Datasets:
Synthyra
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SwissProt

Dataset card Data Studio Files Community
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Entry
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Entry Name
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Sequence
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35.2k
EC number
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118
⌀
Cofactor
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1.77k
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Gene Ontology (biological process)
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11.3k
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Gene Ontology (cellular component)
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Gene Ontology (molecular function)
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2.09k
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Pfam
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232
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Gene3D
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250
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Protein families
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237
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Post-translational modification
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8.52k
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Subcellular location [CC]
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6.18k
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Catalytic activity
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35.7k
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Kinetics
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Pathway
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908
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pH dependence
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955
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Temperature dependence
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1.16k
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Function [CC]
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Organism
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196
A4GXA9
EME2_HUMAN
MARVGPGRAGVSCQGRGRGRGGSGQRRPPTWEISDSDAEDSAGSEAAARARDPAGERRAAAEALRLLRPEQVLKRLAVCVDTAILEDAGADVLMEALEALGCECRIEPQRPARSLRWTRASPDPCPRSLPPEVWAAGEQELLLLLEPEEFLQGVATLTQISGPTHWVPWISPETTARPHLAVIGLDAYLWSRQHVSRGTQQPESPKVAGAEVAVSWPEVEEALVLLQLWANLDVLLVASWQELSRHVCAVTKALAQYPLKQYRESQAFSFCTAGRWAAGEPVARDGAGLQAAWRRQIRQFSRVSPAVADAVVTAFPSPRLLQQALEACSTERERMGLLADLPVPPSEGGRPRRVGPDLSRRICLFLTTANPDLLLDLGS
3.1.22.-
null
double-strand break repair [GO:0006302]; mitotic intra-S DNA damage checkpoint signaling [GO:0031573]; replication fork processing [GO:0031297]; resolution of meiotic recombination intermediates [GO:0000712]
endodeoxyribonuclease complex [GO:1905347]; Holliday junction resolvase complex [GO:0048476]; nuclear replication fork [GO:0043596]
crossover junction DNA endonuclease activity [GO:0008821]; DNA binding [GO:0003677]
PF21292;PF02732;
3.40.50.10130;1.10.150.670;
EME1/MMS4 family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
null
null
null
null
null
FUNCTION: Interacts with MUS81 to form a DNA structure-specific endonuclease which cleaves substrates such as 3'-flap structures. {ECO:0000269|PubMed:17289582}.
Homo sapiens (Human)
A4IFH6
PPLA_BOVIN
MDKVQYLTRSAIRRASTIEMPQQARQNLQNLFINFCLISICLLLICIIVMLL
null
null
acrosome assembly [GO:0001675]; intracellular calcium ion homeostasis [GO:0006874]; negative regulation of ATPase-coupled calcium transmembrane transporter activity [GO:1901895]; negative regulation of calcium ion import into sarcoplasmic reticulum [GO:1902081]; negative regulation of heart rate [GO:0010459]
endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; mitochondrial membrane [GO:0031966]; sarcoplasmic reticulum [GO:0016529]; sarcoplasmic reticulum membrane [GO:0033017]
ATPase inhibitor activity [GO:0042030]; protein homodimerization activity [GO:0042803]
PF04272;
1.20.5.290;
Phospholamban family
PTM: Phosphorylation by PKA abolishes the inhibition of ATP2A2-mediated calcium uptake. Phosphorylated at Thr-17 by CaMK2, and in response to beta-adrenergic stimulation. Phosphorylation by DMPK may stimulate sarcoplasmic reticulum calcium uptake in cardiomyocytes (By similarity). {ECO:0000250|UniProtKB:P26678}.; PTM: Palmitoylated by ZDHHC16, promoting formation of the homopentamer. {ECO:0000250|UniProtKB:P61014}.; PTM: In elongated spermatids, proteolytically cleaved by SPPL2C which modulates intracellular Ca(2+) homeostasis. {ECO:0000250|UniProtKB:P61014}.
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P26678}; Single-pass membrane protein {ECO:0000255}. Sarcoplasmic reticulum membrane {ECO:0000250|UniProtKB:P26678}; Single-pass membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000269|PubMed:17060615}; Single-pass membrane protein {ECO:0000255}. Membrane {ECO:0000250|UniProtKB:P61014}; Single-pass membrane protein {ECO:0000255}. Note=Colocalizes with HAX1 at the endoplasmic reticulum. Colocalizes with DMPK a the sarcoplasmic reticulum. {ECO:0000250|UniProtKB:P26678}.
null
null
null
null
null
FUNCTION: Reversibly inhibits the activity of ATP2A2 in cardiac sarcoplasmic reticulum by decreasing the apparent affinity of the ATPase for Ca(2+). Modulates the contractility of the heart muscle in response to physiological stimuli via its effects on ATP2A2. Modulates calcium re-uptake during muscle relaxation and plays an important role in calcium homeostasis in the heart muscle. The degree of ATP2A2 inhibition depends on the oligomeric state of PLN. ATP2A2 inhibition is alleviated by PLN phosphorylation. Controls intracellular Ca(2+) levels in elongated spermatids. May play a role in germ cell differentiation. {ECO:0000250|UniProtKB:P61014}.
Bos taurus (Bovine)
A4IFJ5
PA24A_BOVIN
MSFIDPYQHIIVEHHYSHKFTVVVLRATKVTKGTFGDMLDTPDPYVELFISSTPDSRKRTRHFNNDINPVWNETFEFILDPNQENILEITLMDANYVMDETLGTTTFPISSMKVGEKKQVPFIFNQVTEMILEMSLEVCSSPDLRFSMALCDQEKAFRQQRKENIKENMKKLLGPKNSEGLHSTRDVPVVAILGSGGGFRAMVGFSGVMKALYESGILDCATYIAGLSGSTWYMSTLYSHPDFPEKGPEEINKELMKNVSHNPLLLLTPQKIKRYVESLWRKKSSGQPVTFTDIFGMLIGETLIHNRMNTTLSSLKEKVNTGQCPLPLFTCLHVKPDVSELMFADWVEFSPFEIGMAKYGTFMAPDLFGSKFFMGTVVKKYEENPLHFLMGVWGSAFSILFNRVLGVSGSQSKGSTMEEELENITAKHIVSNDSSDSDDESQGPKGTEHEEAEREYQNDNQASWVQRMLMALVSDSALFNTREGRAGKVHNFMLGLNLNTSYPMSPLRDFTMQESLDEDELDAAVADPDEFEQIYEPLDVKSKKIHVVDSGLTFNLPYPLILRPQRGVDLIISFDFSARPSDSSPPFKELLLAEKWAKMNKLPFPKIDPYVFDREGLKECYVFKPKNPDVEKDCPTIIHFVLANINFRKYKAPGVPRETNEEKEIADFDIFDDPESPFSTFNFQYPNQAFKRLHDLMYFNTLNNIDVIKNAIVESIEYRRQNPSRCSVSLSSVEARRFFNKEFLSKPTA
3.1.1.4; 3.1.1.5
null
arachidonic acid metabolic process [GO:0019369]; glycerol metabolic process [GO:0006071]; glycerophospholipid catabolic process [GO:0046475]; leukotriene biosynthetic process [GO:0019370]; monoacylglycerol biosynthetic process [GO:0006640]; phosphatidylcholine acyl-chain remodeling [GO:0036151]; phosphatidylcholine catabolic process [GO:0034638]; phosphatidylglycerol catabolic process [GO:0034478]; positive regulation of platelet activation [GO:0010572]; prostaglandin biosynthetic process [GO:0001516]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; nuclear envelope [GO:0005635]; nucleus [GO:0005634]
calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; calcium-dependent phospholipid binding [GO:0005544]; calcium-independent phospholipase A2 activity [GO:0047499]; ceramide 1-phosphate binding [GO:1902387]; lysophospholipase activity [GO:0004622]; O-acyltransferase activity [GO:0008374]; phosphatidyl phospholipase B activity [GO:0102545]; phosphatidylinositol-3-phosphate binding [GO:0032266]; phosphatidylinositol-4-phosphate binding [GO:0070273]; phosphatidylinositol-5-phosphate binding [GO:0010314]; phospholipase A2 activity [GO:0004623]
PF00168;PF01735;
2.60.40.150;3.40.1090.10;
null
PTM: Phosphorylated at both Ser-505 and Ser-727 in response to mitogenic stimuli. {ECO:0000250|UniProtKB:P47712}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P47712}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P47712}. Nucleus envelope {ECO:0000250|UniProtKB:P47712}. Note=Translocates to intracellular membranes in a calcium-dependent way. {ECO:0000250|UniProtKB:P47712}.
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000250|UniProtKB:P47712}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802; Evidence={ECO:0000250|UniProtKB:P47712}; CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5; Evidence={ECO:0000250|UniProtKB:P47712}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15178; Evidence={ECO:0000250|UniProtKB:P47712}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40427, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:72998, ChEBI:CHEBI:73003; Evidence={ECO:0000250|UniProtKB:P47712}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40428; Evidence={ECO:0000250|UniProtKB:P47712}; CATALYTIC ACTIVITY: Reaction=1,2-di-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:41075, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:60657, ChEBI:CHEBI:74344; Evidence={ECO:0000250|UniProtKB:P47712}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41076; Evidence={ECO:0000250|UniProtKB:P47712}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-octadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40519, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:73858, ChEBI:CHEBI:74965; Evidence={ECO:0000250|UniProtKB:P47712}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40520; Evidence={ECO:0000250|UniProtKB:P47712}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine + H2O = (9Z,12Z)-octadecadienoate + 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40811, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:72998, ChEBI:CHEBI:73002; Evidence={ECO:0000250|UniProtKB:P47712}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40812; Evidence={ECO:0000250|UniProtKB:P47712}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(9Z,12Z,15Z-octadecatrienoyl)-sn-glycero-3-phosphocholine + H2O = (9Z,12Z,15Z)-octadecatrienoate + 1-octadecanoyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:41307, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32387, ChEBI:CHEBI:73858, ChEBI:CHEBI:78022; Evidence={ECO:0000250|UniProtKB:P47712}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41308; Evidence={ECO:0000250|UniProtKB:P47712}; CATALYTIC ACTIVITY: Reaction=1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-2-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:41071, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:74344, ChEBI:CHEBI:77694; Evidence={ECO:0000250|UniProtKB:P47712}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41072; Evidence={ECO:0000250|UniProtKB:P47712}; CATALYTIC ACTIVITY: Reaction=1-O-hexadecyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-O-hexadecyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:41067, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:55430, ChEBI:CHEBI:64496; Evidence={ECO:0000250|UniProtKB:P47712}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41068; Evidence={ECO:0000250|UniProtKB:P47712}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-sn-glycerol) + H2O = (9Z)-octadecenoate + 1-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-sn-glycerol) + H(+); Xref=Rhea:RHEA:41123, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72828, ChEBI:CHEBI:75163; Evidence={ECO:0000250|UniProtKB:P47712}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41124; Evidence={ECO:0000250|UniProtKB:P47712}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-octadecanoyl-sn-glycero-3-phosphate + H(+); Xref=Rhea:RHEA:40451, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:74565, ChEBI:CHEBI:77091; Evidence={ECO:0000250|UniProtKB:P47712}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40452; Evidence={ECO:0000250|UniProtKB:P47712}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) + hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40435, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:72998; Evidence={ECO:0000250|UniProtKB:P47712}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436; Evidence={ECO:0000250|UniProtKB:P47712}; CATALYTIC ACTIVITY: Reaction=2-(prostaglandin E2)-sn-glycero-3-phosphoethanolamine + H2O = H(+) + prostaglandin E2 + sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:53704, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:137581, ChEBI:CHEBI:143890, ChEBI:CHEBI:606564; Evidence={ECO:0000250|UniProtKB:P47712}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53705; Evidence={ECO:0000250|UniProtKB:P47712}; CATALYTIC ACTIVITY: Reaction=2-[(15S)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl]-sn-glycero-3-phosphocholine + H2O = (15S)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:53700, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:57409, ChEBI:CHEBI:137584; Evidence={ECO:0000250|UniProtKB:P47712}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53701; Evidence={ECO:0000250|UniProtKB:P47712}; CATALYTIC ACTIVITY: Reaction=2-[(15R)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl]-sn-glycero-3-phosphocholine + H2O = (15R)-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:53696, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:78837, ChEBI:CHEBI:137583; Evidence={ECO:0000250|UniProtKB:P47712}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53697; Evidence={ECO:0000250|UniProtKB:P47712}; CATALYTIC ACTIVITY: Reaction=2-(prostaglandin E2)-sn-glycero-3-phosphocholine + H2O = H(+) + prostaglandin E2 + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:53692, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:137585, ChEBI:CHEBI:606564; Evidence={ECO:0000250|UniProtKB:P47712}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53693; Evidence={ECO:0000250|UniProtKB:P47712}; CATALYTIC ACTIVITY: Reaction=2-[(11R)-hydroxy-(5Z,8Z,12E,14Z)-eicosatetraenoyl]-sn-glycero-3-phosphocholine + H2O = (11R)-hydroxy-(5Z,8Z,12E,14Z)-eicosatetraenoate + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:53688, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:78836, ChEBI:CHEBI:137582; Evidence={ECO:0000250|UniProtKB:P47712}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53689; Evidence={ECO:0000250|UniProtKB:P47712}; CATALYTIC ACTIVITY: Reaction=1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-2-O-hexadecyl-sn-glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 2-O-hexadecyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:41271, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:77695, ChEBI:CHEBI:77696; Evidence={ECO:0000250|UniProtKB:P47712}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41272; Evidence={ECO:0000250|UniProtKB:P47712}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine + glycerol = 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + 1-octadecanoyl-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:41099, ChEBI:CHEBI:17754, ChEBI:CHEBI:73858, ChEBI:CHEBI:74965, ChEBI:CHEBI:75612; Evidence={ECO:0000250|UniProtKB:P47712}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41100; Evidence={ECO:0000250|UniProtKB:P47712}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(9Z,12Z,15Z-octadecatrienoyl)-sn-glycero-3-phosphocholine + glycerol = 1-(9Z,12Z,15Z-octadecatrienoyl)-glycerol + 1-octadecanoyl-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:41087, ChEBI:CHEBI:17754, ChEBI:CHEBI:73858, ChEBI:CHEBI:75610, ChEBI:CHEBI:78022; Evidence={ECO:0000250|UniProtKB:P47712}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41088; Evidence={ECO:0000250|UniProtKB:P47712};
null
PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism. {ECO:0000250|UniProtKB:P47713}.; PATHWAY: Lipid metabolism; arachidonate metabolism. {ECO:0000250|UniProtKB:P47712}.; PATHWAY: Lipid metabolism; prostaglandin biosynthesis. {ECO:0000250|UniProtKB:P47712}.; PATHWAY: Lipid metabolism; leukotriene B4 biosynthesis. {ECO:0000250|UniProtKB:P47712}.
null
null
FUNCTION: Has primarily calcium-dependent phospholipase and lysophospholipase activities, with a major role in membrane lipid remodeling and biosynthesis of lipid mediators of the inflammatory response (By similarity). Plays an important role in embryo implantation and parturition through its ability to trigger prostanoid production (By similarity). Preferentially hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity). Selectively hydrolyzes sn-2 arachidonoyl group from membrane phospholipids, providing the precursor for eicosanoid biosynthesis via the cyclooxygenase pathway. In an alternative pathway of eicosanoid biosynthesis, hydrolyzes sn-2 fatty acyl chain of eicosanoid lysophopholipids to release free bioactive eicosanoids. Hydrolyzes the ester bond of the fatty acyl group attached at sn-1 position of phospholipids (phospholipase A1 activity) only if an ether linkage rather than an ester linkage is present at the sn-2 position. This hydrolysis is not stereospecific. Has calcium-independent phospholipase A2 and lysophospholipase activities in the presence of phosphoinositides. Has O-acyltransferase activity. Catalyzes the transfer of fatty acyl chains from phospholipids to a primary hydroxyl group of glycerol (sn-1 or sn-3), potentially contributing to monoacylglycerol synthesis (By similarity). {ECO:0000250|UniProtKB:P47712, ECO:0000250|UniProtKB:P47713}.
Bos taurus (Bovine)
A4IG62
SUV3_DANRE
MSVNRCIYLLSRSHIRYRVCASTNLSTVSTLSTTQHSTRRTFDKLSTRHSSSGSSRPLDTSLFIPLPVKTDEDAEGSVGAELTKPLDKNELLKVLNRFYKRKEMQKLASDQGLDARLFHQAFVSFRKYVLEMNSLNADLHIILNDICCGAGHIDDIFPYFMRHAKQIFPMLDCIDDLRKISDLRVPANWYPEARAIQRKIVFHAGPTNSGKTYHAIKRYLEAKSGVYCGPLKLLAHEIYEKSNAAGVPCDLVTGEERIFVDPEGKPSGHIASTIEMCSVTTPYEVAVIDEIQMIKDPARGWAWTRALLGLCAEEIHVCGEAAAVDFITELMFTTGEEVEVHNYKRLTPFSISNHAVESLDNLKPGDCIVCFSKNDIYSISRQIEIRGLECAVIYGSLPPGTKLAQAKKFNDPDDPCKILVATDAIGMGLNLSIRRIIFNSLVKHSLNEKGEKEVDTISTSQALQIAGRAGRFSSVFKEGEVTTMHRDDLPVLKEILGKPVDPIATAGLHPTAEQIEMFAYHLPQATLSNLIDIFVSLSQVDGLYFVCNIDDFKFLADMIQHIPLNLRSRYVFCTAPINKKQPFVCTSFLKFARQFSRDEPLTFNWVCRQVNWPLSPPKNIKDLVHLEAVHDVLDLYLWLSYRFMDMFPDSNQIREIQKELDENIQIGVRNITRLIRAIDSQPTDTESNSSSTVPESETSQRKGRVLRSQNQRKELPRKSSLSSRLLRDGLLTKELLSQLQKEWAREQNEDNSIPVNNGKRKKK
3.6.4.13
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
DNA duplex unwinding [GO:0032508]; DNA recombination [GO:0006310]; liver development [GO:0001889]; mitochondrial mRNA catabolic process [GO:0000958]; mitochondrial mRNA surveillance [GO:0035946]; mitochondrial ncRNA surveillance [GO:0035945]; mitochondrial RNA 3'-end processing [GO:0000965]; mitochondrial RNA surveillance [GO:2000827]; mitochondrion organization [GO:0007005]; negative regulation of apoptotic process [GO:0043066]; positive regulation of cell growth [GO:0030307]; positive regulation of mitochondrial RNA catabolic process [GO:0000962]; RNA catabolic process [GO:0006401]
mitochondrial degradosome [GO:0045025]; mitochondrial matrix [GO:0005759]; mitochondrial nucleoid [GO:0042645]; mitochondrion [GO:0005739]; nucleus [GO:0005634]
3'-5' RNA helicase activity [GO:0034458]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; DNA helicase activity [GO:0003678]; double-stranded RNA binding [GO:0003725]; RNA helicase activity [GO:0003724]
PF00271;PF12513;PF18147;PF18114;
1.10.1740.140;1.20.272.40;1.20.58.1080;3.40.50.300;
Helicase family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Mitochondrion matrix {ECO:0000250}. Mitochondrion matrix, mitochondrion nucleoid {ECO:0000250}.
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: Major helicase player in mitochondrial RNA metabolism. Component of the mitochondrial degradosome (mtEXO) complex, that degrades 3' overhang double-stranded RNA with a 3'-to-5' directionality in an ATP-dependent manner. ATPase and ATP-dependent multisubstrate helicase, able to unwind double-stranded (ds) DNA and RNA, and RNA/DNA heteroduplexes in the 5'-to-3' direction. Plays a role in the RNA surveillance system in mitochondria; regulates the stability of mature mRNAs, the removal of aberrantly formed mRNAs and the rapid degradation of non coding processing intermediates. Also implicated in recombination and chromatin maintenance pathways. May protect cells from apoptosis. Associates with mitochondrial DNA (By similarity). {ECO:0000250}.
Danio rerio (Zebrafish) (Brachydanio rerio)
A4IGL7
PXDN_XENTR
MAGAGSWLYLTAGLLVVALPQLSHSCPSRCLCFRTTVRCMHLMLESVPAVPPHTTILDLRFNRIKDIQTGAFKHLKNLNTLLLNNNQIKRIPSEAFKDLENLKYLYLYKNEIQSIDRQAFKGLASLEQLYLHFNQIETLEPESFNYLPKLERLFLHNNRITHLVPGTFSQLESMKRLRLDSNALHCDCEILWLADLLKIYSESGNAQAAATCEYPRRLQGRSVSTITPSELNCERPRITSEPQDVDVTFGNTVYFTCRAEGNPKPEIIWLRNNNELSMKDDSRLNLLNDGTLMIQNTKETDQGIYQCMAKNVAGEVKTHEVTLRYYGTPATPTFVIQPQNTEVLVGESVTLECSATGQPHPRVTWTRGDRTPLPSDPRINITPSGGLYIQNVNQDDAGEYTCFATNSVETIHSTAYIIVQAVPQFTVVPQDRNVFEGHTVDFHCEAQGNPKPVIAWTKGGNQLSVDRRHQVLSSGTLRILRVALHDQGQYECQAVNIVGSKSTAAQLIVQTRVTPVFATVPNDMTVEVGTDVQIPCSSQGDPLPIITWNKDGIQVTESGKFHISPHGYLAIRDAGLADQGRYECVARNPIGYSSVSMVLSVLVPEVSRTGDPFVATSIIEAIATVDRAINSTRTHLFDSRPRSPGDLLALFRYPRDPYTVEQARAAEIFERTLQLIQDHVQSGLMVDLNGTSYHYNDLVSPQYLNMIANLSGCATHRRINNCSNMCFHQKYRTHDGTCNNLQHPMWGASLTAFERLLKSVYENGFNLPRGISGRIYNGFPLPLPRLVSTTLIGTHTITPDEQFTHMLMQWGQFLDHDLDSTVVALSQARFSDGQDCSVVCTNDAPCFPIMVPPNDPRVRNNARCMSMVRSSPVCGSGMTSLLMNSVYPREQMNQLTSYIDASNVYGSSDHESNEIRDSASHRGLLKQGIVQRSGKPLLPFATGPPTECMRDENESPIPCFLAGDHRANEQLGLTSMHTLWFREHNRIATELLRLNPHWDGDTIYHETRKIVGAQMQHITYSHWLPKIFGDVGMKMLGEYKSYDPNVNAGILNEFATAAFRFGHTLINPILYRLDEKFEPIPQGHVPLHRAFFSPFRIVNEGGIDPLLRGLIGVAAKMRVTSQLLNTELTEKLFSMAHAVALDLAALNVQRGRDHGIPPYHDFRVFCNLSTVQTFDDLRNEIKNPDVREKLKRLYGSPLNIDLFPALMVEDLIPGSRLGPTLMCLLTTQFRNIRDGDRFWYENPGVFTAAQLTQIKQTSLARVLCDNGDNITKVQHDLFRVAEFPHGYVSCKNIAKMDLRVWQDCCEDCRTRGQFSTFSNHFRGKRSTEHSYKEDNKEPSSLLNQSVNTTCNTEQPKNLPHVNDFKEFVLDMQKTITGLRKQIKKLESRLSNTDCTDETGESHSTKEKWNKDACTKCECYNGHITCFVKSCPPVNCSRPQRIEGVCCPVCTDDKIQST
1.11.2.-
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00298}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000255|PROSITE-ProRule:PRU00298}; COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250|UniProtKB:A5JUY8, ECO:0000255|PROSITE-ProRule:PRU00298}; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group covalently per subunit. {ECO:0000250|UniProtKB:A5JUY8, ECO:0000255|PROSITE-ProRule:PRU00298};
angiogenesis [GO:0001525]; basement membrane assembly [GO:0070831]; basement membrane organization [GO:0071711]; cell adhesion [GO:0007155]; hydrogen peroxide catabolic process [GO:0042744]; protein homooligomerization [GO:0051260]; protein homotrimerization [GO:0070207]; response to oxidative stress [GO:0006979]
basement membrane [GO:0005604]; cell surface [GO:0009986]; endoplasmic reticulum [GO:0005783]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]
heme binding [GO:0020037]; lactoperoxidase activity [GO:0140825]; metal ion binding [GO:0046872]; oxidoreductase activity, acting on peroxide as acceptor [GO:0016684]
PF03098;PF07679;PF00560;PF13855;PF01463;PF00093;
6.20.200.20;1.10.640.10;2.60.40.10;3.80.10.10;
Peroxidase family, XPO subfamily
PTM: Glycosylated. {ECO:0000250|UniProtKB:Q92626}.; PTM: Processed by FURIN and the proteolytic processing largely depends on the peroxidase activity of PXDN (By similarity). The proteolytic cleavage occurs after intracellular homotrimerization and releases into the extracellular matrix a large, catalytically active fragment and a smaller fragment consisting primarily of the C-terminal VWFC domain. The processing enhances both peroxidase activity and sulfilimine cross-links formation (By similarity). {ECO:0000250|UniProtKB:Q92626}.
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q92626}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q92626}. Cell surface {ECO:0000250|UniProtKB:Q92626}. Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000250|UniProtKB:Q3UQ28}. Note=Enriched in the peritubular space of fibrotic kidneys. Adheres on the cell surface in 'hot spots'. {ECO:0000250|UniProtKB:Q92626}.; SUBCELLULAR LOCATION: [PXDN active fragment]: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q92626}.
CATALYTIC ACTIVITY: Reaction=H2O2 + L-lysyl-[collagen] + L-methionyl-[collagen] = [collagen]-L-lysyl-N-S-L-methionyl-[collagen] + H(+) + 2 H2O; Xref=Rhea:RHEA:66020, Rhea:RHEA-COMP:12751, Rhea:RHEA-COMP:16949, Rhea:RHEA-COMP:16951, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16044, ChEBI:CHEBI:16240, ChEBI:CHEBI:29969, ChEBI:CHEBI:166867; Evidence={ECO:0000250|UniProtKB:Q92626}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66021; Evidence={ECO:0000250|UniProtKB:Q92626}; CATALYTIC ACTIVITY: Reaction=bromide + H2O2 = H2O + hypobromite; Xref=Rhea:RHEA:66016, ChEBI:CHEBI:15377, ChEBI:CHEBI:15858, ChEBI:CHEBI:16240, ChEBI:CHEBI:29250; Evidence={ECO:0000250|UniProtKB:Q92626}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66017; Evidence={ECO:0000250|UniProtKB:Q92626}; CATALYTIC ACTIVITY: Reaction=hypobromite + L-lysyl-[collagen] + L-methionyl-[collagen] = [collagen]-L-lysyl-N-S-L-methionyl-[collagen] + bromide + H(+) + H2O; Xref=Rhea:RHEA:66024, Rhea:RHEA-COMP:12751, Rhea:RHEA-COMP:16949, Rhea:RHEA-COMP:16951, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15858, ChEBI:CHEBI:16044, ChEBI:CHEBI:29250, ChEBI:CHEBI:29969, ChEBI:CHEBI:166867; Evidence={ECO:0000250|UniProtKB:Q92626}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66025; Evidence={ECO:0000250|UniProtKB:Q92626}; CATALYTIC ACTIVITY: Reaction=bromide + H(+) + H2O2 + L-tyrosyl-[protein] = 3-bromo-L-tyrosyl-[protein] + 2 H2O; Xref=Rhea:RHEA:69360, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:17686, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15858, ChEBI:CHEBI:16240, ChEBI:CHEBI:46858, ChEBI:CHEBI:183512; Evidence={ECO:0000250|UniProtKB:Q92626}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69361; Evidence={ECO:0000250|UniProtKB:Q92626}; CATALYTIC ACTIVITY: Reaction=H(+) + hypobromite + L-tyrosyl-[protein] = 3-bromo-L-tyrosyl-[protein] + H2O; Xref=Rhea:RHEA:69356, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:17686, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29250, ChEBI:CHEBI:46858, ChEBI:CHEBI:183512; Evidence={ECO:0000250|UniProtKB:Q92626}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69357; Evidence={ECO:0000250|UniProtKB:Q92626};
null
null
null
null
FUNCTION: Catalyzes the two-electron oxidation of bromide by hydrogen peroxide and generates hypobromite as a reactive intermediate which mediates the formation of sulfilimine cross-links between methionine and hydroxylysine residues within an uncross-linked collagen IV/COL4A1 NC1 hexamer and participates to the basement membrane integrity. Moreover brominates alpha2 collagen IV chain/COL4A2 and leads to bromine enrichment of the basement membranes. {ECO:0000250|UniProtKB:Q92626}.
Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
A4IGM9
AURKB_XENTR
MSYKENLNPSSYTSKFATPSSATAAQRVLRKEPYVSTFTTPSDNLLAQRAQLARITPSASSSVPGRVAVSMDASSQNTALAELPKRKFTIDDFDIGRPLGKGKFGNVYLARDKQNKFIMALKVLFKSQLEKEGVEHQLRREIEIQSHLRHPNILRMYNYFHDRKRIYLMLEFAPRGELYKELQKHGRFDEQRSATFMEELADALQYCHERKVIHRDIKPENLLMGYKGELKIADFGWSVHAPSLRRRTMCGTLDYLPPEMIEGKTHDEKVDLWCAGVLCFEFLVGMPPFDSPSHTETHRRIVNVDLKFPPFLSDGSKDLISKLLRYHPPQRLPLKGVMEHPWVKANSRRVLPPVFQSSSK
2.7.11.1
null
abscission [GO:0009838]; cellular response to UV [GO:0034644]; cleavage furrow formation [GO:0036089]; mitotic cytokinesis checkpoint signaling [GO:0044878]; mitotic spindle midzone assembly [GO:0051256]; negative regulation of B cell apoptotic process [GO:0002903]; negative regulation of cytokinesis [GO:0032466]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of cytokinesis [GO:0032467]; positive regulation of mitotic sister chromatid segregation [GO:0062033]; post-translational protein modification [GO:0043687]; protein localization to kinetochore [GO:0034501]; protein phosphorylation [GO:0006468]; spindle assembly [GO:0051225]
chromatin [GO:0000785]; chromosome [GO:0005694]; chromosome passenger complex [GO:0032133]; chromosome, centromeric region [GO:0000775]; cytoplasm [GO:0005737]; kinetochore [GO:0000776]; midbody [GO:0030496]; nucleus [GO:0005634]; spindle microtubule [GO:0005876]; spindle midzone [GO:0051233]; spindle pole centrosome [GO:0031616]
ATP binding [GO:0005524]; histone H3S10 kinase activity [GO:0035175]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
PF00069;
1.10.510.10;
Protein kinase superfamily, Ser/Thr protein kinase family, Aurora subfamily
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96GD4}. Chromosome {ECO:0000250|UniProtKB:Q96GD4}. Chromosome, centromere {ECO:0000250|UniProtKB:Q96GD4}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q96GD4}. Midbody {ECO:0000250|UniProtKB:Q96GD4}. Note=Localizes on chromosome arms and inner centromeres from prophase through metaphase and then transferring to the spindle midzone and midbody from anaphase through cytokinesis. Localization (and probably targeting of the CPC) to the inner centromere occurs predominantly in regions with overlapping mitosis-specific histone phosphorylations H3pT3 and H2ApT12. {ECO:0000250|UniProtKB:Q96GD4}.
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:Q96GD4}; 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:Q96GD4};
null
null
null
null
FUNCTION: Serine/threonine-protein kinase component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Involved in the bipolar attachment of spindle microtubules to kinetochores and is a key regulator for the onset of cytokinesis during mitosis. Required for central/midzone spindle assembly and cleavage furrow formation. Key component of the cytokinesis checkpoint, a process required to delay abscission to prevent both premature resolution of intercellular chromosome bridges and accumulation of DNA damage. Phosphorylates 'Ser-10' of histone H3 during mitosis. {ECO:0000250|UniProtKB:Q96GD4}.
Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
A4IGY6
S39AE_XENTR
MPLLLLSALLPFSLMAGPTPSTGKELSAASFLQDILQRYGENESLSMPQLQSLLENLEVGKGGGNQRNMSQCLSSSTLFAAHNLTSGSVVDAEGFQSFCPTILQQLETRACQESPAFQNETTPGAEGRPSPGEVWGYGFLCVTVISLCSLFGAGVVPFMKKACYKRLLLFCIALAIGTLFSNALFQLIPEAFGFNPLEDSYVFTSSVIFGGFYLFFFTEKVLKMMLKQKHEHGHSHYSADTSKRDAEEGVTEKLQNGDLDHMIPPPHGSESDLRGDEKAVQQQDLPGQQSSCYWLKGIRYSDIGTLAWMITLSDGLHNFIDGLAIGASFTVSVFQGVSTSIAILCEEFPHELGDFVILLNAGMSIPQALFFNFLSACCCYLGLAFGILAGSHFSSNWIFALAGGMFLYIALSDMFPEMNEVSKEDEEGGRAFSAFMIQNAGLLTGFAIMLLLTTFSGQIQLG
null
null
cellular response to glucose stimulus [GO:0071333]; cellular response to insulin stimulus [GO:0032869]; import across plasma membrane [GO:0098739]; inorganic cation transmembrane transport [GO:0098662]; intracellular zinc ion homeostasis [GO:0006882]; iron import into cell [GO:0033212]; iron ion transmembrane transport [GO:0034755]; manganese ion homeostasis [GO:0055071]; manganese ion transmembrane transport [GO:0071421]; negative regulation of cyclic-nucleotide phosphodiesterase activity [GO:0051344]; positive regulation of G protein-coupled receptor signaling pathway [GO:0045745]; zinc ion import across plasma membrane [GO:0071578]; zinc ion transmembrane transport [GO:0071577]
apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; early endosome membrane [GO:0031901]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; plasma membrane [GO:0005886]
cadmium ion transmembrane transporter activity [GO:0015086]; iron ion transmembrane transporter activity [GO:0005381]; manganese ion transmembrane transporter activity [GO:0005384]; monoatomic anion:monoatomic cation symporter activity [GO:0015296]; monoatomic cation:bicarbonate symporter activity [GO:0140410]; zinc ion transmembrane transporter activity [GO:0005385]
PF02535;
null
ZIP transporter (TC 2.A.5) family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q15043}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:Q15043}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q15043}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000250|UniProtKB:Q15043}; Multi-pass membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000250|UniProtKB:Q15043}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:Q15043}; Multi-pass membrane protein {ECO:0000255}.
CATALYTIC ACTIVITY: Reaction=2 hydrogencarbonate(out) + Zn(2+)(out) = 2 hydrogencarbonate(in) + Zn(2+)(in); Xref=Rhea:RHEA:62252, ChEBI:CHEBI:17544, ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q75N73}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62253; Evidence={ECO:0000250|UniProtKB:Q75N73}; CATALYTIC ACTIVITY: Reaction=2 hydrogencarbonate(out) + Mn(2+)(out) = 2 hydrogencarbonate(in) + Mn(2+)(in); Xref=Rhea:RHEA:62260, ChEBI:CHEBI:17544, ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q75N73}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62261; Evidence={ECO:0000250|UniProtKB:Q75N73}; CATALYTIC ACTIVITY: Reaction=Fe(2+)(out) + 2 hydrogencarbonate(out) = Fe(2+)(in) + 2 hydrogencarbonate(in); Xref=Rhea:RHEA:62368, ChEBI:CHEBI:17544, ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:Q75N73}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62369; Evidence={ECO:0000250|UniProtKB:Q75N73}; CATALYTIC ACTIVITY: Reaction=Cd(2+)(out) + 2 hydrogencarbonate(out) = Cd(2+)(in) + 2 hydrogencarbonate(in); Xref=Rhea:RHEA:62256, ChEBI:CHEBI:17544, ChEBI:CHEBI:48775; Evidence={ECO:0000250|UniProtKB:Q75N73}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62257; Evidence={ECO:0000250|UniProtKB:Q75N73};
null
null
null
null
FUNCTION: Electroneutral transporter of the plasma membrane mediating the cellular uptake of the divalent metal cations zinc, manganese and iron that are important for tissue homeostasis, metabolism, development and immunity (By similarity). Functions as an energy-dependent symporter, transporting through the membranes an electroneutral complex composed of a divalent metal cation and two bicarbonate anions. Beside these endogenous cellular substrates, can also import cadmium a non-essential metal which is cytotoxic and carcinogenic (By similarity). {ECO:0000250|UniProtKB:Q15043, ECO:0000250|UniProtKB:Q75N73}.
Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
A4IH17
BAG6_XENTR
MEVTVKTLDSQTRTFTVDAEITVKEFKTHISSDVGISPEKQRLIYQGRVLQEDKKLKEYNVDGKVIHLVERAPPQTQPSTGGPSTSSSTSPSSSNAANVPGAGAPERNGNSYVMVGTFNLPHVMSGLGEASRGPRVSTVSGNDGSTLDVHINLDQQLPVQSEPRVRLVLAQQILQDIQRILDRLEGQPVNEQTAEPMDTAVSEGEASSRETLPQTTQNTDGQSNTAPTSHPSPSEYVEVLQSLSRVEERLAPFMQRYREILSSATSDAYENQEEREQSQRIINLVGESLRLLGNALVAVSDLRCNLSSASPRHLHVVRPMSHYTGPMLLQQAAIPIQINVGTTVTMTGNGTHAGQMPSDGNAAHTPTNTSEPQRSNSDNQPPSSGERPASEIPPTSVPHPHPRVVRITHQTVEPVMMMHMNIQDSGPGGPTNIPPPTAGHGGSAHIHMPGLPPEFMQAISHQITQQAVAAASGQQIPGFQAPPRFVFTRPAAPSFPPQPGVATTPPGPGGATTAVPGATVGPAGNASLAQMISGLVGQLLMHPVIVAQGGSNTPSSTSTPTSTSSSSSSSSSTVTTSTTTTSSTSFPTVSSGPSPQPPPGTDQHLSQLLGSLLGTAGSGMSNFAMGSPSITVTVPGMPAFLQGVTDILQATQTVPVSTSPPQSASQAPPPSSPSPPPAHSSPPPAAAPESLPPEFFTSVVQGVLSSMLGSLSAADQSGTESIAAFIQRLSGSHNIFQPDAEGPGGFFGDLLTLICHNFSLVDMVMLLHGHSQPLQNLQPQLRSFFLQEYLHQADPTPNNIQMASRNLTNGLEEYIRESFASVTVRDDVDITRTNLEFLQDQFNRITTHILHCADSTFGQRLLEMCNQSLFEWLALNLYCLRGDQSALTSVINERIRRLSLDVSPVLVSWVTSVLSLRLQVLLGQMPVTEGEIQRHIRRVGDVPQAPEASSQDQPMETTPVDCQNGAASPVPATTVEEVLFLPPQSSVPTICTDSEHPTQEDTGSEQWAASVPPEWVPVIRQDMQNQRKMKQQPPLSDAYLSGMPAKRRKTMQGEGPHLSLSEAVSRAMKATGAKPESSTDCVRRELDNSEAQGRYREQLCQDIQNILQDNESYSAQRFPNTQRAFRGDP
null
null
brain development [GO:0007420]; chromatin organization [GO:0006325]; endoplasmic reticulum stress-induced pre-emptive quality control [GO:0061857]; ERAD pathway [GO:0036503]; internal peptidyl-lysine acetylation [GO:0018393]; intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [GO:0042771]; intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress [GO:0070059]; kidney development [GO:0001822]; lung development [GO:0030324]; negative regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032435]; negative regulation of proteolysis [GO:0045861]; proteasomal protein catabolic process [GO:0010498]; protein stabilization [GO:0050821]; regulation of apoptotic process [GO:0042981]; regulation of embryonic development [GO:0045995]; spermatogenesis [GO:0007283]; synaptonemal complex assembly [GO:0007130]; tail-anchored membrane protein insertion into ER membrane [GO:0071816]; ubiquitin-dependent protein catabolic process [GO:0006511]
BAT3 complex [GO:0071818]; cytosol [GO:0005829]; extracellular region [GO:0005576]; nucleus [GO:0005634]
misfolded protein binding [GO:0051787]; polyubiquitin modification-dependent protein binding [GO:0031593]; proteasome binding [GO:0070628]; ribosome binding [GO:0043022]
PF12057;PF20960;PF00240;
null
null
null
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P46379}. Nucleus {ECO:0000250|UniProtKB:P46379}. Secreted, extracellular exosome {ECO:0000250|UniProtKB:P46379}.
null
null
null
null
null
FUNCTION: ATP-independent molecular chaperone preventing the aggregation of misfolded and hydrophobic patches-containing proteins. Functions as part of a cytosolic protein quality control complex, the bag6/bat3 complex, which maintains these client proteins in a soluble state and participates in their proper delivery to the endoplasmic reticulum or alternatively can promote their sorting to the proteasome where they undergo degradation. The bag6/bat3 complex is involved in the post-translational delivery of tail-anchored/type II transmembrane proteins to the endoplasmic reticulum membrane. Similarly, the bag6/bat3 complex also functions as a sorting platform for proteins of the secretory pathway that are mislocalized to the cytosol either delivering them to the proteasome for degradation or to the endoplasmic reticulum. The bag6/bat3 complex also plays a role in the endoplasmic reticulum-associated degradation (ERAD), a quality control mechanism that eliminates unwanted proteins of the endoplasmic reticulum through their retrotranslocation to the cytosol and their targeting to the proteasome. It maintains these retrotranslocated proteins in an unfolded yet soluble state condition in the cytosol to ensure their proper delivery to the proteasome. Also required for selective ubiquitin-mediated degradation of defective nascent chain polypeptides by the proteasome. Also involved in endoplasmic reticulum stress-induced pre-emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for proteasomal degradation. May ensure the proper degradation of these proteins and thereby protects the endoplasmic reticulum from protein overload upon stress. By stabilizing a large spectrum of proteins, may indirectly affect different biological processes including apoptosis. By controlling the steady-state expression of the IGF1R receptor, indirectly regulates the insulin-like growth factor receptor signaling pathway. {ECO:0000250|UniProtKB:P46379}.; FUNCTION: When nuclear, may also act as a component of some chromatin regulator complex. {ECO:0000250|UniProtKB:P46379}.
Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
A4IHB9
SL9B2_XENTR
MEDSLFSVDKAGPGKDASAASADCNHMVAEDGIITEQHKEIPLVALKVPDGHAPIDECELLNSDDQLPKGSQNQTNICMRIRAFACPPQGCFSLAITNVTMVILIWAVVWSITGPECLPGGNLFGILALLFSAALGGKLISLIKIPSLPPLPPLLGMLLAGFLIRNIPVITDQVQIHHKWSAALRNIALAIILVRAGLGLDPKALRKLKAVCLRLSFGPCVVESCTAAVVSHFIMGFPLTWGFMLGFVLGAVSPAVVVPSMLILQKEGFGVDKGIPTLLMAAGSFDDVLAITGFNTCLGMAFSSGSTLNTIVRGVLEVVVGIAAGLLFGFFLHYFPSKDQENLKGKRSYLILALSVFAVFGSLYFGFPGSGGLCTLVMAFLAGIGWSTDKTVVEDIIAVSWDIFQPLLFGLIGAEISVASLKPETVGLCTATLIIALIIRICISFLMVCFSGFSLKEKIFISLAWMPKATVQAAIGSVALDTARTLENKQFEDYGMDVLTVAFLGILVTAPIGALVIGLTGPKMLEKSESRTVTEEGSV
null
null
proton transmembrane transport [GO:1902600]; sodium ion homeostasis [GO:0055078]; sodium ion transport [GO:0006814]
apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; mitochondrial membrane [GO:0031966]; recycling endosome [GO:0055037]; recycling endosome membrane [GO:0055038]; synaptic vesicle membrane [GO:0030672]
antiporter activity [GO:0015297]; metal ion binding [GO:0046872]
PF00999;
1.20.1530.20;
Monovalent cation:proton antiporter 1 (CPA1) transporter (TC 2.A.36) family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q5BKR2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A0A6P3HVI0}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q5BKR2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A0A6P3HVI0}. Endosome membrane {ECO:0000250|UniProtKB:Q5BKR2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A0A6P3HVI0}. Recycling endosome membrane {ECO:0000250|UniProtKB:Q5BKR2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A0A6P3HVI0}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:Q5BKR2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A0A6P3HVI0}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q5BKR2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A0A6P3HVI0}. Apical cell membrane {ECO:0000250|UniProtKB:Q5BKR2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A0A6P3HVI0}.
CATALYTIC ACTIVITY: Reaction=H(+)(in) + Li(+)(out) = H(+)(out) + Li(+)(in); Xref=Rhea:RHEA:72407, ChEBI:CHEBI:15378, ChEBI:CHEBI:49713; Evidence={ECO:0000250|UniProtKB:Q86UD5}; CATALYTIC ACTIVITY: Reaction=Li(+)(in) + Na(+)(out) = Li(+)(out) + Na(+)(in); Xref=Rhea:RHEA:72415, ChEBI:CHEBI:29101, ChEBI:CHEBI:49713; Evidence={ECO:0000250|UniProtKB:Q86UD5}; CATALYTIC ACTIVITY: Reaction=H(+)(out) + Na(+)(in) = H(+)(in) + Na(+)(out); Xref=Rhea:RHEA:29419, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101; Evidence={ECO:0000250|UniProtKB:Q86UD5};
null
null
null
null
FUNCTION: Electroneutral Na(+) Li(+)/H(+) antiporter that extrudes Na(+) or Li(+) in exchange for external protons across the membrane (By similarity). Uses the proton gradient/membrane potential to extrude sodium (By similarity). Contributes to the regulation of intracellular pH and sodium homeostasis (By similarity). Also able to mediate Na(+)/Li(+) antiporter activity in kidney (By similarity). {ECO:0000250|UniProtKB:Q5BKR2, ECO:0000250|UniProtKB:Q86UD5}.
Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
A4IHS0
TM10C_XENTR
MAFVNTLLRTIRCSAVHTLVQEGRSLSLLKASHQLTQSRKIMLSNHVRKEEAKSEPNETLDLEEWKSILKSDIGNAEMVKTETQEDSSLNEMQELVEMWRLAGRAVPQSITTEQLQVLMELPTKTARKKYLKYLSVREVMKTNRKEKKKELKESKSKIESLDQLETKEDTPEKKNTFLLHVWDKSIDTMQRWKCVQAMKFGQPLVFDMVYEKNMSRYELENTVCQLMESEGWNRRSTDPFHIYFCSLQPYSMYHKELVKRYIGAWDNVFVTATDKSHVEMFPKEQLVYLTADSPNELKHFDHTKIYIIGSLVDRCQQTGLSLANAKRLNLATARLPLDRYLKWDVGAKNLTLDQMIRILLCLKDTGDWKKALSFVPNRKHDGFAEPAASKKRNIKNDGGMEYAASTKRNLQKNSKMYKFGASKSFIKPERTDDTSIRSTRKRWWEEEN
2.1.1.-; 2.1.1.218; 2.1.1.221
null
mitochondrial tRNA 5'-end processing [GO:0097745]; mitochondrial tRNA processing [GO:0090646]; mRNA methylation [GO:0080009]; positive regulation of mitochondrial translation [GO:0070131]
mitochondrial nucleoid [GO:0042645]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]
tRNA (adenine(9)-N1)-methyltransferase activity [GO:0160106]; tRNA (guanosine(9)-N1)-methyltransferase activity [GO:0052905]; tRNA binding [GO:0000049]
PF01746;
3.40.1280.30;
Class IV-like SAM-binding methyltransferase superfamily, TRM10 family
null
SUBCELLULAR LOCATION: Mitochondrion matrix, mitochondrion nucleoid {ECO:0000250|UniProtKB:Q7L0Y3}.
CATALYTIC ACTIVITY: Reaction=adenosine(9) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methyladenosine(9) in tRNA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:43148, Rhea:RHEA-COMP:10363, Rhea:RHEA-COMP:10364, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74411, ChEBI:CHEBI:74491; EC=2.1.1.218; Evidence={ECO:0000250|UniProtKB:Q7L0Y3}; CATALYTIC ACTIVITY: Reaction=guanosine(9) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(9) in tRNA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:43156, Rhea:RHEA-COMP:10367, Rhea:RHEA-COMP:10368, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:73542, ChEBI:CHEBI:74269; EC=2.1.1.221; Evidence={ECO:0000250|UniProtKB:Q7L0Y3}; CATALYTIC ACTIVITY: Reaction=an adenosine in mRNA + S-adenosyl-L-methionine = an N(1)-methyladenosine in mRNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:55392, Rhea:RHEA-COMP:12414, Rhea:RHEA-COMP:12415, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74411, ChEBI:CHEBI:74491; Evidence={ECO:0000250|UniProtKB:Q7L0Y3};
null
null
null
null
FUNCTION: Mitochondrial tRNA N(1)-methyltransferase involved in mitochondrial tRNA maturation. Component of mitochondrial ribonuclease P, which cleaves tRNA molecules in their 5'-ends. Together with hsd17b10/mrpp2, forms a subcomplex of the mitochondrial ribonuclease P, named MRPP1-MRPP2 subcomplex, which displays functions that are independent of the ribonuclease P activity. The MRPP1-MRPP2 subcomplex catalyzes the formation of N(1)-methylguanine and N(1)-methyladenine at position 9 (m1G9 and m1A9, respectively) in tRNAs; trmt10c/mrpp1 acting as the catalytic N(1)-methyltransferase subunit. The MRPP1-MRPP2 subcomplex also acts as a tRNA maturation platform: following 5'-end cleavage by the mitochondrial ribonuclease P complex, the MRPP1-MRPP2 subcomplex enhances the efficiency of 3'-processing catalyzed by ELAC2, retains the tRNA product after elac2 processing and presents the nascent tRNA to the mitochondrial CCA tRNA nucleotidyltransferase TRNT1 enzyme. In addition to tRNA N(1)-methyltransferase activity, trmt10c/mrpp1 also acts as a mRNA N(1)-methyltransferase by mediating methylation of adenosine residues at the N(1) position of MT-ND5 mRNA. {ECO:0000250|UniProtKB:Q7L0Y3}.
Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
A4II96
CNOT7_XENTR
MPAATVDLSQRICEVWACNLDDQMKRIRQVIRKYNYVAMDTEFPGVVARPIGEFRSNADYQYQLLRCNVDLLKIIQLGLTFVNEQGEYPPGTSTWQFNFKFNLTEDMYAQDSIELLTSSGIQFKKHEEEGIETQYFAELFMTSGVVLCEGVKWLSFHSGYDFGYLIKILTNSNLPEVELDFFEILRLFFPVIYDVKYLMKSCKNLKGGLQEVAEQLELKRIGPQHQAGSDSLLTGMAFFKMREMFFEDHIDDAKYCGHLYGLGSGSSYVQNGTGNAYEEEANKQS
3.1.13.4
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q9UIV1}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9UIV1}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250|UniProtKB:Q9UIV1}; Note=Binds 2 divalent metal cations per subunit with RNAase activity being higher in presence of Mn(2+) than of Mg(2+) or Co(2+). {ECO:0000250|UniProtKB:Q9UIV1};
exonucleolytic catabolism of deadenylated mRNA [GO:0043928]; negative regulation of cell population proliferation [GO:0008285]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:1900153]; positive regulation of nuclear-transcribed mRNA poly(A) tail shortening [GO:0060213]; regulation of translation [GO:0006417]; regulatory ncRNA-mediated gene silencing [GO:0031047]
CCR4-NOT complex [GO:0030014]; CCR4-NOT core complex [GO:0030015]; nucleus [GO:0005634]; P-body [GO:0000932]
3'-5'-RNA exonuclease activity [GO:0000175]; metal ion binding [GO:0046872]; poly(A)-specific ribonuclease activity [GO:0004535]; RNA binding [GO:0003723]; RNA exonuclease activity [GO:0004532]
PF04857;
3.30.420.10;
CAF1 family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.; EC=3.1.13.4;
null
null
null
null
FUNCTION: Has 3'-5' poly(A) exoribonuclease activity for synthetic poly(A) RNA substrate. Catalytic component of the CCR4-NOT complex which is one of the major cellular mRNA deadenylases and is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. During miRNA-mediated repression the complex seems also to act as translational repressor during translational initiation. Additional complex functions may be a consequence of its influence on mRNA expression.
Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
A4IID1
MGT4A_XENTR
MRLRNGTVATALVFITTFLSLSWYTAWQNGKEKLMAYQREFHALKERLRIAEHRTLQRSSELHAILDHFRRMIKEANGSRDALNHFSDETQKLIKDLTNRKALQVPNIYYHMPHLLNHDGSLQPAVQVGLGRTGVSVVMGIPTVKRRVKSYLKETLHSLIDKLSPEEKLDCVIIVFVGETDLEYVNSVVASLQKEFATEISSGLVEVISPPATYYPDLNNLKETFGDSKERVRWRTKQNLDYCFLMMYAQRKGIYYIQLEDDIVAKQNYFSTIKNFALQLSSEDWMILEFSQLGFIGKMFQAPDITLIVEFILMFYKEKPIDWLLDHILWVKVCNPEKDAKHCDRQKSNLRIRFRPSLFQHVGLHSSLAGKIQKLTDKDFLKPLLHKIHVNPPAEVSTSLKVYQGHTLEKTYLGEDFFWAITPVAGDYILFKFDKPVNVERYLFRSGNPEHPGDQLWNTTVEVLPYRKDIVELRSDTKDKRLSDGFFRIGKFEDGLAEGPVNSYLNPISALRLSVLQNSAVWVILNEIHIKRNPAD
2.4.1.145
COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000250|UniProtKB:O77836};
glyoxylate metabolic process [GO:0046487]; N-glycan processing [GO:0006491]; protein N-linked glycosylation [GO:0006487]
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; extracellular region [GO:0005576]; Golgi membrane [GO:0000139]; Golgi stack [GO:0005795]; peroxisome [GO:0005777]
alanine-glyoxylate transaminase activity [GO:0008453]; alpha-1,3-mannosylglycoprotein 4-beta-N-acetylglucosaminyltransferase activity [GO:0008454]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]
PF04666;
null
Glycosyltransferase 54 family
PTM: N-glycosylated. {ECO:0000250|UniProtKB:O77836}.
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9D4R2}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9D4R2}.; SUBCELLULAR LOCATION: [Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase A soluble form]: Secreted {ECO:0000250|UniProtKB:O77836}.
CATALYTIC ACTIVITY: Reaction=N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N(4)-{beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP; Xref=Rhea:RHEA:16057, Rhea:RHEA-COMP:13526, Rhea:RHEA-COMP:14374, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:60651, ChEBI:CHEBI:139507; EC=2.4.1.145; Evidence={ECO:0000250|UniProtKB:Q9UM21}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16058; Evidence={ECO:0000250|UniProtKB:Q9UM21}; CATALYTIC ACTIVITY: Reaction=N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N(4)-{beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP; Xref=Rhea:RHEA:69615, Rhea:RHEA-COMP:14369, Rhea:RHEA-COMP:17732, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:60615, ChEBI:CHEBI:187873; Evidence={ECO:0000250|UniProtKB:Q9UM21}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69616; Evidence={ECO:0000250|UniProtKB:Q9UM21}; CATALYTIC ACTIVITY: Reaction=N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-{beta-D-GlcNAc-(1->6)}-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-asparaginyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N(4)-{beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-{beta-D-GlcNAc-(1->6)}-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-asparaginyl-[protein] + UDP; Xref=Rhea:RHEA:69619, Rhea:RHEA-COMP:17733, Rhea:RHEA-COMP:17734, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:187874, ChEBI:CHEBI:187875; Evidence={ECO:0000250|UniProtKB:Q9UM21}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69620; Evidence={ECO:0000250|UniProtKB:Q9UM21}; CATALYTIC ACTIVITY: Reaction=N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-[alpha-L-Fuc-(1->6)]-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N(4)-{beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-[alpha-L-Fuc-(1->6)]-beta-D-GlcNAc}-asparaginyl-[protein] + UDP; Xref=Rhea:RHEA:69623, Rhea:RHEA-COMP:13532, Rhea:RHEA-COMP:18198, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:137207, ChEBI:CHEBI:187877; Evidence={ECO:0000250|UniProtKB:Q9UM21}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69624; Evidence={ECO:0000250|UniProtKB:Q9UM21}; CATALYTIC ACTIVITY: Reaction=N(4)-{beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-asparaginyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N(4)-{beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP; Xref=Rhea:RHEA:69627, Rhea:RHEA-COMP:17737, Rhea:RHEA-COMP:17738, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:187878, ChEBI:CHEBI:187879; Evidence={ECO:0000250|UniProtKB:Q9UM21}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69628; Evidence={ECO:0000250|UniProtKB:Q9UM21}; CATALYTIC ACTIVITY: Reaction=N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-{alpha-D-Man-(1->6)}-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-asparaginyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N(4)-{beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-{alpha-D-Man-(1->6)}-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-asparaginyl-[protein] + UDP; Xref=Rhea:RHEA:69631, Rhea:RHEA-COMP:17739, Rhea:RHEA-COMP:17740, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:187880, ChEBI:CHEBI:187881; Evidence={ECO:0000250|UniProtKB:Q9UM21}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69632; Evidence={ECO:0000250|UniProtKB:Q9UM21}; CATALYTIC ACTIVITY: Reaction=N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-asparaginyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N(4)-{beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-asparaginyl-[protein] + UDP; Xref=Rhea:RHEA:69635, Rhea:RHEA-COMP:17741, Rhea:RHEA-COMP:17742, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:187882, ChEBI:CHEBI:187883; Evidence={ECO:0000250|UniProtKB:Q9UM21}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69636; Evidence={ECO:0000250|UniProtKB:Q9UM21};
null
PATHWAY: Protein modification; protein glycosylation. {ECO:0000250|UniProtKB:O77836}.
null
null
FUNCTION: Glycosyltransferase that catalyze the transfer of GlcNAc from UDP-GlcNAc to the GlcNAcbeta1-2Manalpha1-3 arm of the core structure of N-linked glycans through a beta1-4 linkage and participates in the production of tri- and tetra-antennary N-linked sugar chains (By similarity). Involved in glucose transport by mediating SLC2A2/GLUT2 glycosylation, thereby controlling cell-surface expression of SLC2A2 in pancreatic beta cells (By similarity). {ECO:0000250|UniProtKB:O77836, ECO:0000250|UniProtKB:Q812G0}.
Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
A4IIN5
TISD_XENTR
MSTTLLSAFYDIDLLYKNEKVLNNLALSTMLDKKAVGSPVSSTNSNLFPGFLRRHSASNLQALSGNTNPAKFCPNNNQLKEPAAGSTALLNRENKFRDRSFSENGERSQHLLHLQQQQQQKAGAQVNSTRYKTELCRPFEESGACKYGEKCQFAHGFHELRSLTRHPKYKTELCRTFHTIGFCPYGPRCHFIHNAEERRQAPGAGERPKLHHSLSFSGFPNHSLDSPLLESPTSRTPPPQSSSSLYCQELLQLNNNNNPCANNAFTFSGQELGLIAPLAIHTQNPPYCRQPSSSPPLSFQPLRRVSESPVFDAPPSPPDSLSDRDSYLSGSLSSGSLSGSDSPTLDSNRRLPIFSRLSISDD
null
null
3'-UTR-mediated mRNA destabilization [GO:0061158]; cellular response to epidermal growth factor stimulus [GO:0071364]; cellular response to fibroblast growth factor stimulus [GO:0044344]; cellular response to glucocorticoid stimulus [GO:0071385]; cellular response to granulocyte macrophage colony-stimulating factor stimulus [GO:0097011]; cellular response to transforming growth factor beta stimulus [GO:0071560]; cellular response to tumor necrosis factor [GO:0071356]; definitive hemopoiesis [GO:0060216]; ERK1 and ERK2 cascade [GO:0070371]; hemopoiesis [GO:0030097]; MAPK cascade [GO:0000165]; mRNA catabolic process [GO:0006402]; negative regulation of fat cell differentiation [GO:0045599]; negative regulation of mitotic cell cycle phase transition [GO:1901991]; negative regulation of stem cell differentiation [GO:2000737]; nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:0000288]; nuclear-transcribed mRNA catabolic process, deadenylation-independent decay [GO:0031086]; positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:1900153]; pronephros development [GO:0048793]; regulation of B cell differentiation [GO:0045577]; regulation of mRNA stability [GO:0043488]; somatic stem cell division [GO:0048103]; somatic stem cell population maintenance [GO:0035019]
cytoplasm [GO:0005737]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:1990904]
metal ion binding [GO:0046872]; mRNA 3'-UTR AU-rich region binding [GO:0035925]
PF04553;PF00642;
4.10.1000.10;
null
PTM: Phosphorylated (By similarity). {ECO:0000250|UniProtKB:P23949, ECO:0000250|UniProtKB:P47974}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P23949}. Cytoplasm {ECO:0000250|UniProtKB:P23949}. Note=Shuttles between the nucleus and the cytoplasm in a XPO1/CRM1-dependent manner. {ECO:0000250|UniProtKB:P23949}.
null
null
null
null
null
FUNCTION: Zinc-finger RNA-binding protein that destabilizes several cytoplasmic AU-rich element (ARE)-containing mRNA transcripts by promoting their poly(A) tail removal or deadenylation, and hence provide a mechanism for attenuating protein synthesis (By similarity). Acts as a 3'-untranslated region (UTR) ARE mRNA-binding adapter protein to communicate signaling events to the mRNA decay machinery (By similarity). Functions by recruiting the CCR4-NOT deadenylase complex and probably other components of the cytoplasmic RNA decay machinery to the bound ARE-containing mRNAs, and hence promotes ARE-mediated mRNA deadenylation and decay processes (By similarity). Binds to 3'-UTR ARE of numerous mRNAs (By similarity). Induces also the degradation of ARE-containing mRNAs even in absence of poly(A) tail (By similarity). Required for tubulogenesis during pronephros development (By similarity). {ECO:0000250|UniProtKB:P23949, ECO:0000250|UniProtKB:P47974, ECO:0000250|UniProtKB:Q7ZXW9, ECO:0000250|UniProtKB:Q805B4}.
Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
A4IU28
LADA_GEOTN
MTKKIHINAFEMNCVGHIAHGLWRHPENQRHRYTDLNYWTELAQLLEKGKFDALFLADVVGIYDVYRQSRDTAVREAVQIPVNDPLMLISAMAYVTKHLAFAVTFSTTYEHPYGHARRMSTLDHLTKGRIAWNVVTSHLPSADKNFGIKKILEHDERYDLADEYLEVCYKLWEGSWEDNAVIRDIENNIYTDPSKVHEINHSGKYFEVPGPHLCEPSPQRTPVIYQAGMSERGREFAAKHAECVFLGGKDVETLKFFVDDIRKRAKKYGRNPDHIKMFAGICVIVGKTHDEAMEKLNSFQKYWSLEGHLAHYGGGTGYDLSKYSSNDYIGSISVGEIINNMSKLDGKWFKLSVGTPKKVADEMQYLVEEAGIDGFNLVQYVSPGTFVDFIELVVPELQKRGLYRVDYEEGTYREKLFGKGNYRLPDDHIAARYRNISSNV
1.14.14.28
null
null
extracellular region [GO:0005576]
monooxygenase activity [GO:0004497]; nucleotide binding [GO:0000166]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen [GO:0016705]
PF00296;
3.20.20.30;
NtaA/SnaA/DszA monooxygenase family
null
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17372208}.
CATALYTIC ACTIVITY: Reaction=a long-chain alkane + FMNH2 + O2 = a long chain fatty alcohol + FMN + H(+) + H2O; Xref=Rhea:RHEA:49060, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17135, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:83563; EC=1.14.14.28; Evidence={ECO:0000269|PubMed:17372208, ECO:0000269|PubMed:18164311, ECO:0000269|PubMed:22526792}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49061; Evidence={ECO:0000269|PubMed:17372208, ECO:0000269|PubMed:18164311, ECO:0000269|PubMed:22526792};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=9.1 mM for hexadecane {ECO:0000269|PubMed:22526792}; Note=kcat is 1.3 min(-1) with hexadecane as substrate. {ECO:0000269|PubMed:22526792};
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:22526792};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 60 degrees Celsius. {ECO:0000269|PubMed:22526792};
FUNCTION: Involved in the degradation of long-chain alkanes (PubMed:17372208, PubMed:22526792). Converts alkanes ranging from C(15) to C(36) into their corresponding primary alcohols (PubMed:17372208). {ECO:0000269|PubMed:17372208, ECO:0000269|PubMed:22526792}.
Geobacillus thermodenitrificans (strain NG80-2)
A4K144
M2_I54A2
MSLLTEVETPIRNEWGCRCNDSSDPLIIAASVVGILHLILWILDRLFFKCIYRLFKHGLKRGPSTEGVPESMREEYRKEQQSAVDADDSHFVNIELE
null
null
protein complex oligomerization [GO:0051259]; suppression by virus of host autophagy [GO:0039521]
host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion membrane [GO:0055036]
monoatomic ion channel activity [GO:0005216]; proton transmembrane transporter activity [GO:0015078]
PF00599;
6.10.250.1640;
Influenza viruses matrix protein M2 family
null
SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04069}. Host apical cell membrane {ECO:0000255|HAMAP-Rule:MF_04069}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04069}. Note=Abundantly expressed at the apical plasma membrane in infected polarized epithelial cells, in close proximity to budding and assembled virions. Minor component of virions (only 16-20 molecules/virion). {ECO:0000255|HAMAP-Rule:MF_04069}.
null
null
null
null
null
FUNCTION: Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry. After attaching to the cell surface, the virion enters the cell by endocytosis. Acidification of the endosome triggers M2 ion channel activity. The influx of protons into virion interior is believed to disrupt interactions between the viral ribonucleoprotein (RNP), matrix protein 1 (M1), and lipid bilayers, thereby freeing the viral genome from interaction with viral proteins and enabling RNA segments to migrate to the host cell nucleus, where influenza virus RNA transcription and replication occur. Also plays a role in viral proteins secretory pathway. Elevates the intravesicular pH of normally acidic compartments, such as trans-Golgi network, preventing newly formed hemagglutinin from premature switching to the fusion-active conformation. {ECO:0000255|HAMAP-Rule:MF_04069}.
Influenza A virus (strain A/Malaysia:Malaya/302/1954 H1N1)
A4K2M3
STK4_PAPAN
METVQLRNPPRRQLKKLDEDSLTKQPEEVFDVLEKLGEGSYGSVYKAIHKETGQIVAIKQVPVESDLQEIIKEISIMQQCDSPHVVKYYGSYFKNTDLWIVMEYCGAGSVSDIIRLRNKTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGQAKLADFGVAGQLTDTMAKRNTVIGTPFWMAPEVIQEIGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPELWSDNFTDFVKQCLVKSPEQRATATQLLQHPFVKSAKGVSILRDLINEAMDVKLKRQESQQREVDQDDEENSEEDEMDSGTMVRAVGDEMGTVRVASTMTDGANTMIEHDDTLPSQLGTMVINTEDEEEEGTMKRRDETMQPAKPSFLEYFEQKEKENQINSFGKSVPGPLKNSSDWKIPQDGDYEFLKSWTVEDLQKRLLALDPMMEQEIEEIRQKYQSKRQPILDAIEAKKRRQQNF
2.7.11.1
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
apoptotic process [GO:0006915]; hippo signaling [GO:0035329]; phosphorylation [GO:0016310]; protein tetramerization [GO:0051262]; regulation of MAPK cascade [GO:0043408]
cytoplasm [GO:0005737]; nucleus [GO:0005634]
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
PF11629;PF00069;
1.10.287.4270;4.10.170.10;1.10.510.10;
Protein kinase superfamily, STE Ser/Thr protein kinase family, STE20 subfamily
PTM: Autophosphorylated on serine and threonine residues. Phosphorylation at Thr-387 by PKB/AKT1, leads to inhibition of its: kinase activity, nuclear translocation and autophosphorylation at Thr-183. It also diminishes its cleavage by caspases and its ability to phosphorylate FOXO3 (By similarity). {ECO:0000250|UniProtKB:Q13043}.; PTM: Proteolytically cleaved by caspase-3 during apoptosis at Asp-326 and Asp-349 resulting in a 37 kDa or a 39 kDa subunit respectively. The 39 kDa subunit is further cleaved into the 37 kDa form. Proteolytic cleavage results in kinase activation and nuclear translocation of the truncated form (MST1/N). It is less likely that cleavage at Asp-349 is a prerequisite for activation as this site is not conserved in the murine ortholog (By similarity). {ECO:0000250}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=The caspase-cleaved form cycles between the nucleus and cytoplasm. {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=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q13043}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; Evidence={ECO:0000250|UniProtKB:Q13043}; 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:Q13043}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609; Evidence={ECO:0000250|UniProtKB:Q13043};
null
null
null
null
FUNCTION: Stress-activated, pro-apoptotic kinase which, following caspase-cleavage, enters the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. Key component of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. STK3/MST2 and STK4/MST1 are required to repress proliferation of mature hepatocytes, to prevent activation of facultative adult liver stem cells (oval cells), and to inhibit tumor formation. Phosphorylates 'Ser-14' of histone H2B (H2BS14ph) during apoptosis. Phosphorylates FOXO3 upon oxidative stress, which results in its nuclear translocation and cell death initiation. Phosphorylates MOBKL1A, MOBKL1B and RASSF2. Phosphorylates TNNI3 (cardiac Tn-I) and alters its binding affinity to TNNC1 (cardiac Tn-C) and TNNT2 (cardiac Tn-T). Phosphorylates FOXO1 on 'Ser-212' and regulates its activation and stimulates transcription of PMAIP1 in a FOXO1-dependent manner. Phosphorylates SIRT1 and inhibits SIRT1-mediated p53/TP53 deacetylation, thereby promoting p53/TP53 dependent transcription and apoptosis upon DNA damage. Acts as an inhibitor of PKB/AKT1. Phosphorylates AR on 'Ser-650' and suppresses its activity by intersecting with PKB/AKT1 signaling and antagonizing formation of AR-chromatin complexes. {ECO:0000250|UniProtKB:Q13043, ECO:0000250|UniProtKB:Q9JI11}.
Papio anubis (Olive baboon)
A4K2P5
STK4_COLGU
METVQLRNPPRRQLKKLDEDSLTKQPEEVFDVLEKLGEGSYGSVYKAIHKETGQIVAIKQVPVESDLQEIIKEISIMQQCDSPHVVKYYGSYFKNTDLWIVMEYCGAGSVSDIIRLRNKTLTEDEIATVLQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTMAKRNTVIGTPFWMAPEVIQEIGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPELWSDNFTDFVKQCLVKSPEQRATATQLLQHPFVKSAKGVSILRDLINEAMDVKLKRQESQQREVDQDDEENSEEDEMDSGTMVRAVGDEMGTVRVASTMTDGANTMIEHDDTLPSQLGTMVINTEDEEEEGTMKRRDETMQPAKPSFLEYFEQKEKENQINSFGKSVPGPLKNSSDWKIPQDGDYEFLKSWTVEDLQKRLLALDPMMEQEIEEIRQKYQSKRQPILDAIEAKKRRQQNF
2.7.11.1
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
apoptotic process [GO:0006915]; hippo signaling [GO:0035329]; phosphorylation [GO:0016310]; protein tetramerization [GO:0051262]; regulation of MAPK cascade [GO:0043408]
cytoplasm [GO:0005737]; nucleus [GO:0005634]
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
PF11629;PF00069;
1.10.287.4270;4.10.170.10;1.10.510.10;
Protein kinase superfamily, STE Ser/Thr protein kinase family, STE20 subfamily
PTM: Autophosphorylated on serine and threonine residues. Phosphorylation at Thr-387 by PKB/AKT1, leads to inhibition of its: kinase activity, nuclear translocation and autophosphorylation at Thr-183. It also diminishes its cleavage by caspases and its ability to phosphorylate FOXO3 (By similarity). {ECO:0000250|UniProtKB:Q13043}.; PTM: Proteolytically cleaved by caspase-3 during apoptosis at Asp-326 and Asp-349 resulting in a 37 kDa or a 39 kDa subunit respectively. The 39 kDa subunit is further cleaved into the 37 kDa form. Proteolytic cleavage results in kinase activation and nuclear translocation of the truncated form (MST1/N). It is less likely that cleavage at Asp-349 is a prerequisite for activation as this site is not conserved in the murine ortholog (By similarity). {ECO:0000250}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=The caspase-cleaved form cycles between the nucleus and cytoplasm. {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=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q13043}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; Evidence={ECO:0000250|UniProtKB:Q13043}; 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:Q13043}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609; Evidence={ECO:0000250|UniProtKB:Q13043};
null
null
null
null
FUNCTION: Stress-activated, pro-apoptotic kinase which, following caspase-cleavage, enters the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. Key component of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. STK3/MST2 and STK4/MST1 are required to repress proliferation of mature hepatocytes, to prevent activation of facultative adult liver stem cells (oval cells), and to inhibit tumor formation. Phosphorylates 'Ser-14' of histone H2B (H2BS14ph) during apoptosis. Phosphorylates FOXO3 upon oxidative stress, which results in its nuclear translocation and cell death initiation. Phosphorylates MOBKL1A, MOBKL1B and RASSF2. Phosphorylates TNNI3 (cardiac Tn-I) and alters its binding affinity to TNNC1 (cardiac Tn-C) and TNNT2 (cardiac Tn-T). Phosphorylates FOXO1 on 'Ser-212' and regulates its activation and stimulates transcription of PMAIP1 in a FOXO1-dependent manner. Phosphorylates SIRT1 and inhibits SIRT1-mediated p53/TP53 deacetylation, thereby promoting p53/TP53 dependent transcription and apoptosis upon DNA damage. Acts as an inhibitor of PKB/AKT1. Phosphorylates AR on 'Ser-650' and suppresses its activity by intersecting with PKB/AKT1 signaling and antagonizing formation of AR-chromatin complexes. {ECO:0000250|UniProtKB:Q13043, ECO:0000250|UniProtKB:Q9JI11}.
Colobus guereza (Mantled guereza) (Eastern black-and-white colobus monkey)
A4K2Q5
STK4_OTOGA
METVQLRNPPRRQLKKLDEDSLTKQPEEVFDVLEKLGEGSYGSVYKAIHKETGQIVAIKQVPVESDLQEIIKEISIMQQCDSPHVVKYYGSYFKNTDLWIVMEYCGAGSVSDIIRLRNKTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTMAKRNTVIGTPFWMAPEVIQEIGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPELWSDNFTDFVRQCLVKSPDQRATATQLLQHPFVKSAKGVSILRDLINEAMDVKLKRQEAQQREVDQDDEENSEEDELDSGTMVRAVGDEMGTVRVASTMSDGANTMIEHDDTLPSQLGTMVINADDEEEEGTMKRRDETMQPAKPSFLEYFEQKEKENQINSFGKSVPGPLKNSSDWKVPQDGDYEFLKSWTVEDLQKRLLALDPMMEQEIEEIRQKYQSKRQPILDAIEAKKRRQQNF
2.7.11.1
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
apoptotic process [GO:0006915]; hippo signaling [GO:0035329]; phosphorylation [GO:0016310]; protein tetramerization [GO:0051262]; regulation of MAPK cascade [GO:0043408]
cytoplasm [GO:0005737]; nucleus [GO:0005634]
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
PF11629;PF00069;
1.10.287.4270;4.10.170.10;1.10.510.10;
Protein kinase superfamily, STE Ser/Thr protein kinase family, STE20 subfamily
PTM: Autophosphorylated on serine and threonine residues. Phosphorylation at Thr-387 by PKB/AKT1, leads to inhibition of its: kinase activity, nuclear translocation and autophosphorylation at Thr-183. It also diminishes its cleavage by caspases and its ability to phosphorylate FOXO3 (By similarity). {ECO:0000250|UniProtKB:Q13043}.; PTM: Proteolytically cleaved by caspase-3 during apoptosis at Asp-326 and Asp-349 resulting in a 37 kDa or a 39 kDa subunit respectively. The 39 kDa subunit is further cleaved into the 37 kDa form. Proteolytic cleavage results in kinase activation and nuclear translocation of the truncated form (MST1/N). It is less likely that cleavage at Asp-349 is a prerequisite for activation as this site is not conserved in the murine ortholog (By similarity). {ECO:0000250}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=The caspase-cleaved form cycles between the nucleus and cytoplasm. {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=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q13043}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; Evidence={ECO:0000250|UniProtKB:Q13043}; 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:Q13043}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609; Evidence={ECO:0000250|UniProtKB:Q13043};
null
null
null
null
FUNCTION: Stress-activated, pro-apoptotic kinase which, following caspase-cleavage, enters the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. Key component of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. STK3/MST2 and STK4/MST1 are required to repress proliferation of mature hepatocytes, to prevent activation of facultative adult liver stem cells (oval cells), and to inhibit tumor formation. Phosphorylates 'Ser-14' of histone H2B (H2BS14ph) during apoptosis. Phosphorylates FOXO3 upon oxidative stress, which results in its nuclear translocation and cell death initiation. Phosphorylates MOBKL1A, MOBKL1B and RASSF2. Phosphorylates TNNI3 (cardiac Tn-I) and alters its binding affinity to TNNC1 (cardiac Tn-C) and TNNT2 (cardiac Tn-T). Phosphorylates FOXO1 on 'Ser-212' and regulates its activation and stimulates transcription of PMAIP1 in a FOXO1-dependent manner. Phosphorylates SIRT1 and inhibits SIRT1-mediated p53/TP53 deacetylation, thereby promoting p53/TP53 dependent transcription and apoptosis upon DNA damage. Acts as an inhibitor of PKB/AKT1. Phosphorylates AR on 'Ser-650' and suppresses its activity by intersecting with PKB/AKT1 signaling and antagonizing formation of AR-chromatin complexes. {ECO:0000250|UniProtKB:Q13043, ECO:0000250|UniProtKB:Q9JI11}.
Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby)
A4K2S1
STK4_LEMCA
METVQLRNPPRRQLKKLDEDSLTKQPEEVFDVLEKLGEGSYGSVYKAIHKETGQIVAIKQVPVESDLQEIIKEISIMQQCDSPHVVKYYGSYFKNTDLWIVMEYCGAGSVSDIIRLRNKTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTMAKRNTVIGTPFWMAPEVIQEIGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPELWSDNFMDFVRQCLVKSPDQRATATQLLQHPFVKSAKGVSILRDLINEAMDVKLKRQEAQQREVDQDDEENSEEDELDSGTMVRAVGDDMGTVRVASTMSDEANTMIEHDDTLPSQLGTMVINAEDEEEEGTMKRRDETMQPAKPSFLEYFEQKEKENQISSFGKSVPGPLKNSADWKVPQDGDYEFLKSWTVEDLQKRLLALDPMMEQEIEEIRQKYQSKRQPILDAIEAKKRRQQNF
2.7.11.1
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
apoptotic process [GO:0006915]; hippo signaling [GO:0035329]; phosphorylation [GO:0016310]; protein tetramerization [GO:0051262]; regulation of MAPK cascade [GO:0043408]
cytoplasm [GO:0005737]; nucleus [GO:0005634]
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
PF11629;PF00069;
1.10.287.4270;4.10.170.10;1.10.510.10;
Protein kinase superfamily, STE Ser/Thr protein kinase family, STE20 subfamily
PTM: Autophosphorylated on serine and threonine residues. Phosphorylation at Thr-387 by PKB/AKT1, leads to inhibition of its: kinase activity, nuclear translocation and autophosphorylation at Thr-183. It also diminishes its cleavage by caspases and its ability to phosphorylate FOXO3 (By similarity). {ECO:0000250|UniProtKB:Q13043}.; PTM: Proteolytically cleaved by caspase-3 during apoptosis at Asp-326 and Asp-349 resulting in a 37 kDa or a 39 kDa subunit respectively. The 39 kDa subunit is further cleaved into the 37 kDa form. Proteolytic cleavage results in kinase activation and nuclear translocation of the truncated form (MST1/N). It is less likely that cleavage at Asp-349 is a prerequisite for activation as this site is not conserved in the murine ortholog (By similarity). {ECO:0000250}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=The caspase-cleaved form cycles between the nucleus and cytoplasm. {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=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q13043}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; Evidence={ECO:0000250|UniProtKB:Q13043}; 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:Q13043}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609; Evidence={ECO:0000250|UniProtKB:Q13043};
null
null
null
null
FUNCTION: Stress-activated, pro-apoptotic kinase which, following caspase-cleavage, enters the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. Key component of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. STK3/MST2 and STK4/MST1 are required to repress proliferation of mature hepatocytes, to prevent activation of facultative adult liver stem cells (oval cells), and to inhibit tumor formation. Phosphorylates 'Ser-14' of histone H2B (H2BS14ph) during apoptosis. Phosphorylates FOXO3 upon oxidative stress, which results in its nuclear translocation and cell death initiation. Phosphorylates MOBKL1A, MOBKL1B and RASSF2. Phosphorylates TNNI3 (cardiac Tn-I) and alters its binding affinity to TNNC1 (cardiac Tn-C) and TNNT2 (cardiac Tn-T). Phosphorylates FOXO1 on 'Ser-212' and regulates its activation and stimulates transcription of PMAIP1 in a FOXO1-dependent manner. Phosphorylates SIRT1 and inhibits SIRT1-mediated p53/TP53 deacetylation, thereby promoting p53/TP53 dependent transcription and apoptosis upon DNA damage. Acts as an inhibitor of PKB/AKT1. Phosphorylates AR on 'Ser-650' and suppresses its activity by intersecting with PKB/AKT1 signaling and antagonizing formation of AR-chromatin complexes. {ECO:0000250|UniProtKB:Q13043, ECO:0000250|UniProtKB:Q9JI11}.
Lemur catta (Ring-tailed lemur)
A4K2T0
STK4_MACMU
METVQLRNPPRRQLKKLDEDSLTKQPEEVFDVLEKLGEGSYGSVYKAIHKETGQIVAIKQVPVESDLQEIIKEISIMQQCDSPHVVKYYGSYFKNTDLWIVMEYCGAGSVSDIIRLRNKTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTMAKRNTVIGTPFWMAPEVIQEIGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPELWSDNFTDFVKQCLVKSPEQRATATQLLQHPFVKSAKGVSILRDLINEAMDVKLKRQESQQREVDQDDEENSEEDEMDSGTMVRAVGDEMGTVRVASTMTDGASTMIEHDDTLPSQLGTMVINTEDEEEEGTMKRRDETMQPAKPSFLEYFEQKEKENQINSFGKSVPGPLKNSSDWKIPQDGDYEFLKSWTVEDLQKRLLALDPMMEQEIEEIRQKYQSKRQPILDAIEAKKRRQQNF
2.7.11.1
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
apoptotic process [GO:0006915]; hippo signaling [GO:0035329]; intracellular signal transduction [GO:0035556]; phosphorylation [GO:0016310]; protein tetramerization [GO:0051262]; regulation of MAPK cascade [GO:0043408]
cytoplasm [GO:0005737]; nucleus [GO:0005634]
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
PF11629;PF00069;
1.10.287.4270;4.10.170.10;1.10.510.10;
Protein kinase superfamily, STE Ser/Thr protein kinase family, STE20 subfamily
PTM: Autophosphorylated on serine and threonine residues. Phosphorylation at Thr-387 by PKB/AKT1, leads to inhibition of its: kinase activity, nuclear translocation and autophosphorylation at Thr-183. It also diminishes its cleavage by caspases and its ability to phosphorylate FOXO3 (By similarity). {ECO:0000250|UniProtKB:Q13043}.; PTM: Proteolytically cleaved by caspase-3 during apoptosis at Asp-326 and Asp-349 resulting in a 37 kDa or a 39 kDa subunit respectively. The 39 kDa subunit is further cleaved into the 37 kDa form. Proteolytic cleavage results in kinase activation and nuclear translocation of the truncated form (MST1/N). It is less likely that cleavage at Asp-349 is a prerequisite for activation as this site is not conserved in the murine ortholog (By similarity). {ECO:0000250}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=The caspase-cleaved form cycles between the nucleus and cytoplasm. {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=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q13043}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; Evidence={ECO:0000250|UniProtKB:Q13043}; 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:Q13043}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609; Evidence={ECO:0000250|UniProtKB:Q13043};
null
null
null
null
FUNCTION: Stress-activated, pro-apoptotic kinase which, following caspase-cleavage, enters the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. Key component of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. STK3/MST2 and STK4/MST1 are required to repress proliferation of mature hepatocytes, to prevent activation of facultative adult liver stem cells (oval cells), and to inhibit tumor formation. Phosphorylates 'Ser-14' of histone H2B (H2BS14ph) during apoptosis. Phosphorylates FOXO3 upon oxidative stress, which results in its nuclear translocation and cell death initiation. Phosphorylates MOBKL1A, MOBKL1B and RASSF2. Phosphorylates TNNI3 (cardiac Tn-I) and alters its binding affinity to TNNC1 (cardiac Tn-C) and TNNT2 (cardiac Tn-T). Phosphorylates FOXO1 on 'Ser-212' and regulates its activation and stimulates transcription of PMAIP1 in a FOXO1-dependent manner. Phosphorylates SIRT1 and inhibits SIRT1-mediated p53/TP53 deacetylation, thereby promoting p53/TP53 dependent transcription and apoptosis upon DNA damage. Acts as an inhibitor of PKB/AKT1. Phosphorylates AR on 'Ser-650' and suppresses its activity by intersecting with PKB/AKT1 signaling and antagonizing formation of AR-chromatin complexes. {ECO:0000250|UniProtKB:Q13043, ECO:0000250|UniProtKB:Q9JI11}.
Macaca mulatta (Rhesus macaque)
A4K2W5
STK4_AOTNA
METVQLRNPPRRQLKKLDEDSLTKQPEEVFDVLEKLGEGSYGSVYKAIHKETGQIVAIKQVPVESDLQEIIKEISIMQQCDSHHVVKYYGSYFKNTDLWIVMEYCGAGSVSDIIRLRNKTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTMAKRNTVIGTPFWMAPEVIQEIGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPELWSDNFTDFVKQCLVKSPEQRATATQLLQHPFVKSAKGVSILRDLINEAMDVKLKRQESQQREVDQDDEENSEEDEMDSGTMVRAVGDEMGTVRVASTMTDGANTMIEHDDTLPSQLGTMVINAEDEEEEGTMKRRDETMQPAKPSFLEYFEQKEKENQINSFGKSIPGPLQNSSDWKVPQDGDYEFLKSWTVEDLQKRLLALDPMMEQEIEEIRQKYQSKRQPILDAIEAKKRRQQNF
2.7.11.1
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
apoptotic process [GO:0006915]; intracellular signal transduction [GO:0035556]; phosphorylation [GO:0016310]; protein tetramerization [GO:0051262]; regulation of MAPK cascade [GO:0043408]
cytoplasm [GO:0005737]; nucleus [GO:0005634]
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
PF11629;PF00069;
1.10.287.4270;4.10.170.10;1.10.510.10;
Protein kinase superfamily, STE Ser/Thr protein kinase family, STE20 subfamily
PTM: Autophosphorylated on serine and threonine residues. Phosphorylation at Thr-387 by PKB/AKT1, leads to inhibition of its: kinase activity, nuclear translocation and autophosphorylation at Thr-183. It also diminishes its cleavage by caspases and its ability to phosphorylate FOXO3 (By similarity). {ECO:0000250|UniProtKB:Q13043}.; PTM: Proteolytically cleaved by caspase-3 during apoptosis at Asp-326 and Asp-349 resulting in a 37 kDa or a 39 kDa subunit respectively. The 39 kDa subunit is further cleaved into the 37 kDa form. Proteolytic cleavage results in kinase activation and nuclear translocation of the truncated form (MST1/N). It is less likely that cleavage at Asp-349 is a prerequisite for activation as this site is not conserved in the murine ortholog (By similarity). {ECO:0000250}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=The caspase-cleaved form cycles between the nucleus and cytoplasm. {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=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q13043}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; Evidence={ECO:0000250|UniProtKB:Q13043}; 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:Q13043}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609; Evidence={ECO:0000250|UniProtKB:Q13043};
null
null
null
null
FUNCTION: Stress-activated, pro-apoptotic kinase which, following caspase-cleavage, enters the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. Key component of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. STK3/MST2 and STK4/MST1 are required to repress proliferation of mature hepatocytes, to prevent activation of facultative adult liver stem cells (oval cells), and to inhibit tumor formation. Phosphorylates 'Ser-14' of histone H2B (H2BS14ph) during apoptosis. Phosphorylates FOXO3 upon oxidative stress, which results in its nuclear translocation and cell death initiation. Phosphorylates MOBKL1A, MOBKL1B and RASSF2. Phosphorylates TNNI3 (cardiac Tn-I) and alters its binding affinity to TNNC1 (cardiac Tn-C) and TNNT2 (cardiac Tn-T). Phosphorylates FOXO1 on 'Ser-212' and regulates its activation and stimulates transcription of PMAIP1 in a FOXO1-dependent manner. Phosphorylates SIRT1 and inhibits SIRT1-mediated p53/TP53 deacetylation, thereby promoting p53/TP53 dependent transcription and apoptosis upon DNA damage. Acts as an inhibitor of PKB/AKT1. Phosphorylates AR on 'Ser-650' and suppresses its activity by intersecting with PKB/AKT1 signaling and antagonizing formation of AR-chromatin complexes. {ECO:0000250|UniProtKB:Q13043, ECO:0000250|UniProtKB:Q9JI11}.
Aotus nancymaae (Ma's night monkey)
A4K2Y1
STK4_CHLAE
METVQLRNPPRRQLKKLDEDSLTKQPEEVFDVLEKLGEGSYGSVYKAIHKETGQIVAIKQVPVESDLQEIIKEISIMQQCDSPHVVKYYGSYFKNTDLWIVMEYCGAGSVSDIIRLRNKTLTEDEIATILQSTLKGLEYLHFMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTMAKRNTVIGTPFWMAPEVIQEIGYNCVADIWSLGITAIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPELWSDNFTDFVKQCLVKSPEQRATATQLLQHPFVKSAKGVSILRDLINEAMDVKLKRQESQQREVDQDDEENSEEDEMDSGTMVRAVGDEMGTVRVASTMTDGANTMIEHDDTLPSQLGTMVINTEDEEEEGTMKRRDETMQPAKPSFLEYFEQKEKENQINSFGKSVPGPLKNSSDWKIPQDGDYEFLKSWTVEDLQKRLLALDPMMEQEIEEIRQKYQSKRQPILDAIEAKKRRQQNF
2.7.11.1
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
apoptotic process [GO:0006915]; hippo signaling [GO:0035329]; phosphorylation [GO:0016310]; protein tetramerization [GO:0051262]; regulation of MAPK cascade [GO:0043408]
cytoplasm [GO:0005737]; nucleus [GO:0005634]
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
PF11629;PF00069;
1.10.287.4270;4.10.170.10;1.10.510.10;
Protein kinase superfamily, STE Ser/Thr protein kinase family, STE20 subfamily
PTM: Autophosphorylated on serine and threonine residues. Phosphorylation at Thr-387 by PKB/AKT1, leads to inhibition of its: kinase activity, nuclear translocation and autophosphorylation at Thr-183. It also diminishes its cleavage by caspases and its ability to phosphorylate FOXO3 (By similarity). {ECO:0000250|UniProtKB:Q13043}.; PTM: Proteolytically cleaved by caspase-3 during apoptosis at Asp-326 and Asp-349 resulting in a 37 kDa or a 39 kDa subunit respectively. The 39 kDa subunit is further cleaved into the 37 kDa form. Proteolytic cleavage results in kinase activation and nuclear translocation of the truncated form (MST1/N). It is less likely that cleavage at Asp-349 is a prerequisite for activation as this site is not conserved in the murine ortholog (By similarity). {ECO:0000250}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=The caspase-cleaved form cycles between the nucleus and cytoplasm. {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=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q13043}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; Evidence={ECO:0000250|UniProtKB:Q13043}; 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:Q13043}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609; Evidence={ECO:0000250|UniProtKB:Q13043};
null
null
null
null
FUNCTION: Stress-activated, pro-apoptotic kinase which, following caspase-cleavage, enters the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. Key component of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. STK3/MST2 and STK4/MST1 are required to repress proliferation of mature hepatocytes, to prevent activation of facultative adult liver stem cells (oval cells), and to inhibit tumor formation. Phosphorylates 'Ser-14' of histone H2B (H2BS14ph) during apoptosis. Phosphorylates FOXO3 upon oxidative stress, which results in its nuclear translocation and cell death initiation. Phosphorylates MOBKL1A, MOBKL1B and RASSF2. Phosphorylates TNNI3 (cardiac Tn-I) and alters its binding affinity to TNNC1 (cardiac Tn-C) and TNNT2 (cardiac Tn-T). Phosphorylates FOXO1 on 'Ser-212' and regulates its activation and stimulates transcription of PMAIP1 in a FOXO1-dependent manner. Phosphorylates SIRT1 and inhibits SIRT1-mediated p53/TP53 deacetylation, thereby promoting p53/TP53 dependent transcription and apoptosis upon DNA damage. Acts as an inhibitor of PKB/AKT1. Phosphorylates AR on 'Ser-650' and suppresses its activity by intersecting with PKB/AKT1 signaling and antagonizing formation of AR-chromatin complexes. {ECO:0000250|UniProtKB:Q13043, ECO:0000250|UniProtKB:Q9JI11}.
Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops)
A4K436
RTEL1_BOVIN
MPKITLKGVTVDFPFQPYKCQEEYMSKVLECLQEKVNGILESPTGTGKTLCLLCSTLAWREHLRDAVSARRIAERASGELFPDRTLASWGNAIPEGDVPACYTDIPKIIYASRTHSQLTQVISELRNTSYRPRVCVLGSREQLCIHPEVKKQESNHMQVHLCRRKVASRSCHFYNNVEEKSLEQELATPILDIEDLVRSGTKHKLCPYYLSRNLKQQADIIFMPYNYLLDAKSRRAHGIDLKGTVVIFDEAHNVEKMCEEAASFDLTPHDVASELDVIDRVLEERTKVAQQAELHPEFSADSARSGLNLEPEDLAKLKMILLRLEGAIDAVELPGDNSGVTKPGSYIFELFAEAQITFQTKGCILDSLDQLIQHLAGRAGLFTNTAGLQKLVDIIQIVFSVDSAEGDPGPMVGLASQSYKVHIHLDAGHRRTAQRSDVWNTTAARKPGKVLSYWCFSPGHSMRELVRQGVRTLILTSGTLAPMASFSLEMQIPFPVCLENPHVINQHQIWVGVIPKGPDGAQLSSAFDRRFSDECLSSLGKVLSNISRVVPHGLLVFFPSYPVMEKSLEFWRARDFTRKLEVRKPLFVEPRSKGGFSEVMEAFYARVAAPESSGAIFLAVCRGKASEGLDFADVNGRGVIVTGLPYPPRMDPRVLLKMQFLDEMKAQSGAGGQFLSGHDWYRQQASRAVNQAIGRVIRHRHDYGAVFLCDHRFAHADTRAQLPSWVRPHVKVYDSFGHVIRDVAQFFRVAQKTMPEPAPRAAAPSLGEGGGIVSVSVSPGPLPTRKAMSLDVHVPSLRQRHTGSPVTKDTEGSLCVEYEQEPVRAQRRPAGLLAALGHNEQLAEGPGDEALPVEEACGCPTLLGPREKRPAEEQRGRRRKVRLVGSSEVPAASTDTGRAKLFMVAVKQALSQASFDTFTQALRDYKSSDDLEALVARLSPLFAEDPKKHSLLQGFYQFVRPHHKQQFEEVCLQLTGQGCSSPHKHGHPQRQGAQLALDSSGRKESDPKLTVSQGATRQLDPCEQLNQGRPHLASGPFPAGDLNCSLHKGSRAPGAEKQHPSTVSAYLADVRRTLGAAGYSQLLTALTTYKQDDDFEKVVAVVAALTTEKPEDLPLLQRFGMFVRPHHKQRFRQMCVDLSGPGTQAPGPQEGGPAMPSDPVCEAPSPGPRKTQSKISSFLRCQACWRQHLQVSRKCPGCCAATRKQTLAQVFWPEPQ
3.6.4.12
null
DNA duplex unwinding [GO:0032508]; DNA recombination [GO:0006310]; DNA repair [GO:0006281]; DNA replication [GO:0006260]; negative regulation of DNA recombination [GO:0045910]; negative regulation of t-circle formation [GO:1904430]; regulation of double-strand break repair via homologous recombination [GO:0010569]; telomere maintenance [GO:0000723]; telomeric loop disassembly [GO:0090657]
nucleus [GO:0005634]
4 iron, 4 sulfur cluster binding [GO:0051539]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; DNA helicase activity [GO:0003678]; DNA polymerase binding [GO:0070182]; metal ion binding [GO:0046872]
PF06733;PF13307;
1.20.1160.20;3.40.50.300;
Helicase family, RAD3/XPD subfamily
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03065}. Note=Colocalizes with PCNA within the replication foci in S-phase cells. {ECO:0000255|HAMAP-Rule:MF_03065}.
CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; Evidence={ECO:0000255|HAMAP-Rule:MF_03065};
null
null
null
null
FUNCTION: ATP-dependent DNA helicase implicated in telomere-length regulation, DNA repair and the maintenance of genomic stability. Acts as an anti-recombinase to counteract toxic recombination and limit crossover during meiosis. Regulates meiotic recombination and crossover homeostasis by physically dissociating strand invasion events and thereby promotes noncrossover repair by meiotic synthesis dependent strand annealing (SDSA) as well as disassembly of D loop recombination intermediates. Also disassembles T loops and prevents telomere fragility by counteracting telomeric G4-DNA structures, which together ensure the dynamics and stability of the telomere. {ECO:0000255|HAMAP-Rule:MF_03065}.
Bos taurus (Bovine)
A4KZ49
POLG_TRMVU
MSSKKMMWVPKSAHKAPVVSREPVIRKKEWVARQIPKYIPVSNPSDCRDEISQTLLHFDSEEAVYDFVWRFPMGSIFWDTNGRIKPVVNCLLRATRMNLDYDVAADVYVCRDCLSCASSYMYFSNYHYDCRELRENHEAVVSCKYEQHIVSTFDVFPRYCTQEIEQNVVNWMTETLERYDNEPLRIEKQLQFYNHKTEQMESRVQEVQVTTAEYAVSDTYVPQQLSRKGSVSAKLTQRRANKIIMRTHEVENLIRETIDLCDERQIPITFVDVKHKRCLPRIPLRHMQAKPDISEIVEQGDMYNEVGQFIEQYQNLAEPFRVIRDYEVTRGWSGVILHRDDLALDPQTQARCLNNLFVVMGRCEHGHLQNALRPDCLEGLTYYSDTFGKVFNESLVKHHPGKHQFRIGSRTDYEWEELAMWVNAVCPVSFRCADCRPPQSLNEYIENIRMSKAMAELAGRQDALSKTLHKWTTMLISSVLTTEIRARDNLEPIQERIFTRNMPLGPLYDVAGAMNRAVIDIQTAVQNMQLSIGNSNMNEQQRNQTLLNEINKIKQHSFMQTKEMLSRFENIAQTYQNIISSASQPLSIHSMRQLMMDSRMDESFEFDIMRKKGSIASIAPMAFRTFEDIYSQPGVYNQKWLNLTPSGRFQTDIDYLRLDLPIDVIQKKKHVVNRNEIKEETCYVIVGQVNVSFCEVVARCFVPIPHVLRVGSPQNPTMIKIQDQEGGKTLVPKSGFCYVLQLVLMLGYVPDQLTAAFVKDVGIVVESLGPWPLFVDYLGAIKNLIIRYPTTIKAPTALHIVDHVDTVIHVMTTLGCVNKGEHYLTLQSVAQLHDAAMTVNIETFKDYRIGGVVPQLKHMLQSEEHMLEVLEAKPQWLVHLLLSPTQIWALSQSVVKYQVIHKVMTSNPDLAVALAQLVAISSNFSIFKNTEHVIQKYFEVSKQLQNVSGVILGEHNEYFETAFAQYSALRFSTDVVLLMDQFSTRKKTLDDLEDYYRKTIPSILIECGLLGPSDFGWRKRLVRGVVDRGSGLKSTVKSLGSFSTKEKWISWSGLGSGTITCVKFPFVCLQRSGSWLYSSTKTTAFNAVWMAGIKCVKSNVRSILLDSALYGAITLALLCAIKLIRKAFRFVEGLIKEDTSDDEDYVLHAKAASDSLYIQCLAWLALVVGCFNSGLANDIYFSTTKYRTLLDMVKTAHSDSFVFHAGDEEEGEIVELITRDNFVDYVYNHSDPLMEFDSETLLGWYTRISYQGRVLEHPLRVGTNCHLTRENVDEIAKNIATGAGNEFIVVGDVGSGKSTKLPIAVSTYGPVLILVPSRELVNNLCSSIWHVGKKQASTYMMNCITRGTSNISIMTYGYALALFSHCPIELQKYRFIQMDECHEFSSHMITFYSWWRESGKFTKLFKTTATPPGTVIKGGCVPTNHKVDVIEIRDVSVEEFCRRSIDSHAEGLRSLMPNGGRVIMFVPSRRECELARSSLISIPGARTWVVYRAAATQATKLVAELADDKHYFQIIITTTVLQNGVNLDPDCVVDFGQTFEAAYDRDSRQLGVRRRNINPGELIQRVGRVGRNKPGKFIQVGKRLEHEVVPNSCCVTDAILMSFTLELAPFISSHLIDEVNFVTREQVRTAMKFSAPLLFMIHYVRRDGRMLNGYYQQLKGLLLQTSDVALCDTLVGDAETNSFLTLRQYQLRGIIEAQEVLPDLPIPFYSSEFALPFYLEIGQITKEAIRARSFTLRIKTPDVKKAVMRLSTSATQIDQTIGILRTRLQLTRERLSKFSELKATAHNLRLTPIFNTCFDMGAAKSESTLRASLTAGEELLSALELARTEKSDKALEKLILDNPVLGDCLVFHGGPEEYFDQTLFQTSTGLINKYTVGIACLTVGLGCTIWYYLKKREKYVMHGKVHTRETGLTTNHLFVPGMKEHIQEWTGGDHEIGNRFGEAYKRRFIGRQPTEEQKLSKEKWDKREGQQTSVYKTLYDLDPTKFKYVVVECPDFDLKKKLNRQEKKQLDTTIVEACRTRMLDKGQHDFKDVERATVYLFNDNGVGHKVQLTPHNPLAVSRTTTHPVGFPAEAGRLRQTGQAMEMTPEELEKALDDNYVPHSRCQIDISHLHRHLAIVNTGGMSTQCFITQTMCVAPYHLAMGFKDNTKLTIYCSNGVYVMPVPKVEKMENMDLVVFRMPQDFPPLKRCATIREPKSSDEVTLITGKRTTHGIQLQFSKVVSIDRKSDTVWKYMIDSVPGVCGGMVMCVEDGCVVGFHSAAAIRNKVSNGSIFTPVTPQLLDSLQSSEGHLFDWYFNDDLISWKGVPTNMDPRNFPVSETISEFIFHNDSKGHGTDKYYGENLTIEGRVLQSFNTRHVVKGLDDAFAEYVNKFGEPPADTFTHLPSDLSSDAFYKDFMKYSTPVEVGTVNIENFEKAVQAVVELLEQQGFEQGEFSPEMDFYKILNSFNLDTAMGALYQCKKKDVLPMASHEQLATWFWNSLENLATGKLGLWKASLKAELRPKEKVLEKKTRVFTAAPFDVSFGAKAFVDDFNNKFYATQAGSNWTVGINKFNCGWDELARRFNPDWKFIDADGSRYDSSLTPLLFNAVLRIRQHFLRANGFERRMLSNFYTQLVWTPISTITGQIVKKNKGGPSGQPSTVVDNTMMLMIAVEYAKLQYGVTDLKYVCNGDDLILNAPQGVCETIRANFSHSFKELGLTYEFEQEVDSIDQVEYMSHKWIDCGGVLIPKLKPERIVSVLQWNKSLDLASQANKINAAWIESFGYGDLSKFIREYANWWGERNGQVGFLCSEEKVASLYLTNDVTIHTEEHDEFVFHSGADQSGVVKDQTGDKAEGSGTKTEDPPNQTTDPVNNPSNGGNKDAPQNLNATVVTKSYTYIPPIMKSLVTIDTAKKMADYTPPDALISTQACTLEQFGRWANAAANGLGLSMQAFQTDVVPYWIYWCIVNSASDEHKKLSSWTKVNMTIDDATGQINLNEGEAQTIYEMSPMFDEAKPTLRAVMRHFGALAYRWVKFSIAKRKPIIPHNAIKAGLMDVTYFPCCIDFVTVDQLSPQEQNVRNQVINARVSDTPRALFKHAQRAGAGEEDTNLRRDDDANYGRTRVGGAMFGTR
2.7.7.48; 3.4.-.-; 3.4.22.44; 3.4.22.45; 3.6.4.-
null
DNA-templated transcription [GO:0006351]; proteolysis [GO:0006508]; viral RNA genome replication [GO:0039694]; virus-mediated perturbation of host defense response [GO:0019049]
helical viral capsid [GO:0019029]; host cell cytoplasmic vesicle [GO:0044161]
ATP binding [GO:0005524]; cysteine-type endopeptidase activity [GO:0004197]; helicase activity [GO:0004386]; hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides [GO:0016818]; RNA binding [GO:0003723]; RNA-dependent RNA polymerase activity [GO:0003968]; serine-type peptidase activity [GO:0008236]; structural molecule activity [GO:0005198]
PF00270;PF00271;PF00863;PF00851;PF13611;PF00767;PF08440;PF00680;
3.30.70.270;3.90.70.150;3.40.50.300;2.40.10.10;
Potyviridae genome polyprotein family
PTM: [Viral genome-linked protein]: VPg is uridylylated by the polymerase and is covalently attached to the 5'-end of the genomic RNA. This uridylylated form acts as a nucleotide-peptide primer for the polymerase (By similarity). {ECO:0000250|UniProtKB:P09814}.; PTM: [Genome polyprotein]: Genome polyprotein of potyviruses undergoes post-translational proteolytic processing by the main proteinase NIa-pro resulting in the production of at least ten individual proteins. The P1 proteinase and the HC-pro cleave only their respective C-termini autocatalytically. 6K1 is essential for proper proteolytic separation of P3 from CI (By similarity). {ECO:0000250}.
SUBCELLULAR LOCATION: [6 kDa protein 1]: Host cytoplasmic vesicle. Note=Probably colocalizes with 6K2-induced vesicles associated with host chloroplasts. {ECO:0000250|UniProtKB:P13529}.; SUBCELLULAR LOCATION: [6 kDa protein 2]: Host cytoplasmic vesicle {ECO:0000250|UniProtKB:P09814}. Note=6K-induced vesicles associate with host chloroplasts. {ECO:0000250|UniProtKB:P09814}.; SUBCELLULAR LOCATION: [Capsid protein]: Virion {ECO:0000305}.
CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYTIC ACTIVITY: Reaction=Hydrolyzes glutaminyl bonds, and activity is further restricted by preferences for the amino acids in P6 - P1' that vary with the species of potyvirus, e.g. Glu-Xaa-Xaa-Tyr-Xaa-Gln-|-(Ser or Gly) for the enzyme from tobacco etch virus. The natural substrate is the viral polyprotein, but other proteins and oligopeptides containing the appropriate consensus sequence are also cleaved.; EC=3.4.22.44; Evidence={ECO:0000250|UniProtKB:P04517}; CATALYTIC ACTIVITY: Reaction=Hydrolyzes a Gly-|-Gly bond at its own C-terminus, commonly in the sequence -Tyr-Xaa-Val-Gly-|-Gly, in the processing of the potyviral polyprotein.; EC=3.4.22.45; Evidence={ECO:0000250|UniProtKB:P04517};
null
null
null
null
FUNCTION: [Helper component proteinase]: Required for aphid transmission and also has proteolytic activity. Only cleaves a Gly-Gly dipeptide at its own C-terminus. Interacts with virions and aphid stylets. Acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. May have RNA-binding activity. {ECO:0000250|UniProtKB:P04517}.; FUNCTION: [Cytoplasmic inclusion protein]: Has helicase activity. It may be involved in replication.; FUNCTION: [6 kDa protein 1]: Indispensable for virus replication. {ECO:0000250|UniProtKB:P13529}.; FUNCTION: [6 kDa protein 2]: Indispensable for virus replication. {ECO:0000250|UniProtKB:P09814}.; FUNCTION: [Viral genome-linked protein]: Mediates the cap-independent, EIF4E-dependent translation of viral genomic RNAs (By similarity). Binds to the cap-binding site of host EIF4E and thus interferes with the host EIF4E-dependent mRNA export and translation (By similarity). VPg-RNA directly binds EIF4E and is a template for transcription (By similarity). Also forms trimeric complexes with EIF4E-EIF4G, which are templates for translation (By similarity). {ECO:0000250|UniProtKB:P18247}.; FUNCTION: [Nuclear inclusion protein A]: Has RNA-binding and proteolytic activities. {ECO:0000250|UniProtKB:P04517}.; FUNCTION: [Nuclear inclusion protein B]: An RNA-dependent RNA polymerase that plays an essential role in the virus replication.; FUNCTION: [Capsid protein]: Involved in aphid transmission, cell-to-cell and systemis movement, encapsidation of the viral RNA and in the regulation of viral RNA amplification. {ECO:0000250|UniProtKB:P04517}.
Triticum mosaic virus (isolate Triticum aestivum/United States/U06-123/2006) (TriMV)
A4L691
PINX1_RAT
MSMLAERRRKQKWAVDPRNTAWSNDDSKFGQKMLEKMGWSKGKGLGAQEQGATEHIKVKVKNNHLGLGATNNNEDNWIAHQDDFNQLLAALNTCHGQETADSSDNKEKKSFSLEEKSKISKNRVHYMKFTKGKDLSSRSETDLDCIFGKRRNKKLAQDGCSNSTADEADTSLTTTTTTTSAFTIQEYFAKRMAQLKSKSQAAAPGSDLSETPIEWKKGKKKTKEAAGTDIENSPQHKAKRHKKKKRVEAERGPAAKKRDQVELQPGGPSGDECSDASVEAAEDRVQTPDTQDDVPKPRKRRAKKTLQRPGGVAVDTAPDSAPVKKKKKVSR
null
null
mitotic metaphase chromosome alignment [GO:0007080]; negative regulation of G2/M transition of mitotic cell cycle [GO:0010972]; negative regulation of protein ubiquitination [GO:0031397]; negative regulation of telomere maintenance via telomerase [GO:0032211]; positive regulation of protein localization to nucleolus [GO:1904751]; protein localization to chromosome, telomeric region [GO:0070198]; protein localization to nucleolus [GO:1902570]; regulation of protein stability [GO:0031647]; telomere maintenance via telomerase [GO:0007004]
chromosome, telomeric region [GO:0000781]; kinetochore [GO:0000776]; nuclear chromosome [GO:0000228]; nucleolus [GO:0005730]; spindle [GO:0005819]
protein-containing complex binding [GO:0044877]; telomerase inhibitor activity [GO:0010521]; telomerase RNA binding [GO:0070034]
PF01585;
null
PINX1 family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96BK5}. Nucleus, nucleolus {ECO:0000269|PubMed:17624691}. Chromosome, telomere {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}. Note=Localizes in nucleoli, at telomere speckles and to the outer plate of kinetochores. Localization to the kinetochore is mediated by its central region and depends on NDC80 and CENPE (By similarity). {ECO:0000250}.
null
null
null
null
null
FUNCTION: Microtubule-binding protein essential for faithful chromosome segregation. Mediates TRF1 and TERT accumulation in nucleolus and enhances TRF1 binding to telomeres. Inhibits telomerase activity. May inhibit cell proliferation and act as tumor suppressor (By similarity). {ECO:0000250, ECO:0000269|PubMed:17624691}.
Rattus norvegicus (Rat)
A4L7N3
FOXO1_PIG
MAEAPQVVEIDPDFEPLPRPRSCTWPLPRPEFSQSNSATSSPAPSGGAAANPDAAAGLPSASAAAVNADFMSNLSLLEESEDFPQAPGSVAAAAAAAAAVAAAAAAAATGGLCGDFQGPEAGCLHPAPPQQPPPPGPLSQHPPVPPAAAGSLAGQPRKSSSSRRNAWGNLSYADLITKAIESSAEKRLTLSQIYEWMVKSVPYFKDKGDSNSSAGWKNSIRHNLSLHSKFIRVQNEGTGKSSWWMLNPEGGKSGKSPRRRAASMDNNSKFAKSRGRAAKKKASLQSGQEGAGDSPGSQFSKWPASPGSHSNDDFDNWSTFRPRTSSNASTISGRLSPIMTEQDDLGNGDVHSMVYPPSAAKMASTLPSLSEISNPENMENLLDNLNLLSSPTSLTVSTQSSPGTIMQQTPCYSFAPPNTSLNSPSPNYQKYTYGQSSMSPLPQMPMQTLQDSKSSYGGMAQYNCAAGLLKELLTSDSPPHNDIMTPVDPGVAQPNSRVLGQNVLMGPSSVMPAYGGQASHNKMMNPSSHSHPGHAQSTSAVNGRALPHAVNTMPHASGMNRLTQEKTALQVPLPHPMQMNALGGYSPASTCNGYGRMGLLHQEKLPSDLDGMFIERLDCDMESIIRNDLMDGDTLDFNFDNVLPNQSFPHSVKTTTHSWVSG
null
null
apoptotic process [GO:0006915]; autophagy [GO:0006914]; cell differentiation [GO:0030154]; cellular response to hyperoxia [GO:0071455]; cellular response to insulin stimulus [GO:0032869]; cellular response to nitric oxide [GO:0071732]; cellular response to oxidative stress [GO:0034599]; cellular response to starvation [GO:0009267]; DNA damage response [GO:0006974]; insulin receptor signaling pathway [GO:0008286]; negative regulation of fat cell differentiation [GO:0045599]; negative regulation of gene expression [GO:0010629]; negative regulation of insulin secretion [GO:0046676]; peptidyl-serine phosphorylation [GO:0018105]; peptidyl-threonine phosphorylation [GO:0018107]; positive regulation of apoptotic process [GO:0043065]; positive regulation of autophagy [GO:0010508]; positive regulation of complement-dependent cytotoxicity [GO:1903661]; positive regulation of gluconeogenesis [GO:0045722]; positive regulation of protein catabolic process [GO:0045732]; positive regulation of smooth muscle cell apoptotic process [GO:0034393]; regulation of transcription by RNA polymerase II [GO:0006357]; regulation of transcription initiation by RNA polymerase II [GO:0060260]; response to fatty acid [GO:0070542]
cytoplasm [GO:0005737]; nucleus [GO:0005634]
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 phosphatase 2A binding [GO:0051721]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]
PF00250;PF16676;PF16675;
1.10.10.10;
null
PTM: Phosphorylation by NLK promotes nuclear export and inhibits the transcriptional activity. In response to growth factors, phosphorylation on Thr-24, Ser-263 and Ser-326 by PKB/AKT1 promotes nuclear export and inactivation of transactivational activity. Phosphorylation on Thr-24 is required for binding 14-3-3 proteins. Phosphorylation of Ser-263 decreases DNA-binding activity and promotes the phosphorylation of Thr-24 and Ser-326, permitting phosphorylation of Ser-329 and Ser-332, probably by CDK1, leading to nuclear exclusion and loss of function. Stress signals, such as response to oxygen or nitric oxide, attenuate the PKB/AKT1-mediated phosphorylation leading to nuclear retention. Phosphorylation of Ser-336 is independent of IGF1 and leads to reduced function. Dephosphorylated on Thr-24 and Ser-263 by PP2A in beta-cells under oxidative stress leading to nuclear retention. Phosphorylation of Ser-256 by CDK1 disrupts binding of 14-3-3 proteins leading to nuclear accumulation and has no effect on DNA binding nor transcriptional activity. Phosphorylation by STK4/MST1 on Ser-219, upon oxidative stress, inhibits binding to 14-3-3 proteins and nuclear export (By similarity). PPIA/CYPA promotes its dephosphorylation on Ser-263 (By similarity). {ECO:0000250|UniProtKB:Q12778, ECO:0000250|UniProtKB:Q9R1E0}.; PTM: Ubiquitinated by SKP2 (By similarity). Ubiquitination leads to proteasomal degradation (By similarity). Ubiquitinated by STUB1/CHIP; when Ser-263 is phosphorylated (By similarity). {ECO:0000250|UniProtKB:Q12778, ECO:0000250|UniProtKB:Q9R1E0}.; PTM: Methylation inhibits AKT1-mediated phosphorylation at Ser-263 and is increased by oxidative stress. {ECO:0000250|UniProtKB:Q9R1E0}.; PTM: Acetylated. Acetylation at Lys-269 and Lys-281 are necessary for autophagic cell death induction. Deacetylated by SIRT2 in response to oxidative stress or serum deprivation, thereby negatively regulating FOXO1-mediated autophagic cell death. Once in the nucleus, acetylated by CREBBP/EP300. Acetylation diminishes the interaction with target DNA and attenuates the transcriptional activity. It increases the phosphorylation at Ser-263. Deacetylation by SIRT1 results in reactivation of the transcriptional activity. Oxidative stress by hydrogen peroxide treatment appears to promote deacetylation and uncoupling of insulin-induced phosphorylation. By contrast, resveratrol acts independently of acetylation. Acetylated at Lys-430, promoting its localization to the nucleus and transcription factor activity. Deacetylation at Lys-430 by SIRT6, promotes its translocation into the cytoplasm, preventing its transcription factor activity. Deacetylation and subsequent inhibition by SIRT6 has different effects depending on cell types: it inhibits gluconeogenesis in hepatocytes, promotes glucose sensing in pancreatic beta-cells and regulates lipid catabolism in brown adipocytes. {ECO:0000250|UniProtKB:Q12778}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9R1E0}. Nucleus {ECO:0000250|UniProtKB:Q9R1E0}. Note=Shuttles between the cytoplasm and nucleus (By similarity). Largely nuclear in unstimulated cells (By similarity). In osteoblasts, colocalizes with ATF4 and RUNX2 in the nucleus. Serum deprivation increases localization to the nucleus, leading to activate expression of SOX9 and subsequent chondrogenesis (By similarity). Insulin-induced phosphorylation at Ser-253 by PKB/AKT1 leads, via stimulation of Thr-24 phosphorylation, to binding of 14-3-3 proteins and nuclear export to the cytoplasm where it is degraded by the ubiquitin-proteasomal pathway (By similarity). Phosphorylation at Ser-249 by CDK1 disrupts binding of 14-3-3 proteins and promotes nuclear accumulation (By similarity). Phosphorylation by NLK results in nuclear export (By similarity). Translocates to the nucleus upon oxidative stress-induced phosphorylation at Ser-212 by STK4/MST1 (By similarity). SGK1-mediated phosphorylation also results in nuclear translocation. Retained in the nucleus under stress stimuli including oxidative stress, nutrient deprivation or nitric oxide. Methylated form is nuclear (By similarity). PPIA/CYPA stimulates its nuclear accumulation (By similarity). Deacetylation by SIRT6, promotes its translocation into the cytoplasm (By similarity). {ECO:0000250|UniProtKB:Q12778, ECO:0000250|UniProtKB:Q9R1E0}.
null
null
null
null
null
FUNCTION: Transcription factor that is the main target of insulin signaling and regulates metabolic homeostasis in response to oxidative stress (PubMed:18293098). Binds to the insulin response element (IRE) with consensus sequence 5'-TT[G/A]TTTTG-3' and the related Daf-16 family binding element (DBE) with consensus sequence 5'-TT[G/A]TTTAC-3' (By similarity). Activity suppressed by insulin (By similarity). Main regulator of redox balance and osteoblast numbers and controls bone mass (By similarity). Orchestrates the endocrine function of the skeleton in regulating glucose metabolism (By similarity). Also acts as a key regulator of chondrogenic commitment of skeletal progenitor cells in response to lipid availability: when lipids levels are low, translocates to the nucleus and promotes expression of SOX9, which induces chondrogenic commitment and suppresses fatty acid oxidation (By similarity). Acts synergistically with ATF4 to suppress osteocalcin/BGLAP activity, increasing glucose levels and triggering glucose intolerance and insulin insensitivity (By similarity). Also suppresses the transcriptional activity of RUNX2, an upstream activator of osteocalcin/BGLAP (By similarity). Acts as an inhibitor of glucose sensing in pancreatic beta cells by acting as a transcription repressor and suppressing expression of PDX1 (By similarity). In hepatocytes, promotes gluconeogenesis by acting together with PPARGC1A and CEBPA to activate the expression of genes such as IGFBP1, G6PC1 and PCK1 (By similarity). Also promotes gluconeogenesis by directly promoting expression of PPARGC1A and G6PC1 (By similarity). Important regulator of cell death acting downstream of CDK1, PKB/AKT1 and STK4/MST1 (By similarity). Promotes neural cell death (By similarity). Mediates insulin action on adipose tissue (By similarity). Regulates the expression of adipogenic genes such as PPARG during preadipocyte differentiation and, adipocyte size and adipose tissue-specific gene expression in response to excessive calorie intake (By similarity). Regulates the transcriptional activity of GADD45A and repair of nitric oxide-damaged DNA in beta-cells (By similarity). Required for the autophagic cell death induction in response to starvation or oxidative stress in a transcription-independent manner (By similarity). Mediates the function of MLIP in cardiomyocytes hypertrophy and cardiac remodeling (By similarity). Positive regulator of apoptosis in cardiac smooth muscle cells as a result of its transcriptional activation of pro-apoptotic genes (By similarity). Regulates endothelial cell (EC) viability and apoptosis in a PPIA/CYPA-dependent manner via transcription of CCL2 and BCL2L11 which are involved in EC chemotaxis and apoptosis (By similarity). {ECO:0000250|UniProtKB:Q12778, ECO:0000250|UniProtKB:Q9R1E0, ECO:0000269|PubMed:18293098}.
Sus scrofa (Pig)
A4L9P5
HIPK1_RAT
MASQLQVFSPPSVSSSAFCSAKKLKIEPSGWDVSGQSSNDKYYTHSKTLPATQGQASSSHQVANFNIPAYDQGLLLQAPAVEHIVVTAADSSGSAATATFQSSQTLTHRSNVSLLEPYQKCGLKRKSEEVDSNGSVQIIEEHPPLMLQNRTVVGAAATTTTVTTKSSSSSGEGDYQLVQHEILCSMTNSYEVLEFLGRGTFGQVAKCWKRSTKEIVAIKILKNHPSYARQGQIEVSILSRLSSENADEYNFVRSYECFQHKNHTCLVFEMLEQNLYDFLKQNKFSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLVDPVRQPYRVKVIDFGSASHVSKAVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGASEYDQIRYISQTQGLPAEYLLSAGTKTTRFFNRDPNLGYPLWRLKTPEEHELETGIKSKEARKYIFNCLDDMAQVNMSTDLEGTDMLAEKADRREYIDLLKKMLTIDADKRVTPLKTLNHQFVTMTHLLDFPHSNHVKSCFQNMEICKRRVHMYDTVSQIKSPFTTHVAPSTSTNLTMSFSNQLSTVHNQASVLASSSTAAAATLSLANSDVSLLNYQSALYPPSAAPVPGVAQQGVSLQPGTTQICTQTDPFQQTFIVCPPAFQTGLQATTKHSGFPVRMDNAVPLVPQAPAAQPLQIQSGVLTQGSCTPLMVATLHPQVATITPQYAVPFTLSCAAGRPALVEQTAAVQQAWPGGTQQILLPSAWQQLPGVALHNSVQPTAVIPEAMGSSQQLADWRNAHSHGNQYSTIMQQPSLLTNHVTLATAQPLNVGVAHVVRQQQSSSLPSRKNKQSAPVSSTSSLEVLPSQVYSLVGSSPLRTTSSYNSLVPVQDQHQPIIIPDTPSPPVSVITIRSDTDEEEDNKFKPSSSSLKARSNVISYVTVNDSPDSDSSLSSPYPTDTLSALRGNSGTLLEGPGRTAADGIGTRTIIVPPLKTQLGDCTGATQASGLLSSSKTKPVASVSGQSSGCCITPTGYRAQRGGASAVQPLNLSQNQQSSSASTSQERSSNPAPRRQQAFVAPLSQAPYAFQHGSPLHSTGHPHLAPAPAHLPSQPHLYTYAAPTSAAALGSTSSIAHLFSPQGSSRHAAAYTTHPSTLVHQVPVSVGPSLLTSASVAPAQYQHQFATQSYIGSSRGSTIYTGYPLSPTKISQYSYL
2.7.11.1
null
adherens junction assembly [GO:0034333]; anterior/posterior pattern specification [GO:0009952]; cell population proliferation [GO:0008283]; embryonic camera-type eye morphogenesis [GO:0048596]; embryonic retina morphogenesis in camera-type eye [GO:0060059]; endothelial cell apoptotic process [GO:0072577]; extrinsic apoptotic signaling pathway [GO:0097191]; intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [GO:0042771]; iris morphogenesis [GO:0061072]; lens induction in camera-type eye [GO:0060235]; neuron differentiation [GO:0030182]; phosphorylation [GO:0016310]; positive regulation of cell population proliferation [GO:0008284]; regulation of tumor necrosis factor-mediated signaling pathway [GO:0010803]; retina layer formation [GO:0010842]; smoothened signaling pathway [GO:0007224]
cytoplasm [GO:0005737]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; PML body [GO:0016605]
ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein tyrosine kinase activity [GO:0004713]
PF00069;
1.10.510.10;
Protein kinase superfamily, CMGC Ser/Thr protein kinase family, HIPK subfamily
PTM: Phosphorylated and activated by JNK1. Autophosphorylated (By similarity). {ECO:0000250|UniProtKB:Q86Z02}.; PTM: Sumoylated. When conjugated it is directed to nuclear speckles. SENP1-mediated desumoylation is mediated by TNF in response to stress stimuli, triggering transient translocation from nucleus to cytoplasm (By similarity). {ECO:0000250}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O88904}. Cytoplasm {ECO:0000250|UniProtKB:O88904}. Nucleus speckle {ECO:0000250|UniProtKB:O88904}. Note=Predominantly nuclear. Translocates from nucleus to cytoplasm in response to stress stimuli via SENP1-mediated desumoylation (By similarity). {ECO:0000250|UniProtKB:O88904}.
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:O88904}; 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:O88904};
null
null
null
null
FUNCTION: Serine/threonine-protein kinase involved in transcription regulation and TNF-mediated cellular apoptosis. Plays a role as a corepressor for homeodomain transcription factors. Phosphorylates DAXX and MYB. Phosphorylates DAXX in response to stress, and mediates its translocation from the nucleus to the cytoplasm. Inactivates MYB transcription factor activity by phosphorylation. Prevents MAP3K5-JNK activation in the absence of TNF. TNF triggers its translocation to the cytoplasm in response to stress stimuli, thus activating nuclear MAP3K5-JNK by derepression and promoting apoptosis. May be involved in anti-oxidative stress responses. Involved in the regulation of eye size, lens formation and retinal lamination during late embryogenesis. Promotes angiogenesis and to be involved in erythroid differentiation. May be involved in malignant squamous cell tumor formation (By similarity). Phosphorylates PAGE4 at 'Thr-51' which is critical for the ability of PAGE4 to potentiate the transcriptional activator activity of JUN (By similarity). {ECO:0000250|UniProtKB:Q86Z02}.
Rattus norvegicus (Rat)
A4PBQ9
VM3VA_CROAT
MIQVLLVTICLAAFPYQGSSIILESGNVNDYEIVYPRKVTALPKGAVQPKYEDAMQYELKVNGEPVVLHLEKNKQLFSKDYSETHYSPDGREITTYPLVEDHCYYHGRIENDADSTASISACNGLKGHFKLQGEMYLIEPLKLSDSEAHAVYKYENVEKEDEAPKMCGVTQNWKSYEPIKKASQLVVTAEHQKYNPFRFVELVLVVDKAMVTKNNGDLDKIKTRMYELANTVNDIYRYMYIHVALVGLEIWSNEDKITVKPEADYTLNAFGEWRKTDLLTRKKHDNAQLLTAIDLDRVIGLAYVGSMCHPKRSTGIIQDYSPINLVVAVIMAHEMGHNLGINHDRGYCSCGDYACIMRPEISPEPSTFFSNCSYFDCWDFITNHNPECIVNEPLGTDIISPPVCGNELLEVGEECDCGTPENCQNECCDAATCKLKSGSQCGHGDCCEQCKFSKSGTECRASMSECDPAEHCTGQSSECPADVFHKNGQPCLDNYGYNGNCPIMYHQCYDLFGADVYEAEDSCFERNQKGNYYGYCRKENGNKIPCAPEDVKCGRLYCKDNSPGQNNSCKMFYSNEDEHKGMVLPGTKCADGKVCSNGHCVDVATAY
3.4.24.-
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250};
envenomation resulting in damage of muscle extracellular matrix in another organism [GO:0044523]; envenomation resulting in hemorrhagic damage in another organism [GO:0044358]; envenomation resulting in negative regulation of platelet aggregation in another organism [GO:0044477]; proteolysis [GO:0006508]
extracellular region [GO:0005576]; plasma membrane [GO:0005886]
metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; metallopeptidase activity [GO:0008237]; toxin activity [GO:0090729]
PF08516;PF00200;PF01562;PF01421;
3.40.390.10;4.10.70.10;
Venom metalloproteinase (M12B) family, P-III subfamily, P-IIIc sub-subfamily
null
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17497365, ECO:0000269|PubMed:9578458}.
null
null
null
null
null
FUNCTION: Is implied in permanent muscle damage by attacking the collagen scaffold and other important basement membrane proteins of muscle, and by preventing muscle regeneration through disrupting the functions of satellite cells (PubMed:30695027). Displays collagenolytic activity, fibrinogenolytic activity (on both Aalpha and Bbeta, but not gamma chains) and inhibits CRP-XL-induced platelet aggregation (PubMed:30695027). In vivo, induces hemorrhage and fluctuations in muscle size by intramuscular injection into mice (PubMed:30695027). Also induces apoptosis in endothelial cells, without triggering cell detachment (PubMed:9578458). {ECO:0000269|PubMed:30695027, ECO:0000269|PubMed:9578458}.
Crotalus atrox (Western diamondback rattlesnake)
A4PES0
WEE2_PIG
MGDNGDNKELKQKLNFSYSEEEQEDEGQKEAQESKKVQYHTPERCGHQDSEAKFTPPRTPLNHVCELSTPQVKDRASPDQGLRTPVSRPHTRPETPAPPDKSKPPPHCESPFTPRGHSSQSVISTGKLPSRGSKHLRLTPGPLTDEMTSLALVNINPFTPESYRRQFLKSNGKRKTRRDLEEAGPEEGKVEKGLPAKRCVLRETNMACRYEKEFLEVEKIGVGEFGTVYKCIKRLDGCVYAIKRSTKPVSGLSDENLAMHEVYAHSVLGHHPHVVRYYSSWAEDDHMMIQNEYCNGGSLQAAISENAKSGNHFQEPKLKDILLQISLGLKYIHNYGMVHMDIKPSNIFICHKIPSDSPVVPEEAENEADWFLSANVTYKIGDLGHVTSISEPQVEEGDSRFLAKEILQENYQHLPKADIFALGLTIAVAAGAEALPTNGTSWHHIREGQLPNIPQDLSKEFYNLLKDMIDPDPVARPSAAALTRSRVLCPSLGRTEELQQQLNLEKFKTATLERELKEVQRAQSSKEGQSSPGVTGTHTGSRSTRRLVGGKSAKSSSFTWGQSSP
2.7.10.2
null
female meiotic nuclear division [GO:0007143]; mitotic cell cycle [GO:0000278]; negative regulation of G2/MI transition of meiotic cell cycle [GO:0110031]; negative regulation of meiotic cell cycle process involved in oocyte maturation [GO:1904145]; negative regulation of oocyte development [GO:0060283]; phosphorylation [GO:0016310]; positive regulation of phosphorylation [GO:0042327]; regulation of fertilization [GO:0080154]; regulation of meiosis I [GO:0060631]
cytoplasm [GO:0005737]; nucleus [GO:0005634]
ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein tyrosine kinase activity [GO:0004713]
PF00069;
1.10.510.10;
Protein kinase superfamily, Ser/Thr protein kinase family, WEE1 subfamily
PTM: Phosphorylation leads to increase its activity. {ECO:0000269|PubMed:21123961}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21123961}.
CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU10027};
null
null
null
null
FUNCTION: Oocyte-specific protein tyrosine kinase that phosphorylates and inhibits CDK1 and acts as a key regulator of meiosis during both prophase I and metaphase II. Required to maintain meiotic arrest in oocytes during the germinal vesicle (GV) stage, a long period of quiescence at dictyate prophase I, by phosphorylating CDK1 at 'Tyr-15', leading to inhibit CDK1 activity and prevent meiotic reentry. Also required for metaphase II exit during egg activation by phosphorylating CDK1 at 'Tyr-15', to ensure exit from meiosis in oocytes and promote pronuclear formation. {ECO:0000269|PubMed:19633431}.
Sus scrofa (Pig)
A4Q998
PNPH_ANOGA
MSKFSYLQNGKASTNGVPHANGHHQQHQNGHSNGVARNGGTATDTLPVAYQQKAATSGPFHMPRTEHVGYTYDTLQEIATYLLERTELRPKVGIICGSGLGTLAEQLTDVDSFDYETIPHFPVSTVAGHVGRLVFGYLAGVPVMCMQGRFHHYEGYPLAKCAMPVRVMHLIGCTHLIATNAAGGANPKYRVGDIMLIKDHINLMGFAGNNPLQGPNDERFGPRFFGMANTYDPKLNQQAKVIARQIGIENELREGVYTCLGGPNFETVAEVKMLSMLGVDAIGMSTVHEIITARHCGMTCFAFSLITNMCTMSYEEEEEHCHDSIVGVGKNREKTLGEFVSRIVKHIHYEAKK
2.4.2.1
null
purine ribonucleoside salvage [GO:0006166]
cytoplasm [GO:0005737]
purine-nucleoside phosphorylase activity [GO:0004731]
PF01048;
3.40.50.1580;
PNP/MTAP phosphorylase family
null
null
CATALYTIC ACTIVITY: Reaction=inosine + phosphate = alpha-D-ribose 1-phosphate + hypoxanthine; Xref=Rhea:RHEA:27646, ChEBI:CHEBI:17368, ChEBI:CHEBI:17596, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.1; Evidence={ECO:0000269|PubMed:17918964}; CATALYTIC ACTIVITY: Reaction=guanosine + phosphate = alpha-D-ribose 1-phosphate + guanine; Xref=Rhea:RHEA:13233, ChEBI:CHEBI:16235, ChEBI:CHEBI:16750, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.1; Evidence={ECO:0000269|PubMed:17918964}; CATALYTIC ACTIVITY: Reaction=2'-deoxyguanosine + phosphate = 2-deoxy-alpha-D-ribose 1-phosphate + guanine; Xref=Rhea:RHEA:27738, ChEBI:CHEBI:16235, ChEBI:CHEBI:17172, ChEBI:CHEBI:43474, ChEBI:CHEBI:57259; EC=2.4.2.1; Evidence={ECO:0000269|PubMed:17918964}; CATALYTIC ACTIVITY: Reaction=2'-deoxyinosine + phosphate = 2-deoxy-alpha-D-ribose 1-phosphate + hypoxanthine; Xref=Rhea:RHEA:27750, ChEBI:CHEBI:17368, ChEBI:CHEBI:28997, ChEBI:CHEBI:43474, ChEBI:CHEBI:57259; EC=2.4.2.1; Evidence={ECO:0000269|PubMed:17918964};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=585 uM for inosine (at 25 degrees Celsius and pH 7.4) {ECO:0000269|PubMed:17918964}; KM=187 uM for guanosine (at 25 degrees Celsius and pH 7.4) {ECO:0000269|PubMed:17918964}; KM=190 uM for 2-deoxyinosine (at 25 degrees Celsius and pH 7.4) {ECO:0000269|PubMed:17918964}; KM=50 uM for 2-deoxyguanosine (at 25 degrees Celsius and pH 7.4) {ECO:0000269|PubMed:17918964}; Note=kcat is 41 sec(-1) with inosine as substrate (PubMed:17918964). kcat is 1 sec(-1) with guanosine as substrate (PubMed:17918964). kcat is 54 sec(-1) with 2-deoxyinosine as substrate (PubMed:17918964). kcat is 5.4 sec(-1) with 2-deoxyguanosine as substrate (PubMed:17918964). {ECO:0000269|PubMed:17918964};
PATHWAY: Purine metabolism; purine nucleoside salvage. {ECO:0000269|PubMed:17918964}.
null
null
FUNCTION: As part of the purine salvage pathway, catalyzes the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate (PubMed:17918964). Preferentially acts on 2'-deoxyinosine and inosine, and to a lesser extent on 2'-deoxyguanosine and guanosine (PubMed:17918964). Has no activity towards adenosine or 2'-deoxyadenosine (PubMed:17918964). {ECO:0000269|PubMed:17918964}.
Anopheles gambiae (African malaria mosquito)
A4Q9E5
TTLL3_MOUSE
MQGVSSALLLSAGQLGPGAAWYRQEGSSECSWLRRSQPSELRTNFSSRWPWPRNSESRRSERLQWPGPASAKPEVASCGDSRRDYSSLPARHLSSARESSMPGALGTVNPQPVRTLVPPTLDEPLPDALRPPDDSLLLWRGLTKGPNHMGRLRNAKIHVERAVKQKKIFMIHGRYPVIRCLLRQRGWVEKKMVHPPGTALPAPQKDLDSSMLGDSDATEDEDEEENEMFRESQLLDLDGFLEFDDLDGIHALMSRMVRNETPYLIWTTRRDVLDCRFLSKDQMINHYARAGSFTTKVGLCLNLRNLPWFDEADADSFFPRCYRLGAEDDKKAFIEDFWLTAARNVLKLVVKLEEKSQSISIQAREEEAPEDTQPKKQEKKLVTVSSDFVDEALSACQEHLSSIAHKDIDKDPNSPLYLSPDDWSQFLQRYYQIVHEGAELRYLEVQVQRCEDILQQLQNVVPQLDMEGDRNIWIVKPGAKSRGRGIMCMNRLDEMLKLVDCNPMLMKDGKWIVQKYIERPLLIFGTKFDLRQWFLVTDWNPLTVWFYRDSYIRFSTQPFSLKNLDNSVHLCNNSIQRHLEASCHRHPMLPPDNMWSSQRFQAHLQEVDAPKAWSSVIVPGMKAAVIHALQTSQDNVQCRKASFELYGADFVFGEDFQPWLIEINASPTMAPSTAVTARLCAGVQADTLRVVIDRRLDRSCDTGAFELIYKQPAVEVPQYVGIRLLVEGSTIKKPVPVGHRRTGVRSSLPHLLTQQGSGESKDSGSPTHRSASRKNARAESLEHTEKPEPAAVASVSGKGKKAPFHFPSLHSKAWLPSPRVHRPQGRVLRLQHDQLVGSKALSTTGKALMTLPTAKVLMSFPPHPDLKLAPSMLKPGKVGFELCCTTWRVVLSGGIGEEGHRQRAAPRPSSAPGKGLSSTEPCSKTET
6.3.2.-
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A4Q9E8};
axoneme assembly [GO:0035082]; cilium assembly [GO:0060271]; cilium movement [GO:0003341]; flagellated sperm motility [GO:0030317]; protein polyglycylation [GO:0018094]
axoneme [GO:0005930]; cilium [GO:0005929]; microtubule [GO:0005874]; microtubule cytoskeleton [GO:0015630]; sperm flagellum [GO:0036126]
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein-glycine ligase activity [GO:0070735]; protein-glycine ligase activity, initiating [GO:0070736]
PF03133;
3.30.470.20;
null
null
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19524510}. Cell projection, cilium {ECO:0000305|PubMed:19524510}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000305|PubMed:19524510}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000305|PubMed:33414192}.
CATALYTIC ACTIVITY: Reaction=ATP + glycine + L-glutamyl-[protein] = ADP + glycyl-L-glutamyl-[protein] + H(+) + phosphate; Xref=Rhea:RHEA:67180, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:17207, ChEBI:CHEBI:15378, ChEBI:CHEBI:29973, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57305, ChEBI:CHEBI:167890, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:19524510}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67181; Evidence={ECO:0000305|PubMed:19524510};
null
null
null
null
FUNCTION: Monoglycylase which modifies alpha- and beta-tubulin, adding a single glycine on the gamma-carboxyl groups of specific glutamate residues to generate monoglycine side chains within the C-terminal tail of tubulin (PubMed:19524510). Not involved in elongation step of the polyglycylation reaction (PubMed:19524510). Preferentially glycylates a beta-tail peptide over the alpha-tail, although shifts its preference toward alpha-tail as beta-tail glutamylation increases (By similarity). Competes with polyglutamylases for modification site on beta-tubulin substrate, thereby creating an anticorrelation between glycylation and glutamylation reactions (PubMed:33414192). Together with TTLL8, mediates microtubule glycylation of primary and motile cilia, which is essential for their stability and maintenance (PubMed:23897886, PubMed:25180231). Involved in microtubule glycylation of primary cilia in colon which controls cell proliferation of epithelial cells and plays an essential role in colon cancer development (PubMed:25180231). Together with TTLL8, glycylates sperm flagella which regulates axonemal dynein motor activity, thereby controlling flagellar beat, directional sperm swimming and male fertility (PubMed:33414192). {ECO:0000250|UniProtKB:B2GUB3, ECO:0000269|PubMed:19524510, ECO:0000269|PubMed:23897886, ECO:0000269|PubMed:25180231, ECO:0000269|PubMed:33414192}.
Mus musculus (Mouse)
A4Q9E8
TTLL6_MOUSE
MLQCLTSESEEGAEEREESSTEDLEELKEFVTLAFVRENTQKRLQNAQQHGKKKRKKKRLVINLSNCRYDSVRRAAQQYGLREAGDNDDWTLYWTDYSVSLERVMEMKSYQKINHFPGMSEICRKDLLARNMSRMLKLFPKDFHFFPRTWCLPADWGDLQTYSRTRKNKTYICKPDSGCQGRGIFITRSVKEIKPGEDMICQLYISKPFIIDGFKFDLRVYVLVTSCDPLRVFVYNEGLARFATTSYSHPNLDNLDEICMHLTNYSINKHSSNFVQDAFSGSKRKLSTFNSYMKTHGYDVEQIWRGIEDVIIKTLISAHPVIKHNYHTCFPSHTLNSACFEILGFDILLDRKLKPWLLEVNHSPSFSTDSKLDKEVKDSLLYDALVLINLGNCDKKKVLEEERQRGRFLQQCPNREIRLEEVKGFQAMRLQKTEEYEKKNCGGFRLIYPGLNLEKYDKFFQDNSSLFQNTVASRARELYARQLIQELRQKQEKKVFLKKARKEETQGESAGEQARDKVVRLQRQRQQPKCKTVATCPPKQSLHPVTLVSCTSGLLLNIRGLKKGEISESLEQKDTKEAMLIPCKPVSARNYSSVPDLRSANPSCFEPEFHVPNAKVKEVKSAFMVNIESTAQPITSVESSRDATAPISTSLESLASMSLSTSPECSSPESVHMVSYNHKQQKASFHKPMQEKKSKPLMFSKSRHLDLNCTSMKNDINRQYLMSEILQKVQMKKKRPLFPAPKSQYPTLSKERCPHSRSSSRKKEMNSPSVFVLQASHSRAESLNDLLVVATQARLDPRPSRSHSGTTTRDSSTQDPKHTATA
6.3.2.-
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:32747782};
microtubule bundle formation [GO:0001578]; microtubule cytoskeleton organization [GO:0000226]; microtubule severing [GO:0051013]; positive regulation of cilium movement [GO:0003353]; protein polyglutamylation [GO:0018095]; regulation of cilium beat frequency involved in ciliary motility [GO:0060296]
9+0 non-motile cilium [GO:0097731]; ciliary basal body [GO:0036064]; cilium [GO:0005929]; cytoplasm [GO:0005737]; microtubule [GO:0005874]
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein-glutamic acid ligase activity [GO:0070739]; tubulin binding [GO:0015631]; tubulin-glutamic acid ligase activity [GO:0070740]
PF03133;
3.30.470.20;
Tubulin--tyrosine ligase family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:26829768}. Cytoplasm, cytoskeleton {ECO:0000305|PubMed:20530212}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:17499049}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:17499049}. Note=CEP41 is required for its transport between the basal body and the cilium axoneme. {ECO:0000250|UniProtKB:Q8N841}.
CATALYTIC ACTIVITY: Reaction=ATP + L-glutamate + L-glutamyl-[protein] = ADP + gamma-L-glutamyl-L-glutamyl-[protein] + H(+) + phosphate; Xref=Rhea:RHEA:60144, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:15517, ChEBI:CHEBI:15378, ChEBI:CHEBI:29973, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:143622, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:17499049, ECO:0000269|PubMed:32747782}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60145; Evidence={ECO:0000305|PubMed:17499049, ECO:0000305|PubMed:32747782}; CATALYTIC ACTIVITY: Reaction=(L-glutamyl)(n)-gamma-L-glutamyl-L-glutamyl-[protein] + ATP + L-glutamate = (L-glutamyl)(n+1)-gamma-L-glutamyl-L-glutamyl-[protein] + ADP + H(+) + phosphate; Xref=Rhea:RHEA:60148, Rhea:RHEA-COMP:15519, Rhea:RHEA-COMP:15675, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:143623, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:17499049, ECO:0000269|PubMed:20530212, ECO:0000269|PubMed:21074048, ECO:0000269|PubMed:26829768, ECO:0000269|PubMed:32747782}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60149; Evidence={ECO:0000305|PubMed:17499049, ECO:0000305|PubMed:20530212, ECO:0000305|PubMed:21074048, ECO:0000305|PubMed:26829768, ECO:0000305|PubMed:32747782};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.22 uM for glutamylated tubulin {ECO:0000269|PubMed:32747782}; KM=1.92 uM for non-glutamylated tubulin {ECO:0000269|PubMed:32747782}; Note=kcat is 0.73 min(-1) with glutamylated tubulin as substrate (PubMed:32747782). kcat is 0.04 min(-1) with non-glutamylated tubulin as substrate (PubMed:32747782). {ECO:0000269|PubMed:32747782};
null
null
null
FUNCTION: Polyglutamylase which modifies both tubulin and non-tubulin proteins, generating alpha-linked polyglutamate side chains on the gamma-carboxyl group of specific glutamate residues of target proteins (PubMed:17499049, PubMed:20530212, PubMed:21074048, PubMed:26829768, PubMed:32747782). Preferentially mediates ATP-dependent long polyglutamate chain elongation over the initiation step of the polyglutamylation reaction (PubMed:17499049, PubMed:20530212, PubMed:21074048, PubMed:26829768, PubMed:32747782). Preferentially modifies the alpha-tubulin tail over a beta-tail (PubMed:17499049, PubMed:20530212, PubMed:21074048, PubMed:32747782). Promotes tubulin polyglutamylation which stimulates spastin/SPAST-mediated microtubule severing, thereby regulating microtubule functions (PubMed:20530212). Mediates microtubule polyglutamylation in primary cilia axoneme which is important for ciliary structural formation and motility (PubMed:22246503). Mediates microtubule polyglutamylation in motile cilia, necessary for the regulation of ciliary coordinated beating (PubMed:23897886). Polyglutamylates non-tubulin protein nucleotidyltransferase CGAS, leading to CGAS DNA-binding inhibition, thereby preventing antiviral defense response (PubMed:26829768). {ECO:0000269|PubMed:17499049, ECO:0000269|PubMed:20530212, ECO:0000269|PubMed:21074048, ECO:0000269|PubMed:22246503, ECO:0000269|PubMed:23897886, ECO:0000269|PubMed:26829768, ECO:0000269|PubMed:32747782}.
Mus musculus (Mouse)
A4Q9F0
TTLL7_MOUSE
MPSLPQDGVIQGSSPVDLGTELPYQCTMKRKVRKKKKKGIITANVAGTKFEIVRLVIDEMGFMKTPDEDETSNLIWCDAAVQQEKITDLQNYQRINHFPGMGEICRKDFLARNMTKMIKSRPMDYTFVPRTWIFPSEYTQFQNYVKELKKKRKQKTFIVKPANGAMGHGISLIRNGDKVPSQDHLIVQEYIEKPFLMEGYKFDLRIYILVTSCDPLKIFLYHDGLVRMGTEKYIPPNESNLTQLYMHLTNYSVNKHNERFERNETEDKGSKRSIKWFTEFLQANQHDVTKFWSDISELVVKTLIVAEPHVLHAYRMCRPGQPPGSESVCFEVLGFDILLDRKLKPWLLEINRAPSFGTDQKIDYDVKRGVLLNALKLLNIRTSDKRKNLAKQKAEAQRRLYGQNPVRRLSPGSSDWEQQRHQLERRKEELKERLLQVRKQVSQEEHENRHMGNYRRIYPPEDKALLEKYEGLLAVAFQTFLSGRAASFQREMNNPLKKMREEDLLDLLEQCEIDDEKLMGKTGRVRGPKPLCCMPECAEVTKKQKYYGSSDSSYDSSSSSSNSELDENEKELCQKRLDQVPYSLKHTSHCKIIQQPSGSHNLIYSESPVYLTTLVFLSEFPDSMRRSVSCPRSISAHLPSRGDVRPFSSQQVIPLARPTSASRSHSLNRASSYARHLPHGSDTGSTNTLNESLRQLKTKEQEDDLTSQTLFVLKDMRIRFPGKSDAESELLIEDIMDNWKHYKTKVASYWLIKLDSVKQRKVLDIVKSSIRTVLPRIWRVPDAEELSLYRIFNRVFNRLLWSHGQGLWSCFCDSGSSWESIFSKSPEVVTPLQLQCCQRLVELCKQCLLVVYKYTTETRGPISGIGPDWGNSRYLLPGSTQFLMRSPLYNMKYNSPGMTRSNVLFTSRYGRL
6.3.2.-
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A4Q9E8};
cell differentiation [GO:0030154]; microtubule cytoskeleton organization [GO:0000226]; nervous system development [GO:0007399]; protein polyglutamylation [GO:0018095]
9+0 non-motile cilium [GO:0097731]; ciliary basal body [GO:0036064]; cilium [GO:0005929]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; microtubule [GO:0005874]; perikaryon [GO:0043204]
alpha-tubulin binding [GO:0043014]; ATP binding [GO:0005524]; beta-tubulin binding [GO:0048487]; metal ion binding [GO:0046872]; tubulin binding [GO:0015631]; tubulin-glutamic acid ligase activity [GO:0070740]
PF03133;
3.30.470.20;
Tubulin--tyrosine ligase family
null
SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000269|PubMed:16901895, ECO:0000269|PubMed:17499049}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:16901895, ECO:0000269|PubMed:17499049}. Cell projection, dendrite {ECO:0000269|PubMed:16901895, ECO:0000269|PubMed:17499049}. Perikaryon {ECO:0000269|PubMed:16901895, ECO:0000269|PubMed:17499049}. Note=In cells with primary cilia, found in both cilia and basal bodies. In neuronal cells, found in dendrites and perikaryon. {ECO:0000269|PubMed:16901895, ECO:0000269|PubMed:17499049}.
CATALYTIC ACTIVITY: Reaction=ATP + L-glutamate + L-glutamyl-[protein] = ADP + gamma-L-glutamyl-L-glutamyl-[protein] + H(+) + phosphate; Xref=Rhea:RHEA:60144, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:15517, ChEBI:CHEBI:15378, ChEBI:CHEBI:29973, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:143622, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:16901895, ECO:0000269|PubMed:17499049, ECO:0000269|PubMed:19152315}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60145; Evidence={ECO:0000305|PubMed:16901895, ECO:0000305|PubMed:17499049, ECO:0000305|PubMed:19152315}; CATALYTIC ACTIVITY: Reaction=(L-glutamyl)(n)-gamma-L-glutamyl-L-glutamyl-[protein] + ATP + L-glutamate = (L-glutamyl)(n+1)-gamma-L-glutamyl-L-glutamyl-[protein] + ADP + H(+) + phosphate; Xref=Rhea:RHEA:60148, Rhea:RHEA-COMP:15519, Rhea:RHEA-COMP:15675, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:143623, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:16901895, ECO:0000269|PubMed:17499049, ECO:0000269|PubMed:19152315}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60149; Evidence={ECO:0000305|PubMed:16901895, ECO:0000305|PubMed:17499049, ECO:0000305|PubMed:19152315};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=20.2 uM for Glu (with 17 uM of tubulin for adult mouse) {ECO:0000269|PubMed:19152315}; KM=19.1 uM for ATP (with 17 uM of tubulin for adult mouse) {ECO:0000269|PubMed:19152315}; KM=19.6 uM for Glu (with 17 uM of tubulin for newborn mouse) {ECO:0000269|PubMed:19152315}; KM=26.5 uM for ATP (with 17 uM of tubulin for newborn mouse) {ECO:0000269|PubMed:19152315}; KM=5.4 uM for Glu (with 50 uM of ATP for adult mouse) {ECO:0000269|PubMed:19152315}; KM=21.8 uM for tubulin (with 50 uM of ATP for adult mouse) {ECO:0000269|PubMed:19152315}; KM=4.4 uM for Glu (with 50 uM of ATP for newborn mouse) {ECO:0000269|PubMed:19152315}; KM=15.8 uM for tubulin (with 50 uM of ATP for newborn mouse) {ECO:0000269|PubMed:19152315}; KM=7.5 uM for ATP (with 6 uM of Glu for adult mouse) {ECO:0000269|PubMed:19152315}; KM=3.1 uM for tubulin (with 6 uM of Glu for adult mouse) {ECO:0000269|PubMed:19152315}; KM=16 uM for ATP (with 6 uM of Glu for newborn mouse) {ECO:0000269|PubMed:19152315}; KM=6.7 uM for tubulin (with 6 uM of Glu for newborn mouse) {ECO:0000269|PubMed:19152315};
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:19152315};
null
FUNCTION: Polyglutamylase which modifies tubulin, generating polyglutamate side chains of variable lengths on the gamma-carboxyl group of specific glutamate residues within the C-terminal tail of tubulin (PubMed:16901895, PubMed:17499049, PubMed:19152315). Mediates both ATP-dependent initiation and elongation steps of the polyglutamylation reaction (PubMed:16901895, PubMed:17499049, PubMed:19152315). Preferentially modifies the beta-tubulin tail over an alpha-tail (PubMed:16901895, PubMed:17499049, PubMed:19152315). Competes with monoglycylase TTLL3 for modification site on beta-tubulin substrate, thereby creating an anticorrelation between glycylation and glutamylation reactions (By similarity). Required for neurite growth; responsible for the strong increase in tubulin polyglutamylation during postnatal neuronal maturation (PubMed:16901895). {ECO:0000250|UniProtKB:F7E540, ECO:0000269|PubMed:16901895, ECO:0000269|PubMed:17499049, ECO:0000269|PubMed:19152315}.
Mus musculus (Mouse)
A4Q9F1
TTLL8_MOUSE
MSCPPTPNPPFRPPSHTRVLRTPPLPPWVCLNSKSLSTGVGGQKNQLREASMENGERKKLSSTLSDGDHKEENKLKQGIPQDLSSSPKLDRYKIARQLTEKAIKERKIFSIYGHYPVIRATLRRKGWVEKKFNFFPKALQNLGSEDKSAETKENQEIALERFDDIHDVMSRLVKNEIPYLLWTIKRDVVDYHSLTCDQMLNHYGKTASFTTKIGLCLNMRSLPWYVQANPNTFFPRCYGLCTESEKQEFLDDFRRTVAASILKWVVLHQNYCSKVKGKSKKEEAKNSDPSPKKDPENPDLKLPSLSGQVVDTACKVCQAYLGQLEHEDIDVSEASTEALSEEEWNDLTQQYYLLVHGNASITDSKSYFAQCQALLSKISSVNPQTEIDGIRNIWIIKPAAKSRGRDIVCMDRVENILSLVAADSQTTKDNKWVVQKYIETPMLIYDTKFDIRQWFLVTDWNPLTIWFYKESYLRFSTQRFSLDKLDSAIHLCNNSIQRRLKNDKERSPLLPCHNMWTSTRFQEYLQKRGRGGTWGSIIYPSMKRAVTNAMRVAQDHVEARKNSFELYGADFILGRDFKPWLIEINSSPTMHPSTPVTAQLCAQVQEDTIKVVVDRKLDRNCDIGNFELLWRQPAVELPPFNGSDLCVEGISVKKAKKQMPPIASVGLSESLLDAPPKVRSARALMETVIRPPRTTVRQDWKREEAKVLSTTWSMPVMDAEVRGRAKPIYAFEVNDYQHVDNKSHKSGYTRVQSSKVPGVTLTSAQHPALFAQTMKPTQMTSSPPPTASGNHRDSSPFCPIVFEELWLHPNSQRRPSSCILQSRAQGWIRGIP
6.3.2.-
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A4Q9E8};
cilium assembly [GO:0060271]; cilium movement [GO:0003341]; flagellated sperm motility [GO:0030317]; protein polyglycylation [GO:0018094]
axoneme [GO:0005930]; cilium [GO:0005929]; microtubule [GO:0005874]; microtubule cytoskeleton [GO:0015630]; sperm flagellum [GO:0036126]
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein-glycine ligase activity [GO:0070735]; protein-glycine ligase activity, initiating [GO:0070736]
PF03133;
3.30.470.20;
null
null
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19427864, ECO:0000269|PubMed:19524510, ECO:0000269|PubMed:33414192}. Cell projection, cilium {ECO:0000305|PubMed:19524510}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000305|PubMed:19524510}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:33414192}.
CATALYTIC ACTIVITY: Reaction=ATP + glycine + L-glutamyl-[protein] = ADP + glycyl-L-glutamyl-[protein] + H(+) + phosphate; Xref=Rhea:RHEA:67180, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:17207, ChEBI:CHEBI:15378, ChEBI:CHEBI:29973, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57305, ChEBI:CHEBI:167890, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:19524510, ECO:0000269|PubMed:28576883}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67181; Evidence={ECO:0000305|PubMed:19524510, ECO:0000305|PubMed:28576883};
null
null
null
null
FUNCTION: Monoglycylase which modifies both tubulin and non-tubulin proteins, adding a single glycine on the gamma-carboxyl groups of specific glutamate residues to generate monoglycine side chains within the C-terminal tail of target proteins (PubMed:19524510, PubMed:28576883). Not involved in elongation step of the polyglycylation reaction (PubMed:19524510). Preferentially monoglycylates alpha-tubulin over beta-tubulin (PubMed:19524510). Together with TTLL3, mediates microtubule glycylation of primary and motile cilia, which is essential for their stability and maintenance (PubMed:19524510, PubMed:23897886, PubMed:25180231). Together with TTLL3, glycylates sperm flagella which regulates axonemal dynein motor activity, thereby controlling flagellar beat, directional sperm swimming and male fertility (PubMed:33414192). Monoglycylates non-tubulin proteins such as ANP32A, ANP32B, SET, NCL and NAP1 (PubMed:19427864, PubMed:19524510). {ECO:0000269|PubMed:19427864, ECO:0000269|PubMed:19524510, ECO:0000269|PubMed:23897886, ECO:0000269|PubMed:25180231, ECO:0000269|PubMed:28576883, ECO:0000269|PubMed:33414192}.
Mus musculus (Mouse)
A4Q9F3
TTL10_MOUSE
MALHPQAGRPHRDGSEAQAEAAAQDLGRLPSPSKVGAAVCRIQGLGHRAARRPRRGIGTTSASRVPRPGALMPATRNRPRFIHCRGQPPRTRVSSKRSKRSRIHPCHTEVPGWTHEKQMGSSVKERLRPELSQLDQDADDLEEEEAARLPVTSPDGLLMEGDKQPSPGQGPFFYIGGTNGASIISNYCESKGWQRTQDSHCEDYKLKWCEIKCRDNYCSFREGQQLLFQLPNNKLLTTKIGLLSALREHARTLSKARMLPSTQTKVLKMEEFFPETYRLDIRDERQAFFALFDETQMWICKPTASNQGKGIFLIRSQEEAAALQAKTQSIEDDPIYRKMPFRAPQARVVQRYVQNPLLLDGKKFDVRSYMLIACAMPYMVFFGHGYARLTLSLYNPHSSDLSGHLTNQFMQKKSPLYTLLKESTVWTMEHLNRYINDKFRKTKGLPRDWVFTTFTKRMQQIMSHCFLAVKSKLECKLGYFDLIGCDFLIDENFKVWLLEMNANPALHTNCEVLKAVIPGVVIETLDLALETCQKSLHSQKMLPLLSQRRFVLLYNGETTDLWPRLASSRPLNRLPNPNPNPNPNANPHPHPHPNPHPHPNPHPNANPHPPRPTCEAASSALSSARAAISERPGARKSMPSRGAPVCTPRKSRLSDSSGSSIAESEPSLCSGSLEGSRDTAREPSLGPPEEEREEEQRSTSHRGS
6.3.2.-
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A4Q9E8};
protein polyglycylation [GO:0018094]
axoneme [GO:0005930]; cilium [GO:0005929]; microtubule [GO:0005874]; microtubule cytoskeleton [GO:0015630]
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein-glycine ligase activity [GO:0070735]; protein-glycine ligase activity, elongating [GO:0070737]
PF03133;
3.30.470.20;
null
null
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19427864, ECO:0000269|PubMed:19524510}. Cell projection, cilium {ECO:0000305}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000305}.
CATALYTIC ACTIVITY: [Protein polyglycylase TTLL10]: Reaction=(glycyl)(n)-glycyl-L-glutamyl-[protein] + ATP + glycine = (glycyl)(n+1)-glycyl-L-glutamyl-[protein] + ADP + H(+) + phosphate; Xref=Rhea:RHEA:67184, Rhea:RHEA-COMP:17208, Rhea:RHEA-COMP:17209, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57305, ChEBI:CHEBI:167891, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:18331838, ECO:0000269|PubMed:19427864, ECO:0000269|PubMed:19524510}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67185; Evidence={ECO:0000305|PubMed:18331838, ECO:0000305|PubMed:19427864, ECO:0000305|PubMed:19524510};
null
null
null
null
FUNCTION: Polyglycylase which modifies both tubulin and non-tubulin proteins, generating polyglycine side chains of variable lengths on the gamma-carboxyl groups of specific glutamate residues of target proteins (PubMed:18331838, PubMed:19427864, PubMed:19524510). Involved in the elongation step rather than the initiation step of the polyglycylation reaction (PubMed:18331838, PubMed:19427864, PubMed:19524510). Polyglycylates alpha-tubulin and beta-tubulin (PubMed:19427864, PubMed:19524510). Polyglycylates non-tubulin proteins such as nucleosome assembly protein NAP1 (PubMed:18331838). {ECO:0000269|PubMed:18331838, ECO:0000269|PubMed:19427864, ECO:0000269|PubMed:19524510}.
Mus musculus (Mouse)
A4Q9F4
TTL11_MOUSE
MRRSSPEKKPEAEWEADAAAAAAATAAATESLPAETEKQQGVDAGAAGDPERLELEEQPKDVGRIPTPTRRHAPEEGEARVVRRLPPALPLAQPRPAARALSQLVKARGRSRSRVYRRSAGSMRPVTVDSSKARTSLDALKISLRQLRWKEFPFGRRLPCDIYWHGVSFRDSDILSGQVNKFPGMTEMVRKVTLSRALRIMQNLFPEEYNFYPRSWILPEEFQLFVSQVQTVKEGDPSWKPTFIVKPDSGCQGDGIYLIKDPCDGRLTGTLHNRPAVVQEYIRKPLLIDKLKFDIRLYVLLKSLDPLEIYIAKDGLSRFCTEPYQEPNPQNLHHVFMHLTNYSLNIHSGKFVHSDSASTGSKRTFSSILCRLSSKGVDIKKVWSDIISLVIKTVIALTPELKVFYQSDIPTGRPGPTCFQILGFDILLMKNLKPMLLEVNANPSMRIEHEYELSPGVFENIPSLVDEEVKVAVIRDTLRLMDPLKKKKEIHFPDIYMDRKHRIPPVSDRMSSWKHKGSSLSIVRSQQMEKSFTSKEDLNCDPTGGDSEPNPEAHLPSICLKQVFPKYAKQFNYLRLVDRMANLFIRFLGIKGTMKLGPTGFRTFIRNCKLSSSSLSMAAVDILYIDITRRWNSVTVDQRDSGMCLQAFVEAFFFLAQRKFKLQPLHEQVASLIDLCEYHLSVLDEKRLLCHRGRPLQRNPPQMNRPEHSATGSSAPRVIGASKLSQS
6.3.2.-
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A4Q9E8};
microtubule cytoskeleton organization [GO:0000226]; microtubule severing [GO:0051013]; protein modification process [GO:0036211]
ciliary basal body [GO:0036064]; cilium [GO:0005929]; cytoplasm [GO:0005737]; microtubule [GO:0005874]
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; tubulin binding [GO:0015631]; tubulin-glutamic acid ligase activity [GO:0070740]
PF03133;
3.30.470.20;
Tubulin--tyrosine ligase family
null
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:17499049}. Cytoplasm, cytoskeleton {ECO:0000305|PubMed:20530212}.
CATALYTIC ACTIVITY: Reaction=ATP + L-glutamate + L-glutamyl-[protein] = ADP + gamma-L-glutamyl-L-glutamyl-[protein] + H(+) + phosphate; Xref=Rhea:RHEA:60144, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:15517, ChEBI:CHEBI:15378, ChEBI:CHEBI:29973, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:143622, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:17499049}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60145; Evidence={ECO:0000305|PubMed:17499049}; CATALYTIC ACTIVITY: Reaction=(L-glutamyl)(n)-gamma-L-glutamyl-L-glutamyl-[protein] + ATP + L-glutamate = (L-glutamyl)(n+1)-gamma-L-glutamyl-L-glutamyl-[protein] + ADP + H(+) + phosphate; Xref=Rhea:RHEA:60148, Rhea:RHEA-COMP:15519, Rhea:RHEA-COMP:15675, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:143623, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:17499049, ECO:0000269|PubMed:20530212}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60149; Evidence={ECO:0000305|PubMed:17499049, ECO:0000305|PubMed:20530212};
null
null
null
null
FUNCTION: Polyglutamylase which modifies tubulin, generating polyglutamate side chains of variable lengths on the gamma-carboxyl group of specific glutamate residues within the C-terminal tail of tubulin (PubMed:17499049, PubMed:20530212). Preferentially mediates ATP-dependent polyglutamate long side-chain elongation over the initiation step of the polyglutamylation reaction (PubMed:17499049, PubMed:20530212). Preferentially modifies the alpha-tubulin tail over a beta-tail (PubMed:17499049). Required for CCSAP localization to both spindle and cilia microtubules (By similarity). Promotes tubulin polyglutamylation which stimulates spastin/SPAST-mediated microtubule severing, thereby regulating microtubule functions (PubMed:20530212). {ECO:0000250|UniProtKB:Q8NHH1, ECO:0000269|PubMed:17499049, ECO:0000269|PubMed:20530212}.
Mus musculus (Mouse)
A4QB65
AROE_CORGB
MNDSILLGLIGQGLDLSRTPAMHEAEGLAQGRATVYRRIDTLGSRASGQDLKTLLDAALYLGFNGLNITHPYKQAVLPLLDEVSEQATQLGAVNTVVIDANGHTTGHNTDVSGFGRGMEEGLPNAKLDSVVQVGAGGVGNAVAYALVTHGVQKLQVADLDTSRAQALADVINNAVGREAVVGVDARGIEDVIAAADGVVNATPMGMPAHPGTAFDVSCLTKDHWVGDVVYMPIETELLKAARALGCETLDGTRMAIHQAVDAFRLFTGLEPDVSRMRETFLSL
1.1.1.-; 1.1.1.24
null
amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; shikimate metabolic process [GO:0019632]
cytosol [GO:0005829]
NAD+ binding [GO:0070403]; NADP binding [GO:0050661]; quinate 3-dehydrogenase (NAD+) activity [GO:0030266]; shikimate 3-dehydrogenase (NAD+) activity [GO:0052734]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764]
PF18317;PF08501;
3.40.50.10860;3.40.50.720;
Shikimate dehydrogenase family
null
null
CATALYTIC ACTIVITY: Reaction=L-quinate + NAD(+) = 3-dehydroquinate + H(+) + NADH; Xref=Rhea:RHEA:22364, ChEBI:CHEBI:15378, ChEBI:CHEBI:29751, ChEBI:CHEBI:32364, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.24; Evidence={ECO:0000250|UniProtKB:Q9X5C9}; CATALYTIC ACTIVITY: Reaction=NAD(+) + shikimate = 3-dehydroshikimate + H(+) + NADH; Xref=Rhea:RHEA:17741, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000250|UniProtKB:Q9X5C9};
null
PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. {ECO:0000303|PubMed:19376919}.; PATHWAY: Aromatic compound metabolism; 3,4-dihydroxybenzoate biosynthesis; 3-dehydroquinate from D-quinate (NAD(+) route). {ECO:0000303|PubMed:19376919}.
null
null
FUNCTION: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids, and plays a key role in the quinate degradation pathway. Catalyzes the NAD(+)-dependent oxidation of both quinate and shikimate to 3-dehydroquinate and 3-dehydroshikimate, respectively. {ECO:0000269|PubMed:19376919}.
Corynebacterium glutamicum (strain R)
A4QPC6
BT2A2_MOUSE
MEPTTSLRSCPIASLLFFLVLSLFVLVSAQFTVIGPAEPILAMVGENTTLHCHLSPERNAEEMEVRWFRWRFFPAVLVYRGHQERPEEQMVAYRGRTTFMRTDISKGRVALIIHNVTAYDNGIYCCYFQEGRSYDQATMKLMVASLGSEPLIKMKTLEDGSILLECTSEGWYPEPRAVWRDPYDEVVPALEEEYTADREGLFTVTMTIIIRDCSVRNMTCSVNNTLLSQEVESVILIPESFVPSLPLWMVAVAVTLPVVMLILLTSGSICLVKKHRRKKSILSAEKEAEYEEKEAARQLQEELRWRRTLLHAADVVLDPDTAHPELFLSDDQRSVIRGSSRQSVPDNPERFDCRPCVLGRESFSSGKHYWEVEVENVMVWAIGVCRDSVERKGEALLVPQNGFWTLEMFGSQYRALSSPEKIIPLKERLHRIAVFLDCEGGDISFYNMRDRSHIYTCPPVTFTGPLRPFFRLGSDDSPLFICPAFTGAQGVTIPEGGLFLYKTRPISQSLVRKP
null
null
ERK1 and ERK2 cascade [GO:0070371]; G1/S transition of mitotic cell cycle [GO:0000082]; negative regulation of activated T cell proliferation [GO:0046007]; negative regulation of cytokine production [GO:0001818]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of G1/S transition of mitotic cell cycle [GO:2000134]; negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051898]; negative regulation of T cell receptor signaling pathway [GO:0050860]; phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0043491]; positive regulation of regulatory T cell differentiation [GO:0045591]; regulation of cytokine production [GO:0001817]; T cell receptor signaling pathway [GO:0050852]
cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]
signaling receptor binding [GO:0005102]
PF13765;PF00622;PF07686;
2.60.120.920;2.60.40.10;
Immunoglobulin superfamily, BTN/MOG family
PTM: N-glycosylated. {ECO:0000269|PubMed:20208008}.
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
null
null
null
null
null
FUNCTION: Inhibits the proliferation of CD4 and CD8 T-cells activated by anti-CD3 antibodies, T-cell metabolism and IL2 and IFNG secretion. {ECO:0000269|PubMed:20208008}.
Mus musculus (Mouse)
A4QUT2
KATG2_PYRO7
MHASLSSWLLAASLLTQPISVSGQGCPFAKRDGTVDSSLPQKRADAPETTTFGRCAVKSNQAGGGTRSHDWWPCQLRLDVLRQFQPSQNPLGGDFDYAEAFQSLDYEAVKKDIAALMTESQDWWPADFGNYGGLFVRMAWHSAGTYRAMDGRGGGGMGQQRFAPLNSWPDNQNLDKARRLIWPIKQKYGNKISWADLMLLTGNVALENMGFKTLGFGGGRADTWQSDEAVYWGAETTFVPQGNDVRYNNSVDINARADKLEKPLAATHMGLIYVNPEGPNGTPDPAASAKDIREAFGRMGMNDTETVALIAGGHAFGKTHGAVKGSNIGPAPEAADLGMQGLGWHNSVGDGNGPNQMTSGLEVIWTKTPTKWSNGYLESLINNNWTLVESPAGAHQWEAVNGTVDYPDPFDKTKFRKATMLTSDLALINDPEYLKISQRWLEHPEELADAFAKAWFKLLHRDLGPTTRYLGPEVPKESFIWQDPLPAREGDLIDDADVDKLKAAILSTDGLDVSKLASTAMACATTYRNSDKRGGCNGARIALEPQRNWVSNNPTQLSAVLDALKKVQSDFNGSNGNKKVSLADLIVLGGTAAVEKAAKDAGVDIKVPFSAGRVDATQEQTDVTQFSYLEPQADGFRNYGRGTARARTEEIMVDKASQLTLTPPELTVLVGGMRALGANYDGSDVGVFTANKGKLTPDFFVNLVDMNIAWTASGADGESWVGTDRKSRSEKYKGSRADLVFGSHAELRAIAEVYAENGNQEKFVKDFVAAWTKVMNLDRFDLKVKK
1.11.1.21
COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000255|HAMAP-Rule:MF_03108, ECO:0000269|PubMed:22822072}; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per monomer. {ECO:0000255|HAMAP-Rule:MF_03108, ECO:0000269|PubMed:22822072};
cellular response to hydrogen peroxide [GO:0070301]; hydrogen peroxide catabolic process [GO:0042744]
cytosol [GO:0005829]; extracellular region [GO:0005576]
catalase activity [GO:0004096]; heme binding [GO:0020037]; metal ion binding [GO:0046872]
PF00141;
1.10.520.10;1.10.420.10;
Peroxidase family, Peroxidase/catalase subfamily
PTM: Formation of the three residue Trp-Tyr-Met cross-link is important for the catalase, but not the peroxidase activity of the enzyme. {ECO:0000255|HAMAP-Rule:MF_03108}.
SUBCELLULAR LOCATION: Secreted {ECO:0000255|HAMAP-Rule:MF_03108, ECO:0000269|PubMed:21043575}.
CATALYTIC ACTIVITY: Reaction=AH2 + H2O2 = A + 2 H2O; Xref=Rhea:RHEA:30275, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:17499; EC=1.11.1.21; Evidence={ECO:0000255|HAMAP-Rule:MF_03108}; CATALYTIC ACTIVITY: Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.21; Evidence={ECO:0000255|HAMAP-Rule:MF_03108};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.84 mM for H(2)O(2) for the catalase reaction (at pH 5.25) {ECO:0000269|PubMed:21971530, ECO:0000269|PubMed:22822072}; KM=2.77 mM for H(2)O(2) for the catalase reaction (at pH 7.0) {ECO:0000269|PubMed:21971530, ECO:0000269|PubMed:22822072}; Note=kcat is 6446 sec(-1) with H(2)O(2) as substrate at pH 5.25 and 3290 sec(-1) with H(2)O(2) as substrate at pH 7.0.;
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.25 for the catalase reaction. Stable from pH 5.5 to pH 11. {ECO:0000269|PubMed:21971530, ECO:0000269|PubMed:22822072};
null
FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. Confers resistance to H(2)O(2) in hyphae. May play an antioxidative role in fungal defense against the host-produced H(2)O(2) (oxidative burst) at the early stage of plant infection. {ECO:0000255|HAMAP-Rule:MF_03108, ECO:0000269|PubMed:21043575, ECO:0000269|PubMed:21971530}.
Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Magnaporthe oryzae)
A4QXX4
SSN3_PYRO7
MSHSNPPTGASGGPGSASASAAPARGYYSLKRSIQTAFNDPLDRGLGPPAYQSKVRVMDKYQVIGFISSGTYGRVYKARGRQGQPGEFAIKKFKPDKEGEQITYTGISQSAIREMALCSELRHPNVIRLVETILEDKAIFMVFEYAEHDLLQIIHHHTQQPKHPIPPQTIKSIMFQLLNGCQYLHTNWVLHRDLKPANIMVTSSGEVKVGDLGLARIFWKPVRTLMQGDKVVVTIWYRAPELLMGSHHYTPAVDMWAVGCIFAELLSLRPIFKGEEAKMDNTKKGGSRDMPFQRHQMQKIVDIMGMPTKERWPLLTSMPDYDKLPLLQPPLSASGYSQQPAHSHHHHQHYNQGPQYGGRAGGPTSSSSANSSSAAAAASQSHLDKWYYHTVSQGQTAGPMPHAPPGSLASLGVEGYKLLAGLLEYDPEKRLTAAAALQHNFFSTGDRVSANCFEGCKAEYPHRRVSQEDNDIRTGSVPGTKRSGMPDDSMGRPGKRVKE
2.7.11.22; 2.7.11.23
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
negative regulation of filamentous growth [GO:0060258]; negative regulation of transcription by RNA polymerase II [GO:0000122]; nuclear-transcribed mRNA catabolic process, non-stop decay [GO:0070481]; phosphorylation [GO:0016310]; positive regulation of developmental process [GO:0051094]; positive regulation of transcription from RNA polymerase II promoter by galactose [GO:0000435]; protein destabilization [GO:0031648]
CKM complex [GO:1990508]; mediator complex [GO:0016592]
ATP binding [GO:0005524]; cyclin-dependent protein serine/threonine kinase activity [GO:0004693]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; RNA polymerase II CTD heptapeptide repeat kinase activity [GO:0008353]
PF00069;
1.10.510.10;
Protein kinase superfamily, CMGC Ser/Thr protein kinase family, CDC2/CDKX subfamily
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.22; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.22; CATALYTIC ACTIVITY: Reaction=[DNA-directed RNA polymerase] + ATP = ADP + H(+) + phospho-[DNA-directed RNA polymerase]; Xref=Rhea:RHEA:10216, Rhea:RHEA-COMP:11321, Rhea:RHEA-COMP:11322, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546, ChEBI:CHEBI:456216; EC=2.7.11.23;
null
null
null
null
FUNCTION: Component of the SRB8-11 complex. The SRB8-11 complex is a regulatory module of the Mediator complex which is itself involved in regulation of basal and activated RNA polymerase II-dependent transcription. The SRB8-11 complex may be involved in the transcriptional repression of a subset of genes regulated by Mediator. It may inhibit the association of the Mediator complex with RNA polymerase II to form the holoenzyme complex. The SRB8-11 complex phosphorylates the C-terminal domain (CTD) of the largest subunit of RNA polymerase II (By similarity). {ECO:0000250}.
Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Magnaporthe oryzae)
A4R5S9
KATG1_PYRO7
MGECPLRTANVAGGGTRNRDWWPNTLKLNILRQHTEATNPYDPNFDYAEAFKSLDYEGLKKDLRALMTDSQEYWPADFGHYGGLFVRMAWHSAGTYRVMDGRGGGGQGQQRFAPLNSWPDNVSLDKARRLLWPIKQKYGNKISWADLMLLTGNVALEDMGFKTFGFAGGRPDTWEADESTYWGGETTWLGNEVRYSSGNEGHKESGVIDGSESKKGHKDIHTRDLEKPVSAAHMGLIYVNPEGPDGIPDPVAAARDIRTTFSRMAMNDEETVALIAGGHTVGKTHGAAPSDNVGPEPEAAPIENQGLGWSNKHGSGKGPDTITSGLEVIWTKEPAKFTMNYLEYLFKYEWELTKSPAGANQWVAKNAEEFIPDAFDPSKKHKPRMLTTDLSLRFDPEYEKISRRFLENPEQFKDAFARAWFKLLHRDMGPRSRWLGPEVPKETLLWEDPIPTPDHPIIDGSDVDSLKKAILATGVAPSKLIQTAWASASTFRGGDKRGGANGARIRLEPQNKWEVNNPQQLAEVLKALEGVKADFEKSGKKVSIADLIVLAGVAAVEQAAGVPVPFTPGRGDATQEQTDVESFTHLEPAADAFRNYGKGTSRVTTEQIMVDRAQQLTLTAPELTVLVGGLRVLGANYDGSSHGVWTDKPGKLTNDFFVTLLDPYTSWKSVDGEVFEGTNSKSGKKLTGTRADLVFGSHSELRALAEVYGSADGQQKFTKDFVAAWDKVMNLDRFDVRRGIYDETRLKSKL
1.11.1.21
COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000255|HAMAP-Rule:MF_03108, ECO:0000269|PubMed:19000033}; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per monomer. {ECO:0000255|HAMAP-Rule:MF_03108, ECO:0000269|PubMed:19000033};
cellular response to hydrogen peroxide [GO:0070301]; hydrogen peroxide catabolic process [GO:0042744]
cytosol [GO:0005829]
catalase activity [GO:0004096]; heme binding [GO:0020037]; metal ion binding [GO:0046872]
PF00141;
1.10.520.10;1.10.420.10;
Peroxidase family, Peroxidase/catalase subfamily
PTM: Formation of the three residue Trp-Tyr-Met cross-link is important for the catalase, but not the peroxidase activity of the enzyme. {ECO:0000255|HAMAP-Rule:MF_03108}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03108}.
CATALYTIC ACTIVITY: Reaction=AH2 + H2O2 = A + 2 H2O; Xref=Rhea:RHEA:30275, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:17499; EC=1.11.1.21; Evidence={ECO:0000255|HAMAP-Rule:MF_03108, ECO:0000269|PubMed:19000033}; CATALYTIC ACTIVITY: Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.21; Evidence={ECO:0000255|HAMAP-Rule:MF_03108, ECO:0000269|PubMed:19000033};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.8 mM for H(2)O(2) for the catalase reaction {ECO:0000269|PubMed:19000033}; Note=kcat is 7010 sec(-1) with H(2)O(2) as substrate.;
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0 for the catalase reaction. {ECO:0000269|PubMed:19000033};
null
FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. {ECO:0000255|HAMAP-Rule:MF_03108, ECO:0000269|PubMed:19000033}.
Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Magnaporthe oryzae)
A4RD09
ARO1_PYRO7
MSTANGSSPTRISILGEESIIVDYGLWLNYVTHDLLNNIPSSTYVLITDTNLHSLYVPQFETAFTSASAAATSNSSATPPPPRAPRLLTYAIPPGEGSKSRDTKAEIEDWLLEQQCTRDTVIIALGGGVIGDMIGYVAATFMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPMGKNLVGAFWQPRRIYIDLAFLNTLPAREFINGMAEVIKTAAIWDAEEFSALEQNAPAILSAVRTPASAAADPNARLLPISDILKRIVLGSARVKAHIVSADEKEGGLRNLLNFGHSIGHAFEAILTPQVLHGEAVAVGMVKEAELARHLGILRPAAVARLVKCIASYDLPISLEDKRLVRMTGGKSCPVDIVLAKMAVDKKNEGKQKKIVLLSAIGKTHEPKASSVDDRAIRVVLSAAVRVQPGVRPGLKVDVTPPGSKSISNRALILAALGKGPCRIKNLLHSDDTEHMLNAIGKLRGASFSWEDDGEILVVEGRGGQLFAPSEGELYLGNAGTASRFLTTVAALCSPSSDGDATSTVLTGNARMKLRPIGALVDALRSNGINIEYMGKESSLPIRVDAAGGFGGGVIELAATVSSQYVSSLLMAAPYAKEPVTLRLVGGKPISQPYIDMTIAMMRSFGIDVQRSTTEADTYHIPQGIYTNPAEYTVESDASSATYPLAVAAITGTTCTIPNIGSASLQGDARFAVEVLRPMGCTVEQSASSTTVTGPPLGQLKGIPHVDMEPMTDAFLTASVLAAVASGTTQITGIANQRVKECNRIKAMKDQLAKFGVHCNELDDGIEVTGNSWTELTEPREIYCYDDHRVAMSFSVLSVISPHPVLILERECTGKTWPGWWDVLSGVFGVAMDGEEPLSHSTVTGSGPNNRSVFVIGMRGAGKSTAGKWMASTLGRTFMDLDTELERRHNTTIPDMVKSEVGWEGFRKFEVELLREMMETKPEGYIFSCGGGIVETPEAREALISYCRAGGAVLLVHRDTTHVLEYLNRDKSRPAWSEEIEKVYIRRKPWYQECSNFEYHSPHLGVEESAVEMPVDFARFVSLICGKSSHLREVKAKPHSFFVSLTVPNITAHTATIPKAVVGSDAVELRVDLLQDHSPEFVVRQVALLRSLCKMPIIFTVRTVSQGGRFPDADHAGALALYRVALRMGVEYVDVEMTMPEDVIETVTKAKGYTSIIASHHDPKGTLSWRNGAWMQYYNKALHYGDVIKLVGWCRTDEDNFSLLTFKTRMLAAHESTPIIALNMGEQGKLSRVLNGFMTPVTHAALPAAAAPGQLTAAEIRQALSLLSKIPKRKFYLFGKPISKSRSPILHNTLFQQTGLPHTYSRLETDKVAEVETTIRASDFGGASVTIPLKLDIMPMLDEITDAAKTIGAVNTIIPVPVQAGKQRLRGDNTDWCGMVHSLRMAGVTGKRACPASGVVVGSGGTTRAAIFALHSLGFSPIYIIARNATSVETIASSFPAEYDIRNLQGTLAYTEGMARPEVVISTIPATGDVDEGILMAVDSVLTLPMGTSNTGAARVLLEMAYTPTFTNMMARAKDAGWGTVPGFEVLAAQGWFQFQLWTDIKPVYSTASSIVMNGTSDSS
1.1.1.25; 2.5.1.19; 2.7.1.71; 4.2.1.10; 4.2.3.4
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.;
amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; phosphorylation [GO:0016310]
cytoplasm [GO:0005737]
3-dehydroquinate dehydratase activity [GO:0003855]; 3-dehydroquinate synthase activity [GO:0003856]; 3-phosphoshikimate 1-carboxyvinyltransferase activity [GO:0003866]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764]; shikimate kinase activity [GO:0004765]
PF01761;PF01487;PF00275;PF08501;PF01202;
3.40.50.1970;3.20.20.70;1.20.1090.10;3.65.10.10;3.40.50.10860;3.40.50.720;3.40.50.300;
Sugar phosphate cyclases superfamily, Dehydroquinate synthase family; EPSP synthase family; Shikimate kinase family; Type-I 3-dehydroquinase family; Shikimate dehydrogenase family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03143}.
CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=ATP + shikimate = 3-phosphoshikimate + ADP + H(+); Xref=Rhea:RHEA:13121, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36208, ChEBI:CHEBI:145989, ChEBI:CHEBI:456216; EC=2.7.1.71; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate; Xref=Rhea:RHEA:21256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57701, ChEBI:CHEBI:58702, ChEBI:CHEBI:145989; EC=2.5.1.19; Evidence={ECO:0000255|HAMAP-Rule:MF_03143};
null
PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7. {ECO:0000255|HAMAP-Rule:MF_03143}.
null
null
FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03143}.
Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Magnaporthe oryzae)
A4RPM5
UBA4_PYRO7
MEEADKRAEELRAQIAECEATLQSLKEQLAAAEAAKTPPYSDSTETDRGSSSSTWKWPLAEAEYERYGRQLILPSVGIQGQLRLKAASVLIVGAGGLGCPASAYFAGAGVGTIGLVDGDTVEASNLHRQVAHGTSRVGMLKVDSAISYLRELNPLVKYNAHQSHLTPENAESIVSGYDLVLDCTDHPTSRYLISDVCVLLRKPLVSASALRTDGQLIVLNTPAAPQADLSGGPCYRCVFPKPPPPDAVTSCGEGGILGPVVGVMGVLQALEGIRLLAAGRHLSPSPEQQQTAISPSLLLFSAPPDGSPAGFRSVRMRGRRKDCFACGEKSALSLATLREGGLDYVQFCGGSRKPVALLKSEERVSAEQLNALLQQQAGEHGKPVLLDVREREHFEIANIPGAINIPFSKTQNPGARHNAEDTPKLDWLPDGVADGHSPVYVVCRVGNDSQTVARQLKEFGLDNQGKRFIGDVKGGMLAWKREVDSTLPFM
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}.
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. {ECO:0000255|HAMAP-Rule:MF_03049}.
Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Magnaporthe oryzae)
A4STF2
FADB_AERS4
MIYQGETLSVSYLENGIAELRFDAPGSVNKLDRATLLSLSEAIAALQQQADLKGLILTSGKDAFIVGADITEFLELFDLPQEDLLGWLKKANDIFSAIEDLPVPTLSAIKGHALGGGCETILSTDFRLADTSAKIGLPETKLGIMPGFGGTVRLPRVIGADNALEWITTGKDYRADDALKVGAIDAVVAPDALHSAAVQMMKDAIAGKLNWQSRRAAKKAPLRLSKLEAMMSFSTAAGMVAAVAGKHYPAPMTAVKTVEAAAGMSRDEALVVEAQGFIKLAKTDVAKALVGIFLNDQHIKALAKKAAKQAAKATRHAAVLGAGIMGGGIAYQSASKGIPAVMKDINEKALALGMGEATKLLNGQLEKGRIDGIKMGQVLSAITPTLSYDNVKHVDLVVEAVVENPKVKAAVLGEVEGIIGDDAVLASNTSTIPISLLAKGLKRPQNFCGMHFFNPVHRMPLVEIIRGEQTSDETINRVVAYAAAMGKSPVVVNDCPGFFVNRVLFPYFFGFNKLVADGADFAAVDKVMEKEFGWPMGPAYLLDVVGIDTGHHAGDVMAQGFPARMSKEGRTAIDVMYDASRFGQKNGKGFYAYEQDKKGKPKKVADVAAYELLAPIAKPKQDFDKEAIIAGMMIPMINEVVLCLEEGIVATPAEADIALVYGLGFPPFRGGVFRYLDTIGLDRYVAMADQYADLGPLYRVSDRLREMAAQGKTFY
1.1.1.35; 4.2.1.17; 5.1.2.3; 5.3.3.8
null
fatty acid beta-oxidation [GO:0006635]
fatty acid beta-oxidation multienzyme complex [GO:0036125]
3-hydroxyacyl-CoA dehydrogenase activity [GO:0003857]; 3-hydroxybutyryl-CoA epimerase activity [GO:0008692]; delta(3)-delta(2)-enoyl-CoA isomerase activity [GO:0004165]; enoyl-CoA hydratase activity [GO:0004300]; NAD+ binding [GO:0070403]
PF00725;PF02737;PF00378;
1.10.1040.50;3.40.50.720;
Enoyl-CoA hydratase/isomerase family; 3-hydroxyacyl-CoA dehydrogenase family
null
null
CATALYTIC ACTIVITY: Reaction=a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:22432, ChEBI:CHEBI:15378, ChEBI:CHEBI:57318, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726; EC=1.1.1.35; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; CATALYTIC ACTIVITY: Reaction=a (3S)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O; Xref=Rhea:RHEA:16105, ChEBI:CHEBI:15377, ChEBI:CHEBI:57318, ChEBI:CHEBI:58856; EC=4.2.1.17; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; CATALYTIC ACTIVITY: Reaction=a 4-saturated-(3S)-3-hydroxyacyl-CoA = a (3E)-enoyl-CoA + H2O; Xref=Rhea:RHEA:20724, ChEBI:CHEBI:15377, ChEBI:CHEBI:58521, ChEBI:CHEBI:137480; EC=4.2.1.17; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; CATALYTIC ACTIVITY: Reaction=(3S)-3-hydroxybutanoyl-CoA = (3R)-3-hydroxybutanoyl-CoA; Xref=Rhea:RHEA:21760, ChEBI:CHEBI:57315, ChEBI:CHEBI:57316; EC=5.1.2.3; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; CATALYTIC ACTIVITY: Reaction=a (3Z)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA; Xref=Rhea:RHEA:45900, ChEBI:CHEBI:85097, ChEBI:CHEBI:85489; EC=5.3.3.8; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; CATALYTIC ACTIVITY: Reaction=a (3E)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA; Xref=Rhea:RHEA:45228, ChEBI:CHEBI:58521, ChEBI:CHEBI:85097; EC=5.3.3.8; Evidence={ECO:0000255|HAMAP-Rule:MF_01621};
null
PATHWAY: Lipid metabolism; fatty acid beta-oxidation. {ECO:0000255|HAMAP-Rule:MF_01621}.
null
null
FUNCTION: Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. {ECO:0000255|HAMAP-Rule:MF_01621}.
Aeromonas salmonicida (strain A449)
A4U6V3
M2_I45A0
MSLLTEVETPIRNEWGCRCNDSSDPLVVAANIIGILHLILWILDRLFFKCIYRLFKHGLKRGPSTEGVPESMREEYRKEQQSAVDADDSHFVNIELE
null
null
protein complex oligomerization [GO:0051259]; suppression by virus of host autophagy [GO:0039521]
host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion membrane [GO:0055036]
monoatomic ion channel activity [GO:0005216]; proton transmembrane transporter activity [GO:0015078]
PF00599;
6.10.250.1640;
Influenza viruses matrix protein M2 family
null
SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04069}. Host apical cell membrane {ECO:0000255|HAMAP-Rule:MF_04069}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04069}. Note=Abundantly expressed at the apical plasma membrane in infected polarized epithelial cells, in close proximity to budding and assembled virions. Minor component of virions (only 16-20 molecules/virion). {ECO:0000255|HAMAP-Rule:MF_04069}.
null
null
null
null
null
FUNCTION: Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry. After attaching to the cell surface, the virion enters the cell by endocytosis. Acidification of the endosome triggers M2 ion channel activity. The influx of protons into virion interior is believed to disrupt interactions between the viral ribonucleoprotein (RNP), matrix protein 1 (M1), and lipid bilayers, thereby freeing the viral genome from interaction with viral proteins and enabling RNA segments to migrate to the host cell nucleus, where influenza virus RNA transcription and replication occur. Also plays a role in viral proteins secretory pathway. Elevates the intravesicular pH of normally acidic compartments, such as trans-Golgi network, preventing newly formed hemagglutinin from premature switching to the fusion-active conformation. {ECO:0000255|HAMAP-Rule:MF_04069}.
Influenza A virus (strain A/USA:Huston/AA/1945 H1N1)
A4U7A7
M2_I51A0
MSLLTEVETPIRNEWGCRCNDSSDPLVVAASIIGILHLILWILDRLFFKCIYRLFKHGLKRGPSTEGVPESMREEYRKEQQSAVDADDSHFVNIELE
null
null
protein complex oligomerization [GO:0051259]; suppression by virus of host autophagy [GO:0039521]
host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion membrane [GO:0055036]
monoatomic ion channel activity [GO:0005216]; proton transmembrane transporter activity [GO:0015078]
PF00599;
6.10.250.1640;
Influenza viruses matrix protein M2 family
null
SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04069}. Host apical cell membrane {ECO:0000255|HAMAP-Rule:MF_04069}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04069}. Note=Abundantly expressed at the apical plasma membrane in infected polarized epithelial cells, in close proximity to budding and assembled virions. Minor component of virions (only 16-20 molecules/virion). {ECO:0000255|HAMAP-Rule:MF_04069}.
null
null
null
null
null
FUNCTION: Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry. After attaching to the cell surface, the virion enters the cell by endocytosis. Acidification of the endosome triggers M2 ion channel activity. The influx of protons into virion interior is believed to disrupt interactions between the viral ribonucleoprotein (RNP), matrix protein 1 (M1), and lipid bilayers, thereby freeing the viral genome from interaction with viral proteins and enabling RNA segments to migrate to the host cell nucleus, where influenza virus RNA transcription and replication occur. Also plays a role in viral proteins secretory pathway. Elevates the intravesicular pH of normally acidic compartments, such as trans-Golgi network, preventing newly formed hemagglutinin from premature switching to the fusion-active conformation. {ECO:0000255|HAMAP-Rule:MF_04069}.
Influenza A virus (strain A/USA:Albany/12/1951 H1N1)
A4UGR9
XIRP2_HUMAN
MSPESGHSRIFEATAGPNKPESGFAEDSAARGEGVSDLHEVVSLKERMARYQAAVSRGDCRSFSANMMEESEMCAVPGGLAKVKKQFEDEITSSRNTFAQYQYQHQNRSEQEAIHSSQVGTSRSSQEMARNEQEGSKVQKIDVHGTEMVSHLEKHTEEVNQASQFHQYVQETVIDTPEDEEIPKVSTKLLKEQFEKSAQEKILYSDKEMTTPAKQIKTESEYEETFKPSSVVSTSSTSCVSTSQRKETSTTRYSDHSVTSSTLAQINATSSGMTEEFPPPPPDVLQTSVDVTAFSQSPELPSPPRRLPVPKDVYSKQRNLYELNRLYKHIHPELRKNLEKDYISEVSEIVSSQMNSGSSVSADVQQARYVFENTNDSSQKDLNSEREYLEWDEILKGEVQSIRWIFENQPLDSINNGSPDEGDISRGIADQEIIAGGDVKYTTWMFETQPIDTLGAYSSDTVENAEKIPELARGDVCTARWMFETRPLDSMNKMHQSQEESAVTISKDITGGDVKTVRYMFETQHLDQLGQLHSVDEVHLLQLRSELKEIKGNVKRSIKCFETQPLYVIRDGSGQMLEIKTVHREDVEKGDVRTARWMFETQPLDTINKDITEIKVVRGISMEENVKGGVSKAKWLFETQPLEKIKESEEVIIEKEKIIGTDVSRKCWMFETQPLDILKEVPDADSLQREEIIGGDVQTTKHLFETLPIEALKDSPDIGKLQKITASEEEKGDVRHQKWIFETQPLEDIRKDKKEYTRTVKLEEVDRGDVKNYTHIFESNNLIKFDASHKIEVEGVTRGAVELNKSLFETTPLYAIQDPLGKYHQVKTVQQEEIVRGDVRSCRWLFETRPIDQFDESIHKFQIIRGISAQEIQTGNVKSAKWLFETQPLDSIKYFSDVEETESKTEQTRDIVKGDVKTCKWLFETQPMESLYEKVSLMTSSEEIHKGDVKTCTWLFETQPLDTIKDDSETAVKLQTVKQEEIQGGDVRTACFLFETENLDSIQGEEVKEIKPVEMDIQAGDVSSMRYKFENQSLDSISSSSEEVLKKIKTLKTEDIQKGNVLNCRWLFENQPIDKIKESQEGDECVKTVTDIQGGDVRKGCFIFETFSLDEIKEESDYISTKKTITEEVIQGDVKSYRMLFETQPLYAIQDREGSYHEVTTVKKEEVIHGDVRGTRWLFETKPLDSINKSETVYVIKSVTQEDIQKGDVSSVRYRFETQPLDQISEESHNIMPSIDHIQGGNVKTSRQFFESENFDKNNYIRTVSVNEIQKGNVKTSTWLFETHTMDELRGEGLEYENIKTVTQEDVQKGDVKQAVWLFENRTFDSIMEAHKGITKMTKEEIPPSDVKTTTWLFETTPLHEFNETRVEKIEIIGKSIKETLEDLYSQKVIQAPGIIIEADEIGDVRMAKYKLMNQASPEIQKEEIIRADLRNIMVNLLSKRDCTEREILISEEEKGNVNLTKTQLLNRSTEFHAEKEEIVKGDVQQAIKNLFSEERSVKKGILIQEDEKGDINMTIYCLLHENDGDTIEREEVIGGDVKRTIHNLLSSTSNNKISERAKIDASERGNVQFFTTCIEAGALDYLKQLHTESNETLTAKKQEGEKEIIGGDVEGTKLLLKKRQSLVERTVSETDIIPGDVHNTVKVFMTEPQSTFGKIPKEEIIKGDLTSTLNSLSQAVNQKTVTKTEEIIKGNMLATLKSLKESSHRWKESKQPDAIPGDIEKAIECLEKATNTKTEILKKELLKDDLETSLRSLKEAQRSFKEVHKEGVIKKDAKAVMAGSSGEQKTDIHQVAVQRNKNSLLQPKPGPFEPAAKWQGGADTLSQTMGKSCHGNLVEERTEVNLPKAPKGTVKIVIDREQNNDALEKSLRRLSNSHHKSNVLESGDKTGVWTDTTGEQHLRDEYMSRQLTSTVSVKNNLTTKESDRAVRELKKDDVFNSIQSAGKTVGKQQTYELRNDHQKMEGFHIKSPKKTKNIKILTDTQSSKPSPTQHPVSMPVGGTYDLSGDFQKQTLLKQETKYSNKDIKKKNINLQPMWQLLPVEQDTSNVTEMKVSEKSHNTFKATNKKRETDVHLKSQDFLMKTNTSTGLKMAMERSLNPINFNPENNVKESECPLPPPSPPPPPPSNASSEIEFPLPPPPPLMMFPEKNGFLPSLSTEKIKAEFESFPGLPLPPPPVDEKSERESSSMFLPPPPPPTPSQKPAHLLSSSAPEKHSGDFMQQYSQKEASNSQNSQAKIITGKTGVLPPPTLPKPKLPKHIKDNKNDFSPKVELATSLSDMECKITTSKDQKKVMVMTSSEHTETKQNVISKSLDERKQLSIDSANCLSHTVPGTSAPRKKQIAPLIKSHSFPESSGQQNPKPYMRKFKTPLMIAEEKYRQQKEEIEKQKQESSYYNIVKTQSQNQHITEVEKEMPLQKTNEEVSLSGIDSECTVVQPSPGSQSNARILGVCSDNQLSTTSPETVAAKRLHHVLAASEDKDKMKKEVLQSSRDIMQSKSACEIKQSHQECSTQQTQQKKYLEQLHLPQSKPISPNFKVKTIKLPTLDHTLNETDHSYESHKQQSEIDVQTFTKKQYLKTKKTEASTECSHKQSLAERHYQLPKKEKRVTVQLPTESIQKNQEDKLKMVPRKQREFSGSDRGKLPGSEEKNQGPSMIGRKEERLITERKHEHLKNKSAPKVVKQKVIDAHLDSQTQNFQQTQIQTAESKAEHKKLPQPYNSLQEEKCLEVKGIQEKQVFSNTKDSKQEITQNKSFFSSVKESQRDDGKGALNIVEFLRKREELQQILSRVKQFEAEPNKSGLKTFQTLLNTIPGWLISEDKREYAVHIAMENNLEKVKEEITHIKTQAEDMLVSYENIIQTAMMSSKTGKPGNKPTSLDETSSKVSNVHVSNNKNSEQKENKIAKEKTVQHQVAAHHEATVRSHVKTHQEIKLDDSNIPPPSLKTRPPSPTFITIESTARRTENPTKNELSQSPKKDSYVEPPPRRPMSQKSEIHRANTSPSPPRSRSEQLVRLKDTTAKLSKGAIPCPAATPVPIVEKRSEIIMSPATLRRQIKIETRGRDSPPTITIPVNINHAASGSFRESVDAQEEIRKVEKRATYVHKDGLNSTDHMVPDTESYDAVEIIRKVAVPPRLSEHTQRYEAANRTVQMAENFVNDPENEINRWFREFEHGPVSEAKSNRRVYAKGETNHNIQQESRTFCKEEFGLTSLGNTSFTDFSCKHPRELREKIPVKQPRICSETRSLSEHFSGMDAFESQIVESKMKTSSSHSSEAGKSGCDFKHAPPTYEDVIAGHILDISDSPKEVRKNFQKTWQESGRVFKGLGYATADASATEMRTTFQEESAFISEAAAPRQGNMYTLSKDSLSNGVPSGRQAEFS
null
null
actin filament organization [GO:0007015]; cardiac muscle tissue morphogenesis [GO:0055008]; cell-cell junction organization [GO:0045216]; ventricular septum development [GO:0003281]
focal adhesion [GO:0005925]; stress fiber [GO:0001725]; Z disc [GO:0030018]
actin filament binding [GO:0051015]; alpha-actinin binding [GO:0051393]
PF08043;
null
Xin family
null
SUBCELLULAR LOCATION: Cell junction {ECO:0000269|PubMed:15454575}. Note=Colocalizes with actin stress fibers. {ECO:0000250}.
null
null
null
null
null
FUNCTION: Protects actin filaments from depolymerization. {ECO:0000269|PubMed:15454575}.
Homo sapiens (Human)
A4UHT7
SALR_PAPBR
MPETCPNTVTKMRCAVVTGGNKGIGFEICKQLSSSGIMVVLTCRDVTRGLEAVEKLKNSNHENVVFHQLDVTDPITTMSSLADFIKARFGKLDILVNNAGVAGFSVDADRFKAMISDIGEDSEEVVKIYEKPEAQELMSETYELAEECLKINYYGVKSVTEVLLPLLQLSDSPRIVNVSSSTGSLKYVSNETALEILGDGDALTEERIDMVVNMLLKDFKENLIETNGWPSFGAAYTTSKACLNAYTRVLAKKIPKFQVNCVCPGLVKTEMNYGIGNYTADEGAKHVVRIALFPDDGPSGFFYDCSELSAF
1.1.1.248
null
alkaloid metabolic process [GO:0009820]
membrane [GO:0016020]
salutaridine reductase (NADPH) activity [GO:0047037]
PF00106;PF13561;
3.40.50.720;
Short-chain dehydrogenases/reductases (SDR) family
null
null
CATALYTIC ACTIVITY: Reaction=(7S)-salutaridinol + NADP(+) = H(+) + NADPH + salutaridine; Xref=Rhea:RHEA:10108, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58061, ChEBI:CHEBI:58349, ChEBI:CHEBI:58463; EC=1.1.1.248; Evidence={ECO:0000269|PubMed:17337529, ECO:0000269|PubMed:19648114};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=7.9 uM for salutaridine (Termination and extraction with NaHCO(3) and ethylacetate, respectively) {ECO:0000269|PubMed:17337529, ECO:0000269|PubMed:19648114}; KM=2.1 uM for salutaridine (Termination with methanol without extraction) {ECO:0000269|PubMed:17337529, ECO:0000269|PubMed:19648114}; KM=1.5 uM for salutaridinol {ECO:0000269|PubMed:17337529, ECO:0000269|PubMed:19648114}; KM=3.5 uM for NADPH {ECO:0000269|PubMed:17337529, ECO:0000269|PubMed:19648114}; KM=1190 uM for NADH {ECO:0000269|PubMed:17337529, ECO:0000269|PubMed:19648114}; KM=7 uM for NADP(+) {ECO:0000269|PubMed:17337529, ECO:0000269|PubMed:19648114}; Vmax=63.2 nmol/sec/mg enzyme with salutaridine as substrate (Termination and extraction with NaHCO(3) and ethylacetate, respectively) {ECO:0000269|PubMed:17337529, ECO:0000269|PubMed:19648114}; Vmax=35.6 nmol/sec/mg enzyme with salutaridine as substrate (Termination with methanol without extraction) {ECO:0000269|PubMed:17337529, ECO:0000269|PubMed:19648114}; Vmax=588 nmol/sec/mg enzyme with salutaridinol as substrate {ECO:0000269|PubMed:17337529, ECO:0000269|PubMed:19648114}; Vmax=57.3 nmol/sec/mg enzyme with NADPH as substrate {ECO:0000269|PubMed:17337529, ECO:0000269|PubMed:19648114}; Vmax=102 nmol/sec/mg enzyme with NADH as substrate {ECO:0000269|PubMed:17337529, ECO:0000269|PubMed:19648114}; Vmax=598 nmol/sec/mg enzyme with NADP(+) as substrate {ECO:0000269|PubMed:17337529, ECO:0000269|PubMed:19648114}; Note=The enzyme does not obey Michaelis-Menten kinetics because the theorectical Vmax cannot be achieved due to strong substrate inhibition, instead the optimal velocity, Vopt, is taken as the measure of enzyme performance. {ECO:0000269|PubMed:17337529, ECO:0000269|PubMed:19648114};
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6 for the reverse reaction (reduction) with activity decreasing sharply towards pH 4.5 and pH 7.5. Optimum pH is 9.5 for the forward reaction (oxidation) with greatly reduced activity at pH 6. {ECO:0000269|PubMed:17337529, ECO:0000269|PubMed:19648114};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius. {ECO:0000269|PubMed:17337529, ECO:0000269|PubMed:19648114};
FUNCTION: Involved in biosynthesis of morphinan-type benzylisoquinoline alkaloids. Catalyzes the stereospecific conversion of salutaridine to salutaridinol. {ECO:0000269|PubMed:17337529, ECO:0000269|PubMed:19648114}.
Papaver bracteatum (Great scarlet poppy)
A4UTP7
MEF2C_PIG
MGRKKIQITRIMDERNRQVTFTKRKFGLMKKAYELSVLCDCEIALIIFNSTNKLFQYASTDMDKVLLKYTEYNEPHESRTNSDIVEALNKKENKGCESPDPDSSYALTPRTEEKYKKINEEFDNMIKSHKIPAVPPPNFEMPVSIPVSSHNSLVYSNPVSSLGNPNFLPLAHPSLQRNSMSPGVTHRPPSAGNTGGLMGGDLTSGAGTSAGNGYGNPRNSPGLLVSPGNLNKNMQAKSPPPMNLGMNNRKPDLRVLIPPGSKNTMPSVSQRINNSQSAQSLATPVVSVATPTLPGQGMGGYPSAISTTYGTEYSLSSADLSSLSGFNTASALHLGSVTGWQQQHLHNMPPSALSQLGACTSTHLSQSSNLSLPSTQSLNIKSEPVSPPRDRTTTPSRYPQHTRHEAGRSPVDSLSSCSSSYDGSDREDHRNEFHSPIGLTRPSPDERESPSVKRMRLSEGWAT
null
null
B cell homeostasis [GO:0001782]; B cell proliferation [GO:0042100]; B cell receptor signaling pathway [GO:0050853]; blood vessel development [GO:0001568]; blood vessel remodeling [GO:0001974]; cardiac ventricle formation [GO:0003211]; cardiocyte differentiation [GO:0035051]; cellular response to calcium ion [GO:0071277]; cellular response to fluid shear stress [GO:0071498]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to parathyroid hormone stimulus [GO:0071374]; cellular response to transforming growth factor beta stimulus [GO:0071560]; cellular response to trichostatin A [GO:0035984]; cellular response to xenobiotic stimulus [GO:0071466]; chondrocyte differentiation [GO:0002062]; endochondral ossification [GO:0001958]; epithelial cell proliferation involved in renal tubule morphogenesis [GO:2001013]; germinal center formation [GO:0002467]; glomerulus morphogenesis [GO:0072102]; heart development [GO:0007507]; heart looping [GO:0001947]; humoral immune response [GO:0006959]; learning or memory [GO:0007611]; MAPK cascade [GO:0000165]; melanocyte differentiation [GO:0030318]; muscle cell fate determination [GO:0007521]; negative regulation of gene expression [GO:0010629]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of ossification [GO:0030279]; negative regulation of transcription by RNA polymerase II [GO:0000122]; nephron tubule epithelial cell differentiation [GO:0072160]; neural crest cell differentiation [GO:0014033]; neuron development [GO:0048666]; neuron differentiation [GO:0030182]; osteoblast differentiation [GO:0001649]; outflow tract morphogenesis [GO:0003151]; platelet formation [GO:0030220]; positive regulation of alkaline phosphatase activity [GO:0010694]; positive regulation of B cell proliferation [GO:0030890]; positive regulation of behavioral fear response [GO:2000987]; positive regulation of bone mineralization [GO:0030501]; positive regulation of cardiac muscle cell differentiation [GO:2000727]; positive regulation of cardiac muscle cell proliferation [GO:0060045]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of gene expression [GO:0010628]; positive regulation of macrophage apoptotic process [GO:2000111]; positive regulation of myoblast differentiation [GO:0045663]; positive regulation of neuron differentiation [GO:0045666]; positive regulation of osteoblast differentiation [GO:0045669]; positive regulation of skeletal muscle cell differentiation [GO:2001016]; positive regulation of skeletal muscle tissue development [GO:0048643]; positive regulation of transcription by RNA polymerase II [GO:0045944]; primary heart field specification [GO:0003138]; regulation of germinal center formation [GO:0002634]; regulation of megakaryocyte differentiation [GO:0045652]; regulation of synaptic activity [GO:0060025]; regulation of transcription by RNA polymerase II [GO:0006357]; renal tubule morphogenesis [GO:0061333]; secondary heart field specification [GO:0003139]; sinoatrial valve morphogenesis [GO:0003185]; skeletal muscle tissue development [GO:0007519]; smooth muscle cell differentiation [GO:0051145]; ventricular cardiac muscle cell differentiation [GO:0055012]
cytoplasm [GO:0005737]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; sarcoplasm [GO:0016528]
DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; 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]; transcription cis-regulatory region binding [GO:0000976]
PF12347;PF00319;
3.40.1810.10;
null
PTM: Phosphorylated on Ser-59; which enhances DNA binding activity. Phosphorylated on Ser-386; which is required for Lys-381 sumoylation and inhibits transcriptional activity. {ECO:0000250}.; PTM: Acetylated by p300 on several sites in diffentiating myocytes. Acetylation on Lys-4 increases DNA binding and transactivation (By similarity). {ECO:0000250}.; PTM: Sumoylated on Lys-381 with SUMO2 but not SUMO1; which represses transcriptional activity. {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:0000250|UniProtKB:A0A096MJY4}. Cytoplasm, sarcoplasm {ECO:0000250|UniProtKB:A0A096MJY4}.
null
null
null
null
null
FUNCTION: Transcription activator which binds specifically to the MEF2 element present in the regulatory regions of many muscle-specific genes. Controls cardiac morphogenesis and myogenesis, and is also involved in vascular development. Enhances transcriptional activation mediated by SOX18. Plays an essential role in hippocampal-dependent learning and memory by suppressing the number of excitatory synapses and thus regulating basal and evoked synaptic transmission. Crucial for normal neuronal development, distribution, and electrical activity in the neocortex. Necessary for proper development of megakaryocytes and platelets and for bone marrow B-lymphopoiesis. Required for B-cell survival and proliferation in response to BCR stimulation, efficient IgG1 antibody responses to T-cell-dependent antigens and for normal induction of germinal center B-cells. May also be involved in neurogenesis and in the development of cortical architecture (By similarity). {ECO:0000250|UniProtKB:Q06413, ECO:0000250|UniProtKB:Q8CFN5}.
Sus scrofa (Pig)
A4UUI3
GBP4_MOUSE
MTQPQMAPICLVENHNEQLSVNQEAIEILDKISQPVVVVAIVGWSHTGKSYLMNCLAGQNHVSGTLPTSQRFPSGLHRAVSDQGHLDVVHAPPHQARALVLLDTEGLGDVEKGDPKNDLWIFALSVLLSSTFVYNSMNTINHQALEQLHYVTELTELIRAKSSPNPHGIKNSTEFVSFFPDFVWTVRDFMLELKLNGEDITSDEYLENALKLIPGNNPRIQASNSARECIRRFFPNRKCFVFEWPTHDIELIKQLETISEDQLDPTFKESAMAFASYIFTYAKIKTLREGIKVTGNGLGTLVTTYVDAINSGAVPCLDDAVTTLAQRENSVAVQKAASHYSEQMAQRLSLPTDTIQELLDVHAACEKEAMAVFMEHSFKDENQQFLKKLVELLREKNGLFLLKNEEASDKYCQEELDRLSKDLMDNISTFSVPGGHRLYMDMREKIEHDYWQVPRKGVKASEVFQNFLQSQAIIESSILQADTALTAGQKAIAEKHTKKEAAEKEQDLLRQKQKEHQEYMEAQEKRNKENLEQLRRKLEQEREQLIKDHNMMLEKLTKEQKTFREEGYKTQAEELRREIHQLGHNIKEMKQNGDSLVESILRSWFSFISPPSESEKAISSVLSLLRKKDRL
3.6.5.-
null
cellular response to type II interferon [GO:0071346]; defense response to Gram-positive bacterium [GO:0050830]; defense response to protozoan [GO:0042832]; negative regulation of interferon-alpha production [GO:0032687]; negative regulation of protein import into nucleus [GO:0042308]; negative regulation of protein phosphorylation [GO:0001933]; negative regulation of protein ubiquitination [GO:0031397]; negative regulation of transcription by RNA polymerase II [GO:0000122]; regulation of defense response to virus [GO:0050688]
cytoplasmic vesicle [GO:0031410]; Golgi membrane [GO:0000139]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]
GTP binding [GO:0005525]; GTPase activity [GO:0003924]; ubiquitin-protein transferase inhibitor activity [GO:0055105]
PF02263;PF02841;
1.20.1000.10;3.40.50.300;
TRAFAC class dynamin-like GTPase superfamily, GB1/RHD3 GTPase family, GB1 subfamily
null
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q96PP9}. Cytoplasm {ECO:0000250|UniProtKB:Q96PP9}. Nucleus {ECO:0000250|UniProtKB:Q96PP9}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q96PP9}. Note=Heterodimers with GBP1, GBP2 and GBP5 localize in the compartment of the prenylated GBPs: with GBP1 in a vesicle-like compartment, with GBP2, around the nucleus and with GBP5, at the Golgi apparatus. {ECO:0000250|UniProtKB:Q96PP9}.
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:P32455};
null
null
null
null
FUNCTION: Interferon (IFN)-inducible GTPase that plays important roles in innate immunity against a diverse range of bacterial, viral and protozoan pathogens (PubMed:18025219). Negatively regulates the antiviral response by inhibiting activation of IRF7 transcription factor (PubMed:22095711). {ECO:0000269|PubMed:18025219, ECO:0000269|PubMed:22095711}.
Mus musculus (Mouse)
A4UVI1
FADS1_PAPAN
MAPDPVAAKTPVQGPTPRYFTWDEVAQRSGCEERWLVIDRKVYDISEFTRRHPGGSRVISHYAGQDATDPFVAFHSNKGLVKKYMNSLLIGELSPEQPSFEPTKNKELTDEFRELRATVEQMGLMKANHVFFLLYLLHILLLDGAAWLTLWIFGTSFLPFLLCAVLLTAAQIQAGWLQHDLGHLSVFSTSKWNHLVHHFVIGHLKGVPASWWNHMHFQHHAKPNCFGKDPDINMHPFFFALGKILSVELGKQKKKYMPYNHQHKYFFLIGPPALVPFFFQWYVFYFVIQRKKWVDLAWMITFYIRLLLTYVPLLGLKAFLGLYFIVRFLESNWFVWVTQMNHIPMHIDHDRNMDWVSTQLQATCNVHKSAFNDWFSGHLNFQIEHHLFPMMPRHNYHKVAPLVQSLCAKHGIEYQSKPLLSAFADIIHSLKESGQLWLDAYLHQ
1.14.19.44
null
unsaturated fatty acid biosynthetic process [GO:0006636]
endoplasmic reticulum membrane [GO:0005789]; mitochondrion [GO:0005739]
acyl-CoA delta5-desaturase activity [GO:0062076]
PF00173;PF00487;
3.10.120.10;
Fatty acid desaturase type 1 family
null
SUBCELLULAR LOCATION: [Isoform 1]: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22619218}; Multi-pass membrane protein {ECO:0000269|PubMed:22619218}. Mitochondrion {ECO:0000269|PubMed:22619218}.; SUBCELLULAR LOCATION: [Isoform 2]: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22619218}; Multi-pass membrane protein {ECO:0000269|PubMed:22619218}.
CATALYTIC ACTIVITY: Reaction=(8Z,11Z,14Z)-eicosatrienoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:46424, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:57368, ChEBI:CHEBI:74264; EC=1.14.19.44; Evidence={ECO:0000269|PubMed:22619218}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46425; Evidence={ECO:0000305|PubMed:22619218}; CATALYTIC ACTIVITY: Reaction=(8Z,11Z,14Z,17Z)-eicosatetraenoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:46420, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:73862, ChEBI:CHEBI:74265; EC=1.14.19.44; Evidence={ECO:0000250|UniProtKB:O60427, ECO:0000305|PubMed:22619218}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46421; Evidence={ECO:0000305|PubMed:22619218}; CATALYTIC ACTIVITY: Reaction=(11E)-octadecenoyl-CoA + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = (5Z,11E)-octadecadienoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:46060, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:74296, ChEBI:CHEBI:85651; Evidence={ECO:0000250|UniProtKB:Q920R3}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46061; Evidence={ECO:0000250|UniProtKB:Q920R3};
null
PATHWAY: Lipid metabolism; polyunsaturated fatty acid biosynthesis.
null
null
FUNCTION: [Isoform 1]: Acts as a front-end fatty acyl-coenzyme A (CoA) desaturase that introduces a cis double bond at carbon 5 located between a preexisting double bond and the carboxyl end of the fatty acyl chain. Involved in biosynthesis of highly unsaturated fatty acids (HUFA) from the essential polyunsaturated fatty acids (PUFA) linoleic acid (LA) (18:2n-6) and alpha-linolenic acid (ALA) (18:3n-3) precursors. Specifically, desaturates dihomo-gamma-linoleoate (DGLA) (20:3n-6) and eicosatetraenoate (ETA) (20:4n-3) to generate arachidonate (AA) (20:4n-6) and eicosapentaenoate (EPA) (20:5n-3), respectively (Probable). As a rate limiting enzyme for DGLA (20:3n-6) and AA (20:4n-6)-derived eicosanoid biosynthesis, controls the metabolism of inflammatory lipids like prostaglandin E2, critical for efficient acute inflammatory response and maintenance of epithelium homeostasis. Contributes to membrane phospholipid biosynthesis by providing AA (20:4n-6) as a major acyl chain esterified into phospholipids. In particular, regulates phosphatidylinositol-4,5-bisphosphate levels, modulating inflammatory cytokine production in T-cells (By similarity). Also desaturates (11E)-octadecenoate (trans-vaccenoate)(18:1n-9), a metabolite in the biohydrogenation pathway of LA (18:2n-6) (By similarity). {ECO:0000250|UniProtKB:Q920L1, ECO:0000250|UniProtKB:Q920R3, ECO:0000305|PubMed:22619218}.; FUNCTION: [Isoform 2]: Does not exhibit any catalytic activity toward 20:3n-6, but it may enhance FADS2 activity. {ECO:0000269|PubMed:22619218}.
Papio anubis (Olive baboon)
A4VBF0
PA2H_VIPBN
MRTLWIVAVCLIGVEGNLFQFGDMILQKTGKEAVHSYAIYGCYCGWGGQGRAQDATDRCCFAQDCCYGRVNDCNPKTATYTYSFENGDIVCGDNDLCLRAVCECDRAAAICLGENVNTYDKNYEYYSISHCTEESEQC
null
null
arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; negative regulation of T cell proliferation [GO:0042130]; phospholipid metabolic process [GO:0006644]
extracellular region [GO:0005576]
calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipase A2 inhibitor activity [GO:0019834]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729]
PF00068;
1.20.90.10;
Phospholipase A2 family, Group II subfamily, D49 sub-subfamily
null
SUBCELLULAR LOCATION: Secreted.
null
null
null
null
null
FUNCTION: Heterodimer: slightly affects neuromuscular transmission acting presynaptically. It has a low catalytic activity, a low anticoagulant activity and weakly inhibits ADP-induced platelet aggregation. {ECO:0000269|PubMed:18083205}.; FUNCTION: Monomer: has no activity (neurotoxic, catalytic, anticoagulant and a ADP-induced platelet aggregation), but inhibits phospholipase A2. {ECO:0000269|PubMed:18083205}.
Vipera berus nikolskii (Nikolsky's adder) (Vipera nikolskii)
A4VCL2
FA20C_DROME
MAVLRTMKLKERLVISLGATLVLLTLLLIVDVQMDFGVANRHLLQQQHQKIRLGNDYDGGTGGGGMLHEFKRKFLQKSNASGSKEASTQAGASQSGGATSGQDAAAGASGGAAGPGTSRSTSTRKPTPHDRYADLQKHLLSDEYSHVIVDNAPDVSRDNPTLAEMLHRKASANASNLERFQLRITKKELYGEQDTLVDAVLRDMIKLPIQHVVQKEGGTQLKLIIEYPNDIKALMKPMRFPREQQTLPNHFYFTDYERHNAEIAAFHLDRILGFRRAMPVAGRTLNITTEIYQLAEENLLKTFFVSPSLNLCFHGKCSYYCDTSHAICGNPDMLEGSFAAFLPNFESGNRKLWRHPWRRSYHKRKKAQWETDANYCALVRDIPPYDDGRRLYDLMDMAVFDFLTGNMDRHHYETFKVYGNETFPLHLDHGRGFGRPFHDELSILAPVLQCCLIRKSTLVKLLDFHNGPKPLSQLMSESLSQDPVSPVLWQPHLEALDRRTGIILQSIRDCIKRNPPGDVDGSETDVSS
2.7.11.1
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q9XTW2};
protein phosphorylation [GO:0006468]
extracellular region [GO:0005576]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
PF06702;
null
FAM20 family
null
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:22900076}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q8IXL6}. Secreted {ECO:0000250|UniProtKB:Q8IXL6}. Note=Resides in the Golgi apparatus membrane and is secreted following propeptide cleavage. {ECO:0000250|UniProtKB:Q8IXL6}.
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:0000303|PubMed:22900076}; 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:0000303|PubMed:22900076};
null
null
null
null
FUNCTION: Golgi serine/threonine protein kinase that phosphorylates secretory pathway proteins within Ser-x-Glu/pSer motifs. {ECO:0000250|UniProtKB:Q8IXL6, ECO:0000250|UniProtKB:Q9XTW2, ECO:0000303|PubMed:22900076}.
Drosophila melanogaster (Fruit fly)
A4VFY3
AKECT_STUS1
MHTVEKIGGTSMSRFEEVLDNIFIGRREGAALYQRIFVVSAYSGMTNLLLEHKKTGEPGVYQRFADAQSEGAWREALEGVRQRMLAKNAELFSSEYELHAANQFINSRIDDASECMHSLQKLCAYGHFQLSEHLMKVREMLASLGEAHSAFNSVLALKQRGVNARLADLTGWQQEAPLPFEEMISSHFAGFDFSRELVVATGYTHCAEGLMNTFDRGYSEITFAQIAAATGAREAIIHKEFHLSSADPNLVGADKVVTIGRTNYDVADQLSNLGMEAIHPRAAKTLRRAGVELRIKNAFEPEHGGTLISQDYKSEKPCVEIIAGRKDVFGIEVFDQDMLGDIGYDMEISKLLKQLKLYVVNKDSDANSITYYASGSRKLINRAARLIEEQYPAAEVTVHNLAIVSAIGSDLKVKGILAKTVAALAEAGISIQAIHQSIRQVEMQCVVNEEDYDAAIAALHRALIEPENHGDVIAAA
2.7.2.4
null
ectoine biosynthetic process [GO:0019491]; homoserine biosynthetic process [GO:0009090]; lysine biosynthetic process via diaminopimelate [GO:0009089]; phosphorylation [GO:0016310]
cytosol [GO:0005829]
aspartate kinase activity [GO:0004072]; ATP binding [GO:0005524]
PF00696;PF13840;
3.40.1160.10;3.30.2130.10;
Aspartokinase family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=ATP + L-aspartate = 4-phospho-L-aspartate + ADP; Xref=Rhea:RHEA:23776, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, ChEBI:CHEBI:57535, ChEBI:CHEBI:456216; EC=2.7.2.4; Evidence={ECO:0000269|PubMed:21725014};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.3 mM for ATP {ECO:0000269|PubMed:21725014}; KM=29.7 mM for L-aspartate {ECO:0000269|PubMed:21725014}; Vmax=6.9 umol/min/mg enzyme {ECO:0000269|PubMed:21725014};
PATHWAY: Amine and polyamine biosynthesis; ectoine biosynthesis.
null
null
FUNCTION: Involved in the biosynthesis of L-aspartate-beta-semialdehyde, which is an intermediate in the biosynthesis of ectoine, a highly soluble organic osmolyte, called compatible solute. Ectoine is used to avoid excessive water efflux, plasmolysis, molecular crowding of the cytoplasm, and cessation of growth in high salinity environments. Catalyzes the phosphorylation of the beta-carboxyl group of L-aspartate to yield 4-phospho-L-aspartate. {ECO:0000269|PubMed:21725014}.
Stutzerimonas stutzeri (strain A1501) (Pseudomonas stutzeri)
A4VGK4
D2HDH_STUS1
MTDPALIDELKTLVEPGKVLTDADSLNAYGKDWTKHFAPAPSAIVFPKSIEQVQAIVRWANAHKVALVPSGGRTGLSAAAVAANGEVVVSFDYMNQILEFNEMDRTAVCQPGVVTAQLQQFAEDKGLYYPVDFASAGSSQIGGNIGTNAGGIKVIRYGMTRNWVAGMKVVTGKGDLLELNKDLIKNATGYDLRQLFIGAEGTLGFVVEATMRLERQPTNLTALVLGTPDFDSIMPVLHAFQDKLDLTAFEFFSDKALAKVLGRGDVPAPFETDCPFYALLEFEATTEERAEQALATFEHCVEQGWVLDGVMSQSEQQLQNLWKLREYISETISHWTPYKNDISVTVGKVPAFLKEIDAIVGEHYPDFEIVWFGHIGDGNLHLNILKPDAMDKDEFFGKCATVNKWVFETVQKYNGSISAEHGVGMTKRDYLEYSRSPAEIEYMKAVKAVFDPNGIMNPGKIFAA
1.1.99.-; 1.1.99.39
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:28827360, ECO:0000269|PubMed:30131334}; Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:28827360};
lactate oxidation [GO:0019516]; respiratory electron transport chain [GO:0022904]
null
FAD binding [GO:0071949]; metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491]
PF02913;PF01565;
3.30.465.10;3.30.70.2190;3.30.70.2740;
FAD-binding oxidoreductase/transferase type 4 family
null
null
CATALYTIC ACTIVITY: Reaction=(R)-2-hydroxyglutarate + A = 2-oxoglutarate + AH2; Xref=Rhea:RHEA:38295, ChEBI:CHEBI:13193, ChEBI:CHEBI:15801, ChEBI:CHEBI:16810, ChEBI:CHEBI:17499; EC=1.1.99.39; Evidence={ECO:0000269|PubMed:28827360, ECO:0000269|PubMed:30131334}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38296; Evidence={ECO:0000269|PubMed:28827360, ECO:0000269|PubMed:30131334}; CATALYTIC ACTIVITY: Reaction=(R)-malate + A = AH2 + oxaloacetate; Xref=Rhea:RHEA:67460, ChEBI:CHEBI:13193, ChEBI:CHEBI:15588, ChEBI:CHEBI:16452, ChEBI:CHEBI:17499; Evidence={ECO:0000269|PubMed:28827360, ECO:0000269|PubMed:30131334}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67461; Evidence={ECO:0000269|PubMed:30131334};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.17 mM for D-2-hydroxyglutarate (at pH 7.4 and 37 degrees Celsius) {ECO:0000269|PubMed:28827360}; KM=7.71 uM for electron transfer flavoprotein (at pH 7.4 and 37 degrees Celsius) {ECO:0000269|PubMed:28827360}; KM=210 uM for cytochrome c (at pH 7.4 and 37 degrees Celsius) {ECO:0000269|PubMed:28827360}; KM=3.61 mM for D-malate (at pH 7.4 and 30 degrees Celsius) {ECO:0000269|PubMed:30131334}; Vmax=4.56 umol/min/mg enzyme with D-2-hydroxyglutarate as substrate and DCIP as the electron acceptor (at pH 7.4 and 37 degrees Celsius) {ECO:0000269|PubMed:28827360}; Vmax=7.5 umol/min/mg enzyme with D-2-hydroxyglutarate as substrate and electron transfer flavoprotein (ETF) as the electron acceptor (at pH 7.4 and 37 degrees Celsius) {ECO:0000269|PubMed:28827360}; Vmax=0.84 umol/min/mg enzyme with D-2-hydroxyglutarate as substrate and cytochrome c as the electron acceptor (at pH 7.4 and 37 degrees Celsius) {ECO:0000269|PubMed:28827360}; Vmax=6.87 umol/min/mg enzyme with D-2-malate as substrate and DCIP as the electron acceptor (at pH 7.4 and 30 degrees Celsius) {ECO:0000269|PubMed:30131334}; Note=kcat is 7.9 sec(-1) with D-2-hydroxyglutarate as substrate and DCIP as the electron acceptor (at pH 7.4 and 37 degrees Celsius). kcat is 13.0 sec(-1) with D-2-hydroxyglutarate as substrate and electron transfer flavoprotein (ETF) as the electron acceptor (at pH 7.4 and 37 degrees Celsius). kcat is 1.45 sec(-1) with D-2-hydroxyglutarate as substrate and cytochrome c as the electron acceptor (at pH 7.4 and 37 degrees Celsius) (PubMed:28827360). kcat is 11.7 sec(-1) with D-malate as substrate and DCIP as the electron acceptor (at pH 7.4 and 30 degrees Celsius) (PubMed:30131334). {ECO:0000269|PubMed:28827360, ECO:0000269|PubMed:30131334};
null
null
null
FUNCTION: Catalyzes the dehydrogenation of (R)-2-hydroxyglutarate (D-2-hydroxyglutarate or D-2-HG) to 2-oxoglutarate and of (R)-malate (D-malate) to oxaloacetate. Is functionally tied to L-serine biosynthesis, via its coupling with the D-3-phosphoglycerate dehydrogenase SerA, encoded by the adjacent gene in the locus. Is required for the utilization of D-2-hydroxyglutarate as well as D-malate as the sole carbon source for growth of P.stutzeri. Active in vitro with artificial electron acceptors such as 2,6-dichlorophenolindophenol (DCPIP) and appears to couple with electron transfer flavoprotein (ETF) for efficient oxidation of both D-2-hydroxyglutarate and D-malate in vivo. Cannot catalyze the oxidation of L-2-hydroxyglutarate, D-lactate, D-tartrate, D-2-hydroxybutanoate, D-mandelate, D-glycerate and D-phenyllactate. {ECO:0000269|PubMed:28827360, ECO:0000269|PubMed:30131334}.
Stutzerimonas stutzeri (strain A1501) (Pseudomonas stutzeri)
A4VJB4
AKLYS_STUS1
MALIVQKFGGTSVGTVERIEQVAEKVKKFRDGGDDIVVVVSAMSGETNRLIDLAKQISEQPVPRELDVMVSTGEQVTIALLAMALIKRGVPAVSYTGNQVRILTDSAHTKARILQIDAQRIQRDIKAGRVVVVAGFQGVDEKGNITTLGRGGSDTTGVALAAALKADECQIYTDVDGVYTTDPRVVAKAQRLDKITFEEMLEMASLGSKVLQIRAVEFAGKYSVPLRVLHSFQEGPGTLITLDEEESMEQPIISGIAFNRDEAKLTIRGVPDTPGVAFKILGPISAANVEVDMIVQNVAHDNTTDFTFTVHRNDYNNALQVLQGIAAEMGAREAIGDTNIAKVSIVGVGMRSHAGVASRMFEALAKENINIQMISTSEIKVSVVIEEKYLELAVRALHTAFELDAPAGNTAE
2.7.2.4
null
diaminopimelate biosynthetic process [GO:0019877]; homoserine biosynthetic process [GO:0009090]; lysine biosynthetic process via diaminopimelate [GO:0009089]; methionine biosynthetic process [GO:0009086]; phosphorylation [GO:0016310]; threonine biosynthetic process [GO:0009088]
cytosol [GO:0005829]
aspartate kinase activity [GO:0004072]; ATP binding [GO:0005524]
PF00696;PF01842;PF13840;
3.40.1160.10;3.30.2130.10;
Aspartokinase family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=ATP + L-aspartate = 4-phospho-L-aspartate + ADP; Xref=Rhea:RHEA:23776, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, ChEBI:CHEBI:57535, ChEBI:CHEBI:456216; EC=2.7.2.4; Evidence={ECO:0000269|PubMed:21725014};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.8 mM for ATP {ECO:0000269|PubMed:21725014}; KM=21.6 mM for L-aspartate {ECO:0000269|PubMed:21725014}; Vmax=5.1 umol/min/mg enzyme {ECO:0000269|PubMed:21725014};
PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.; PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 1/3.; PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 1/5.
null
null
FUNCTION: Involved in the biosynthesis of L-aspartate-beta-semialdehyde which is a central intermediate in the biosynthesis of different amino acids (L-lysine, L-methionine, L-threonine). Catalyzes the phosphorylation of the beta-carboxyl group of L-aspartate to yield 4-phospho-L-aspartate. {ECO:0000269|PubMed:21725014}.
Stutzerimonas stutzeri (strain A1501) (Pseudomonas stutzeri)
A4WFX4
FADB_ENT38
MLYKGDTLYVDWLEDGIAELVFDAPGSVNKLDTATVASLGHALDVLEKQSDLKGLLLRSEKAAFIVGADITEFLSLFQVPEEQLSQWLHFANSVFNRLEDLPVPTISAVNGYALGGGCECVLATDYRLATPDLRIGLPETKLGIMPGFGGSVRMPRMLGADSALEIIAAGKDVGADQALKIGLIDGIVKAEKLRDGAISILRQAINGDLDWKAKRQRKLEPLKLSKIEATMSFTIAKGMVMQTAGKHYPAPITAVKTIEAAARLGREEALKLENQSFVPLAHTNEARALVGIFLNDQFVKGKAKQLTKNVEMPKQAAVLGAGIMGGGIAYQSAWKGVPVIMKDINDKSLTLGMTEAAKLLNKQLERGKIDGLKLSGVISTIHPTLEYSGFDRVDVVVEAVVENPKIKKAVLAETEDKVRPDTVLASNTSTIPIGELASVLKRPENFCGMHFFNPVHRMPLVEVIRGEKTSDETIAKVVAWASKMGKTPIVVNDCPGFFVNRVLFPYFAGFSQLLRDGADFRKVDKVMEKQFGWPMGPAYLLDVVGIDTAHHAQAVMAAGFPQRMQKDYRDAIDALFDANRFGQKNGLGFWRYKEDSKGKPKKEDDTAVESLLADVSQPTRDFSDEEIIARMMIPMVNEVVRCLEEGIIASPAEADMALVYGLGFPPFHGGAFRWLDTLGSAKYLDMAQQYQQLGPLYEVPDGLRNKARHNEPYYPPVEPARPVGALKTA
1.1.1.35; 4.2.1.17; 5.1.2.3; 5.3.3.8
null
fatty acid beta-oxidation [GO:0006635]
fatty acid beta-oxidation multienzyme complex [GO:0036125]
3-hydroxyacyl-CoA dehydrogenase activity [GO:0003857]; 3-hydroxybutyryl-CoA epimerase activity [GO:0008692]; delta(3)-delta(2)-enoyl-CoA isomerase activity [GO:0004165]; enoyl-CoA hydratase activity [GO:0004300]; NAD+ binding [GO:0070403]
PF00725;PF02737;PF00378;
1.10.1040.50;3.40.50.720;
Enoyl-CoA hydratase/isomerase family; 3-hydroxyacyl-CoA dehydrogenase family
null
null
CATALYTIC ACTIVITY: Reaction=a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:22432, ChEBI:CHEBI:15378, ChEBI:CHEBI:57318, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726; EC=1.1.1.35; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; CATALYTIC ACTIVITY: Reaction=a (3S)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O; Xref=Rhea:RHEA:16105, ChEBI:CHEBI:15377, ChEBI:CHEBI:57318, ChEBI:CHEBI:58856; EC=4.2.1.17; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; CATALYTIC ACTIVITY: Reaction=a 4-saturated-(3S)-3-hydroxyacyl-CoA = a (3E)-enoyl-CoA + H2O; Xref=Rhea:RHEA:20724, ChEBI:CHEBI:15377, ChEBI:CHEBI:58521, ChEBI:CHEBI:137480; EC=4.2.1.17; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; CATALYTIC ACTIVITY: Reaction=(3S)-3-hydroxybutanoyl-CoA = (3R)-3-hydroxybutanoyl-CoA; Xref=Rhea:RHEA:21760, ChEBI:CHEBI:57315, ChEBI:CHEBI:57316; EC=5.1.2.3; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; CATALYTIC ACTIVITY: Reaction=a (3Z)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA; Xref=Rhea:RHEA:45900, ChEBI:CHEBI:85097, ChEBI:CHEBI:85489; EC=5.3.3.8; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; CATALYTIC ACTIVITY: Reaction=a (3E)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA; Xref=Rhea:RHEA:45228, ChEBI:CHEBI:58521, ChEBI:CHEBI:85097; EC=5.3.3.8; Evidence={ECO:0000255|HAMAP-Rule:MF_01621};
null
PATHWAY: Lipid metabolism; fatty acid beta-oxidation. {ECO:0000255|HAMAP-Rule:MF_01621}.
null
null
FUNCTION: Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. {ECO:0000255|HAMAP-Rule:MF_01621}.
Enterobacter sp. (strain 638)
A4WYU7
AGO_CERS5
MAPVQAADEMYDSNPHPDRRQLVSNGFEVNLPDQVEVIVRDLPDPSKVKEERTRLMGYWFVHWFDGKLFHLRIKAGGPNVDGEHRAIRTAEHPWLLRARLDDALEEALPKYAAVKKRPFTFLAQKDELIDAAATAAGLSHRLLNSFKVIPRFALSPKIYEPVDGTTRVGVFVTIGMRYDIEASLRDLLEAGIDLRGMYVVRRKRQPGERGLLGRVRAISDDMVQLFEETDLASVNVNDAKLEGSKENFTRCLSALLGHNYKKLLNALDDQEAGYRTGPRFDDAVRRMGEFLAKKPIRLADNINAQVGDRIVFSNEGQARNVRLAPKVEYVFDRTGAKSAEYAWRGLSQFGPFDRPSFANRSPRILVVYPSSTQGKVENFLSAFRDGMGSNYSGFSKGFVDLMGLTKVEFVMCPVEVSSADRNGAHTKYNSAIEDKLAGAGEVHAGIVVLFEDHARLPDDRNPYIHTKSLLLTLGVPTQQVRMPTVLLEPKSLQYTLQNFSIATYAKLNGTPWTVNHDKAINDELVVGMGLAELSGSRTEKRQRFVGITTVFAGDGSYLLGNVSKECEYEGYSDAIRESMTGILRELKKRNNWRPGDTVRVVFHAHRPLKRVDVASIVFECTREIGSDQNIQMAFVTVSHDHPFVLIDRSERGLEAYKGSTARKGVFAPPRGAISRVGRLTRLLAVNSPQLIKRANTPLPTPLLVSLHPDSTFKDVDYLAEQALKFTSLSWRSTLPAATPVTIFYSERIAELLGRLKSIPNWSSANLNIKLKWSRWFL
null
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:27325485}; Note=Mg(2+) contributes to binding the 5'-end of the gRNA. {ECO:0000269|PubMed:27325485};
clearance of foreign intracellular DNA [GO:0044355]
null
DNA binding [GO:0003677]; metal ion binding [GO:0046872]; RNA binding [GO:0003723]
PF02171;
3.40.50.2300;3.30.420.10;
Argonaute family, Long pAgo subfamily
null
null
null
null
null
null
null
FUNCTION: A catalytically inactive argonaute protein. Binds 5'-phosphorylated RNA as the guide (gRNA) and short DNA as target DNA (tDNA); does not bind other nucleic acid combinations, does not bind tDNA alone (PubMed:27325485, PubMed:29996105, PubMed:33333714). Has highest affinity for gRNA that begins with 5'-phospho-U and poor affinity for gRNA with 5'-OH (PubMed:27325485, PubMed:29996105). Upon expression in E.coli, plasmid sequences are found in RsAgo, its induction leads to plasmid degradation and suppression of genes encoded on foreign plasmids, suggesting it may also interfere with transcription (PubMed:24034694, PubMed:27325485). Does not interact with preformed gRNA:tDNA duplexes. Mismatches and nt bulges are tolerated in the ternary complex, however, they significantly reduce the affinity of RsAgo:gRNA for tDNA. Mismatched tDNA can cause dissociation of gRNA from RsAgo (PubMed:29996105). In situ binds 2 populations of RNA (15-19 and 45 nucleotides, nt) and a population of ssDNA 22-24 nt in length. The small sense RNA is probably derived from mRNA degradation and strongly enriched for U in the first and U/C in the second positions. The small DNA is enriched for sequences complementary to the RNA, with 3 nt overhangs on both ends; another nuclease may trim the ends. The sequences are largely derived from exogenous plasmids or genome-encoded foreign elements such as prophages and transposons (PubMed:24034694). Forms a ternary complex with gRNA and double-stranded tDNA only when the tDNA is open (PubMed:33333714). {ECO:0000269|PubMed:24034694, ECO:0000269|PubMed:27325485, ECO:0000269|PubMed:29996105, ECO:0000269|PubMed:33333714}.
Cereibacter sphaeroides (strain ATCC 17025 / ATH 2.4.3) (Rhodobacter sphaeroides)
A4X3Q0
SALL_SALTO
MQHNLIAFLSDVGSADEAHALCKGVMYGVAPAATIVDITHDVAPFDVREGALFLADVPHSFPAHTVICAYVYPETGTATHTIAVRNEKGQLLVGPNNGLLSFALDASPAVECHEVLSPDVMNQPVTPTWYGKDIVAACAAHLAAGTDLAAVGPRIDPKQIVRLPYASASEVEGGIRGEVVRIDRAFGNVWTNIPTHLIGSMLQDGERLEVKIEALSDTVLELPFCKTFGEVDEGQPLLYLNSRGRLALGLNQSNFIEKWPVVPGDSITVSPRVPDSNLGPVLG
2.5.1.94
null
null
null
transferase activity, transferring alkyl or aryl (other than methyl) groups [GO:0016765]
PF20257;PF01887;
2.40.30.90;3.40.50.10790;
SAM hydrolase / SAM-dependent halogenase family
null
null
CATALYTIC ACTIVITY: Reaction=chloride + S-adenosyl-L-methionine = 5'-chloro-5'-deoxyadenosine + L-methionine; Xref=Rhea:RHEA:28110, ChEBI:CHEBI:17996, ChEBI:CHEBI:47133, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.94; Evidence={ECO:0000269|PubMed:18059261};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1 uM for SAM (at pH 7.9 and 37 degrees Celsius) {ECO:0000269|PubMed:18059261}; KM=45 mM for chloride (at pH 7.9 and 37 degrees Celsius) {ECO:0000269|PubMed:18059261}; KM=150 mM for bromide (at pH 7.9 and 37 degrees Celsius) {ECO:0000269|PubMed:18059261}; KM=260 mM for iodide (at pH 7.9 and 37 degrees Celsius) {ECO:0000269|PubMed:18059261};
null
null
null
FUNCTION: Involved in the biosynthesis of the proteosome inhibitor salinosporamide A (SalA). Catalyzes the halogenation of S-adenosyl-L-methionine (SAM) with chloride to generate 5'-chloro-5'-deoxyadenosine (5'-CIDA) and L-methionine. It can also use bromide and iodide, producing halogenated 5'-deoxyadenosine (5'-XDA) and L-methionine, however no halogenase activity is detected in the presence of fluoride. {ECO:0000269|PubMed:18059261}.
Salinispora tropica (strain ATCC BAA-916 / DSM 44818 / JCM 13857 / NBRC 105044 / CNB-440)
A4XF23
MAND_NOVAD
MKITAARVIITCPGRNFVTLKIETDQGVYGIGDATLNGRELSVVAYLQEHVAPCLIGMDPRRIEDIWQYVYRGAYWRRGPVTMRAIAAVDMALWDIKAKMAGMPLYQLLGGRSRDGIMVYGHANGSDIAETVEAVGHYIDMGYKAIRAQTGVPGIKDAYGVGRGKLYYEPADASLPSVTGWDTRKALNYVPKLFEELRKTYGFDHHLLHDGHHRYTPQEAANLGKMLEPYQLFWLEDCTPAENQEAFRLVRQHTVTPLAVGEIFNTIWDAKDLIQNQLIDYIRATVVGAGGLTHLRRIADLASLYQVRTGCHGATDLSPVTMGCALHFDTWVPNFGIQEYMRHTEETDAVFPHDYWFEKGELFVGETPGHGVDIDEELAAKYPYKPAYLPVARLEDGTMWNW
4.2.1.8
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:17944491, ECO:0000269|PubMed:24697546}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000269|PubMed:17944491, ECO:0000269|PubMed:24697546};
amino acid catabolic process [GO:0009063]; carbohydrate catabolic process [GO:0016052]
null
magnesium ion binding [GO:0000287]; mannonate dehydratase activity [GO:0008927]
PF13378;PF02746;
3.20.20.120;3.30.390.10;
Mandelate racemase/muconate lactonizing enzyme family, GalD subfamily
null
null
CATALYTIC ACTIVITY: Reaction=D-mannonate = 2-dehydro-3-deoxy-D-gluconate + H2O; Xref=Rhea:RHEA:20097, ChEBI:CHEBI:15377, ChEBI:CHEBI:17767, ChEBI:CHEBI:57990; EC=4.2.1.8; Evidence={ECO:0000269|PubMed:17944491, ECO:0000269|PubMed:24697546};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Note=kcat is 1.3 sec(-1) with D-mannonate. {ECO:0000269|PubMed:17944491, ECO:0000269|PubMed:24697546};
PATHWAY: Carbohydrate metabolism; pentose and glucuronate interconversion.
null
null
FUNCTION: Catalyzes the dehydration of D-mannonate. Has no detectable activity with a panel of 70 other acid sugars (in vitro). {ECO:0000269|PubMed:17944491, ECO:0000269|PubMed:24697546}.
Novosphingobium aromaticivorans (strain ATCC 700278 / DSM 12444 / CCUG 56034 / CIP 105152 / NBRC 16084 / F199)
A4YDR9
HBCL2_METS5
MGGFKIPNYEGVDPTGSWYSVLTPLLFLERAGKYFKDKTAVVYRDSRYTYSTFYDNVMVQASALMRRGFSREDKLSFISRNRPEFLESFFGVPYAGGVLVPINFRLSPKEMAYIINHSDSKFVVVDEPYLNSLLEVKDQIKAEIILLEDPDNPSASETARKEVRMTYRELVKGGSRDPLPIPAKEEYSMITLYYTSGTTGLPKGVMHHHRGAFLNAMAEVLEHQMDLNSVYLWTLPMFHAASWGFSWATVAVGATNVCLDKVDYPLIYRLVEKERVTHMCAAPTVYVNLADYMKRNNLKFSNRVHMLVAGAAPAPATLKAMQEIGGYMCHVYGLTETYGPHSICEWRREWDSLPLEEQAKLKARQGIPYVSFEMDVFDANGKPVPWDGKTIGEVVMRGHNVALGYYKNPEKTAESFRDGWFHSGDAAVVHPDGYIEIVDRFKDLINTGGEKVSSILVEKTLMEIPGVKAVAVYGTPDEKWGEVVTARIELQEGVKLTEEEVIKFCKERLAHFECPKIVEFGPIPMTATGKMQKYVLRNEAKAKANKEKS
6.2.1.1; 6.2.1.17; 6.2.1.2; 6.2.1.40
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q08AH3}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q08AH3};
fatty acid metabolic process [GO:0006631]
null
acetate-CoA ligase activity [GO:0003987]; ATP binding [GO:0005524]; butyrate-CoA ligase activity [GO:0047760]; medium-chain fatty acid-CoA ligase activity [GO:0031956]; propionate-CoA ligase activity [GO:0050218]
PF00501;PF13193;
3.30.300.30;3.40.50.12780;
ATP-dependent AMP-binding enzyme family
null
null
CATALYTIC ACTIVITY: Reaction=4-hydroxybutanoate + ATP + CoA = 4-hydroxybutanoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:23128, ChEBI:CHEBI:16724, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:58574, ChEBI:CHEBI:456215; EC=6.2.1.40; Evidence={ECO:0000269|PubMed:23258541}; CATALYTIC ACTIVITY: Reaction=acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:23176, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:456215; EC=6.2.1.1; Evidence={ECO:0000269|PubMed:23258541}; CATALYTIC ACTIVITY: Reaction=ATP + CoA + propanoate = AMP + diphosphate + propanoyl-CoA; Xref=Rhea:RHEA:20373, ChEBI:CHEBI:17272, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57392, ChEBI:CHEBI:456215; EC=6.2.1.17; Evidence={ECO:0000269|PubMed:23258541}; CATALYTIC ACTIVITY: Reaction=a medium chain fatty acid + ATP + CoA = a medium-chain fatty acyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:48340, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:59558, ChEBI:CHEBI:90546, ChEBI:CHEBI:456215; EC=6.2.1.2; Evidence={ECO:0000269|PubMed:23258541};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=60 uM for butyrate {ECO:0000269|PubMed:23258541}; KM=120 uM for valerate {ECO:0000269|PubMed:23258541}; KM=540 uM for propionate {ECO:0000269|PubMed:23258541}; KM=680 uM for acetate {ECO:0000269|PubMed:23258541}; KM=1540 uM for 4HB {ECO:0000269|PubMed:23258541}; KM=1880 uM for 3HB {ECO:0000269|PubMed:23258541}; Vmax=0.22 umol/min/mg enzyme with 4HB as substrate {ECO:0000269|PubMed:23258541}; Vmax=0.21 umol/min/mg enzyme with butyrate as substrate {ECO:0000269|PubMed:23258541}; Vmax=0.2 umol/min/mg enzyme with valerate as substrate {ECO:0000269|PubMed:23258541}; Vmax=0.2 umol/min/mg enzyme with propionate as substrate {ECO:0000269|PubMed:23258541}; Vmax=0.13 umol/min/mg enzyme with acetate as substrate {ECO:0000269|PubMed:23258541}; Vmax=0.07 umol/min/mg enzyme with 3HB as substrate {ECO:0000269|PubMed:23258541}; Note=kcat is 0.24 sec(-1) for ligase activity with 4HB as substrate. kcat is 0.23 sec(-1) for ligase activity with butyrate as substrate. kcat is 0.22 sec(-1) for ligase activity with valerate as substrate. kcat is 0.21 sec(-1) for ligase activity with propionate as substrate. kcat is 0.14 sec(-1) for ligase activity with acetate as substrate. kcat is 0.08 sec(-1) for ligase activity with 3HB as substrate. {ECO:0000269|PubMed:23258541};
null
null
null
FUNCTION: Catalyzes the ligation of coenzyme A (CoA) to 4-hydroxybutyrate (4HB). It can also use butyrate, valerate, propionate, acetate and 3-hydroxybutyrate (3HB) as substrates. {ECO:0000269|PubMed:23258541}.
Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2)
A4YDT1
HBCL1_METS5
MVTVQDFFRKFIEFQNSPNEKSLQEIVKLVGQLDLRRFNWVRDVFEDIHVKERGSKTALIWRDINTGEEAKLSYHELSLMSNRVLSTLRKHGLKKGDVVYLMTKVHPMHWAVFLAVIKGGFVMVPSATNLTVAEMKYRFSDLKPSAIISDSLRASVMEEALGSLKVEKFLIDGKRETWNSLEDESSNAEPEDTRGEDVIINYFTSGTTGMPKRVIHTAVSYPVGSITTASIVGVRESDLHLNLSATGWAKFAWSSFFSPLLVGATVVGINYEGKLDTRRYLGEVENLGVTSFCAPPTAWRQFITLDLDQFRFERLRSVVSAGEPLNPEVIKIWKDKFNLTIRDFYGQTETTAMVGNFPFLKVKPGSMGKPHPLYDIRLLDDEGKEITKPYEVGHITVKLNPRPIGLFLGYSDEKKNMESFREGYYYTGDKAYFDEEGYFYFVGRGDDVIKTSDYRVGPFEVESALLEHPAVAEAAVVGVPDTVRWQLVKAYIVLKKGYMPSKELAEEIREKMKTLLSPYKVPRIIEFVDELPKTISGKIRRVELRKREEEKRKKGEVGQNEYVF
6.2.1.1; 6.2.1.17; 6.2.1.2; 6.2.1.40
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q08AH3}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q08AH3};
acyl-CoA metabolic process [GO:0006637]; fatty acid biosynthetic process [GO:0006633]
membrane [GO:0016020]
acetate-CoA ligase activity [GO:0003987]; ATP binding [GO:0005524]; butyrate-CoA ligase activity [GO:0047760]; fatty-acyl-CoA synthase activity [GO:0004321]; medium-chain fatty acid-CoA ligase activity [GO:0031956]; propionate-CoA ligase activity [GO:0050218]
PF00501;PF13193;
3.30.300.30;3.40.50.12780;
ATP-dependent AMP-binding enzyme family
null
SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
CATALYTIC ACTIVITY: Reaction=4-hydroxybutanoate + ATP + CoA = 4-hydroxybutanoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:23128, ChEBI:CHEBI:16724, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:58574, ChEBI:CHEBI:456215; EC=6.2.1.40; Evidence={ECO:0000269|PubMed:23258541}; CATALYTIC ACTIVITY: Reaction=acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:23176, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:456215; EC=6.2.1.1; Evidence={ECO:0000269|PubMed:23258541}; CATALYTIC ACTIVITY: Reaction=ATP + CoA + propanoate = AMP + diphosphate + propanoyl-CoA; Xref=Rhea:RHEA:20373, ChEBI:CHEBI:17272, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57392, ChEBI:CHEBI:456215; EC=6.2.1.17; Evidence={ECO:0000269|PubMed:23258541}; CATALYTIC ACTIVITY: Reaction=a medium chain fatty acid + ATP + CoA = a medium-chain fatty acyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:48340, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:59558, ChEBI:CHEBI:90546, ChEBI:CHEBI:456215; EC=6.2.1.2; Evidence={ECO:0000269|PubMed:23258541};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=320 uM for butyrate {ECO:0000269|PubMed:23258541}; KM=380 uM for propionate {ECO:0000269|PubMed:23258541}; KM=740 uM for valerate {ECO:0000269|PubMed:23258541}; KM=810 uM for 3HB {ECO:0000269|PubMed:23258541}; KM=2000 uM for 4HB {ECO:0000269|PubMed:23258541}; KM=2030 uM for acetate {ECO:0000269|PubMed:23258541}; Vmax=15.1 umol/min/mg enzyme with propionate as substrate {ECO:0000269|PubMed:23258541}; Vmax=7.9 umol/min/mg enzyme with butyrate as substrate {ECO:0000269|PubMed:23258541}; Vmax=6 umol/min/mg enzyme with acetate as substrate {ECO:0000269|PubMed:23258541}; Vmax=5.2 umol/min/mg enzyme with valerate as substrate {ECO:0000269|PubMed:23258541}; Vmax=2.4 umol/min/mg enzyme with 3HB as substrate {ECO:0000269|PubMed:23258541}; Vmax=1.7 umol/min/mg enzyme with 4HB as substrate {ECO:0000269|PubMed:23258541}; Note=kcat is 16.2 sec(-1) for ligase activity with propionate as substrate. kcat is 8.4 sec(-1) for ligase activity with butyrate as substrate. kcat is 6.4 sec(-1) for ligase activity with acetate as substrate. kcat is 5.6 sec(-1) for ligase activity with valerate as substrate. kcat is 2.6 sec(-1) for ligase activity with 3HB as substrate. kcat is 1.8 sec(-1) for ligase activity with 4HB as substrate. {ECO:0000269|PubMed:23258541};
null
null
null
FUNCTION: Involved in the 3-hydroxypropionate/4-hydroxybutyrate cycle which incorporates carbon dioxide into cellular carbon. Catalyzes the ligation of coenzyme A (CoA) to 4-hydroxybutyrate (4HB). It can also use butyrate, valerate, propionate, acetate and 3-hydroxybutyrate (3HB) as substrates. {ECO:0000269|PubMed:23258541}.
Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2)
A4ZDL6
GNK2_GINBI
MKTMRMNSAFILAFALAAAMLILTEAANTAFVSSACNTQKIPSGSPFNRNLRAMLADLRQNTAFSGYDYKTSRAGSGGAPTAYGRATCKQSISQSDCTACLSNLVNRIFSICNNAIGARVQLVDCFIQYEQRSF
null
null
defense response to bacterium [GO:0042742]; defense response to fungus [GO:0050832]; induction of programmed cell death [GO:0012502]; killing of cells of another organism [GO:0031640]
extracellular space [GO:0005615]; plasmodesma [GO:0009506]
actin binding [GO:0003779]; aspartic-type endopeptidase inhibitor activity [GO:0019828]; mannose binding [GO:0005537]
PF01657;
3.30.430.20;
null
null
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26315821}.
null
null
null
null
null
FUNCTION: Possesses antifungal activity against F.oxysporum, T.reesei and C.albicans. Weakly inhibits the aspartic acid protease pepsin activity (PubMed:17338634). Exerts antifungal activity against S.cerevisiae and F.culmorum through its carbohydrate-binding specificity. Acts as a lectin that stricly recognizes alpha-1,2-linked mannose moieties and interacts with the yeast cell wall mannan polysaccharide (PubMed:25139159). Can interfere with the fungal actin remodeling resulting to the activation of an actin-dependent cell death (PubMed:26315821). {ECO:0000269|PubMed:17338634, ECO:0000269|PubMed:25139159, ECO:0000269|PubMed:26315821}.
Ginkgo biloba (Ginkgo) (Maidenhair tree)
A4ZFB2
SCAF_BP80A
MEENKLKFNLQFFADQSDDPDEPGGDGKKGNPDKKENDEGTEITFTPEQQKKVDEILERRVAHEKKKADEYAKEKAAEAAKEAAKLAKMNKDQKDEYEREQMEKELEQLRSEKQLNEMRSEARKMLSEAEVDSSDEVVNLVVTDTAEQTKSNVEAFSNAVKKAVNEAVKVNARQSPLTGGDSFNHSTKNKPQNLAEIARQKRIIKN
null
null
virus-mediated perturbation of host defense response [GO:0019049]
viral scaffold [GO:0046806]
null
PF14265;
null
null
PTM: The N-terminus is cleaved by ribosomal processing protease Prp (PubMed:25388641). {ECO:0000269|PubMed:25388641}.
SUBCELLULAR LOCATION: Note=Found in provirions but not in mature virions. {ECO:0000269|PubMed:17693489, ECO:0000269|PubMed:18565341, ECO:0000269|PubMed:28984245}.
null
null
null
null
null
FUNCTION: Scaffolding protein involved in icosahedric procapsid assembly. Coassembles with capsid protein(s) to form the procapsid (PubMed:28984245). The scaffolding protein is found within the capsid as a series of concentric shells. During DNA packaging, the scaffolding protein molecules are released from the procapsid (By similarity). {ECO:0000250|UniProtKB:P13848, ECO:0000269|PubMed:28984245}.
Staphylococcus phage 80alpha
A5A3E0
POTEF_HUMAN
MVVEVDSMPAASSVKKPFGLRSKMGKWCCRCFPCCRESGKSNVGTSGDHDDSAMKTLRSKMGKWCRHCFPCCRGSGKSNVGASGDHDDSAMKTLRNKMGKWCCHCFPCCRGSSKSKVGAWGDYDDSAFMEPRYHVRGEDLDKLHRAAWWGKVPRKDLIVMLRDTDVNKQDKQKRTALHLASANGNSEVVKLLLDRRCQLNVLDNKKRTALIKAVQCQEDECALMLLEHGTDPNIPDEYGNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNALDRYGRTALILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYAVSSHHHVICQLLSDYKEKQMLKISSENSNPEQDLKLTSEEESQRFKGSENSQPEKMSQEPEINKDGDREVEEEMKKHESNNVGLLENLTNGVTAGNGDNGLIPQRKSRTPENQQFPDNESEEYHRICELLSDYKEKQMPKYSSENSNPEQDLKLTSEEESQRLKGSENGQPEKRSQEPEINKDGDRELENFMAIEEMKKHRSTHVGFPENLTNGATAGNGDDGLIPPRKSRTPESQQFPDTENEEYHSDEQNDTQKQFCEEQNTGILHDEILIHEEKQIEVVEKMNSELSLSCKKEKDILHENSTLREEIAMLRLELDTMKHQSQLREKKYLEDIESVKKRNDNLLKALQLNELTMDDDTAVLVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRQQGMMGGMHQKESYVGKEAQSKRGILTLKYPMEHGIITNWDDMEKIWHHTFYNELRVAPEEHPVLLTEATLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYTSGRTTGIVMDSGDGVTHTVPIYEGNALPHATLRLDLAGRELPDYLMKILTEHGYRFTTMAEREIVRDIKEKLCYVALDFEQEMATVASSSSLEKSYELPDGQVITIGNERFRCPEALFQPCFLGMESCGIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAALAPSMMKIRIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDESGPSIVHRKCL
null
null
axonogenesis [GO:0007409]; cell motility [GO:0048870]
actin filament [GO:0005884]; axon [GO:0030424]; blood microparticle [GO:0072562]; cell cortex [GO:0005938]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; membrane [GO:0016020]; NuA4 histone acetyltransferase complex [GO:0035267]; synapse [GO:0045202]
protein kinase binding [GO:0019901]; structural constituent of postsynaptic actin cytoskeleton [GO:0098973]
PF00022;PF12796;PF14915;
3.30.420.40;1.25.40.20;
POTE family; Actin family
null
SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000269|PubMed:17101985}. Note=Colocalizes with actin filaments.
null
null
null
null
null
null
Homo sapiens (Human)
A5A616
MGTS_ECOLI
MLGNMNVFMAVLGIILFSGFLAAYFSHKWDD
null
null
cellular response to magnesium starvation [GO:0010350]
plasma membrane [GO:0005886]
null
null
null
null
null
SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:21778229, ECO:0000305|PubMed:19121005}; Single-pass membrane protein {ECO:0000269|PubMed:21778229}.
null
null
null
null
null
FUNCTION: Modulates intracellular Mg(2+) levels to maintain cellular integrity upon Mg(2+) limitation. Acts by binding and stabilizing the Mg(2+) transporter MgtA, thereby leading to increased intracellular level of Mg(2+). May inhibit FtsH proteolysis of MgtA. {ECO:0000269|PubMed:28512220}.
Escherichia coli (strain K12)
A5A6H8
ITM2B_PANTR
MVKVTFNSALAQKEAKKDEPKSGEEALIIPPDAVAVDCKDPDDVVPVGQRRAWCWCMCFGLAFMLAGVILGGAYLYKYFALQPDDVYYCGIKYIKDDVILNEPSADAPAALYQTIEENIKIFEEEEVEFISVPVPEFADSDPANIVHDFNKKLTAYLDLNLDKCYVIPLNTSIVMPPRNLLELLINIKAGTYLPQSYLIHEHMVITDRIENIDHLGFFIYRLCHDKETYKLQRRETIKGIQKREASNCFAIRHFENKFAVETLICS
null
null
negative regulation of amyloid precursor protein biosynthetic process [GO:0042985]
endosome membrane [GO:0010008]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; Golgi-associated vesicle membrane [GO:0030660]; organelle membrane [GO:0031090]; plasma membrane [GO:0005886]
amyloid-beta binding [GO:0001540]; ATP binding [GO:0005524]
PF04089;
null
ITM2 family
PTM: The ectodomain C-terminal part of the imBRI2 is processed by furin producing a secreted Bri23 peptide and a mature BRI2, membrane form (mBRI2). The remaining part of the ectodomain of mBRI2 containing the BRICHOS domain is cleaved by ADAM10 and is secreted (BRI2C, soluble form). The membrane-bound N-terminal fragment (BRI2C, membrane form) is further proteolytically processed by SPPL2A and SPPL2B through regulated intramembrane proteolysis producing a secreted C-peptide and a BRI2 intracellular domain (BRI2 ICD) released in the cytosol. Shedding by ADAM10 facilitates intramembrane cleavage but is not absolutely required for BRI2 ICD generation (By similarity). {ECO:0000250}.; PTM: Glycosylation at Asn-170 is important for cell surface localization, but doesn't affect furin- and ADAM10-induced proteolytic processing. {ECO:0000250}.
SUBCELLULAR LOCATION: [Integral membrane protein 2B]: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9Y287}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9Y287}. Note=Immature BRI2 (imBRI2) is cleaved by furin in the Golgi into mBRI2 and a Bri23 peptide. mBRI2 is transported to the plasma membrane and Bri23 peptide is secreted. {ECO:0000250|UniProtKB:Q9Y287}.; SUBCELLULAR LOCATION: [BRI2, membrane form]: Cell membrane {ECO:0000250|UniProtKB:Q9Y287}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9Y287}. Endosome membrane {ECO:0000250|UniProtKB:Q9Y287}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q9Y287}. Note=Mature BRI2 (mBRI2) needs to be transported from the endoplasmic reticulum compartment to the cell membrane in order to be able to inhibit APP processing. {ECO:0000250|UniProtKB:Q9Y287}.; SUBCELLULAR LOCATION: [Bri23 peptide]: Secreted {ECO:0000250|UniProtKB:Q9Y287}. Note=Detected in the cerebral spinal fluid (CSF). {ECO:0000250|UniProtKB:Q9Y287}.; SUBCELLULAR LOCATION: [BRI2C, soluble form]: Secreted {ECO:0000250|UniProtKB:Q9Y287}.
null
null
null
null
null
FUNCTION: Plays a regulatory role in the processing of the amyloid-beta A4 precursor protein (APP) and acts as an inhibitor of the amyloid-beta peptide aggregation and fibrils deposition. Plays a role in the induction of neurite outgrowth. Functions as a protease inhibitor by blocking access of secretases to APP cleavage sites (By similarity). {ECO:0000250}.; FUNCTION: Mature BRI2 (mBRI2) functions as a modulator of the amyloid-beta A4 precursor protein (APP) processing leading to a strong reduction in the secretion of secretase-processed amyloid-beta protein 40 and amyloid-beta protein 42. {ECO:0000250}.; FUNCTION: Bri23 peptide prevents aggregation of APP amyloid-beta protein 42 into toxic oligomers. {ECO:0000250}.
Pan troglodytes (Chimpanzee)
A5A6J1
TBA1A_PANTR
MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSVEGEGEEEGEEY
3.6.5.-
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P68363};
microtubule cytoskeleton organization [GO:0000226]; mitotic cell cycle [GO:0000278]
cytoplasm [GO:0005737]; microtubule [GO:0005874]
GTP binding [GO:0005525]; hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]; structural constituent of cytoskeleton [GO:0005200]
PF00091;PF03953;
1.10.287.600;3.30.1330.20;3.40.50.1440;
Tubulin family
PTM: Some glutamate residues at the C-terminus are polyglycylated, resulting in polyglycine chains on the gamma-carboxyl group. Glycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella) whereas glutamylation is prevalent in neuronal cells, centrioles, axonemes, and the mitotic spindle. Both modifications can coexist on the same protein on adjacent residues, and lowering polyglycylation levels increases polyglutamylation, and reciprocally. Cilia and flagella glycylation is required for their stability and maintenance. Flagella glycylation controls sperm motility. {ECO:0000250|UniProtKB:P68369}.; PTM: Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group (By similarity). Polyglutamylation plays a key role in microtubule severing by spastin (SPAST). SPAST preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity by SPAST increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold (By similarity). Glutamylation is also involved in cilia motility (By similarity). {ECO:0000250|UniProtKB:P68369, ECO:0000250|UniProtKB:Q71U36}.; PTM: Acetylation of alpha chains at Lys-40 is located inside the microtubule lumen. This modification has been correlated with increased microtubule stability, intracellular transport and ciliary assembly. {ECO:0000250|UniProtKB:Q71U36}.; PTM: Methylation of alpha chains at Lys-40 is found in mitotic microtubules and is required for normal mitosis and cytokinesis contributing to genomic stability. {ECO:0000250|UniProtKB:P68363}.; PTM: Nitration of Tyr-451 is irreversible and interferes with normal dynein intracellular distribution. {ECO:0000250|UniProtKB:Q71U36}.; PTM: Undergoes a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue by the enzymes tubulin tyrosine carboxypeptidase (MATCAP, VASH1 or VASH2) and tubulin tyrosine ligase (TTL), respectively. {ECO:0000250|UniProtKB:P68369, ECO:0000250|UniProtKB:Q71U36}.; PTM: [Tubulin alpha-1A chain]: Tyrosination promotes microtubule interaction with CAP-Gly domain-containing proteins such as CLIP1, CLIP2 and DCTN1 (By similarity). Tyrosination regulates the initiation of dynein-dynactin motility via interaction with DCTN1, which brings the dynein-dynactin complex into contact with microtubules. In neurons, tyrosinated tubulins mediate the initiation of retrograde vesicle transport (By similarity). {ECO:0000250|UniProtKB:P68369, ECO:0000250|UniProtKB:Q71U36}.; PTM: [Detyrosinated tubulin alpha-1A chain]: Detyrosination is involved in metaphase plate congression by guiding chromosomes during mitosis: detyrosination promotes interaction with CENPE, promoting pole-proximal transport of chromosomes toward the equator (By similarity). Detyrosination increases microtubules-dependent mechanotransduction in dystrophic cardiac and skeletal muscle. In cardiomyocytes, detyrosinated microtubules are required to resist to contractile compression during contraction: detyrosination promotes association with desmin (DES) at force-generating sarcomeres, leading to buckled microtubules and mechanical resistance to contraction (By similarity). {ECO:0000250|UniProtKB:P68369, ECO:0000250|UniProtKB:Q71U36}.
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
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:P68363}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:P68363};
null
null
null
null
FUNCTION: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Pan troglodytes (Chimpanzee)
A5A6J2
DDX5_PANTR
MSGYSSDRDRGRDRGFGAPRFGGSRAGPLSGKKFGNPGEKLVKKKWNLDELPKFEKNFYQEHPDLARRTAQEVETYRRSKEITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLERGDGPICLVLAPTRELAQQVQQVAAEYCRACRLKSTCIYGGAPKGPQIRDLERGVENCIATPGRLIDFLECGKTNLRRTTYLVLDEADRMLDMGFEPQIRKIVDQIRPDRQTLMWSATWPKEVRQLAEDFLKDYIHINIGALELSANHNILQIVDVCHDVEKDEKLIRLMEEIMSEKENKTIVFVETKRRCDELTRKMRRDGWPAMGIHGDKSQQERDWVLNEFKHGKAPILIATDVASRGLDVEDVKFVINYDYPNSSEDYIHRIGRTARSTKTGTAYTFFTPNNIKQVSDLISVLREANQAINPKLLQLVEDRGSGRSRGRGGMKDDRRDRYSAGKRGGFNTFRDRENYDRGYSSLLKRDFGAKTQNGVYSAANYTNGSFGSNFVSAGIQASFRTGNPTGTYQNGYDSTQQYGSNVPNMHNGMNQQAYAYPATAAAPMIGYPMPTGYSQ
3.6.4.13
null
alternative mRNA splicing, via spliceosome [GO:0000380]; androgen receptor signaling pathway [GO:0030521]; epithelial to mesenchymal transition [GO:0001837]; intracellular estrogen receptor signaling pathway [GO:0030520]; intrinsic apoptotic signaling pathway by p53 class mediator [GO:0072332]; miRNA transcription [GO:0061614]; myoblast differentiation [GO:0045445]; negative regulation of transcription by RNA polymerase II [GO:0000122]; nuclear-transcribed mRNA catabolic process [GO:0000956]; positive regulation of DNA damage response, signal transduction by p53 class mediator [GO:0043517]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; regulation of androgen receptor signaling pathway [GO:0060765]; regulation of osteoblast differentiation [GO:0045667]; regulation of skeletal muscle cell differentiation [GO:2001014]; regulation of transcription by RNA polymerase II [GO:0006357]; rhythmic process [GO:0048511]
cytoplasm [GO:0005737]; nuclear speck [GO:0016607]; nucleolus [GO:0005730]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:1990904]; spliceosomal complex [GO:0005681]
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; mRNA 3'-UTR binding [GO:0003730]; nuclear androgen receptor binding [GO:0050681]; promoter-specific chromatin binding [GO:1990841]; ribonucleoprotein complex binding [GO:0043021]; RNA helicase activity [GO:0003724]
PF00270;PF00271;PF08061;
3.40.50.300;
DEAD box helicase family, DDX5/DBP2 subfamily
PTM: Sumoylated; sumoylation, promoted by PIAS1, promotes interaction with HDAC1 and transcriptional repression activity. Sumoylation also significantly increases stability, and reduces polyubiquitination (By similarity). {ECO:0000250|UniProtKB:P17844}.; PTM: Polyubiquitinated, leading to proteasomal degradation. {ECO:0000250|UniProtKB:P17844}.; PTM: Weakly phosphorylated in the G1/S phase of the cell cycle and much more at G2/M, especially at Thr and Tyr residues. {ECO:0000250|UniProtKB:P17844}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P17844}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P17844}. Cytoplasm {ECO:0000250|UniProtKB:P17844}. Note=During the G0 phase, predominantly located in the nucleus. Cytoplasmic levels increase during the G1/S phase. During the M phase, located at the vicinity of the condensed chromosomes. At G1, localizes in the cytoplasm. {ECO:0000250|UniProtKB:P17844}.
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: Involved in the alternative regulation of pre-mRNA splicing; its RNA helicase activity is necessary for increasing tau exon 10 inclusion and occurs in a RBM4-dependent manner. Binds to the tau pre-mRNA in the stem-loop region downstream of exon 10. The rate of ATP hydrolysis is highly stimulated by single-stranded RNA. Involved in transcriptional regulation; the function is independent of the RNA helicase activity. Transcriptional coactivator for androgen receptor AR but probably not ESR1. Synergizes with DDX17 and SRA1 RNA to activate MYOD1 transcriptional activity and involved in skeletal muscle differentiation. Transcriptional coactivator for p53/TP53 and involved in p53/TP53 transcriptional response to DNA damage and p53/TP53-dependent apoptosis. Transcriptional coactivator for RUNX2 and involved in regulation of osteoblast differentiation. Acts as a transcriptional repressor in a promoter-specific manner; the function probably involves association with histone deacetylases, such as HDAC1. As component of a large PER complex is involved in the inhibition of 3' transcriptional termination of circadian target genes such as PER1 and NR1D1 and the control of the circadian rhythms (By similarity). {ECO:0000250}.
Pan troglodytes (Chimpanzee)
A5A6J7
RAP1B_PANTR
MREYKLVVLGSGGVGKSALTVQFVQGIFVEKYDPTIEDSYRKQVEVDAQQCMLEILDTAGTEQFTAMRDLYMKNGQGFALVYSITAQSTFNDLQDLREQILRVKDTDDVPMILVGNKCDLEDERVVGKEQGQNLARQWNNCAFLESSAKSKINVNEIFYDLVRQINRKTPVPGKARKKSSCQLL
3.6.5.2
null
calcium-ion regulated exocytosis [GO:0017156]; cell population proliferation [GO:0008283]; cellular response to cAMP [GO:0071320]; establishment of endothelial barrier [GO:0061028]; establishment of localization in cell [GO:0051649]; modification of postsynaptic structure [GO:0099010]; negative regulation of calcium ion-dependent exocytosis [GO:0045955]; negative regulation of synaptic vesicle exocytosis [GO:2000301]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of integrin activation [GO:0033625]; Rap protein signal transduction [GO:0032486]; regulation of cell junction assembly [GO:1901888]; regulation of establishment of cell polarity [GO:2000114]
cell-cell junction [GO:0005911]; cytosol [GO:0005829]; glutamatergic synapse [GO:0098978]; lipid droplet [GO:0005811]; plasma membrane [GO:0005886]
G protein activity [GO:0003925]; GDP binding [GO:0019003]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; protein-containing complex binding [GO:0044877]
PF00071;
3.40.50.300;
null
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P61224}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P61224}. Cell junction {ECO:0000250|UniProtKB:P61224}. Note=May shuttle between plasma membrane and cytosol (By similarity). Presence of KRIT1 and CDH5 is required for its localization to the cell junction (By similarity). {ECO:0000250|UniProtKB:P61224}.
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; EC=3.6.5.2; Evidence={ECO:0000250|UniProtKB:P61224};
null
null
null
null
FUNCTION: GTP-binding protein that possesses intrinsic GTPase activity. Contributes to the polarizing activity of KRIT1 and CDH5 in the establishment and maintenance of correct endothelial cell polarity and vascular lumen. Required for the localization of phosphorylated PRKCZ, PARD3 and TIAM1 to the cell junction. Plays a role in the establishment of basal endothelial barrier function (By similarity). {ECO:0000250|UniProtKB:P61224}.
Pan troglodytes (Chimpanzee)
A5A6K9
HS90A_PANTR
MPEETQTQDQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSGKELHINLIPNKQDRTLTIVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAGGSFTVRTDTGEPMGRGTKVIPHLKEDQTEYLEERRIKEIVKKHSQFIGYPITLFVEKERDKEVSDDEAEEKEDKEEEKEKEEKESEDKPEIEDVGSDEEEEEKKDGDKKKKKKIKEKYIDQEELNKTKPIWTRNPDDITNEEYGEFYKSLTNDWEDHLAVKHFSVEGQLEFRALLFVPRRAPFDLFENRKKKNNIKLYVRRVFIMDNCEELIPEYLNFIRGVVDSEDLPLNISREMLQQSKILKVIRKNLVKKCLELFTELAEDKENYKKFYEQFSKNIKLGIHEDSQNRKKLSELLRYYTSASGDEMVSLKDYCTRMKENQKHIYYITGETKDQVANSAFVERLRKHGLEVIYMIEPIDEYCVQQLKEFEGKTLVSVTKEGLELPEDEEEKKKQEEKKTKFENLCKIMKDILEKKVEKVVVSNRLVTSPCCIVTSTYGWTANMERIMKAQALRDNSTMGYMAAKKHLEINPDHSIIETLRQKAEADKNDKSVKDLVILLYETALLSSGFSLEDPQTHANRIYRMIKLGLGIDEDDPTADDTSAAVTEEMPPLEGDDDTSRMEEVD
null
null
cellular response to heat [GO:0034605]; protein folding [GO:0006457]; protein stabilization [GO:0050821]; response to antibiotic [GO:0046677]; response to cold [GO:0009409]; response to heat [GO:0009408]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; melanosome [GO:0042470]; myelin sheath [GO:0043209]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein folding chaperone [GO:0140662]; disordered domain specific binding [GO:0097718]; unfolded protein binding [GO:0051082]
PF13589;PF00183;
3.30.230.80;3.40.50.11260;1.20.120.790;3.30.565.10;
Heat shock protein 90 family
PTM: ISGylated. {ECO:0000250|UniProtKB:P07900}.; PTM: S-nitrosylated; negatively regulates the ATPase activity and the activation of eNOS by HSP90AA1. {ECO:0000250|UniProtKB:P07900}.; PTM: Ubiquitinated via 'Lys-63'-linked polyubiquitination by HECTD1. Ubiquitination promotes translocation into the cytoplasm away from the membrane and secretory pathways. {ECO:0000250|UniProtKB:P07901}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07901}. Cytoplasm {ECO:0000250|UniProtKB:P07901}. Melanosome {ECO:0000250|UniProtKB:P07900}. Cell membrane {ECO:0000250|UniProtKB:P07900}.
null
null
null
null
null
FUNCTION: Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle. Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels. In the first place, they alter the steady-state levels of certain transcription factors in response to various physiological cues. Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment. Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression. Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes. {ECO:0000250|UniProtKB:P07900}.
Pan troglodytes (Chimpanzee)
A5A6M2
ANXA1_PANTR
MAMVSEFLKQAWFIENEEQEYVQTVKSSKGGPGSAVSPYPTFNPSSDVAALHKAIMVKGVDEATIIDILTRRNNAQRQQIKAAYLQETGKPLDETLKKALTGHLEEVVLALLKTPAQFDADELRAAMKGLGTDEDTLIEILASRTNKEIRDINRVYREELKRDLAKDITSDTSGDFRNALLSLAKGDRSEDFGVNEDLADSDARALYEAGERRKGTDVNVFNTILTTRSYPQLRRVFQKYTKYSKHDMNKVLDLELKGDIEKCLTAIVKCATSKPAFFAEKLHQAMKGVGTRHKALIRIMVSRSEIDMNDIKAFYQKMYGISLCQAILDETKGDYEKILVALCGGN
null
null
actin cytoskeleton organization [GO:0030036]; adaptive immune response [GO:0002250]; alpha-beta T cell differentiation [GO:0046632]; arachidonic acid secretion [GO:0050482]; cell surface receptor signaling pathway [GO:0007166]; cellular response to glucocorticoid stimulus [GO:0071385]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to vascular endothelial growth factor stimulus [GO:0035924]; DNA duplex unwinding [GO:0032508]; endocrine pancreas development [GO:0031018]; estrous cycle [GO:0044849]; G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger [GO:0007187]; gliogenesis [GO:0042063]; granulocyte chemotaxis [GO:0071621]; hepatocyte differentiation [GO:0070365]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; insulin secretion [GO:0030073]; keratinocyte differentiation [GO:0030216]; monocyte chemotaxis [GO:0002548]; myoblast migration involved in skeletal muscle regeneration [GO:0014839]; negative regulation of exocytosis [GO:0045920]; negative regulation of T-helper 2 cell differentiation [GO:0045629]; neutrophil activation [GO:0042119]; neutrophil clearance [GO:0097350]; phagocytosis [GO:0006909]; positive regulation of cell migration involved in sprouting angiogenesis [GO:0090050]; positive regulation of G1/S transition of mitotic cell cycle [GO:1900087]; positive regulation of interleukin-2 production [GO:0032743]; positive regulation of neutrophil apoptotic process [GO:0033031]; positive regulation of prostaglandin biosynthetic process [GO:0031394]; positive regulation of T cell proliferation [GO:0042102]; positive regulation of T-helper 1 cell differentiation [GO:0045627]; positive regulation of vesicle fusion [GO:0031340]; positive regulation of wound healing [GO:0090303]; prolactin secretion [GO:0070459]; prostate gland development [GO:0030850]; regulation of cell shape [GO:0008360]; regulation of hormone secretion [GO:0046883]; regulation of inflammatory response [GO:0050727]; regulation of interleukin-1 production [GO:0032652]; regulation of leukocyte migration [GO:0002685]; response to estradiol [GO:0032355]; response to interleukin-1 [GO:0070555]; response to peptide hormone [GO:0043434]; response to X-ray [GO:0010165]; signal transduction [GO:0007165]
apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; cytoplasm [GO:0005737]; early endosome membrane [GO:0031901]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; lateral plasma membrane [GO:0016328]; motile cilium [GO:0031514]; nucleus [GO:0005634]; phagocytic cup [GO:0001891]; plasma membrane [GO:0005886]
cadherin binding involved in cell-cell adhesion [GO:0098641]; calcium ion binding [GO:0005509]; calcium-dependent phospholipid binding [GO:0005544]; phosphatidylserine binding [GO:0001786]; phospholipase A2 inhibitor activity [GO:0019834]
PF00191;
1.10.220.10;
Annexin family
PTM: Phosphorylated by protein kinase C, EGFR and TRPM7. Phosphorylated in response to EGF treatment. {ECO:0000250|UniProtKB:P04083}.; PTM: Sumoylated. {ECO:0000250|UniProtKB:P10107}.; PTM: Proteolytically cleaved by cathepsin CTSG to release the active N-terminal peptide Ac2-26. {ECO:0000250|UniProtKB:P04083}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07150}. Cytoplasm {ECO:0000250|UniProtKB:P10107}. Cell projection, cilium {ECO:0000250|UniProtKB:P10107}. Basolateral cell membrane {ECO:0000250|UniProtKB:P51662}. Lateral cell membrane {ECO:0000250|UniProtKB:P10107}. Cell membrane {ECO:0000250|UniProtKB:P10107}; Peripheral membrane protein {ECO:0000250|UniProtKB:P10107}. Apical cell membrane {ECO:0000250|UniProtKB:P10107}. Membrane {ECO:0000250|UniProtKB:P10107}; Peripheral membrane protein {ECO:0000250|UniProtKB:P10107}. Early endosome {ECO:0000250|UniProtKB:P19619}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P19619}; Peripheral membrane protein {ECO:0000250|UniProtKB:P19619}. Endosome membrane {ECO:0000250|UniProtKB:P07150}; Peripheral membrane protein {ECO:0000250|UniProtKB:P07150}. Secreted {ECO:0000250|UniProtKB:P10107}. Secreted, extracellular space {ECO:0000250|UniProtKB:P04083}. Cell membrane {ECO:0000250|UniProtKB:P04083}; Peripheral membrane protein {ECO:0000250|UniProtKB:P04083}; Extracellular side {ECO:0000250|UniProtKB:P04083}. Secreted, extracellular exosome {ECO:0000250|UniProtKB:P10107}. Cytoplasmic vesicle, secretory vesicle lumen {ECO:0000250|UniProtKB:P10107}. Cell projection, phagocytic cup {ECO:0000250|UniProtKB:P10107}. Note=Colocalizes with actin fibers at phagocytic cups. Secreted, at least in part via exosomes and other secretory vesicles. Detected in exosomes and other extracellular vesicles. Secretion is increased in response to wounding and inflammation (By similarity). Alternatively, the secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10; it results in the protein translocation from the cytoplasm into ERGIC (endoplasmic reticulum-Golgi intermediate compartment) followed by vesicle entry and secretion (By similarity). Detected in gelatinase granules in resting neutrophils. Neutrophil adhesion to endothelial cells stimulates secretion via gelatinase granules, but foreign particle phagocytosis has no effect. Displays calcium-dependent binding to phospholipid membranes (By similarity). {ECO:0000250|UniProtKB:P04083, ECO:0000250|UniProtKB:P10107}.
null
null
null
null
null
FUNCTION: Plays important roles in the innate immune response as effector of glucocorticoid-mediated responses and regulator of the inflammatory process. Has anti-inflammatory activity. Plays a role in glucocorticoid-mediated down-regulation of the early phase of the inflammatory response. Contributes to the adaptive immune response by enhancing signaling cascades that are triggered by T-cell activation, regulates differentiation and proliferation of activated T-cells. Promotes the differentiation of T-cells into Th1 cells and negatively regulates differentiation into Th2 cells (By similarity). Has no effect on unstimulated T-cells. Negatively regulates hormone exocytosis via activation of the formyl peptide receptors and reorganization of the actin cytoskeleton (By similarity). Has high affinity for Ca(2+) and can bind up to eight Ca(2+) ions (By similarity). Displays Ca(2+)-dependent binding to phospholipid membranes (By similarity). Plays a role in the formation of phagocytic cups and phagosomes. Plays a role in phagocytosis by mediating the Ca(2+)-dependent interaction between phagosomes and the actin cytoskeleton (By similarity). {ECO:0000250|UniProtKB:P04083, ECO:0000250|UniProtKB:P10107, ECO:0000250|UniProtKB:P19619}.; FUNCTION: [Annexin Ac2-26]: Functions at least in part by activating the formyl peptide receptors and downstream signaling cascades. Promotes chemotaxis of granulocytes and monocytes via activation of the formyl peptide receptors. Promotes rearrangement of the actin cytoskeleton, cell polarization and cell migration. Promotes resolution of inflammation and wound healing. Acts via neutrophil N-formyl peptide receptors to enhance the release of CXCL2. {ECO:0000250|UniProtKB:P04083}.
Pan troglodytes (Chimpanzee)
A5A6M3
RBMX_PANTR
MVEADRPGKLFIGGLNTETNEKALEAVFGKYGRIVEVLLMKDRETNKSRGFAFVTFESPADAKDAARDMNGKSLDGKAIKVEQATKPSFESGRRGPPPPPRSRGPPRGLRGGRGGSGGTRGPPSRGGHMDDGGYSMNFNMSSSRGPLPVKRGPPPRSGGPPPKRSAPSGPVRSSSGMGGRAPVSRGRDSYGGPPRREPLPSRRDVYLSPRDDGYSTKDSYSSRDYPSSRDTRDYAPPPRDYTYRDYGHSSSRDDYPSRGYSDRDGYGRDRDYSDHPSGGSYRDSYESYGNSRSAPPTRGPPPSYGGSSRYDDYSSSRDGYGGSRDSYSSSRSDLYSSGRDRVGRQERGLPPSMERGYPPPRDSYSSSSRGAPRGGGRGGSRSDRGGGRSRY
null
null
cellular response to interleukin-1 [GO:0071347]; membrane protein ectodomain proteolysis [GO:0006509]; mRNA processing [GO:0006397]; negative regulation of mRNA splicing, via spliceosome [GO:0048025]; positive regulation of mRNA splicing, via spliceosome [GO:0048026]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein homooligomerization [GO:0051260]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; RNA splicing [GO:0008380]; transcription by RNA polymerase II [GO:0006366]
catalytic step 2 spliceosome [GO:0071013]; euchromatin [GO:0000791]; extracellular exosome [GO:0070062]; nucleus [GO:0005634]; spliceosomal complex [GO:0005681]; supraspliceosomal complex [GO:0044530]
chromatin binding [GO:0003682]; mRNA binding [GO:0003729]; RNA binding [GO:0003723]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
PF08081;PF00076;
3.30.70.330;
null
PTM: O-glycosylated. {ECO:0000250}.; PTM: Arg-185 is dimethylated, probably to asymmetric dimethylarginine. {ECO:0000250}.
SUBCELLULAR LOCATION: Nucleus. Note=Localizes in numerous small granules in the nucleus. Component of ribonucleosomes (By similarity). {ECO:0000250}.
null
null
null
null
null
FUNCTION: RNA-binding protein that plays several role in the regulation of pre- and post-transcriptional processes. Implicated in tissue-specific regulation of gene transcription and alternative splicing of several pre-mRNAs. Binds to and stimulates transcription from the tumor suppressor TXNIP gene promoter; may thus be involved in tumor suppression. When associated with SAFB, binds to and stimulates transcription from the SREBF1 promoter. Associates with nascent mRNAs transcribed by RNA polymerase II. Component of the supraspliceosome complex that regulates pre-mRNA alternative splice site selection. Can either activate or suppress exon inclusion; acts additively with TRA2B to promote exon 7 inclusion of the survival motor neuron SMN2. Represses the splicing of MAPT/Tau exon 10. Binds preferentially to single-stranded 5'-CC[A/C]-rich RNA sequence motifs localized in a single-stranded conformation; probably binds RNA as a homodimer. Binds non-specifically to pre-mRNAs. Also plays a role in the cytoplasmic TNFR1 trafficking pathways; promotes both the IL-1-beta-mediated inducible proteolytic cleavage of TNFR1 ectodomains and the release of TNFR1 exosome-like vesicles to the extracellular compartment (By similarity). {ECO:0000250}.
Pan troglodytes (Chimpanzee)
A5A6N6
EMP2_PANTR
MLVLLAFIIAFHITSAALLFIATIDNAWWVGDEFFADVWRICTNNTNCTVINDSFQEYSTLQAVQATMILSTILCCIAFFIFVLQLFRLKQGERFVLTSIIQLMSCLCVMIAASIYTDRREDIHHKNAKFYPVTREGSYGYSYILAWVAFACTFISGMMYLILRKRK
null
null
actin filament organization [GO:0007015]; actin-mediated cell contraction [GO:0070252]; activation of protein kinase activity [GO:0032147]; apoptotic process [GO:0006915]; bleb assembly [GO:0032060]; blood vessel endothelial cell migration [GO:0043534]; cell adhesion [GO:0007155]; cell migration [GO:0016477]; cell-matrix adhesion [GO:0007160]; early endosome to late endosome transport [GO:0045022]; embryo implantation [GO:0007566]; embryonic process involved in female pregnancy [GO:0060136]; heart formation [GO:0060914]; membrane raft assembly [GO:0001765]; natural killer cell proliferation [GO:0001787]; neutrophil migration [GO:1990266]; plasma membrane raft assembly [GO:0044854]; positive regulation of angiogenesis [GO:0045766]; positive regulation of cardiac epithelial to mesenchymal transition [GO:0062043]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of integrin-mediated signaling pathway [GO:2001046]; protein localization to cell surface [GO:0034394]; protein localization to plasma membrane [GO:0072659]; regulation of angiogenesis [GO:0045765]; regulation of cell-matrix adhesion [GO:0001952]; regulation of endothelial cell migration [GO:0010594]; regulation of glomerular filtration [GO:0003093]; regulation of kinase activity [GO:0043549]; regulation of vasculogenesis [GO:2001212]; T cell mediated cytotoxicity [GO:0001913]
apical part of cell [GO:0045177]; apical plasma membrane [GO:0016324]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; membrane raft [GO:0045121]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]
protein kinase binding [GO:0019901]
PF00822;
1.20.140.150;
PMP-22/EMP/MP20 family
null
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:O88662}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:O88662, ECO:0000250|UniProtKB:P54851}. Apical cell membrane {ECO:0000250|UniProtKB:O88662}. Membrane raft {ECO:0000250|UniProtKB:O88662, ECO:0000250|UniProtKB:P54851}. Cytoplasm {ECO:0000250|UniProtKB:O88662, ECO:0000250|UniProtKB:P54851, ECO:0000250|UniProtKB:Q66HH2}. Nucleus {ECO:0000250|UniProtKB:Q66HH2}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O88662}. Note=Localizes in cytoplasm, foot processes and cell bodies of podocytes and nucleus of endothelial cells of kidney. Localizes to the apical cell surface in the luminal epithelium and glandular epithelium. Colocalized with ITGB1 and GPI-anchor proteins on plasma membrane on plasma membrane. {ECO:0000250|UniProtKB:O88662, ECO:0000250|UniProtKB:Q66HH2}.
null
null
null
null
null
FUNCTION: Functions as a key regulator of cell membrane composition by regulating protein surface expression. Also, plays a role in regulation of processes including cell migration, cell proliferation, cell contraction and cell adhesion. Regulates transepithelial migration of neutrophils into the alveolar lumen, potentially via mediation of cell surface expression of adhesion markers and lipid raft formation (By similarity). Negatively regulates caveolae formation by reducing CAV1 expression and CAV1 amount by increasing lysosomal degradation (By similarity). Facilitates surface trafficking and the formation of lipid rafts bearing GPI-anchor proteins (By similarity). Regulates surface expression of MHC1 and ICAM1 proteins increasing susceptibility to T-cell mediated cytotoxicity (By similarity). Regulates the plasma membrane expression of the integrin heterodimers ITGA6-ITGB1, ITGA5-ITGB3 and ITGA5-ITGB1 resulting in modulation of cell-matrix adhesion (By similarity). Also regulates many processes through PTK2 (By similarity). Regulates blood vessel endothelial cell migration and angiogenesis by regulating VEGF protein expression through PTK2 activation (By similarity). Regulates cell migration and cell contraction through PTK2 and SRC activation. Regulates focal adhesion density, F-actin conformation and cell adhesion capacity through interaction with PTK2 (By similarity). Positively regulates cell proliferation (By similarity). Plays a role during cell death and cell blebbing (By similarity). Promotes angiogenesis and vasculogenesis through induction of VEGFA via a HIF1A-dependent pathway (By similarity). Also plays a role in embryo implantation by regulating surface trafficking of integrin heterodimer ITGA5-ITGB3 (By similarity). Plays a role in placental angiogenesis and uterine natural killer cell regulation at the maternal-fetal placental interface, however not required in the maternal tissues for a viable pregnancy (By similarity). Involved in the early stages of embryogenic development and cardiogenesis, potentially via regulation of epithelial-mesenchymal transition timing (By similarity). May play a role in glomerular filtration (By similarity). {ECO:0000250|UniProtKB:F1QIK8, ECO:0000250|UniProtKB:O88662, ECO:0000250|UniProtKB:P54851}.
Pan troglodytes (Chimpanzee)
A5A6P2
ASAH1_PANTR
MPGRSRVALVLLAAAVSCAVAQHAPPWTEDCRKSTYPPSGPTYRGPVPWYTINLDLPPYKRWHELMLDKAPMLKVIVNSLKNMINTFVPSGKIVQVVDEKLPGLLGNFPGPFEEEMKGIAAVTDIPLGEIISFNIFYELFTICTSIVAEDKKGHLIHGRNMDFGVFLGWNINNDTWVITEQLKPLTVNLDFQRNNKTVFKASSFAGYVGMLTGFKPGLFSLSLNERFSINGGYLGILEWILGKKDAMWIGFLTRTVLENSTSYEEAKNLLTKTKILAPAYFILGGNQSGEGCVITRDRKESLDVYELDAKQGRWYVVQTNYDRWKHPFFLDDRRTPAKMCLNRTSQENISFETMYDVLSTKPVLNKLTVYTTLIDVTKGQFETYLRDCPDPCIGW
3.5.1.-; 3.5.1.23
null
cellular response to tumor necrosis factor [GO:0071356]; ceramide biosynthetic process [GO:0046513]; ceramide catabolic process [GO:0046514]; fatty acid metabolic process [GO:0006631]; keratinocyte differentiation [GO:0030216]; regulation of programmed necrotic cell death [GO:0062098]; regulation of steroid biosynthetic process [GO:0050810]; sphingosine biosynthetic process [GO:0046512]
extracellular space [GO:0005615]; lysosome [GO:0005764]
ceramidase activity [GO:0102121]; fatty acid amide hydrolase activity [GO:0017064]; N-acylsphingosine amidohydrolase activity [GO:0017040]
PF02275;PF15508;
null
Acid ceramidase family
PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q13510}.; PTM: Proteolytically cleaved into two chains alpha and beta that remain associated via a disulfide bond. Cleavage gives rise to a conformation change that activates the enzyme. The same catalytic Cys residue mediates the autoproteolytic cleavage and subsequent hydrolysis of lipid substrates. The beta chain may undergo an additional C-terminal processing. {ECO:0000250|UniProtKB:Q13510}.
SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:Q13510}. Secreted {ECO:0000250|UniProtKB:Q13510}. Note=Secretion is extremely low and localization to lysosomes is mannose-6-phosphate receptor-dependent. {ECO:0000250|UniProtKB:Q13510}.
CATALYTIC ACTIVITY: Reaction=an N-acylsphing-4-enine + H2O = a fatty acid + sphing-4-enine; Xref=Rhea:RHEA:20856, ChEBI:CHEBI:15377, ChEBI:CHEBI:28868, ChEBI:CHEBI:52639, ChEBI:CHEBI:57756; EC=3.5.1.23; Evidence={ECO:0000250|UniProtKB:Q13510}; CATALYTIC ACTIVITY: Reaction=H2O + N-dodecanoylsphing-4-enine = dodecanoate + sphing-4-enine; Xref=Rhea:RHEA:41291, ChEBI:CHEBI:15377, ChEBI:CHEBI:18262, ChEBI:CHEBI:57756, ChEBI:CHEBI:72956; Evidence={ECO:0000250|UniProtKB:Q13510}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41292; Evidence={ECO:0000250|UniProtKB:Q13510}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:41293; Evidence={ECO:0000250|UniProtKB:Q13510}; CATALYTIC ACTIVITY: Reaction=H2O + N-tetradecanoylsphing-4-enine = sphing-4-enine + tetradecanoate; Xref=Rhea:RHEA:41287, ChEBI:CHEBI:15377, ChEBI:CHEBI:30807, ChEBI:CHEBI:57756, ChEBI:CHEBI:72957; Evidence={ECO:0000250|UniProtKB:Q13510}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:41289; Evidence={ECO:0000250|UniProtKB:Q13510}; CATALYTIC ACTIVITY: Reaction=H2O + N-hexadecanoylsphing-4-enine = hexadecanoate + sphing-4-enine; Xref=Rhea:RHEA:38891, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:57756, ChEBI:CHEBI:72959; Evidence={ECO:0000250|UniProtKB:Q13510}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38892; Evidence={ECO:0000250|UniProtKB:Q13510}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:38893; Evidence={ECO:0000250|UniProtKB:Q13510}; CATALYTIC ACTIVITY: Reaction=H2O + N-octadecanoylsphing-4-enine = octadecanoate + sphing-4-enine; Xref=Rhea:RHEA:41279, ChEBI:CHEBI:15377, ChEBI:CHEBI:25629, ChEBI:CHEBI:57756, ChEBI:CHEBI:72961; Evidence={ECO:0000250|UniProtKB:Q13510}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41280; Evidence={ECO:0000250|UniProtKB:Q13510}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:41281; Evidence={ECO:0000250|UniProtKB:Q13510}; CATALYTIC ACTIVITY: Reaction=H2O + N-dodecanoyl-(4R)-hydroxysphinganine = (4R)-hydroxysphinganine + dodecanoate; Xref=Rhea:RHEA:41303, ChEBI:CHEBI:15377, ChEBI:CHEBI:18262, ChEBI:CHEBI:64124, ChEBI:CHEBI:78001; Evidence={ECO:0000250|UniProtKB:Q13510}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:41305; Evidence={ECO:0000250|UniProtKB:Q13510}; CATALYTIC ACTIVITY: Reaction=H2O + N-(dodecanoyl)-sphinganine = dodecanoate + sphinganine; Xref=Rhea:RHEA:45448, ChEBI:CHEBI:15377, ChEBI:CHEBI:18262, ChEBI:CHEBI:57817, ChEBI:CHEBI:85261; Evidence={ECO:0000250|UniProtKB:Q13510}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:45450; Evidence={ECO:0000250|UniProtKB:Q13510}; CATALYTIC ACTIVITY: Reaction=H2O + N-(acetyl)-sphing-4-enine = acetate + sphing-4-enine; Xref=Rhea:RHEA:58484, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089, ChEBI:CHEBI:46979, ChEBI:CHEBI:57756; Evidence={ECO:0000250|UniProtKB:Q13510}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58485; Evidence={ECO:0000250|UniProtKB:Q13510}; CATALYTIC ACTIVITY: Reaction=H2O + N-(hexanoyl)sphing-4-enine = hexanoate + sphing-4-enine; Xref=Rhea:RHEA:41295, ChEBI:CHEBI:15377, ChEBI:CHEBI:17120, ChEBI:CHEBI:57756, ChEBI:CHEBI:63867; Evidence={ECO:0000250|UniProtKB:Q13510}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41296; Evidence={ECO:0000250|UniProtKB:Q13510}; CATALYTIC ACTIVITY: Reaction=H2O + N-octanoylsphing-4-enine = octanoate + sphing-4-enine; Xref=Rhea:RHEA:45092, ChEBI:CHEBI:15377, ChEBI:CHEBI:25646, ChEBI:CHEBI:45815, ChEBI:CHEBI:57756; Evidence={ECO:0000250|UniProtKB:Q13510}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45093; Evidence={ECO:0000250|UniProtKB:Q13510}; CATALYTIC ACTIVITY: Reaction=H2O + N-(9Z-octadecenoyl)-sphing-4-enine = (9Z)-octadecenoate + sphing-4-enine; Xref=Rhea:RHEA:41299, ChEBI:CHEBI:15377, ChEBI:CHEBI:30823, ChEBI:CHEBI:57756, ChEBI:CHEBI:77996; Evidence={ECO:0000250|UniProtKB:Q13510}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41300; Evidence={ECO:0000250|UniProtKB:Q13510}; CATALYTIC ACTIVITY: Reaction=H2O + N-dodecanoylethanolamine = dodecanoate + ethanolamine; Xref=Rhea:RHEA:45456, ChEBI:CHEBI:15377, ChEBI:CHEBI:18262, ChEBI:CHEBI:57603, ChEBI:CHEBI:85263; Evidence={ECO:0000250|UniProtKB:Q13510}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45457; Evidence={ECO:0000250|UniProtKB:Q13510};
null
PATHWAY: Lipid metabolism; sphingolipid metabolism. {ECO:0000250|UniProtKB:Q13510}.
null
null
FUNCTION: Lysosomal ceramidase that hydrolyzes sphingolipid ceramides into sphingosine and free fatty acids at acidic pH (By similarity). Ceramides, sphingosine, and its phosphorylated form sphingosine-1-phosphate are bioactive lipids that mediate cellular signaling pathways regulating several biological processes including cell proliferation, apoptosis and differentiation (By similarity). Has a higher catalytic efficiency towards C12-ceramides versus other ceramides (By similarity). Also catalyzes the reverse reaction allowing the synthesis of ceramides from fatty acids and sphingosine (By similarity). For the reverse synthetic reaction, the natural sphingosine D-erythro isomer is more efficiently utilized as a substrate compared to D-erythro-dihydrosphingosine and D-erythro-phytosphingosine, while the fatty acids with chain lengths of 12 or 14 carbons are the most efficiently used (By similarity). Has also an N-acylethanolamine hydrolase activity (By similarity). By regulating the levels of ceramides, sphingosine and sphingosine-1-phosphate in the epidermis, mediates the calcium-induced differentiation of epidermal keratinocytes (By similarity). Also indirectly regulates tumor necrosis factor/TNF-induced apoptosis (By similarity). By regulating the intracellular balance between ceramides and sphingosine, in adrenocortical cells, probably also acts as a regulator of steroidogenesis (By similarity). {ECO:0000250|UniProtKB:Q13510}.
Pan troglodytes (Chimpanzee)
A5A6P7
GPC3_PANTR
MAGTVRTACLVVAMLLSLDFPGQAQPPPPPPDATCHQVRSFFQRLQPGLKWVPETPVPGSDLQVCLPKGPTCCSRKMEEKYQLTARLNMEQLLQSASKELKFLIIQNAAVFQEAFEIVVRHAKNYTNAMFKNNYPSLTPQAFEFVGEFFTDVSLYILGSDINVDDMVNELFDSLFPVIYTQLMNPGLPDSALDINECLRGARRDLKVFGNFPKLIMTQVSKSLQVTRIFLQALNLGIEVINTTDHLKFSKDCGRMLTRMWYCSYCQGLMMVKPCGGYCNVVMQGCMAGVVEIDKYWREYILSLEELVNGMYRIYDMENVLLGLFSTIHDSIQYVQKNAGKLTTTIGKLCAHSQQRQYRSAYYPEDLFIDKKVLKVARVEHEETLSSRRRELIQKLKSFISFYSALPGYICSHSPVAENDTLCWNGQELVERYSQKAARNGMKNQFNLHELKMKGPEPVVSQIIDKLKHINQLLRTMSVPKGRVLDKNLDEEGFESGDCGDDEDECIGGSGDGMMKVKNQLRFLAELAYDLDVDDAPGSNQQATPKDNEISTFHNLGNVHSPLKLLTSMAISVVCFFFLVH
null
null
cell migration [GO:0016477]; cell migration involved in gastrulation [GO:0042074]; cell proliferation involved in kidney development [GO:0072111]; coronary vasculature development [GO:0060976]; mesonephric duct morphogenesis [GO:0072180]; negative regulation of smoothened signaling pathway [GO:0045879]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of endocytosis [GO:0045807]; positive regulation of protein catabolic process [GO:0045732]; regulation of canonical Wnt signaling pathway [GO:0060828]; regulation of non-canonical Wnt signaling pathway [GO:2000050]; regulation of protein localization to membrane [GO:1905475]
cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; extracellular region [GO:0005576]; lysosomal lumen [GO:0043202]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]
peptidyl-dipeptidase inhibitor activity [GO:0060422]
PF01153;
null
Glypican family
PTM: O-glycosylated; contains heparan sulfate and/or chondroitin sulfate. {ECO:0000250|UniProtKB:P51654}.; PTM: Cleaved intracellularly by a furin-like convertase to generate 2 subunits, alpha and beta, which remain associated through disulfide bonds and are associated with the cell surface via the GPI-anchor. This processing is essential for its role in inhibition of hedgehog signaling. A second proteolytic event may result in cleavage of the protein on the cell surface, separating it from the GPI-anchor and leading to its shedding from the cell surface. {ECO:0000250|UniProtKB:P51654}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P13265}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P13265}; Extracellular side {ECO:0000250|UniProtKB:P13265}.
null
null
null
null
null
FUNCTION: Cell surface proteoglycan (By similarity). Negatively regulates the hedgehog signaling pathway when attached via the GPI-anchor to the cell surface by competing with the hedgehog receptor PTC1 for binding to hedgehog proteins (By similarity). Binding to the hedgehog protein SHH triggers internalization of the complex by endocytosis and its subsequent lysosomal degradation (By similarity). Positively regulates the canonical Wnt signaling pathway by binding to the Wnt receptor Frizzled and stimulating the binding of the Frizzled receptor to Wnt ligands (By similarity). Positively regulates the non-canonical Wnt signaling pathway (By similarity). Binds to CD81 which decreases the availability of free CD81 for binding to the transcriptional repressor HHEX, resulting in nuclear translocation of HHEX and transcriptional repression (By similarity). Inhibits the dipeptidyl peptidase activity of DPP4 (By similarity). Plays a role in limb patterning and skeletal development by controlling the cellular response to BMP4 (By similarity). Modulates the effects of growth factors BMP2, BMP7 and FGF7 on renal branching morphogenesis (By similarity). Required for coronary vascular development (By similarity). Plays a role in regulating cell movements during gastrulation (By similarity). {ECO:0000250|UniProtKB:P51654, ECO:0000250|UniProtKB:Q6V9Y8, ECO:0000250|UniProtKB:Q8CFZ4}.
Pan troglodytes (Chimpanzee)
A5A7I8
CDPK5_SOLTU
MGNACRGSFGGKTFQGYPQPQDHSESNSNPKHNSDSPKPKKEQQPLVTMNRTSTNQSYYVLGHKTPNIRDLYTLGRKLGQGQFGTTYLCTELSSGIDYACKSIAKRKLISKEDVEDVRREIQIMHHLAGHKNIVSIKGAYEDPLYVHIVMELCGGGELFDRIIQRGHYTERKAADLTKIIVGVVEACHSLGVMHRDLKPENFLLVNKDDDFSLKAIDFGLSVFFKPGQIFTDVVGSPYYVAPEVLLKHYGPEADVWTAGVILYILLSGVPPFWAETQQGIFDAVLKGHIDFDSDPWPLLSESAKDLIRKMLCMRPSERLTAHEVLCHPWICENGVAPDRALDPAVLSRLKHFSAMNKLKKMALRVIAESLSEEEIAGLKEMFKAMDTDNSGAITFDELKAGLRKYGSTLKDIEIRELMDAADVDNSGTIDYGEFIAATIHLNKLDREEHLMAAFQYFDKDGSGYITVDELQQACADHNITDVFFEDIIREVDQDNDGRIDYGEFVAMMQKGNPCIGRRTMRNSLNFSMRDAPGAH
2.7.11.1
null
intracellular signal transduction [GO:0035556]; phosphorylation [GO:0016310]
cytoplasm [GO:0005737]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
ATP binding [GO:0005524]; calcium ion binding [GO:0005509]; calcium-dependent protein serine/threonine kinase activity [GO:0009931]; calmodulin binding [GO:0005516]; calmodulin-dependent protein kinase activity [GO:0004683]; protein serine kinase activity [GO:0106310]
PF13499;PF00069;
1.10.238.10;1.10.510.10;
Protein kinase superfamily, Ser/Thr protein kinase family, CDPK subfamily
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:17400895}; Lipid-anchor {ECO:0000305|PubMed:17400895}.
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
null
null
null
null
FUNCTION: Regulates the production of reactive oxygen species (ROS) by NADPH oxidase. {ECO:0000269|PubMed:17400895}.
Solanum tuberosum (Potato)
A5ABG0
PYNA_ASPNC
MDTPLSSSEISPRFSNTVPSSVSSMTPNADPSVIVGLACRVPGATNPSQLWENIVAQKDLQRKMPADRFNVDAFYHPDGTNKGTTNAKFGYFLDQDIGMFDAGFFRISGKEAEAMDPQQRLLLEVVYEALEDAGITLDEVNGSNTAVFCGSFTNDYNAMVTKDLEYYPKYTVTGTGNAILSNRISYFYNLHGPSVTIDTACSSSLNESDIAIVVGSALHFDPNVFITMTDLGMLSSDGRCRTFDSMGSGYVRGEGICAAVLKRRRDAVYNGDNIRAVVRASGVNHDGIKQGITLPNTNAQEKLIRRTYDLAGLDPNDTQYFEAHGTGTARGDPIEARAIGAVFGSTRSEPLYVGSVKSNIGHLEGASGLAGIIKATLALEESQIPPNMHFKRPNPEIKFDEWKIQVPQDIISWPASANGIRRASINSFGYGGTNAHVILDAYKPEDSEAELQAIPAISSSIPVDRPYLIPLSAHSTKAGALWEDKLTKYLSNEPIGRPAVSDLAVSLSTRRTMHGNRSFIIGKDMPTVLQGLEQPPSPAAAWTRPLKETPRLGFVFTGQGAQWFAMGRKLIQQSHLYRQTLERCDAVLQSLPDGPDWTVLEELLRTEEASRLKETRLSQPICTAMQLATVCLLKQWGIEPSAVVGHSSGEVAAAYAAGILTFENAMIAAYYRGLYMSSGVDGSMTTDGAMMAVGLTEAEAKKEFETYTGQICVAAVNSASSLTLSGDKDAIVRLRDSLVERKIFARLLQVAQAFHSHHMLPLAPKYEEALKNCAGFGTSPARVRMFSSVTARLARPGEMGAGYWTANMTGTVRFSDALTGILLNEEDEQNVDILVEIGPHPALKGPSRQVMNALKLNLPYLASLTRGVNDYESLLTLAGQLFQYGFPVDLIAVNSDHFLQRETGMIQSELHGKRLRDLPTYAWDHKRYWSETRPIREHRLRKQRHSILGARMPGIPERTPHWRNYLRLKEIPWLADHVIDGNAVFPAAGYFSMAIEAAVSMCAEDSVIKEIALRDLNVQSALLLSDSEEGTEVIMELRPATQSAKSKSALWYEFTIYSYGESKILNEHCSGLVSVETNALTLPMRWESSKTFDDLAKESQESIPAETLYDHLTALGLQYGPSFQLLTGDVQTGPGFALAGLDFQPSQFSVQAADLTIAHPTLLDASFHAIFPAIESALGRSLDEPLVPTFVRSFKVSGDFLACCRESREQKFQVTCFTRLPGPRVALSDLTVCSKESNKPLLQFNGLEVTALGSDKTDNSAGRSLFFRTRWQPAFTFLGPDHPAVAQKNISEILDIFAHQFPDTRILHVSDTVDGTRDVLKYLGGRSNERRRFHSITPVFQTQIALEEIDALSQEWPGLVEISEPEPNAYGLVVLSSDAADLDSRQFVKEGGFVLALGPHPQPEGLHDVFFTKDLAVWQKSTDNAQKPKQLSLILPSCPSQRTLDIADGMEMQHGSSVFVTRTSLAALSNEALQAEDIVVLANLDEDVLFEHSSSDQSTFLGIKRLLTAGGKNIVWVLEGGSMDAPKPEHAMIIGLARVARSENDQLRFVTLDLPRASTQETVVRHVWRLLDRSITEDEVAVRDNCIFIPRVEADDQLNSKLRNGTNSQPREEPLGAGRPLALKIGRVGLLETLVFEDDEQILDTQLADDEIEIEVKASAINFRDIAASMGIIDDYKLGDECAGIVTRIGAQVNPQDFQVGDRVAAWRPGQGAHKTIVRNPASLSYKLGDMSFVDAASLPCILTTAYYSLVHVAHLQPGETVLIHSAAGGVGQMAIQVAQYVGARVIATVGSQAKRSLLKSRYGLADDMIFNSRDDSFVRDVLDTTGGRGVDVILNSLAGKLLHATWSCVAPFGRFIEIGKRDIHENSKIDMDPFRRNVAFASVDLVTIFEKNKPLGARLLKECGTLVHKGHITPPETVTELPYSDAVKAFRLLQMGKHTGKVVLVPHAGDRVPVLPSTYRNQPLFKHEKTYLLVGGLGGLGRTLAEWMVRKNARRLAFLSRSGADKEEAKRTVEWLRERGVSVTVFKGDVSRYEDVERAVKAIDNLGGIFQAAMVLQDAPLENMSYQQWQICVEPKVKGTYNLHQATLGKQLDFFICFSSASGSIGSKGQANYSSANCYLDALMRHRREMGLAGTTMNCGMIVGIGAVAANQALLKVMMRSGYDGVNKEELLYQIEEAVLSDNNKKVSRRGVDLHQTITGINMTKADFYWCQKPLYRNLYNNHEFLGQTAIKQGTKSLASQLQGTKSVEERTTLVLSAFIEKVADVLSVSVDSIESANPLSAYGLDSIIAVEFRKWFSRSVGVEIALFDVLGAPSIFALVTKASGLITITTSNDDKAENVDNEGAKGNEDQEVETQQGQLNQPIPPAAAVGPVPMSSFQQRLWFIHNFGDDKTFLNLSITSYLEGNPDATILEKALNELVNRNAILRTGYTEGDEFAEQTVLDMPSISLERIDVSSKPSPTVSLQDVIQRRRAIELEIEEGEVVRPMLVRLSDDQHALVLICHHIAIDRGSAKSSLNQLTGIYDAIRQGRDLDMVPRPGVSYADFAVWHNRLLSSPSLQADLTFWKENLSGMPKTCKLLPFAKSERPLHDDLQRTVVSGILKKSLLNRMKRICSQSGATPFQFLLAAFRAFIFRYTEDSDLGILMIDGDRPHPDLEDVLGFFVNMTPIRCQDSCEGAFDQLLEATKTRTLEAMSHSKAPFDSIVDVVKAKKTTSHFPLAQIALNYQIHGTFPVYRTQDFNVHDVQSVDVPTACDMQLEALEHPERGLDLRLEYSSTLYGSGDMNRFFDNFVTFMSSLIRDHRQPIAEVNLCGALEIAHLEKNFWNTQFTQNPWGSVGVCQRIMENAAKQPEAVAIAASDGAAITYSELVERAQRVAASLKASGVTERQKICVLVDPGVDAVIALLAVLLTRSCYVALDSSFAVDRLAFMASDCGAGVLLFGPELQGLAETVASKSKSGLRLLDTKKAALCEDRFVGDLPSVNEDPFFIIYTSGSTGKPKGVVLSHANTQQMLASVGEYFRFTSDDRFLQQSSLCFDLSVVQIFSALTAGARVCVAKHDIRKDPAALAAFMHETGVTITYFTPTHFALLLEHSWETLHQCSQYRAALFAGERLPVRIARAFYDLQTPAVVYNTWSPSELVVQTTIHKVDKPDDDVFDIPIGRPLPNCRHYVVDAVLNPLPAGFVGEICVGGAQVGLEYLNRPLANATSFVRDLNSTPEDQARGWKKMFRTGDKGSFLPNGLLTFKGRIAGDKQIKLRGFRIDLGEVEQVLYKNASTPDGQGIVDISVIARDSEKSDATSPLTDERRLIAFVIPKKPLQSTQERDEYANYLHRMAQGSLNEYMCPNGYQFLERLPMTIGGKVDRRSLLTMKLDLAQHTTTCTDSRPVTEVAGDDAEILQGVTGQVCSLLGIDRSIAPNDNFFELGGQSILLLRLQSRLKKKFKVTLKLQELIHAPTPLAIAGMIQKQLKGPAGVQNENASKSIDWSEEISLPASLMNTDYSQLSRFPRTDVSSILLTGIDTFIGLHMLATILSNNHNATVYVIGIHDELTADHLVEGLTKYKLLDAHLSTEDVLSRTCAVPGKMTSPRFGLAEEAFRNLADKVRVIFNIAADVSLLKTYVDLKTVNTSAILTLIELATSSHGHLLEIHHLSTWSVPHLQTWKKTSRTRAFASNREEDPSHFTPPTADEYGYFKSRWAAEMYLTQAAARGVPVSIYRASSVSGSRATNVPVPEMDFISNMIMHMIQHRAIPEINSSSLIDEAGDFVVDFLPVDALTSSMYTLASEESAAAPGLQVYHLGSSQPLPLQALVDVIPSLDQSGAAGKCRVVPMQEWLRLVSEGASEEEQLHWMVVKKYFQHGHSMFALDKSHTVAALKKAGKEVEFPAIDVDYLKRLLDERGPGLKR
2.3.1.-; 6.3.2.-
null
fatty acid biosynthetic process [GO:0006633]; heterocycle biosynthetic process [GO:0018130]; organic cyclic compound biosynthetic process [GO:1901362]; organonitrogen compound biosynthetic process [GO:1901566]; secondary metabolic process [GO:0019748]; secondary metabolite biosynthetic process [GO:0044550]
null
fatty acid synthase activity [GO:0004312]; ligase activity [GO:0016874]; oxidoreductase activity [GO:0016491]; phosphopantetheine binding [GO:0031177]
PF00698;PF13602;PF00501;PF00668;PF16197;PF00109;PF02801;PF08659;PF07993;PF21089;PF00550;PF14765;
3.30.300.30;3.30.70.3290;3.40.47.10;1.10.1200.10;3.30.559.10;3.40.366.10;3.90.180.10;3.40.50.12780;3.40.50.720;3.30.559.30;3.10.129.110;
NRP synthetase family
null
null
null
null
PATHWAY: Secondary metabolite biosynthesis. {ECO:0000269|PubMed:24106156, ECO:0000269|PubMed:26414728}.
null
null
FUNCTION: Hybrid PKS-NRPS synthetase; part of the gene cluster that mediates the biosynthesis of pyranonigrins, a family of antioxidative compounds (PubMed:24106156, PubMed:26414728). The first step of pyranonigrins biosynthesis is performed by the hybrid PKS-NRPS synthetase that condenses 6 malonyl-CoA units to an acetyl starter unit, to form a 1,3,5-trioxotetradecane-6,8-dienyl-ACP (PubMed:24106156). The enoyl reductase (ER) domain of pynA is likely to be functional during the first two rounds of polyketide chain extension, to generate the saturated C-C bonds of the alkyl side chain (Probable). PynA subsequently forms the amide bond between the acyl chain and L-serine (PubMed:24106156, PubMed:26414728). Although pynA has a terminal reductase domain, it appears to require the thioesterase pynI for the release of the straight-chain intermediate from pynA via the formation of a tetramic acid pyranonigrin J (PubMed:26414728). The methyltransferase pynC then coverts pyranonigrin J to pyranonigrin I via N-methylation (PubMed:26414728). The FAD-dependent monooxygenase pynG catalyzes an epoxidation-mediated cyclization to form the dihydro-gamma-pyrone moiety, followed by pynD-catalyzed oxidation of the alcohol to the ketone and enolization to yield the characteristic tetramic acid-fused gamma-pyrone core of pyranonigrin H (PubMed:26414728). Pyranonigrin H is substrate of pynH for dehydration-mediated exo-methylene formation from the serine side chain to produce pyranonigrin E, before the oxidase pynE reduces the exo-methylene of pyranonigrin E into a pendant methyl to form pyranonigrin G (PubMed:26414728). The FAD-linked oxidoreductase pynB performs the reverse reaction and converts pyranonigrin G back to pyranonigrin E (PubMed:26414728). {ECO:0000269|PubMed:24106156, ECO:0000269|PubMed:26414728, ECO:0000305|PubMed:24106156}.
Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
A5CAL1
2KGR_VITVI
MESIGVLLTCPMNPYLEQELDKRFKLFRFWDFPSANDLFREHSNSIRAVVGNSFIGADAQMIEALPKMEIVSSFSVGLDKIDLVRCKEKGIRVTNTPDVLTEDVADLALALILATLRRICESDRYVRSGSWKKGDFKLTTKFTGKSVGIIGLGRIGSAIAKRAEGFSCPISYHSRTEKPGTNYKYYPSVVELASNCQILVVACALTPETRHIINREVINALGPKGVVINIGRGLHVDEPELVSALVEGRLGGAGLDVFENEPNVPEELLAMDNVVLLPHVGSGTVETRKDMADLVLGNLEAHFLNKPLLTPVV
1.1.1.-; 1.1.1.26; 1.1.1.28; 1.1.1.79
null
null
cytosol [GO:0005829]
D-lactate dehydrogenase activity [GO:0008720]; glyoxylate reductase (NAD+) activity [GO:0047964]; glyoxylate reductase (NADP+) activity [GO:0030267]; hydroxypyruvate reductase activity [GO:0016618]; NAD binding [GO:0051287]
PF00389;PF02826;
3.40.50.720;
D-isomer specific 2-hydroxyacid dehydrogenase family
null
null
CATALYTIC ACTIVITY: Reaction=L-idonate + NADP(+) = 2-dehydro-L-idonate + H(+) + NADPH; Xref=Rhea:RHEA:29839, ChEBI:CHEBI:15378, ChEBI:CHEBI:17796, ChEBI:CHEBI:36602, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; Evidence={ECO:0000269|PubMed:31488549}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29840; Evidence={ECO:0000269|PubMed:31488549}; CATALYTIC ACTIVITY: Reaction=L-idonate + NAD(+) = 2-dehydro-L-idonate + H(+) + NADH; Xref=Rhea:RHEA:27818, ChEBI:CHEBI:15378, ChEBI:CHEBI:17796, ChEBI:CHEBI:36602, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; Evidence={ECO:0000269|PubMed:31488549}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27819; Evidence={ECO:0000269|PubMed:31488549}; CATALYTIC ACTIVITY: Reaction=(R)-glycerate + NADP(+) = 3-hydroxypyruvate + H(+) + NADPH; Xref=Rhea:RHEA:18657, ChEBI:CHEBI:15378, ChEBI:CHEBI:16659, ChEBI:CHEBI:17180, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; Evidence={ECO:0000269|PubMed:31488549}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18659; Evidence={ECO:0000269|PubMed:31488549}; CATALYTIC ACTIVITY: Reaction=glycolate + NADP(+) = glyoxylate + H(+) + NADPH; Xref=Rhea:RHEA:10992, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:36655, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.79; Evidence={ECO:0000269|PubMed:31488549}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:10994; Evidence={ECO:0000269|PubMed:31488549}; CATALYTIC ACTIVITY: Reaction=glycolate + NAD(+) = glyoxylate + H(+) + NADH; Xref=Rhea:RHEA:18229, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:36655, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.26; Evidence={ECO:0000269|PubMed:31488549}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18231; Evidence={ECO:0000269|PubMed:31488549}; CATALYTIC ACTIVITY: Reaction=(R)-lactate + NADP(+) = H(+) + NADPH + pyruvate; Xref=Rhea:RHEA:62968, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16004, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; Evidence={ECO:0000269|PubMed:31488549}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:62970; Evidence={ECO:0000269|PubMed:31488549}; CATALYTIC ACTIVITY: Reaction=(R)-lactate + NAD(+) = H(+) + NADH + pyruvate; Xref=Rhea:RHEA:16369, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16004, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.28; Evidence={ECO:0000269|PubMed:31488549}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:16371; Evidence={ECO:0000269|PubMed:31488549};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.7 mM for 2-keto-L-gulonate (in presence of NADPH) {ECO:0000269|PubMed:31488549}; KM=1.56 mM for 2-keto-L-gulonate (in presence of NADH) {ECO:0000269|PubMed:31488549}; KM=0.096 mM for hydroxypyruvate (in presence of NADPH) {ECO:0000269|PubMed:31488549}; KM=0.044 mM for glyoxylate (in presence of NADPH) {ECO:0000269|PubMed:31488549}; KM=0.248 mM for glyoxylate (in presence of NADH) {ECO:0000269|PubMed:31488549}; KM=1.37 mM for pyruvate (in presence of NADPH) {ECO:0000269|PubMed:31488549}; KM=3.45 mM for pyruvate (in presence of NADH) {ECO:0000269|PubMed:31488549}; Vmax=7.54 umol/min/mg enzyme with 2-keto-L-gulonate as substrate (in presence of NADPH) {ECO:0000269|PubMed:31488549}; Vmax=17.19 umol/min/mg enzyme with 2-keto-L-gulonate as substrate (in presence of NADH) {ECO:0000269|PubMed:31488549}; Vmax=6.29 umol/min/mg enzyme with hydroxypyruvate as substrate (in presence of NADPH) {ECO:0000269|PubMed:31488549}; Vmax=13.82 umol/min/mg enzyme with glyoxylate as substrate (in presence of NADPH) {ECO:0000269|PubMed:31488549}; Vmax=69.38 umol/min/mg enzyme with glyoxylate as substrate (in presence of NADH) {ECO:0000269|PubMed:31488549}; Vmax=0.55 umol/min/mg enzyme with pyruvate as substrate (in presence of NADPH) {ECO:0000269|PubMed:31488549}; Vmax=0.44 umol/min/mg enzyme with pyruvate as substrate (in presence of NADH) {ECO:0000269|PubMed:31488549};
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:31488549};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. {ECO:0000269|PubMed:31488549};
FUNCTION: Involved in the biosynthesis of L-tartarate from L-ascorbate (PubMed:31488549). Catalyzes the NAD(P)H-dependent reduction of 2-dehydro-L-idonate (2-keto-L-gulonate) to L-idonate (PubMed:31488549). Can also reduce hydroxypyruvate to glycerate, glyoxylate to glycolate and pyruvate to D-lactate (PubMed:31488549). Prefers NADPH to NADH as proton donor (PubMed:31488549). {ECO:0000269|PubMed:31488549}.
Vitis vinifera (Grape)
A5D7B7
SEPR_BOVIN
MKTWLKIVFGVATSAVLALLVMCIVLRPSRVHNSEESTTRALTLKDILNGTFSYKTFFPNWISGQEYLHQSTDNNVVFYNIETGESYTILSNTTMKSVNASNYGLSPDRQFAYLESDYSKLWRYSYTATYHIYDLTNGEFIRRNELPRPIQYLCWSPVGSKLAYVYQNNIYLKQRPEDPPFQITYNGKENKIFNGIPDWVYEEEMLATKYALWWSPNGKFLAYAEFNDTEIPVIAYSYYGDEQYPRTINIPYPKAGAKNPVVRIFIIDATYPEHIGPREVPVPAMIASSDYYFSWLTWVTDDRICLQWLKRIQNVSVLSTCDFREDWQTWNCPKTQEHIEESRTGWAGGFFVSTPVFSHDTISYYKIFSDKDGYKHIHYIRDTVENAIQITSGKWEAINIFRVTQDSLFYSSNEFEGYPGRRNIYRISIGSHSPSKKCITCHLRKKRCQYYTASFSDYAKYYALVCYGPGLPISTLHDGRTDQEIKILEDNKELENALKNIQLPKEEIKKLKVDDITLWYKMILPPQFDKSKKYPLLIQVYGGPCSQSVRSIFAVSWISYLASKEGIVIALVDGRGTAFQGDKLLYAVYRKLGVYEVEDQITAVRKFIEMGFIDEKRIAIWGWSYGGYVSSLALASGTGLFKCGIAVAPVSSWEYYASIYTERFMGLPTKDDNLKHYKNSTVMARAEYFRNVDYLLIHGTADDNVHFQNSAQIAKALVNAQVDFQAMWYSDQNHGLSGLSTKHLYTHMTHFLKQCFSLSD
3.4.14.5; 3.4.21.-; 3.4.21.26
null
angiogenesis [GO:0001525]; apoptotic process [GO:0006915]; cell adhesion [GO:0007155]; proteolysis [GO:0006508]
anchoring junction [GO:0070161]; cell surface [GO:0009986]; extracellular region [GO:0005576]; lamellipodium membrane [GO:0031258]; plasma membrane [GO:0005886]; ruffle membrane [GO:0032587]
dipeptidyl-peptidase activity [GO:0008239]; serine-type endopeptidase activity [GO:0004252]
PF00930;PF00326;
3.40.50.1820;2.140.10.30;
Peptidase S9B family
PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q12884}.; PTM: The N-terminus may be blocked. {ECO:0000250|UniProtKB:Q12884}.
SUBCELLULAR LOCATION: [Prolyl endopeptidase FAP]: Cell surface {ECO:0000250|UniProtKB:Q12884}. Cell membrane {ECO:0000250|UniProtKB:Q12884}; Single-pass type II membrane protein {ECO:0000255}. Cell projection, lamellipodium membrane {ECO:0000250|UniProtKB:Q12884}; Single-pass type II membrane protein {ECO:0000255}. Cell projection, invadopodium membrane {ECO:0000250|UniProtKB:Q12884}; Single-pass type II membrane protein {ECO:0000255}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:Q12884}; Single-pass type II membrane protein {ECO:0000255}. Membrane {ECO:0000250|UniProtKB:Q12884}; Single-pass type II membrane protein {ECO:0000255}. Note=Localized on cell surface with lamellipodia and invadopodia membranes and on shed vesicles. Colocalized with DPP4 at invadopodia and lamellipodia membranes of migratory activated endothelial cells in collagenous matrix. Colocalized with DPP4 on endothelial cells of capillary-like microvessels but not large vessels within invasive breast ductal carcinoma. Anchored and enriched preferentially by integrin alpha-3/beta-1 at invadopodia, plasma membrane protrusions that correspond to sites of cell invasion, in a collagen-dependent manner. Localized at plasma and ruffle membranes in a collagen-independent manner. Colocalized with PLAUR preferentially at the cell surface of invadopodia membranes in a cytoskeleton-, integrin- and vitronectin-dependent manner. Concentrated at invadopodia membranes, specialized protrusions of the ventral plasma membrane in a fibrobectin-dependent manner. Colocalizes with extracellular components (ECM), such as collagen fibers and fibronectin. {ECO:0000250|UniProtKB:Q12884}.; SUBCELLULAR LOCATION: [Antiplasmin-cleaving enzyme FAP, soluble form]: Secreted {ECO:0000250|UniProtKB:Q12884}. Note=Found in blood plasma and serum. {ECO:0000250|UniProtKB:Q12884}.
CATALYTIC ACTIVITY: Reaction=Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline.; EC=3.4.14.5; Evidence={ECO:0000250|UniProtKB:Q12884, ECO:0000255|PROSITE-ProRule:PRU10084}; CATALYTIC ACTIVITY: Reaction=Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides.; EC=3.4.21.26; Evidence={ECO:0000269|PubMed:15313476};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.27 mM for Gly-Pro (Prolyl endopeptidase activity) {ECO:0000269|PubMed:15313476}; KM=0.206 mM for Gly-Pro-Phe-His (Prolyl endopeptidase activity) {ECO:0000269|PubMed:15313476};
null
null
null
FUNCTION: Cell surface glycoprotein serine protease that participates in extracellular matrix degradation and involved in many cellular processes including tissue remodeling, fibrosis, wound healing, inflammation and tumor growth. Both plasma membrane and soluble forms exhibit post-proline cleaving endopeptidase activity, with a marked preference for Ala/Ser-Gly-Pro-Ser/Asn/Ala consensus sequences, on substrate such as alpha-2-antiplasmin SERPINF2 and SPRY2. Degrade also gelatin, heat-denatured type I collagen, but not native collagen type I and IV, vibronectin, tenascin, laminin, fibronectin, fibrin or casein. Also has dipeptidyl peptidase activity, exhibiting the ability to hydrolyze the prolyl bond two residues from the N-terminus of synthetic dipeptide substrates provided that the penultimate residue is proline, with a preference for Ala-Pro, Ile-Pro, Gly-Pro, Arg-Pro and Pro-Pro. Natural neuropeptide hormones for dipeptidyl peptidase are the neuropeptide Y (NPY), peptide YY (PYY), substance P (TAC1) and brain natriuretic peptide 32 (NPPB). The plasma membrane form, in association with either DPP4, PLAUR or integrins, is involved in the pericellular proteolysis of the extracellular matrix (ECM), and hence promotes cell adhesion, migration and invasion through the ECM. Plays a role in tissue remodeling during development and wound healing. Participates in the cell invasiveness towards the ECM in malignant melanoma cancers. Enhances tumor growth progression by increasing angiogenesis, collagen fiber degradation and apoptosis and by reducing antitumor response of the immune system. Promotes glioma cell invasion through the brain parenchyma by degrading the proteoglycan brevican. Acts as a tumor suppressor in melanocytic cells through regulation of cell proliferation and survival in a serine protease activity-independent manner. {ECO:0000250|UniProtKB:Q12884, ECO:0000269|PubMed:15313476}.
Bos taurus (Bovine)
A5D7D1
ACTN4_BOVIN
MVDYHAANQSYQYGPSSGSNGAGGGGTMGDYMAQEDDWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIDEDFRDGLKLMLLLEVISGERLPKPERGKMRVHKINNVNKALDFIASKGVKLVSIGAEEIVDGNAKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVAEKYLDIPKMLDAEDIVNTARPDEKAIMTYVSSFYHAFSGAQKAETAANRICKVLAVNQENEHLMEDYERLASDLLEWIRRTIPWLEDRVPQKTIQEMQQKLEDFRDYRRVHKPPKVQEKCQLEINFNTLQTKLRLSNRPAFMPSEGKMVSDINNGWQHLEQAEKGYEEWLLNEIRRLERLDHLAEKFRQKASIHEAWTDGKEAMLKHRDYETATLSDIKALIRKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSHNVNTRCQKICDQWDALGSLTHSRREALEKTEKQLETIDQLHLEYAKRAAPFNNWMESAMEDLQDMFIVHTIEEIEGLISAHDQFKSTLPDADREREAILAIHKEAQRIAESNHIKLSGSNPYTTVTPQIINSKWEKVQQLVPKRDHALLEEQSKQQSNEHLRRQFASQANIVGPWIQTKMEEIGRISIEMNGTLEDQLSHLKQYERSIVDYKPNLDLLEQQHQLIQEALIFDNKHTNYTMEHIRVGWEQLLTTIARTINEVENQILTRDAKGISQEQMQEFRASFNHFDKDHGGALGPEEFKACLISLGYDVENDRQGDAEFNRIMSVVDPNHSGLVTFQAFIDFMSRETTDTDTADQVIASFKVLAGDKNFITAEELRRELPPDQAEYCIARMAPYQGPDAVPGALDYKSFSTALYGESDL
null
null
actin cytoskeleton organization [GO:0030036]; muscle cell development [GO:0055001]; peroxisome proliferator activated receptor signaling pathway [GO:0035357]; protein transport [GO:0015031]; retinoic acid receptor signaling pathway [GO:0048384]
anchoring junction [GO:0070161]; cell junction [GO:0030054]; cell projection [GO:0042995]; cortical actin cytoskeleton [GO:0030864]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; ribonucleoprotein complex [GO:1990904]; stress fiber [GO:0001725]; Z disc [GO:0030018]
actin filament binding [GO:0051015]; calcium ion binding [GO:0005509]; nuclear receptor coactivator activity [GO:0030374]
PF00307;PF08726;PF00435;
1.20.58.60;1.10.418.10;1.10.238.10;
Alpha-actinin family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O43707}. Cytoplasm {ECO:0000250|UniProtKB:O43707}. Cell junction {ECO:0000250|UniProtKB:P57780}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000250|UniProtKB:O43707}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P57780}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Expressed in the perinuclear rim and manchette structure in early elongating spermatids during spermiogenesis (By similarity). {ECO:0000250|UniProtKB:O43707, ECO:0000250|UniProtKB:P57780}.
null
null
null
null
null
FUNCTION: F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein. Probably involved in vesicular trafficking via its association with the CART complex. The CART complex is necessary for efficient transferrin receptor recycling but not for EGFR degradation. Involved in tight junction assembly in epithelial cells probably through interaction with MICALL2. Links MICALL2 to the actin cytoskeleton and recruits it to the tight junctions. May also function as a transcriptional coactivator, stimulating transcription mediated by the nuclear hormone receptors PPARG and RARA. {ECO:0000250|UniProtKB:O43707}.
Bos taurus (Bovine)
A5D7F8
SH3R1_BOVIN
MDESALLDLLECPVCLERLDASAKVLPCQHTFCKRCLLGIVGSRNELRCPECRTLVGSGVEQLPSNILLVRLLDGIKQRPWKPGPVGGSGTNGTSALRAQSSAVVTCSPKDGPSSQGGPQPRAQAWSPPVRGIPQLPCAKALYNYEGKEPGDLKFSKGDIIVLRRQVDENWYHGEVGGVHGFFPTNFVQIIKPLPQPPPQCKALYDFEVKDKEADKDCLPFAKDDVLTVIRRVDENWAEGMLADKIGIFPISYVEFNSAAKQLIEWDQPPGPGVAAGEGALATTPSSTTTKQPDGKKNTKKRHSFTSLSMASKASQAAQQRHSMEISPPVLISSSNPAAAARIGELAGLSCSAPSQVHISTTGLIVTPPPSSPVTTGPSFTFPAEAPYPAALATLNPPLPPPPLQAATPTGTAVAAAAGMGPRPTAGPTDQTTHPRPQPRPSVYVAIYPYTPRKEDELELRKGEMFLVFERCQDGWFKGTSMHTSKIGVFPGNYVAPVTRAVTSASQGKVPMLTTGPASRGGVLANPPSTGGPAQKPPGNGVAGGPGVPTAVVSAAHVQTSPQAKVLLHASGQMTVNQARSAARTVSAHSQERPTAAVTPIQVQSTPGQSHHPLVSPQPPAPLGPPAHAAASGLGRVGGPLACATAPASIPAASLEPEPSSRPATLLPGTPTSPDSGSAARPDKDGKKEKKGLLKLLSGASTKRKPRGSPPASPTLDAELGAELSCGPPGPPCACPGPCDGDTMAPGPQRRASSLDSAPVAPPPRQPCSSLGPAASEVRPAVCERHRVVVSYPPQSEAELELKEGDIVFVHKKREDGWFKGTLQRNGKTGLFPGSFVENI
2.3.2.27
null
negative regulation of apoptotic process [GO:0043066]; neuron migration [GO:0001764]; positive regulation of JNK cascade [GO:0046330]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; protein autoubiquitination [GO:0051865]; protein ubiquitination [GO:0016567]; regulation of CD4-positive, alpha-beta T cell differentiation [GO:0043370]; regulation of CD8-positive, alpha-beta T cell proliferation [GO:2000564]
cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; lamellipodium [GO:0030027]; perinuclear region of cytoplasm [GO:0048471]
MAP-kinase scaffold activity [GO:0005078]; metal ion binding [GO:0046872]; ubiquitin protein ligase activity [GO:0061630]
PF00018;PF07653;PF14604;PF13923;
2.30.30.40;3.30.40.10;
SH3RF family
PTM: Phosphorylated at Ser-304 by AKT1 and AKT2. When phosphorylated, it has reduced ability to bind Rac. {ECO:0000250|UniProtKB:Q7Z6J0}.; PTM: Autoubiquitinated. Ubiquitinated by SH3RF2, leading to proteasome-mediated degradation. {ECO:0000250|UniProtKB:Q71F54}.
SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q71F54}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q69ZI1}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q69ZI1}. Note=Colocalizes, with AKT2, in lamellipodia. Colocalizes, with HERP1, in trans-Golgi network. {ECO:0000250|UniProtKB:Q69ZI1, ECO:0000250|UniProtKB:Q7Z6J0}.
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:Q7Z6J0};
null
PATHWAY: Protein modification; protein ubiquitination.
null
null
FUNCTION: Has E3 ubiquitin-protein ligase activity. In the absence of an external substrate, it can catalyze self-ubiquitination. Stimulates ubiquitination of potassium channel KCNJ1, enhancing it's dynamin-dependent and clathrin-independent endocytosis. Acts as a scaffold protein that coordinates with MAPK8IP1/JIP1 in organizing different components of the JNK pathway, including RAC1 or RAC2, MAP3K11/MLK3 or MAP3K7/TAK1, MAP2K7/MKK7, MAPK8/JNK1 and/or MAPK9/JNK2 into a functional multiprotein complex to ensure the effective activation of the JNK signaling pathway. Regulates the differentiation of CD4(+) and CD8(+) T-cells and promotes T-helper 1 (Th1) cell differentiation. Regulates the activation of MAPK8/JNK1 and MAPK9/JNK2 in CD4(+) T-cells and the activation of MAPK8/JNK1 in CD8(+) T-cells. Plays a crucial role in the migration of neocortical neurons in the developing brain. Controls proper cortical neuronal migration and the formation of proximal cytoplasmic dilation in the leading process (PCDLP) in migratory neocortical neurons by regulating the proper localization of activated RAC1 and F-actin assembly. {ECO:0000250|UniProtKB:Q69ZI1, ECO:0000250|UniProtKB:Q7Z6J0}.
Bos taurus (Bovine)
A5D7L5
S39AE_BOVIN
MELLRPALPSYFLLTLLSIWTAASEARAVSTGMPTISAASFLQNLMHRYGEGDSLTLQQLKALLNHLDVGVGRGNISQPVQGPRNLSTCFSSGELFAAHNLSHQSQIGEREFQEFCPTILQQLDSRACSSENQENEENEQTEEGRPSSVEVWGYGLLCVTVISLCSLLGASVVPFMKKTFYKRLLLYFIALAIGTLYSNALFQLIPEAFGFNPMEDYYVSKSAVVFGGFYLFFFTEKILKMLLKQKNEHHHGHSHYTSETLPSQKDQEEGVTEKLQNGDLDHMIPQHCSGELDGKTPVVDEKVIVGSLSVQDLQASQSACHWLKGVRYSDIGTLAWMITLSDGLHNFIDGLAIGASFTVSVFQGISTSVAILCEEFPHELGDFVILLNAGMSLQQALFFNFLSACCCYVGLGFGILAGSHFSANWIFALAGGMFLYISLADMFPEMNEVSQEDERKGSALIPFVIQNLGLLTGFGIMLVLTMYSGHIQIG
null
null
cellular response to glucose stimulus [GO:0071333]; cellular response to insulin stimulus [GO:0032869]; import across plasma membrane [GO:0098739]; inorganic cation transmembrane transport [GO:0098662]; intracellular zinc ion homeostasis [GO:0006882]; iron import into cell [GO:0033212]; iron ion transmembrane transport [GO:0034755]; manganese ion homeostasis [GO:0055071]; manganese ion transmembrane transport [GO:0071421]; negative regulation of cyclic-nucleotide phosphodiesterase activity [GO:0051344]; positive regulation of G protein-coupled receptor signaling pathway [GO:0045745]; zinc ion import across plasma membrane [GO:0071578]; zinc ion transmembrane transport [GO:0071577]
apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; early endosome membrane [GO:0031901]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; plasma membrane [GO:0005886]
cadmium ion transmembrane transporter activity [GO:0015086]; iron ion transmembrane transporter activity [GO:0005381]; manganese ion transmembrane transporter activity [GO:0005384]; monoatomic anion:monoatomic cation symporter activity [GO:0015296]; monoatomic cation:bicarbonate symporter activity [GO:0140410]; zinc ion transmembrane transporter activity [GO:0005385]
PF02535;
null
ZIP transporter (TC 2.A.5) family
PTM: Ubiquitinated. Ubiquitination occurs upon iron depletion. The ubiquitinated form undergoes proteasomal degradation. {ECO:0000250|UniProtKB:Q15043}.; PTM: N-glycosylated. N-glycosylation at Asn-100 is required for iron-regulated extraction of the transporter from membranes and subsequent proteasomal degradation. {ECO:0000250|UniProtKB:Q15043}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q15043}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:Q15043}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q15043}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000250|UniProtKB:Q15043}; Multi-pass membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000250|UniProtKB:Q15043}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:Q15043}; Multi-pass membrane protein {ECO:0000255}.
CATALYTIC ACTIVITY: Reaction=2 hydrogencarbonate(out) + Zn(2+)(out) = 2 hydrogencarbonate(in) + Zn(2+)(in); Xref=Rhea:RHEA:62252, ChEBI:CHEBI:17544, ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q75N73}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62253; Evidence={ECO:0000250|UniProtKB:Q75N73}; CATALYTIC ACTIVITY: Reaction=2 hydrogencarbonate(out) + Mn(2+)(out) = 2 hydrogencarbonate(in) + Mn(2+)(in); Xref=Rhea:RHEA:62260, ChEBI:CHEBI:17544, ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q75N73}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62261; Evidence={ECO:0000250|UniProtKB:Q75N73}; CATALYTIC ACTIVITY: Reaction=Fe(2+)(out) + 2 hydrogencarbonate(out) = Fe(2+)(in) + 2 hydrogencarbonate(in); Xref=Rhea:RHEA:62368, ChEBI:CHEBI:17544, ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:Q75N73}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62369; Evidence={ECO:0000250|UniProtKB:Q75N73}; CATALYTIC ACTIVITY: Reaction=Cd(2+)(out) + 2 hydrogencarbonate(out) = Cd(2+)(in) + 2 hydrogencarbonate(in); Xref=Rhea:RHEA:62256, ChEBI:CHEBI:17544, ChEBI:CHEBI:48775; Evidence={ECO:0000250|UniProtKB:Q75N73}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62257; Evidence={ECO:0000250|UniProtKB:Q75N73};
null
null
null
null
FUNCTION: Electroneutral transporter of the plasma membrane mediating the cellular uptake of the divalent metal cations zinc, manganese and iron that are important for tissue homeostasis, metabolism, development and immunity (By similarity). Functions as an energy-dependent symporter, transporting through the membranes an electroneutral complex composed of a divalent metal cation and two bicarbonate anions. Beside these endogenous cellular substrates, can also import cadmium a non-essential metal which is cytotoxic and carcinogenic (By similarity). {ECO:0000250|UniProtKB:Q15043, ECO:0000250|UniProtKB:Q75N73}.
Bos taurus (Bovine)
A5D8Q0
XIAP_XENLA
MEPQIVKFVFKEEMTCQCPKMSDSACDVDTDQNYFEEEVRLASFANFSSSYPVSAPALARAGFYYTGDGDRVKCFSCMAMVEDWQHGDTAIGKHRKISPNCKFINGFNNFRSDCIQTQAPVMQNSHANGFPNSAEDPGEKSSSEIMADYMLRTGRVVDMSKPKYPRHMAMCSEEARLQTFQNWPGYSPLMPKELANAGLFYTGINDQVKCFCCGGKLMNWEPSDRAWTEHKKHFPECYFVLGRDVGNVTRDASVQGSTYMNSYNARLETFSSWPFPIDKETLAKAGFYRIGDEDATKCFSCGGMLNCWAANDDPWEEHAKAYPGCQFLIEEKGQQFINNAQLQRPILHKANSGEASPALPKDTSFLKNPLVIYAQQMGFPLEEIKKVMGQKLKTTGNNYTCVEEFVSDLLCAQSETIADKPMKREISIEEKLRQLEEEKVCKVCMDRRITIVFIPCGHLVACAVCADVLDKCPICCTIIERRQKIFMS
2.3.2.27
null
apoptotic process [GO:0006915]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154]; negative regulation of proteolysis [GO:0045861]; nucleotide-binding oligomerization domain containing 2 signaling pathway [GO:0070431]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of protein linear polyubiquitination [GO:1902530]; regulation of cell cycle [GO:0051726]; Wnt signaling pathway [GO:0016055]
cytoplasm [GO:0005737]; 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]
PF00653;PF21290;PF13920;
1.10.8.10;3.30.40.10;
IAP family
PTM: Degraded in a 2-step mechanism; a caspase-independent first step and a caspase-dependent second step (PubMed:15853809). Stabilized indirectly by MAPK, which acts to delay caspase activation, rather than directly phosphorylating xiap (PubMed:15853809). {ECO:0000269|PubMed:15853809}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P98170}. Nucleus {ECO:0000250|UniProtKB:P98170}.
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:P98170};
null
null
null
null
FUNCTION: Multi-functional protein which regulates not only caspases and apoptosis, but also acts as an E3 ubiquitin-protein ligase mediating ubiquitination and subsequent proteasomal degradation of its target proteins (By similarity). Acts as a direct caspase inhibitor (By similarity). E3 ubiquitin-protein ligase that acts as an important regulator of innate immunity by mediating 'Lys-63'-linked polyubiquitination of ripk2 downstream of NOD1 and NOD2, thereby transforming ripk2 into a scaffolding protein for downstream effectors, ultimately leading to activation of the NF-kappa-B and MAP kinases signaling (By similarity). A key apoptotic suppressor in eggs (PubMed:15853809). Acts as a positive regulator of Wnt signaling (PubMed:22304967). {ECO:0000250|UniProtKB:P98170, ECO:0000269|PubMed:15853809, ECO:0000269|PubMed:22304967}.
Xenopus laevis (African clawed frog)
A5D8S5
SH3R1_DANRE
MDESALLDLLECPVCLERLDATAKVLPCQHTFCRRCLLGIVGSRGELRCPECRTLVESGVDELPSNILLVRLLDGIKQRPRRTGSVHGTCANGSAVAGVRAQGAGGSQRDPGPTGGQSQRVQAKSTPVRGVPQLPCAKALYNYDGKEPGDLKFSKGDIIILRRQVDENWYHGEMGGVHGFFPTNFVQVIKPLPQPPPQCKALYDFELKDKEADKDCLPFSKDDILTVIRRVDENWAEGMLGDKIGIFPISYVEFNSAARQLIELDKPSEGGGDSSEGPSSSSSGPQANGSQKAPGEKKNSKKRHSFTSLTMSHKPCLAPPPQRHSMEISGPVLISSSNPTAAARIGELSGGLSSSAPSQVHICTTGLIVTPPPSSPVTTATVFTFPPETSYASIPVDALPPPPPPPPQSQSSVVGAAALNAGQRPSPAAGDQSGRQRPTVYVAMFPYSPRKEDELELRKGEMFLVLERCQDGWFKGTSMHTGKIGVFPGNYMSPVSRTVSGSSQPKVPLTLCSQAGRGVTIVSPSSALGSMDLSKPLPVCPNATPSCSLPAAVVTAAHLPTGQHPKVLMHVTSQMTVNQARNAVRTAVSHSQDRPTAAVTPIQSHNPVAYLPSTAVVLQASPVLNSSSGCSSARVGVALGCAAASLTPPNVSAASLDTDAMRPVPMVALPVNAGSTKPLGAASNHGVACRLDKDCKREKKGLLKLLSNKKKLRPSPPSSPTLEAEQSVSMELPQGAVGPEMALSGSAGHNGRIGACPMDSELSMSSSSSNTDAVTHRSSPQDNTAPIAPPPRQPCSSLLSMQHDGRPIVCERYRVVVSYPPQSEAELELKEGDIVFVHKKREDGWFKGTLQRNGRTGLFPGSFVDSI
2.3.2.27
null
negative regulation of apoptotic process [GO:0043066]; neuron migration [GO:0001764]; positive regulation of JNK cascade [GO:0046330]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; protein autoubiquitination [GO:0051865]; protein ubiquitination [GO:0016567]; regulation of CD4-positive, alpha-beta T cell differentiation [GO:0043370]; regulation of CD8-positive, alpha-beta T cell proliferation [GO:2000564]
Golgi apparatus [GO:0005794]; lamellipodium [GO:0030027]; perinuclear region of cytoplasm [GO:0048471]
MAP-kinase scaffold activity [GO:0005078]; metal ion binding [GO:0046872]; ubiquitin protein ligase activity [GO:0061630]
PF00018;PF14604;PF13445;
2.30.30.40;3.30.40.10;
SH3RF family
PTM: Autoubiquitinated. Ubiquitinated by SH3RF2, leading to proteasome-mediated degradation. {ECO:0000250|UniProtKB:Q71F54}.
SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q71F54}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q69ZI1}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q69ZI1}.
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:Q7Z6J0};
null
PATHWAY: Protein modification; protein ubiquitination.
null
null
FUNCTION: Has E3 ubiquitin-protein ligase activity. In the absence of an external substrate, it can catalyze self-ubiquitination. Acts as a scaffold protein that contributes to the effective activation of the JNK signaling pathway. {ECO:0000250|UniProtKB:Q69ZI1, ECO:0000250|UniProtKB:Q7Z6J0}.
Danio rerio (Zebrafish) (Brachydanio rerio)
A5D8T8
CL18A_HUMAN
MLHPETSPGRGHLLAVLLALLGTAWAEVWPPQLQEQAPMAGALNRKESFLLLSLHNRLRSWVQPPAADMRRLDWSDSLAQLAQARAALCGTPTPSLASGLWRTLQVGWNMQLLPAGLVSFVEVVSLWFAEGQRYSHAAGECARNATCTHYTQLVWATSSQLGCGRHLCSAGQAAIEAFVCAYSPRGNWEVNGKTIVPYKKGAWCSLCTASVSGCFKAWDHAGGLCEVPRNPCRMSCQNHGRLNISTCHCHCPPGYTGRYCQVRCSLQCVHGRFREEECSCVCDIGYGGAQCATKVHFPFHTCDLRIDGDCFMVSSEADTYYRARMKCQRKGGVLAQIKSQKVQDILAFYLGRLETTNEVIDSDFETRNFWIGLTYKTAKDSFRWATGEHQAFTSFAFGQPDNHGFGNCVELQASAAFNWNDQRCKTRNRYICQFAQEHISRWGPGS
null
null
null
endoplasmic reticulum [GO:0005783]; endosome [GO:0005768]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]
polysaccharide binding [GO:0030247]
PF00188;PF00059;
3.40.33.10;2.10.25.10;3.10.100.10;
null
PTM: N-glycosylated. {ECO:0000269|PubMed:26170455}.
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26170455}. Endoplasmic reticulum {ECO:0000305|PubMed:26170455}. Golgi apparatus {ECO:0000305|PubMed:26170455}. Endosome {ECO:0000305|PubMed:26170455}.
null
null
null
null
null
FUNCTION: Binds polysaccharides in a Ca(2+)-independent manner with a preferentially binding to fucoidan, beta-glucans and galactans (PubMed:26170455). {ECO:0000269|PubMed:26170455}.
Homo sapiens (Human)
A5D8V6
VP37C_HUMAN
METLKDKTLQELEELQNDSEAIDQLALESPEVQDLQLEREMALATNRSLAERNLEFQGPLEISRSNLSDRYQELRKLVERCQEQKAKLEKFSSALQPGTLLDLLQVEGMKIEEESEAMAEKFLEGEVPLETFLENFSSMRMLSHLRRVRVEKLQEVVRKPRASQELAGDAPPPRPPPPVRPVPQGTPPVVEEQPQPPLAMPPYPLPYSPSPSLPVGPTAHGALPPAPFPVVSQPSFYSGPLGPTYPAAQLGPRGAAGYSWSPQRSMPPRPGYPGTPMGASGPGYPLRGGRAPSPGYPQQSPYPATGGKPPYPIQPQLPSFPGQPQPSVPLQPPYPPGPAPPYGFPPPPGPAWPGY
null
null
macroautophagy [GO:0016236]; membrane fission [GO:0090148]; multivesicular body assembly [GO:0036258]; protein targeting to membrane [GO:0006612]; protein targeting to vacuole [GO:0006623]; protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway [GO:0043328]; ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway [GO:0043162]; viral budding via host ESCRT complex [GO:0039702]
endosome membrane [GO:0010008]; ESCRT I complex [GO:0000813]; extracellular exosome [GO:0070062]; late endosome membrane [GO:0031902]
calcium-dependent protein binding [GO:0048306]
PF07200;
1.10.287.660;
VPS37 family
PTM: Phosphorylated by TBK1. {ECO:0000269|PubMed:21270402}.
SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000305|PubMed:15509564}; Peripheral membrane protein {ECO:0000305|PubMed:15509564}. Note=Probably associates with membranes. Recruited to the plasma membrane by HIV-1.
null
null
null
null
null
FUNCTION: Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies. May be involved in cell growth and differentiation. {ECO:0000269|PubMed:15509564}.
Homo sapiens (Human)
A5D8V7
ODAD3_HUMAN
MTSPLCRAASANALPPQDQASTPSSRVKGREASGKPSHLRGKGTAQAWTPGRSKGGSFHRGAGKPSVHSQVAELHKKIQLLEGDRKAFFESSQWNIKKNQETISQLRKETKALELKLLDLLKGDEKVVQAVIREWKWEKPYLKNRTGQALEHLDHRLREKVKQQNALRHQVVLRQRRLEELQLQHSLRLLEMAEAQNRHTEVAKTMRNLENRLEKAQMKAQEAEHITSVYLQLKAYLMDESLNLENRLDSMEAEVVRTKHELEALHVVNQEALNARDIAKNQLQYLEETLVRERKKRERYISECKKRAEEKKLENERMERKTHREHLLLQSDDTIQDSLHAKEEELRQRWSMYQMEVIFGKVKDATGTDETHSLVRRFLAQGDTFAQLETLKSENEQTLVRLKQEKQQLQRELEDLKYSGEATLVSQQKLQAEAQERLKKEERRHAEAKDQLERALRAMQVAKDSLEHLASKLIHITVEDGRFAGKELDPQADNYVPNLLGLVEEKLLKLQAQLQGHDVQEMLCHIANREFLASLEGRLPEYNTRIALPLATSKDKFFDEESEEEDNEVVTRASLKIRSQKLIESHKKHRRSRRS
null
null
brain development [GO:0007420]; cerebrospinal fluid circulation [GO:0090660]; cilium movement [GO:0003341]; determination of heart left/right asymmetry [GO:0061371]; determination of left/right symmetry [GO:0007368]; epithelial cilium movement involved in determination of left/right asymmetry [GO:0060287]; flagellated sperm motility [GO:0030317]; multicellular organism growth [GO:0035264]; outer dynein arm assembly [GO:0036158]; regulation of cilium assembly [GO:1902017]; spermatogenesis [GO:0007283]
axoneme [GO:0005930]; centriole [GO:0005814]; ciliary basal body [GO:0036064]; ciliary rootlet [GO:0035253]; ciliary tip [GO:0097542]; cilium [GO:0005929]; extracellular region [GO:0005576]; outer dynein arm docking complex [GO:0120228]
null
null
null
null
null
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q8BSN3}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q8BSN3}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:25192045}.
null
null
null
null
null
FUNCTION: Component of the outer dynein arm-docking complex (ODA-DC) that mediates outer dynein arms (ODA) binding onto the doublet microtubule (PubMed:25192045). Involved in mediating assembly of both ODAs and their axonemal docking complex onto ciliary microtubules (PubMed:25192045). {ECO:0000269|PubMed:25192045}.
Homo sapiens (Human)
A5D8W1
CFA69_HUMAN
MWTEEAGATAEAQESGIRNKSSSSSQIPVVGVVTEDDEAQDVFKPMDLNRVIKLLEETDKDGLEEKQLKFVKKLVQCYQNGLPLRDLAQIFKILNLCSGKIKNQPRFIESAYDIIKLCGLPFLKKKVSDEITYAEDTANSIALLGDLMKIPSSELRIQICKCIVDFYHAEPPKKHIPGYQQASSSYKIQMAEVGGLAKTMVQSMTLLENQLVEKLWVLKVLQHLSTSEVNCTIMMKAQAASGICTHLNDPDPSGQLLFRSSEILWNLLEKSSKEEVIQQLSNLECLLALKEVFKNLFMRGFSHYDRQLRNDILVITTIIAQNPEAPMIECGFTKDLILFATFNEVKSQNLLVKGLKLSNSYEDFELKKLLFNVIVILCKDLPTVQLLIDGKVILALFTYVKKPEKQKIIDWSAAQHEELQLHAIATLSSVAPLLIEEYMSCQGNARVLAFLEWCESEDPFFSHGNSFHGTGGRGNKFAQMRYSLRLLRAVVYLEDETVNKDLCEKGTIQQMIGIFKNIISKPNEKEEAIVLEIQSDILLILSGLCENHIQRKEIFGTEGVDIVLHVMKTDPRKLQSGLGYNVLLFSTLDSIWCCILGCYPSEDYFLEKEGIFLLLDLLALNQKKFCNLILGIMVEFCDNPKTAAHVNAWQGKKDQTAASLLIKLWRKEEKELGVKRDKNGKIIDTKKPLFTSFQEEQKIIPLPANCPSIAVMDVSENIRAKIYAILGKLDFENLPGLSAEDFVTLCIIHRYLDFKIGEIWNEIYEEIKLEKLRPVTTDKKALEAITTASENIGKMVASLQSDIIESQACQDMQNEQKVYAKIQATHKQRELANKSWEDFLARTSNAKTLKKAKSLQEKAIEASRYHKRPQNAIFHQTHIKGLNTTVPSGGVVTVESTPARLVGGPLVDTDIALKKLPIRGGALQRVKAVKIVDAPKKSIPT
null
null
flagellated sperm motility [GO:0030317]; olfactory behavior [GO:0042048]; positive regulation of fertilization [GO:1905516]; positive regulation of flagellated sperm motility [GO:1902093]; response to odorant [GO:1990834]; sensory perception of smell [GO:0007608]; sperm axoneme assembly [GO:0007288]
cytoplasm [GO:0005737]; non-motile cilium [GO:0097730]; sperm midpiece [GO:0097225]
null
PF21049;
1.25.10.10;
null
null
SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000250|UniProtKB:Q8BH53}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:29606301}. Note=Localizes to the midpiece of the sperm flagellum. {ECO:0000269|PubMed:29606301}.
null
null
null
null
null
FUNCTION: Cilium- and flagellum-associated protein (PubMed:29606301). In the olfactory epithelium, regulates the speed of activation and termination of the odor response and thus contributes to the robustness of olfactory transduction pathways (By similarity). Required for sperm flagellum assembly and stability (PubMed:29606301). {ECO:0000250|UniProtKB:Q8BH53, ECO:0000269|PubMed:29606301}.
Homo sapiens (Human)
A5D979
SPRTN_BOVIN
MDEDLVLALQLQEEWNLQVSEREPAQEPLSLVDASWELVDPTPDLQGLFVLFNDRFFWGQLEAVEVKWSVRMTLCAGICSYEGRGGMCSIRLSEPLLKLRPRKDLVETLLHEMIHAYLFVTNNDKDREGHGPEFCKHMHRINRLTGANITVYHTFHDEVDEYRRHWWRCNGPCQNSKPYYGYVKRATNRAPSAHDYWWAEHQKTCGGTYIKIKEPENYSKKGKGKTKLRKQPVSEAENKDKPNRGEKQLLIPFTGKGYVLGETSNFSSGKCITSHAINESQEPLSQDHSANALRPHSKTEVKFEQNGPSKKTSVASPVLSTSHQNVLSNYFSKVSVASSKAFRSVSGSPVKSLTVGDSTTKSVSAGSQRRVTSSRTSLRNSLKAMESTYVTVPQDAGGPEGKLPSKRPRIEDKTFFDLFFIKKEQAQSGGGDVTSSSHPPAAAQSPSGASGQSRVVHCPVCQDEVSETQINEHLDWCLERDSTQVKS
3.4.24.-
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q9H040};
DNA damage response [GO:0006974]; positive regulation of protein ubiquitination [GO:0031398]; protein autoprocessing [GO:0016540]; protein-DNA covalent cross-linking repair [GO:0106300]; proteolysis [GO:0006508]; response to UV [GO:0009411]; S-adenosylmethionine biosynthetic process [GO:0006556]; translesion synthesis [GO:0019985]
chromatin [GO:0000785]; nucleus [GO:0005634]
double-stranded DNA binding [GO:0003690]; K63-linked polyubiquitin modification-dependent protein binding [GO:0070530]; metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; methionine adenosyltransferase activity [GO:0004478]; polyubiquitin modification-dependent protein binding [GO:0031593]; single-stranded DNA binding [GO:0003697]; ubiquitin binding [GO:0043130]
PF10263;
3.30.160.60;
Spartan family
PTM: Autocatalytically cleaved in response to double-stranded DNA-binding: autocatalytic cleavage takes place in trans and leads to inactivation. {ECO:0000250|UniProtKB:Q9H040}.; PTM: Monoubiquitinated; monoubiquitination promotes exclusion from chromatin. Deubiquitinated by VCPIP1: deubiquitination is required for subsequent acetylation and recruitment to chromatin and DNA damage sites. {ECO:0000250|UniProtKB:Q9H040}.; PTM: Acetylated following deubiquitination by VCPIP1, leading to recruitment to chromatin and DNA damage sites. {ECO:0000250|UniProtKB:Q9H040}.; PTM: Phosphorylation by CHEK1 promotes recruitment to chromatin. {ECO:0000250|UniProtKB:Q9H040}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H040}. Chromosome {ECO:0000250|UniProtKB:Q9H040}. Note=Localizes to sites of UV damage via the PIP-box. Recruited to stalled replication forks at sites of replication stress following deubiquitination. CHEK1 stimulates recruitment to chromatin. {ECO:0000250|UniProtKB:Q9H040}.
null
null
null
null
null
FUNCTION: DNA-dependent metalloendopeptidase that mediates the proteolytic cleavage of covalent DNA-protein cross-links (DPCs) during DNA synthesis, thereby playing a key role in maintaining genomic integrity. DPCs are highly toxic DNA lesions that interfere with essential chromatin transactions, such as replication and transcription, and which are induced by reactive agents, such as UV light or formaldehyde. Associates with the DNA replication machinery and specifically removes DPCs during DNA synthesis. Catalyzes proteolytic cleavage of the HMCES DNA-protein cross-link following unfolding by the BRIP1/FANCJ helicase. Acts as a pleiotropic protease for DNA-binding proteins cross-linked with DNA, such as TOP1, TOP2A, histones H3 and H4. Mediates degradation of DPCs that are not ubiquitinated, while it is not able to degrade ubiquitinated DPCs. SPRTN activation requires polymerase collision with DPCs followed by helicase bypass of DPCs. Involved in recruitment of VCP/p97 to sites of DNA damage. Also acts as an activator of CHEK1 during normal DNA replication by mediating proteolytic cleavage of CHEK1, thereby promoting CHEK1 removal from chromatin and subsequent activation. Does not activate CHEK1 in response to DNA damage. May also act as a 'reader' of ubiquitinated PCNA: recruited to sites of UV damage and interacts with ubiquitinated PCNA and RAD18, the E3 ubiquitin ligase that monoubiquitinates PCNA. Facilitates chromatin association of RAD18 and is required for efficient PCNA monoubiquitination, promoting a feed-forward loop to enhance PCNA ubiquitination and translesion DNA synthesis. {ECO:0000250|UniProtKB:A0A1L8G2K9, ECO:0000250|UniProtKB:Q9H040}.
Bos taurus (Bovine)
A5D9M6
BAG6_PIG
MEPNDSTSTTMEEPESLEVLVKTLDSQTRTFIVGAQMNVKEFKEHIAASVSIPSEKQRLIYQGRVLQDDKKLQEYNVGGKVIHLVERAPPQTQLPSGASSGTGSASATHGGGPPPGTRGPGASVHDRNANSYVMVGTFNLPSDGSAVDVHINMEQAPIQSEPRVRLVMAQHMIRDIQTLLSRMECRGGSQAQHSQPPSQMPTVAPEPVALSSQTSESVESEVPPREPMAAEEVEERASAQSPGLSPSGPAPAGPTPAPETNAPNHPSPAEYVEVLQELQRLESRLQPFLQRYYEVLGAAATTDYNNNQEGREEDQRLINLVGESLRLLGNTFVALSDLRCNLACAPPRHLHVVRPMSHYTTPMVLQQAAIPIQINVGTTVTMTGNGTRPPPTPNAEAPPPGPGQASSLAPSSTTVESSTEGAPPPGPAPPPAASHPRVIRISHQSVEPVVMMHMNIQDSGTQPGGVPSAPTGPLGPTGHGQTLGQQVPGFPTAPTRVVIARPTPPQSRPSHPGGPPVSGALPGAGLGTNASLAQMVSGLVGQLLMQPVLVAQGTPGMAPPPAPATASASAGTTNTATTAGPAPGGPAQPPPPQPSASDLQFSQLLGNLLGPAGPGAGGPGMTSPTITVAMPGVPAFLQGMTDFLQATQTAAPPAPPPPPPPPPPAPEQQTAPPPGSPPGGAGSPGGLGPESLPLEFFTSVVQGVLSSLLGSLGARAGSSESIAAFIQRLSGSSNIFEPGADGALGFFGALLSLLCQNFSMVDVVMLLHGHFQPLQRLQPQLRSFFHQHYLGGQEPTPGNIRTATHTLITGLEEYVRESFSLVQVQPGVDIIRTNLEFLQEQFNSIAAHVMHCTDSGFGARLLELCNQGLFECLALNLHCLGGQQMELAAVINGRIRRMSRGVNPSLVSWLTTMMGLRLQVVLEHMPVGPDAILRYVRRVGDPPQPLPEEPMEVQGSERTSPEPQRENASPAPGTTAEEAMSRGPPPAPEGGSRDEQDGAAAETEPWAAAVPPEWVPIIQQDIQSQRKVKPQPPLSDAYLSGMPAKRRKTMQGEGPQLLLSEAVSRAAKAAGARPLTSPESLSRDLEAPEVQESYRQQLRADIQKRLQEDPNYSPQRFPNAHRAFAEDP
null
null
apoptotic process [GO:0006915]; brain development [GO:0007420]; cell differentiation [GO:0030154]; chromatin organization [GO:0006325]; endoplasmic reticulum stress-induced pre-emptive quality control [GO:0061857]; ERAD pathway [GO:0036503]; immune system process [GO:0002376]; internal peptidyl-lysine acetylation [GO:0018393]; intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [GO:0042771]; intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress [GO:0070059]; kidney development [GO:0001822]; lung development [GO:0030324]; negative regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032435]; negative regulation of proteolysis [GO:0045861]; proteasomal protein catabolic process [GO:0010498]; protein stabilization [GO:0050821]; regulation of apoptotic process [GO:0042981]; regulation of embryonic development [GO:0045995]; spermatogenesis [GO:0007283]; synaptonemal complex assembly [GO:0007130]; tail-anchored membrane protein insertion into ER membrane [GO:0071816]; ubiquitin-dependent protein catabolic process [GO:0006511]
BAT3 complex [GO:0071818]; cytosol [GO:0005829]; extracellular region [GO:0005576]; nucleus [GO:0005634]
misfolded protein binding [GO:0051787]; polyubiquitin modification-dependent protein binding [GO:0031593]; proteasome binding [GO:0070628]; ribosome binding [GO:0043022]
PF12057;PF20960;PF00240;
null
null
PTM: Ricin can induce a cleavage by the caspase CASP3. The released C-terminal peptide induces apoptosis. {ECO:0000250|UniProtKB:P46379}.
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P46379}. Nucleus {ECO:0000250|UniProtKB:P46379}. Secreted, extracellular exosome {ECO:0000250|UniProtKB:P46379}. Note=Normally localized in cytosol and nucleus, it can also be released extracellularly, in exosomes, by tumor and myeloid dendritic cells. {ECO:0000250|UniProtKB:P46379}.
null
null
null
null
null
FUNCTION: ATP-independent molecular chaperone preventing the aggregation of misfolded and hydrophobic patches-containing proteins. Functions as part of a cytosolic protein quality control complex, the BAG6/BAT3 complex, which maintains these client proteins in a soluble state and participates in their proper delivery to the endoplasmic reticulum or alternatively can promote their sorting to the proteasome where they undergo degradation. The BAG6/BAT3 complex is involved in the post-translational delivery of tail-anchored/type II transmembrane proteins to the endoplasmic reticulum membrane. Recruited to ribosomes, it interacts with the transmembrane region of newly synthesized tail-anchored proteins and together with SGTA and ASNA1 mediates their delivery to the endoplasmic reticulum. Client proteins that cannot be properly delivered to the endoplasmic reticulum are ubiquitinated by RNF126, an E3 ubiquitin-protein ligase associated with BAG6 and are sorted to the proteasome. SGTA which prevents the recruitment of RNF126 to BAG6 may negatively regulate the ubiquitination and the proteasomal degradation of client proteins. Similarly, the BAG6/BAT3 complex also functions as a sorting platform for proteins of the secretory pathway that are mislocalized to the cytosol either delivering them to the proteasome for degradation or to the endoplasmic reticulum. The BAG6/BAT3 complex also plays a role in the endoplasmic reticulum-associated degradation (ERAD), a quality control mechanism that eliminates unwanted proteins of the endoplasmic reticulum through their retrotranslocation to the cytosol and their targeting to the proteasome. It maintains these retrotranslocated proteins in an unfolded yet soluble state condition in the cytosol to ensure their proper delivery to the proteasome. BAG6 is also required for selective ubiquitin-mediated degradation of defective nascent chain polypeptides by the proteasome. In this context, it may participate in the production of antigenic peptides and play a role in antigen presentation in immune response. BAG6 is also involved in endoplasmic reticulum stress-induced pre-emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for proteasomal degradation. BAG6 may ensure the proper degradation of these proteins and thereby protects the endoplasmic reticulum from protein overload upon stress. By inhibiting the polyubiquitination and subsequent proteasomal degradation of HSPA2 it may also play a role in the assembly of the synaptonemal complex during spermatogenesis. Also positively regulates apoptosis by interacting with and stabilizing the proapoptotic factor AIFM1. By controlling the steady-state expression of the IGF1R receptor, indirectly regulates the insulin-like growth factor receptor signaling pathway. {ECO:0000250|UniProtKB:P46379}.; FUNCTION: Involved in DNA damage-induced apoptosis: following DNA damage, accumulates in the nucleus and forms a complex with p300/EP300, enhancing p300/EP300-mediated p53/TP53 acetylation leading to increase p53/TP53 transcriptional activity. When nuclear, may also act as a component of some chromatin regulator complex that regulates histone 3 'Lys-4' dimethylation (H3K4me2). {ECO:0000250|UniProtKB:P46379}.; FUNCTION: Released extracellularly via exosomes, it is a ligand of the natural killer/NK cells receptor NCR3 and stimulates NK cells cytotoxicity. It may thereby trigger NK cells cytotoxicity against neighboring tumor cells and immature myeloid dendritic cells (DC). {ECO:0000250|UniProtKB:P46379}.; FUNCTION: May mediate ricin-induced apoptosis. {ECO:0000250|UniProtKB:P46379}.
Sus scrofa (Pig)
A5F120
NHAD_VIBC3
MTGRIALLSLTLFSPLSLASTPDGQALDFTHSTIGYAALLIFAIAYTLVMLEEYLQLRKSKPVLLAAGLIWAMIGYVYQQTGSTEVARQALEHNLLEYAELLLFLLVAMTYISAMEERRLFDALKAWMINRGFNFHTLFWITGWLAFFISPIADNLTTALLMCAVVMKVGGENPKFVSLACINIVIAANAGGAFSPFGDITTLMVWQAGHVSFLEFMDLFLPSLANYLVPALVMSLFVPHQTPSSIQEVVELKRGAKRIVVLFLFTILSAIGFHAFFHFPPVIGMMMGLAYLQFFGYFLRKTLARSLAKKTAIAMAKNDEAALKRIGSVVPFDVFRSISHAEWDTLLFFYGVVMCVGGLSLLGYLGLVSEILYTEWNPIWANVLVGLLSSVVDNIPVMFAVLSMQPEMSLGNWLLVTLTAGVGGSLLSIGSAAGVALMGAAHGKYTFLSHLKWTPVILLGYVVSIVLHLLLNHQSFT
null
null
sodium ion transport [GO:0006814]
plasma membrane [GO:0005886]
antiporter activity [GO:0015297]
PF03600;
null
NhaD Na(+)/H(+) (TC 2.A.62) antiporter family
null
SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:11936836, ECO:0000269|PubMed:16186100}; Multi-pass membrane protein {ECO:0000269|PubMed:11936836, ECO:0000269|PubMed:16186100}.
null
null
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. Totally inactive at pH 9.0. {ECO:0000269|PubMed:11936836};
null
FUNCTION: Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons. Can also transport lithium. {ECO:0000269|PubMed:11936836, ECO:0000269|PubMed:12101001, ECO:0000269|PubMed:16186100}.
Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)
A5F465
FADB_VIBC3
MIYQAKTLQVKQLANGIAELSFCAPASVNKLDLHTLESLDKALDALAADSSVKGLLLSSDKEAFIVGADITEFLGLFAKPEAELDEWLQFANRIFNKLEDLPFPTLSALKGHTLGGGCECVLATDFRIGDATTSIGLPETKLGIMPGFGGTVRLPRLIGADSAMEIITQGKACRAEEALKVGLLDAIVDSDKLIDSAITTLTQAIEEKLDWQKRRQQKTSALTLSKLEAMMSFTMAKGMVAQVAGKHYPAPMTSVVTIEEAARLPRDAALDIERKHFIKLAKSTEAQALVGIFLNDQYIKGLAKQSAKAASQDTQHAAVLGAGIMGGGIAYQSALKGVPVLMKDIAPHSLELGMTEAAKLLNKQLERGKIDGFKMAGILASITPSLHYAGIDQADVIVEAVVENPKVKAAVLSEVEGLVDAETILTSNTSTIPINLLAKSLKRPQNFCGMHFFNPVHRMPLVEIIRGEHTSEDTINRVVAYAAKMGKSPIVVNDCPGFFVNRVLFPYFAGFSLLMRDGANFTEIDKVMERQFGWPMGPAYLLDVVGIDTAHHAQAVMAEGFPTRMAKSGREAIDALYEAKKFGQKNGSGFYQYTVDKKGKPKKAFSDDVLAILAPVCGAPQNFDPQTLIERTMIPMINEVVLCLEEGIIASAQEADMALVYGLGFPPFRGGVFRYLDTIGIANYVAMAEKYADLGALYQVPQLLKNMAQQGTSFYSAQQASAL
1.1.1.35; 4.2.1.17; 5.1.2.3; 5.3.3.8
null
fatty acid beta-oxidation [GO:0006635]
fatty acid beta-oxidation multienzyme complex [GO:0036125]
3-hydroxyacyl-CoA dehydrogenase activity [GO:0003857]; 3-hydroxybutyryl-CoA epimerase activity [GO:0008692]; delta(3)-delta(2)-enoyl-CoA isomerase activity [GO:0004165]; enoyl-CoA hydratase activity [GO:0004300]; NAD+ binding [GO:0070403]
PF00725;PF02737;PF00378;
1.10.1040.50;3.40.50.720;
Enoyl-CoA hydratase/isomerase family; 3-hydroxyacyl-CoA dehydrogenase family
null
null
CATALYTIC ACTIVITY: Reaction=a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) + NADH; Xref=Rhea:RHEA:22432, ChEBI:CHEBI:15378, ChEBI:CHEBI:57318, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726; EC=1.1.1.35; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; CATALYTIC ACTIVITY: Reaction=a (3S)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O; Xref=Rhea:RHEA:16105, ChEBI:CHEBI:15377, ChEBI:CHEBI:57318, ChEBI:CHEBI:58856; EC=4.2.1.17; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; CATALYTIC ACTIVITY: Reaction=a 4-saturated-(3S)-3-hydroxyacyl-CoA = a (3E)-enoyl-CoA + H2O; Xref=Rhea:RHEA:20724, ChEBI:CHEBI:15377, ChEBI:CHEBI:58521, ChEBI:CHEBI:137480; EC=4.2.1.17; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; CATALYTIC ACTIVITY: Reaction=(3S)-3-hydroxybutanoyl-CoA = (3R)-3-hydroxybutanoyl-CoA; Xref=Rhea:RHEA:21760, ChEBI:CHEBI:57315, ChEBI:CHEBI:57316; EC=5.1.2.3; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; CATALYTIC ACTIVITY: Reaction=a (3Z)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA; Xref=Rhea:RHEA:45900, ChEBI:CHEBI:85097, ChEBI:CHEBI:85489; EC=5.3.3.8; Evidence={ECO:0000255|HAMAP-Rule:MF_01621}; CATALYTIC ACTIVITY: Reaction=a (3E)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA; Xref=Rhea:RHEA:45228, ChEBI:CHEBI:58521, ChEBI:CHEBI:85097; EC=5.3.3.8; Evidence={ECO:0000255|HAMAP-Rule:MF_01621};
null
PATHWAY: Lipid metabolism; fatty acid beta-oxidation. {ECO:0000255|HAMAP-Rule:MF_01621}.
null
null
FUNCTION: Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. {ECO:0000255|HAMAP-Rule:MF_01621}.
Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)
A5F5X0
NQRB_VIBC3
MGLKKFLEDIEHHFEPGGKHEKWFALYEAAATLFYTPGLVTKRSSHVRDSVDLKRIMIMVWLAVFPAMFWGMYNAGGQAIAALNHLYSGDQLAAIVAGNWHYWLTEMLGGTMSSDAGWGSKMLLGATYFLPIYATVFIVGGFWEVLFCMVRKHEVNEGFFVTSILFALIVPPTLPLWQAALGITFGVVVAKEVFGGTGRNFLNPALAGRAFLFFAYPAQISGDLVWTAADGYSGATALSQWAQGGAGALINNATGQTITWMDAFIGNIPGSIGEVSTLALMIGAAFIVYMGIASWRIIGGVMIGMILLSTLFNVIGSDTNAMFNMPWHWHLVLGGFAFGMFFMATDPVSASFTNSGKWAYGILIGVMCVLIRVVNPAYPEGMMLAILFANLFAPLFDHVVVERNIKRRLARYGKQ
7.2.1.1
COFACTOR: Name=riboflavin; Xref=ChEBI:CHEBI:57986; Evidence={ECO:0000269|PubMed:20558724}; COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000255|HAMAP-Rule:MF_00426, ECO:0000269|PubMed:11888296, ECO:0000269|PubMed:20558724, ECO:0000269|PubMed:22366169};
respiratory electron transport chain [GO:0022904]; sodium ion transport [GO:0006814]; transmembrane transport [GO:0055085]
plasma membrane [GO:0005886]
FMN binding [GO:0010181]; oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor [GO:0016655]; riboflavin binding [GO:1902444]
PF03116;
null
NqrB/RnfD family
null
SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00426, ECO:0000305}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00426}.
CATALYTIC ACTIVITY: Reaction=a ubiquinone + H(+) + n Na(+)(in) + NADH = a ubiquinol + n Na(+)(out) + NAD(+); Xref=Rhea:RHEA:47748, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, ChEBI:CHEBI:29101, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.2.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00426, ECO:0000269|PubMed:11888296};
null
null
null
null
FUNCTION: NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol. {ECO:0000255|HAMAP-Rule:MF_00426}.
Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)
A5F5Y4
NQRF_VIBC3
MSTIIFGVVMFTLIILALVLVILFAKSKLVPTGDITISINGDPEKAIVTQPGGKLLTALAGAGVFVSSACGGGGSCGQCRVKIKSGGGDILPTELDHISKGEAREGERLACQVAVKADMDLELPEEIFGVKKWECTVISNDNKATFIKELKLAIPDGESVPFRAGGYIQIEAPAHHVKYADFDVPEKYRGDWDKFNLFRYESKVDEPIIRAYSMANYPEEFGIIMLNVRIATPPPNNPNVPPGQMSSYIWSLKAGDKCTISGPFGEFFAKDTDAEMVFIGGGAGMAPMRSHIFDQLKRLKSKRKMSYWYGARSKREMFYVEDFDGLAAENDNFVWHCALSDPQPEDNWTGYTGFIHNVLYENYLKDHEAPEDCEYYMCGPPMMNAAVINMLKNLGVEEENILLDDFGG
7.2.1.1
COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000255|HAMAP-Rule:MF_00430, ECO:0000269|PubMed:15379571}; Note=Binds 1 [2Fe-2S] cluster. {ECO:0000255|HAMAP-Rule:MF_00430, ECO:0000269|PubMed:15379571}; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000255|HAMAP-Rule:MF_00430, ECO:0000269|PubMed:15379571};
sodium ion transport [GO:0006814]
plasma membrane [GO:0005886]
2 iron, 2 sulfur cluster binding [GO:0051537]; electron transfer activity [GO:0009055]; FAD binding [GO:0071949]; metal ion binding [GO:0046872]; oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor [GO:0016655]
PF00970;PF00111;PF00175;
3.10.20.30;3.40.50.80;2.40.30.10;
NqrF family
null
SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00430, ECO:0000305}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00430}.
CATALYTIC ACTIVITY: Reaction=a ubiquinone + H(+) + n Na(+)(in) + NADH = a ubiquinol + n Na(+)(out) + NAD(+); Xref=Rhea:RHEA:47748, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, ChEBI:CHEBI:29101, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.2.1.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00430, ECO:0000269|PubMed:11888296};
null
null
null
null
FUNCTION: NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. The first step is catalyzed by NqrF, which accepts electrons from NADH and reduces ubiquinone-1 to ubisemiquinone by a one-electron transfer pathway. {ECO:0000255|HAMAP-Rule:MF_00430}.
Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)
A5F7A4
NANH_VIBC3
MRFKNVKKTALMLAMFGMATSSNAALFDYNATGDTEFDSPAKQGWMQDNTNNGSGVLTNADGMPAWLVQGIGGRAQWTYSLSTNQHAQASSFGWRMTTEMKVLSGGMITNYYANGTQRVLPIISLDSSGNLVVEFEGQTGRTVLATGTAATEYHKFELVFLPGSNPSASFYFDGKLIRDNIQPTASKQNMIVWGNGSSNTDGVAAYRDIKFEIQGDVIFRGPDRIPSIVASSVTPGVVTAFAEKRVGGGDPGALSNTNDIITRTSRDGGITWDTELNLTEQINVSDEFDFSDPRPIYDPSSNTVLVSYARWPTDAAQNGDRIKPWMPNGIFYSVYDVASGNWQAPIDVTDQVKERSFQIAGWGGSELYRRNTSLNSQQDWQSNAKIRIVDGAANQIQVADGSRKYVVTLSIDESGGLVANLNGVSAPIILQSEHAKVHSFHDYELQYSALNHTTTLFVDGQQITTWAGEVSQENNIQFGNADAQIDGRLHVQKIVLTQQGHNLVEFDAFYLAQQTPEVEKDLEKLGWTKIKTGNTMSLYGNASVNPGPGHGITLTRQQNISGSQNGRLIYPAIVLDRFFLNVMSIYSDDGGSNWQTGSTLPIPFRWKSSSILETLEPSEADMVELQNGDLLLTARLDFNQIVNGVNYSPRQQFLSKDGGITWSLLEANNANVFSNISTGTVDASITRFEQSDGSHFLLFTNPQGNPAGTNGRQNLGLWFSFDEGVTWKGPIQLVNGASAYSDIYQLDSENAIVIVETDNSNMRILRMPITLLKQKLTLSQN
3.2.1.18
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
ganglioside catabolic process [GO:0006689]; oligosaccharide catabolic process [GO:0009313]
cytoplasm [GO:0005737]; extracellular region [GO:0005576]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]
exo-alpha-(2->3)-sialidase activity [GO:0052794]; exo-alpha-(2->6)-sialidase activity [GO:0052795]; exo-alpha-(2->8)-sialidase activity [GO:0052796]; sialic acid binding [GO:0033691]
PF13088;PF09264;
2.120.10.10;2.60.120.200;
Glycosyl hydrolase 33 family
null
SUBCELLULAR LOCATION: Secreted.
CATALYTIC ACTIVITY: Reaction=Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.; EC=3.2.1.18;
null
null
null
null
FUNCTION: Cleaves the terminal sialic acid (N-acetyl neuraminic acid) from carbohydrate chains in glycoproteins providing free sialic acid which can be used as carbon and energy sources. Sialidases have been suggested to be pathogenic factors in microbial infections. Facilitates cholera toxin binding to host intestinal epithelial cells by converting cell surface polysialogangliosides to GM1 monogangliosides.
Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)
A5FB63
CHIA_FLAJ1
MKHYYRLLFLLLFPLLASAQPAHGKKVVGYYAQWSIYARDFNVPKIDGSKLTHLNYSFYGTTYDPAHPENTKLKCLDTYADFEHMEGGIPWDAPVKGNFYDLMKLKQKYPHLKILISVGGWTKGQDLSPIAASPVARAALAADMANFIVTYPFIDGFDIDWEYPLSGGTDGTEIVNGMPVPPQKYSPDDNKNLVLLLKAMRQAMPNKLVTIAAGNNVRNVSKQYLGPNNRAQYGMTEDISTYCDYITYFGYDFGGNWYDKTCYNAPLYASGNPNDPLYGATQSESLDELTNQYLNVIGFPANKLIMGLPFYGKKFDNVAANSTNGLFVAAPRYIVPGCTNPQNPTGTWDGSGACEKSGSIEICDLVGNPVTNSHAYLDPNTMMVTPSAASAGWVRYFDNTTKVPYLYNSTLKQFISYEDKQSMDLKVQYIKSRNLAGGMIWELSQDTRGSIPNSLLNQVDTSFGSVVPGTVSISGSVKNGSALVTDVTVELRNASNAVIQTVVSANGNFAFNNLTSGQNYSLTALKATYTFTPVTLVNVTVNQTAVVINGTQPTYTVSGTVLDGSTPVSGVTVTAVSGSTTLTAVSNASGVYSIAGLTAGLNFTVTAAKSGFSYAPASTVYNAIDSNKTLNFTQGAPVVNYTVSGTVLNSTTPVSGVTVTASFTGGSYAAVTNASGTYSLSLPSGGNYTVTAALTGQTFTPASTVYSNLNANKTLNFTQDVVVSTSKISGTVKNGTNPVAGAKVELVLPWTDNTHNWKSVIATTDAQGKYSFDNSVVDGYTQVLSLKLNSWQNGEVAYYPNNLANFAVPANPTVYNFNTSSTAKSALAAAANLISGTVKNGTTPVAGAKVEIVLPWTDNTHNWKSVLATTDASGNYSFDNSVVAGYTQILSLKLNGWENGDVTYYPNNLANFAVPTTPTIYNFNRQAVVATKPVVTITAPTASAIAINLGSAINFVASVGLSAVDATTISSVVFSLDGQSLSTANSSGTYTAAWTPAANQFSLSHTLTVTATASNGTTDSKTYSFTLTCSGANCPNALPVITWNSPSNTTVYQNTFQVVPISVTAVDSDGTVSGVTITINGGTFNMTAGTNNTYTYNFTPSAYQDYPVVIKATDNKSGVTTLNNTIKIATVSTNRFIPLPSKIILGYAHSWENAGAPFLYFSQMVGSKFNVVDYSFVETVNRDGYTPILTTNDTRYLTNGVFNKQLLKNDIKSLRDSGVPVIVSIGGQNGHVVLDNVTQKNIFVNGLKAIIDEYQFDGVDIDFEGGSMNFNAGGLRDISYAGISAYPRLKNVVDAFKELKAYYGPGFLLTAAPETQYVQGGYTTYTDTFGSFLPIIQNLRNELDLLAVQLYNTGGENGLDGQYYGTAKKSNMVTALTDMVIKGYNIASTGMRFDGLPASKVLIALPACPSAAGSGYLTPTEGINAMHYLRTGTTFSGRTYTMQPGGPYPSLRGLMTWSVNWDASSCGNSSELSKAYAAYFASQTAAKTLVLDDISAKSNATIAYFKNNALSVTNENEDIAQVDVFNVLGQNLVSHRNVQNNKEVLLHNQSFSSKQLFLVVVTDKAGNKKSFKVMNFLN
3.2.1.14
null
chitin catabolic process [GO:0006032]; polysaccharide catabolic process [GO:0000272]
extracellular region [GO:0005576]
carbohydrate binding [GO:0030246]; chitin binding [GO:0008061]; chitinase activity [GO:0004568]
PF17957;PF13620;PF00704;
3.10.50.10;2.60.40.1120;3.20.20.80;2.60.40.10;
Glycosyl hydrolase 18 family, Chitinase class II subfamily
null
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24363341}. Note=Translocated across the cytoplasmic membrane via the Sec system, and across the outer membrane via the type IX secretion system (T9SS).
CATALYTIC ACTIVITY: Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14; Evidence={ECO:0000269|PubMed:24363341};
null
null
null
null
FUNCTION: Major extracellular chitinase, which is essential for chitin utilization. {ECO:0000269|PubMed:24363341}.
Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / JCM 8514 / NBRC 14942 / NCIMB 11054 / UW101) (Cytophaga johnsonae)
A5GFS8
VAPB_PIG
MAKVEQVLSLEPQHELKFRGPFTDVVTTNLKLGNPTDRNVCFKVKTTAPRRYCVRPNSGIIDAGASINVSVMLQPFDYDPNEKSKHKFMVQSMFAPADTSDMEAAWKEAKPEDLMDSKLRCVFELPAENDKPHDVEINKIISTTASKTETPVVSKALSSALDDTEVKKVMEECKRLQSEVQRLREENKQLKEEDGLRMRKPVLSNSPAPAPATPGKEEGLSTRLLALVVLFFIVGVIIGKIAL
null
null
endoplasmic reticulum membrane organization [GO:0090158]; endoplasmic reticulum unfolded protein response [GO:0030968]; endoplasmic reticulum-plasma membrane tethering [GO:0061817]; intracellular calcium ion homeostasis [GO:0006874]; IRE1-mediated unfolded protein response [GO:0036498]; positive regulation of viral genome replication [GO:0045070]
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; plasma membrane [GO:0005886]
beta-tubulin binding [GO:0048487]; enzyme binding [GO:0019899]; FFAT motif binding [GO:0033149]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]
PF00635;
2.60.40.10;
VAMP-associated protein (VAP) (TC 9.B.17) family
null
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O95292}; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:Q9P0L0}. Note=Present in mitochondria-associated membranes that are endoplasmic reticulum membrane regions closely apposed to the outer mitochondrial membrane. {ECO:0000250|UniProtKB:O95292}.
null
null
null
null
null
FUNCTION: Endoplasmic reticulum (ER)-anchored protein that mediates the formation of contact sites between the ER and endosomes via interaction with FFAT motif-containing proteins such as STARD3 or WDR44. Interacts with STARD3 in a FFAT motif phosphorylation dependent manner. Via interaction with WDR44 participates in neosynthesized protein export. Participates in the endoplasmic reticulum unfolded protein response (UPR) by inducing ERN1/IRE1 activity. Involved in cellular calcium homeostasis regulation. {ECO:0000250|UniProtKB:O95292}.
Sus scrofa (Pig)
A5GFW1
AURKA_PIG
MDKCKENCISGLKTTVPPGDGPKRVPVTQHFPAQHLPSANSGQAQRVLCPSNSSQRLPSHTQKLVSSHKPVQNLKQKQSQATSGPRPVSRPLSNTQQSEQPQPAAPGNNPEKEAASKQKNEESKKRQWALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKTQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRVYLILEYAPLGAVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPSSRRTTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFPDFVPEGARDLISRLLKHNPSHRPTLKEVLEHPWITANSKPASSHKKESTSKQP
2.7.11.1
null
cell division [GO:0051301]; cilium disassembly [GO:0061523]; meiotic spindle organization [GO:0000212]; mitotic centrosome separation [GO:0007100]; mitotic spindle organization [GO:0007052]; phosphorylation [GO:0016310]; positive regulation of meiotic cell cycle process involved in oocyte maturation [GO:1904146]; positive regulation of mitotic cell cycle [GO:0045931]; positive regulation of translation [GO:0045727]; regulation of cytokinesis [GO:0032465]
basolateral plasma membrane [GO:0016323]; centriole [GO:0005814]; centrosome [GO:0005813]; chromosome passenger complex [GO:0032133]; ciliary basal body [GO:0036064]; cytoplasm [GO:0005737]; kinetochore [GO:0000776]; mitotic spindle pole [GO:0097431]; neuron projection [GO:0043005]; spindle microtubule [GO:0005876]; spindle midzone [GO:0051233]; spindle pole [GO:0000922]; spindle pole centrosome [GO:0031616]
ATP binding [GO:0005524]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
PF00069;
1.10.510.10;
Protein kinase superfamily, Ser/Thr protein kinase family, Aurora subfamily
PTM: Activated by phosphorylation at Thr-288; this brings about a change in the conformation of the activation segment (By similarity). Phosphorylation at Thr-288 varies during the cell cycle and is highest during M phase (By similarity). Autophosphorylated at Thr-288 upon TPX2 binding (By similarity). Thr-288 can be phosphorylated by several kinases, including PAK and PKA (By similarity). Protein phosphatase type 1 (PP1) binds AURKA and inhibits its activity by dephosphorylating Thr-288 during mitosis (By similarity). Phosphorylation at Ser-342 decreases the kinase activity (By similarity). PPP2CA controls degradation by dephosphorylating Ser-51 at the end of mitosis (By similarity). {ECO:0000250|UniProtKB:O14965}.; PTM: Ubiquitinated by CHFR, leading to its degradation by the proteasome (By similarity). Ubiquitinated by the anaphase-promoting complex (APC), leading to its degradation by the proteasome (By similarity). Ubiquitinated by the E3 ubiquitin-protein ligase complex SCF(FBXL7) during mitosis, leading to its degradation by the proteasome (By similarity). Ubiquitinated by the CUL3-KLHL18 ligase leading to its activation at the centrosome which is required for initiating mitotic entry (By similarity). Ubiquitination mediated by CUL3-KLHL18 ligase does not lead to its degradation by the proteasome (By similarity). {ECO:0000250|UniProtKB:O14965, ECO:0000250|UniProtKB:P97477}.
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:O14965}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:O14965}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:P97477}. Cell projection, neuron projection {ECO:0000250|UniProtKB:P97477}. Cell projection, cilium {ECO:0000250|UniProtKB:O14965}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:P97477}. Basolateral cell membrane {ECO:0000250|UniProtKB:F1PNY0}. Note=Detected at the neurite hillock in developing neurons. Localizes at the centrosome in mitotic cells from early prophase until telophase, but also localizes to the spindle pole MTs from prophase to anaphase. Moves to the midbody during both telophase and cytokinesis. Associates with both the pericentriolar material (PCM) and centrioles. Colocalized with SIRT2 at centrosome. The localization to the spindle poles is regulated by AAAS (By similarity). {ECO:0000250|UniProtKB:O14965, ECO:0000250|UniProtKB:P97477}.
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:O14965}; 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:O14965};
null
null
null
null
FUNCTION: Mitotic serine/threonine kinase that contributes to the regulation of cell cycle progression (By similarity). Associates with the centrosome and the spindle microtubules during mitosis and plays a critical role in various mitotic events including the establishment of mitotic spindle, centrosome duplication, centrosome separation as well as maturation, chromosomal alignment, spindle assembly checkpoint, and cytokinesis (By similarity). Required for normal spindle positioning during mitosis and for the localization of NUMA1 and DCTN1 to the cell cortex during metaphase (By similarity). Required for initial activation of CDK1 at centrosomes (By similarity). Phosphorylates numerous target proteins, including ARHGEF2, BORA, BRCA1, CDC25B, DLGP5, HDAC6, KIF2A, LATS2, NDEL1, PARD3, PPP1R2, PLK1, RASSF1, TACC3, p53/TP53 and TPX2 (By similarity). Regulates KIF2A tubulin depolymerase activity (By similarity). Required for normal axon formation (By similarity). Plays a role in microtubule remodeling during neurite extension (By similarity). Important for microtubule formation and/or stabilization (By similarity). Also acts as a key regulatory component of the p53/TP53 pathway, and particularly the checkpoint-response pathways critical for oncogenic transformation of cells, by phosphorylating and destabilizing p53/TP53 (By similarity). Phosphorylates its own inhibitors, the protein phosphatase type 1 (PP1) isoforms, to inhibit their activity (By similarity). Inhibits cilia outgrowth (By similarity). Required for cilia disassembly via phosphorylation of HDAC6 and subsequent deacetylation of alpha-tubulin (By similarity). Regulates protein levels of the anti-apoptosis protein BIRC5 by suppressing the expression of the SCF(FBXL7) E3 ubiquitin-protein ligase substrate adapter FBXL7 through the phosphorylation of the transcription factor FOXP1 (By similarity). {ECO:0000250|UniProtKB:A0A8I3S724, ECO:0000250|UniProtKB:O14965}.
Sus scrofa (Pig)
A5GFZ6
MOCS3_PIG
MAAREEVLALQAEVARREEELSSLKHRLAAALLAEQESERLLPVSPLPPKAALSQDEILRYSRQLVLPELGVQGQLRLATASVLIVGCGGLGCPLAQYLAAAGVGRLGLVDYDVVEVSNLARQVLHGEALAGQAKVFSAAASLRRLNSAVECVPYAQALTPATALDLVRRYDVVADCSDNVPTRYLVNDACVLAGRPLVSASALRFEGQITVYHYGGGPCYRCVFPQPPPAETVTNCADGGVLGVVTGVLGCLQALEVLKIAAGLGPSYSGSLLLFDALRGLFRRIQLRRRRPDCAACGERPTVTELQDYEGFCGSSATDKCRSLQLLSPEERVSVIDYKRLLDSGSPHLLLDVRPQVEVDICRLPHALHIPLKHLERRDAESLKLLGEAIREGKQGTQEGASLPIYVICKLGNDSQKAVKILQSLPDLDSLLVQDVVGGLMAWAAKVDGTFPQY
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};
Mo-molybdopterin cofactor biosynthetic process [GO:0006777]; 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]
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}.
Sus scrofa (Pig)