTFNDFSYLHTNCLELSIYLGCDKFPHESELPREWENNKEALLTFMEQVHRGIKGVVTDEQGIPIANATISVSGINHGVKTASGGDYWRILNPGEYRVTAHAEGYTSSAKICNVDYDIGATQCNFILARSNWKRIREILAMNGNRPILRVDPSRPMTPQQRRLQQRRLRYRLRMREQMRLRRLNSTTGPATSPTPALTLPPSPTPGSTSRLWEILPTTAAGWEESETETYTEVVTEFETEYGPDLEVEELEEEEEEEEEMDTGLTFPVTTVETYTVNFGDF
| null | null |
negative regulation of transcription by RNA polymerase II [GO:0000122]; peptide metabolic process [GO:0006518]; protein processing [GO:0016485]; regulation of collagen fibril organization [GO:1904026]; regulation of DNA-templated transcription [GO:0006355]
|
extracellular space [GO:0005615]
|
calmodulin binding [GO:0005516]; carboxypeptidase activity [GO:0004180]; collagen binding [GO:0005518]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; metallocarboxypeptidase activity [GO:0004181]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; zinc ion binding [GO:0008270]
|
PF13620;PF00754;PF00246;
|
2.60.40.1120;2.60.120.260;3.40.630.10;
|
Peptidase M14 family
|
PTM: Phosphorylated by MAPK1 in vitro. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q640N1}.
| null | null | null | null | null |
FUNCTION: As a positive regulator of collagen fibrillogenesis, it is probably involved in the organization and remodeling of the extracellular matrix (By similarity). May positively regulate MAP-kinase activity in adipocytes, leading to enhanced adipocyte proliferation and reduced adipocyte differentiation. May also positively regulate NF-kappa-B activity in macrophages by promoting the phosphorylation and subsequent degradation of I-kappa-B-alpha (NFKBIA), leading to enhanced macrophage inflammatory responsiveness. Can act as a transcriptional repressor. {ECO:0000250|UniProtKB:Q640N1, ECO:0000250|UniProtKB:Q8IUX7}.
|
Rattus norvegicus (Rat)
|
A2RUW1
|
TOLIP_RAT
|
MATTVSTQRGPVYIGELPQDFLRITPTQQQQQIQLDAQAAQQLQYGGAVGTVGRLSITVVQAKLAKNYGMTRMDPYCRLRLGYAVYETPTAHNGAKNPRWNKVIQCTVPPGVDSFYLEIFDERAFSMDDRIAWTHITIPESLKQGQVEDEWYSLSGRQGDDKEGMINLVMSYTSLPAAMMMPPQPVVLMPTVYQQGVGYVPIAGMPAVCSPGMVPMAMPPPAVAPQPRCNEEDLKAIQDMFPNMDREVIRSVLEAQRGNKDAAINSLLQMGEES
| null | null |
autophagy [GO:0006914]; epithelial cell differentiation [GO:0030855]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; interleukin-1-mediated signaling pathway [GO:0070498]; phosphorylation [GO:0016310]; positive regulation of protein sumoylation [GO:0033235]; protein localization to endosome [GO:0036010]; signal transduction [GO:0007165]; ubiquitin-dependent protein catabolic process [GO:0006511]
|
cytoplasm [GO:0005737]; early endosome [GO:0005769]; nuclear body [GO:0016604]; perinuclear region of cytoplasm [GO:0048471]; protein-containing complex [GO:0032991]
|
interleukin-1, type I receptor binding [GO:0005150]; kinase binding [GO:0019900]; molecular adaptor activity [GO:0060090]; SUMO binding [GO:0032183]; Toll-like receptor binding [GO:0035325]; ubiquitin binding [GO:0043130]; ubiquitin conjugating enzyme binding [GO:0031624]; ubiquitin protein ligase binding [GO:0031625]
|
PF00168;PF02845;
|
2.60.40.150;1.10.8.10;
|
Tollip family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9H0E2}. Endosome {ECO:0000250|UniProtKB:Q9H0E2}. Early endosome {ECO:0000250|UniProtKB:Q9H0E2}. Note=Localized to endo/exosomal vesicles. {ECO:0000250|UniProtKB:Q9H0E2}.
| null | null | null | null | null |
FUNCTION: Component of the signaling pathway of IL-1 and Toll-like receptors (By similarity). Inhibits cell activation by microbial products (By similarity). Recruits IRAK1 to the IL-1 receptor complex (By similarity). Inhibits IRAK1 phosphorylation and kinase activity. Connects the ubiquitin pathway to autophagy by functioning as a ubiquitin-ATG8 family adapter and thus mediating autophagic clearance of ubiquitin conjugates (By similarity). The TOLLIP-dependent selective autophagy pathway plays an important role in clearance of cytotoxic polyQ proteins aggregates (By similarity). In a complex with TOM1, recruits ubiquitin-conjugated proteins onto early endosomes (By similarity). Binds to phosphatidylinositol 3-phosphate (PtdIns(3)P) (By similarity). {ECO:0000250|UniProtKB:Q9H0E2}.
|
Rattus norvegicus (Rat)
|
A2RVJ8
|
HIT4_ARATH
|
MKKGAKRKGVSKAGRKAAVAETQNDEVIEETTKTTQEESQQHEEEVVDEVKENGEEEEAKGDQEEEEDAKPDSLEEDEENQEDEVKAEEVKEEVEKKPVARRGGKRKRATKKDTEIKDEKKPVPKAKKPRAAKVKEEPVYFEEKRSLEDLWKVAFPVGTEWDQLDALYEFNWDFQNLEEALEEGGKLYGKKVYVFGCTEPQLVPYKGANKIVHVPAVVVIESPFPPSDKIGITSVQREVEEIIPMKKMKMDWLPYIPIEKRDRQVDKMNSQIFTLGCTQRRSALRHMKEDQLKKFEYCLPYFYQPFKEDELEQSTEVQIMFPSEPPVVCEFDWEFDELQEFVDKLVEEEALPAEQADEFKEYVKEQVRAAKKANREAKDARKKAIEEMSEDTKQAFQKMKFYKFYPQPSPDTPDVSGVQSPFINRYYGKAHEVL
| null | null |
heat acclimation [GO:0010286]; negative regulation of gene expression, epigenetic [GO:0045814]; negative regulation of heterochromatin formation [GO:0031452]; regulation of cellular response to heat [GO:1900034]; response to heat [GO:0009408]
|
chromocenter [GO:0010369]; nucleolus [GO:0005730]
| null | null |
6.10.250.2770;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:23408827, ECO:0000269|PubMed:25329561}. Nucleus, nucleolus {ECO:0000269|PubMed:25329561}. Note=Localizes to the chromocentre at 23 degrees Celsius, a condensed heterochromatin domain that harbors repetitive elements for which transcription is normally suppressed by transcriptional gene silencing (TGS) (PubMed:23408827, PubMed:25329561). Relocates from the chromocenter to the nucleolus in response to heat (30 hours at 37 degrees Celsius or 30 minutes at 44 degrees Celsius), before heat-induced decondensation of chromocenters occurs (PubMed:25329561). {ECO:0000269|PubMed:23408827, ECO:0000269|PubMed:25329561}.
| null | null | null | null | null |
FUNCTION: Essential protein required for basal thermotolerance, especially during heat-induced chromocentre decondensation, thus regulating transcriptional gene silencing (TGS). {ECO:0000269|PubMed:23408827, ECO:0000269|PubMed:25329561}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
A2RVK7
|
RP41L_ARATH
|
MAAKPGAATPTYSPKIVGRSRLPIFKDSDLDWSRPDGRGFHQCRPALLQTGAVSSASGSAYAEFGNTKVIVSVFGPRESKKAMVYSDVGRLNCNVSYTNFASPTLGQGTDHKEYSSMLHKALEGVIMMETFPKTTVDVFALVLESGGSDLSVLISCASLALADAGIMMYDLITAVSVSCIGKSLMIDPVTEEEGCEDGSFMMTCMPSRYEITQLTITGEWTTPNINEAMQLCLDASSKLGEIMRDCLKQSASASDE
| null | null |
nuclear mRNA surveillance [GO:0071028]; nuclear-transcribed mRNA catabolic process, exonucleolytic, 3'-5' [GO:0034427]; polyadenylation-dependent snoRNA 3'-end processing [GO:0071051]; rRNA catabolic process [GO:0016075]; rRNA processing [GO:0006364]; seed germination [GO:0009845]; seedling development [GO:0090351]; U4 snRNA 3'-end processing [GO:0034475]
|
cytoplasm [GO:0005737]; cytoplasmic exosome (RNase complex) [GO:0000177]; nuclear exosome (RNase complex) [GO:0000176]; nucleolus [GO:0005730]; nucleus [GO:0005634]
|
3'-5' exonuclease activity [GO:0008408]; RNA binding [GO:0003723]
|
PF01138;PF03725;
|
3.30.230.70;
|
RNase PH family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23132787}. Nucleus {ECO:0000269|PubMed:23132787}.
| null | null | null | null | null |
FUNCTION: Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing, maturation and degradation events. In vitro, is a processive phosphorolytic exonuclease and requires a single-stranded poly(A) tail on the substrate RNA for its activity (By similarity). Plays an important role in seed germination and early seedling growth by mediating specific cytoplasmic mRNA decay of transcripts coding for the abscisic acid (ABA) biosynthetic enzymes NCED5 and NCED6, and the ABA signaling transcription factors ABI3 and ABI4 (PubMed:23132787). {ECO:0000250|UniProtKB:Q9SP08, ECO:0000269|PubMed:23132787}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
A2RVM0
|
TIC32_ARATH
|
MWFFGSKGASGFSSRSTAEEVTHGVDGTGLTAIVTGASSGIGVETARVLSLRGVHVVMAVRNTDSGAKVKEDIVKQVPGAKLDVMELDLSSMQSVRKFASEYKSTGLPLNLLINNAGIMACPFMLSKDNIELQFATNHLGHFLLTKLLLDTMKSTSRESKREGRIVNLSSEAHRFSYPEGVRFDKINDKSSYSSMRAYGQSKLCNVLHANELTKQLKEDGVNITANSLHPGAIMTNLGRYFNPYLAVAVGAVAKYILKSVPQGAATTCYVALNPQVAGVSGEYFQDSNIAKPLPLVKDTELAKKVWDFSTKLTDSQSGESSS
|
1.1.1.-
| null |
protein transport [GO:0015031]
|
chloroplast [GO:0009507]; chloroplast envelope [GO:0009941]; chloroplast inner membrane [GO:0009706]; cytosol [GO:0005829]; plasma membrane [GO:0005886]
|
oxidoreductase activity [GO:0016491]
|
PF00106;
|
3.40.50.720;
|
Short-chain dehydrogenases/reductases (SDR) family
| null |
SUBCELLULAR LOCATION: Plastid, chloroplast inner membrane {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Involved in protein precursor import into chloroplasts. Part of the redox regulon consisting of TIC32, TIC 55 and TIC62. {ECO:0000269|PubMed:15180984}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
A2RVQ5
|
AGL16_ARATH
|
MGRGKIAIKRINNSTSRQVTFSKRRNGLLKKAKELAILCDAEVGVIIFSSTGRLYDFSSSSMKSVIERYSDAKGETSSENDPASEIQFWQKEAAILKRQLHNLQENHRQMMGEELSGLSVEALQNLENQLELSLRGVRMKKDQMLIEEIQVLNREGNLVHQENLDLHKKVNLMHQQNMELHEKVSEVEGVKIANKNSLLTNGLDMRDTSNEHVHLQLSQPQHDHETHSKAIQLNYFSFIA
| null | null |
flower development [GO:0009908]; positive regulation of transcription by RNA polymerase II [GO:0045944]; stomatal lineage progression [GO:0010440]
|
nucleus [GO:0005634]
|
DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; protein homodimerization activity [GO:0042803]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; transcription cis-regulatory region binding [GO:0000976]
|
PF01486;PF00319;
|
3.40.1810.10;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251}.
| null | null | null | null | null |
FUNCTION: Probable transcription factor involved in the regulation of flowering time in long-day photoperiod. Participates in the repression of FT expression and floral transition, by interacting closely with the FLC-SVP pathways (PubMed:24876250). Functions in the satellite meristemoid lineage of stomatal development (PubMed:17704216). {ECO:0000269|PubMed:17704216, ECO:0000269|PubMed:24876250}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
A2RVU1
|
MWL1_ARATH
|
MFIFLFGLAAFFLCLSAEFQKAKALLRAQVFLKGKDLKWDGESCYLPENRAFGLGIAALVCVSVAQIVGNVVICRGFTKTDKTRTTIFCIILLLFSWVNFAVAVTLISVGASMNREQIYGKGWLNRECYLVKDGVFAASGFLSVTTMAAILGAFAFKVKPSLQVENHDKRHTQNV
| null | null |
lignin biosynthetic process [GO:0009809]; lignin metabolic process [GO:0009808]
|
membrane [GO:0016020]; plasma membrane [GO:0005886]
| null |
PF06749;
| null |
DESIGUAL family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26930070}; Multi-pass membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Together with MWL2, contributes to secondary cell wall biology, specifically lignin biosynthesis. {ECO:0000269|PubMed:26930070}.
|
Arabidopsis thaliana (Mouse-ear cress)
|
A2SW69
|
ANXA2_SHEEP
|
MSTVHEILCKLSLEGDHSTPPSAYGSVKAYTNFDAERDALNIETAIKTKGVDEVTIVNILTNRSNEQRQDIAFAYQRRTKKELASALKSALSGHLETVILGLLKTPAQYDASELKASMKGLGTDEDSLIEIICSRTNQELQEINRVYKEMYKTDLEKDIVSDTSGDFRKLMVALAKGRRAEDGSVIDYELIDQDARDLYDAGVKRKGTDVPKWISIMTERSVCHLQKVFERYKSYSPYDMLESIKKEVKGDLENAFLNLVQCIQNKPLYFADRLYDSMKGKGTRDKVLIRIMVSRSEVDMLKIRSEFKKKYGKSLYYYIQQDTKGDYQKALLYLCGGDD
| null | null | null |
basement membrane [GO:0005604]; cytoplasm [GO:0005737]; endosome [GO:0005768]; extracellular space [GO:0005615]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
cadherin binding involved in cell-cell adhesion [GO:0098641]; calcium channel activity [GO:0005262]; calcium ion binding [GO:0005509]; calcium-dependent phospholipid binding [GO:0005544]; cytoskeletal protein binding [GO:0008092]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; phosphatidylserine binding [GO:0001786]; phospholipase A2 inhibitor activity [GO:0019834]; protease binding [GO:0002020]; virion binding [GO:0046790]
|
PF00191;
|
1.10.220.10;
|
Annexin family
|
PTM: ISGylated. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane. Note=In the lamina beneath the plasma membrane. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Calcium-regulated membrane-binding protein whose affinity for calcium is greatly enhanced by anionic phospholipids. It binds two calcium ions with high affinity. May be involved in heat-stress response. Inhibits PCSK9-enhanced LDLR degradation, probably reduces PCSK9 protein levels via a translational mechanism but also competes with LDLR for binding with PCSK9. {ECO:0000250|UniProtKB:P07355}.
|
Ovis aries (Sheep)
|
A2SWM2
|
SPNS2_DANRE
|
MCVESDGCEIEGCSSSDEVHTLSGSMSPALKSRDLHHCRPGQKFHAALLRCRTPLVAAGILSFGNVLNYMDRYTVAGVLLDIQKQFKVGDSSAGLLQTVFICSFMVAAPIFGYLGDRFNRKIILSCGIFFWSAVTLLSSFITKEYYWLLVLSRCLVGIGESSYSSISPTIIGDLFTNNKRTVMLSVFYLAIPLGSGLGYILGSIAKDAGGHWYWALRVSPMLGLTAGTLILIFVSEPKRGSADQPGGRLKTRTSWVCDMKALAKNRSYVFSSLASAAVSFATGAFGIWIPQYLVRAQVVQKSAESCTYQPCSSRDSLIFGAITCVTGLLGVVIGAVTTRLCRQKTERADPLVCAVSMLGSAIFICLIFVVAKKSIVGAYICIFIGETLLFLNWAITADILMYVVIPTRRATAVAFQGFTSHLLGDAGSPYLIGLISDSLQESYATSEIWQFLSLGYALMLCPFVIVLGGMFFLATALFFLDDRDKAAKQVNQLARPPSTVKVTK
| null | null |
branching involved in blood vessel morphogenesis [GO:0001569]; cardioblast migration to the midline involved in heart rudiment formation [GO:0003319]; embryonic heart tube morphogenesis [GO:0003143]; embryonic viscerocranium morphogenesis [GO:0048703]; lipid transport [GO:0006869]; regulation of cartilage development [GO:0061035]; regulation of humoral immune response [GO:0002920]; regulation of T cell migration [GO:2000404]; sensory perception of sound [GO:0007605]; sphingosine-1-phosphate receptor signaling pathway [GO:0003376]; vasculature development [GO:0001944]
|
endosome membrane [GO:0010008]; membrane [GO:0016020]; plasma membrane [GO:0005886]
|
sphingolipid transporter activity [GO:0046624]; transmembrane transporter activity [GO:0022857]
|
PF07690;
|
1.20.1250.20;
|
Major facilitator superfamily, Spinster (TC 2.A.1.49) family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19074308}; Multi-pass membrane protein {ECO:0000255}. Endosome membrane {ECO:0000269|PubMed:19074308}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=sphing-4-enine 1-phosphate(in) = sphing-4-enine 1-phosphate(out); Xref=Rhea:RHEA:38667, ChEBI:CHEBI:60119; Evidence={ECO:0000250|UniProtKB:Q8IVW8}; CATALYTIC ACTIVITY: Reaction=sphinganine 1-phosphate(in) = sphinganine 1-phosphate(out); Xref=Rhea:RHEA:38671, ChEBI:CHEBI:57939; Evidence={ECO:0000269|PubMed:19074308};
| null | null | null | null |
FUNCTION: Lipid transporter that specifically mediates export of sphingosine-1-phosphate (sphing-4-enine 1-phosphate, S1P) and sphinganine-1-phosphate, which play critical roles in regulating heart development (PubMed:19062281, PubMed:19074308). Mediates the export of S1P from cells in the extraembryonic yolk syncytial layer (YSL), thereby regulating myocardial precursor migration (PubMed:19062281, PubMed:19074308). {ECO:0000269|PubMed:19062281, ECO:0000269|PubMed:19074308}.
|
Danio rerio (Zebrafish) (Brachydanio rerio)
|
A2SZS3
|
L_RVFV
|
MDSILSKQLVDKTGFVRVPIKHFDCTMLTLALPTFDVSKMVDRITIDFNLDDIQGASEIGSTLLPSMSIDVEDMANFVHDFTFGHLADKTDRLLMREFPMMNDGFDHLSPDMIIKTTSGMYNIVEFTTFRGDERGAFQAAMTKLAKYEVPCENRSQGRTVVLYVVSAYRHGVWSNLELEDSEAEEMVYRYRLALSVMDELRTLFPELSSTDEELGKTERELLAMVSSIQINWSVTESVFPPFSREMFDRFRSSPPDSEYITRIVSRCLINSQEKLINSSFFAEGNDKALRFSKNAEECSLAVERALNQYRAEDNLRDLNDHKSTIQLPPWLSYHDVDGKDLCPLQGLDVRGDHPMCNLWREVVTSANLEEIERMHDDAAAELEFALSGVKDRPDERNRYHRVHLNMGSDDSVYIAALGVNGKKHKADTLVQQMRDRSKQPFSPDHDVDHISEFLSACSSDLWATDEDLYNPLSCDKELRLAAQRIHQPSLSERGFNEIITEHYKFMGSRIGSWCQMVSLIGAELSASVKQHVKPNYFVIKRLLGSGIFLLIKPTSSKSHIFVSFAIKRSCWAFDLSTSRVFKPYIDAGDLLVTDFVSYKLSKLTNLCKCVSLMESSFSFWAEAFGIPSWNFVGDLFRSSDSAAMDASYMGKLSLLTLLEDKAATEELQTIARYIIMEGFVSPPEIPKPHKMTSKFPKVLRSELQVYLLNCLCRTIQRIAGEPFILKKKDGSISWGGMFNPFSGRPLLDMQPLISCCYNGYFKNKEEETEPSSLSGMYKKIIELEHLRPQSDAFLGYKDPELPRMHEFSVSYLKEACNHAKLVLRSLYGQNFMEQIDNQIIRELSGLTLERLATLKATSNFNENWYVYKDVADKNYTRDKLLVKMSKYASEGKSLAIQKFEDCMRQIESQGCMHICLFKKQQHGGLREIYVMGAEERIVQSVVETIARSIGKFFASDTLCNPPNKVKIPETHGIRARKQCKGPVWTCATSDDARKWNQGHFVTKFALMLCEFTSPKWWPLIIRGCSMFTRKRMMMNLNYLKILDGHRELDIRDDFVMDLFKAYHGEAEVPWAFKGKTYLETTTGMMQGILHYTSSLLHTIHQEYIRSLSFKIFNLKVAPEMSKGLVCDMMQGSDDSSMLISFPADDEKVLTRCKVAAAICFRMKKELGVYLAIYPSEKSTANTDFVMEYNSEFYFHTQHVRPTIRWIAACCSLPEVETLVARQEEASNLMTSVTEGGGSFSLAAMIQQAQCTLHYMLMGMGVSELFLEYKKAVLKWNDPGLGFFLLDNPYACGLGGFRFNLFKAITRTDLQKLYAFFMKKVKGSAARDWADEDVTIPETCSVSPGGALILSSSLKWGSRKKFQKLRDRLNIPENWIELINENPEVLYRAPRTGPEILLRIAEKVHSPGVVSSLSSGNAVCKVMASAVYFLSATIFEDTGRPEFNFLEDSKYSLLQKMAAYSGFHGFNDMEPEDILFLFPNIEELESLDSIVYNKGEIDIIPRVNIRDATQTRVTIFNEQKTLRTSPEKLVSDKWFGTQKSRIGKTTFLAEWEKLKKIVKWLEDTPEATLAHTPLNNHIQVRNFFARMESKPRTVRITGAPVKKRSGVSKIAMVIRDNFSRMGHLRGVEDLAGFTRSVSAEILKHFLFCILQGPYSESYKLQLIYRVLSSVSNVEIKESDGKTKTNLIGILQRFLDGDHVVPIIEEMGAGTVGGFIKRQQSKVVQNKVVYYGVGIWRGFMDGYQVHLEIENDIGQPPRLRNVTTNCQSSPWDLSIPIRQWAEDMGVTNNQDYSSKSSRGARYWMHSFRMQGPSKPFGCPVYIIKGDMSDVIRLRKEEVEMKVRGSTLNLYTKHHSHQDLHILSYTASDNDLSPGIFKSISDEGVAQALQLFEREPSNCWVRCESVAPKFISAILEICEGKRQIRGINRTRLSEIVRICSESSLRSKVGSMFSFVANVEEAHDVDYDALMDLMIEDAKNNAFSHVVDCIELDVSGPYEMESFDTSDVNLFGPAHYKDISSLSMIAHPLMDKFVDYAISKMGRASVRKVLETGRCSSKDYDLSKVLFRTLQRPEESIRIDDLELYEETDVADDMLG
|
2.7.7.48; 3.1.-.-
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:A5HC98}; Note=For endonuclease activity. Binds 2 Mn(2+) ions in the active site (By similarity). The divalent metal ions are crucial for catalytic activity (PubMed:31948728). {ECO:0000250|UniProtKB:A5HC98, ECO:0000269|PubMed:31948728}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:I0DF35}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:I0DF35}; Note=For polymerase activity. Initiation activity is stronger in the presence of Mn(2+) than in the presence of Mg(2+). {ECO:0000250|UniProtKB:I0DF35};
|
DNA-templated transcription [GO:0006351]; viral RNA genome replication [GO:0039694]
|
host cell endoplasmic reticulum [GO:0044165]; host cell endoplasmic reticulum-Golgi intermediate compartment [GO:0044172]; host cell Golgi apparatus [GO:0044177]; virion component [GO:0044423]
|
hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]; nucleoside binding [GO:0001882]; RNA-dependent RNA polymerase activity [GO:0003968]
|
PF04196;PF12603;PF15518;
| null |
Bunyavirales RNA polymerase family
| null |
SUBCELLULAR LOCATION: Host Golgi apparatus {ECO:0000250|UniProtKB:I0DF35}. Host endoplasmic reticulum {ECO:0000250|UniProtKB:I0DF35}. Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250|UniProtKB:I0DF35}. Virion {ECO:0000250|UniProtKB:P20470}.
|
CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539};
| null | null | null | null |
FUNCTION: RNA-dependent RNA polymerase, which is responsible for the replication and transcription of the viral RNA genome using antigenomic RNA as an intermediate (Probable). During transcription, synthesizes subgenomic RNAs and assures their capping by a cap-snatching mechanism, which involves the endonuclease activity cleaving the host capped pre-mRNAs (By similarity). These short capped RNAs are then used as primers for viral transcription. The 3'-end of subgenomic mRNAs molecules are not polyadenylated. During replication, the polymerase binds the 5' and 3' vRNA extremities at distinct sites (By similarity). In turn, significant conformational changes occur in the polymerase and in vRNA to initiate active RNA synthesis (By similarity). As a consequence of the use of the same enzyme for both transcription and replication, these mechanisms need to be well coordinated (By similarity). {ECO:0000250|UniProtKB:A5HC98, ECO:0000250|UniProtKB:I0DF35, ECO:0000305}.
|
Rift valley fever virus (RVFV)
|
A2T1U1
|
ORANG_BRAOB
|
MSCLGRILSVSYPPDPYGSRLSVSKLSSPGRNRRLRWRFTALDSDSSSLDSDSSDKFAAGFCIIEGPETVQDFAKMQLQEIQDNIRSRRNKIFLHMEEVRRLRIQQRIRNTELGIIDEEQEHELPNFPSFIPFLPPLTAANLRVYYATCFSLIAGIILFGGLLAPTLELKLGIGGTSYKDFIQSLHLPMQLSQVDPIVASFSGGAVGVISALMVVEVNNVKQQEHKRCKYCLGTGYLACARCSSTGSLIISEPVSAIAGGNHSVSTSKTERCSNCSGAGKVMCPTCLCTGMAMASEHDPRIDPFL
| null | null |
chromoplast organization [GO:0009661]; positive regulation of carotenoid biosynthetic process [GO:1904143]; unidimensional cell growth [GO:0009826]
|
chloroplast membrane [GO:0031969]; nucleus [GO:0005634]
| null | null | null |
Orange-like family
| null |
SUBCELLULAR LOCATION: Plastid, chloroplast membrane {ECO:0000305}. Plastid {ECO:0000269|PubMed:17172359}. Nucleus {ECO:0000269|PubMed:21175633}. Note=Targeted to non-green plastids. {ECO:0000269|PubMed:17172359}.
| null | null | null | null | null |
FUNCTION: Involved in chromoplast differentiation. Is associated with a cellular process that triggers the differentiation of pro-plastids or other non-colored plastids into chromoplasts for carotenoid accumulation (PubMed:17172359, PubMed:18256051). Associated with carotenoid accumulation in de-etiolated cotyledons (PubMed:23887833). Controls leaf petiole elongation by suppressing the expression of ERF1 genes (PubMed:21175633). {ECO:0000269|PubMed:17172359, ECO:0000269|PubMed:18256051, ECO:0000269|PubMed:21175633, ECO:0000269|PubMed:23887833}.
|
Brassica oleracea var. botrytis (Cauliflower)
|
A2T2X4
|
IFT46_CHLRE
|
MDDSMDYPDRDGDDLDQFQGTARSQVVQNQPHDEEVNLSESESFAGADEPPAAPRDASLIESHDMDEGPAAPARTLSPTGYEAGKHAPGGIANSDEAPPGAYNAQEYKHLNVGEDVRELFSYIGRYKPQTVELDTRIKPFIPDYIPAVGGIDEFIKVPRPDTKPDYLGLKVLDEPAAKQSDPTVLTLQLRQLSKEAPGAKADMVGRLEHTDENKAKKIQQWIASINDIHKAKPAATVNYSKRMPEIEALMQEWPPEVETFLKTMHMPSGDVELDIKTYARLVCTLLDIPVYDDPVESLHVLFTLYLEFKNNPIFRQHMEMENKLDGMSGGGGGMMGGGADVLGL
| null | null |
axoneme assembly [GO:0035082]; cilium assembly [GO:0060271]; cilium organization [GO:0044782]; cilium-dependent cell motility [GO:0060285]; intraciliary transport [GO:0042073]; outer dynein arm assembly [GO:0036158]; protein stabilization [GO:0050821]; protein transport [GO:0015031]; regulation of cilium assembly [GO:1902017]; regulation of protein stability [GO:0031647]
|
ciliary base [GO:0097546]; ciliary membrane [GO:0060170]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; intraciliary transport particle B [GO:0030992]; motile cilium [GO:0031514]
| null |
PF12317;
| null |
IFT46 family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:15955805, ECO:0000269|PubMed:17312020, ECO:0000269|PubMed:18852297, ECO:0000269|PubMed:19382199, ECO:0000269|PubMed:19412537}. Cell projection, cilium {ECO:0000269|PubMed:15955805, ECO:0000269|PubMed:17312020, ECO:0000269|PubMed:18852297, ECO:0000269|PubMed:19382199, ECO:0000269|PubMed:19412537}. Note=Expression is concentrated at the cilium basal body but is also detected along the length of the cilium. {ECO:0000269|PubMed:15955805, ECO:0000269|PubMed:17312020, ECO:0000269|PubMed:18852297, ECO:0000269|PubMed:19382199, ECO:0000269|PubMed:19412537}.
| null | null | null | null | null |
FUNCTION: Forms part of a complex involved in intraflagellar transport (IFT), the bi-directional movement of particles required for the assembly, maintenance and functioning of primary cilia. Plays a role in maintaining IFT complex B stability. {ECO:0000269|PubMed:17312020, ECO:0000269|PubMed:20435895}.
|
Chlamydomonas reinhardtii (Chlamydomonas smithii)
|
A2T3P0
|
NSP2_ROTSH
|
MAELACFCYPHLENDSYKFIPFNNLAIKAMLTAKVDKKDMDKFYDSIIYGIAPPPQFKKRYNTNDNSRGMNFETIMFTKVAMLICEALNSLKVTQANVSNVLSRVVSIRHLENLVIRKENPQDILFHSKDLLLKSTLIAIGQSKEIETTITAEGGEIVFQNAAFTMWKLTYLEHQLMPILDQNFIEYKVTLNEDKPISDVHVKELVAELRWQYNKFAVITHGKGHYRIVKYSSVANHADRVYATFKSNVKTGVNNDFNLLDQRIIWQNWYAFTSSMKQGNTLDVCKRLLFQKMKPEKNPFKGLSTDRKMDEVSQVGV
|
3.6.4.-
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_04089};
|
viral genome replication [GO:0019079]
|
host cell cytoplasm [GO:0030430]
|
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; nucleoside diphosphate kinase activity [GO:0004550]; ribonucleoside triphosphate phosphatase activity [GO:0017111]; RNA binding [GO:0003723]
|
PF02509;PF21067;
|
3.30.428.20;3.90.1400.10;
|
Rotavirus NSP2 family
| null |
SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04089}. Note=Found in spherical cytoplasmic structures, called viral factories, that appear early after infection and are the site of viral replication and packaging. {ECO:0000255|HAMAP-Rule:MF_04089}.
| null | null | null | null | null |
FUNCTION: Participates in replication and packaging of the viral genome. Plays a crucial role, together with NSP5, in the formation of virus factories (viroplasms), which are large inclusions in the host cytoplasm where replication intermediates are assembled and viral RNA replication takes place. Displays ssRNA binding, NTPase, RNA triphosphatase (RTPase) and ATP-independent helix-unwinding activities. The unwinding activity may prepare and organize plus-strand RNAs for packaging and replication by removing interfering secondary structures. The RTPase activity plays a role in the removal of the gamma-phosphate from the rotavirus RNA minus strands of dsRNA genome segments (PubMed:14699117). Participates in the selective exclusion of host proteins from stress granules (SG) and P bodies (PB). Participates also in the sequestration of these remodeled organelles in viral factories (By similarity). {ECO:0000255|HAMAP-Rule:MF_04089, ECO:0000269|PubMed:14699117}.
|
Rotavirus A (isolate RVA/Monkey/South Africa/SA11-H96/1958/G3P5B[2]) (RV-A) (Simian Agent 11 (isolate SI/South Africa/H96/58))
|
A2T3P5
|
VP7_ROTSH
|
MYGIEYTTVLTFLISIILLNYILKSLTRIMDFIIYRFLFIIVILSPFLRAQNYGINLPITGSMDTAYANSTQEETFLTSTLCLYYPTEAATEINDNSWKDTLSQLFLTKGWPTGSVYFKEYTNIASFSVDPQLYCDYNVVLMKYDATLQLDMSELADLILNEWLCNPMDITLYYYQQTDEANKWISMGSSCTIKVCPLNTQTLGIGCLTTDATTFEEVATAEKLVITDVVDGVNHKLDVTTATCTIRNCKKLGPRENVAVIQVGGSDILDITADPTTAPQTERMMRINWKKWWQVFYTVVDYVDQIIQVMSKRSRSLNSAAFYYRV
| null | null |
receptor-mediated virion attachment to host cell [GO:0046813]
|
host cell endoplasmic reticulum lumen [GO:0044166]; T=13 icosahedral viral capsid [GO:0039621]; viral outer capsid [GO:0039624]
|
metal ion binding [GO:0046872]
|
PF00434;
|
3.40.50.11130;2.60.120.800;
|
Rotavirus VP7 family
|
PTM: N-glycosylated. {ECO:0000255|HAMAP-Rule:MF_04131}.; PTM: The N-terminus is blocked possibly by pyroglutamic acid. {ECO:0000255|HAMAP-Rule:MF_04131}.
|
SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04131, ECO:0000269|PubMed:1649333, ECO:0000269|PubMed:19036817}. Host endoplasmic reticulum lumen {ECO:0000255|HAMAP-Rule:MF_04131}. Note=The outer layer contains 780 copies of VP7, grouped as 260 trimers. Immature double-layered particles assembled in the cytoplasm bud across the membrane of the endoplasmic reticulum, acquiring during this process a transient lipid membrane that is modified with the ER resident viral glycoproteins NSP4 and VP7; these enveloped particles also contain VP4. As the particles move towards the interior of the ER cisternae, the transient lipid membrane and the non-structural protein NSP4 are lost, while the virus surface proteins VP4 and VP7 rearrange to form the outermost virus protein layer, yielding mature infectious triple-layered particles. {ECO:0000255|HAMAP-Rule:MF_04131}.
| null | null | null | null | null |
FUNCTION: Calcium-binding protein that interacts with rotavirus cell receptors once the initial attachment by VP4 has been achieved. Rotavirus attachment and entry into the host cell probably involves multiple sequential contacts between the outer capsid proteins VP4 and VP7, and the cell receptors (PubMed:10590110, PubMed:9144247). Following entry into the host cell, low intracellular or intravesicular Ca(2+) concentration probably causes the calcium-stabilized VP7 trimers to dissociate from the virion. This step is probably necessary for the membrane-disrupting entry step and the release of VP4, which is locked onto the virion by VP7 (By similarity). {ECO:0000255|HAMAP-Rule:MF_04131, ECO:0000269|PubMed:10590110, ECO:0000269|PubMed:9144247, ECO:0000303|PubMed:15165605}.
|
Rotavirus A (isolate RVA/Monkey/South Africa/SA11-H96/1958/G3P5B[2]) (RV-A) (Simian Agent 11 (isolate SI/South Africa/H96/58))
|
A2T3Q9
|
NSP5_ROTSH
|
MSLSIDVTSLPSIPSTIYKNESSSTTSTLSGKSIGRSEQYISPDAEAFNKYMLSKSPEDIGPSDSASNDPLTSFSIRSNAVKTNADAGVSMDSSAQSRPSSNVGCDQVDFSLNKGLKVKANLDSSISISTDTKKEKSKQNHKSRKHYPRIEAESDSDDYVLDDSDSDDGKCKNCKYKKKYFALRMRMKQVAMQLIEDL
| null |
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_04092};
|
viral genome replication [GO:0019079]
|
host cell cytoplasm [GO:0030430]
|
ATP hydrolysis activity [GO:0016887]; magnesium ion binding [GO:0000287]; nucleotide binding [GO:0000166]; RNA binding [GO:0003723]
|
PF01525;
| null |
Rotavirus NSP5 family
|
PTM: O-glycosylated. {ECO:0000255|HAMAP-Rule:MF_04092}.; PTM: Hyperphosphorylated on serine residues, when in dimeric form. Phosphorylation by host CK1 is required for the hyperphosphorylation of NSP5 dimer. {ECO:0000255|HAMAP-Rule:MF_04092, ECO:0000269|PubMed:11884570, ECO:0000269|PubMed:15520389, ECO:0000269|PubMed:17872534, ECO:0000269|PubMed:8811003}.
|
SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04092, ECO:0000269|PubMed:11884570, ECO:0000269|PubMed:14993647, ECO:0000269|PubMed:17182692}. Note=Found in spherical cytoplasmic structures, called virus factories, that appear early after infection and are the site of viral replication and packaging. {ECO:0000255|HAMAP-Rule:MF_04092}.
| null | null | null | null | null |
FUNCTION: Plays an essential role in the viral genome replication. Participates, together with NSP2, in the formation of viral factories (viroplasms), which are large inclusions in the host cytoplasm where replication intermediates are assembled and viral RNA replication takes place. Orchestrates the recruitment of viroplasmic proteins such as capsid proteins to these factories (PubMed:11884570, PubMed:17825341). Participates in the selective exclusion of host proteins from stress granules (SG) and P bodies (PB). Participates also in the sequestration of these remodeled organelles in viral factories (By similarity). {ECO:0000255|HAMAP-Rule:MF_04092, ECO:0000269|PubMed:11884570, ECO:0000269|PubMed:17825341}.
|
Rotavirus A (isolate RVA/Monkey/South Africa/SA11-H96/1958/G3P5B[2]) (RV-A) (Simian Agent 11 (isolate SI/South Africa/H96/58))
|
A2T3S5
|
VP3_ROTSH
|
MKVLALRHSVAQVYADTQVYVHDDTKDSYENAFLISNLTTHNILYLNYSIKTLEILNKSGIAAIALQSLEELFTLIRCNFTYDYELDIIYLHDYSYYTNNEIRTDQHWITKTNIEEYLLPGWKLTYVGYNGSETRGHYNFSFKCQNAATDDDLIIEYIYSEALDFQNFMLKKIKERMTTSLPIARLSNRVFRDKLFPSLLKEHKNVVNVGPRNESMFTFLNYPTIKQFSNGAYLVKDTIKLKQERWLGKRISQFDIGQYKNMLNVLTAIYYYYNLYKSKPIIYMIGSAPSYWIYDVRHYSDFFFETWDPLDTPYSSIHHKELFFINDVKKLKDNSILYIDIRTDRGNADWKKWRKTVEEQTINNLDIAYEYLRTGKAKVCCVKMTAMDLELPISAKLLHHPTTEIRSEFYLLLDTWDLTNIRRFIPKGVLYSFINNIITENVFIQQPFKVKVLNDSYIVALYALSNDFNNRSEVIKLINNQKQSLITVRINNTFKDEPKVGFKNIYDWTFLPTDFDTKEAIITSYDGCLGLFGLSISLASKPTGNNHLFILSGTDKYYKLDQFANHTSISRRSHQIRFSESATSYSGYIFRDLSNNNFNLIGTNIENSVSGHVYNALIYYRYNYSFDLKRWIYLHSIDKVDIEGGKYYELAPIELIYACRSAKEFATLQDDLTVLRYSNEIENYINTVYSITYADDPNYFIGIQFRNIPYKYDVKIPHLTFGVLHISDNMVPDVIDILKIMKNELFKMDITTSYTYMLSDGIYVANVSGVLSTYFKIYNVFYKNQITFGQSRMFIPHITLSFNNMRTVRIETTKLQIKSIYLRKIKGDTVFDMVE
|
2.1.1.56; 2.7.7.50; 3.1.4.-
| null |
RNA 5'-cap (guanine-N7)-methylation [GO:0106005]; virus-mediated perturbation of host defense response [GO:0019049]
|
viral nucleocapsid [GO:0019013]
|
GTP binding [GO:0005525]; mRNA 5'-cap (guanine-N7-)-methyltransferase activity [GO:0004482]; mRNA guanylyltransferase activity [GO:0004484]; phosphoric diester hydrolase activity [GO:0008081]; RNA binding [GO:0003723]
|
PF05213;PF06929;
| null |
Rotavirus VP3 family
| null |
SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04128}. Note=Attached inside the inner capsid as a minor component. There are about 11 to 12 copies per virion. {ECO:0000255|HAMAP-Rule:MF_04128}.
|
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:0000255|HAMAP-Rule:MF_04128, ECO:0000269|PubMed:10603323}; CATALYTIC ACTIVITY: Reaction=a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:67008, Rhea:RHEA-COMP:17166, Rhea:RHEA-COMP:17167, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:156461, ChEBI:CHEBI:167617; EC=2.1.1.56; Evidence={ECO:0000255|HAMAP-Rule:MF_04128, ECO:0000269|PubMed:10603323}; CATALYTIC ACTIVITY: Reaction=5'-triphosphoadenylyl-(2'->5')-adenylyl-(2'->5')-adenosine + 2 H2O = 2 AMP + ATP + 2 H(+); Xref=Rhea:RHEA:45964, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:67143, ChEBI:CHEBI:456215; Evidence={ECO:0000255|HAMAP-Rule:MF_04128, ECO:0000269|PubMed:23878220};
| null | null | null | null |
FUNCTION: Multifunctional enzyme involved in mRNA capping. Catalyzes the formation of the 5' cap structure on the viral plus-strand transcripts. Specifically binds to GTP and displays guanylyltransferase and methyltransferase activities. Has affinity for ssRNA but not for dsRNA. Capping activity is non-specific and caps RNAs that initiate with either a G or an A residue. Together with VP1 polymerase, forms a VP1-VP3 complex positioned near the channels situated at each of the five-fold vertices of the core. Following infection, the outermost layer of the virus is lost, leaving a double-layered particle (DLP) made up of the core and VP6 shell. VP1 then catalyzes the transcription of fully conservative plus-strand genomic RNAs that are capped by VP3 and extruded through the DLP's channels into the cytoplasm where they function as mRNAs for translation of viral proteins. DLPs probably have an RNA triphosphatase activity as well, whereas open cores do not. {ECO:0000255|HAMAP-Rule:MF_04128, ECO:0000305|PubMed:10603323}.; FUNCTION: Counteracts the host innate immune response thanks to its phosphodiesterase that degrades the 5'-triphosphorylated, 2'-5' linked adenylate oligomers produced by the host cell IFN-inducible 2',5'-oligoadenylate synthetase (OAS). The host RNaseL is therefore not activated. {ECO:0000255|HAMAP-Rule:MF_04128, ECO:0000269|PubMed:23878220}.
|
Rotavirus A (isolate RVA/Monkey/South Africa/SA11-H96/1958/G3P5B[2]) (RV-A) (Simian Agent 11 (isolate SI/South Africa/H96/58))
|
A2T3T2
|
VP4_ROTSH
|
MASLIYRQLLTNSYTVDLSDEIQEIGSTKSQNVTINPGPFAQTGYAPVNWGPGEINDSTTVEPLLDGPYQPTTFNPPVDYWMLLAPTTPGVIVEGTNNTDRWLATILIEPNVQSENRTYTIFGIQEQLTVSNTSQDQWKFIDVVKTTANGSIGQYGPLLSSPKLYAVMKHNEKLYTYEGQTPNARTAHYSTTNYDSVNMTAFCDFYIIPRSEESKCTEYINNGLPPIQNTRNVVPLSLTARDVIHYRAQANEDIVISKTSLWKEMQYNRDITIRFKFANTIIKSGGLGYKWSEISFKPANYQYTYTRDGEEVTAHTTCSVNGVNDFSFNGGYLPTDFVVSKFEVIKENSYVYIDYWDDSQAFRNVVYVRSLAANLNSVMCTGGSYNFSLPVGQWPVLTGGAVSLHSAGVTLSTQFTDFVSLNSLRFRFRLAVEEPHFKLTRTRLDRLYGLPAADPNNGKEYYEIAGRFSLISLVPSNDDYQTPIANSVTVRQDLERQLGELREEFNALSQEIAMSQLIDLALLPLDMFSMFSGIKSTIDAAKSMATNVMKKFKKSGLANSVSTLTDSLSDAASSISRGSSIRSIGSSASAWTDVSTQITDISSSVSSVSTQTSTISRRLRLKEMATQTEGMNFDDISAAVLKTKIDKSTQISPNTIPDIVTEASEKFIPNRAYRVINNDDVFEAGIDGKFFAYKVDTFEEIPFDVQKFADLVTDSPVISAIIDFKTLKNLNDNYGITKQQAFNLLRSDPRVLREFINQDNPIIRNRIEQLIMQCRL
| null | null |
permeabilization of host organelle membrane involved in viral entry into host cell [GO:0039665]; symbiont entry into host cell via permeabilization of inner membrane [GO:0099008]; virion attachment to host cell [GO:0019062]
|
host cell endoplasmic reticulum-Golgi intermediate compartment [GO:0044172]; host cell plasma membrane [GO:0020002]; host cell rough endoplasmic reticulum [GO:0044168]; host cytoskeleton [GO:0044163]; membrane [GO:0016020]; viral outer capsid [GO:0039624]
| null |
PF17477;PF00426;PF17478;
|
1.20.5.170;2.60.120.200;
|
Rotavirus VP4 family
|
PTM: [Outer capsid protein VP4]: Proteolytic cleavage by trypsin results in activation of VP4 functions and greatly increases infectivity. The penetration into the host cell is dependent on trypsin treatment of VP4. It produces two peptides, VP5* and VP8* that remain associated with the virion. Cleavage of VP4 by trypsin probably occurs in vivo in the lumen of the intestine prior to infection of enterocytes. Trypsin seems to be incorporated into the three-layered viral particles but remains inactive as long as the viral outer capsid is intact and would only be activated upon the solubilization of the latter. {ECO:0000255|HAMAP-Rule:MF_04132}.
|
SUBCELLULAR LOCATION: [Outer capsid protein VP4]: Virion {ECO:0000255|HAMAP-Rule:MF_04132, ECO:0000269|PubMed:1649333}. Host rough endoplasmic reticulum {ECO:0000255|HAMAP-Rule:MF_04132}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04132}. Host cytoplasm, host cytoskeleton {ECO:0000255|HAMAP-Rule:MF_04132}. Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000255|HAMAP-Rule:MF_04132}. Note=The outer layer contains 180 copies of VP4, grouped as 60 dimers (PubMed:2153941). Immature double-layered particles assembled in the cytoplasm bud across the membrane of the endoplasmic reticulum, acquiring during this process a transient lipid membrane that is modified with the ER resident viral glycoproteins NSP4 and VP7; these enveloped particles also contain VP4. As the particles move towards the interior of the ER cisternae, the transient lipid membrane and the non-structural protein NSP4 are lost, while the virus surface proteins VP4 and VP7 rearrange to form the outermost virus protein layer, yielding mature infectious triple-layered particles. VP4 also seems to associates with lipid rafts of the host cell membrane probably for the exit of the virus from the infected cell by an alternate pathway (By similarity). {ECO:0000255|HAMAP-Rule:MF_04132, ECO:0000269|PubMed:2153941}.; SUBCELLULAR LOCATION: [Outer capsid protein VP8*]: Virion {ECO:0000255|HAMAP-Rule:MF_04132, ECO:0000269|PubMed:1649333}. Note=Outer capsid protein. {ECO:0000255|HAMAP-Rule:MF_04132}.; SUBCELLULAR LOCATION: [Outer capsid protein VP5*]: Virion {ECO:0000255|HAMAP-Rule:MF_04132, ECO:0000269|PubMed:1649333}. Note=Outer capsid protein. {ECO:0000255|HAMAP-Rule:MF_04132}.
| null | null | null | null | null |
FUNCTION: [Outer capsid protein VP4]: Spike-forming protein that mediates virion attachment to the host epithelial cell receptors and plays a major role in cell penetration, determination of host range restriction and virulence (PubMed:1649333). Rotavirus attachment and entry into the host cell probably involves multiple sequential contacts between the outer capsid proteins VP4 and VP7, and the cell receptors (PubMed:15165605, PubMed:9144247). It is subsequently lost, together with VP7, following virus entry into the host cell (PubMed:15165605). Following entry into the host cell, low intracellular or intravesicular Ca(2+) concentration probably causes the calcium-stabilized VP7 trimers to dissociate from the virion. This step is probably necessary for the membrane-disrupting entry step and the release of VP4, which is locked onto the virion by VP7. During the virus exit from the host cell, VP4 seems to be required to target the newly formed virions to the host cell lipid rafts (By similarity). {ECO:0000255|HAMAP-Rule:MF_04132, ECO:0000269|PubMed:1649333, ECO:0000269|PubMed:9144247, ECO:0000303|PubMed:15165605}.; FUNCTION: [Outer capsid protein VP5*]: Forms the spike 'foot' and 'body' and acts as a membrane permeabilization protein that mediates release of viral particles from endosomal compartments into the cytoplasm. During entry, the part of VP5* that protrudes from the virus folds back on itself and reorganizes from a local dimer to a trimer. This reorganization may be linked to membrane penetration by exposing VP5* hydrophobic region. In integrin-dependent strains, VP5* targets the integrin heterodimer ITGA2/ITGB1 for cell attachment. {ECO:0000255|HAMAP-Rule:MF_04132}.; FUNCTION: [Outer capsid protein VP8*]: Forms the head of the spikes and mediates the recognition of specific host cell surface glycans. It is the viral hemagglutinin and an important target of neutralizing antibodies. In sialic acid-dependent strains, VP8* binds to host cell sialic acid, most probably a ganglioside, providing the initial contact. In some other strains, VP8* mediates the attachment to histo-blood group antigens (HBGAs) for viral entry. {ECO:0000255|HAMAP-Rule:MF_04132}.
|
Rotavirus A (isolate RVA/Monkey/South Africa/SA11-H96/1958/G3P5B[2]) (RV-A) (Simian Agent 11 (isolate SI/South Africa/H96/58))
|
A2T6K4
|
OSTCN_MACNE
|
MRALTLLALLALATLCITGQAGAKPSGAESSKGAAFVSKQEGSEVVKRPRRYLYQWLGAPAPYPDPLEPKREVCELNPDCDELADHIGFQEAYRRFYGPV
| null | null |
biomineral tissue development [GO:0031214]; bone development [GO:0060348]; brain development [GO:0007420]; cellular response to insulin stimulus [GO:0032869]; cognition [GO:0050890]; glucose homeostasis [GO:0042593]; learning or memory [GO:0007611]; negative regulation of bone development [GO:1903011]; osteoblast differentiation [GO:0001649]; positive regulation of neurotransmitter secretion [GO:0001956]; regulation of bone mineralization [GO:0030500]; regulation of cellular response to insulin stimulus [GO:1900076]; regulation of testosterone biosynthetic process [GO:2000224]; response to vitamin D [GO:0033280]; response to vitamin K [GO:0032571]; type B pancreatic cell proliferation [GO:0044342]
|
cytoplasm [GO:0005737]; extracellular region [GO:0005576]
|
calcium ion binding [GO:0005509]; hormone activity [GO:0005179]; hydroxyapatite binding [GO:0046848]; structural constituent of bone [GO:0008147]
| null | null |
Osteocalcin/matrix Gla protein family
|
PTM: Gamma-carboxyglutamate residues are formed by vitamin K dependent carboxylation by GGCX. These residues are essential for the binding of calcium (By similarity). Decarboxylation promotes the hormone activity (By similarity). {ECO:0000250|UniProtKB:P86546, ECO:0000255|PROSITE-ProRule:PRU00463}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P86546}.
| null | null | null | null | null |
FUNCTION: The carboxylated form is one of the main organic components of the bone matrix, which constitutes 1-2% of the total bone protein: it acts as a negative regulator of bone formation and is required to limit bone formation without impairing bone resorption or mineralization. The carboxylated form binds strongly to apatite and calcium. {ECO:0000250|UniProtKB:P86546}.; FUNCTION: The uncarboxylated form acts as a hormone secreted by osteoblasts, which regulates different cellular processes, such as energy metabolism, male fertility and brain development. Regulates of energy metabolism by acting as a hormone favoring pancreatic beta-cell proliferation, insulin secretion and sensitivity and energy expenditure. Uncarboxylated osteocalcin hormone also promotes testosterone production in the testes: acts as a ligand for G protein-coupled receptor GPRC6A at the surface of Leydig cells, initiating a signaling response that promotes the expression of enzymes required for testosterone synthesis in a CREB-dependent manner. Also acts as a regulator of brain development: osteocalcin hormone crosses the blood-brain barrier and acts as a ligand for GPR158 on neurons, initiating a signaling response that prevents neuronal apoptosis in the hippocampus, favors the synthesis of all monoamine neurotransmitters and inhibits that of gamma-aminobutyric acid (GABA). Osteocalcin also crosses the placenta during pregnancy and maternal osteocalcin is required for fetal brain development. {ECO:0000250|UniProtKB:P86546}.
|
Macaca nemestrina (Pig-tailed macaque)
|
A2T6Y4
|
APEX1_PANTR
|
MPKRGKKGAVAEDGDELRTEPEAKKSKTAAKKNDKEAAGEGPALYEDPPDQKTSPSGKPATLKICSWNVDGLRAWIKKKGLDWVKEEAPDILCLQETKCSENKLPAELQELPGLSHQYWSAPSDKEGYSGVGLLSRQCPLKVSYGIGEEEHDQEGRVIVAEFDSFVLVTAYVPNAGRGLVRLEYRQRWDEAFRKFLKGLASRKPLVLCGDLNVAHEEIDLRNPKGNKKNAGFTPQERQGFGELLQAVPLADSFRHLYPNTPYAYTFWTYMMNARSKNVGWRLDYFLLSHSLLPALCDSKIRSKALGSDHCPITLYLAL
|
3.1.11.2; 3.1.21.-
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P27695}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P27695}; Note=Probably binds two magnesium or manganese ions per subunit. {ECO:0000250|UniProtKB:P27695};
|
base-excision repair [GO:0006284]; DNA recombination [GO:0006310]; DNA repair [GO:0006281]; positive regulation of gene expression via CpG island demethylation [GO:0044029]; regulation of apoptotic process [GO:0042981]; regulation of mRNA stability [GO:0043488]
|
cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; mitochondrion [GO:0005739]; nuclear speck [GO:0016607]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
3'-5' exonuclease activity [GO:0008408]; chromatin DNA binding [GO:0031490]; class II DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0052720]; damaged DNA binding [GO:0003684]; DNA-(abasic site) binding [GO:0140431]; DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0003906]; double-stranded DNA 3'-5' DNA exonuclease activity [GO:0008311]; metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491]; phosphoric diester hydrolase activity [GO:0008081]; RNA binding [GO:0003723]; site-specific endodeoxyribonuclease activity, specific for altered base [GO:0016890]
|
PF03372;
|
3.60.10.10;
|
DNA repair enzymes AP/ExoA family
|
PTM: Phosphorylated. Phosphorylation by kinase PKC or casein kinase CK2 results in enhanced redox activity that stimulates binding of the FOS/JUN AP-1 complex to its cognate binding site. AP-endodeoxyribonuclease activity is not affected by CK2-mediated phosphorylation. Phosphorylation of Thr-233 by CDK5 in response to MPP(+)/MPTP (1-methyl-4-phenylpyridinium) reduces AP-endodeoxyribonuclease activity resulting in accumulation of DNA damage and contributing to neuronal death (By similarity). {ECO:0000250|UniProtKB:P27695}.; PTM: Acetylated on Lys-6 and Lys-7. Acetylation is increased by the transcriptional coactivator EP300 acetyltransferase, genotoxic agents like H(2)O(2) and methyl methanesulfonate (MMS). Acetylation increases its binding affinity to the negative calcium response element (nCaRE) DNA promoter. The acetylated form induces a stronger binding of YBX1 to the Y-box sequence in the MDR1 promoter than the unacetylated form. Deacetylated on lysines. Lys-6 and Lys-7 are deacetylated by SIRT1 (By similarity). {ECO:0000250|UniProtKB:P27695}.; PTM: Cleaved at Lys-31 by granzyme A to create the mitochondrial form; leading in reduction of binding to DNA, AP endodeoxyribonuclease activity, redox activation of transcription factors and to enhanced cell death. Cleaved by granzyme K; leading to intracellular ROS accumulation and enhanced cell death after oxidative stress (By similarity). {ECO:0000250|UniProtKB:P27695}.; PTM: Cys-69 and Cys-93 are nitrosylated in response to nitric oxide (NO) and lead to the exposure of the nuclear export signal (NES). {ECO:0000250|UniProtKB:P27695}.; PTM: Ubiquitinated by MDM2; leading to translocation to the cytoplasm and proteasomal degradation. {ECO:0000250|UniProtKB:P27695}.
|
SUBCELLULAR LOCATION: Nucleus. Nucleus, nucleolus {ECO:0000250}. Nucleus speckle {ECO:0000255|PROSITE-ProRule:PRU00764}. Endoplasmic reticulum {ECO:0000250}. Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00764}. Note=Detected in the cytoplasm of B-cells stimulated to switch. Colocalized with SIRT1 in the nucleus. Colocalized with YBX1 in nuclear speckles after genotoxic stress. Together with OGG1 is recruited to nuclear speckles in UVA-irradiated cells. Colocalized with nucleolin and NPM1 in the nucleolus. Its nucleolar localization is cell cycle dependent and requires active rRNA transcription (By similarity). Colocalized with calreticulin in the endoplasmic reticulum. Translocation from the nucleus to the cytoplasm is stimulated in presence of nitric oxide (NO) and function in a CRM1-dependent manner, possibly as a consequence of demasking a nuclear export signal (amino acid position 64-80). S-nitrosylation at Cys-93 and Cys-310 regulates its nuclear-cytosolic shuttling. Ubiquitinated form is localized predominantly in the cytoplasm (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: [DNA repair nuclease/redox regulator APEX1, mitochondrial]: Mitochondrion. Note=Translocation from the cytoplasm to the mitochondria is mediated by ROS signaling and cleavage mediated by granzyme A. Tom20-dependent translocated mitochondrial APEX1 level is significantly increased after genotoxic stress. The cleaved APEX2 is only detected in mitochondria (By similarity). {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.; EC=3.1.11.2; Evidence={ECO:0000250|UniProtKB:P27695};
| null | null | null | null |
FUNCTION: Multifunctional protein that plays a central role in the cellular response to oxidative stress. The two major activities of APEX1 are DNA repair and redox regulation of transcriptional factors. Functions as an apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DNA lesions induced by oxidative and alkylating agents. Initiates repair of AP sites in DNA by catalyzing hydrolytic incision of the phosphodiester backbone immediately adjacent to the damage, generating a single-strand break with 5'-deoxyribose phosphate and 3'-hydroxyl ends. Also incises at AP sites in the DNA strand of DNA/RNA hybrids, single-stranded DNA regions of R-loop structures, and single-stranded RNA molecules. Has 3'-5' exoribonuclease activity on mismatched deoxyribonucleotides at the 3' termini of nicked or gapped DNA molecules during short-patch BER. Possesses DNA 3' phosphodiesterase activity capable of removing lesions (such as phosphoglycolate) blocking the 3' side of DNA strand breaks. May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation. Acts as a loading factor for POLB onto non-incised AP sites in DNA and stimulates the 5'-terminal deoxyribose 5'-phosphate (dRp) excision activity of POLB. Plays a role in the protection from granzyme-mediated cellular repair leading to cell death. Also involved in the DNA cleavage step of class switch recombination (CSR). On the other hand, APEX1 also exerts reversible nuclear redox activity to regulate DNA binding affinity and transcriptional activity of transcriptional factors by controlling the redox status of their DNA-binding domain, such as the FOS/JUN AP-1 complex after exposure to IR. Involved in calcium-dependent down-regulation of parathyroid hormone (PTH) expression by binding to negative calcium response elements (nCaREs). Together with HNRNPL or the dimer XRCC5/XRCC6, associates with nCaRE, acting as an activator of transcriptional repression. Stimulates the YBX1-mediated MDR1 promoter activity, when acetylated at Lys-6 and Lys-7, leading to drug resistance. Acts also as an endoribonuclease involved in the control of single-stranded RNA metabolism. Plays a role in regulating MYC mRNA turnover by preferentially cleaving in between UA and CA dinucleotides of the MYC coding region determinant (CRD). In association with NMD1, plays a role in the rRNA quality control process during cell cycle progression. Associates, together with YBX1, on the MDR1 promoter. Together with NPM1, associates with rRNA. Binds DNA and RNA (By similarity). {ECO:0000250|UniProtKB:P27695}.
|
Pan troglodytes (Chimpanzee)
|
A2T756
|
PDX1_PANTR
|
MNGEEQYYAATQLYKDSCAFQRGPAPEFSAGPPACLYMGRQPPPPPPHPFPGALGALEQGSPPDISPYEVPPLADDPAVAHLHHHLPAQLALPHPPAGPFPEGAEPGVLEEPNRVQLPFPWMKSTKAHAWKGQWAGGAYAAEPEENKRTRTAYTRAQLLELEKEFLFNKYISRPRRVELAVMLNLTERHIKIWFQNRRMKWKKEEDKKRGGGTAVGGGGVAEPEQDCAVTSGEELLALPPPPPPGGAVPPAAPVAAREGRLPPGLSASPQPSSVAPRRPQEPR
| null | null |
digestive tract development [GO:0048565]; exocrine pancreas development [GO:0031017]; glucose homeostasis [GO:0042593]; glucose metabolic process [GO:0006006]; insulin secretion [GO:0030073]; intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress [GO:0070059]; liver development [GO:0001889]; morphogenesis of embryonic epithelium [GO:0016331]; negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway [GO:1902236]; negative regulation of epithelial cell proliferation [GO:0050680]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of type B pancreatic cell apoptotic process [GO:2000675]; positive regulation of insulin secretion [GO:0032024]; positive regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0035774]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of type B pancreatic cell proliferation [GO:1904692]; regulation of transcription by RNA polymerase II [GO:0006357]; type B pancreatic cell apoptotic process [GO:0097050]; type B pancreatic cell differentiation [GO:0003309]; type B pancreatic cell proliferation [GO:0044342]
|
cytosol [GO:0005829]; nuclear speck [GO:0016607]; nucleus [GO:0005634]
|
chromatin binding [GO:0003682]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF00046;
|
1.10.10.60;
|
Antp homeobox family, IPF1/XlHbox-8 subfamily
|
PTM: Phosphorylated by the SAPK2 pathway at high intracellular glucose concentration. Phosphorylated by HIPK2 on Ser-268 upon glucose accumulation. This phosphorylation mediates subnuclear localization shifting. Phosphorylation by PASK may lead to translocation into the cytosol (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}. Cytoplasm, cytosol {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Activates insulin and somatostatin gene transcription. Key regulator of islet peptide hormone expression but also responsible for the development of the pancreas, most probably by determining maturation and differentiation of common pancreatic precursor cells in the developing gut. As part of a PDX1:PBX1b:MEIS2b complex in pancreatic acinar cells is involved in the transcriptional activation of the ELA1 enhancer; the complex binds to the enhancer B element and cooperates with the transcription factor 1 complex (PTF1) bound to the enhancer A element. Binds the DNA sequence 5'-CC[CT]TAATGGG-3' (By similarity). {ECO:0000250}.
|
Pan troglodytes (Chimpanzee)
|
A2T7I6
|
APEX1_PONPY
|
MPKRGKKGAVAEDGDELKTEPEAKKSKTTAKKNDKEAAGEGPALYEDPPDQKTSPSGKPATLKICSWNVDGLRAWIKKKGLDWVKEEAPDILCLQETKCSENKLPAELQELPGLSHQYWSAPSDKEGYSGVGLLSRQCPLKVSYGIGEEEHDQEGRVIVAEFDSFVLVTAYVPNAGRGLVRLEYRQRWDEAFRRFLKGLASRKPLVLCGDLNVAHEEIDLRNPKGNKKNAGFTPQERQGFGELLQAVPLADSFRHLYPNTPYAYTFWTYMMNARSKNVGWRLDYFLLSHSLLTALCDSKIRSKALGSDHCPITLYLAL
|
3.1.11.2; 3.1.21.-
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P27695}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P27695}; Note=Probably binds two magnesium or manganese ions per subunit. {ECO:0000250|UniProtKB:P27695};
|
base-excision repair [GO:0006284]; DNA recombination [GO:0006310]; DNA repair [GO:0006281]; positive regulation of gene expression via CpG island demethylation [GO:0044029]; regulation of apoptotic process [GO:0042981]; regulation of mRNA stability [GO:0043488]
|
cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; mitochondrion [GO:0005739]; nuclear speck [GO:0016607]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
3'-5' exonuclease activity [GO:0008408]; chromatin DNA binding [GO:0031490]; class II DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0052720]; damaged DNA binding [GO:0003684]; DNA-(abasic site) binding [GO:0140431]; DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0003906]; double-stranded DNA 3'-5' DNA exonuclease activity [GO:0008311]; metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491]; phosphoric diester hydrolase activity [GO:0008081]; RNA binding [GO:0003723]; site-specific endodeoxyribonuclease activity, specific for altered base [GO:0016890]
|
PF03372;
|
3.60.10.10;
|
DNA repair enzymes AP/ExoA family
|
PTM: Phosphorylated. Phosphorylation by kinase PKC or casein kinase CK2 results in enhanced redox activity that stimulates binding of the FOS/JUN AP-1 complex to its cognate binding site. AP-endodeoxyribonuclease activity is not affected by CK2-mediated phosphorylation. Phosphorylation of Thr-233 by CDK5 in response to MPP(+)/MPTP (1-methyl-4-phenylpyridinium) reduces AP-endodeoxyribonuclease activity resulting in accumulation of DNA damage and contributing to neuronal death (By similarity). {ECO:0000250|UniProtKB:P27695}.; PTM: Acetylated on Lys-6 and Lys-7. Acetylation is increased by the transcriptional coactivator EP300 acetyltransferase, genotoxic agents like H(2)O(2) and methyl methanesulfonate (MMS). Acetylation increases its binding affinity to the negative calcium response element (nCaRE) DNA promoter. The acetylated form induces a stronger binding of YBX1 to the Y-box sequence in the MDR1 promoter than the unacetylated form. Deacetylated on lysines. Lys-6 and Lys-7 are deacetylated by SIRT1 (By similarity). {ECO:0000250|UniProtKB:P27695}.; PTM: Cleaved at Lys-31 by granzyme A to create the mitochondrial form; leading in reduction of binding to DNA, AP endodeoxyribonuclease activity, redox activation of transcription factors and to enhanced cell death. Cleaved by granzyme K; leading to intracellular ROS accumulation and enhanced cell death after oxidative stress (By similarity). {ECO:0000250|UniProtKB:P27695}.; PTM: Cys-69 and Cys-93 are nitrosylated in response to nitric oxide (NO) and lead to the exposure of the nuclear export signal (NES). {ECO:0000250|UniProtKB:P27695}.; PTM: Ubiquitinated by MDM2; leading to translocation to the cytoplasm and proteasomal degradation. {ECO:0000250|UniProtKB:P27695}.
|
SUBCELLULAR LOCATION: Nucleus. Nucleus, nucleolus {ECO:0000250}. Nucleus speckle {ECO:0000255|PROSITE-ProRule:PRU00764}. Endoplasmic reticulum {ECO:0000250}. Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00764}. Note=Detected in the cytoplasm of B-cells stimulated to switch. Colocalized with SIRT1 in the nucleus. Colocalized with YBX1 in nuclear speckles after genotoxic stress. Together with OGG1 is recruited to nuclear speckles in UVA-irradiated cells. Colocalized with nucleolin and NPM1 in the nucleolus. Its nucleolar localization is cell cycle dependent and requires active rRNA transcription (By similarity). Colocalized with calreticulin in the endoplasmic reticulum. Translocation from the nucleus to the cytoplasm is stimulated in presence of nitric oxide (NO) and function in a CRM1-dependent manner, possibly as a consequence of demasking a nuclear export signal (amino acid position 64-80). S-nitrosylation at Cys-93 and Cys-310 regulates its nuclear-cytosolic shuttling. Ubiquitinated form is localized predominantly in the cytoplasm (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: [DNA repair nuclease/redox regulator APEX1, mitochondrial]: Mitochondrion. Note=Translocation from the cytoplasm to the mitochondria is mediated by ROS signaling and cleavage mediated by granzyme A. Tom20-dependent translocated mitochondrial APEX1 level is significantly increased after genotoxic stress. The cleaved APEX2 is only detected in mitochondria (By similarity). {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.; EC=3.1.11.2; Evidence={ECO:0000250|UniProtKB:P27695};
| null | null | null | null |
FUNCTION: Multifunctional protein that plays a central role in the cellular response to oxidative stress. The two major activities of APEX1 are DNA repair and redox regulation of transcriptional factors. Functions as an apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DNA lesions induced by oxidative and alkylating agents. Initiates repair of AP sites in DNA by catalyzing hydrolytic incision of the phosphodiester backbone immediately adjacent to the damage, generating a single-strand break with 5'-deoxyribose phosphate and 3'-hydroxyl ends. Also incises at AP sites in the DNA strand of DNA/RNA hybrids, single-stranded DNA regions of R-loop structures, and single-stranded RNA molecules. Has 3'-5' exoribonuclease activity on mismatched deoxyribonucleotides at the 3' termini of nicked or gapped DNA molecules during short-patch BER. Possesses DNA 3' phosphodiesterase activity capable of removing lesions (such as phosphoglycolate) blocking the 3' side of DNA strand breaks. May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation. Acts as a loading factor for POLB onto non-incised AP sites in DNA and stimulates the 5'-terminal deoxyribose 5'-phosphate (dRp) excision activity of POLB. Plays a role in the protection from granzyme-mediated cellular repair leading to cell death. Also involved in the DNA cleavage step of class switch recombination (CSR). On the other hand, APEX1 also exerts reversible nuclear redox activity to regulate DNA binding affinity and transcriptional activity of transcriptional factors by controlling the redox status of their DNA-binding domain, such as the FOS/JUN AP-1 complex after exposure to IR. Involved in calcium-dependent down-regulation of parathyroid hormone (PTH) expression by binding to negative calcium response elements (nCaREs). Together with HNRNPL or the dimer XRCC5/XRCC6, associates with nCaRE, acting as an activator of transcriptional repression. Stimulates the YBX1-mediated MDR1 promoter activity, when acetylated at Lys-6 and Lys-7, leading to drug resistance. Acts also as an endoribonuclease involved in the control of single-stranded RNA metabolism. Plays a role in regulating MYC mRNA turnover by preferentially cleaving in between UA and CA dinucleotides of the MYC coding region determinant (CRD). In association with NMD1, plays a role in the rRNA quality control process during cell cycle progression. Associates, together with YBX1, on the MDR1 promoter. Together with NPM1, associates with rRNA. Binds DNA and RNA (By similarity). {ECO:0000250|UniProtKB:P27695}.
|
Pongo pygmaeus (Bornean orangutan)
|
A2T7L5
|
MYC_PONPY
|
MPLNVSFTNRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVTPFSPRGDNDGGGGSFSTADQLEMVTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAKLVSEKLASYQAARKDSGSPNPARGHSVCSTSSLYLQDLSAAASECIDPSVVFPYPLNDSSLPKSCTSPDSSAFSPSSDSLLSSTESSPQASPEPLVLHEETPPTTSSDSEEEQEDEEEIDVVSVEKRQAPGKRSESGSPSAGGHIKPPHSPLVLKRCHVSTHQHNYAAPPSTRKDYPAAKRVKLDSVRVLRQISNNRKCTSPRSSDAEENDKRRTHNVLERQRRNELKRSFFALRDQIPELENNEKAPKVVILKKATAYILSIQAEEQKLISEKDLLRKRREQLKHKLEQLRNSCA
| null | null |
chromatin remodeling [GO:0006338]; chromosome organization [GO:0051276]; DNA damage response [GO:0006974]; G1/S transition of mitotic cell cycle [GO:0000082]; intracellular iron ion homeostasis [GO:0006879]; MAPK cascade [GO:0000165]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell division [GO:0051782]; negative regulation of monocyte differentiation [GO:0045656]; negative regulation of stress-activated MAPK cascade [GO:0032873]; positive regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043280]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of epithelial cell proliferation [GO:0050679]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of DNA-templated transcription [GO:0006355]; regulation of somatic stem cell population maintenance [GO:1904672]; regulation of telomere maintenance [GO:0032204]; response to gamma radiation [GO:0010332]; response to xenobiotic stimulus [GO:0009410]
|
cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; E-box binding [GO:0070888]; protein dimerization activity [GO:0046983]; protein-containing complex binding [GO:0044877]
|
PF00010;PF02344;PF01056;
|
4.10.280.10;
| null |
PTM: Phosphorylated by PRKDC (By similarity). Phosphorylation at Ser-329 by PIM2 leads to the stabilization of MYC (By similarity). Phosphorylation at Ser-62 by CDK2 prevents Ras-induced senescence. Phosphorylated at Ser-62 by DYRK2; this primes the protein for subsequent phosphorylation by GSK3B at Thr-58. Phosphorylation at Thr-58 and Ser-62 by GSK3 is required for ubiquitination and degradation by the proteasome. Dephosphorylation at Ser-62 by protein phosphatase 2A (PPP2CA) promotes its degradation; interaction with PPP2CA is enhanced by AMBRA1 (By similarity). {ECO:0000250|UniProtKB:P01106, ECO:0000250|UniProtKB:P01108}.; PTM: Ubiquitinated by the SCF(FBXW7) complex when phosphorylated at Thr-58 and Ser-62, leading to its degradation by the proteasome. Ubiquitination is counteracted by USP28 in the nucleoplasm and USP36 in the nucleolus, both interacting with of FBXW7, leading to its deubiquitination and preventing degradation. Also polyubiquitinated by the DCX(TRPC4AP) complex. Ubiquitinated by TRIM6 in a phosphorylation-independent manner. {ECO:0000250|UniProtKB:P01106, ECO:0000250|UniProtKB:P01108}.
|
SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P01106}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P01106}. Nucleus {ECO:0000250|UniProtKB:P01106}. Cytoplasm {ECO:0000250|UniProtKB:P01106}.
| null | null | null | null | null |
FUNCTION: Transcription factor that binds DNA in a non-specific manner, yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3'. Activates the transcription of growth-related genes. Binds to the VEGFA promoter, promoting VEGFA production and subsequent sprouting angiogenesis. Regulator of somatic reprogramming, controls self-renewal of embryonic stem cells. Functions with TAF6L to activate target gene expression through RNA polymerase II pause release (By similarity). Positively regulates transcription of HNRNPA1, HNRNPA2 and PTBP1 which in turn regulate splicing of pyruvate kinase PKM by binding repressively to sequences flanking PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion and production of the PKM M2 isoform (By similarity). {ECO:0000250|UniProtKB:P01106, ECO:0000250|UniProtKB:P01108}.
|
Pongo pygmaeus (Bornean orangutan)
|
A2T928
|
RARGB_DANRE
|
MRDVFREATPMTCRSPLPDLRDMMEKLTVFEPTIDSTVETQSTSSEEMIPSSPSPPPPPRVYKPCFVCQDKSSGYHYGVSSCEGCKGFFRRSIQKNMVYTCHRDKNCQINKVTRNRCQYCRLRKCFEVGMSKEAVRNDRNKKKKDVKEEVVLPESYELSGELEELVNKVSKAHRETFPSLCQLGKYTTNSSADHRVQLDLGLWDKFSELSTKCIIKIVEFAKRLPGFTSLTIADQITLLKSACLDILMLRICTRYTPEQDTMTFSDGLTLNRTQMHNAGFGPLTDLVFAFAGQLLPLEMDDTETGLLSAICLICGDRMDLEEPHRVDQLQEPLLEALKIYARRRRPNKPHMFPRMLMKVTDLRGISTKGAERAITLKMEIPGPMPPLIREMLENPEIFEDSSDSNDSGAAAVVPAPNIKRMGQRQAAWVKGERPEWVRGRRRGSKSRYKAGFKAGKARSRDSPDNNGEIRQGDERSEMSVRAEQDFALE
| null | null |
cell differentiation [GO:0030154]; cellular response to corticotropin-releasing hormone stimulus [GO:0071376]; determination of digestive tract left/right asymmetry [GO:0071907]; determination of heart left/right asymmetry [GO:0061371]; determination of left/right asymmetry in lateral mesoderm [GO:0003140]; determination of liver left/right asymmetry [GO:0071910]; determination of pancreatic left/right asymmetry [GO:0035469]; hormone-mediated signaling pathway [GO:0009755]; intrahepatic bile duct development [GO:0035622]; negative regulation of BMP signaling pathway [GO:0030514]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of transcription by RNA polymerase II [GO:0045944]; retinoic acid receptor signaling pathway [GO:0048384]
|
nucleus [GO:0005634]; transcription regulator complex [GO:0005667]
|
nuclear glucocorticoid receptor binding [GO:0035259]; nuclear receptor activity [GO:0004879]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; zinc ion binding [GO:0008270]
|
PF00104;PF00105;
|
3.30.50.10;1.10.565.10;
|
Nuclear hormone receptor family, NR1 subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
| null | null | null | null | null |
FUNCTION: Receptor for retinoic acid. Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The rar/rxr heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5 (By similarity). Required for hindbrain development. {ECO:0000250, ECO:0000269|PubMed:18929555}.
|
Danio rerio (Zebrafish) (Brachydanio rerio)
|
A2TGX5
|
CLM8_RAT
|
MTQLASAVWPPTLLLLLLFWVPGCVPLRGPSSVTGTVGESLNVTCQYEERFKMNKKYWCRGSLVLLCKDIVRTGGSEEARNGRVSIRDDRDNLTFTVTLQNLTLEDAGTYMCAVDIPLIDHSFKVELSVVPGNIPVSSPGTTRETTVVPTSFSTKGPTQGSIPEGHHEHYEPQGLSLPVLLSVLALLLLLLVGTSLLAWRMFQKRSVKADKHPEMSQNLRQAEEQSESQYVNLQLHTLPLREEPVPPSQVEVEYSTLALPQEELHYTSVVFDSQRQNSHANGDPPCQSPDQKTEYSEIRKPREGLSDPHP
| null | null |
establishment of localization in cell [GO:0051649]; mast cell degranulation [GO:0043303]; negative regulation of B cell proliferation [GO:0030889]; negative regulation of B cell receptor signaling pathway [GO:0050859]; negative regulation of eosinophil activation [GO:1902567]; negative regulation of eosinophil migration [GO:2000417]; negative regulation of fibroblast proliferation [GO:0048147]; negative regulation of mast cell activation involved in immune response [GO:0033007]; negative regulation of mast cell degranulation [GO:0043305]; negative regulation of MyD88-dependent toll-like receptor signaling pathway [GO:0034125]; negative regulation of neutrophil activation [GO:1902564]; negative regulation of NK T cell activation [GO:0051134]; negative regulation of phagocytosis, engulfment [GO:0060101]; negative regulation of serotonin secretion [GO:0014063]; receptor-mediated endocytosis [GO:0006898]; regulation of T cell receptor signaling pathway [GO:0050856]; serotonin secretion [GO:0001820]; serotonin secretion by mast cell [GO:0002552]
|
membrane [GO:0016020]; plasma membrane [GO:0005886]
|
phosphatase binding [GO:0019902]; phosphatidylethanolamine binding [GO:0008429]; phosphatidylserine binding [GO:0001786]; signaling receptor activity [GO:0038023]; transmembrane signaling receptor activity [GO:0004888]
|
PF15330;PF07686;
|
2.60.40.10;
|
CD300 family
|
PTM: Phosphorylated on tyrosine. {ECO:0000250|UniProtKB:Q6SJQ0}.; PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q6SJQ0}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6SJQ0}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q6SJQ0}.
| null | null | null | null | null |
FUNCTION: Inhibitory receptor which may contribute to the down-regulation of cytolytic activity in natural killer (NK) cells, and to the down-regulation of mast cell degranulation. Negatively regulates the Toll-like receptor (TLR) signaling mediated by MYD88 but not TRIF through activation of PTPN6. {ECO:0000250|UniProtKB:Q9UGN4}.
|
Rattus norvegicus (Rat)
|
A2TJ54
|
CLN5_SHEEP
|
MAQAGGAGAGAWGRRGAGAGAGPERAPWRWAPALLWLAAATAAAAAAGDPSRRQWPVPYKRFSFRPEPDPYCQAKYTFCPTGSPIPVMKDDDVIEVFRLQAPVWEFKYGDLLGHLKIMHDAIGFRSTLTEKNYTMEWYELFQLGNCTFPHLRPEMNAPFWCNQGAACFFEGIDDNHWKENGTLVLVATISGGMFNKMAKWVKQDNETGIYYETWTVQASPKKEAEKWFESYDCSKFVLRTYEKLAELGADFKKIETNYTRIFLYSGEPTYLGNETSVFGPTGNKTLALAIKKFYYPFKPHLSTKEFLLSLLQIFDAVVIHREFYLFYNFEYWFLPMKSPFIKITYEEIPLPNRKNRTLSGL
|
2.3.1.-; 3.1.2.22
| null |
glycosylation [GO:0070085]; lysosome organization [GO:0007040]; positive regulation of GTP binding [GO:1904426]; retrograde transport, endosome to Golgi [GO:0042147]; signal peptide processing [GO:0006465]
|
cytosol [GO:0005829]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]
|
hydrolase activity, acting on glycosyl bonds [GO:0016798]; mannose binding [GO:0005537]; transferase activity [GO:0016740]
|
PF15014;
| null |
CLN5 family
|
PTM: N-glycosylated with both high mannose and complex type sugars. Glycosylation is important for proper folding and trafficking to the lysosomes. {ECO:0000250|UniProtKB:O75503}.; PTM: [Bis(monoacylglycero)phosphate synthase CLN5]: The type II membrane signal anchor is proteolytically cleaved to produce a mature form that is transported to the lysosomes (Bis(monoacylglycero)phosphate synthase CLN5, secreted form). {ECO:0000250|UniProtKB:O75503}.; PTM: Can undergo proteolytic cleavage at the C-terminus, probably by a cysteine protease and may involve the removal of approximately 10-15 residues from the C-terminal end. {ECO:0000250|UniProtKB:O75503}.
|
SUBCELLULAR LOCATION: [Bis(monoacylglycero)phosphate synthase CLN5, secreted form]: Lysosome {ECO:0000250|UniProtKB:O75503}.; SUBCELLULAR LOCATION: [Bis(monoacylglycero)phosphate synthase CLN5]: Membrane {ECO:0000250|UniProtKB:O75503}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:O75503}. Note=An amphipathic anchor region facilitates its association with the membrane. {ECO:0000250|UniProtKB:O75503}.
|
CATALYTIC ACTIVITY: Reaction=H2O + S-hexadecanoyl-L-cysteinyl-[protein] = H(+) + hexadecanoate + L-cysteinyl-[protein]; Xref=Rhea:RHEA:19233, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:74151; EC=3.1.2.22; Evidence={ECO:0000250|UniProtKB:O75503}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19234; Evidence={ECO:0000250|UniProtKB:O75503}; CATALYTIC ACTIVITY: [Bis(monoacylglycero)phosphate synthase CLN5, secreted form]: Reaction=2 a 3-acyl-sn-glycero-1-phospho-(1'-sn-glycerol) = a 3-acyl-sn-glycero-1-phospho-(3'-acyl-1'-sn-glycerol) + sn-glycero-1-phospho-(1'-sn-glycerol); Xref=Rhea:RHEA:77619, ChEBI:CHEBI:77717, ChEBI:CHEBI:197411, ChEBI:CHEBI:197425; Evidence={ECO:0000250|UniProtKB:O75503}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77620; Evidence={ECO:0000250|UniProtKB:O75503}; CATALYTIC ACTIVITY: [Bis(monoacylglycero)phosphate synthase CLN5, secreted form]: Reaction=2 3-(9Z-octadecenoyl)-sn-glycero-1-phospho-(1'-sn-glycerol) = 3-(9Z-octadecenoyl)-sn-glycero-1-phospho-(3'-(9Z-octadecenoyl)-1'-sn-glycerol) + sn-glycero-1-phospho-(1'-sn-glycerol); Xref=Rhea:RHEA:77599, ChEBI:CHEBI:139150, ChEBI:CHEBI:139152, ChEBI:CHEBI:197411; Evidence={ECO:0000250|UniProtKB:O75503}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77600; Evidence={ECO:0000250|UniProtKB:O75503}; CATALYTIC ACTIVITY: [Bis(monoacylglycero)phosphate synthase CLN5, secreted form]: Reaction=2 3-octadecanoyl-sn-glycero-1-phospho-(1'-sn-glycerol) = 3-octadecanoyl-sn-glycero-1-phospho-(3'-octadecanoyl-1'-sn-glycerol) + sn-glycero-1-phospho-(1'-sn-glycerol); Xref=Rhea:RHEA:77603, ChEBI:CHEBI:197411, ChEBI:CHEBI:197412, ChEBI:CHEBI:197414; Evidence={ECO:0000250|UniProtKB:O75503}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77604; Evidence={ECO:0000250|UniProtKB:O75503}; CATALYTIC ACTIVITY: [Bis(monoacylglycero)phosphate synthase CLN5, secreted form]: Reaction=2 3-hexadecanoyl-sn-glycero-1-phospho-(1'-sn-glycerol) = 3-hexadecanoyl-sn-glycero-1-phospho-(3'-hexadecanoyl-1'-sn-glycerol) + sn-glycero-1-phospho-(1'-sn-glycerol); Xref=Rhea:RHEA:77607, ChEBI:CHEBI:44859, ChEBI:CHEBI:197411, ChEBI:CHEBI:197415; Evidence={ECO:0000250|UniProtKB:O75503}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77608; Evidence={ECO:0000250|UniProtKB:O75503}; CATALYTIC ACTIVITY: [Bis(monoacylglycero)phosphate synthase CLN5, secreted form]: Reaction=2 3-tetradecanoyl-sn-glycero-1-phospho-(1'-sn-glycerol) = 3-tetradecanoyl-sn-glycero-1-phospho-(3'-tetradecanoyl-1'-sn-glycerol) + sn-glycero-1-phospho-(1'-sn-glycerol); Xref=Rhea:RHEA:77611, ChEBI:CHEBI:197411, ChEBI:CHEBI:197413, ChEBI:CHEBI:197416; Evidence={ECO:0000250|UniProtKB:O75503}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77612; Evidence={ECO:0000250|UniProtKB:O75503};
| null | null | null | null |
FUNCTION: [Bis(monoacylglycero)phosphate synthase CLN5, secreted form]: Catalyzes the synthesis of bis(monoacylglycero)phosphate (BMP) via transacylation of 2 molecules of lysophosphatidylglycerol (LPG). BMP also known as lysobisphosphatidic acid plays a key role in the formation of intraluminal vesicles and in maintaining intracellular cholesterol homeostasis. Can use only LPG as the exclusive lysophospholipid acyl donor for base exchange and displays BMP synthase activity towards various LPGs (LPG 14:0, LPG 16:0, LPG 18:0, LPG 18:1) with a higher preference for longer chain lengths. Plays a role in influencing the retrograde trafficking of lysosomal sorting receptors SORT1 and IGF2R from the endosomes to the trans-Golgi network by controlling the recruitment of retromer complex to the endosomal membrane. Regulates the localization and activation of RAB7A which is required to recruit the retromer complex to the endosomal membrane. {ECO:0000250|UniProtKB:O75503}.; FUNCTION: Exhibits palmitoyl protein thioesterase (S-depalmitoylation) activity in vitro and most likely plays a role in protein S-depalmitoylation. {ECO:0000250|UniProtKB:O75503}.
|
Ovis aries (Sheep)
|
A2TK72
|
VM3A2_DEIAC
|
KREAEANRTPEQQIYDPYKYVETVFVVDKAMVTKYNGDLDKIKTRMYEAANNMNEMYRYMFFRVVMVGLIIWTEEDKITVKPDVDYTLNAFAEWRKTYLLAEKKHDNAQLITGIDFRGSIIGYAYIGSMCHPKRSVGIIQDYSPINLVLAVIMAHEMGHNLGIHHDDGYCYCGGYPCIMGPSISPEPSKFFSNCSYIQCWDFIMNHNPECIDNEPLGTDIISPPLCGNELLEA
|
3.4.24.-
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q9PW35}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9PW35};
|
proteolysis [GO:0006508]
|
extracellular region [GO:0005576]; plasma membrane [GO:0005886]
|
metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; toxin activity [GO:0090729]
|
PF01421;
|
3.40.390.10;
|
Venom metalloproteinase (M12B) family, P-III subfamily
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9W6M5}.
| null |
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=538.2 uM for N-(p-Tosyl)-Gly-Pro-Lys-pNA {ECO:0000269|PubMed:19013210};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0-10.5. {ECO:0000269|PubMed:19013210};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30-50 degrees Celsius. {ECO:0000269|PubMed:19013210};
|
FUNCTION: Snake venom zinc metalloprotease that acts at several levels. It has direct fibrino(geno)lytic activity (Aalpha chain of fibrinogen is cleaved quickly, Bbeta chain slowly, and gamma chain even more slowly) and degradation of TNF-alpha. These activities permit to protect against sepsis and disseminated intravascular coagulation (PubMed:17964518, PubMed:18634754, PubMed:19013210, PubMed:19070354). It inhibits ADP-induced platelet aggregation in human platelet-rich plasma (IC(50)=65.4 ug/ml) (PubMed:19013210). It decreases the activity of complement by degrading human C5, C6 and C9 in vitro, decreasing serum levels of C1q, C3 and C4 in rat, and inhibiting the MAC deposition on HUVECs membrane. This inhibition of complement protects against hyperacute rejection that is the main barrier in xenotransplantation (PubMed:23178656). Has preference for Lys at the P1 position. Cleaves insulin B chain at '36-Val-|-Glu-37', '39-Leu-|-Tyr-40', and '48-Phe-|-Phe-49' bonds. Also cleaves fibronectin and type IV collagen (PubMed:19013210). {ECO:0000269|PubMed:17964518, ECO:0000269|PubMed:18634754, ECO:0000269|PubMed:19013210, ECO:0000269|PubMed:19070354, ECO:0000269|PubMed:23178656}.
|
Deinagkistrodon acutus (Hundred-pace snake) (Agkistrodon acutus)
|
A2V9Y8
|
OXDA_MACFA
|
MRVVVIGAGVIGLSTALCIHECYHSVLQPLDIKVYADRFTPLTTTDVAAGFWQPYLSDPSNPKEADWSQQTFDYLLSHIHSPNAEKLGLFLISGYNLFHEAIPDPSWKDTVLGFRKLTPRELDIFPDYSYGWFHTSLILEGKNYLQWLTERLTERGVKFFQRKVESFEEVAREGADVIVNCTGVWAGVLQPDPLLQPGRGQIIKVDAPWIKHFILTHEPESGIYNSPYIIPGTQTVTLGGIFQLGNWNELNNIQDHNTIWEGCCRLEPTLKNARIVDERTGFRPVRPKIRLEREQLRVGPSNTEVIHNYGHGGYGLTIHWGCALEAAKLFGRILEEKKLSKMPPSHL
|
1.4.3.3
|
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:P18894};
|
D-alanine catabolic process [GO:0055130]; D-serine catabolic process [GO:0036088]; digestion [GO:0007586]; dopamine biosynthetic process [GO:0042416]; neutrophil-mediated killing of gram-negative bacterium [GO:0070945]; proline catabolic process [GO:0006562]
|
peroxisomal matrix [GO:0005782]; peroxisome [GO:0005777]; presynaptic active zone [GO:0048786]
|
D-amino-acid oxidase activity [GO:0003884]; FAD binding [GO:0071949]
|
PF01266;
|
3.30.9.10;3.40.50.720;
|
DAMOX/DASOX family
|
PTM: Phosphorylated in the cerebellum; probably not by PRKACA, PRKCA or PRKCE. {ECO:0000250|UniProtKB:P14920}.; PTM: May be S-nitrosylated, which partially inactivates the enzyme. {ECO:0000250|UniProtKB:P14920}.
|
SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000250|UniProtKB:P18894}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P14920}. Presynaptic active zone {ECO:0000250|UniProtKB:O35078}. Secreted {ECO:0000250|UniProtKB:P18894}. Note=Transiently present in the cytosol before being delivered to the peroxisomes (By similarity). In the cerebellum, a fraction of protein localizes to the presynaptic active zone, where its activity is regulated by protein BSN (By similarity). Secreted into the lumen of the small intestine (By similarity). {ECO:0000250|UniProtKB:O35078, ECO:0000250|UniProtKB:P14920, ECO:0000250|UniProtKB:P18894}.
|
CATALYTIC ACTIVITY: Reaction=a D-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 + NH4(+); Xref=Rhea:RHEA:21816, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179, ChEBI:CHEBI:59871; EC=1.4.3.3; Evidence={ECO:0000250|UniProtKB:P18894}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21817; Evidence={ECO:0000250|UniProtKB:P18894}; CATALYTIC ACTIVITY: Reaction=D-alanine + H2O + O2 = H2O2 + NH4(+) + pyruvate; Xref=Rhea:RHEA:22688, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:57416; Evidence={ECO:0000250|UniProtKB:P18894}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22689; Evidence={ECO:0000250|UniProtKB:P18894}; CATALYTIC ACTIVITY: Reaction=D-cysteine + H2O + O2 = 2-oxo-3-sulfanylpropanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:78791, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35236, ChEBI:CHEBI:57678; Evidence={ECO:0000250|UniProtKB:P14920}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78792; Evidence={ECO:0000250|UniProtKB:P14920}; CATALYTIC ACTIVITY: Reaction=D-dopa + H2O + O2 = 3-(3,4-dihydroxyphenyl)pyruvate + H2O2 + NH4(+); Xref=Rhea:RHEA:70971, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:29055, ChEBI:CHEBI:149689; Evidence={ECO:0000250|UniProtKB:P14920}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70972; Evidence={ECO:0000250|UniProtKB:P14920}; CATALYTIC ACTIVITY: Reaction=D-leucine + H2O + O2 = 4-methyl-2-oxopentanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:78211, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17865, ChEBI:CHEBI:28938, ChEBI:CHEBI:143079; Evidence={ECO:0000250|UniProtKB:P18894}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78212; Evidence={ECO:0000250|UniProtKB:P18894}; CATALYTIC ACTIVITY: Reaction=D-lysine + H2O + O2 = 6-amino-2-oxohexanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:37583, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:32557, ChEBI:CHEBI:58183; EC=1.4.3.3; Evidence={ECO:0000250|UniProtKB:P00371}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37584; Evidence={ECO:0000250|UniProtKB:P00371}; CATALYTIC ACTIVITY: Reaction=D-methionine + H2O + O2 = 4-methylsulfanyl-2-oxobutanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:78207, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16723, ChEBI:CHEBI:28938, ChEBI:CHEBI:57932; Evidence={ECO:0000250|UniProtKB:P00371}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78208; Evidence={ECO:0000250|UniProtKB:P00371}; CATALYTIC ACTIVITY: Reaction=D-phenylalanine + H2O + O2 = 3-phenylpyruvate + H2O2 + NH4(+); Xref=Rhea:RHEA:70963, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:18005, ChEBI:CHEBI:28938, ChEBI:CHEBI:57981; Evidence={ECO:0000250|UniProtKB:P18894}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70964; Evidence={ECO:0000250|UniProtKB:P18894}; CATALYTIC ACTIVITY: Reaction=D-proline + O2 = 1-pyrroline-2-carboxylate + H2O2; Xref=Rhea:RHEA:78259, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:39785, ChEBI:CHEBI:57726; Evidence={ECO:0000250|UniProtKB:P14920}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78260; Evidence={ECO:0000250|UniProtKB:P14920}; CATALYTIC ACTIVITY: Reaction=D-serine + H2O + O2 = 3-hydroxypyruvate + H2O2 + NH4(+); Xref=Rhea:RHEA:70951, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17180, ChEBI:CHEBI:28938, ChEBI:CHEBI:35247; Evidence={ECO:0000250|UniProtKB:P18894}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70952; Evidence={ECO:0000250|UniProtKB:P18894}; CATALYTIC ACTIVITY: Reaction=D-tryptophan + H2O + O2 = H2O2 + indole-3-pyruvate + NH4(+); Xref=Rhea:RHEA:78247, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17640, ChEBI:CHEBI:28938, ChEBI:CHEBI:57719; Evidence={ECO:0000250|UniProtKB:P18894}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78248; Evidence={ECO:0000250|UniProtKB:P18894}; CATALYTIC ACTIVITY: Reaction=D-valine + H2O + O2 = 3-methyl-2-oxobutanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:78203, ChEBI:CHEBI:11851, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:74338; Evidence={ECO:0000250|UniProtKB:P18894}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:78204; Evidence={ECO:0000250|UniProtKB:P18894};
| null | null | null | null |
FUNCTION: Catalyzes the oxidative deamination of D-amino acids with broad substrate specificity. Required to catabolize D-amino acids synthesized endogenously, of gastrointestinal bacterial origin or obtained from the diet, and to use these as nutrients. Regulates the level of D-amino acid neurotransmitters in the brain, such as D-serine, a co-agonist of N-methyl D-aspartate (NMDA) receptors, and may modulate synaptic transmission. Catalyzes the first step of the racemization of D-DOPA to L-DOPA, for possible use in an alternative dopamine biosynthesis pathway. Also catalyzes the first step of the chiral inversion of N(gamma)-nitro-D-arginine methyl ester (D-NNA) to its L-enantiomer L-NNA that acts as a nitric oxide synthase inhibitor. The hydrogen peroxide produced in the reaction provides protection against microbial infection; it contributes to the oxidative killing activity of phagocytic leukocytes and protects against bacterial colonization of the small intestine. Enzyme secreted into the lumen of the intestine may not be catalytically active and could instead be proteolytically cleaved into peptides with antimicrobial activity (By similarity). The hydrogen peroxide produced in the reaction may also play a role in promoting cellular senescence in response to DNA damage (By similarity). Could act as a detoxifying agent which removes D-amino acids accumulated during aging (By similarity). {ECO:0000250|UniProtKB:O35078, ECO:0000250|UniProtKB:P14920, ECO:0000250|UniProtKB:P18894}.
|
Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
|
A2VBC4
|
PA1_POLPI
|
MNFKYSILFICFGTLDRGLIPECPFNEYDILFFVYTRQQRDGIVLTEETLQNYDLFKKSTISRQVVFIDHGFLSNGNNENFIAMAKALIEKDNFLVISVDWKKGACNAFASTLDYLGYSTAVGNTRHVGKYVADFTKLLVEQYKVSMSNIRLIGHSLGAHTSGFAGKEVQELKLNKYSNIDGLDPAGPSFDSNDCPERLCETDAEYVQIIHTSNILGVYSKIGTVDFYMNYGSHQPGCGRFFSPSCSHTKAVKYLTECIKHECCLIGTPWKKYFSTPKPISQCTKDTCVCVGLNAKSYPARGSFYVPVEATAPYCHNEGIKL
|
3.1.1.32
| null |
killing of cells of another organism [GO:0031640]; lipid catabolic process [GO:0016042]
|
extracellular region [GO:0005576]
|
1-acyl-2-lysophosphatidylserine acylhydrolase activity [GO:0052740]; phosphatidylserine 1-acylhydrolase activity [GO:0052739]; phospholipase A1 activity [GO:0008970]
|
PF00151;
|
3.40.50.1820;
|
AB hydrolase superfamily, Lipase family
|
PTM: Contains six disulfide bonds. {ECO:0000269|PubMed:17761205}.; PTM: Is not glycosylated. {ECO:0000269|PubMed:17761205}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17761205}.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32; Evidence={ECO:0000269|PubMed:17761205};
| null | null | null | null |
FUNCTION: Catalyzes the hydrolysis of phosphatidylcholine with phospholipase A1 activity (PubMed:17761205). Shows hemolytic activity (PubMed:17761205). Acts as an allergen (PubMed:17761205). {ECO:0000269|PubMed:17761205}.
|
Polybia paulista (Neotropical social wasp) (Swarm-founding polistine wasp)
|
A2VCW5
|
S38A5_RAT
|
MAISCAVGMEMQEPKMNGTLSTGAAAGYRQEREGFLPTTHGPAPGRKPVQFLDFEGKTSFGMSVFNLSNAIMGSGILGLAYAMAHTGVIFFLALLLCIALLSSYSIHLLLTCASVVGIRAYEQLGQRAFGPAGKVVVAIIICLHNVGAMSSYLFIIKSELPLVIGTFLHMDPEGDWFLKGNLLIILVSLLIILPLALMKHLGYLGYTSSLSLTCMLFFLISVIYKKFQLGCVVSHNDTVVESEPAPLQAFNSSCEAKLFTVDSQMSYTVPIMAFAFVCHPEVLPIYTELCCPTQRRMQAVANMSIGAMFIMYGLTATFGYLTFYSTVKAEMLEMYTQEDLLILCVRLAVLLAVTLTVPVVLFPIRRALQQLLFPSKAFSWPRHVAIALILLILVNILVICVPTIRDIFGFIGSTSAPSLIFILPSVFYLRIVPADMEPLFSWPKIQALCFGVLGVLFMAISLGFMFANWATGQSRMSGH
| null | null |
amino acid export across plasma membrane [GO:0032973]; amino acid import across plasma membrane [GO:0089718]; asparagine transmembrane transport [GO:1903713]; glutamine transport [GO:0006868]; glycine transport [GO:0015816]; L-alanine transmembrane transport [GO:1904557]; L-glutamine import across plasma membrane [GO:1903803]; L-histidine transmembrane transport [GO:0089709]; L-serine import across plasma membrane [GO:1903812]; L-serine transport [GO:0015825]; neutral amino acid transport [GO:0015804]; serine transport [GO:0032329]
|
plasma membrane [GO:0005886]
|
alanine transmembrane transporter activity [GO:0022858]; amino acid transmembrane transporter activity [GO:0015171]; glycine transmembrane transporter activity [GO:0015187]; L-asparagine transmembrane transporter activity [GO:0015182]; L-glutamine transmembrane transporter activity [GO:0015186]; L-glutamine, sodium:proton antiporter activity [GO:0140830]; L-histidine transmembrane transporter activity [GO:0005290]; L-serine transmembrane transporter activity [GO:0015194]; neutral amino acid, sodium:proton antiporter activity [GO:0140893]; neutral L-amino acid transmembrane transporter activity [GO:0015175]
|
PF01490;
| null |
Amino acid/polyamine transporter 2 family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15390093, ECO:0000269|PubMed:22821889}; Multi-pass membrane protein {ECO:0000255}. Note=Localized at astroglial membrane. {ECO:0000269|PubMed:22821889}.
|
CATALYTIC ACTIVITY: Reaction=H(+)(in) + L-serine(out) + Na(+)(out) = H(+)(out) + L-serine(in) + Na(+)(in); Xref=Rhea:RHEA:71159, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:33384; Evidence={ECO:0000269|PubMed:11698233, ECO:0000269|PubMed:15218073, ECO:0000269|PubMed:16629640, ECO:0000269|PubMed:22821889}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71160; Evidence={ECO:0000269|PubMed:11698233, ECO:0000305|PubMed:15218073, ECO:0000305|PubMed:16629640}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71161; Evidence={ECO:0000305|PubMed:15218073}; CATALYTIC ACTIVITY: Reaction=H(+)(in) + L-alanine(out) + Na(+)(out) = H(+)(out) + L-alanine(in) + Na(+)(in); Xref=Rhea:RHEA:71163, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:57972; Evidence={ECO:0000269|PubMed:11698233, ECO:0000269|PubMed:22821889}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71164; Evidence={ECO:0000269|PubMed:11698233}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71165; Evidence={ECO:0000305|PubMed:15218073}; CATALYTIC ACTIVITY: Reaction=glycine(out) + H(+)(in) + Na(+)(out) = glycine(in) + H(+)(out) + Na(+)(in); Xref=Rhea:RHEA:71167, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:57305; Evidence={ECO:0000269|PubMed:11698233, ECO:0000269|PubMed:22821889}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71168; Evidence={ECO:0000269|PubMed:11698233, ECO:0000269|PubMed:22821889}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71169; Evidence={ECO:0000269|PubMed:22821889, ECO:0000305|PubMed:15218073}; CATALYTIC ACTIVITY: Reaction=H(+)(in) + L-glutamine(out) + Na(+)(out) = H(+)(out) + L-glutamine(in) + Na(+)(in); Xref=Rhea:RHEA:71127, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:58359; Evidence={ECO:0000269|PubMed:11698233, ECO:0000269|PubMed:15218073, ECO:0000269|PubMed:16249471, ECO:0000269|PubMed:22821889}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71128; Evidence={ECO:0000269|PubMed:11698233, ECO:0000269|PubMed:15218073, ECO:0000269|PubMed:22821889}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71129; Evidence={ECO:0000269|PubMed:15218073, ECO:0000269|PubMed:22821889}; CATALYTIC ACTIVITY: Reaction=H(+)(in) + L-asparagine(out) + Na(+)(out) = H(+)(out) + L-asparagine(in) + Na(+)(in); Xref=Rhea:RHEA:71131, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:58048; Evidence={ECO:0000269|PubMed:11698233, ECO:0000269|PubMed:22821889}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71132; Evidence={ECO:0000269|PubMed:11698233}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71133; Evidence={ECO:0000305|PubMed:15218073}; CATALYTIC ACTIVITY: Reaction=H(+)(in) + L-histidine(out) + Na(+)(out) = H(+)(out) + L-histidine(in) + Na(+)(in); Xref=Rhea:RHEA:71135, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:57595; Evidence={ECO:0000269|PubMed:11698233, ECO:0000269|PubMed:15218073}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71136; Evidence={ECO:0000269|PubMed:11698233, ECO:0000305|PubMed:15218073}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71137; Evidence={ECO:0000305|PubMed:15218073}; CATALYTIC ACTIVITY: Reaction=H(+)(in) + L-cysteine(out) + Na(+)(out) = H(+)(out) + L-cysteine(in) + Na(+)(in); Xref=Rhea:RHEA:71171, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:35235; Evidence={ECO:0000269|PubMed:22821889}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71172; Evidence={ECO:0000269|PubMed:22821889}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71173; Evidence={ECO:0000305|PubMed:22821889};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.92 mM for L-serine (at pH 8.0) {ECO:0000269|PubMed:16629640}; KM=0.99 mM for L-glutamine influx (at pH 8.0) {ECO:0000269|PubMed:15218073}; KM=0.73 mM for L-serine (at pH 8.0) {ECO:0000269|PubMed:15218073}; KM=0.21 mM for L-histidine (at pH 8.0) {ECO:0000269|PubMed:15218073}; KM=1.2 mM for L-glutamine efflux (at pH 8.0) {ECO:0000269|PubMed:15218073}; KM=7.1 mM for glycine {ECO:0000269|PubMed:22821889}; KM=1.2 mM for L-glutamine {ECO:0000269|PubMed:22821889}; KM=76.7 mM for sodium ion {ECO:0000269|PubMed:22821889}; Vmax=192 nmol/min/mg enzyme toward glycine (at (-) 80 mV) {ECO:0000269|PubMed:22821889}; Vmax=87 nmol/min/mg enzyme toward L-glutamine (at (-) 80 mV) {ECO:0000269|PubMed:22821889};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:15218073, ECO:0000269|PubMed:16249471};
| null |
FUNCTION: Symporter that cotransports neutral amino acids and sodium ions, coupled to an H(+) antiporter activity (PubMed:11698233, PubMed:15218073, PubMed:16249471, PubMed:16629640, PubMed:22821889). Releases L-glutamine and glycine from astroglial cells and may participate in the glutamate/GABA-glutamine cycle and the NMDA receptors activation (PubMed:22821889). In addition contributes significantly to L-glutamine uptake in retina, namely in ganglion and Mueller cells and, therefore participates in the retinal glutamate-glutamine cycle (PubMed:16249471). The transport activity is pH sensitive (PubMed:22821889, PubMed:15218073, PubMed:11698233), Li(+) tolerant (PubMed:22821889, PubMed:15218073, PubMed:11698233), bidirectional (PubMed:22821889, PubMed:15218073) and associated with large uncoupled fluxes of protons (PubMed:11698233, PubMed:15218073, PubMed:22821889). The transport is electroneutral coupled to the cotransport of 1 Na(+) and the antiport of 1 H(+) (PubMed:22821889). May have particular importance for modulation of net hepatic glutamine flux (PubMed:15218073). {ECO:0000269|PubMed:11698233, ECO:0000269|PubMed:15218073, ECO:0000269|PubMed:16249471, ECO:0000269|PubMed:16629640, ECO:0000269|PubMed:22821889}.
|
Rattus norvegicus (Rat)
|
A2VD12
|
PBIP1_RAT
|
MASCPDSDNSWVLAGSETLPVETLGPESRVDPESEEAPQALQDSSKADGKESAGTLNGEEMLFQTESSQGEGAALPEESEAKGALGGDDGHGTKRPGDTAVQEDLQETPMVTSLGPDTQDLERNIHPQNLPSSPRAVWKEHGCSSSDDDTDVDVEGLRRRRGREPSPPQPTAAVDGEDQAKGEGIGELGISLNMCFLGALVLLGLGILLFSGALLEPETEPVEEAELQVFPETELVQTVGNRQDEVEQLQASVPPDSVPSLQSMGLLLDKLAKENQDIRLLQAQLQAQKEELQSLLHQPKGLEEENARLREALQQGKTSHQALESELQQLRARLQGLEANCVRGVDGVCLNWGGSPQGGKATTEQGHKGQEPDTSLLEQHKQLEAEAKALRQELQKQWQLLGSVHRNLQRGLQDAGQGAPAHAGLAELGHMLAQTLQGLESQGINTGRSSNDSEAWHQKKPRFQHPREWSGREKWRGGQRDQKAEHWKLKKEESGQDRKKSWRDEGREFTGHWKENRPRAEESGSRKDSKRQDPKVHPRKSGNSHSGERQKHSWGKDNSPDSVSWEELLRRKYRPPQGCSGVADCARQEGLALFGVELAPVRQQELASVLREYLARLPWAGQLTKELPLSPAYFGEDGIFRHDRLRFRDFVDALEDSLEEVALKQTGDDDEVDDFEDFIFSHFFGDKALKRRSKKKEKQPWNHRAVGPREEHSRHPHHYHQG
| null | null |
articular cartilage development [GO:0061975]; cell adhesion [GO:0007155]; cell migration [GO:0016477]; extracellular matrix disassembly [GO:0022617]; gene expression [GO:0010467]; gene expression involved in extracellular matrix organization [GO:1901148]; hemopoiesis [GO:0030097]; negative regulation of DNA-templated transcription [GO:0045892]; positive regulation of chondrocyte proliferation [GO:1902732]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of Wnt signaling pathway [GO:0030177]; production of molecular mediator involved in inflammatory response [GO:0002532]
|
chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; microtubule [GO:0005874]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667]
|
DNA-binding transcription factor binding [GO:0140297]; transcription coactivator activity [GO:0003713]; transcription corepressor activity [GO:0003714]
| null | null | null | null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q96AQ6}. Nucleus {ECO:0000250|UniProtKB:Q96AQ6}. Note=Shuttles between the nucleus and the cytosol. Mainly localized in the cytoplasm, associated with microtubules. Detected in small amounts in the nucleus. {ECO:0000250|UniProtKB:Q96AQ6}.
| null | null | null | null | null |
FUNCTION: Regulator of pre-B-cell leukemia transcription factors (BPXs) function. Inhibits the binding of PBX1-HOX complex to DNA and blocks the transcriptional activity of E2A-PBX1. Tethers estrogen receptor-alpha (ESR1) to microtubules and allows them to influence estrogen receptors-alpha signaling (By similarity). {ECO:0000250}.
|
Rattus norvegicus (Rat)
|
A2VD92
|
DDX1_XENLA
|
MAAFSEMGVMPEIAQAVEEMDWLLPTDIQAESIPLILGGGDVLMAAETGSGKTGAFSIPVIQIVYETLKDQQEGKKGKASVKTGSTVLNKWQMNPYDRGSAFAIGSDGLCCQSREIKEWHGCRSTRGVNKGKYYYEVSCHDQGLCRVGWSTLSASLDLGTDKFGFGFGGTGKKSHNKQFDNYGEEFTMHDTIGCYLDIDNSIVKFSKNGKDLGLAFQIPSHMKNQAFFTSCVLKNAELKFNFGEEDFKFPPKDGFVALSKAPDGHVVKSQNTGSAQVSQTKSLPNAPKALIIEPSRELAEQTLNNVKQFKKYVDNPKLRELLIIGGVAAKEQLTILENGVDIVVGTPGRIDDLISTGKLSLSQVRFLVLDEADGLLSQGYSDFINRIYGQIPQITSDGKRLQVIVCSATLHSFDVKKLSEKIMHFPTWVDLKGEDSVPETVHHVVVPVNPKKDKQWEKLAKNHIRTDGVHDKDNTRPGGNSAEVWSEAIKVLKGEYIVRAIKEHKMDQAIIFCRTKLDCDNMEQYFIQQGGGPDKKGHQFSCVCLHSDRKPPERKHNLERFKKCEVRFLICTDVAARGIDIRGVPYVINVTLPDEKQNYVHRIGRVGRAERMGLAISLVASEKEKVWYHVCSSRGKGCYNTRLKEDGGCTIWYNEMQLLSEIEEHLTCTISQVEPDIKVPLDDFDGKVVYGQRRATGGGLYKGHVDILAPTVQELASLEKEAQTSFLHLGYLSNQLFRSF
|
3.6.4.13
| null |
DNA duplex unwinding [GO:0032508]; double-strand break repair [GO:0006302]; mRNA processing [GO:0006397]; rRNA processing [GO:0006364]; tRNA splicing, via endonucleolytic cleavage and ligation [GO:0006388]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleolus [GO:0005730]; nucleus [GO:0005634]; tRNA-splicing ligase complex [GO:0072669]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA/RNA helicase activity [GO:0033677]; exonuclease activity [GO:0004527]; nuclease activity [GO:0004518]; poly(A) binding [GO:0008143]; RNA helicase activity [GO:0003724]; transcription coregulator activity [GO:0003712]
|
PF00270;PF00271;PF00622;
|
2.60.120.920;3.40.50.300;
|
DEAD box helicase family, DDX1 subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92499}. Cytoplasm {ECO:0000250|UniProtKB:Q92499}. Cytoplasmic granule {ECO:0000250|UniProtKB:Q92499}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q91VR5}. Mitochondrion {ECO:0000250|UniProtKB:Q91VR5}.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
| null | null | null | null |
FUNCTION: Acts as an ATP-dependent RNA helicase, able to unwind both RNA-RNA and RNA-DNA duplexes. Possesses 5' single-stranded RNA overhang nuclease activity. Acts as a positive regulator of transcription. May be involved in 3'-end cleavage and polyadenylation of pre-mRNAs. Binds DNA and RNA. Component of the tRNA-splicing ligase complex required to facilitate the enzymatic turnover of catalytic subunit rtcb (By similarity). Binds (via helicase ATP-binding domain) on both short and long poly(I:C) dsRNA (By similarity). {ECO:0000250|UniProtKB:Q91VR5, ECO:0000250|UniProtKB:Q92499}.
|
Xenopus laevis (African clawed frog)
|
A2VDJ0
|
T131L_HUMAN
|
MAGLRRPQPGCYCRTAAAVNLLLGVFQVLLPCCRPGGAQGQAIEPLPNVVELWQAEEGELLLPTQGDSEEGLEEPSQEQSFSDKLFSGKGLHFQPSVLDFGIQFLGHPVAKILHAYNPSRDSEVVVNSVFAAAGHFHVPPVPCRVIPAMGKTSFRIIFLPTEEGSIESSLFINTSSYGVLSYHVSGIGTRRISTEGSAKQLPNAYFLLPKVQSIQLSQMQAETTNTSLLQVQLECSLHNKVCQQLKGCYLESDDVLRLQMSIMVTMENFSKEFEENTQHLLDHLSIVYVATDESETSDDSAVNMYILHSGNSLIWIQDIRHFSQRDALSLQFEPVLLPTSTTNFTKIASFTCKATSCDSGIIEDVKKTTHTPTLKACLFSSVAQGYFRMDSSATQFHIETHENTSGLWSIWYRNHFDRSVVLNDVFLSKETKHMLKILNFTGPLFLPPGCWNIFSLKLAVKDIAINLFTNVFLTTNIGAIFAIPLQIYSAPTKEGSLGFEVIAHCGMHYFMGKSKAGNPNWNGSLSLDQSTWNVDSELANKLYERWKKYKNGDVCKRNVLGTTRFAHLKKSKESESFVFFLPRLIAEPGLMLNFSATALRSRMIKYFVVQNPSSWPVSLQLLPLSLYPKPEALVHLLHRWFGTDMQMINFTTGEFQLTEACPYLGTHSEESRFGILHLHLQPLEMKRVGVVFTPADYGKVTSLILIRNNLTVIDMIGVEGFGARELLKVGGRLPGAGGSLRFKVPESTLMDCRRQLKDSKQILSITKNFKVENIGPLPITVSSLKINGYNCQGYGFEVLDCHQFSLDPNTSRDISIVFTPDFTSSWVIRDLSLVTAADLEFRFTLNVTLPHHLLPLCADVVPGPSWEESFWRLTVFFVSLSLLGVILIAFQQAQYILMEFMKTRQRQNASSSSQQNNGPMDVISPHSYKSNCKNFLDTYGPSDKGRGKNCLPVNTPQSRIQNAAKRSPATYGHSQKKHKCSVYYSKHKTSTAAASSTSTTTEEKQTSPLGSSLPAAKEDICTDAMRENWISLRYASGINVNLQKNLTLPKNLLNKEENTLKNTIVFSNPSSECSMKEGIQTCMFPKETDIKTSENTAEFKERELCPLKTSKKLPENHLPRNSPQYHQPDLPEISRKNNGNNQQVPVKNEVDHCENLKKVDTKPSSEKKIHKTSREDMFSEKQDIPFVEQEDPYRKKKLQEKREGNLQNLNWSKSRTCRKNKKRGVAPVSRPPEQSDLKLVCSDFERSELSSDINVRSWCIQESTREVCKADAEIASSLPAAQREAEGYYQKPEKKCVDKFCSDSSSDCGSSSGSVRASRGSWGSWSSTSSSDGDKKPMVDAQHFLPAGDSVSQNDFPSEAPISLNLSHNICNPMTVNSLPQYAEPSCPSLPAGPTGVEEDKGLYSPGDLWPTPPVCVTSSLNCTLENGVPCVIQESAPVHNSFIDWSATCEGQFSSAYCPLELNDYNAFPEENMNYANGFPCPADVQTDFIDHNSQSTWNTPPNMPAAWGHASFISSPPYLTSTRSLSPMSGLFGSIWAPQSDVYENCCPINPTTEHSTHMENQAVVCKEYYPGFNPFRAYMNLDIWTTTANRNANFPLSRDSSYCGNV
| null | null |
negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of immature T cell proliferation in thymus [GO:0033088]; Wnt signaling pathway [GO:0016055]
|
cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; plasma membrane [GO:0005886]
| null |
PF19532;PF12371;
|
2.60.40.10;
|
TMEM131 family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23690469}; Single-pass type I membrane protein {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:23690469}. Note=During intrathymic development, resides in punctate cytoplasmic structures in DN1 and DN2 cells. In DN3 cells, found in large crescent-shaped membrane structures, which preferentially localize in cell-to-cell contact zones. {ECO:0000269|PubMed:23690469}.; SUBCELLULAR LOCATION: [Isoform 1]: Endoplasmic reticulum {ECO:0000269|PubMed:23690469}. Note=Transmembrane localization is essential for Wnt signaling inhibition. {ECO:0000269|PubMed:23690469}.; SUBCELLULAR LOCATION: [Isoform 5]: Cytoplasm {ECO:0000269|PubMed:23690469}. Note=Scattered throughout the cytoplasm in small-sized punctate structures. {ECO:0000269|PubMed:23690469}.
| null | null | null | null | null |
FUNCTION: [Isoform 1]: Membrane-associated form that antagonizes canonical Wnt signaling by triggering lysosome-dependent degradation of Wnt-activated LRP6. Regulates thymocyte proliferation. {ECO:0000269|PubMed:23690469}.
|
Homo sapiens (Human)
|
A2VDL6
|
AT1A2_BOVIN
|
MGRGAGREYSPAATTAENGGGKKKQKEKELDELKKEVAMDDHKLSLDELGRKYQVDLSKGLTNQRAQDILARDGPNALTPPPTTPEWVKFCRQLFGGFSILLWIGAILCFLAFGIQAAMEDEPSNDNLYLGVVLAAVVIVTGCFSYYQEAKSSKIMDSFKNMVPQQALVVREGEKMQINAEEVVVGDLVEVKGGDRVPADLRIISSHGCKVDNSSLTGESEPQTRSPEFTHENPLETRNICFFSTNCVEGTARGIVIATGDRTVMGRIATLASGLEVGRTPIAMEIEHFIQLITGVAVFLGVSFFVLSLILGYSWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTEDQSGATFDKRSPTWTALSRIAGLCNRAVFKAGQENISVSKRDTAGDASESALLKCIELSCGSVRKMRDRNPKVAEIPFNSTNKYQLSIHEREDSPQSHVLVMKGAPERILDRCSSILVQGKEIPLDKEMQDAFQNAYLELGGLGERVLGFCQLNLPSAKFPRGFKFDTDELNFPTEKLCFVGLMSMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPVSQVNPREAKACVVHGSDLKDMTSEQLDEILKNHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGIAMGIAGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPFLLFIIANIPLPLGTVTILCIDLGTDMVPAISLAYEAAESDIMKRQPRNPQTDKLVNERLISMAYGQIGMIQALGGFFTYFVILAENGFLPSRLLGIRLDWDDRSMNDLEDSYGQEWTYEQRKVVEFTCHTAFFASIVVVQWADLIICKTRRNSVFQQGMKNKILIFGLLEETALAAFLSYCPGMGVALRMYPLKVTWWFCAFPYSLLIFIYDEVRKLILRRYPGGWVEKETYY
|
7.2.2.13
| null |
intracellular potassium ion homeostasis [GO:0030007]; intracellular sodium ion homeostasis [GO:0006883]; potassium ion import across plasma membrane [GO:1990573]; proton transmembrane transport [GO:1902600]; sodium ion export across plasma membrane [GO:0036376]
|
cell projection [GO:0042995]; plasma membrane [GO:0005886]; sodium:potassium-exchanging ATPase complex [GO:0005890]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; metal ion binding [GO:0046872]; P-type sodium:potassium-exchanging transporter activity [GO:0005391]
|
PF13246;PF00689;PF00690;PF00122;PF00702;
|
3.40.1110.10;2.70.150.10;1.20.1110.10;3.40.50.1000;
|
Cation transport ATPase (P-type) (TC 3.A.3) family, Type IIC subfamily
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O + K(+)(out) + Na(+)(in) = ADP + H(+) + K(+)(in) + Na(+)(out) + phosphate; Xref=Rhea:RHEA:18353, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:29103, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.13;
| null | null | null | null |
FUNCTION: This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium, providing the energy for active transport of various nutrients (By similarity). {ECO:0000250}.
|
Bos taurus (Bovine)
|
A2VDN5
|
SPAST_BOVIN
|
MNSPGGRGKKKGSGGPSSPVPPRPPPPCQARSRPAPKPAPPPQSPHKRNLYYFSYPLFLGFALLRLVAFHLGLLFVWLCQRFSRALMAAKRSSGAAPASASPPAPVPGGEAERVRAFHKQAFEYISVALRIDEDEKVGQKDQAVEWYKKGIEELEKGIAVVVTGQGEQCERARRLQAKMMTNLVMAKDRLQLLEKLQPSLQFSKSQTDVYNDSTNLTCRNGHLQSESGAVPKRKDPLTHASNSLPRSKTVMKTGPTGLSGHHRAPSCSGLSMVSGVRQGPGSAAATHKSTPKTNRTNKPSTPTTAARKKKDLKNFRNVDSNLANLIMNEIVDNGTAVKFDDIAGQELAKQALQEIVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDEVDSLLCERREGEHDASRRLKTEFLIEFDGVQSAGDDRVLVMGATNRPQELDEAVLRRFTKRVYVSLPNEETRLLLLKNLLCKQGSPLTQKELAQLARMTNGYSGSDLTALAKDAALGPIRELKPEQVKNMSASEMRNIRLSDFTESLKKIKRSVSPQTLEAYIRWNKDFGDTTV
|
5.6.1.1
| null |
anterograde axonal transport [GO:0008089]; axonal transport of mitochondrion [GO:0019896]; axonogenesis [GO:0007409]; cytokinetic process [GO:0032506]; endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; exit from mitosis [GO:0010458]; membrane fission [GO:0090148]; metabolic process [GO:0008152]; microtubule bundle formation [GO:0001578]; microtubule severing [GO:0051013]; mitotic cytokinesis [GO:0000281]; mitotic spindle disassembly [GO:0051228]; nuclear membrane reassembly [GO:0031468]; positive regulation of microtubule depolymerization [GO:0031117]; protein hexamerization [GO:0034214]; protein homooligomerization [GO:0051260]
|
axon [GO:0030424]; axon cytoplasm [GO:1904115]; centrosome [GO:0005813]; endoplasmic reticulum [GO:0005783]; endosome [GO:0005768]; microtubule [GO:0005874]; microtubule cytoskeleton [GO:0015630]; midbody [GO:0030496]; nuclear membrane [GO:0031965]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; spindle pole [GO:0000922]
|
alpha-tubulin binding [GO:0043014]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; beta-tubulin binding [GO:0048487]; isomerase activity [GO:0016853]; microtubule binding [GO:0008017]; microtubule severing ATPase activity [GO:0008568]
|
PF00004;PF17862;PF09336;
|
1.10.8.60;3.40.50.300;1.20.58.80;
|
AAA ATPase family, Spastin subfamily
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000255|HAMAP-Rule:MF_03021}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03021}. Endoplasmic reticulum {ECO:0000255|HAMAP-Rule:MF_03021}. Midbody {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, perinuclear region {ECO:0000255|HAMAP-Rule:MF_03021}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton, spindle {ECO:0000255|HAMAP-Rule:MF_03021}. Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03021}. Cell projection, axon {ECO:0000250|UniProtKB:Q9UBP0}. Note=Forms an intramembrane hairpin-like structure in the membrane. Localization to the centrosome is independent of microtubules. Localizes to the midbody of dividing cells, and this requires CHMP1B. Enriched in the distal axons and branches of postmitotic neurons. Localizes to endoplasmic reticulum tubular network. Mainly nuclear in interphase cells and becomes associated with the centrosomes, spindle microtubules, midzone and finally the midbody during cell division (By similarity). {ECO:0000250|UniProtKB:Q9UBP0, ECO:0000255|HAMAP-Rule:MF_03021}.
|
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_03021};
| null | null | null | null |
FUNCTION: ATP-dependent microtubule severing protein that specifically recognizes and cuts microtubules that are polyglutamylated. Preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold. Severing activity is not dependent on tubulin acetylation or detyrosination. Microtubule severing promotes reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. It is critical for the biogenesis and maintenance of complex microtubule arrays in axons, spindles and cilia. SPAST is involved in abscission step of cytokinesis and nuclear envelope reassembly during anaphase in cooperation with the ESCRT-III complex. Recruited at the midbody, probably by IST1, and participates in membrane fission during abscission together with the ESCRT-III complex. Recruited to the nuclear membrane by IST1 and mediates microtubule severing, promoting nuclear envelope sealing and mitotic spindle disassembly during late anaphase. Required for membrane traffic from the endoplasmic reticulum (ER) to the Golgi and endosome recycling. Recruited by IST1 to endosomes and regulates early endosomal tubulation and recycling by mediating microtubule severing. Probably plays a role in axon growth and the formation of axonal branches. {ECO:0000255|HAMAP-Rule:MF_03021}.
|
Bos taurus (Bovine)
|
A2VDP1
|
BRE1A_BOVIN
|
MSGIGSKRAAGEPGTSVPPEKKTAVEDSGTTVETIKLGGVSSTEELDIRTLQTKNRKLAEMLDQRQAIEDELREHIEKLERRQATDDASLLIVNRYWSQFDENIRIILKRYDLEQGLGDLLTERKALVVPEPEPDSDSNQERKDDRERGEGQEPAFSFLATLASSSSEEMESQLQERVESSRRAVSQIVTVYDKLQEKVELLSRKLNSGDSLMVEEAVQELNSFLAQENTRLQELTDLLQEKHCTMSQEFSKLQSKVETAESRVSVLESMIDDLQWDIDKIRKREQRLNRHLAEVLERVNSKGYKVYGAGSSLYGGTITINARKFEEMNAELEENKELAQNRHCELEKLRQDFEEVTSQNEKLKVELRSAVEEVVKETPEYRCMQSQFSVLYNESLQLKAHLDEARTLLHGTRGTHQRQVELIERDEVSLHKKLRTEVIQLEDTLAQVRKEYEMLRIEFEQTLAANEQAGPINREMRHLISSLQNHNHQLKGEVLRYKRKLREAQSDLNKTRLRSGSALLQSQSSTEDPKDEPAELKQDSEDLATQSAASKASQEEVNEIKSKRDEEERERERREKEREREREREKEKEREREKQKLKESEKERESAKDKEKGKHDDGRKKEAEIIKQLKIELKKAQESQKEMKLLLDMYRSAPKEQRDKVQLMAAEKKSKAELEDLRQRLKDLEDKEKKENKKMADEDALRKIRAVEEQIEYLQKKLAMAKQEEEALLSEMDVTGQAFEDMQEQNIRLMQQLREKDDANFKLMSERIKSNQIHKLLKEEKEELADQVLTLKTQVDAQLQVVRKLEEKEHLLQSNIGTGEKELGLRTQALEMNKRKAMEAAQLADDLKAQLEMAQKKLHDFQDEIVENSVTKEKDMFNFKRAQEDISRLRRKLETTKKPDNVPKCDEILMEEIKDYKARLTCPCCNMRKKDAVLTKCFHVFCFECVKTRYDTRQRKCPKCNAAFGANDFHRIYIG
|
2.3.2.27
| null |
chromatin organization [GO:0006325]; negative regulation of cell migration [GO:0030336]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein polyubiquitination [GO:0000209]; regulation of DNA-templated transcription [GO:0006355]; ubiquitin-dependent protein catabolic process [GO:0006511]
|
HULC complex [GO:0033503]; nucleolus [GO:0005730]; nucleus [GO:0005634]; ubiquitin ligase complex [GO:0000151]
|
histone binding [GO:0042393]; metal ion binding [GO:0046872]; p53 binding [GO:0002039]; transcription coactivator activity [GO:0003713]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin protein ligase binding [GO:0031625]
|
PF00097;
|
1.20.1170.10;3.30.40.10;
|
BRE1 family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q5VTR2}.
|
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; Evidence={ECO:0000250|UniProtKB:Q5VTR2};
| null |
PATHWAY: Protein modification; protein ubiquitination.
| null | null |
FUNCTION: Component of the RNF20/40 E3 ubiquitin-protein ligase complex that mediates monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1). H2BK120ub1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation (H3K4me and H3K79me, respectively). It thereby plays a central role in histone code and gene regulation. The RNF20/40 complex forms a H2B ubiquitin ligase complex in cooperation with the E2 enzyme UBE2A or UBE2B; reports about the cooperation with UBE2E1/UBCH are contradictory. Required for transcriptional activation of Hox genes. Recruited to the MDM2 promoter, probably by being recruited by p53/TP53, and thereby acts as a transcriptional coactivator. Mediates the polyubiquitination of PA2G4 leading to its proteasome-mediated degradation. {ECO:0000250|UniProtKB:Q5VTR2}.
|
Bos taurus (Bovine)
|
A2VDU3
|
M3K7_BOVIN
|
MSTASAASSSSSSSAGEMIEAPSQVLNFEEIDYKEIEVEEVVGRGAFGVVCKAKWRAKDVAIKQIESESERKAFIVELRQLSRVNHPNIVKLYGACLNPVCLVMEYAEGGSLYNVLHGAEPLPYYTAAHAMSWCLQCSQGVAYLHSMQPKALIHRDLKPPNLLLVAGGTVLKICDFGTACDIQTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAFRIMWAVHNGTRPPLIKNLPKPIESLMTRCWSKDPSQRPSMEEIVKIMTHLMRYFPGADEPLQYPCQYSDEGQSNSATSTGSFMDITSTNTSNKSDTNMEQVPATNDTIKRLESKLLKNQAKQQSESGRLSLGASRGSSVESLPPTSEGKRMSADMSEIEARIAATTGNGQPRRRSIQDLTVTGTDPGQVSSRSSSPSVRMITTSGPTSEKPARSHPWTPDDSTDTNGSDNSIPMAYLTLDHQLQPLAPCPNSKESMAVFEQHCKMAQEYMKVQTEIALLLQRKQELVAELDQDEKDQQNTSRLVQEHKKLLDENKSLSTYYQQCKKQLEVIRSQQQKRQGTS
|
2.7.11.25
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O43318};
|
apoptotic process [GO:0006915]; I-kappaB phosphorylation [GO:0007252]; immune response [GO:0006955]; JNK cascade [GO:0007254]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of JUN kinase activity [GO:0043507]
|
cytoplasm [GO:0005737]; plasma membrane [GO:0005886]
|
ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; MAP kinase kinase kinase activity [GO:0004709]; protein serine kinase activity [GO:0106310]
|
PF07714;
|
1.10.510.10;
|
Protein kinase superfamily, STE Ser/Thr protein kinase family, MAP kinase kinase kinase subfamily
|
PTM: Association with TAB1/MAP3K7IP1 promotes autophosphorylation at Ser-192 and subsequent activation. Association with TAB2/MAP3K7IP2, itself associated with free unanchored Lys-63 polyubiquitin chain, promotes autophosphorylation and subsequent activation of MAP3K7. Dephosphorylation at Ser-192 by PPM1B/PP2CB and at Thr-187 by PP2A and PPP6C leads to inactivation (By similarity). {ECO:0000250}.; PTM: 'Lys-48'-linked polyubiquitination at Lys-72 is induced by TNFalpha, and leads to proteasomal degradation. Undergoes 'Lys-48'-linked polyubiquitination catalyzed by ITCH. 'Lys-63'-linked polyubiquitination at Lys-158 by TRIM8 does not lead to proteasomal degradation but contributes to autophosphorylation and activation. Deubiquitinated by CYLD, a protease that selectively cleaves 'Lys-63'-linked ubiquitin chains. {ECO:0000250|UniProtKB:O43318, ECO:0000250|UniProtKB:Q62073}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Although the majority of MAP3K7/TAK1 is found in the cytosol, when complexed with TAB1/MAP3K7IP1 and TAB2/MAP3K7IP2, it is also localized at the cell membrane. {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.25; Evidence={ECO:0000250|UniProtKB:O43318}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.25; Evidence={ECO:0000250|UniProtKB:O43318};
| null | null | null | null |
FUNCTION: Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. Plays an important role in the cascades of cellular responses evoked by changes in the environment. Mediates signal transduction of TRAF6, various cytokines including interleukin-1 (IL-1), transforming growth factor-beta (TGFB), TGFB-related factors like BMP2 and BMP4, toll-like receptors (TLR), tumor necrosis factor receptor CD40 and B-cell receptor (BCR). Once activated, acts as an upstream activator of the MKK/JNK signal transduction cascade and the p38 MAPK signal transduction cascade through the phosphorylation and activation of several MAP kinase kinases like MAP2K1/MEK1, MAP2K3/MKK3, MAP2K6/MKK6 and MAP2K7/MKK7. These MAP2Ks in turn activate p38 MAPKs and c-jun N-terminal kinases (JNKs); both p38 MAPK and JNK pathways control the transcription factors activator protein-1 (AP-1). Independently of MAP2Ks and p38 MAPKs, acts as a key activator of NF-kappa-B by promoting activation of the I-kappa-B-kinase (IKK) core complex. Mechanistically, recruited to polyubiquitin chains of RIPK2 and IKBKG/NEMO via TAB2/MAP3K7IP2 and TAB3/MAP3K7IP3, and catalyzes phosphorylation and activation of IKBKB/IKKB component of the IKK complex, leading to NF-kappa-B activation. In osmotic stress signaling, plays a major role in the activation of MAPK8/JNK1, but not that of NF-kappa-B. Promotes TRIM5 capsid-specific restriction activity. Phosphorylates RIPK1 at 'Ser-321' which positively regulates RIPK1 interaction with RIPK3 to promote necroptosis but negatively regulates RIPK1 kinase activity and its interaction with FADD to mediate apoptosis. Phosphorylates STING1 in response to cGAMP-activation, promoting association between STEEP1 and STING1 and STING1 translocation to COPII vesicles. {ECO:0000250|UniProtKB:O43318, ECO:0000250|UniProtKB:Q62073}.
|
Bos taurus (Bovine)
|
A2VDZ3
|
MEF2A_BOVIN
|
MGRKKIQITRIMDERNRQVTFTKRKFGLMKKAYELSVLCDCEIALIIFNSSNKLFQYASTDMDKVLLKYTEYNEPHESRTNSDIVEALNKKEHRGCDSPDPDTSYVLTPHTEEKYKKINEEFDNMMRNHKIAPGLPPQNFSMSVTVPVTSPSALSYTNPGSSLVSPSLAASSALADTSMLSPPQATLHRNVSPGAPQRPPSTGSAGGMLSTSDLTVPNGAGSSPVGNGFVNSRASPNLIGTTGANSLGKVMPTKSPPPPGGGSLGMNSRKPDLRVVIPPSSKGMMPPLNTQRISSSQATQPLATPVVSVTTPSLPPQGLVYSAMPTAYNTDYSLTSADLSALQGFNSPGMLSLGQVSAWQQHHLGQAALNSLVAGGQLSQGSNLSINTNQNINIKSEPISPPRDRMTPSGFQQQQQPQPPPPPPQAPQPQPRQEVGRSPVDSLSSSSSSYDGSDREDPRGDFHSPVVLGRPPNSEDRESPSVKRMRMDAWVT
| null | null |
apoptotic process [GO:0006915]; cardiac conduction [GO:0061337]; cellular response to calcium ion [GO:0071277]; dendrite morphogenesis [GO:0048813]; DNA-templated transcription [GO:0006351]; ERK5 cascade [GO:0070375]; MAPK cascade [GO:0000165]; mitochondrial genome maintenance [GO:0000002]; mitochondrion distribution [GO:0048311]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of cardiac muscle hypertrophy [GO:0010613]; positive regulation of gene expression [GO:0010628]; positive regulation of glucose import [GO:0046326]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]; ventricular cardiac myofibril assembly [GO:0055005]
|
chromatin [GO:0000785]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667]
|
chromatin binding [GO:0003682]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription factor binding [GO:0140297]; histone acetyltransferase binding [GO:0035035]; histone deacetylase binding [GO:0042826]; protein heterodimerization activity [GO:0046982]; protein kinase binding [GO:0019901]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; SMAD binding [GO:0046332]
|
PF12347;PF00319;
|
3.40.1810.10;
| null |
PTM: Constitutive phosphorylation on Ser-400 promotes Lys-395 sumoylation thus preventing acetylation at this site. Dephosphorylation on Ser-400 by PPP3CA upon neuron depolarization promotes a switch from sumoylation to acetylation on residue Lys-395 leading to inhibition of dendrite claw differentiation. Phosphorylation on Thr-304 and Thr-311 are the main sites involved in p38 MAPK signaling and activate transcription. Phosphorylated on these sites by MAPK14/p38alpha and MAPK11/p38beta, but not by MAPK13/p38delta nor by MAPK12/p38gamma. Phosphorylation on Ser-400 by CDK5 induced by neurotoxicity inhibits MEF2A transcriptional activation leading to apoptosis of cortical neurons. Phosphorylation on Thr-304, Thr-311 and Ser-347 can be induced by EGF (By similarity). {ECO:0000250}.; PTM: Sumoylation on Lys-395 is enhanced by PIAS1 and represses transcriptional activity. Phosphorylation on Ser-400 is required for sumoylation. Has no effect on nuclear location nor on DNA binding. Sumoylated with SUMO1 and, to a lesser extent with SUMO2 and SUMO3. PIASx facilitates sumoylation in postsynaptic dendrites in the cerebellar cortex and promotes their morphogenesis (By similarity). {ECO:0000250}.; PTM: Acetylation on Lys-395 activates transcriptional activity. Acetylated by p300 on several sites in diffentiating myocytes. Acetylation on Lys-4 increases DNA binding and transactivation (By similarity). Hyperacetylation by p300 leads to enhanced cardiac myocyte growth and heart failure (By similarity). {ECO:0000250}.; PTM: Proteolytically cleaved in cerebellar granule neurons on several sites by caspase 3 and caspase 7 following neurotoxicity. Preferentially cleaves the CDK5-mediated hyperphosphorylated form which leads to neuron apoptosis and transcriptional inactivation (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251}.
| null | null | null | null | null |
FUNCTION: Transcriptional activator which binds specifically to the MEF2 element, 5'-YTA[AT](4)TAR-3', found in numerous muscle-specific genes. Also involved in the activation of numerous growth factor- and stress-induced genes. Mediates cellular functions not only in skeletal and cardiac muscle development, but also in neuronal differentiation and survival. Plays diverse roles in the control of cell growth, survival and apoptosis via p38 MAPK signaling in muscle-specific and/or growth factor-related transcription. In cerebellar granule neurons, phosphorylated and sumoylated MEF2A represses transcription of NUR77 promoting synaptic differentiation. Associates with chromatin to the ZNF16 promoter (By similarity). {ECO:0000250}.
|
Bos taurus (Bovine)
|
A2VDZ4
|
PLK4_BOVIN
|
MATCIGEKIEDFRVGNLLGKGSFAGVYRAESIHTGLEVAIKMIDKKAMYKAGMVQRVQNEVKIHCQLKHPSILELYNYFEDNNYVYLVLEMCHNGEMNRYLKNRRKPFSENEARHFMHQIITGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLAAQLKMPHEKHYTLCGTPNYISPEIATRSAHGLESDIWSLGCMFYTLLIGRPPFDTDTVKNTLNKVVLADYEMPTFLSREAKDLIHQLLRRNPADRLSLSSVLDHPFMSRNSSKKSKDLGTVEDSIDSGHATISTAITASSSTSISGSLFDRRRLLIEQPLPNKMTIFPKNKNPSDFSSSGDGISFYTSWGNQEQETSNSGRGRVIQEAEERPHSRYLRRAHSSDRSETSHGQSRVKTYTMERCYSAEMLSKSKRSGVEENERYSPTNNDANIFHFFKEKTSNSSGSFEGPDNNQALSNHLCPGKTPFPFPEQTPQTEMVQQWFGNLQINDPSCEQSKTRGVEPPLVYQKRTLRSITSPLTAYRLKPIRQKTKKAVVSILDSEEVCVELLKDYASQEYVKEVLQISSDGSMITIYYPNDGRGFLLADRPPSPTDNISRYSFDNLPEKYWRKYQYASRFVQLVRSKSPKITYFTRYAKCVLMENSPGADFEVWFYDGAKIHKTEDLIQVIEKTGRSYTLKGESEVNSLKEEVKMYMNHANEGHRICLALESIISEEEKKSGSAPFFPIIVGRRPSSTSSPKALTPPPPVDPNYPMRETPSLNRMIINSAASPKQAPVLNPPVVTNEGLGLMGAASETNSSPRSLKDCLPKSAQLLKSVFVKNVGWATQLTSGAVWVQFNDGSQLVVQAGVSSISYTSPDGQTTRYGENEKLPEYIKQKLQCLSSILLMFSNPTPSFH
|
2.7.11.21
| null |
centriole replication [GO:0007099]; cilium assembly [GO:0060271]; de novo centriole assembly involved in multi-ciliated epithelial cell differentiation [GO:0098535]; mitotic spindle organization [GO:0007052]; positive regulation of centriole replication [GO:0046601]; protein phosphorylation [GO:0006468]; trophoblast giant cell differentiation [GO:0060707]
|
centriole [GO:0005814]; centrosome [GO:0005813]; cleavage furrow [GO:0032154]; cytoplasm [GO:0005737]; deuterosome [GO:0098536]; kinetochore [GO:0000776]; nucleolus [GO:0005730]; spindle pole [GO:0000922]
|
ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00069;PF18190;PF18409;
|
2.40.50.930;3.30.1120.120;3.30.1120.130;1.10.510.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family, CDC5/Polo subfamily
|
PTM: Ubiquitinated; leading to its degradation by the proteasome. {ECO:0000250}.; PTM: Tyrosine-phosphorylated by TEC. {ECO:0000250}.; PTM: Acetylation by KAT2A and KAT2B impairs kinase activity by shifting the kinase to an inactive conformation. {ECO:0000250|UniProtKB:O00444}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:O00444}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q64702}. Cleavage furrow {ECO:0000250|UniProtKB:Q64702}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:O00444}. Note=Associates with centrioles throughout the cell cycle. Component of the deuterosome, a structure that promotes de novo centriole amplification in multiciliated cells that can generate more than 100 centrioles (By similarity). {ECO:0000250|UniProtKB:O00444, ECO:0000250|UniProtKB:Q64702}.
|
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=2.7.11.21; Evidence={ECO:0000250|UniProtKB:O00444}; 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=2.7.11.21; Evidence={ECO:0000250|UniProtKB:O00444};
| null | null | null | null |
FUNCTION: Serine/threonine-protein kinase that plays a central role in centriole duplication. Able to trigger procentriole formation on the surface of the parental centriole cylinder, leading to the recruitment of centriole biogenesis proteins such as SASS6, CENPJ/CPAP, CCP110, CEP135 and gamma-tubulin. When overexpressed, it is able to induce centrosome amplification through the simultaneous generation of multiple procentrioles adjoining each parental centriole during S phase. Phosphorylates 'Ser-151' of FBXW5 during the G1/S transition, leading to inhibit FBXW5 ability to ubiquitinate SASS6. Its central role in centriole replication suggests a possible role in tumorigenesis, centrosome aberrations being frequently observed in tumors. Also involved in deuterosome-mediated centriole amplification in multiciliated that can generate more than 100 centrioles. Also involved in trophoblast differentiation by phosphorylating HAND1, leading to disrupt the interaction between HAND1 and MDFIC and activate HAND1. Phosphorylates CDC25C and CHEK2. Required for the recruitment of STIL to the centriole and for STIL-mediated centriole amplification (By similarity). Phosphorylates CEP131 and PCM1 which is essential for proper organization and integrity of centriolar satellites (By similarity). {ECO:0000250|UniProtKB:O00444, ECO:0000250|UniProtKB:Q64702}.
|
Bos taurus (Bovine)
|
A2VE31
|
S38A2_BOVIN
|
MKKAEMGRFNISPDEDSSSYSSNSDFNYSYPTKQAALKSHYADVDPENQNFLLESNLGKKKYETDFHPGTTSFGMSVFNLSNAIVGSGILGLSYAMANTGIALFIILLTFVSIFSLYSVHLLLKTANEGGSLLYEQLGHKAFGMVGKLTASGSITMQNIGAMSSYLFIVKYELPLVIQALMNIEDTNGLWYLNGDYLVLLVSLVLILPLSLLRNLGYLGYTSGLSLLCMMFFLIVVIFKKFQISCPAEIAFLVNETVNSSLTQPATFLPDMGFNRTESDSCQPRYFIFNSQTVYAVPILTFSFVCHPAILPIYEELKGRSRRRMMNVSKISFFAMFLMYLLAALFGYLTFYGHVESELLHTYSSVMETDILLLIVRLAVLVAVTLTVPVVIFPIRSSITHLLCASKEFSWWRHSVITVSILVFTNLLVIFVPNIRDIFGFIGASAAAMLIFILPSAFYIKLVKKEPMKSVQKIGAMFFLLSGIVVMTGSMALIVLDWVHNAPGGGH
| null | null |
alanine transport [GO:0032328]; amino acid import [GO:0043090]; amino acid transmembrane transport [GO:0003333]; amino acid transport [GO:0006865]; glutamine transport [GO:0006868]; L-glutamine import across plasma membrane [GO:1903803]; L-proline import across plasma membrane [GO:1904271]; L-serine import across plasma membrane [GO:1903812]; neutral amino acid transport [GO:0015804]; proline transport [GO:0015824]; regulation of glutamate secretion, neurotransmission [GO:1903294]
|
plasma membrane [GO:0005886]
|
acidic amino acid transmembrane transporter activity [GO:0015172]; alanine:sodium symporter activity [GO:0015655]; amino acid transmembrane transporter activity [GO:0015171]; amino acid:sodium symporter activity [GO:0005283]; L-glutamine transmembrane transporter activity [GO:0015186]; neutral L-amino acid transmembrane transporter activity [GO:0015175]; neutral L-amino acid:sodium symporter activity [GO:0005295]; proline:sodium symporter activity [GO:0005298]
|
PF01490;
| null |
Amino acid/polyamine transporter 2 family
|
PTM: Polyubiquitination by NEDD4L regulates the degradation and the activity of SLC38A2. {ECO:0000250|UniProtKB:Q8CFE6}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9JHE5}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9JHE5}. Note=Insulin promotes recruitment to the plasma membrane from a pool localized in the trans-Golgi network or endosomes. Enriched in the somatodendritic compartment of neurons, it is also detected at the axonal shaft but excluded from the nerve terminal. {ECO:0000250|UniProtKB:Q9JHE5}.
|
CATALYTIC ACTIVITY: Reaction=L-alanine(in) + Na(+)(in) = L-alanine(out) + Na(+)(out); Xref=Rhea:RHEA:29283, ChEBI:CHEBI:29101, ChEBI:CHEBI:57972; Evidence={ECO:0000250|UniProtKB:Q9JHE5}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29285; Evidence={ECO:0000250|UniProtKB:Q9JHE5}; CATALYTIC ACTIVITY: Reaction=glycine(in) + Na(+)(in) = glycine(out) + Na(+)(out); Xref=Rhea:RHEA:68228, ChEBI:CHEBI:29101, ChEBI:CHEBI:57305; Evidence={ECO:0000250|UniProtKB:Q9JHE5}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:68230; Evidence={ECO:0000250|UniProtKB:Q9JHE5}; CATALYTIC ACTIVITY: Reaction=L-serine(in) + Na(+)(in) = L-serine(out) + Na(+)(out); Xref=Rhea:RHEA:29575, ChEBI:CHEBI:29101, ChEBI:CHEBI:33384; Evidence={ECO:0000250|UniProtKB:Q9JHE5}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29577; Evidence={ECO:0000250|UniProtKB:Q9JHE5}; CATALYTIC ACTIVITY: Reaction=L-proline(in) + Na(+)(in) = L-proline(out) + Na(+)(out); Xref=Rhea:RHEA:28967, ChEBI:CHEBI:29101, ChEBI:CHEBI:60039; Evidence={ECO:0000250|UniProtKB:Q9JHE5}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28969; Evidence={ECO:0000250|UniProtKB:Q9JHE5}; CATALYTIC ACTIVITY: Reaction=L-methionine(in) + Na(+)(in) = L-methionine(out) + Na(+)(out); Xref=Rhea:RHEA:68240, ChEBI:CHEBI:29101, ChEBI:CHEBI:57844; Evidence={ECO:0000250|UniProtKB:Q9JHE5}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:68242; Evidence={ECO:0000250|UniProtKB:Q9JHE5}; CATALYTIC ACTIVITY: Reaction=L-histidine(in) + Na(+)(in) = L-histidine(out) + Na(+)(out); Xref=Rhea:RHEA:71583, ChEBI:CHEBI:29101, ChEBI:CHEBI:57595; Evidence={ECO:0000250|UniProtKB:Q9JHE5}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71585; Evidence={ECO:0000250|UniProtKB:Q9JHE5}; CATALYTIC ACTIVITY: Reaction=L-asparagine(in) + Na(+)(in) = L-asparagine(out) + Na(+)(out); Xref=Rhea:RHEA:71383, ChEBI:CHEBI:29101, ChEBI:CHEBI:58048; Evidence={ECO:0000250|UniProtKB:Q9JHE5}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71385; Evidence={ECO:0000250|UniProtKB:Q9JHE5}; CATALYTIC ACTIVITY: Reaction=L-glutamine(in) + Na(+)(in) = L-glutamine(out) + Na(+)(out); Xref=Rhea:RHEA:68236, ChEBI:CHEBI:29101, ChEBI:CHEBI:58359; Evidence={ECO:0000250|UniProtKB:Q9JHE5}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:68238; Evidence={ECO:0000250|UniProtKB:Q9JHE5}; CATALYTIC ACTIVITY: Reaction=L-threonine(in) + Na(+)(in) = L-threonine(out) + Na(+)(out); Xref=Rhea:RHEA:69999, ChEBI:CHEBI:29101, ChEBI:CHEBI:57926; Evidence={ECO:0000250|UniProtKB:Q9JHE5}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70001; Evidence={ECO:0000250|UniProtKB:Q9JHE5}; CATALYTIC ACTIVITY: Reaction=L-leucine(in) + Na(+)(in) = L-leucine(out) + Na(+)(out); Xref=Rhea:RHEA:29263, ChEBI:CHEBI:29101, ChEBI:CHEBI:57427; Evidence={ECO:0000250|UniProtKB:Q9JHE5}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:29265; Evidence={ECO:0000250|UniProtKB:Q9JHE5}; CATALYTIC ACTIVITY: Reaction=L-phenylalanine(in) + Na(+)(in) = L-phenylalanine(out) + Na(+)(out); Xref=Rhea:RHEA:68244, ChEBI:CHEBI:29101, ChEBI:CHEBI:58095; Evidence={ECO:0000250|UniProtKB:Q9JHE5}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:68246; Evidence={ECO:0000250|UniProtKB:Q9JHE5};
| null | null | null | null |
FUNCTION: Symporter that cotransports neutral amino acids and sodium ions from the extracellular to the intracellular side of the cell membrane. The transport is pH-sensitive, Li(+)-intolerant, electrogenic, driven by the Na(+) electrochemical gradient and cotransports of neutral amino acids and sodium ions with a stoichiometry of 1:1. May function in the transport of amino acids at the blood-brain barrier (By similarity). May function in the transport of amino acids in the supply of maternal nutrients to the fetus through the placenta (By similarity). Maintains a key metabolic glutamine/glutamate balance underpinning retrograde signaling by dendritic release of the neurotransmitter glutamate (By similarity). Transports L-proline in differentiating osteoblasts for the efficient synthesis of proline-enriched proteins and provides proline essential for osteoblast differentiation and bone formation during bone development (By similarity). {ECO:0000250|UniProtKB:Q8CFE6, ECO:0000250|UniProtKB:Q9JHE5}.
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Bos taurus (Bovine)
|
A2VE79
|
NUDT3_BOVIN
|
MMKLKSNQTRTYDGDGYKKRAACLCFRSESEEEVLLVSSSRHPDRWIVPGGGMEPEEEPGTAAVREVCEEAGVKGTLGRLVGIFENQERKHRTYVYVLIVTEVLEDWEDSVSIGRKREWFKIEDAINVLQCHKPVQASYFETLRQGYSANNGTPLVAPTYSVSAQSSMPGIR
|
3.6.1.10; 3.6.1.52; 3.6.1.59; 3.6.1.61; 3.6.1.62
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O95989}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:O95989}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:O95989}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:O95989};
|
adenosine 5'-(hexahydrogen pentaphosphate) catabolic process [GO:1901911]; diadenosine hexaphosphate catabolic process [GO:1901909]; diadenosine pentaphosphate catabolic process [GO:1901907]; diphosphoinositol polyphosphate catabolic process [GO:0071544]; diphosphoinositol polyphosphate metabolic process [GO:0071543]; RNA decapping [GO:0110154]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]
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5'-(N(7)-methyl 5'-triphosphoguanosine)-[mRNA] diphosphatase activity [GO:0140932]; 5'-(N(7)-methylguanosine 5'-triphospho)-[mRNA] hydrolase activity [GO:0140933]; bis(5'-adenosyl)-hexaphosphatase activity [GO:0034431]; bis(5'-adenosyl)-pentaphosphatase activity [GO:0034432]; diphosphoinositol-polyphosphate diphosphatase activity [GO:0008486]; endopolyphosphatase activity [GO:0000298]; inositol diphosphate pentakisphosphate diphosphatase activity [GO:0052842]; inositol diphosphate tetrakisphosphate diphosphatase activity [GO:0052840]; inositol-3,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 5-diphosphatase activity [GO:0052848]; inositol-5-diphosphate-1,2,3,4,6-pentakisphosphate diphosphatase activity [GO:0052845]; magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030145]; zinc ion binding [GO:0008270]
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PF00293;
|
3.90.79.10;
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Nudix hydrolase family, DIPP subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O95989}. Nucleus {ECO:0000250|UniProtKB:O95989}.
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CATALYTIC ACTIVITY: Reaction=diphospho-myo-inositol polyphosphate + H2O = myo-inositol polyphosphate + phosphate.; EC=3.6.1.52; Evidence={ECO:0000250|UniProtKB:O95989}; CATALYTIC ACTIVITY: Reaction=5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate + H2O = 1D-myo-inositol hexakisphosphate + H(+) + phosphate; Xref=Rhea:RHEA:22384, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58130, ChEBI:CHEBI:58628; EC=3.6.1.52; Evidence={ECO:0000250|UniProtKB:O95989}; CATALYTIC ACTIVITY: Reaction=3,5-bis(diphospho)-1D-myo-inositol 1,2,4,6-tetrakisphosphate + H2O = 3-diphospho-1D-myo-inositol 1,2,4,5,6-pentakisphosphate + 2 H(+) + phosphate; Xref=Rhea:RHEA:56312, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:140372, ChEBI:CHEBI:140374; EC=3.6.1.52; Evidence={ECO:0000250|UniProtKB:O95989}; CATALYTIC ACTIVITY: Reaction=[phosphate](n+1) + n H2O = n H(+) + (n+1) phosphate; Xref=Rhea:RHEA:22452, Rhea:RHEA-COMP:14280, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16838, ChEBI:CHEBI:43474; EC=3.6.1.10; Evidence={ECO:0000250|UniProtKB:O95989}; CATALYTIC ACTIVITY: Reaction=H2O + P(1),P(5)-bis(5'-adenosyl) pentaphosphate = ADP + ATP + 2 H(+); Xref=Rhea:RHEA:30527, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:62041, ChEBI:CHEBI:456216; EC=3.6.1.61; Evidence={ECO:0000250|UniProtKB:O95989}; CATALYTIC ACTIVITY: Reaction=H2O + P(1),P(6)-bis(5'-adenosyl) hexaphosphate = 2 ATP + 2 H(+); Xref=Rhea:RHEA:32043, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:63740; EC=3.6.1.61; Evidence={ECO:0000250|UniProtKB:O95989}; CATALYTIC ACTIVITY: Reaction=H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = AMP + ATP + 2 H(+); Xref=Rhea:RHEA:32039, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58141, ChEBI:CHEBI:456215; EC=3.6.1.61; Evidence={ECO:0000250|UniProtKB:O95989}; CATALYTIC ACTIVITY: Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + H2O = a 5'-end diphospho-ribonucleoside in mRNA + 2 H(+) + N(7)-methyl-GMP; Xref=Rhea:RHEA:65388, Rhea:RHEA-COMP:17165, Rhea:RHEA-COMP:17167, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58285, ChEBI:CHEBI:156461, ChEBI:CHEBI:167616; EC=3.6.1.59; Evidence={ECO:0000250|UniProtKB:Q9JI46}; 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:0000250|UniProtKB:Q9JI46};
| null | null | null | null |
FUNCTION: Cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate) and [PP]2-InsP4 (bisdiphosphoinositol tetrakisphosphate), suggesting that it may play a role in signal transduction (By similarity). InsP6 (inositol hexakisphosphate) is not a substrate (By similarity). Also able to catalyze the hydrolysis of dinucleoside oligophosphates, with diadenosine 5',5'''-P1,P6-hexaphosphate (Ap6A) and diadenosine 5',5'''- P1,P5-pentaphosphate (Ap5A) being the preferred substrates (By similarity). The major reaction products are ADP and p4a from Ap6A and ADP and ATP from Ap5A (By similarity). Also able to hydrolyze 5- phosphoribose 1-diphosphate (By similarity). Acts as a decapping enzyme that can hydrolyze both monomethylated and unmethylated capped RNAs (By similarity). Hydrolyzes monomethylated capped RNA after both the alpha- and beta-phosphates generating m7GMP + ppRNA and m7GDP + pRNA (By similarity). Modulates the stability of a subset of mRNAs implicated in cell motility (By similarity). Divalent cations zinc, magnesium and manganese determine its substrate specificity (By similarity). Exhibits diphosphoinositol polyphosphate phosphohydrolase in the presence of magnesium ions, diadenosine hexaphosphate hydrolase activity in the presence of manganese ions and endopolyphosphatase activity in the presence of zinc ions (By similarity). Plays an important role in limiting DNA damage and maintaining cell survival upon oxidative stress via its endopolyphosphatase activity (By similarity). {ECO:0000250|UniProtKB:O95989, ECO:0000250|UniProtKB:Q566C7}.
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Bos taurus (Bovine)
|
A2VEA3
|
ARI1_BOVIN
|
MDSDEGYNYEFDEDEECSEEDSGAEEEEDEDDDEPDDDNLDLGEVELVEPGLGVGGERDGLLCGETGGGGGSALGPGGGGGGGGGGGGPGHEQEEDYRYEVLTAEQILQHMVECIREVNEVIQNPATITRILLSHFNWDKEKLMERYFDGNLEKLFAECHVINPSKKSRTRQMNTRSSAQDMPCQICYLNYPNSYFTGLECGHKFCMQCWSEYLTTKIMEEGMGQTISCPAHGCDILVDDNTVMRLITDSKVKLKYQHLITNSFVECNRLLKWCPAPDCHHVVKVQYPDAKPVRCKCGRQFCFNCGENWHDPVKCKWLKKWIKKCDDDSETSNWIAANTKECPKCHVTIEKDGGCNHMVCRNQNCKAEFCWVCLGPWEPHGSAWYNCNRYNEDDAKAARDAQERSRAALQRYLFYCNRYMNHMQSLRFEHKLYAQVKQKMEEMQQHNMSWIEVQFLKKAVDVLCQCRATLMYTYVFAFYLKKNNQSIIFENNQADLENATEVLSGYLERDISQDSLQDIKQKVQDKYRYCESRRRVLLQHVHEGYEKDLWEYIED
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2.3.2.31
| null |
positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; protein polyubiquitination [GO:0000209]; protein ubiquitination [GO:0016567]; ubiquitin-dependent protein catabolic process [GO:0006511]
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Cajal body [GO:0015030]; cytoplasm [GO:0005737]; Lewy body [GO:0097413]; nuclear body [GO:0016604]; nucleus [GO:0005634]; ubiquitin ligase complex [GO:0000151]
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ubiquitin conjugating enzyme binding [GO:0031624]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270]
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PF21235;PF19422;PF01485;PF00097;
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1.20.120.1750;3.30.40.10;
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RBR family, Ariadne subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y4X5}. Nucleus {ECO:0000250|UniProtKB:Q9Y4X5}. Nucleus, Cajal body {ECO:0000250|UniProtKB:Q9Y4X5}. Note=Mainly cytoplasmic. Present in Lewy body. {ECO:0000250|UniProtKB:Q9Y4X5}.
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CATALYTIC ACTIVITY: Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.; EC=2.3.2.31; Evidence={ECO:0000250|UniProtKB:Q9Y4X5};
| null |
PATHWAY: Protein modification; protein ubiquitination.
| null | null |
FUNCTION: E3 ubiquitin-protein ligase, which catalyzes ubiquitination of target proteins together with ubiquitin-conjugating enzyme E2 UBE2L3. Acts as an atypical E3 ubiquitin-protein ligase by working together with cullin-RING ubiquitin ligase (CRL) complexes and initiating ubiquitination of CRL substrates: associates with CRL complexes and specifically mediates addition of the first ubiquitin on CRLs targets. The initial ubiquitin is then elongated by CDC34/UBE2R1 and UBE2R2. E3 ubiquitin-protein ligase activity is activated upon binding to neddylated cullin-RING ubiquitin ligase complexes. Plays a role in protein translation in response to DNA damage by mediating ubiquitination of EIF4E2, the consequences of EIF4E2 ubiquitination are however unclear. According to a report, EIF4E2 ubiquitination leads to promote EIF4E2 cap-binding and protein translation arrest. According to another report EIF4E2 ubiquitination leads to its subsequent degradation. Acts as the ligase involved in ISGylation of EIF4E2. In vitro, controls the degradation of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex member SUN2 and may therefore have a role in the formation and localization of the LINC complex, and as a consequence, may act in nuclear subcellular localization and nuclear morphology. {ECO:0000250|UniProtKB:Q9Y4X5}.
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Bos taurus (Bovine)
|
A2VEC9
|
SSPO_HUMAN
|
MLLPALLFGMAWALADGRWCEWTETIRVEEEVAPRQEDLVPCASLDHYSRLGWRLDLPWSGRSGLTRSPAPGLCPIYKPPETRPAKWNRTVRTCCPGWGGAHCTEALAKASPEGHCFAMWQCQLQAGSANASAGSLEECCARPWGQSWWDGSSQACRSCSSRHLPGSASSPALLQPLAGAVGQLWSQHQRPSATCASWSGFHYRTFDGRHYHFLGRCTYLLAGAADSTWAVHLTPGDRCPQPGHCQRVTMGPEEVLIQAGNVSVKGQLVPEGQSWLLHGLSLQWLGDWLVLSGGLGVVVRLDRTGSISISVDHELWGQTQGLCGLYNGWPEDDFMEPGGGLAMLAATFGNSWRLPGSESGCLDAVEVAQGCDSPLGLIDADVEPGHLRAEAQDVCHQLLEGPFGQCHAQVSPAEYHEACLFAYCAGAMAGSGQEGRQQAVCATFASYVQACARRHIHIRWRKPGFCERLCPGGQLYSDCVSLCPPSCEAVGQGEEESCREECVSGCECPRGLFWNGTLCVPAAHCPCYYCRQRYVPGDTVRQLCNPCVCRDGRWHCAQALCPAECAVGGDGHYLTFDGRSYSFWGGQGCRYSLVQDYVKGQLLILLEHGACDAGSCLHAISVSLEDTHIQLRDSGAVLVNGQDVGLPWIGAEGLSVRRASSAFLLLRWPGAQVLWGLSDPVAYITLDPRHAHQVQGLCGTFTQNQQDDFLTPAGDVETSIAAFASKFQVAGKGRCPSEDSALLSPCTTHSQRHAFAEAACAILHSSVFQECHRLVDKEPFYLRCLAAVCGCDPGSDCLCPVLSAYARRCAQEGASPPWRNQTLCPVMCPGGQEYRECAPACGQHCGKPEDCGELGSCVAGCNCPLGLLWDPEGQCVPPSLCPCQLGARRYAPGSATMKECNRCICQERGLWNCTARHCPSQAFCPRELVYAPGACLLTCDSPSANHSCPAGSTDGCVCPPGTVLLDERCVPPDLCPCRHSGQWYLPNATIQEDCNVCVCRGRQWHCTGQRRSGRCQASGAPHYVTFDGLAFTYPGACEYLLVREASGLFTVSAQNLPCGASGLTCTKALAVRLEGTVVHMLRGRAVTVNGVSVTPPKVYTGPGLSLRRAGLFLLLSTHLGLTLLWDGGTRVLVQLSPQFRGRVAGLCGDFDGDASNDLRSRQGVLEPTAELAAHSWRLSPLCPEPGDLPHPCTMNTHRAGWARARCGALLQPLFTLCHAEVPPQQHYEWCLYDACGCDSGGDCECLCSAIATYADECARHGHHVRWRSQELCSLQCEGGQVYEACGPTCPPTCHEQHPEPGWHCQVVACVEGCFCPEGTLLHGGACLEPASCPCEWGRNSFPPGSVLQKDCGNCTCQEGQWHCGGDGGHCEELVPACAEGEALCQENGHCVPHGWLCDNQDDCGDGSDEEGCAAPGCGEGQMTCSSGHCLPLALLCDRQDDCGDGTDEPSYPCPQGLLACADGRCLPPALLCDGHPDCLDAADEESCLGQVTCVPGEVSCVDGTCLGAIQLCDGVWDCPDGADEGPGHCPLPSLPTPPASTLPGPSPGSLDTASSPLASASPAPPCGPFEFRCGSGECTPRGWRCDQEEDCADGSDERGCGGPCAPHHAPCARGPHCVSPEQLCDGVRQCPDGSDEGPDACGGLPALGGPNRTGLPCPEYTCPNGTCIGFQLVCDGQPDCGRPGQVGPSPEEQGCGAWGPWSPWGPCSRTCGPWGQGRSRRCSPLGLLVLQNCPGPEHQSQACFTAACPVDGEWSTWSPWSVCSEPCRGTMTRQRQCHSPQNGGRTCAALPGGLHSTRQTKPCPQDGCPNATCSGELMFQPCAPCPLTCDDISGQVTCPPDWPCGSPGCWCPEGQVLGSEGWCVWPRQCPCLVDGARYWPGQRIKADCQLCICQDGRPRRCRLNPDCAVDCGWSSWSPWAKCLGPCGSQSIQWSFRSSNNPRPSGRGRQCRGIHRKARRCQTEPCEGCEHQGQVHRVGERWHGGPCRVCQCLHNLTAHCSPYCPLGSCPQGWVLVEGTGESCCHCALPGENQTVQPMATPAAAPAPSPQIRFPLATYILPPSGDPCYSPLGLAGLAEGSLHASSQQLEHPTQAALLGAPTQGPSPQGWHAGGDAYAKWHTRPHYLQLDLLQPRNLTGILVPETGSSNAYASSFSLQFSSNGLHWHDYRDLLPGILPLPKLFPRNWDDLDPAVWTFGRMVQARFVRVWPHDVHHSDVPLQVELLGCEPGSPPAPLCPGVGLRCASGECVLRGGPCDGVLDCEDGSDEEGCVLLPEGTGRFHSTAKTLALSSAQPGQLLHWPREGLAETEHWPPGQESPTSPTETRPVSPGPASGVPHHGESVQMVTTTPIPQMEARTLPPGMAAVTVVPPHPVTPATPAGQSVAPGPFPPVQCGPGQTPCEVLGCVEQAQVCDGREDCLDGSDERHCARNLLMWLPSLPALWAASTVPFMMPTMALPGLPASRALCSPSQLSCGSGECLSAERRCDLRPDCQDGSDEDGCVDCVLAPWSVWSSCSRSCGLGLTFQRQELLRPPLPGGSCPRDRFRSQSCFVQACPVAGAWAMWEAWGPCSVSCGGGHQSRQRSCVDPPPKNGGAPCPGASQERAPCGLQPCSGGTDCELGRVYVSADLCQKGLVPPCPPSCLDPKANRSCSGHCVEGCRCPPGLLLHDTRCLPLSECPCLVGEELKWPGVSFLLGNCSQCVCEKGELLCQPGGCPLPCGWSAWSSWAPCDRSCGSGVRARFRSPSNPPAAWGGAPCEGDRQELQGCHTVCGTEVFGWTPWTSWSSCSQSCLAPGGGPGWRSRSRLCPSPGDSSCPGDATQEEPCSPPVCPVPSIWGLWAPWSTCSAPCDGGIQTRGRSCSSLAPGDTTCPGPHSQTRDCNTQPCTAQCPENMLFRSAEQCHQEGGPCPRLCLTQGPGIECTGFCAPGCTCPPGLFLHNASCLPRSQCPCQLHGQLYASGAMARLDSCNNCTCVSGKMACTSERCPVACGWSPWTLWSLCSCSCNVGIRRRFRAGTAPPAAFGGAECQGPTMEAEFCSLRPCPGPGGEWGPWSPCSVPCGGGYRNRTRGSSRSLMEFSTCGLQPCAGPVPGMCPRDKQWLDCAQGPASCAELSAPRGTNQTCHPGCHCPSGMLLLNNVCVPTQDCPCAHEGHLYPPGSTVVRPCENCSCVSGLIANCSSWPCAEGEPTWSPWTPWSQCSASCGPARCHRHRFCARSPSAVPSTVAPLPLPATPTPLCSGPEAEEEPCLLQGCDRAGGWGPWGPWSHCSRSCGGGLRSRTRACDQPPPQGLGDYCEGPRAQGEVCQALPCPVTNCTAIEGAEYSPCGPPCPRSCDDLVHCVWRCQPGCYCPPGQVLSSNGAICVQPGHCSCLDLLTGQRHHPGARLARPDGCNHCTCLEGRLNCTDLPCPVPGGWCPWSEWTMCSQPCRGQTRSRSRACACPTPQHGGAPCTGEAGEAGAQHQREACPSYATCPVDGAWGPWGPWSPCDMCLGQSHRSRACSRPPTPEGGRPCPGNHTQSRPCQENSTQCTDCGGGQSLHPCGQPCPRSCQDLSPGSVCQPGSVGCQPTCGCPLGQLSQDGLCVPPAHCRCQYQPGAMGIPENQSRSAGSRFSSWESLEPGEVVTGPCDNCTCVAGILQCQEVPDCPDPGVWSSWGPWEDCSVSCGGGEQLRSRRCARPPCPGPARQSRTCSTQVCREAGCPAGRLYRECQPGEGCPFSCAHVTQQVGCFSEGCEEGCHCPEGTFQHRLACVQECPCVLTAWLLQELGATIGDPGQPLGPGDELDSGQTLRTSCGNCSCAHGKLSCSLDDCFEADGGFGPWSPWGPCSRSCGGLGTRTRSRQCVLTMPTLSGQGCRGPRQDLEYCPSPDCPGAEGSTVEPVTGLPGGWGPWSSWSPCSRSCTDPARPAWRSRTRLCLANCTMGDPLQERPCNLPSCTELPVCPGPGCGAGNCSWTSWAPWEPCSRSCGVGQQRRLRAYRPPGPGGHWCPNILTAYQERRFCNLRACPVPGGWSRWSPWSWCDRSCGGGQSLRSRSCSSPPSKNGGAPCAGERHQARLCNPMPCEAGCPAGMEVVTCANRCPRRCSDLQEGIVCQDDQVCQKGCRCPKGSLEQDGGCVPIGHCDCTDAQGHSWAPGSQHQDACNNCSCQAGQLSCTAQPCPPPTHCAWSHWSAWSPCSHSCGPRGQQSRFRSSTSGSWAPECREEQSQSQPCPQPSCPPLCLQGTRSRTLGDSWLQGECQRCSCTPEGVICEDTECAVPEAWTLWSSWSDCPVSCGGGNQVRTRACRAAAPHHRSPPCLGPDTQTRQQPCPGLLEACSWGPWGPCSRSCGPGLASRSGSCPCLMAKADPTCNSTFLHLDTQGCYSGPCPEECVWSSWSSWTRCSCRVLVQQRYRHQGPASRGARAGAPCTRLDGHFRPCLISNCSEDSCTPPFEFHACGSPCAGLCATHLSHQLCQDLPPCQPGCYCPKGLLEQAGGCIPPEECNCWHTSAAGAGMTLAPGDRLQLGCKECECRRGELHCTSQGCQGLLPLSEWSEWSPCGPCLPPSALAPASRTALEEHWLRDPTGLSPTLAPLLASEQHRHRLCLDPATGRPWTGAPHLCTAPLSQQRLCPDPGACPDSCQWSLWGPWSPCQVPCSGGFRLRWREAEALCGGGCREPWAQESCNGGPCPESCEAQDTVFTLDCANQCPHSCADLWDRVQCLQGPCRPGCRCPPGQLVQDGRCVPISSCRCGLPSANASWELAPAQAVQLDCQNCTCVNESLVCPHQECPVLGPWSAWSSCSAPCGGGTMERHRTCEGGPGVAPCQAQDTEQRQECNLQPCPECPPGQVLSACATSCPCLCWHLQPGAICVQEPCQPGCGCPGGQLLHNGTCVPPTACPCTQHSLPWGLTLTLEEQAQELPPGTVLTRNCTRCVCHGGAFSCSLVDCQVPPGETWQQVAPGELGLCEQTCLEMNATKTQSNCSSARASGCVCQPGHFRSQAGPCVPEDHCECWHLGRPHLPGSEWQEACESCLCLSGRPVCTQHCSPLTCAQGEEMVLEPGSCCPSCRREAPEEQSPSCQLLTELRNFTKGTCYLDQVEVSYCSGYCPSSTHVMPEEPYLQSQCDCCSYRLDPESPVRILNLRCLGGHTEPVVLPVIHSCQCSSCQGGDFSKR
| null | null |
cell adhesion [GO:0007155]
|
extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; plasma membrane protein complex [GO:0098797]
|
peptidase inhibitor activity [GO:0030414]
|
PF08742;PF00754;PF00057;PF01826;PF00090;PF00094;
|
2.10.70.10;2.60.120.260;2.10.25.10;4.10.400.10;2.20.100.10;
|
Thrombospondin family
| null |
SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250|UniProtKB:P98167}.
| null | null | null | null | null |
FUNCTION: Involved in the modulation of neuronal aggregation (By similarity). May be involved in developmental events during the formation of the central nervous system (By similarity). {ECO:0000250|UniProtKB:P98167}.
|
Homo sapiens (Human)
|
Subsets and Splits
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