Datasets:
Synthyra
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Dataset card Data Studio Files Community
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Sequence
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35.2k
EC number
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118
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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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1.75k
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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
O05131
PBPA_NEIGO
MIKKILTTCFGLFFGFCVFGVGLVAIAILVTYPKLPSLDSLQHYQPKMPLTIYSADGEVIGMYGEQRREFTKIGDFPEVLRNAVIAAEDKRFYRHWGVDVWGVARAAVGNVVSGSVQSGASTITQQVAKNFYLSSEKTFTRKFNEVLLAYKIEQSLSKDKILELYFNQIYLGQRAYGFASAAQIYFNKNVRDLTLAEAAMLAGLPKAPSAYNPIVNPERAKLRQKYILNNMLEEKMITVQQRDQALNEELHYERFVRKIDQSALYVAEMVRRELYEKYGEDAYTQGFKVYTTVRTDHQKAATEALRKALRNFDRGSSYRGAENYIDLSKSEDVEETVSQYLSGLYTVDKMVPAVVLDVTKKKNVVIQLPGGRRVALDRRALGFAARAVDNEKMGEDRIRRGAVIRVKNNGGRWAVVQEPLLQGALVSLDAKTGAVRALVGGYDFHSKTFNRAVQAMRQPGSTFKPFVYSAALSKGMTASTVVNDAPISLPGKGPNGSVWTPKNSDGRYSGYITLRQALTASKNMVSIRILMSIGVGYAQQYIRRFGFRPSELPASLSMALGTGETTPLKVAEAYSVFANGGYRVSSHVIDKIYDRDGRLRAQMQPLVAGQNAPQAIDPRNAYIMYKIMQDVVRVGTARGAAALGRTDIAGKTGTTNDNKDAWFVGFNPDVVTAVYIGFDKPKSMGRAGYGGTIAVPVWVDYMRFALKGKQGKGMKMPEGVVSSNGEYYMKERMVTDPGLMLDNSGIAPQPSRRAKEDDEAAVENEQQGRSDETRQDVQETPVLPSNTDSKQQQLDSLF
2.4.99.28; 3.4.16.4
null
cell wall organization [GO:0071555]; peptidoglycan biosynthetic process [GO:0009252]; proteolysis [GO:0006508]; regulation of cell shape [GO:0008360]; response to antibiotic [GO:0046677]
plasma membrane [GO:0005886]
penicillin binding [GO:0008658]; peptidoglycan glycosyltransferase activity [GO:0008955]; serine-type D-Ala-D-Ala carboxypeptidase activity [GO:0009002]
PF17092;PF00912;PF00905;
1.10.3810.10;3.40.710.10;
Glycosyltransferase 51 family; Transpeptidase family
null
SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+); Xref=Rhea:RHEA:23708, Rhea:RHEA-COMP:9602, Rhea:RHEA-COMP:9603, ChEBI:CHEBI:15378, ChEBI:CHEBI:58405, ChEBI:CHEBI:60033, ChEBI:CHEBI:78435; EC=2.4.99.28; Evidence={ECO:0000250|UniProtKB:P02918}; CATALYTIC ACTIVITY: Reaction=Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.; EC=3.4.16.4; Evidence={ECO:0000250|UniProtKB:P02918};
null
PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
null
null
FUNCTION: Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits). Essential for cell wall synthesis. {ECO:0000250}.
Neisseria gonorrhoeae
O05207
TOP6B_SACSH
MSAKEKFTSLSPAEFFKRNPELAGFPNPARALYQTVRELIENSLDATDVHGILPNIKITIDLIDDARQIYKVNVVDNGIGIPPQEVPNAFGRVLYSSKYVNRQTRGMYGLGVKAAVLYSQMHQDKPIEIETSPVNSKRIYTFKLKIDINKNEPIIVERGSVENTRGFHGTSVAISIPGDWPKAKSRIYEYIKRTYIITPYAEFIFKDPEGNVTYYPRLTNKIPKPPQEVKPHPYGVDREEIKILINNLKRDYTIKEFLVNEFQSIGDTTADKILELAGLKPNKKVKNLTEEEITRLVETFKKYEDFRSPSADSLSVIGEDLIELGLKKIFNPDFAASITRKPKAYQGHPFIVEAGVAFGGSIPVGEEPIVLRYANKIPLIYDEKSDVIWKVVEELDWKRYGIESDQYQMVVMVHLCSTKIPYKSAGKESIAEVEDIEKEIKNALMEVARKLKQYLSEKRKEQEAKKKLLAYLKYIPEVSRSLATFLASGNKELVSKYQNEISEGLFKLISKKLDLINIEEYRKVYRVDSE
5.6.2.2
null
DNA topological change [GO:0006265]; DNA unwinding involved in DNA replication [GO:0006268]
DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex [GO:0009330]
ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity [GO:0003918]; identical protein binding [GO:0042802]
PF02518;PF05833;PF09239;
null
TOP6B family
null
null
CATALYTIC ACTIVITY: Reaction=ATP-dependent breakage, passage and rejoining of double-stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000255|HAMAP-Rule:MF_00322, ECO:0000269|PubMed:16920739};
null
null
null
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 70-80 degrees Celsius. {ECO:0000269|PubMed:7961685};
FUNCTION: Relaxes both positive and negative supercoils and exhibits a strong decatenase and unknotting activity; it cannot introduce DNA supercoils (PubMed:7961685). ATP is absolutely required for DNA cleavage; the nonhydrolyzable analog AMP-PNP generates nicked or linear products from a supercoiled dsDNA substrate. Generates staggered two-nucleotide long 5' overhangs. The enzyme is covalently attached transiently to the 5'-ends of the cleaved strands (PubMed:11485995). {ECO:0000269|PubMed:11485995, ECO:0000269|PubMed:7961685}.
Saccharolobus shibatae (strain ATCC 51178 / DSM 5389 / JCM 8931 / NBRC 15437 / B12) (Sulfolobus shibatae)
O05208
TOP6A_SACSH
MSSEFISKVDKEARRKAANILRDKFLNLVEQLKKGEPLVMEIPMRTLSNAIYDEKRKLLLLGEKKLRRNFLDLNEAKRFMQTVLMASIIYDALVSDEYPTIRDLYYRGKHSLLLKSIEGNKIVSEENTWDEQKESDSVIVDIEVFTSLLREEMLILSKEKGKVVGNLRIRSGNDVIDLSKTGHGAYAIEPTPDLIDFIDVDAEFVLVVEKDAVFQQLHRAGFWKQYKSILITSAGQPDRATRRFVRRLNEELKLPVYILTDADPYGWYIFSVFRIGSISLSYESERLATPDAKFLGVSMGDIFGNSRKKPYLSEAERKNYIIKAKDADIKRAEEIKNYEWFKTKAWQEEINTFLQRKAKLEIEAMASKGLKFLAFQYIPEKITNKDYIA
5.6.2.2
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00132, ECO:0000269|PubMed:11485995, ECO:0000269|PubMed:7961685};
DNA topological change [GO:0006265]; DNA unwinding involved in DNA replication [GO:0006268]
chromosome [GO:0005694]; DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex [GO:0009330]
ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity [GO:0003918]; magnesium ion binding [GO:0000287]
PF21180;PF20768;PF04406;
3.40.1360.10;1.10.10.10;
TOP6A family
null
null
CATALYTIC ACTIVITY: Reaction=ATP-dependent breakage, passage and rejoining of double-stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000255|HAMAP-Rule:MF_00132, ECO:0000305|PubMed:7961685};
null
null
null
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 70-80 degrees Celsius. {ECO:0000269|PubMed:7961685};
FUNCTION: Relaxes both positive and negative supercoils and exhibits a strong decatenase and unknotting activity; it cannot introduce DNA supercoils (PubMed:7961685). ATP is absolutely required for DNA cleavage; the nonhydrolyzable analog AMP-PNP generates nicked or linear products from a supercoiled dsDNA substrate. Generates staggered two-nucleotide long 5' overhangs. The enzyme is covalently attached transiently to the 5'-ends of the cleaved strands (PubMed:11485995). {ECO:0000269|PubMed:11485995, ECO:0000269|PubMed:7961685}.
Saccharolobus shibatae (strain ATCC 51178 / DSM 5389 / JCM 8931 / NBRC 15437 / B12) (Sulfolobus shibatae)
O05306
LOGH_MYCTU
MSAKIDITGDWTVAVYCAASPTHAELLELAAEVGAAIAGRGWTLVWGGGHVSAMGAVASAARACGGWTVGVIPKMLVYRELADHDADELIVTDTMWERKQIMEDRSDAFIVLPGGVGTLDELFDAWTDGYLGTHDKPIVMVDPWGHFDGLRAWLNGLLDTGYVSPTAMERLVVVDNVKDALRACAPS
3.2.2.n1
null
cytokinin biosynthetic process [GO:0009691]
cytosol [GO:0005829]
cytokinin riboside 5'-monophosphate phosphoribohydrolase activity [GO:0102682]; hydrolase activity, hydrolyzing N-glycosyl compounds [GO:0016799]
PF03641;
3.40.50.450;
LOG family
PTM: Pupylated at Lys-74 by the prokaryotic ubiquitin-like protein Pup, which leads to its degradation by the proteasome. The proteasomal control of cytokinin synthesis is essential to protect M.tuberculosis against host-produced NO. {ECO:0000269|PubMed:25728768}.
null
CATALYTIC ACTIVITY: Reaction=H2O + N(6)-(dimethylallyl)adenosine 5'-phosphate = D-ribose 5-phosphate + N(6)-dimethylallyladenine; Xref=Rhea:RHEA:48560, ChEBI:CHEBI:15377, ChEBI:CHEBI:17660, ChEBI:CHEBI:57526, ChEBI:CHEBI:78346; EC=3.2.2.n1; Evidence={ECO:0000269|PubMed:25728768}; CATALYTIC ACTIVITY: Reaction=9-ribosyl-trans-zeatin 5'-phosphate + H2O = D-ribose 5-phosphate + trans-zeatin; Xref=Rhea:RHEA:48564, ChEBI:CHEBI:15377, ChEBI:CHEBI:16522, ChEBI:CHEBI:78346, ChEBI:CHEBI:87947; EC=3.2.2.n1; Evidence={ECO:0000269|PubMed:25728768};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5.59 uM for isopentenyladenine riboside monophosphate (iPRMP) {ECO:0000269|PubMed:25728768}; KM=73.06 uM for AMP {ECO:0000269|PubMed:25728768}; Note=kcat is 434.3 min(-1) for the hydrolysis of iPRMP. kcat is 2.27 min(-1) for the hydrolysis of AMP. {ECO:0000269|PubMed:25728768};
null
null
null
FUNCTION: Catalyzes the hydrolytic removal of ribose 5'-monophosphate from nitrogen N6-modified adenosines, the final step of bioactive cytokinin synthesis. Is involved in the synthesis of isopentenyladenine (iP) and 2-methylthio-iP (2MeS-iP), the most abundant cytokinins detected in M.tuberculosis lysates and supernatants. Is also able to convert trans-zeatin-riboside monophosphate (tZRMP) to trans-zeatin (tZ) in vitro; however, it may not be involved in the biosynthesis of this minor cytokinin in vivo. Accumulation of Rv1205 sensitizes M.tuberculosis to nitric oxide since cytokinin breakdown products synergize with NO to kill M.tuberculosis. Shows a slow AMP hydrolase activity, but is not able to hydrolyze ATP. Displays no lysine decarboxylase (LDC) activity (L-lysine conversion to cadaverine). {ECO:0000269|PubMed:25728768}.
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
O05307
FAC6_MYCTU
MSDYYGGAHTTVRLIDLATRMPRVLADTPVIVRGAMTGLLARPNSKASIGTVFQDRAARYGDRVFLKFGDQQLTYRDANATANRYAAVLAARGVGPGDVVGIMLRNSPSTVLAMLATVKCGAIAGMLNYHQRGEVLAHSLGLLDAKVLIAESDLVSAVAECGASRGRVAGDVLTVEDVERFATTAPATNPASASAVQAKDTAFYIFTSGTTGFPKASVMTHHRWLRALAVFGGMGLRLKGSDTLYSCLPLYHNNALTVAVSSVINSGATLALGKSFSASRFWDEVIANRATAFVYIGEICRYLLNQPAKPTDRAHQVRVICGNGLRPEIWDEFTTRFGVARVCEFYAASEGNSAFINIFNVPRTAGVSPMPLAFVEYDLDTGDPLRDASGRVRRVPDGEPGLLLSRVNRLQPFDGYTDPVASEKKLVRNAFRDGDCWFNTGDVMSPQGMGHAAFVDRLGDTFRWKGENVATTQVEAALASDQTVEECTVYGVQIPRTGGRAGMAAITLRAGAEFDGQALARTVYGHLPGYALPLFVRVVGSLAHTTTFKSRKVELRNQAYGADIEDPLYVLAGPDEGYVPYYAEYPEEVSLGRRPQG
6.2.1.2; 6.2.1.3
null
long-chain fatty acid import into cell [GO:0044539]; long-chain fatty acid metabolic process [GO:0001676]; triglyceride homeostasis [GO:0070328]; very long-chain fatty acid metabolic process [GO:0000038]
lipid droplet [GO:0005811]; peroxisome [GO:0005777]; plasma membrane [GO:0005886]
ATP binding [GO:0005524]; butyrate-CoA ligase activity [GO:0047760]; fatty acid transmembrane transporter activity [GO:0015245]; long-chain fatty acid transporter activity [GO:0005324]; long-chain fatty acid-CoA ligase activity [GO:0004467]; medium-chain fatty acid-CoA ligase activity [GO:0031956]; very long-chain fatty acid-CoA ligase activity [GO:0031957]
PF00501;PF13193;
3.30.300.30;3.40.50.12780;
ATP-dependent AMP-binding enzyme family
null
null
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:15984864, ECO:0000269|PubMed:19182784}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48341; Evidence={ECO:0000269|PubMed:15984864, ECO:0000269|PubMed:19182784}; CATALYTIC ACTIVITY: Reaction=a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:15421, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57560, ChEBI:CHEBI:83139, ChEBI:CHEBI:456215; EC=6.2.1.3; Evidence={ECO:0000269|PubMed:15984864, ECO:0000269|PubMed:19182784, ECO:0000269|PubMed:25490545}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15422; Evidence={ECO:0000269|PubMed:15984864, ECO:0000269|PubMed:19182784, ECO:0000269|PubMed:25490545}; CATALYTIC ACTIVITY: Reaction=ATP + CoA + hexanoate = AMP + diphosphate + hexanoyl-CoA; Xref=Rhea:RHEA:43740, ChEBI:CHEBI:17120, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:62620, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:15984864, ECO:0000269|PubMed:19182784}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43741; Evidence={ECO:0000269|PubMed:15984864, ECO:0000269|PubMed:19182784}; CATALYTIC ACTIVITY: Reaction=ATP + CoA + octanoate = AMP + diphosphate + octanoyl-CoA; Xref=Rhea:RHEA:33631, ChEBI:CHEBI:25646, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57386, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:15984864}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33632; Evidence={ECO:0000269|PubMed:15984864}; CATALYTIC ACTIVITY: Reaction=ATP + CoA + decanoate = AMP + decanoyl-CoA + diphosphate; Xref=Rhea:RHEA:33627, ChEBI:CHEBI:27689, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:61430, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:15984864}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33628; Evidence={ECO:0000269|PubMed:15984864}; CATALYTIC ACTIVITY: Reaction=ATP + CoA + dodecanoate = AMP + diphosphate + dodecanoyl-CoA; Xref=Rhea:RHEA:33623, ChEBI:CHEBI:18262, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:15984864, ECO:0000269|PubMed:19182784}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33624; Evidence={ECO:0000269|PubMed:15984864, ECO:0000269|PubMed:19182784}; CATALYTIC ACTIVITY: Reaction=ATP + CoA + tetradecanoate = AMP + diphosphate + tetradecanoyl-CoA; Xref=Rhea:RHEA:33619, ChEBI:CHEBI:30616, ChEBI:CHEBI:30807, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:15984864}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33620; Evidence={ECO:0000269|PubMed:15984864}; CATALYTIC ACTIVITY: Reaction=ATP + CoA + hexadecanoate = AMP + diphosphate + hexadecanoyl-CoA; Xref=Rhea:RHEA:30751, ChEBI:CHEBI:7896, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:15984864, ECO:0000269|PubMed:19182784, ECO:0000269|PubMed:25490545}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30752; Evidence={ECO:0000269|PubMed:15984864, ECO:0000269|PubMed:19182784, ECO:0000269|PubMed:25490545}; CATALYTIC ACTIVITY: Reaction=ATP + CoA + octadecanoate = AMP + diphosphate + octadecanoyl-CoA; Xref=Rhea:RHEA:33615, ChEBI:CHEBI:25629, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:15984864, ECO:0000269|PubMed:25490545}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33616; Evidence={ECO:0000269|PubMed:15984864, ECO:0000269|PubMed:25490545}; CATALYTIC ACTIVITY: Reaction=9-decenoate + ATP + CoA = 9-decenoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:44228, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:33163, ChEBI:CHEBI:57287, ChEBI:CHEBI:84214, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:15984864}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44229; Evidence={ECO:0000269|PubMed:15984864}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoate + ATP + CoA = (9Z)-octadecenoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:33607, ChEBI:CHEBI:30616, ChEBI:CHEBI:30823, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:15984864, ECO:0000269|PubMed:25490545}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33608; Evidence={ECO:0000269|PubMed:15984864, ECO:0000269|PubMed:25490545}; CATALYTIC ACTIVITY: Reaction=2-hydroxyhexadecanoate + ATP + CoA = 2-hydroxyhexadecanoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:44204, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:65097, ChEBI:CHEBI:74115, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:15984864}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44205; Evidence={ECO:0000269|PubMed:15984864}; CATALYTIC ACTIVITY: Reaction=3-hydroxytetradecanoate + ATP + CoA = 3-hydroxytetradecanoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:44212, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:84197, ChEBI:CHEBI:84198, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:15984864}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44213; Evidence={ECO:0000269|PubMed:15984864}; CATALYTIC ACTIVITY: Reaction=12-hydroxyoctadecanoate + ATP + CoA = 12-hydroxyoctadecanoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:44216, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:84201, ChEBI:CHEBI:84202, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:15984864}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44217; Evidence={ECO:0000269|PubMed:15984864}; CATALYTIC ACTIVITY: Reaction=15-hydroxypentadecanoate + ATP + CoA = 15-hydroxypentadecanoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:44220, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:84203, ChEBI:CHEBI:84205, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:15984864}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44221; Evidence={ECO:0000269|PubMed:15984864}; CATALYTIC ACTIVITY: Reaction=16-hydroxyhexadecanoate + ATP + CoA = 16-hydroxyhexadecanoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:44224, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:55329, ChEBI:CHEBI:57287, ChEBI:CHEBI:84207, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:15984864}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44225; Evidence={ECO:0000269|PubMed:15984864}; CATALYTIC ACTIVITY: Reaction=2-methylhexadecanoate + ATP + CoA = 2-methylhexadecanoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:44192, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:84175, ChEBI:CHEBI:84182, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:15984864}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44193; Evidence={ECO:0000269|PubMed:15984864}; CATALYTIC ACTIVITY: Reaction=3-methylundecanoate + ATP + CoA = 3-methylundecanoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:44196, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:84183, ChEBI:CHEBI:84184, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:15984864}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44197; Evidence={ECO:0000269|PubMed:15984864}; CATALYTIC ACTIVITY: Reaction=12-methyltridecanoate + ATP + CoA = 12-methyltridecanoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:44208, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:84193, ChEBI:CHEBI:84195, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:15984864}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44209; Evidence={ECO:0000269|PubMed:15984864}; CATALYTIC ACTIVITY: Reaction=12-methyloctadecanoate + ATP + CoA = 12-methyloctadecanoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:44200, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:84176, ChEBI:CHEBI:84181, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:15984864}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44201; Evidence={ECO:0000269|PubMed:15984864};
null
null
null
null
FUNCTION: Catalyzes the activation of medium/long-chain fatty acids as acyl-coenzyme A (acyl-CoA) (PubMed:15984864, PubMed:19182784, PubMed:25490545). May play a role in the uptake of fatty acids by trapping them metabolically as CoA esters (PubMed:25490545). May also play an important role in the channeling of fatty acids into triacylglycerol (TAG) for use by Mycobacterium during its dormancy (PubMed:25490545). {ECO:0000269|PubMed:15984864, ECO:0000269|PubMed:19182784, ECO:0000269|PubMed:25490545}.
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
O05394
MCCB_BACSU
MKKKTLMIHGGITGDEKTGAVSVPIYQVSTYKQPKAGQHTGYEYSRTANPTRTALEALVTELESGEAGYAFSSGMAAITAVMMLFNSGDHVVLTDDVYGGTYRVMTKVLNRLGIESTFVDTSSREEVEKAIRPNTKAIYIETPTNPLLKITDLTLMADIAKKAGVLLIVDNTFNTPYFQQPLTLGADIVLHSATKYLGGHSDVVGGLVVTASKELGEELHFVQNSTGGVLGPQDSWLLMRGIKTLGLRMEAIDQNARKIASFLENHPAVQTLYYPGSSNHPGHELAKTQGAGFGGMISFDIGSEERVDAFLGNLKLFTIAESLGAVESLISVPARMTHASIPRERRLELGITDGLIRISVGIEDAEDLLEDIGQALENI
4.4.1.1; 4.4.1.2
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250};
cysteine biosynthetic process via cystathionine [GO:0019343]; homocysteine catabolic process [GO:0043418]; positive regulation of cell population proliferation [GO:0008284]; transsulfuration [GO:0019346]
cytoplasm [GO:0005737]
cystathionine gamma-lyase activity [GO:0004123]; cystathionine gamma-synthase activity [GO:0003962]; homocysteine desulfhydrase activity [GO:0047982]; L-cysteine desulfhydrase activity [GO:0080146]; L-cystine L-cysteine-lyase (deaminating) [GO:0044540]; pyridoxal phosphate binding [GO:0030170]
PF01053;
3.90.1150.10;3.40.640.10;
Trans-sulfuration enzymes family
null
null
CATALYTIC ACTIVITY: Reaction=H2O + L,L-cystathionine = 2-oxobutanoate + L-cysteine + NH4(+); Xref=Rhea:RHEA:14005, ChEBI:CHEBI:15377, ChEBI:CHEBI:16763, ChEBI:CHEBI:28938, ChEBI:CHEBI:35235, ChEBI:CHEBI:58161; EC=4.4.1.1; Evidence={ECO:0000269|PubMed:17056751}; CATALYTIC ACTIVITY: Reaction=H2O + L-homocysteine = 2-oxobutanoate + H(+) + hydrogen sulfide + NH4(+); Xref=Rhea:RHEA:14501, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16763, ChEBI:CHEBI:28938, ChEBI:CHEBI:29919, ChEBI:CHEBI:58199; EC=4.4.1.2; Evidence={ECO:0000269|PubMed:17056751};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3 mM for cystathionine {ECO:0000269|PubMed:17056751}; Vmax=2 umol/min/mg enzyme for cystathionine gamma-lyase reaction {ECO:0000269|PubMed:17056751};
null
null
null
FUNCTION: Catalyzes the conversion of cystathionine to cysteine, and homocysteine to sulfide. {ECO:0000269|PubMed:17056751}.
Bacillus subtilis (strain 168)
O05442
CPNT_MYCTU
MAPLAVDPAALDSAGGAVVAAGAGLGAVISSLTAALAGCAGMAGDDPAGAVFGRSYDGSAAALVQAMSVARNGLCNLGDGVRMSAHNYSLAEAMSDVAGRAAPLPAPPPSGCVGVGAPPSAVGGGGGAPKGWGWVAPYIGMIWPNGDSTKLRAAAVAWRSAGTQFALTEIQSTAGPMGVIRAQQLPEAGLIESAFADAYASTTAVVGQCHQLAAQLDAYAARIDAVHAAVLDLLARICDPLTGIKEVWEFLTDQDEDEIQRIAHDIAVVVDQFSGEVDALAAEITAVVSHAEAVITAMADHAGKQWDRFLHSNPVGVVIDGTGQQLKGFGEEAFGMAKDSWDLGPLRASIDPFGWYRSWEEMLTGMAPLAGLGGENAPGVVESWKQFGKSLIHWDEWTTNPNEALGKTVFDAATLALPGGPLSKLGSKGRDILAGVRGLKERLEPTTPHLEPPATPPRPGPQPPRIEPPESGHPAPAPAAKPAPVPANGPLPHSPTESKPPPVDRPAEPVAPSSASAGQPRVSAATTPGTHVPHGLPQPGEHVPAQAPPATTLLGGPPVESAPATAHQPQWATTPAAPAAAPHSTPGGVHSTESGPHGRSLSAHGSEPTHDGASHGSGHGSGSEPPGLHAPHREQQLAMHSNEPAGEGWHRLSDEAVDPQYGEPLSRHWDFTDNPADRSRINPVVAQLMEDPNAPFGRDPQGQPYTQERYQERFNSVGPWGQQYSNFPPNNGAVPGTRIAYTNLEKFLSDYGPQLDRIGGDQGKYLAIMEHGRPASWEQRALHVTSLRDPYHAYTIDWLPEGWFIEVSEVAPGCGQPGGSIQVRIFDHQNEMRKVEELIRRGVLRQ
3.2.2.5
null
killing by symbiont of host cells [GO:0001907]; monoatomic ion transport [GO:0006811]
cell outer membrane [GO:0009279]; cell surface [GO:0009986]; cytosol [GO:0005829]; extracellular region [GO:0005576]; host cell cytosol [GO:0044164]; peptidoglycan-based cell wall [GO:0009274]; pore complex [GO:0046930]
NAD+ nucleosidase activity [GO:0003953]; NAD+ nucleotidase, cyclic ADP-ribose generating [GO:0061809]; NADP+ nucleosidase activity [GO:0050135]; porin activity [GO:0015288]; toxin activity [GO:0090729]
PF14021;
null
null
PTM: The C-terminal toxic domain is cleaved, probably after integration of CpnT into the outer membrane. {ECO:0000269|PubMed:24753609}.
SUBCELLULAR LOCATION: [N-terminal channel domain]: Cell outer membrane {ECO:0000269|PubMed:24753609}.; SUBCELLULAR LOCATION: [Tuberculosis necrotizing toxin]: Secreted {ECO:0000269|PubMed:24753609}. Cell surface {ECO:0000269|PubMed:24753609}. Host cytoplasm, host cytosol {ECO:0000269|PubMed:26237511}. Note=Secreted into the cytosol of infected macrophages while the bacteria are still confined to the phagosome. Access to the macrophage cytosol depends on the ESX-1 / type VII secretion system (T7SS). {ECO:0000269|PubMed:26237511}.
CATALYTIC ACTIVITY: Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide; Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.5; Evidence={ECO:0000269|PubMed:26237511};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=614 uM for NAD(+) {ECO:0000269|PubMed:26237511}; Note=kcat is 52 sec(-1). {ECO:0000269|PubMed:26237511};
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5. {ECO:0000269|PubMed:26237511};
null
FUNCTION: Has a dual function in uptake of nutrients and induction of host cell death. The N-terminal domain (NTD) forms an outer membrane channel and is used for uptake of nutrients across the outer membrane. The secreted C-terminal toxic domain (TNT) acts as a glycohydrolase, which hydrolyzes the essential cellular coenzyme NAD(+) in the cytosol of infected macrophages, leading to necrotic host cell death. Both functions are required for survival, replication and cytotoxicity of M.tuberculosis in macrophages. {ECO:0000269|PubMed:24753609, ECO:0000269|PubMed:26237511}.
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
O05461
MYCP1_MYCTU
MHRIFLITVALALLTASPASAITPPPIDPGALPPDVTGPDQPTEQRVLCASPTTLPGSGFHDPPWSNTYLGVADAHKFATGAGVTVAVIDTGVDASPRVPAEPGGDFVDQAGNGLSDCDAHGTLTASIIAGRPAPTDGFVGVAPDARLLSLRQTSEAFEPVGSQANPNDPNATPAAGSIRSLARAVVHAANLGVGVINISEAACYKVSRPIDETSLGASIDYAVNVKGVVVVVAAGNTGGDCVQNPAPDPSTPGDPRGWNNVQTVVTPAWYAPLVLSVGGIGQTGMPSSFSMHGPWVDVAAPAENIVALGDTGEPVNALQGREGPVPIAGTSFAAAYVSGLAALLRQRFPDLTPAQIIHRITATARHPGGGVDDLVGAGVIDAVAALTWDIPPGPASAPYNVRRLPPPVVEPGPDRRPITAVALVAVGLTLALGLGALARRALSRR
3.4.21.-
null
modulation by symbiont of host process [GO:0044003]; protein processing [GO:0016485]; proteolysis [GO:0006508]; regulation of secretion [GO:0051046]
cell surface [GO:0009986]; extracellular space [GO:0005615]; membrane [GO:0016020]; plasma membrane [GO:0005886]
serine-type endopeptidase activity [GO:0004252]
PF00082;
3.40.50.200;
Peptidase S8 family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10974545, ECO:0000269|PubMed:12366866}; Single-pass membrane protein {ECO:0000255}. Note=Cell wall-associated. {ECO:0000269|PubMed:10974545, ECO:0000269|PubMed:12366866}.
null
null
null
null
null
FUNCTION: May play a dual role in regulation of ESX-1 secretion and virulence. Acts as a protease that cleaves EspB. Essential for ESX-1 function, required for early replication in macrophages and full virulence in mice. {ECO:0000269|PubMed:20227664}.
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
O05512
MANB_BACSU
MFKKHTISLLIIFLLASAVLAKPIEAHTVSPVNPNAQQTTKTVMNWLAHLPNRTENRVLSGAFGGYSHDTFSMAEADRIRSATGQSPAIYGCDYARGWLETANIEDSIDVSCNGDLMSYWKNGGIPQISLHLANPAFQSGHFKTPITNDQYKKILDSSTVEGKRLNAMLSKIADGLQELENQGVPVLFRPLHEMNGEWFWWGLTSYNQKDNERISLYKQLYKKIYHYMTDTRGLDHLIWVYSPDANRDFKTDFYPGASYVDIVGLDAYFQDAYSINGYDQLTALNKPFAFTEVGPQTANGSFDYSLFINAIKQKYPKTIYFLAWNDEWSAAVNKGASALYHDSWTLNKGEIWNGDSLTPIVE
3.2.1.78
null
polysaccharide catabolic process [GO:0000272]; substituted mannan metabolic process [GO:0006080]
extracellular region [GO:0005576]
mannan endo-1,4-beta-mannosidase activity [GO:0016985]
PF02156;
3.20.20.80;
Glycosyl hydrolase 26 family
null
SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:10658653}.
CATALYTIC ACTIVITY: Reaction=Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.; EC=3.2.1.78; Evidence={ECO:0000269|PubMed:19441796};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.7 mg/ml for glucomannan {ECO:0000269|PubMed:19441796}; KM=4.5 mg/ml for galactomannan {ECO:0000269|PubMed:19441796}; Note=kcat is 330 min(-1) for mannanase activity with galactomannan as substrate. kcat is 350 min(-1) for mannanase activity with glucomannan as substrate. {ECO:0000269|PubMed:19441796};
null
null
null
FUNCTION: Involved in the degradation of glucomannan. Catalyzes the endo hydrolysis of beta-1,4-linked mannan, galactomannan and glucomannan. {ECO:0000269|PubMed:18177310, ECO:0000269|PubMed:19441796}.
Bacillus subtilis (strain 168)
O05542
ADHA_GLUOX
MTSGLLTPIKVTKKRLLSCAAALAFSAAVPVAFAQEDTGTAITSSDNGGHPGDWLSYGRSYSEQRYSPLDQINTENVGKLKLAWHYDLDTNRGQEGTPLIVNGVMYATTNWSKMKALDAATGKLLWSYDPKVPGNIADRGCCDTVSRGAAYWNGKVYFGTFDGRLIALDAKTGKLVWSVYTIPKEAQLGHQRSYTVDGAPRIAKGKVLIGNGGAEFGARGFVSAFDAETGKLDWRFFTVPNPENKPDGAASDDILMSKAYPTWGKNGAWKQQGGGGTVWDSLVYDPVTDLVYLGVGNGSPWNYKFRSEGKGDNLFLGSIVAINPDTGKYVWHFQETPMDEWDYTSVQQIMTLDMPVNGEMRHVIVHAPKNGFFYIIDAKTGKFITGKPYTYENWANGLDPVTGRPNYVPDALWTLTGKPWLGIPGELGGHNFAAMAYSPKTKLVYIPAQQIPLLYDGQKGGFKAYHDAWNLGLDMNKIGLFDDNDPEHVAAKKDFLKVLKGWTVAWDPEKMAPAFTINHKGPWNGGLLATAGNVIFQGLANGEFHAYDATNGNDLYSFPAQSAIIAPPVTYTANGKQYVAVEVGWGGIYPFLYGGVARTSGWTVNHSRVIAFSLDGKDSLPPKNELGFTPVKPVPTYDEARQKDGYFMYQTFCSACHGDNAISGGVLPDLRWSGAPRGRESFYKLVGRGALTAYGMDRFDTSMTPEQIEDIRNFIVKRANESYDDEVKARENSTGVPNDQFLNVPQSTADVPTADHP
1.1.5.5
COFACTOR: Name=pyrroloquinoline quinone; Xref=ChEBI:CHEBI:58442; Evidence={ECO:0000269|PubMed:8617755, ECO:0000305|PubMed:9055427}; Note=Binds 1 PQQ group per subunit. {ECO:0000269|PubMed:8617755}; COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000305|PubMed:8617755}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:Q8GR64}; COFACTOR: Name=heme c; Xref=ChEBI:CHEBI:61717; Evidence={ECO:0000269|PubMed:8617755, ECO:0000305|PubMed:9055427}; Note=Binds 1 heme c group covalently per subunit. {ECO:0000269|PubMed:8617755};
null
outer membrane-bounded periplasmic space [GO:0030288]; plasma membrane [GO:0005886]; respirasome [GO:0070469]
calcium ion binding [GO:0005509]; electron transfer activity [GO:0009055]; heme binding [GO:0020037]; oxidoreductase activity, acting on CH-OH group of donors [GO:0016614]
PF13442;PF01011;PF13360;
1.10.760.10;2.140.10.10;
Bacterial PQQ dehydrogenase family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Periplasmic side {ECO:0000305}.
CATALYTIC ACTIVITY: Reaction=a ubiquinone + ethanol = a ubiquinol + acetaldehyde; Xref=Rhea:RHEA:26442, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15343, ChEBI:CHEBI:16236, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976; EC=1.1.5.5; Evidence={ECO:0000269|PubMed:7592433, ECO:0000269|PubMed:8617755, ECO:0000269|PubMed:9878716};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=7.7 uM for ubiquinone-2 (for ubiquinone reduction activity in inactive ADH at pH 5) {ECO:0000269|PubMed:9878716}; KM=8.4 uM for ubiquinone-2 (for ubiquinone reduction activity in active ADH at pH 5) {ECO:0000269|PubMed:9878716}; KM=13 uM for ubiquinol-2 (for ubiquinol oxidation activity in inactive ADH at pH 5) {ECO:0000269|PubMed:9878716}; KM=32 uM for ethanol (for ubiquinone reduction activity in active ADH at pH 4.5) {ECO:0000269|PubMed:8617755}; KM=36 uM for ubiquinol-2 (for ubiquinol oxidation activity in active ADH at pH 5) {ECO:0000269|PubMed:9878716}; KM=40 uM for ethanol (for ubiquinone reduction activity in inactive ADH at pH 4.5) {ECO:0000269|PubMed:8617755}; KM=170 uM for ferricyanide (for ubiquinol oxidation activity in active ADH at pH 5) {ECO:0000269|PubMed:9878716}; KM=200 uM for ferricyanide (for ubiquinol oxidation activity in inactive ADH at pH 5) {ECO:0000269|PubMed:9878716}; Vmax=175 umol/min/mg enzyme toward ubiquinol-2 (for ubiquinol oxidation activity in inactive ADH at pH 5) {ECO:0000269|PubMed:9878716}; Vmax=167 umol/min/mg enzyme toward ferricyanide (for ubiquinol oxidation activity in inactive ADH at pH 5) {ECO:0000269|PubMed:9878716}; Vmax=104 umol/min/mg enzyme toward ubiquinol-2 (for ubiquinol oxidation activity in active ADH at pH 5) {ECO:0000269|PubMed:9878716}; Vmax=81 umol/min/mg enzyme toward ferricyanide (for ubiquinol oxidation activity in active ADH at pH 5) {ECO:0000269|PubMed:9878716}; Vmax=71 umol/min/mg enzyme toward ethanol (for ubiquinone reduction activity in active ADH at pH 4.5) {ECO:0000269|PubMed:8617755}; Vmax=54 umol/min/mg enzyme toward ubiquinone-2 (for ubiquinone reduction activity in active ADH at pH 5) {ECO:0000269|PubMed:9878716}; Vmax=7.1 umol/min/mg enzyme toward ethanol (for ubiquinone reduction activity in inactive ADH at pH 4.5) {ECO:0000269|PubMed:8617755}; Vmax=2 umol/min/mg enzyme toward ubiquinone-2 (for ubiquinone reduction activity in inactive ADH at pH 5) {ECO:0000269|PubMed:9878716};
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5 for ubiquinol oxidation activity. {ECO:0000269|PubMed:9878716};
null
FUNCTION: Dehydrogenase component of the alcohol dehydrogenase multicomponent enzyme system which is involved in the production of acetic acid and in the ethanol oxidase respiratory chain. Quinohemoprotein alcohol dehydrogenase (ADH) catalyzes the oxidation of ethanol to acetaldehyde by transferring electrons to the ubiquinone embedded in the membrane phospholipids (PubMed:1646200, PubMed:18838797, PubMed:7592433, PubMed:8617755, PubMed:9878716). The electrons transfer from ethanol to membranous ubiquinone occurs from pyrroloquinoline quinone (PQQ) to one heme c in subunit I (AdhA), and finally to two heme c in subunit II (AdhB) (PubMed:18838797, PubMed:8617755, PubMed:9878716). Besides ubiquinone reduction, ADH also has a ubiquinol (QH2) oxidation reaction which mediates electron transfer from ubiquinol to the non-energy generating bypass oxidase system (PubMed:9878716). The electrons transfer occurs from ubiquinol (QH2) to the additional heme c within subunit II (AdhB) (PubMed:8617755, PubMed:9878716). Also able to use quinone analogs such as 2,3-dimethoxy-5-methyl-6-n-decyl-1,4-benzoquinone (DB) and 2,3-dimethoxy-5-methyl-6-n-pentyl-1,4-benzoquinone (PB) (PubMed:9878716). {ECO:0000269|PubMed:1646200, ECO:0000269|PubMed:18838797, ECO:0000269|PubMed:7592433, ECO:0000269|PubMed:8617755, ECO:0000269|PubMed:9878716, ECO:0000305|PubMed:9055427}.
Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans)
O05581
PAT_MYCTU
MDGIAELTGARVEDLAGMDVFQGCPAEGLVSLAASVQPLRAAAGQVLLRQGEPAVSFLLISSGSAEVSHVGDDGVAIIARALPGMIVGEIALLRDSPRSATVTTIEPLTGWTGGRGAFATMVHIPGVGERLLRTARQRLAAFVSPIPVRLADGTQLMLRPVLPGDRERTVHGHIQFSGETLYRRFMSARVPSPALMHYLSEVDYVDHFVWVVTDGSDPVADARFVRDETDPTVAEIAFTVADAYQGRGIGSFLIGALSVAARVDGVERFAARMLSDNVPMRTIMDRYGAVWQREDVGVITTMIDVPGPGELSLGREMVDQINRVARQVIEAVG
2.3.1.-
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:22773105};
null
cytosol [GO:0005829]
acetyltransferase activity [GO:0016407]; acyltransferase activity [GO:0016746]; cAMP binding [GO:0030552]; DNA-binding transcription factor activity [GO:0003700]; metal ion binding [GO:0046872]
PF13302;PF00027;
3.40.630.30;2.60.120.10;
null
null
null
null
null
null
null
null
FUNCTION: Catalyzes specifically the acetylation of the epsilon-amino group of a highly conserved lysine residue in acetyl-CoA synthetase (ACS). This acetylation results in the inactivation of ACS activity and could be important for mycobacteria to adjust to environmental changes. {ECO:0000269|PubMed:20507997, ECO:0000269|PubMed:21627103, ECO:0000269|PubMed:22773105}.
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
O05877
PK21_MYCTU
MDIPSVDVSTATNDGASSRAKGHRSAAPGRRKISDAVYQAELFRLQTEFVKLQEWARHSGARLVVIFEGRDGAGKGGAIKRITEYLNPRVARIAALPAPTDRERGQWYYQRYIAHLPAKGEIVLFDRSWYNRAGVEKVMGFCTPQEYVLFLRQTPIFEQMLIDDGILLRKYWFSVSDAEQLRRFKARRNDPVRQWKLSPMDLESVYRWEDYSRAKDEMMVHTDTPVSPWYVVESDIKKHARLNMMAHLLSTIDYADVEKPKVKLPPRPLVSGNYRRPPRELSTYVDDYVATLIAR
2.7.4.-
null
GTP biosynthetic process [GO:0006183]; protein autophosphorylation [GO:0046777]; regulation of nucleotide biosynthetic process [GO:0030808]
plasma membrane [GO:0005886]
GTP binding [GO:0005525]; polyphosphate kinase activity [GO:0008976]
PF03976;
3.40.50.300;
Polyphosphate kinase 2 (PPK2) family, Class I subfamily
PTM: Autophosphorylated at His-115 and His-247 using polyP as a phosphate donor. {ECO:0000269|PubMed:19843229}.
null
CATALYTIC ACTIVITY: Reaction=[phosphate](n) + GTP = [phosphate](n+1) + GDP; Xref=Rhea:RHEA:55412, Rhea:RHEA-COMP:9859, Rhea:RHEA-COMP:14280, ChEBI:CHEBI:16838, ChEBI:CHEBI:37565, ChEBI:CHEBI:58189; Evidence={ECO:0000269|PubMed:19843229}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:55414; Evidence={ECO:0000269|PubMed:19843229};
null
null
null
null
FUNCTION: Uses inorganic polyphosphate (polyP) as a donor to convert GDP to GTP. In addition, modulates nucleotide triphosphate synthesis catalyzed by the nucleoside diphosphate kinase (Ndk) in favor of GTP production over CTP or UTP. Plays an important role in survival of M.tuberculosis in macrophages. {ECO:0000269|PubMed:19843229}.
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
O05927
CYSH_PSEAE
MLPFATIPATERNSAAQHQDPSPMSQPFDLPALASSLADKSPQDILKAAFEHFGDELWISFSGAEDVVLVDMAWKLNRNVKVFSLDTGRLHPETYRFIDQVREHYGIAIDVLSPDPRLLEPLVKEKGLFSFYRDGHGECCGIRKIEPLKRKLAGVRAWATGQRRDQSPGTRSQVAVLEIDGAFSTPEKPLYKFNPLSSMTSEEVWGYIRMLELPYNSLHERGYISIGCEPCTRPVLPNQHEREGRWWWEEATHKECGLHAGNLISKA
1.8.4.10
COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000255|HAMAP-Rule:MF_00063, ECO:0000269|PubMed:11940598, ECO:0000269|PubMed:15491155, ECO:0000269|PubMed:16289027, ECO:0000269|PubMed:17010373}; Note=Binds 1 [4Fe-4S] cluster per subunit (PubMed:11940598, PubMed:15491155, PubMed:16289027, PubMed:17010373). The cluster is required for activity and may play a role in binding and activating the substrate for thiol-mediated reduction (PubMed:15491155, PubMed:16289027, PubMed:17010373). {ECO:0000269|PubMed:11940598, ECO:0000269|PubMed:15491155, ECO:0000269|PubMed:16289027, ECO:0000269|PubMed:17010373};
cysteine biosynthetic process [GO:0019344]; sulfate assimilation [GO:0000103]; sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin) [GO:0019379]
cytoplasm [GO:0005737]
4 iron, 4 sulfur cluster binding [GO:0051539]; adenylyl-sulfate reductase (thioredoxin) activity [GO:0043866]; metal ion binding [GO:0046872]; phosphoadenylyl-sulfate reductase (thioredoxin) activity [GO:0004604]
PF01507;
3.40.50.620;
PAPS reductase family, CysH subfamily
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00063, ECO:0000305}.
CATALYTIC ACTIVITY: Reaction=[thioredoxin]-disulfide + AMP + 2 H(+) + sulfite = [thioredoxin]-dithiol + adenosine 5'-phosphosulfate; Xref=Rhea:RHEA:21976, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:58243, ChEBI:CHEBI:456215; EC=1.8.4.10; Evidence={ECO:0000255|HAMAP-Rule:MF_00063, ECO:0000269|PubMed:10613872, ECO:0000269|PubMed:11940598, ECO:0000269|PubMed:16289027};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.75 uM for 5'-adenylyl sulfate (at pH 8.5 and 30 degrees Celsius) {ECO:0000269|PubMed:10613872}; KM=19.6 uM for thioredoxin (at pH 8.5 and 30 degrees Celsius) {ECO:0000269|PubMed:10613872}; Vmax=5.8 umol/min/mg enzyme with thioredoxin as electron donor and 5'-adenylyl sulfate as substrate (at pH 8.5 and 30 degrees Celsius) {ECO:0000269|PubMed:10613872};
PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate. {ECO:0000255|HAMAP-Rule:MF_00063, ECO:0000305|PubMed:11940598}.
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5. {ECO:0000269|PubMed:10613872};
null
FUNCTION: Catalyzes the formation of sulfite from adenosine 5'-phosphosulfate (APS) using thioredoxin as an electron donor. {ECO:0000255|HAMAP-Rule:MF_00063, ECO:0000269|PubMed:10613872, ECO:0000269|PubMed:11940598, ECO:0000269|PubMed:16289027}.
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
O06218
AHPR_MYCTU
MKFVNHIEPVAPRRAGGAVAEVYAEARREFGRLPEPLAMLSPDEGLLTAGWATLRETLLVGQVPRGRKEAVAAAVAASLRCPWCVDAHTTMLYAAGQTDTAAAILAGTAPAAGDPNAPYVAWAAGTGTPAGPPAPFGPDVAAEYLGTAVQFHFIARLVLVLLDETFLPGGPRAQQLMRRAGGLVFARKVRAEHRPGRSTRRLEPRTLPDDLAWATPSEPIATAFAALSHHLDTAPHLPPPTRQVVRRVVGSWHGEPMPMSSRWTNEHTAELPADLHAPTRLALLTGLAPHQVTDDDVAAARSLLDTDAALVGALAWAAFTAARRIGTWIGAAAEGQVSRQNPTG
1.11.1.-
null
null
peptidoglycan-based cell wall [GO:0009274]; plasma membrane [GO:0005886]
peroxiredoxin activity [GO:0051920]
PF02627;
1.20.1290.10;
AhpD family
null
null
null
null
null
null
null
FUNCTION: Involved in protection against oxidative stresses (PubMed:27818650, PubMed:35745538). May play a significant role in maintaining the cellular homeostasis during stress and virulence of M.tuberculosis (PubMed:27818650, PubMed:35745538). In vitro, catalyzes the decomposition of cumene hydroperoxide (CHP) to acetophenone (PubMed:27818650). {ECO:0000269|PubMed:27818650, ECO:0000269|PubMed:35745538}.
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
O06319
CULP4_MYCTU
MIPRPQPHSGRWRAGAARRLTSLVAAAFAAATLLLTPALAPPASAGCPDAEVVFARGTGEPPGLGRVGQAFVSSLRQQTNKSIGTYGVNYPANGDFLAAADGANDASDHIQQMASACRATRLVLGGYSQGAAVIDIVTAAPLPGLGFTQPLPPAADDHIAAIALFGNPSGRAGGLMSALTPQFGSKTINLCNNGDPICSDGNRWRAHLGYVPGMTNQAARFVASRI
3.1.1.-
null
lipid catabolic process [GO:0016042]
extracellular region [GO:0005576]; plasma membrane [GO:0005886]
hydrolase activity, acting on ester bonds [GO:0016788]; phospholipase A2 activity [GO:0004623]
PF01083;
3.40.50.1820;
Cutinase family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17416658}. Secreted, cell wall {ECO:0000269|PubMed:17416658}.
CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:41223, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999; Evidence={ECO:0000269|PubMed:20103719}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224; Evidence={ECO:0000269|PubMed:20103719}; CATALYTIC ACTIVITY: Reaction=a butanoate ester + H2O = an aliphatic alcohol + butanoate + H(+); Xref=Rhea:RHEA:47348, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:50477; Evidence={ECO:0000269|PubMed:19225166, ECO:0000269|PubMed:20103719}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47349; Evidence={ECO:0000269|PubMed:19225166, ECO:0000269|PubMed:20103719};
null
null
null
null
FUNCTION: A2-type phospholipase, which is probably involved in the degradation of macrophage membrane (PubMed:20103719). Hydrolyzes dipalmitoylphosphatidylcholine (PubMed:20103719). Also shows moderate esterase activity and hydrolyzes the p-nitrophenol-linked aliphatic ester pNP-butyrate (C4) (PubMed:19225166, PubMed:20103719). Does not exhibit cutinase activity (PubMed:19225166). {ECO:0000269|PubMed:19225166, ECO:0000269|PubMed:20103719}.
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
O06350
LIPF_MYCTU
MSSYYARRPLQSSGCSNSDSCWDGAPIEITESGPSVAGRLAALASRMTIKPLMTVGSYLSPLPLPLGFVDFACRVWRPGQGTVRTTINLPNATAQLVRAPGVRAADGAGRVVLYLHGGAFVMCGPNSHSRIVNALSGFAESPVLIVDYRLIPKHSLGMALDDCHDAYQWLRARGYRPEQIVLAGDSAGGYLALALAQRLQCDDEKPAAIVAISPLLQLAKGPKQDHPNIGTDAMFPARAFDALAAWVRAAAAKNMVDGRPEDLYEPLDHIESSLPPTLIHVSGSEVLLHDAQLGAGKLAAAGVCAEVRVWPGQAHLFQLATPLVPEATRSLRQIGQFIRDATADSSLSPVHRSRYVAGSPRAASRGAFGQSPI
3.1.1.1; 3.1.4.3
null
biological process involved in interaction with host [GO:0051701]; response to host immune response [GO:0052572]
extracellular region [GO:0005576]
carboxylesterase activity [GO:0106435]; phosphatidylcholine phospholipase C activity [GO:0034480]; phospholipase C activity [GO:0004629]; triglyceride lipase activity [GO:0004806]
PF07859;
3.40.50.1820;
'GDXG' lipolytic enzyme family
null
SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000305|PubMed:18535356}. Note=Detected by antibodies in a wild-type strain and upon expression of a probably truncated form in M.smegmatis. {ECO:0000269|PubMed:18535356}.
CATALYTIC ACTIVITY: Reaction=a carboxylic ester + H2O = a carboxylate + an alcohol + H(+); Xref=Rhea:RHEA:21164, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29067, ChEBI:CHEBI:30879, ChEBI:CHEBI:33308; EC=3.1.1.1; Evidence={ECO:0000269|PubMed:15939293}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-sn-glycerol + H(+) + phosphocholine; Xref=Rhea:RHEA:10604, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:57643, ChEBI:CHEBI:295975; EC=3.1.4.3; Evidence={ECO:0000269|PubMed:18535356}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10605; Evidence={ECO:0000269|PubMed:18535356};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.13 mM for triacetin {ECO:0000269|PubMed:15939293}; KM=0.24 mM for tributyrin {ECO:0000269|PubMed:15939293}; KM=0.25 mM for tricaproin {ECO:0000269|PubMed:15939293}; KM=1.46 mM for tricaprylin {ECO:0000269|PubMed:15939293}; KM=0.16 mM for p-nitrophenyl acetate {ECO:0000269|PubMed:15939293}; KM=0.18 mM for p-nitrophenyl butyrate {ECO:0000269|PubMed:15939293}; KM=0.58 mM for p-nitrophenyl caproate {ECO:0000269|PubMed:15939293}; Note=kcat is 581.2 sec(-1) for triacetin. kcat is 223.7 sec(-1) for tributyrin. kcat is 122.9 sec(-1) for tricaproin. kcat is 15.6 sec(-1) for tricaprylin. kcat is 501.8 sec(-1) for p-nitrophenyl acetate. kcat is 119.7 sec(-1) for p-nitrophenyl butyrate. kcat is 33.1 sec(-1) for p-nitrophenyl caproate. {ECO:0000269|PubMed:15939293};
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:15939293};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 35 degrees Celsius. {ECO:0000269|PubMed:15939293};
FUNCTION: Hydrolyzes short-chain esters. Shows maximal activity with triacetin and p-nitrophenyl acetate. Has no enzyme activity on triacylglycerides or p-nitrophenyl esters (p-NP) with long fatty acids (tricaprin, p-NP caprylate, or p-NP caprate); experiments performed with enzyme missing the first 97 residues (PubMed:15939293). Has phospholipase C activity, making 1,2-DAG phosphocholine; experiments performed with enzyme missing the first 97 residues (PubMed:18535356). {ECO:0000269|PubMed:15939293, ECO:0000269|PubMed:18535356}.
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
O06428
NPPPS_MYCTU
MRTPATVVAGVDLGDAVFAAAVRAGVARVEQLMDTELRQADEVMSDSLLHLFNAGGKRFRPLFTVLSAQIGPQPDAAAVTVAGAVIEMIHLATLYHDDVMDEAQVRRGAPSANAQWGNNVAILAGDYLLATASRLVARLGPEAVRIIADTFAQLVTGQMRETRGTSENVDSIEQYLKVVQEKTGSLIGAAGRLGGMFSGATDEQVERLSRLGGVVGTAFQIADDIIDIDSESDESGKLPGTDVREGVHTLPMLYALRESGPDCARLRALLNGPVDDDAEVREALTLLRASPGMARAKDVLAQYAAQARHELALLPDVPGRRALAALVDYTVSRHG
2.5.1.10; 2.5.1.29; 2.5.1.85
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:32495977}; Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q12051};
geranylgeranyl diphosphate biosynthetic process [GO:0033386]; isoprenoid biosynthetic process [GO:0008299]
peptidoglycan-based cell wall [GO:0009274]; plasma membrane [GO:0005886]
all-trans-nonaprenyl-diphosphate synthase (geranylgeranyl-diphosphate specific) activity [GO:0052924]; farnesyltranstransferase activity [GO:0004311]; geranyltranstransferase activity [GO:0004337]; metal ion binding [GO:0046872]; prenyltransferase activity [GO:0004659]
PF00348;
1.10.600.10;
FPP/GGPP synthase family
null
null
CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate + isopentenyl diphosphate = (2E,6E)-farnesyl diphosphate + diphosphate; Xref=Rhea:RHEA:19361, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.10; Evidence={ECO:0000269|PubMed:23091471, ECO:0000269|PubMed:32495977}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19362; Evidence={ECO:0000269|PubMed:23091471, ECO:0000269|PubMed:32495977}; CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate + isopentenyl diphosphate = (2E,6E,10E)-geranylgeranyl diphosphate + diphosphate; Xref=Rhea:RHEA:17653, ChEBI:CHEBI:33019, ChEBI:CHEBI:58756, ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.29; Evidence={ECO:0000269|PubMed:23091471, ECO:0000269|PubMed:30301210, ECO:0000269|PubMed:32495977}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17654; Evidence={ECO:0000269|PubMed:23091471, ECO:0000269|PubMed:30301210, ECO:0000269|PubMed:32495977}; CATALYTIC ACTIVITY: Reaction=(2E,6E,10E)-geranylgeranyl diphosphate + 5 isopentenyl diphosphate = all-trans-nonaprenyl diphosphate + 5 diphosphate; Xref=Rhea:RHEA:27594, ChEBI:CHEBI:33019, ChEBI:CHEBI:58391, ChEBI:CHEBI:58756, ChEBI:CHEBI:128769; EC=2.5.1.85; Evidence={ECO:0000269|PubMed:32495977}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27595; Evidence={ECO:0000269|PubMed:32495977};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.7 uM for IPP {ECO:0000269|PubMed:23091471}; KM=2.3 uM for GPP {ECO:0000269|PubMed:23091471}; KM=11 uM for FPP {ECO:0000269|PubMed:23091471}; KM=5 uM for DMAPP {ECO:0000269|PubMed:23091471}; Note=kcat is 0.3 min(-1) with GPP as substrate. kcat is 0.7 min(-1) with FPP as substrate. kcat is 0.17 min(-1) with DMAPP as substrate. {ECO:0000269|PubMed:23091471};
PATHWAY: Isoprenoid biosynthesis; farnesyl diphosphate biosynthesis; farnesyl diphosphate from geranyl diphosphate and isopentenyl diphosphate. {ECO:0000269|PubMed:32495977}.; PATHWAY: Isoprenoid biosynthesis; geranylgeranyl diphosphate biosynthesis; geranylgeranyl diphosphate from farnesyl diphosphate and isopentenyl diphosphate: step 1/1. {ECO:0000269|PubMed:32495977}.
null
null
FUNCTION: Catalyzes the sequential condensations of isopentenyl pyrophosphate (IPP) with geranyl diphosphate (GPP) to yield (2E,6E)-farnesyl diphosphate (E,E-FPP), with E,E-FPP to yield geranylgeranyl diphosphate (GGPP) and with GGPP to yield nonaprenyl diphosphate (PubMed:23091471, PubMed:30301210, PubMed:32495977). May also have weak activity with dimethylallyl diphosphate (DMAPP) (PubMed:23091471). {ECO:0000269|PubMed:23091471, ECO:0000269|PubMed:30301210, ECO:0000269|PubMed:32495977}.
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
O06543
AMACR_MYCTU
MAGPLSGLRVVELAGIGPGPHAAMILGDLGADVVRIDRPSSVDGISRDAMLRNRRIVTADLKSDQGLELALKLIAKADVLIEGYRPGVTERLGLGPEECAKVNDRLIYARMTGWGQTGPRSQQAGHDINYISLNGILHAIGRGDERPVPPLNLVGDFGGGSMFLLVGILAALWERQSSGKGQVVDAAMVDGSSVLIQMMWAMRATGMWTDTRGANMLDGGAPYYDTYECADGRYVAVGAIEPQFYAAMLAGLGLDAAELPPQNDRARWPELRALLTEAFASHDRDHWGAVFANSDACVTPVLAFGEVHNEPHIIERNTFYEANGGWQPMPAPRFSRTASSQPRPPAATIDIEAVLTDWDG
5.1.99.4
null
acyl-CoA metabolic process [GO:0006637]; bile acid metabolic process [GO:0008206]
null
alpha-methylacyl-CoA racemase activity [GO:0008111]; protein homodimerization activity [GO:0042803]
PF02515;
3.30.60.110;3.30.1540.10;
CoA-transferase III family
null
null
CATALYTIC ACTIVITY: Reaction=a (2S)-2-methylacyl-CoA = a (2R)-2-methylacyl-CoA; Xref=Rhea:RHEA:12657, ChEBI:CHEBI:57313, ChEBI:CHEBI:57314; EC=5.1.99.4; Evidence={ECO:0000269|PubMed:15632186}; CATALYTIC ACTIVITY: Reaction=(2S)-2-methyltetradecanoyl-CoA = (2R)-2-methyltetradecanoyl-CoA; Xref=Rhea:RHEA:46724, ChEBI:CHEBI:86520, ChEBI:CHEBI:86521; Evidence={ECO:0000269|PubMed:15632186}; CATALYTIC ACTIVITY: Reaction=(2R)-pristanoyl-CoA = (2S)-pristanoyl-CoA; Xref=Rhea:RHEA:40447, ChEBI:CHEBI:77099, ChEBI:CHEBI:77275; Evidence={ECO:0000269|PubMed:15632186}; CATALYTIC ACTIVITY: Reaction=(25S)-3-oxocholest-4-en-26-oyl-CoA = (25R)-3-oxocholest-4-en-26-oyl-CoA; Xref=Rhea:RHEA:63172, ChEBI:CHEBI:83819, ChEBI:CHEBI:146202; Evidence={ECO:0000269|PubMed:26348625}; CATALYTIC ACTIVITY: Reaction=(2S)-ibuprofenoyl-CoA = (2R)-ibuprofenoyl-CoA; Xref=Rhea:RHEA:63176, ChEBI:CHEBI:146203, ChEBI:CHEBI:146204; Evidence={ECO:0000269|PubMed:19854148};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=41 uM for (R)-pristanoyl-CoA {ECO:0000269|PubMed:15632186}; KM=6.5 uM for (25R)-3-oxo-cholest-4-en-26-oyl-CoA {ECO:0000269|PubMed:26348625}; KM=86 uM for (2S)-ibuprofenoyl-CoA {ECO:0000269|PubMed:19854148}; KM=48 uM for (2R)-ibuprofenoyl-CoA {ECO:0000269|PubMed:19854148}; Vmax=214 umol/min/mg enzyme with (R)-pristanoyl-CoA as substrate {ECO:0000269|PubMed:15632186}; Note=kcat is 3.7 sec(-1) with (25R)-3-oxo-cholest-4-en-26-oyl-CoA as substrate (PubMed:26348625). kcat is 450 sec(-1) with (2S)-ibuprofenoyl-CoA as substrate (PubMed:19854148). kcat is 291 sec(-1) with (2R)-ibuprofenoyl-CoA as substrate (PubMed:19854148). {ECO:0000269|PubMed:19854148, ECO:0000269|PubMed:26348625};
null
null
null
FUNCTION: Catalyzes the epimerization of (2R)- and (2S)-methylacyl-coenzyme A (CoA) thioesters (PubMed:15632186, PubMed:19854148, PubMed:26348625). Accepts as substrates a wide range of alpha-methylacyl-CoAs, including (2R)-2-methylmyristoyl-CoA and (2S)-2-methylmyristoyl-CoA, (2R)-pristanoyl-CoA and (2S)-pristanoyl-CoA, and the cholesterol esters (25R)-3-oxo-cholest-4-en-26-oyl-CoA and (25S)-3-oxo-cholest-4-en-26-oyl-CoA (PubMed:15632186, PubMed:26348625). Can also catalyze the interconversion of the non-physiologic substrates (2R)-ibuprofenoyl-CoA and (2S)-ibuprofenoyl-CoA, which are potential competitive inhibitors of the enzyme (PubMed:19854148). {ECO:0000269|PubMed:15632186, ECO:0000269|PubMed:19854148, ECO:0000269|PubMed:26348625}.
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
O06582
PRPD_MYCTU
MPDQDTKVRFFRVFCWCPVLRMVRIMLMHAVRAWRSADDFPCTEHMAYKIAQVAADPVDVDPEVADMVCNRIIDNAAVSAASMVRRPVTVARHQALAHPVRHGAKVFGVEGSYSADWAAWANGVAARELDFHDTFLAADYSHPADNIPPLVAVAQQLGVCGAELIRGLVTAYEIHIDLTRGICLHEHKIDHVAHLGPAVAAGIGTMLRLDQETIYHAIGQALHLTTSTRQSRKGAISSWKAFAPAHAGKVGIEAVDRAMRGEGSPAPIWEGEDGVIAWLLAGPEHTYRVPLPAPGEPKRAILDSYTKQHSAEYQSQAPIDLACRLRERIGDLDQIASIVLHTSHHTHVVIGTGSGDPQKFDPDASRETLDHSLPYIFAVALQDGCWHHERSYAPERARRSDTVALWHKISTVEDPEWTRRYHCADPAKKAFGARAEVTLHSGEVIVDELAVADAHPLGTRPFERKQYVEKFTELADGVVEPVEQQRFLAVVESLADLESGAVGGLNVLVDPRVLDKAPVIPPGIFR
4.2.1.3; 4.2.1.79
null
cholesterol metabolic process [GO:0008203]; defense response [GO:0006952]; propionate catabolic process, 2-methylcitrate cycle [GO:0019629]; response to acidic pH [GO:0010447]; tricarboxylic acid cycle [GO:0006099]
cytosol [GO:0005829]; peptidoglycan-based cell wall [GO:0009274]
2-methylcitrate dehydratase activity [GO:0047547]; aconitate decarboxylase activity [GO:0047613]; aconitate hydratase activity [GO:0003994]
PF19305;PF03972;
1.10.4100.10;3.30.1330.120;
PrpD family
null
null
CATALYTIC ACTIVITY: Reaction=(2S,3S)-2-methylcitrate = 2-methyl-cis-aconitate + H2O; Xref=Rhea:RHEA:17725, ChEBI:CHEBI:15377, ChEBI:CHEBI:57872, ChEBI:CHEBI:58853; EC=4.2.1.79; Evidence={ECO:0000250|UniProtKB:H8F0D6}; CATALYTIC ACTIVITY: Reaction=citrate = D-threo-isocitrate; Xref=Rhea:RHEA:10336, ChEBI:CHEBI:15562, ChEBI:CHEBI:16947; EC=4.2.1.3; Evidence={ECO:0000250|UniProtKB:P77243};
null
PATHWAY: Organic acid metabolism; propanoate degradation. {ECO:0000305|PubMed:18375549}.; PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 1/2. {ECO:0000305}.
null
null
FUNCTION: Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the dehydration of 2-methylcitrate (2-MC) to yield the cis isomer of 2-methyl-aconitate (PubMed:18375549, PubMed:22365605). Could also catalyze the dehydration of citrate and the hydration of cis-aconitate (By similarity). {ECO:0000250|UniProtKB:P77243, ECO:0000269|PubMed:18375549, ECO:0000269|PubMed:22365605}.
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
O06644
FCTA_OXAFO
MTKPLDGINVLDFTHVQAGPACTQMMGFLGANVIKIERRGSGDMTRGWLQDKPNVDSLYFTMFNCNKRSIELDMKTPEGKELLEQMIKKADVMVENFGPGALDRMGFTWEYIQELNPRVILASVKGYAEGHANEHLKVYENVAQCSGGAAATTGFWDGPPTVSGAALGDSNSGMHLMIGILAALEMRHKTGRGQKVAVAMQDAVLNLVRIKLRDQQRLERTGILAEYPQAQPNFAFDRDGNPLSFDNITSVPRGGNAGGGGQPGWMLKCKGWETDADSYVYFTIAANMWPQICDMIDKPEWKDDPAYNTFEGRVDKLMDIFSFIETKFADKDKFEVTEWAAQYGIPCGPVMSMKELAHDPSLQKVGTVVEVVDEIRGNHLTVGAPFKFSGFQPEITRAPLLGEHTDEVLKELGLDDAKIKELHAKQVV
2.8.3.16
null
oxalate catabolic process [GO:0033611]
cytoplasm [GO:0005737]
formyl-CoA transferase activity [GO:0033608]
PF02515;
3.30.1540.10;
CoA-transferase III family, Frc subfamily
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:2361939}.
CATALYTIC ACTIVITY: Reaction=formyl-CoA + oxalate = formate + oxalyl-CoA; Xref=Rhea:RHEA:16545, ChEBI:CHEBI:15740, ChEBI:CHEBI:30623, ChEBI:CHEBI:57376, ChEBI:CHEBI:57388; EC=2.8.3.16; Evidence={ECO:0000255|HAMAP-Rule:MF_00742, ECO:0000269|PubMed:15213226, ECO:0000269|PubMed:18162462, ECO:0000269|PubMed:18245280, ECO:0000269|PubMed:2361939, ECO:0000269|PubMed:9150242}; CATALYTIC ACTIVITY: Reaction=formyl-CoA + succinate = formate + succinyl-CoA; Xref=Rhea:RHEA:71735, ChEBI:CHEBI:15740, ChEBI:CHEBI:30031, ChEBI:CHEBI:57292, ChEBI:CHEBI:57376; Evidence={ECO:0000269|PubMed:18245280, ECO:0000269|PubMed:2361939};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2 uM for formyl-CoA (with oxalate as acceptor at pH 6.7 and 30 degrees Celsius) {ECO:0000269|PubMed:18162462, ECO:0000269|PubMed:18245280}; KM=8 uM for formyl-CoA (with oxalate as acceptor at pH 6.7 and 30 degrees Celsius) {ECO:0000269|PubMed:15213226}; KM=16 uM for formyl-CoA (with succinate as acceptor at pH 6.7 and 30 degrees Celsius) {ECO:0000269|PubMed:18245280}; KM=0.32 mM for succinate (with formyl-CoA as donor at pH 6.7 and 30 degrees Celsius) {ECO:0000269|PubMed:18245280}; KM=2.3 mM for succinate (with formyl-CoA as donor at pH 6.8 and 25 degrees Celsius) {ECO:0000269|PubMed:2361939}; KM=3 mM for formyl-CoA (with oxalate as acceptor at pH 6.8 and 25 degrees Celsius) {ECO:0000269|PubMed:2361939}; KM=3.9 mM for oxalate (with formyl-CoA as donor at pH 6.7 and 30 degrees Celsius) {ECO:0000269|PubMed:15213226, ECO:0000269|PubMed:18245280}; KM=5.1 mM for oxalate {ECO:0000269|PubMed:2361939}; Vmax=6.4 umol/min/mg enzyme with oxalate as substrate (with formyl-CoA as donor at pH 6.8 and 25 degrees Celsius) {ECO:0000269|PubMed:2361939}; Vmax=19.2 umol/min/mg enzyme with succinate as substrate (with formyl-CoA as donor at pH 6.8 and 25 degrees Celsius) {ECO:0000269|PubMed:2361939}; Vmax=29.6 umol/min/mg enzyme with formyl-CoA as substrate (with oxalate as acceptor at pH 6.8 and 25 degrees Celsius) {ECO:0000269|PubMed:2361939}; Note=kcat is 5.3 sec(-1) for CoA-transferase activity with formyl-CoA as substrate (with oxalate as acceptor at pH 6.7 and 30 degrees Celsius). kcat is 149 sec(-1) for CoA-transferase activity with formyl-CoA as substrate (with succinate as acceptor at pH 6.7 and 30 degrees Celsius). {ECO:0000269|PubMed:18245280};
PATHWAY: Metabolic intermediate degradation; oxalate degradation; CO(2) and formate from oxalate: step 1/2. {ECO:0000255|HAMAP-Rule:MF_00742}.
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is between 6.5 and 7.5. {ECO:0000269|PubMed:15213226, ECO:0000269|PubMed:18162462, ECO:0000269|PubMed:18245280, ECO:0000269|PubMed:2361939};
null
FUNCTION: Involved in the catabolism of oxalate and in the adapatation to low pH via the induction of the oxalate-dependent acid tolerance response (ATR). Essential enzyme for the bacterium survival, as it relies on oxalic acid as its sole source of energy. Catalyzes the transfer of the CoA moiety from formyl-CoA to oxalate (PubMed:15213226, PubMed:18162462, PubMed:18245280, PubMed:2361939, PubMed:9150242). It can also use succinate as acceptor (PubMed:18245280, PubMed:2361939). {ECO:0000269|PubMed:15213226, ECO:0000269|PubMed:18162462, ECO:0000269|PubMed:18245280, ECO:0000269|PubMed:2361939, ECO:0000269|PubMed:9150242}.
Oxalobacter formigenes
O06652
HADDL_PSES4
MSHRPILKNFPQVDHHQASGKLGDLYNDIHDTLRVPWVAFGIRVMSQFEHFVPAAWEALKPQISTRYAEEGADKVREAAIIPGSAPANPTPALLANGWSEEEIAKLKATLDGLNYGNPKYLILISAWNEAWHGRDAGGGAGKRLDSVQSERLPYGLPQGVEKFHLIDPEAADDQVQCLLRDIRDAFLHHGPASDYRVLAAWPDYLEIAFRDTLKPVALTTEFELTTSRIRKIAREHVRGFDGAGGVAWRDMADRMTPEEIAGLTGVLFMYNRFIADITVAIIRLKQAFGSAEDATENKFRVWPTEKG
3.8.1.10
null
null
null
(R)-2-haloacid dehalogenase activity [GO:0033975]; (S)-2-haloacid dehalogenase activity [GO:0018784]; DL-2 haloacid dehalogenase activity [GO:0018778]
PF10778;
null
HAD-like hydrolase superfamily, S-2-haloalkanoic acid dehalogenase family
null
null
CATALYTIC ACTIVITY: Reaction=an (S)-2-haloacid + H2O = a (2R)-2-hydroxycarboxylate + a halide anion + H(+); Xref=Rhea:RHEA:11192, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16042, ChEBI:CHEBI:58314, ChEBI:CHEBI:137405; EC=3.8.1.10; CATALYTIC ACTIVITY: Reaction=an (R)-2-haloacid + H2O = a (2S)-2-hydroxycarboxylate + a halide anion + H(+); Xref=Rhea:RHEA:22188, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16042, ChEBI:CHEBI:58123, ChEBI:CHEBI:137406; EC=3.8.1.10;
null
null
null
null
FUNCTION: Dehalogenates both (S)- and (R)-2-haloalkanoic acids to the corresponding (R)- and (S)-hydroxyalkanoic acids, respectively, with inversion of configuration at C-2. Acts on 2-haloalkanoic acids whose carbon chain lengths are five or less.
Pseudomonas sp. (strain 113)
O06728
YISP_BACSU
MKEIKEAYQQCGQIVGEYAPACFKALSYLPLKQRQASWAVLSFCHTAASADEKVLPAFEAKADHVYQRTNNGKQHLWKAFDHAYRTFTLESEPFREFIAAQKEDAKPYDDLDELLMYAYRTGGAAGLMLLPILTRRKQDQLKQAAVSLGLAIQLVRFLSDLGTDQQKNRIPRQVMQQFGYTEADLQKGTVNKAFTMTWEYIAFEAEAYLEECQDALPLFPQYSQKTVKAALHLHRAVLEKIRAKQHDVFQYHFALTETEVKQILSDI
3.1.7.6
null
carotenoid biosynthetic process [GO:0016117]
null
15-cis-phytoene synthase activity [GO:0046905]; geranylgeranyl-diphosphate geranylgeranyltransferase activity [GO:0016767]
PF00494;
1.10.600.10;
Phytoene/squalene synthase family
null
null
CATALYTIC ACTIVITY: Reaction=(2E,6E)-farnesyl diphosphate + H2O = (2E,6E)-farnesol + diphosphate; Xref=Rhea:RHEA:27526, ChEBI:CHEBI:15377, ChEBI:CHEBI:16619, ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=3.1.7.6; Evidence={ECO:0000269|PubMed:25308276};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.47 uM for farnesyl pyrophosphate {ECO:0000269|PubMed:20713508}; KM=14.9 uM for geranyl pyrophosphate {ECO:0000269|PubMed:20713508};
null
null
null
FUNCTION: A farnesyl diphosphate (FPP) phosphatase. Involved in biofilm formation, its disruption blocks biofilm synthesis which is restored by exogenous farnesol (PubMed:25308276). Releases diphosphate from FPP, was initally suggested to be a squalene synthase. Diphosphate release is higher from FPP than geranyl pyrophosphate (GPP) or geranylgeranyl pyrophosphate (GGPP). Biofilm synthesis is partially restored by exogenous squalene, beta-carotene or retinol. Required for integrity of cell membrane lipid rafts (PubMed:20713508). Involved in spatial organization of membranes, required for the flotillin-like proteins FloT and FloA to function correctly (PubMed:23651456). {ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:23651456, ECO:0000269|PubMed:25308276}.
Bacillus subtilis (strain 168)
O06769
NCASE_MYCTU
MLSVGRGIADITGEAADCGMLGYGKSDQRTAGIHQRLRSRAFVFRDDSQDGDARLLLIVAELPLPMQNVNEEVLRRLADLYGDTYSEQNTLITATHTHAGPGGYCGYLLYNLTTSGFRPATFAAIVDGIVESVEHAHADVAPAEVSLSHGELYGASINRSPSAFDRNPPADKAFFPKRVDPHTTLVRIDRGEATVGVIHFFATHGTSMTNRNHLISGDNKGFAAYHWERTVGGADYLAGQPDFIAAFAQTNPGDMSPNVDGPLSPEAPPDREFDNTRRTGLCQFEDAFTQLSGATPIGAGIDARFTYVDLGSVLVRGEYTPDGEERRTGRPMFGAGAMAGTDEGPGFHGFRQGRNPFWDRLSRAMYRLARPTAAAQAPKGIVMPARLPNRIHPFVQEIVPVQLVRIGRLYLIGIPGEPTIVAGLRLRRMVASIVGADLADVLCVGYTNAYIHYVTTPEEYLEQRYEGGSTLFGRWELCALMQTVAELAEAMRDGRPVTLGRRPRPTRELSWVRGAPADAGSFGAVIAEPSATYRPGQAVEAVFVSALPNNDLRRGGTYLEVVRREGASWVRIADDGDWATSFRWQRQGRAGSHVSIRWDVPGDTTPGQYRIVHHGTARDRNGMLTAFSATTREFTVV
3.5.1.23
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q9I596}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9I596}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9I596};
ceramide catabolic process [GO:0046514]; long-chain fatty acid biosynthetic process [GO:0042759]; sphingosine biosynthetic process [GO:0046512]
extracellular region [GO:0005576]; peptidoglycan-based cell wall [GO:0009274]
ceramidase activity [GO:0102121]; metal ion binding [GO:0046872]; N-acylsphingosine amidohydrolase activity [GO:0017040]
PF04734;PF17048;
2.60.40.2300;
Neutral ceramidase family
null
null
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:0000269|PubMed:10593963, ECO:0000269|PubMed:20139604}; CATALYTIC ACTIVITY: Reaction=an N-acylsphinganine + H2O = a fatty acid + sphinganine; Xref=Rhea:RHEA:33551, ChEBI:CHEBI:15377, ChEBI:CHEBI:28868, ChEBI:CHEBI:31488, ChEBI:CHEBI:57817; Evidence={ECO:0000269|PubMed:20139604}; CATALYTIC ACTIVITY: Reaction=an N-acyl-(4R)-4-hydroxysphinganine + H2O = (4R)-hydroxysphinganine + a fatty acid; Xref=Rhea:RHEA:33555, ChEBI:CHEBI:15377, ChEBI:CHEBI:28868, ChEBI:CHEBI:31998, ChEBI:CHEBI:64124; Evidence={ECO:0000269|PubMed:20139604}; 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:0000269|PubMed:20139604}; 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:0000269|PubMed:20139604}; 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:0000269|PubMed:20139604}; 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:0000269|PubMed:20139604}; CATALYTIC ACTIVITY: Reaction=H2O + N-eicosanoyl-sphing-4-enine = eicosanoate + sphing-4-enine; Xref=Rhea:RHEA:41275, ChEBI:CHEBI:15377, ChEBI:CHEBI:32360, ChEBI:CHEBI:57756, ChEBI:CHEBI:72962; Evidence={ECO:0000269|PubMed:20139604}; CATALYTIC ACTIVITY: Reaction=H2O + N-(15Z-tetracosenoyl)-sphing-4-enine = (15Z)-tetracosenoate + sphing-4-enine; Xref=Rhea:RHEA:41267, ChEBI:CHEBI:15377, ChEBI:CHEBI:32392, ChEBI:CHEBI:57756, ChEBI:CHEBI:74450; Evidence={ECO:0000269|PubMed:20139604}; CATALYTIC ACTIVITY: Reaction=H2O + N-tetracosanoyl-sphing-4-enine = sphing-4-enine + tetracosanoate; Xref=Rhea:RHEA:41283, ChEBI:CHEBI:15377, ChEBI:CHEBI:31014, ChEBI:CHEBI:57756, ChEBI:CHEBI:72965; Evidence={ECO:0000269|PubMed:20139604};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=98.7 uM for N-dodecanoyl-7-nitrobenz-2-oxa-1,3-4-diazole (NBD)-D-erythro-sphingosine (C12-NBD-Cer) (at pH 8 and at 37 degrees Celsius) {ECO:0000269|PubMed:10593963, ECO:0000269|PubMed:20139604}; Vmax=21.1 pmol/min/mg enzyme (at pH 8 and at 37 degrees Celsius) {ECO:0000269|PubMed:10593963, ECO:0000269|PubMed:20139604};
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is between 8 and 9. {ECO:0000269|PubMed:10593963, ECO:0000269|PubMed:20139604};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: 10 minutes at 100 degrees Celsius abolishes completely the activity. {ECO:0000269|PubMed:10593963, ECO:0000269|PubMed:20139604};
FUNCTION: Catalyzes the cleavage of the N-acyl linkage of the ceramides (Cers) to yield sphingosine (Sph) and free fatty acid. Also catalyzes the synthesis of Cers from Sph and fatty acid. Cers containning C6-C24 fatty acids are well hydrolyzed, and Cers with mono unsaturated fatty acids are much more hydrolyzed than those with saturated fatty acids. {ECO:0000269|PubMed:10593963, ECO:0000269|PubMed:20139604}.
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
O06961
TDCD_SALTY
MNEFPVVLVINCGSSSIKFSVLDVATCDVLMAGIADGMNTENAFLSINGDKPINLAHSNYEDALKAIAFELEKRDLTDSVALIGHRIAHGGELFTQSVIITDEIIDNIRRVSPLAPLHNYANLSGIDAARHLFPAVRQVAVFDTSFHQTLAPEAYLYGLPWEYFSSLGVRRYGFHGTSHRYVSRRAYELLDLDEKDSGLIVAHLGNGASICAVRNGQSVDTSMGMTPLEGLMMGTRSGDVDFGAMAWIAKETGQTLSDLERVVNKESGLLGISGLSSDLRVLEKAWHEGHERARLAIKTFVHRIARHIAGHAASLHRLDGIIFTGGIGENSVLIRQLVIEHLGVLGLTLDVEMNKQPNSHGERIISANPSQVICAVIPTNEEKMIALDAIHLGNVKAPVEFA
2.7.2.15
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_01881};
acetate metabolic process [GO:0006083]; L-threonine catabolic process to propionate [GO:0070689]; phosphorylation [GO:0016310]
cytosol [GO:0005829]
acetate kinase activity [GO:0008776]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; propionate kinase activity [GO:0008980]
PF00871;
3.30.420.40;
Acetokinase family, TdcD subfamily
null
null
CATALYTIC ACTIVITY: Reaction=ATP + propanoate = ADP + propanoyl phosphate; Xref=Rhea:RHEA:23148, ChEBI:CHEBI:17272, ChEBI:CHEBI:30616, ChEBI:CHEBI:58933, ChEBI:CHEBI:456216; EC=2.7.2.15; Evidence={ECO:0000255|HAMAP-Rule:MF_01881};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=112 uM for ATP (at 25 degrees Celsius and pH 7.5) {ECO:0000269|PubMed:16139298}; KM=2.3 mM for propionate (at 25 degrees Celsius and pH 7.5) {ECO:0000269|PubMed:16139298}; KM=26.9 mM for acetate (at 25 degrees Celsius and pH 7.5) {ECO:0000269|PubMed:16139298};
PATHWAY: Amino-acid degradation; L-threonine degradation via propanoate pathway; propanoate from L-threonine: step 4/4. {ECO:0000255|HAMAP-Rule:MF_01881}.
null
null
FUNCTION: Catalyzes the conversion of propionyl phosphate and ADP to propionate and ATP. It can also use acetyl phosphate as phosphate group acceptor.
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
O06967
BMRA_BACSU
MPTKKQKSKSKLKPFFALVRRTNPSYGKLAFALALSVVTTLVSLLIPLLTKQLVDGFSMSNLSGTQIGLIALVFFVQAGLSAYATYALNYNGQKIISGLRELLWKKLIKLPVSYFDTNASGETVSRVTNDTMVVKELITTHISGFITGIISVIGSLTILFIMNWKLTLLVLVVVPLAALILVPIGRKMFSISRETQDETARFTGLLNQILPEIRLVKASNAEDVEYGRGKMGISSLFKLGVREAKVQSLVGPLISLVLMAALVAVIGYGGMQVSSGELTAGALVAFILYLFQIIMPMGQITTFFTQLQKSIGATERMIEILAEEEEDTVTGKQIENAHLPIQLDRVSFGYKPDQLILKEVSAVIEAGKVTAIVGPSGGGKTTLFKLLERFYSPTAGTIRLGDEPVDTYSLESWREHIGYVSQESPLMSGTIRENICYGLERDVTDAEIEKAAEMAYALNFIKELPNQFDTEVGERGIMLSGGQRQRIAIARALLRNPSILMLDEATSSLDSQSEKSVQQALEVLMEGRTTIVIAHRLSTVVDADQLLFVEKGEITGRGTHHELMASHGLYRDFAEQQLKMNADLENKAG
7.6.2.-
null
response to antibiotic [GO:0046677]; transmembrane transport [GO:0055085]
plasma membrane [GO:0005886]
ABC-type transporter activity [GO:0140359]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled lipid transmembrane transporter activity [GO:0034040]
PF00664;PF00005;
1.20.1560.10;3.40.50.300;
ABC transporter superfamily
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
null
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=6.5 umol/min/mg enzyme for ATP {ECO:0000269|PubMed:12968023}; Note=Reconstituted in proteoliposomes (PubMed:12968023).;
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:12225846, ECO:0000269|PubMed:12968023, ECO:0000269|PubMed:16405427};
null
FUNCTION: An efflux transporter able to transport Hoechst 33342, ethidium bromide, doxorubicin and a number of other drugs in vitro into inside out vesicles. The endogenous substrate is unknown. It has been suggested that NBD dimerization induced by ATP-binding causes a large conformational change responsible for substrate translocation (PubMed:18215075). Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation (Probable). {ECO:0000269|PubMed:18215075, ECO:0000305}.
Bacillus subtilis (strain 168)
O07006
PADC_BACSU
MENFIGSHMIYTYENGWEYEIYIKNDHTIDYRIHSGMVAGRWVRDQEVNIVKLTEGVYKVSWTEPTGTDVSLNFMPNEKRMHGIIFFPKWVHEHPEITVCYQNDHIDLMKESREKYETYPKYVVPEFAEITFLKNEGVDNEEVISKAPYEGMTDDIRAGRL
4.1.1.102
null
aromatic compound catabolic process [GO:0019439]; response to toxic substance [GO:0009636]
null
carboxy-lyase activity [GO:0016831]
PF05870;
2.40.128.20;
PadC family
null
null
CATALYTIC ACTIVITY: Reaction=(E)-4-coumarate + H(+) = 4-hydroxystyrene + CO2; Xref=Rhea:RHEA:33227, ChEBI:CHEBI:1883, ChEBI:CHEBI:12876, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526; EC=4.1.1.102; Evidence={ECO:0000269|PubMed:9546183}; CATALYTIC ACTIVITY: Reaction=(E)-cinnamate + H(+) = CO2 + styrene; Xref=Rhea:RHEA:46920, ChEBI:CHEBI:15378, ChEBI:CHEBI:15669, ChEBI:CHEBI:16526, ChEBI:CHEBI:27452; EC=4.1.1.102; CATALYTIC ACTIVITY: Reaction=(E)-ferulate + H(+) = 2-methoxy-4-vinylphenol + CO2; Xref=Rhea:RHEA:33807, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:29749, ChEBI:CHEBI:42438; EC=4.1.1.102; Evidence={ECO:0000269|PubMed:9546183};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.1 mM for ferulic acid {ECO:0000269|PubMed:9546183}; KM=1.3 mM for p-coumaric acid {ECO:0000269|PubMed:9546183}; KM=2.6 mM for caffeic acid {ECO:0000269|PubMed:9546183}; Vmax=280 umol/min/mg enzyme for ferulic acid {ECO:0000269|PubMed:9546183}; Vmax=265 umol/min/mg enzyme for p-coumaric acid {ECO:0000269|PubMed:9546183}; Vmax=180 umol/min/mg enzyme for caffeic acid {ECO:0000269|PubMed:9546183};
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.0. {ECO:0000269|PubMed:9546183};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40-45 degrees Celsius. {ECO:0000269|PubMed:9546183};
FUNCTION: Involved in the decarboxylation and detoxification of phenolic derivatives. It is able to catalyze the decarboxylation of ferulic, p-coumaric and caffeic acids. {ECO:0000269|PubMed:9546183}.
Bacillus subtilis (strain 168)
O07012
BGAL2_BACSU
MLHGGDYNPDQWLDRPDILADDIKLMKLSHTNTFSVGIFAWSALEPEEGVYQFEWLDDIFERIHSIGGRVILATPSGARPAWLSQTYPEVLRVNASRVKQLHGGRHNHCLTSKVYREKTRHINRLLAERYGHHPALLMWHISNEYGGDCHCDLCQHAFREWLKSKYDNSLKTLNHAWWTPFWSHTFNDWSQIESPSPIGENGLHGLNLDWRRFVTDQTISFYENEIIPLKELTPDIPITTNFMADTPDLIPYQGLDYSKFAKHVDAISWDAYPVWHNDWESTADLAMKVGFINDLYRSLKQQPFLLMECTPSAVNWHNVNKAKRPGMNLLSSMQMIAHGSDSVLYFQYRKSRGSSEKLHGAVVDHDNSPKNRVFQEVAKVGETLERLSEVVGTKRPAQTAILYDWENHWALEDAQGFAKATKRYPQTLQQHYRTFWEHDIPVDVITKEQDFSPYKLLIVPMLYLISEDTVSRLKAFTADGGTLVMTYISGVVNEHDLTYTGGWHPDLQAIFGVEPLETDTLYPKDRNAVSYRSQIYEMKDYATVIDVKTASVEAVYQEDFYARTPAVTSHEYQQGKAYFIGARLEDQFQRDFYEGLITDLSLSPVFPVRHGKGVSVQARQDQDNDYIFVMNFTEEKQLVTFDQSVKDIMTGDILSGDLTMEKYEVRIVVNTH
3.2.1.23
null
galactose metabolic process [GO:0006012]
beta-galactosidase complex [GO:0009341]
beta-galactosidase activity [GO:0004565]; metal ion binding [GO:0046872]
PF02449;PF08533;PF08532;
3.40.50.880;3.20.20.80;2.60.40.1180;
Glycosyl hydrolase 42 family
null
null
CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.; EC=3.2.1.23; Evidence={ECO:0000269|PubMed:17056685, ECO:0000269|PubMed:27501980};
null
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.0-6.5. {ECO:0000269|PubMed:17056685};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 50 degrees Celsius. Thermolabile above 50 degrees Celsius. {ECO:0000269|PubMed:17056685};
FUNCTION: Involved in galactan degradation (PubMed:27501980). Hydrolyzes galactooligosaccharides released by the endo-beta-1,4-galactanase GanB from galactan (PubMed:17056685, PubMed:27501980). Degrades galactotetraose, galactotriose and galactobiose, generating galactose as the end product (PubMed:27501980). It is unable to use lactose (PubMed:17056685). In vitro, shows maximal activity with o-nitrophenyl-beta-D-galactopyranoside (ONPG) and p-nitrophenyl-beta-D-galactopyranoside (PNPG) as substrates, trace activity with p-nitrophenyl-alpha-L-arabinopyranoside and o-nitrophenyl-beta-D-fucopyranoside as substrates, but no activity with p-nitrophenyl-alpha-D-galactopyranoside, p-nitrophenyl-beta-D-glucopyranoside, o-nitrophenyl-beta-D-xylopyranoside, p-nitrophenyl-beta-D-mannopyranoside or p-nitrophenyl-alpha-L-arabinofuranoside as substrates (PubMed:17056685). {ECO:0000269|PubMed:17056685, ECO:0000269|PubMed:27501980}.
Bacillus subtilis (strain 168)
O07427
MGLL_MYCTU
MTTTRTERNFAGIGDVRIVYDVWTPDTAPQAVVVLAHGLGEHARRYDHVAQRLGAAGLVTYALDHRGHGRSGGKRVLVRDISEYTADFDTLVGIATREYPGCKRIVLGHSMGGGIVFAYGVERPDNYDLMVLSAPAVAAQDLVSPVVAVAAKLLGVVVPGLPVQELDFTAISRDPEVVQAYNTDPLVHHGRVPAGIGRALLQVGETMPRRAPALTAPLLVLHGTDDRLIPIEGSRRLVECVGSADVQLKEYPGLYHEVFNEPERNQVLDDVVAWLTERL
3.1.1.23
null
glycerolipid catabolic process [GO:0046503]; symbiont-mediated activation of host apoptosis [GO:0052151]
extracellular region [GO:0005576]; membrane [GO:0016020]; peptidoglycan-based cell wall [GO:0009274]; plasma membrane [GO:0005886]
acylglycerol lipase activity [GO:0047372]; lipase activity [GO:0016298]
PF12146;
3.40.50.1820;
AB hydrolase superfamily
null
SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:17784850}. Secreted {ECO:0000305|PubMed:17784850}.
CATALYTIC ACTIVITY: Reaction=a 1-acylglycerol + H2O = a fatty acid + glycerol + H(+); Xref=Rhea:RHEA:34019, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:28868, ChEBI:CHEBI:35759; Evidence={ECO:0000269|PubMed:17784850}; CATALYTIC ACTIVITY: Reaction=Hydrolyzes glycerol monoesters of long-chain fatty acids.; EC=3.1.1.23; Evidence={ECO:0000269|PubMed:17784850}; CATALYTIC ACTIVITY: Reaction=1-butyrylglycerol + H2O = butanoate + glycerol + H(+); Xref=Rhea:RHEA:44324, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:17968, ChEBI:CHEBI:76503; Evidence={ECO:0000269|PubMed:17784850}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44325; Evidence={ECO:0000269|PubMed:17784850}; CATALYTIC ACTIVITY: Reaction=1-octanoylglycerol + H2O = glycerol + H(+) + octanoate; Xref=Rhea:RHEA:44328, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:25646, ChEBI:CHEBI:85241; Evidence={ECO:0000269|PubMed:17784850}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44329; Evidence={ECO:0000269|PubMed:17784850}; CATALYTIC ACTIVITY: Reaction=1-decanoylglycerol + H2O = decanoate + glycerol + H(+); Xref=Rhea:RHEA:44320, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:27689, ChEBI:CHEBI:75547; Evidence={ECO:0000269|PubMed:17784850}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44321; Evidence={ECO:0000269|PubMed:17784850}; CATALYTIC ACTIVITY: Reaction=1-dodecanoylglycerol + H2O = dodecanoate + glycerol + H(+); Xref=Rhea:RHEA:44316, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:18262, ChEBI:CHEBI:75539; Evidence={ECO:0000269|PubMed:17784850}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44317; Evidence={ECO:0000269|PubMed:17784850}; CATALYTIC ACTIVITY: Reaction=1-tetradecanoylglycerol + H2O = glycerol + H(+) + tetradecanoate; Xref=Rhea:RHEA:44312, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30807, ChEBI:CHEBI:75562; Evidence={ECO:0000269|PubMed:17784850}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44313; Evidence={ECO:0000269|PubMed:17784850}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + glycerol + H(+); Xref=Rhea:RHEA:38487, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823, ChEBI:CHEBI:75342; Evidence={ECO:0000269|PubMed:17784850}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38488; Evidence={ECO:0000269|PubMed:17784850}; CATALYTIC ACTIVITY: Reaction=2-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate + glycerol + H(+); Xref=Rhea:RHEA:38491, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823, ChEBI:CHEBI:73990; Evidence={ECO:0000269|PubMed:17784850}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38492; Evidence={ECO:0000269|PubMed:17784850};
null
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9. Highly stable from pH 7.5 to 9.0. At lower pH values, the residual activity decreases rapidly to 50% at pH 6.5, and it is completely abolished after 1 hour of incubation at pH levels of 6.0 and below. {ECO:0000269|PubMed:17784850};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius. The activity increases 3-fold in a linear fashion from 25 to 50 degrees Celsius before decreasing slowly at higher temperatures. {ECO:0000269|PubMed:17784850};
FUNCTION: Involved in the hydrolysis of exogenous host lipids during chronic infection (Probable). Catalyzes the hydrolysis of both monoacylglycerols (MAG) and diacylglycerols (DAG), with a preference for MAG. It hydrolyzes 2-MAG, 1-3-MAG and MAG with short, medium and long chain fatty acids such as 1-monobutyroyl-rac-glycerol (MC4), 1-mono-octanoyl-rac-glycerol (MC8), 1-monodecanoyl-rac-glycerol (MC10), 1-monolauroyl-rac-glycerol (MC12), 1-monomyristoyl-rac-glycerol (MC14) and 1-mono-oleyl-rac-glycerol (MC18:1) (PubMed:17784850). Also able to hydrolyze DAG with short (DiC6) and medium (DiC10) fatty acid chains, but not with longest fatty acid chains (PubMed:17784850). Can also hydrolyze vinyl laurate (VC12), vinyl butyrate (VC4) and vinyl propionate (VC3) (PubMed:17784850). {ECO:0000269|PubMed:17784850, ECO:0000305|PubMed:17784850, ECO:0000305|PubMed:22405030}.; FUNCTION: Induces an inflammatory response and cell apoptosis in the host cells. Increases expression of IL-6, NF-kappaB, TLR-2, TLR-6, TNF-alpha, and MyD88 in mouse alveolar macrophage RAW264.7 cells. Persistent expression induces RAW264.7 cell apoptosis in vitro. {ECO:0000269|PubMed:21076482}.
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
O07431
CAMT_MYCTU
MGMDQQPNPPDVDAFLDSTLVGDDPALAAALAASDAAELPRIAVSAQQGKFLCLLAGAIQARRVLEIGTLGGFSTIWLARGAGPQGRVVTLEYQPKHAEVARVNLQRAGVADRVEVVVGPALDTLPTLAGGPFDLVFIDADKENNVAYIQWAIRLARRGAVIVVDNVIRGGGILAESDDADAVAARRTLQMMGEHPGLDATAIQTVGRKGWDGFALALVR
2.1.1.6
COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000269|PubMed:31147608};
methylation [GO:0032259]
plasma membrane [GO:0005886]
catechol O-methyltransferase activity [GO:0016206]; L-dopa O-methyltransferase activity [GO:0102084]; metal ion binding [GO:0046872]; orcinol O-methyltransferase activity [GO:0102938]; S-adenosylmethionine-dependent methyltransferase activity [GO:0008757]
PF01596;
3.40.50.150;
Class I-like SAM-binding methyltransferase superfamily, Cation-dependent O-methyltransferase family
null
null
CATALYTIC ACTIVITY: Reaction=a catechol + S-adenosyl-L-methionine = a guaiacol + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:17877, ChEBI:CHEBI:15378, ChEBI:CHEBI:33566, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:134251; EC=2.1.1.6; Evidence={ECO:0000269|PubMed:31147608};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.03 mM for 5OMeBA {ECO:0000269|PubMed:31147608}; KM=0.15 mM for PCA {ECO:0000269|PubMed:31147608}; KM=0.49 mM for CA {ECO:0000269|PubMed:31147608}; Note=kcat is 0.080 min(-1) with 5OMeBA as substrate. kcat is 0.22 min(-1) with PCA as substrate. kcat is 0.43 min(-1) with CA as substrate. {ECO:0000269|PubMed:31147608};
null
null
null
FUNCTION: Catechol O-methyltransferase that can use various catechol-like compounds such as gallic acid (GA), 3,4-dihydroxy-5-methoxy-benzoic acid (5OMeBA), protocatechuic acid (PCA), 3,4-dihydroxy-benzaldehyde (DHA), dopamine, caffeic acid (CA), luteolin, quercetin, and 5-hydroxyuridine. {ECO:0000269|PubMed:31147608}.
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
O07532
LYTF_BACSU
MKKKLAAGLTASAIVGTTLVVTPAEAATIKVKSGDSLWKLAQTYNTSVAALTSANHLSTTVLSIGQTLTIPGSKSSTSSSTSSSTTKKSGSSVYTVKSGDSLWLIANEFKMTVQELKKLNGLSSDLIRAGQKLKVSGTVSSSSSSSKKSNSNKSSSSSSKSSSNKSSSSSSSTGTYKVQLGDSLWKIANKVNMSIAELKVLNNLKSDTIYVNQVLKTKSSGSDTSSKDNSSKSNQTSATTKYTVKSGDSLWKIANNYNLTVQQIRNINNLKSDVLYVGQVLKLTGKASSGSSSSSSSSSNASSGTTTTYTVKSGDSLWVIAQKFNVTAQQIREKNNLKTDVLQVGQKLVISGKASSSSSSGSSNTTSSTSAKINTMISAAKAQLGVPYRWGGTTPSGFDCSGFIYYVLNKVTSVSRLTAAGYWNTMKSVSQPAVGDFVFFSTYKAGPSHVGIYLGNGEFINANDSGVVISNMNNSYWKQRYLGAKRYF
3.4.-.-
null
cell wall organization [GO:0071555]; proteolysis [GO:0006508]
extracellular region [GO:0005576]
cysteine-type peptidase activity [GO:0008234]; lytic endotransglycosylase activity [GO:0008932]
PF01476;PF00877;
3.90.1720.10;3.10.350.10;
Peptidase C40 family
null
SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:10206711, ECO:0000269|PubMed:14594841}. Note=LytF is localized at cell separation sites and cell poles of rod-shaped cells during vegetative growth.
null
null
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8. {ECO:0000269|PubMed:10206711};
null
FUNCTION: Cell wall hydrolase that cleaves gamma-D-glutamate-meso-diaminopimelate bonds in peptidoglycan. LytF is necessary and sufficient for vegetative daughter cell separation, and also seems to play a role in cell autolysis. {ECO:0000269|PubMed:10206711, ECO:0000269|PubMed:10322020, ECO:0000269|PubMed:19542270}.
Bacillus subtilis (strain 168)
O07566
NTDA_BACSU
MQKQVKISGKSKENMSLLKHLKGDVQGKELVIEDSIVNERWKQVLKEKIDIEHDLFNYQKNREISKVPFLPVDRLITNDEVEDILNTLTEVLPTGKFTSGPYLEQFEKVLSTYLHKRYVIATSSGTDAIMIGLLALGLNPGDEVIMPANSFSATENAVLASGGVPIYVDINPQTFCIDPDKIEEAITPYTKFILPVHLYGKHSDMQHIRQIANRYKLKVIEDACQGIGLTDLGKYADITTLSFNPYKNFGVCGKAGAIATDNEELAKKCIQFSYHGFEVNVKNKKVINFGFNSKMDNLQAAIGLERMKYLSLNNFKRLFLADRYITQLAELQNKGYIELPELSEDHVWHLFPIKVRTEDRADIMTKLNEDFGVQTDVYYPILSHMQKTPLVQDKYAGLQLVHTEKAHSQVLHLPLYPSFTLEEQDRVMEGLFHVIKQEIGV
2.6.1.104
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:24097983};
antibiotic biosynthetic process [GO:0017000]; polysaccharide biosynthetic process [GO:0000271]
null
pyridoxal phosphate binding [GO:0030170]; transaminase activity [GO:0008483]
PF01041;
3.90.1150.10;3.40.640.10;
DegT/DnrJ/EryC1 family
null
null
CATALYTIC ACTIVITY: Reaction=3-dehydro-D-glucose 6-phosphate + L-glutamate = 2-oxoglutarate + D-kanosamine 6-phosphate; Xref=Rhea:RHEA:37551, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:72748, ChEBI:CHEBI:75052; EC=2.6.1.104; Evidence={ECO:0000269|PubMed:23586652};
null
PATHWAY: Antibiotic biosynthesis; kanosamine biosynthesis.
null
null
FUNCTION: Involved in the biosynthesis of kanosamine (3-amino-3-deoxy-D-glucose), which is known to have antibiotic and antifungal properties, and to be a precursor of the antibiotic neotrehalosadiamine (3,3'-diamino-3,3'-dideoxy-alpha,beta-trehalose (NTD)). Catalyzes the reversible pyridoxal phosphate-dependent transamination of 3-dehydro-alpha-D-glucose 6-phosphate to form alpha-D-kanosamine-6-phosphate. It can only use alpha-anomer and glutamate is the only amino donor. {ECO:0000269|PubMed:14612444, ECO:0000269|PubMed:23586652, ECO:0000269|PubMed:24097983}.
Bacillus subtilis (strain 168)
O07600
FABH2_BACSU
MSKAKITAIGTYAPSRRLTNADLEKIVDTSDEWIVQRTGMRERRIADEHQFTSDLCIEAVKNLKSRYKGTLDDVDMILVATTTSDYAFPSTACRVQEYFGWESTGALDINATCAGLTYGLHLANGLITSGLHQKILVIAGETLSKVTDYTDRTTCVLFGDAAGALLVERDEETPGFLASVQGTSGNGGDILYRAGLRNEINGVQLVGSGKMVQNGREVYKWAARTVPGEFERLLHKAGLSSDDLDWFVPHSANLRMIESICEKTPFPIEKTLTSVEHYGNTSSVSIVLALDLAVKAGKLKKDQIVLLFGFGGGLTYTGLLIKWGM
2.3.1.180; 2.3.1.300
null
fatty acid biosynthetic process [GO:0006633]; secondary metabolite biosynthetic process [GO:0044550]
cytoplasm [GO:0005737]
3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; beta-ketoacyl-acyl-carrier-protein synthase III activity [GO:0033818]
PF08545;PF08541;
3.40.47.10;
Thiolase-like superfamily, FabH family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CATALYTIC ACTIVITY: Reaction=3-methylbutanoyl-CoA + H(+) + malonyl-[ACP] = 5-methyl-3-oxohexanoyl-[ACP] + CO2 + CoA; Xref=Rhea:RHEA:42272, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9941, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57345, ChEBI:CHEBI:78449, ChEBI:CHEBI:78822; EC=2.3.1.300; Evidence={ECO:0000269|PubMed:10629181}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42273; Evidence={ECO:0000269|PubMed:10629181}; CATALYTIC ACTIVITY: Reaction=2-methylpropanoyl-CoA + H(+) + malonyl-[ACP] = 4-methyl-3-oxopentanoyl-[ACP] + CO2 + CoA; Xref=Rhea:RHEA:42268, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9940, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57338, ChEBI:CHEBI:78449, ChEBI:CHEBI:78820; EC=2.3.1.300; Evidence={ECO:0000269|PubMed:10629181}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42269; Evidence={ECO:0000269|PubMed:10629181}; CATALYTIC ACTIVITY: Reaction=(2S)-2-methylbutanoyl-CoA + H(+) + malonyl-[ACP] = (4S)-4-methyl-3-oxohexanoyl-[ACP] + CO2 + CoA; Xref=Rhea:RHEA:42276, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:17148, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:78449, ChEBI:CHEBI:88166, ChEBI:CHEBI:167462; EC=2.3.1.300; Evidence={ECO:0000269|PubMed:10629181}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42277; Evidence={ECO:0000269|PubMed:10629181}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] + CO2 + CoA; Xref=Rhea:RHEA:12080, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9625, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:78449, ChEBI:CHEBI:78450; EC=2.3.1.180; Evidence={ECO:0000255|HAMAP-Rule:MF_01815, ECO:0000269|PubMed:10629181}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12081; Evidence={ECO:0000269|PubMed:10629181}; CATALYTIC ACTIVITY: Reaction=H(+) + malonyl-[ACP] + propanoyl-CoA = 3-oxopentanoyl-[ACP] + CO2 + CoA; Xref=Rhea:RHEA:42244, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9939, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57392, ChEBI:CHEBI:78449, ChEBI:CHEBI:78818; Evidence={ECO:0000269|PubMed:10629181}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42245; Evidence={ECO:0000269|PubMed:10629181}; CATALYTIC ACTIVITY: Reaction=butanoyl-CoA + H(+) + malonyl-[ACP] = 3-oxohexanoyl-[ACP] + CO2 + CoA; Xref=Rhea:RHEA:42248, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9629, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57371, ChEBI:CHEBI:78449, ChEBI:CHEBI:78456; Evidence={ECO:0000269|PubMed:10629181}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42249; Evidence={ECO:0000269|PubMed:10629181}; CATALYTIC ACTIVITY: Reaction=H(+) + malonyl-[ACP] + pentanoyl-CoA = 3-oxoheptanoyl-[ACP] + CO2 + CoA; Xref=Rhea:RHEA:42252, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9943, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57389, ChEBI:CHEBI:78449, ChEBI:CHEBI:78824; Evidence={ECO:0000269|PubMed:10629181}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42253; Evidence={ECO:0000269|PubMed:10629181}; CATALYTIC ACTIVITY: Reaction=H(+) + hexanoyl-CoA + malonyl-[ACP] = 3-oxooctanoyl-[ACP] + CO2 + CoA; Xref=Rhea:RHEA:42256, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9633, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:62620, ChEBI:CHEBI:78449, ChEBI:CHEBI:78460; Evidence={ECO:0000269|PubMed:10629181}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42257; Evidence={ECO:0000269|PubMed:10629181}; CATALYTIC ACTIVITY: Reaction=H(+) + heptanoyl-CoA + malonyl-[ACP] = 3-oxononanoyl-[ACP] + CO2 + CoA; Xref=Rhea:RHEA:42260, Rhea:RHEA-COMP:9623, Rhea:RHEA-COMP:9944, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:78449, ChEBI:CHEBI:78811, ChEBI:CHEBI:78826; Evidence={ECO:0000269|PubMed:10629181}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42261; Evidence={ECO:0000269|PubMed:10629181};
null
PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01815}.
null
null
FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Has some substrate specificity for branched chain acyl-CoA, determining the biosynthesis of branched-chain of fatty acids instead of straight-chain. {ECO:0000269|PubMed:10629181}.
Bacillus subtilis (strain 168)
O07623
SBOA_BACSU
MKKAVIVENKGCATCSIGAACLVDGPIPDFEIAGATGLFGLWG
null
null
defense response to bacterium [GO:0042742]; killing of cells of another organism [GO:0031640]
extracellular region [GO:0005576]
null
PF11420;
null
Bacteriocin class V family
PTM: This sactipeptide undergoes unique processing steps that include proteolytic cleavage after Glu-8, and covalent linkage of the alpha-amino of Asn-9 with the carboxyl of Gly-43 to form a cyclopeptide (PubMed:12696888, PubMed:22366720). Thioether cross-links are formed between cysteines and the alpha-carbons of other amino acids, Cys-12 to Phe-39, Cys-15 to Thr-36, and Cys-21 to Phe-30 (PubMed:12696888, PubMed:22366720). In forming these cross-links, Thr-36 and Phe-39 are converted to D-amino acids (PubMed:12696888). Propeptide cleavage and cyclopeptide formation only occur after all 3 thioether cross-links are formed (PubMed:22366720). {ECO:0000269|PubMed:12696888, ECO:0000269|PubMed:22366720}.
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3936839}.
null
null
null
null
null
FUNCTION: Has bacteriocidal activity against some Gram-positive bacteria such as Listeria, some species of Bacillus and E.faecium (PubMed:10572140, PubMed:19633086, PubMed:3936839). A single mutation (Thr-14-Ile) confers hemolytic activity against rabbit and human blood (PubMed:19633086). {ECO:0000269|PubMed:10572140, ECO:0000269|PubMed:19633086, ECO:0000269|PubMed:3936839}.
Bacillus subtilis (strain 168)
O07732
LIPJ_MYCTU
MAQAPHIHRTRYAKCGDMDIAYQVLGDGPTDLLVLPGPFVPIDSIDDEPSLYRFHRRLASFSRVIRLDHRGVGLSSRLAAITTLGPKFWAQDAIAVMDAVGCEQATIFAPSFHAMNGLVLAADYPERVRSLIVVNGSARPLWAPDYPVGAQVRRADPFLTVALEPDAVERGFDVLSIVAPTVAGDDVFRAWWDLAGNRAGPPSIARAVSKVIAEADVRDVLGHIEAPTLILHRVGSTYIPVGHGRYLAEHIAGSRLVELPGTDTLYWVGDTGPMLDEIEEFITGVRGGADAERMLATIMFTDIVGSTQHAAALGDDRWRDLLDNHDTIVCHEIQRFGGREVNTAGDGFVATFTSPSAAIACADDIVDAVAALGIEVRIGIHAGEVEVRDASHGTDVAGVAVHIGARVCALAGPSEVLVSSTVRDIVAGSRHRFAERGEQELKGVPGRWRLCVLMRDDATRTR
3.1.1.-; 4.6.1.1
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:15678099}; Note=Cannot use Mg(2+) as a cofactor. {ECO:0000269|PubMed:15678099};
cAMP biosynthetic process [GO:0006171]; intracellular signal transduction [GO:0035556]; lipid metabolic process [GO:0006629]
null
adenylate cyclase activity [GO:0004016]; hydrolase activity [GO:0016787]; manganese ion binding [GO:0030145]; protein homodimerization activity [GO:0042803]
PF00561;PF00211;
3.40.50.1820;3.30.70.1230;
AB hydrolase superfamily; Adenylyl cyclase class-4/guanylyl cyclase family
null
null
CATALYTIC ACTIVITY: Reaction=a fatty acid ester + H2O = a fatty acid + an aliphatic alcohol + H(+); Xref=Rhea:RHEA:59388, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:35748; Evidence={ECO:0000269|PubMed:33960821}; CATALYTIC ACTIVITY: Reaction=ATP = 3',5'-cyclic AMP + diphosphate; Xref=Rhea:RHEA:15389, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58165; EC=4.6.1.1; Evidence={ECO:0000269|PubMed:15678099}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15390; Evidence={ECO:0000269|PubMed:15678099}; CATALYTIC ACTIVITY: Reaction=decanoate ester + H2O = an aliphatic alcohol + decanoate + H(+); Xref=Rhea:RHEA:47360, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:27689, ChEBI:CHEBI:87658; Evidence={ECO:0000269|PubMed:33960821}; CATALYTIC ACTIVITY: Reaction=an octanoate ester + H2O = an aliphatic alcohol + H(+) + octanoate; Xref=Rhea:RHEA:47356, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:87657; Evidence={ECO:0000269|PubMed:33960821}; CATALYTIC ACTIVITY: Reaction=a dodecanoate ester + H2O = an aliphatic alcohol + dodecanoate + H(+); Xref=Rhea:RHEA:47364, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18262, ChEBI:CHEBI:87659; Evidence={ECO:0000269|PubMed:33960821}; CATALYTIC ACTIVITY: Reaction=a butanoate ester + H2O = an aliphatic alcohol + butanoate + H(+); Xref=Rhea:RHEA:47348, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:50477; Evidence={ECO:0000269|PubMed:33960821};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=69 uM for pNP-decanoate {ECO:0000269|PubMed:33960821}; KM=83 uM for pNP-decanoate (for N-terminal lipolytic domain) {ECO:0000269|PubMed:33960821}; Vmax=500 nmol/min/mg enzyme (for adenylate cyclase activity) {ECO:0000269|PubMed:15678099}; Vmax=1300 nmol/min/mg enzyme (for C-terminal cyclase domain and adenylate cyclase activity) {ECO:0000269|PubMed:15678099}; Note=kcat is 140 min(-1) for lipolytic activity. kcat is 355 min(-1) for N-terminal lipolytic domain and lipolytic activity. {ECO:0000269|PubMed:33960821};
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0 for lipolytic activity of the full-length protein. {ECO:0000269|PubMed:33960821};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 40 degrees Celsius for lipolytic activity with pNP-decanoate as substrate (PubMed:33960821). Optimum temperature is 45 degrees Celsius for adenylate cyclase activity (PubMed:15678099). {ECO:0000269|PubMed:15678099, ECO:0000269|PubMed:33960821};
FUNCTION: May play a role in cell wall modulation (PubMed:33960821, PubMed:34019937). The N-terminal domain exhibits lipolytic activity (PubMed:33960821). In vitro, hydrolyzes various p-nitrophenyl (pNP) esters (PubMed:33960821). pNP-decanoate (C10) is the best substrate, followed by pNP-octonate (C8), pNP-laurate (C12) and pNP-butyrate (C4) (PubMed:33960821). Exhibits lower activity with pNP-acetate (C2), pNP-myristate (C14) and pNP-palmitate (C16) (PubMed:33960821). Can also use tributyrin (PubMed:33960821). The C-terminal domain catalyzes the biosynthesis of cyclic AMP (cAMP) from ATP (PubMed:15678099). It has a guanylyl cyclase side-activity, corresponding to 7% of the adenylate cyclase activity (PubMed:15678099). {ECO:0000269|PubMed:15678099, ECO:0000269|PubMed:33960821, ECO:0000269|PubMed:34019937}.
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
O07783
VAPC4_MYCTU
MNVRRALADTSVFIGIEATRFDPDRFAGYEWGVSVVTLGELRLGVLQASGPEAAARRLSTYQLAQRFEPLGIDEAVSEAWALLVSKLRAAKLRVPINDSWIAATAVAHGIAILTQDNDYAAMPDVEVITI
3.1.-.-
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00265};
modulation by symbiont of host process [GO:0044003]
extracellular region [GO:0005576]
magnesium ion binding [GO:0000287]; RNA binding [GO:0003723]; RNA nuclease activity [GO:0004540]; toxin sequestering activity [GO:0097351]
PF01850;
3.40.50.1010;
PINc/VapC protein family
null
SUBCELLULAR LOCATION: Secreted. Note=Following 6 weeks of nutrient starvation. {ECO:0000269|PubMed:23345537}.
null
null
null
null
null
FUNCTION: Toxic component of a type II toxin-antitoxin (TA) system. Probably exerts its toxic effect by binding to mRNA, inhibiting translation. Binds to, recognizes and cleaves ssRNA at ACGC and AC(A/U)GC sequences, usually between the G and C; cleavage is not very efficient, nor is cleavage required to inhibit protein synthesis. Upon expression in situ, in M.smegmatis or E.coli inhibits cell growth and colony formation; in at least E.coli also causes increased levels of cellular RNA. Its toxic effect is neutralized by coexpression with cognate antitoxin VapB4. {ECO:0000269|PubMed:19016878, ECO:0000269|PubMed:22354968, ECO:0000269|PubMed:25622615}.
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
O07834
DAPB1_PSEMX
MKPTSLLLAATVLMSTPITSALAASATPPDVAKKPHVVKAPHGAERNDEYYWLRDDKRENKEMLAYLNAENAYTDAVMAPLKPLEDKLYDEVVARIKQDDASVPYRERGWWYYARFVTGKDYPVHARRKDGPGVDAVSIQAANAAGDFAGEQVLLDVNALGAGKDYYNVGDYEVSQDNRLLAYADDTNGRRQYTIRFKNLDTGELLPDTVTNAEPNLVWSDDGRTLFYVDKDPETLLSKRVKAHVLGTPASQDALVYEEEDDSFYMGIGRSRDDKFICISVESTVSSEMRCTPAASPGVFTVLAPRERDVEYQADHLGDRWVIRTNADGATNFKIVTAPTDSTSRKDWKDWVAHRDDVFVEGFELFDGFSVVAERANALESLRVIKADGSSDYVKADESAYSMGLSANPETGTDWLRYSYTSMTTPATTYEINTKTGERRQLKQQPVPGYDASKYVTERVWAPARDGKTKIPVTLVYRKDVARDGKAPMLQYAYGSYGASMDPNFSITNVSLLDRGVVYALAHIRGGQEMGRAWYDDGKLYNKINTFTDFIDVTDYLVKEGYAAKDRVAAMGGSAGGLLMGAVSNMAPEKYKVILTLVPFVDVVTTMLDPTIPLTTNEYDEWGNPEEKGYYDYILTYSPYDNLQAKAYPAMFVGTGLWDSQVQYWEPAKYVARLRDLNTGKGPVVFRTNMEAGHGGKSGRFRQYRERAEMFAFMLDQLGVASK
3.4.14.-
null
proteolysis involved in protein catabolic process [GO:0051603]
cytoskeleton [GO:0005856]
aminopeptidase activity [GO:0004177]; dipeptidyl-peptidase activity [GO:0008239]; serine-type endopeptidase activity [GO:0004252]
PF00326;PF02897;
3.40.50.1820;2.130.10.120;
Peptidase S9A family
null
null
null
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.25 mM for Gly-Arg-pNA (at pH 9 and 37 degrees Celsius) {ECO:0000269|PubMed:8631703}; KM=0.019 mM for Arg-Arg-4-methoxy-beta-naphthylamide (Arg-Arg-MNA) (at pH 9 and 37 degrees Celsius) {ECO:0000269|PubMed:8631703}; KM=0.052 mM for Gly-Arg-MNA (at pH 9 and 37 degrees Celsius) {ECO:0000269|PubMed:8631703}; Vmax=195 umol/min/mg enzyme with Gly-Arg-pNA as substrate (at pH 9 and 37 degrees Celsius) {ECO:0000269|PubMed:8631703}; Vmax=145 umol/min/mg enzyme with Arg-Arg-MNA as substrate (at pH 9 and 37 degrees Celsius) {ECO:0000269|PubMed:8631703}; Vmax=95 umol/min/mg enzyme with Gly-Arg-MNA as substrate (at pH 9 and 37 degrees Celsius) {ECO:0000269|PubMed:8631703};
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.0 for the hydrolysis of Gly-Arg-pNA. No hydrolysis of Gly-Arg-pNA is detected below pH 5.5 or above pH 11.5. Stable over a broad pH range of between 7.5 and 10.0. {ECO:0000269|PubMed:8631703};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is between 35 and 40 degrees Celsius for the hydrolysis of Gly-Arg-pNA. Stable for at least 30 minutes below 20 degrees Celsius.;
FUNCTION: Sequentially removes dipeptide units (NH3-P2-P1-) from the amino termini of peptides and proteins. Is able to catalyze the removal of Asp-Arg from the amino termini of angiotensins I and II. Has slight endopeptidase activity on N-terminally blocked peptide derivatives which contain arginine residues at the P1 position. Does not hydrolyze Ala-Ala-Ala and Ala-Ala-Ala-Ala substrates or insulin beta chain. {ECO:0000269|PubMed:8631703}.
Pseudoxanthomonas mexicana
O08314
TGT_HELPY
MDFQLQATDNNARAGLLNLAHSQVATPVFMPVGTQGCIKSLDATDAQEILGAKLILANTYHMYLRPGEKVVEELGGLHRFAQFYGSFLTDSGGFQAFSLSDNVKLQEDGIVFKSHIDGSKHLFTPAKVLDIQYSLNSDIMMVLDDLVGLPAPLKRLEESIKRSAKWANMSLEYHKEKNRPSNNLFAIIQGGTHLKMRSLSVGLTHEGFDGYAIGGLAVGESADEMLETIAHTAPLLPKDKPRYLMGVGTPENILDAISLGVDMFDCVMPTRNARNATLFTHSGKISIKNAPYKLDNTPIEENCACYACKRYSKAYLHHLFRAKELTYARLASLHNLHFYLELVKNARNAILEKRFLSFKKEFLEKYNSRSH
2.4.2.29
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_00168}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00168};
queuosine biosynthetic process [GO:0008616]; tRNA wobble guanine modification [GO:0002099]; tRNA-guanine transglycosylation [GO:0101030]
cytosol [GO:0005829]
metal ion binding [GO:0046872]; tRNA-guanosine(34) queuine transglycosylase activity [GO:0008479]
PF01702;
3.20.20.105;
Queuine tRNA-ribosyltransferase family
null
null
CATALYTIC ACTIVITY: Reaction=7-aminomethyl-7-carbaguanine + guanosine(34) in tRNA = 7-aminomethyl-7-carbaguanosine(34) in tRNA + guanine; Xref=Rhea:RHEA:24104, Rhea:RHEA-COMP:10341, Rhea:RHEA-COMP:10342, ChEBI:CHEBI:16235, ChEBI:CHEBI:58703, ChEBI:CHEBI:74269, ChEBI:CHEBI:82833; EC=2.4.2.29; Evidence={ECO:0000255|HAMAP-Rule:MF_00168};
null
PATHWAY: tRNA modification; tRNA-queuosine biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00168}.
null
null
FUNCTION: Catalyzes the base-exchange of a guanine (G) residue with the queuine precursor 7-aminomethyl-7-deazaguanine (PreQ1) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr). Catalysis occurs through a double-displacement mechanism. The nucleophile active site attacks the C1' of nucleotide 34 to detach the guanine base from the RNA, forming a covalent enzyme-RNA intermediate. The proton acceptor active site deprotonates the incoming PreQ1, allowing a nucleophilic attack on the C1' of the ribose to form the product. After dissociation, two additional enzymatic reactions on the tRNA convert PreQ1 to queuine (Q), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine). {ECO:0000255|HAMAP-Rule:MF_00168}.
Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
O08333
PFP_STRCO
MKVGVLTGGGDCPGLNAVIRAVVRKGVQEYGYDFTGFRDGWRGPLEGDTVPLDIPAVRGILPRGGTVLGSSRTNPLKQRDGIRRIKDNLAALGVEALITIGGEDTLGVATRLADEYGVPCVGVPKTIDNDLSATDYTFGFDTAVGIATEAIDRLHTTAESHMRVLVVEVMGRHAGWIALHSGLAGGANVILIPEQRFDVEQVCSWVTSRFRASYAPIVVVAEGAMPRDGDMVLKDESLDSYGHVRLSGVGEWLAKQIEKRTGNEARTTVLGHVQRGGTPSAFDRWLATRFGLHAVDCVHDGDFGKMVALRGTDIVRVPIAEATARLKTVDPALYEEVGVFFG
2.7.1.90
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_01976};
canonical glycolysis [GO:0061621]; fructose 1,6-bisphosphate metabolic process [GO:0030388]; fructose 6-phosphate metabolic process [GO:0006002]
6-phosphofructokinase complex [GO:0005945]
6-phosphofructokinase activity [GO:0003872]; AMP binding [GO:0016208]; ATP binding [GO:0005524]; diphosphate-fructose-6-phosphate 1-phosphotransferase activity [GO:0047334]; fructose-6-phosphate binding [GO:0070095]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; monosaccharide binding [GO:0048029]
PF00365;
3.40.50.450;3.40.50.460;
Phosphofructokinase type A (PFKA) family, Mixed-substrate PFK group III subfamily
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01976}.
CATALYTIC ACTIVITY: Reaction=beta-D-fructose 6-phosphate + diphosphate = beta-D-fructose 1,6-bisphosphate + H(+) + phosphate; Xref=Rhea:RHEA:13613, ChEBI:CHEBI:15378, ChEBI:CHEBI:32966, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=2.7.1.90; Evidence={ECO:0000255|HAMAP-Rule:MF_01976};
null
PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. {ECO:0000255|HAMAP-Rule:MF_01976}.
null
null
FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions. {ECO:0000255|HAMAP-Rule:MF_01976}.
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
O08336
CYPB_BACSU
MKQASAIPQPKTYGPLKNLPHLEKEQLSQSLWRIADELGPIFRFDFPGVSSVFVSGHNLVAEVCDEKRFDKNLGKGLQKVREFGGDGLFTSWTHEPNWQKAHRILLPSFSQKAMKGYHSMMLDIATQLIQKWSRLNPNEEIDVADDMTRLTLDTIGLCGFNYRFNSFYRDSQHPFITSMLRALKEAMNQSKRLGLQDKMMVKTKLQFQKDIEVMNSLVDRMIAERKANPDENIKDLLSLMLYAKDPVTGETLDDENIRYQIITFLIAGHETTSGLLSFAIYCLLTHPEKLKKAQEEADRVLTDDTPEYKQIQQLKYIRMVLNETLRLYPTAPAFSLYAKEDTVLGGEYPISKGQPVTVLIPKLHRDQNAWGPDAEDFRPERFEDPSSIPHHAYKPFGNGQRACIGMQFALQEATMVLGLVLKHFELINHTGYELKIKEALTIKPDDFKITVKPRKTAAINVQRKEQADIKAETKPKETKPKHGTPLLVLFGSNLGTAEGIAGELAAQGRQMGFTAETAPLDDYIGKLPEEGAVVIVTASYNGAPPDNAAGFVEWLKELEEGQLKGVSYAVFGCGNRSWASTYQRIPRLIDDMMKAKGASRLTAIGEGDAADDFESHRESWENRFWKETMDAFDINEIAQKEDRPSLSITFLSEATETPVAKAYGAFEGIVLENRELQTAASTRSTRHIELEIPAGKTYKEGDHIGILPKNSRELVQRVLSRFGLQSNHVIKVSGSAHMAHLPMDRPIKVVDLLSSYVELQEPASRLQLRELASYTVCPPHQKELEQLVSDDGIYKEQVLAKRLTMLDFLEDYPACEMPFERFLALLPSLKPRYYSISSSPKVHANIVSMTVGVVKASAWSGRGEYRGVASNYLAELNTGDAAACFIRTPQSGFQMPNDPETPMIMVGPGTGIAPFRGFIQARSVLKKEGSTLGEALLYFGCRRPDHDDLYREELDQAEQDGLVTIRRCYSRVENEPKGYVQHLLKQDTQKLMTLIEKGAHIYVCGDGSQMAPDVERTLRLAYEAEKAASQEESAVWLQKLQDQRRYVKDVWTGM
1.14.14.1; 1.6.2.4
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:15122913}; COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:15122913}; COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000269|PubMed:15122913};
fatty acid oxidation [GO:0019395]; response to hormone [GO:0009725]
cytosol [GO:0005829]
aromatase activity [GO:0070330]; fatty acid binding [GO:0005504]; flavin adenine dinucleotide binding [GO:0050660]; FMN binding [GO:0010181]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; NADPH-hemoprotein reductase activity [GO:0003958]; oxidoreductase activity [GO:0016491]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen [GO:0016712]
PF00667;PF00258;PF00175;PF00067;
3.40.50.360;1.10.630.10;3.40.50.80;2.40.30.10;
Cytochrome P450 family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30879, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:142491; EC=1.14.14.1; Evidence={ECO:0000269|PubMed:14741768, ECO:0000269|PubMed:15122913}; CATALYTIC ACTIVITY: Reaction=NADPH + 2 oxidized [cytochrome P450] = H(+) + NADP(+) + 2 reduced [cytochrome P450]; Xref=Rhea:RHEA:24040, Rhea:RHEA-COMP:14627, Rhea:RHEA-COMP:14628, ChEBI:CHEBI:15378, ChEBI:CHEBI:55376, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:60344; EC=1.6.2.4; Evidence={ECO:0000269|PubMed:14741768, ECO:0000269|PubMed:15122913};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=165 uM for lauric acid {ECO:0000269|PubMed:15122913}; KM=542 uM for myristic acid {ECO:0000269|PubMed:15122913}; KM=337 uM for palmitic acid {ECO:0000269|PubMed:15122913}; KM=68.5 uM for stearic acid {ECO:0000269|PubMed:15122913}; KM=28.7 uM for phytanic acid {ECO:0000269|PubMed:15122913}; KM=68.3 uM for 15-methylpalmitic acid {ECO:0000269|PubMed:15122913}; KM=79 uM for arachidonic acid {ECO:0000269|PubMed:15122913}; KM=5.1 uM for NADPH {ECO:0000269|PubMed:15122913}; KM=2.43 mM for NADH {ECO:0000269|PubMed:15122913}; KM=10.9 uM for cytochrome c (in the reductase assay) {ECO:0000269|PubMed:15122913}; KM=285 uM for ferricyanide (in the reductase assay) {ECO:0000269|PubMed:15122913}; Note=kcat is 104 min(-1) for lauric acid hydroxylation. kcat is 5556 min(-1) for myristic acid hydroxylation. kcat is 676 min(-1) for palmitic acid hydroxylation. kcat is 374 min(-1) for stearic acid hydroxylation. kcat is 794 min(-1) for phytanic acid hydroxylation. kcat is 3845 min(-1) for 15-methylpalmitic acid hydroxylation. kcat is 1690 min(-1) for arachidonic acid hydroxylation. kcat is 3520 min(-1) for the reduction of cytochrome c. kcat is 37050 min(-1) for the reduction of ferricyanide. {ECO:0000269|PubMed:15122913};
null
null
null
FUNCTION: Functions as a fatty acid monooxygenase. Catalyzes hydroxylation of a range of medium to long-chain fatty acids, with a preference for long-chain unsaturated and branched-chain fatty acids over saturated fatty acids. Hydroxylation of myristic acid occurs mainly at the omega-2 and omega-3 positions, in approximately equal proportions. Also displays a NADPH-dependent reductase activity in the C-terminal domain, which allows electron transfer from NADPH to the heme iron of the cytochrome P450 N-terminal domain. {ECO:0000269|PubMed:14741768, ECO:0000269|PubMed:15122913}.
Bacillus subtilis (strain 168)
O08394
CYPD_BACSU
MKETSPIPQPKTFGPLGNLPLIDKDKPTLSLIKLAEEQGPIFQIHTPAGTTIVVSGHELVKEVCDEERFDKSIEGALEKVRAFSGDGLFTSWTHEPNWRKAHNILMPTFSQRAMKDYHEKMVDIAVQLIQKWARLNPNEAVDVPGDMTRLTLDTIGLCGFNYRFNSYYRETPHPFINSMVRALDEAMHQMQRLDVQDKLMVRTKRQFRYDIQTMFSLVDSIIAERRANGDQDEKDLLARMLNVEDPETGEKLDDENIRFQIITFLIAGHETTSGLLSFATYFLLKHPDKLKKAYEEVDRVLTDAAPTYKQVLELTYIRMILNESLRLWPTAPAFSLYPKEDTVIGGKFPITTNDRISVLIPQLHRDRDAWGKDAEEFRPERFEHQDQVPHHAYKPFGNGQRACIGMQFALHEATLVLGMILKYFTLIDHENYELDIKQTLTLKPGDFHISVQSRHQEAIHADVQAAEKAAPDEQKEKTEAKGASVIGLNNRPLLVLYGSDTGTAEGVARELADTASLHGVRTKTAPLNDRIGKLPKEGAVVIVTSSYNGKPPSNAGQFVQWLQEIKPGELEGVHYAVFGCGDHNWASTYQYVPRFIDEQLAEKGATRFSARGEGDVSGDFEGQLDEWKKSMWADAIKAFGLELNENADKERSTLSLQFVRGLGESPLARSYEASHASIAENRELQSADSDRSTRHIEIALPPDVEYQEGDHLGVLPKNSQTNVSRILHRFGLKGTDQVTLSASGRSAGHLPLGRPVSLHDLLSYSVEVQEAATRAQIRELASFTVCPPHRRELEELSAEGVYQEQILKKRISMLDLLEKYEACDMPFERFLELLRPLKPRYYSISSSPRVNPRQASITVGVVRGPAWSGRGEYRGVASNDLAERQAGDDVVMFIRTPESRFQLPKDPETPIIMVGPGTGVAPFRGFLQARDVLKREGKTLGEAHLYFGCRNDRDFIYRDELERFEKDGIVTVHTAFSRKEGMPKTYVQHLMADQADTLISILDRGGRLYVCGDGSKMAPDVEAALQKAYQAVHGTGEQEAQNWLRHLQDTGMYAKDVWAGI
1.14.14.1; 1.6.2.4
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:15122913}; COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:15122913}; COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000269|PubMed:15122913};
fatty acid oxidation [GO:0019395]; response to hormone [GO:0009725]
cytosol [GO:0005829]
aromatase activity [GO:0070330]; fatty acid binding [GO:0005504]; flavin adenine dinucleotide binding [GO:0050660]; FMN binding [GO:0010181]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; NADPH-hemoprotein reductase activity [GO:0003958]; oxidoreductase activity [GO:0016491]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen [GO:0016712]
PF00667;PF00258;PF00175;PF00067;
3.40.50.360;1.10.630.10;3.40.50.80;2.40.30.10;
Cytochrome P450 family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30879, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:142491; EC=1.14.14.1; Evidence={ECO:0000269|PubMed:15122913, ECO:0000269|PubMed:15375636}; CATALYTIC ACTIVITY: Reaction=NADPH + 2 oxidized [cytochrome P450] = H(+) + NADP(+) + 2 reduced [cytochrome P450]; Xref=Rhea:RHEA:24040, Rhea:RHEA-COMP:14627, Rhea:RHEA-COMP:14628, ChEBI:CHEBI:15378, ChEBI:CHEBI:55376, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:60344; EC=1.6.2.4; Evidence={ECO:0000269|PubMed:15122913, ECO:0000269|PubMed:15375636};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=38.8 uM for stearic acid {ECO:0000269|PubMed:15122913}; KM=150 uM for phytanic acid {ECO:0000269|PubMed:15122913}; KM=56.8 uM for 15-methylpalmitic acid {ECO:0000269|PubMed:15122913}; KM=3.6 uM for NADPH {ECO:0000269|PubMed:15122913}; KM=17.9 mM for NADH {ECO:0000269|PubMed:15122913}; KM=6.9 uM for cytochrome c (in the reductase assay) {ECO:0000269|PubMed:15122913}; KM=153.4 uM for ferricyanide (in the reductase assay) {ECO:0000269|PubMed:15122913}; KM=17.36 uM for oleic acid {ECO:0000269|PubMed:15375636}; Note=kcat is 430 min(-1) for stearic acid hydroxylation. kcat is 5430 min(-1) for phytanic acid hydroxylation. kcat is 6105 min(-1) for 15-methylpalmitic acid hydroxylation. kcat is 11400 min(-1) for the reduction of cytochrome c. kcat is 38150 min(-1) for the reduction of ferricyanide (PubMed:15122913). kcat is 2244 min(-1) for oleic acid hydroxylation (PubMed:15375636). {ECO:0000269|PubMed:15122913, ECO:0000269|PubMed:15375636};
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:15375636};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 51 degrees Celsius. However, enzyme stability is dramatically reduced at this temperature, incubation for 30 minutes at 31 and 49 degrees Celsius results in 61% and 17% residual activity, respectively. Incubation at 60 degrees Celsius leads to total inactivation of the enzyme. {ECO:0000269|PubMed:15375636};
FUNCTION: Functions as a fatty acid monooxygenase. Catalyzes hydroxylation of a range of long-chain fatty acids, with a preference for long-chain unsaturated and branched-chain fatty acids over saturated fatty acids. Hydroxylation of myristic acid occurs mainly at the omega-2 position. Also displays a NADPH-dependent reductase activity in the C-terminal domain, which allows electron transfer from NADPH to the heme iron of the cytochrome P450 N-terminal domain (PubMed:15122913, PubMed:15375636). Is also able to catalyze efficient oxidation of sodium dodecyl sulfate (SDS) (PubMed:21048857). {ECO:0000269|PubMed:15122913, ECO:0000269|PubMed:15375636, ECO:0000269|PubMed:21048857}.
Bacillus subtilis (strain 168)
O08467
GLNA_THEKO
MNEIKGIERAVQVEVPRPRFLLLAFTDINGSLKGMEIPMERYEEAVEDGVSFDGSSIPGFEGIEDSDLIFKADPSTYAEIPWEGIGRVYGYIYKGDEPYQADPRGILKRVLERLEKEGLKAHIGPEPEFYIFKKNGTWELHIPDSGGYFDLVGLDKAREIRREIALYMPYLGLKPEVLHHEVGKAQHEIDFRYDEALRTADNIVSFKHVVKAVAELHGYYATFMPKPIYGFPGNGMHLHISLWKDGENVFIGEDGLSDTALHFIGGILKHAKALAALTNPTVNSYKRLVPGYEAPVYISWGYRNRSALIRVPAFKGSGARIEYRCPDPSANPYLALAGILMVGLDGIKKKVEPDSYVETNVYEMDDAERERLGIDTLPGSLGEALEELKKDKTVREALGGAYKNFIDYKEREWEEYIEYLSSRDIPIDTKKVTEWELERYFYV
6.3.1.2
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:9172372}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:9172372}; Note=Binds 2 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250|UniProtKB:P9WN39};
glutamine biosynthetic process [GO:0006542]; polyamine catabolic process [GO:0006598]
cytoplasm [GO:0005737]
ATP binding [GO:0005524]; glutamine synthetase activity [GO:0004356]; metal ion binding [GO:0046872]
PF00120;PF03951;
3.10.20.70;3.30.590.10;
Glutamine synthetase family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CATALYTIC ACTIVITY: Reaction=ATP + L-glutamate + NH4(+) = ADP + H(+) + L-glutamine + phosphate; Xref=Rhea:RHEA:16169, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.1.2; Evidence={ECO:0000269|PubMed:9172372}; CATALYTIC ACTIVITY: Reaction=ATP + hydroxylamine + L-glutamate = ADP + L-glutamine hydroxamate + phosphate; Xref=Rhea:RHEA:45804, ChEBI:CHEBI:15429, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:85433, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:9172372};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=23.5 mM for L-glutamate (at pH 7.8 and 60 degrees Celsius) {ECO:0000269|PubMed:9172372}; KM=15.2 mM for hydroxylamine (when a high concentration is used, at pH 7.8 and 60 degrees Celsius) {ECO:0000269|PubMed:9172372}; KM=1.6 mM for hydroxylamine (when a low concentration is used, at pH 7.8 and 60 degrees Celsius) {ECO:0000269|PubMed:9172372}; KM=28 mM for ATP (at pH 7.8 and 60 degrees Celsius) {ECO:0000269|PubMed:9172372}; KM=5 mM for L-glutamine (at pH 7.2 and 60 degrees Celsius) {ECO:0000269|PubMed:9172372}; KM=6.3 mM for ADP (at pH 7.2 and 60 degrees Celsius) {ECO:0000269|PubMed:9172372}; Note=kcat is 2190 min(-1) towards L-glutamate in the synthetase reaction and 3900 min(-1) towards L-glutamine in the transferase reaction.;
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.8 for the synthetase reaction and pH 7.2 for the transferase reaction. {ECO:0000269|PubMed:9172372};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 60 degrees Celsius for both transferase and synthetase activities. {ECO:0000269|PubMed:9172372};
FUNCTION: Carries out the ATP-dependent synthesis of glutamine from ammonium nitrogen and glutamate. Exhibits both L-gamma-glutamylhydroxamate synthetase and gamma-glutamyltransferase activities when using hydroxylamine as substrate; in fact, the enzyme possesses low biosynthetic activity, suggesting that the reaction is biased towards the degradation of glutamine under ammonia-rich conditions. Might play some role in ammonia assimilation under ammonia-starvation conditions. Can also use GTP instead of ATP in the synthetase reaction, but not CTP or UTP. {ECO:0000269|PubMed:9172372}.
Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1))
O08498
BLAB1_ELIME
MLKKIKISLILALGLTSLQAFGQENPDVKIEKLKDNLYVYTTYNTFNGTKYAANAVYLVTDKGVVVIDCPWGEDKFKSFTDEIYKKHGKKVIMNIATHSHDDRAGGLEYFGKIGAKTYSTKMTDSILAKENKPRAQYTFDNNKSFKVGKSEFQVYYPGKGHTADNVVVWFPKEKVLVGGCIIKSADSKDLGYIGEAYVNDWTQSVHNIQQKFSGAQYVVAGHDDWKDQRSIQHTLDLINEYQQKQKASN
3.5.2.6
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:12684522}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:12684522};
antibiotic catabolic process [GO:0017001]; response to antibiotic [GO:0046677]
periplasmic space [GO:0042597]
beta-lactamase activity [GO:0008800]; zinc ion binding [GO:0008270]
PF00753;
3.60.15.10;
Metallo-beta-lactamase superfamily, Class-B beta-lactamase family
null
SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CATALYTIC ACTIVITY: Reaction=a beta-lactam + H2O = a substituted beta-amino acid; Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627, ChEBI:CHEBI:140347; EC=3.5.2.6; Evidence={ECO:0000269|PubMed:9576862};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=24 uM for cefoxitin {ECO:0000269|PubMed:9576862}; KM=29 uM for cephaloridine {ECO:0000269|PubMed:9576862}; KM=32 uM for penicillin G {ECO:0000269|PubMed:9576862}; KM=43 uM for 6-beta-iodopenicillanate {ECO:0000269|PubMed:9576862}; KM=66 uM for nitrocefin {ECO:0000269|PubMed:9576862}; KM=180 uM for cefotaxime {ECO:0000269|PubMed:9576862}; KM=370 uM for imipenem {ECO:0000269|PubMed:9576862}; Note=kcat is 350 sec(-1) for lactamase activity with imipenem as substrate. kcat is 300 sec(-1) for lactamase activity with 6-beta-iodopenicillanate as substrate. kcat is 280 sec(-1) for lactamase activity with penicillin G as substrate. kcat is 39 sec(-1) for lactamase activity with cefotaxime as substrate. kcat is 17 sec(-1) for lactamase activity with nitrocefin as substrate. kcat is 14 sec(-1) for lactamase activity with cephaloridine as substrate. kcat is 6 sec(-1) for lactamase activity with cefoxitin as substrate. {ECO:0000269|PubMed:9576862};
null
null
null
FUNCTION: Confers resistance to the different beta-lactams antibiotics (penicillin, cephalosporin and carbapenem) via the hydrolysis of the beta-lactam ring. {ECO:0000269|PubMed:9576862}.
Elizabethkingia meningoseptica (Chryseobacterium meningosepticum)
O08522
GOSR1_CRIGR
MAAGTSNYWEDLRKQARQLENELDLKLVSFSKLCTSYSHSSARDGGRDRYSSDTTPLLNGSSQDRMFETMAIEIEQLLARLTGVNDKMAEYTNSAGVPSLNAALMHTLQRHRDILQDYTHEFHKTKANFMAIRERENLMGSVRKDIESYKSGSGVNNRRTELFLKEHDHLRNSDRLIEETISIAMATKENMTSQRGMLKSIHSKMNTLANRFPAVNSLIQRINLRKRRDSLILGGVIGICTILLLLYAFH
null
null
endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; intra-Golgi vesicle-mediated transport [GO:0006891]; protein transport [GO:0015031]; vesicle fusion [GO:0006906]
cis-Golgi network [GO:0005801]; Golgi medial cisterna [GO:0005797]; Golgi membrane [GO:0000139]; Golgi trans cisterna [GO:0000138]; SNARE complex [GO:0031201]
SNAP receptor activity [GO:0005484]
PF12352;
null
GOSR1 family
null
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:8636227}; Single-pass type IV membrane protein {ECO:0000269|PubMed:8636227}. Note=Localizes throughout the Golgi apparatus, with lowest levels in the trans-Golgi network. Enriched on vesicular components at the terminal rims of the Golgi (By similarity). {ECO:0000250}.
null
null
null
null
null
FUNCTION: Involved in transport from the ER to the Golgi apparatus as well as in intra-Golgi transport. It belongs to a super-family of proteins called t-SNAREs or soluble NSF (N-ethylmaleimide-sensitive factor) attachment protein receptor. May play a protective role against hydrogen peroxide induced cytotoxicity under glutathione depleted conditions in neuronal cells by regulating the intracellular ROS levels via inhibition of p38 MAPK (MAPK11, MAPK12, MAPK13 and MAPK14). Participates in docking and fusion stage of ER to cis-Golgi transport. Plays an important physiological role in VLDL-transport vesicle-Golgi fusion and thus in VLDL delivery to the hepatic cis-Golgi. {ECO:0000269|PubMed:8636227}.
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
O08523
TECTA_MOUSE
MNYSSLLRIWVSFIFALVRHQAQPRELMYPFWQNDTRTPKVDDGSSSEIKLAIPVFFFGVPYRTVYVNNNGVVSFNVLVSQFTPESFPLTDGRAFIAPFWADVHNGIRGEIYYRETMDPAILRRATKDIRKYFKDMTTFSATWVFIVTWEEVTFYGGSSTTPVNTFQAVLVSDGSYTFTLFNYYEINWTTGTASGGDPLTGLGGVMAQAGFNGGNLTNFFSLPGSRTPEIVNIQETTNVNVPGRWAFKVDGKEIDPANGCTSRGQFLRRGEVFWDDLNCTIKCRCLDFNNEIYCQEASCSPYEVCEPKGRFFYCSPVETSTCVVFGEPHYHTFDGFLFHFQGSCAYLLARQCLQTSSLPFFSVEAKNEHRGGSAVSWVKELSVEVNGYKILIPKGSYGKVKVNDLVTSLPVTLELGAVKIYQSGMSTAVETDFGLLVTFDGQHYASISIPGSYINSTCGLCGNYNKNPLDDFLRPDGRPAMSVLDLGESWRVYHADWKCGSGCVDNCTQCDAATEALYFGSDYCGFLNKTDGPLWECGTVVDATAFVHSCVYDLCSVRDNGTLLCQAIQAYALVCQALGIPIGDWRIQTGCVSTVRCPSFSHYSVCTSSCPDTCSDLTASQNCATPCTEGCECNEGFVLSTSQCVPLHKCGCDFDGHYYTMGEFFWATANCTVQCLCEEGGDVYCFNKTCRSGEVCAVEDGYQGCFPKRETVCLLSQNQVLHTFDGAAYAFPSELSYTLLKTCPERPEYLEIDINKKKPDAGPAWLRGVRILVADQEVKIGGVGALEVKLNGQDVELPFFHPSGRLEIHRNKNSTTVESKGVVSVQYSDVGLLYIRLSTMYFNCTGGLCGFFNANASDEFCLPNGKCTDNLAVFLESWTTFEEICNGECGDLLKACNNDSELLKFYRSRSRCGIINDPSNSSFLECHGVVNVTAYYRTCLFRLCQSGGNESELCDSVARYASACKNADVEVGPWRTYDFCPLECPENSHFEECMTCTETCETLALGPICVDSCSEGCQCDEGYALQGSQCVPRSECGCNFEGHQLATNETFWVDQDCQIFCYCNGTDNSVHCETIPCRDDEYCMEESGLYYCQPRTDASCIVSGYGHYLTFDGYPFDFQTSCPLILCTTGSRPISDSFPKFIVTAKNEDRDPSLALWVKQVDVNVFGYSIVIHRAYKHTVLVNNERLYLPLKLGQGKINIFSFGFHVVVETDFGLKVVYDWKTFLSITVPRSMQNGTYGLCGRYNGNPDDDLEMPMGLPALSINEFGQSWVKRDTFCQVGCGDRCPSCAKVEGFSKVQQLCSLIPNQNAGFAKCHSKVNPTFFYKNCLFDSCIDGGAVQTACSWLQNYASTCQTQGIAVTGWRNYTSCSVTCPPNSHYESCVSVCQPRCAAIRLKSDCNHYCVEGCQCDAGYVLNGKSCILPHNCGCYSDGKYYEPKQLFWNGDCTRRCRCFRRNLIQCDPRQCKSDEECALRSGVRGCFSTKTSYCLAAGGGVFRTFDGAFLRFPANCAFVLSTICQKLPDISFQLIINFDKWSSPNLTIISPVYFYINEEQILINDRNTVKVNGTQVNVPFITGLATKIYSSEGFLVIDTSPDIQIYYNGFNVIKISISERLQNKVCGLCGNFNGDMTDDYVTLRGKPVVSSVVLAQSWKTNGMQKRPLAPSCNELQFSQYAATCDNVHIQAMQGDGYCLKLTDMKGFFQPCYGLLDPLPFYESCYLDGCYNHKKFQLCGSLAAYGEACRSFGILSTEWIEKENCSGVVEDPCVGADCPNRTCELDNGGELCGCIEPPPYGNNSHDIIDAEVTCKAAQMEVSISKCKLFQLGFEREGVRINDRQCSGIEGEDFISFQINNTKGNCGNIVQSNGTHIMYKNTIWIESANNTGNIITRDRTINVEFSCAYELDIKISLDSVVKPMLSVINLTVPTQEGSFTTKMALYKNASYKHPYRQGEVVLTTRDVLYVGVFVVGADSTHLILTLNKCYATPSRDSNDKLRYFIIEGGCQNIKDNTIGIEENGVSLTCRFHVTVFKFIGDYDEVHLHCAVSLCDSEKYSCKINCPQNSRIATDYSKEHKEQIISVGPIRRKRLDWCEDNGGCEQICTSRVDGPLCSCVTGSLQEDGRSCRASNSSVELQVWTLLLIMTQISLWHLIYKSGATS
null
null
auditory receptor cell stereocilium organization [GO:0060088]; cell-matrix adhesion [GO:0007160]; sensory perception of sound [GO:0007605]
extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]
extracellular matrix structural constituent [GO:0005201]
PF08742;PF06119;PF01826;PF12714;PF00094;PF00100;
2.10.25.10;2.60.40.4100;2.60.40.3210;
null
PTM: 3 products of tectorin seem to exist: HMM, MMM and LMM. They may be generated by active processing or the result of proteolysis occurring between intrachain disulfide bonds.; PTM: The presence of a hydrophobic C-terminus preceded by a potential cleavage site strongly suggests that tectorins are synthesized as glycosylphosphatidylinositol-linked, membrane-bound precursors. Tectorins are targeted to the apical surface of the inner ear epithelia by the lipid and proteolytically released into the extracellular compartment.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:9079715}; Lipid-anchor, GPI-anchor {ECO:0000305|PubMed:9079715}; Extracellular side {ECO:0000305|PubMed:9079715}. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:9079715}. Note=Found in the non-collagenous matrix of the tectorial membrane.
null
null
null
null
null
FUNCTION: One of the major non-collagenous components of the tectorial membrane (By similarity). The tectorial membrane is an extracellular matrix of the inner ear that covers the neuroepithelium of the cochlea and contacts the stereocilia bundles of specialized sensory hair cells. Sound induces movement of these hair cells relative to the tectorial membrane, deflects the stereocilia and leads to fluctuations in hair-cell membrane potential, transducing sound into electrical signals. {ECO:0000250}.
Mus musculus (Mouse)
O08524
TECTB_MOUSE
MVVRAFVLLALFAEASAKSCTPNKADVILVFCYPKTIITKIPECPYGWEVHQLALGGLCYNGVHEGGYYQFVIPDLSPKNKSYCGTQSEYKPPIYHFYSHIVSNDSTVIVKNQPVNYSFSCTYHSTYLVNQAAFDQRVATVHVKNGSMGTFESQLSLNFYTNAKFSTKKEAPFVLETSEIGSDLFAGVEAKGLSVRFKVVLNSCWATPSADFMYPLQWQLINKGCPTDETVLVHENGKDHRATFQFNAFRFQNIPKLSKVWLHCETFICDSEKLSCPVNCDKRKRMLRDQTGGVLVVELSLRSRAFSGLCDFSDVLLHLILMLGTWAVL
null
null
sensory perception of sound [GO:0007605]
cell surface [GO:0009986]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]
extracellular matrix structural constituent [GO:0005201]
PF00100;
2.60.40.4100;
null
PTM: The presence of a hydrophobic C-terminus preceded by a potential cleavage site strongly suggests that tectorins are synthesized as glycosylphosphatidylinositol-linked, membrane-bound precursors. Tectorins are targeted to the apical surface of the inner ear epithelia by the lipid and proteolytically released into the extracellular compartment.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}; Extracellular side {ECO:0000305}. Secreted, extracellular space, extracellular matrix. Note=Found in the non-collagenous matrix of the tectorial membrane. {ECO:0000250}.
null
null
null
null
null
FUNCTION: One of the major non-collagenous components of the tectorial membrane (By similarity). The tectorial membrane is an extracellular matrix of the inner ear that covers the neuroepithelium of the cochlea and contacts the stereocilia bundles of specialized sensory hair cells. Sound induces movement of these hair cells relative to the tectorial membrane, deflects the stereocilia and leads to fluctuations in hair-cell membrane potential, transducing sound into electrical signals. {ECO:0000250}.
Mus musculus (Mouse)
O08528
HXK2_MOUSE
MIASHMIACLFTELNQNQVQKVDQYLYHMRLSDETLLEISRRFRKEMEKGLGATTHPTAAVKMLPTFVRSTPDGTEHGEFLALDLGGTNFRVLRVRVTDNGLQRVEMENQIYAIPEDIMRGSGTQLFDHIAECLANFMDKLQIKEKKLPLGFTFSFPCHQTKLDESFLVSWTKGFKSSGVEGRDVVDLIRKAIQRRGDFDIDIVAVVNDTVGTMMTCGYDDQNCEIGLIVGTGSNACYMEEMRHIDMVEGDEGRMCINMEWGAFGDDGTLNDIRTEFDREIDMGSLNPGKQLFEKMISGMYMGELVRLILVKMAKAELLFQGKLSPELLTTGSFETKDVSDIEDDKDGIQKAYQILVRLGLSPLQEDCVATHRICQIVSTRSASLCAATLAAVLWRIKENKGEERLRSTIGVDGSVYKKHPHFAKRLHKAVRRLVPDCDVRFLRSEDGSGKGAAMVTAVAYRLADQHRARQKTLESLKLSHEQLLEVKRRMKVEMEQGLSKETHEAAPVKMLPTYVCATPDGTEKGDFLALDLGGTNFRVLLVRVRNGKRRGVEMHNKIYSIPQEVMHGTGEELFDHIVQCIADFLEYMGMKGVSLPLGFTFSFPCQQNSLDQSILLKWTKGFKASGCEGEDVVTLLKEAIRRREEFDLDVVAVVNDTVGTMMTCGYEDPHCEVGLIVGTGSNACYMEEMRNVELVDGEEGRMCVNMEWGAFGDNGCLDDLRTVFDVAVDELSLNPGKQRFEKMISGMYLGEIVRNILIDFTKRGLLFRGRISERLKTRGIFETKFLSQIESDCLALLQVRAILRHLGLESTCDDSIIVKEVCTVVARRAAQLCGAGMAAVVDKIRENRGLDNLKVTVGVDGTLYKLHPHFAKVMHETVRDLAPKCDVSFLESEDGSGKGAALITAVACRIREAGQR
2.7.1.1
null
apoptotic mitochondrial changes [GO:0008637]; carbohydrate phosphorylation [GO:0046835]; cellular response to leukemia inhibitory factor [GO:1990830]; establishment of protein localization to mitochondrion [GO:0072655]; fructose 6-phosphate metabolic process [GO:0006002]; glucose 6-phosphate metabolic process [GO:0051156]; glucose metabolic process [GO:0006006]; glycolytic process [GO:0006096]; intracellular glucose homeostasis [GO:0001678]; lactation [GO:0007595]; maintenance of protein location in mitochondrion [GO:0072656]; negative regulation of mitochondrial membrane permeability [GO:0035795]; negative regulation of reactive oxygen species metabolic process [GO:2000378]; positive regulation of angiogenesis [GO:0045766]; positive regulation of autophagy of mitochondrion in response to mitochondrial depolarization [GO:1904925]; regulation of glucose import [GO:0046324]; response to hypoxia [GO:0001666]; response to ischemia [GO:0002931]
centrosome [GO:0005813]; cytosol [GO:0005829]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; sarcoplasmic reticulum [GO:0016529]
ATP binding [GO:0005524]; fructokinase activity [GO:0008865]; glucokinase activity [GO:0004340]; glucose binding [GO:0005536]; hexokinase activity [GO:0004396]
PF00349;PF03727;
3.30.420.40;3.40.367.20;
Hexokinase family
null
SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250|UniProtKB:P52789}; Peripheral membrane protein {ECO:0000250|UniProtKB:P52789}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P52789}. Note=The mitochondrial-binding peptide (MBP) region promotes association with the mitochondrial outer membrane. The interaction with the mitochondrial outer membrane via the mitochondrial-binding peptide (MBP) region promotes higher stability of the protein. Release from the mitochondrial outer membrane into the cytosol induces permeability transition pore (PTP) opening and apoptosis. {ECO:0000250|UniProtKB:P52789}.
CATALYTIC ACTIVITY: Reaction=a D-hexose + ATP = a D-hexose 6-phosphate + ADP + H(+); Xref=Rhea:RHEA:22740, ChEBI:CHEBI:4194, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:229467, ChEBI:CHEBI:456216; EC=2.7.1.1; Evidence={ECO:0000250|UniProtKB:P52789}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22741; Evidence={ECO:0000250|UniProtKB:P52789}; CATALYTIC ACTIVITY: Reaction=ATP + D-fructose = ADP + D-fructose 6-phosphate + H(+); Xref=Rhea:RHEA:16125, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:37721, ChEBI:CHEBI:61527, ChEBI:CHEBI:456216; EC=2.7.1.1; Evidence={ECO:0000250|UniProtKB:P27881}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16126; Evidence={ECO:0000250|UniProtKB:P27881}; CATALYTIC ACTIVITY: Reaction=ATP + D-glucose = ADP + D-glucose 6-phosphate + H(+); Xref=Rhea:RHEA:17825, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:61548, ChEBI:CHEBI:456216; EC=2.7.1.1; Evidence={ECO:0000250|UniProtKB:P52789}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17826; Evidence={ECO:0000250|UniProtKB:P52789};
null
PATHWAY: Carbohydrate metabolism; hexose metabolism. {ECO:0000250|UniProtKB:P52789}.; PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 1/4. {ECO:0000250|UniProtKB:P52789}.
null
null
FUNCTION: Catalyzes the phosphorylation of hexose, such as D-glucose and D-fructose, to hexose 6-phosphate (D-glucose 6-phosphate and D-fructose 6-phosphate, respectively) (By similarity). Mediates the initial step of glycolysis by catalyzing phosphorylation of D-glucose to D-glucose 6-phosphate (By similarity). Plays a key role in maintaining the integrity of the outer mitochondrial membrane by preventing the release of apoptogenic molecules from the intermembrane space and subsequent apoptosis (PubMed:18350175). {ECO:0000250|UniProtKB:P27881, ECO:0000269|PubMed:18350175}.
Mus musculus (Mouse)
O08529
CAN2_MOUSE
MAGIAIKLAKDREAAEGLGSHERAIKYLNQDYETLRNECLEAGALFQDPSFPALPSSLGYKELGPYSSKTRGIEWKRPTEICADPQFIIGGATRTDICQGALGDCWLLAAIASLTLNEEILARVVPPDQSFQENYAGIFHFQFWQYGEWVEVVVDDRLPTKDGELLFVHSAEGSEFWSALLEKAYAKINGCYEALSGGATTEGFEDFTGGIAEWYELRKPPPNLFKIIQKALEKGSLLGCSIDITSAADSEAVTYQKLVKGHAYSVTGAEEVESSGSLQKLIRIRNPWGQVEWTGKWNDNCPSWNTVDPEVRANLTERQEDGEFWMSFSDFLRHYSRLEICNLTPDTLTCDSYKKWKLTKMDGNWRRGSTAGGCRNYPNTFWMNPQYLIKLEEEDEDEEDGERGCTFLVGLIQKHRRRQRKMGEDMHTIGFGIYEVPEELTGQTNIHLGKNFFLTTRARERSDTFINLREVLNRFKLPPGEYVLVPSTFEPHKDGDFCIRVFSEKKADYQAVDDEIEANIEEIDANEEDIDDGFRRLFVQLAGEDAEISAFELQTILRRVLAKRQDIKSDGFSIETCKIMVDMLDEDGSGKLGLKEFYILWTKIQKYQKIYREIDVDRSGTMNSYEMRKALEEAGFKLPCQLHQVIVARFADDELIIDFDNFVRCLVRLETLFKIFKQLDPENTGTIQLNLASWLSFSVL
3.4.22.53
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 7 Ca(2+) ions. {ECO:0000250};
behavioral response to pain [GO:0048266]; blastocyst development [GO:0001824]; cellular response to amino acid stimulus [GO:0071230]; cellular response to interferon-beta [GO:0035458]; cellular response to lipopolysaccharide [GO:0071222]; female pregnancy [GO:0007565]; myoblast fusion [GO:0007520]; positive regulation of cardiac muscle cell apoptotic process [GO:0010666]; positive regulation of myoblast fusion [GO:1901741]; positive regulation of phosphatidylcholine biosynthetic process [GO:2001247]; protein autoprocessing [GO:0016540]; protein catabolic process [GO:0030163]; proteolysis [GO:0006508]; proteolysis involved in protein catabolic process [GO:0051603]; regulation of interleukin-6 production [GO:0032675]; response to hydrogen peroxide [GO:0042542]; response to hypoxia [GO:0001666]; response to mechanical stimulus [GO:0009612]
calpain complex [GO:0110158]; cell projection [GO:0042995]; chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; external side of plasma membrane [GO:0009897]; focal adhesion [GO:0005925]; Golgi apparatus [GO:0005794]; lysosome [GO:0005764]; membrane raft [GO:0045121]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; perinuclear endoplasmic reticulum [GO:0097038]; plasma membrane [GO:0005886]; pseudopodium [GO:0031143]
calcium ion binding [GO:0005509]; calcium-dependent cysteine-type endopeptidase activity [GO:0004198]; cytoskeletal protein binding [GO:0008092]; enzyme binding [GO:0019899]; peptidase activity [GO:0008233]; protein-containing complex binding [GO:0044877]
PF01067;PF13833;PF00648;
2.60.120.380;3.90.70.10;1.10.238.10;
Peptidase C2 family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Translocates to the plasma membrane upon Ca(2+) binding. {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=Broad endopeptidase specificity.; EC=3.4.22.53;
null
null
null
null
FUNCTION: Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. Proteolytically cleaves MYOC at 'Arg-226' (By similarity). Proteolytically cleaves CPEB3 following neuronal stimulation which abolishes CPEB3 translational repressor activity, leading to translation of CPEB3 target mRNAs (PubMed:22711986). {ECO:0000250|UniProtKB:P17655, ECO:0000269|PubMed:22711986}.
Mus musculus (Mouse)
O08530
S1PR1_MOUSE
MVSTSIPEVKALRSSVSDYGNYDIIVRHYNYTGKLNIGAEKDHGIKLTSVVFILICCFIILENIFVLLTIWKTKKFHRPMYYFIGNLALSDLLAGVAYTANLLLSGATTYKLTPAQWFLREGSMFVALSASVFSLLAIAIERYITMLKMKLHNGSNSSRSFLLISACWVISLILGGLPIMGWNCISSLSSCSTVLPLYHKHYILFCTTVFTLLLLSIVILYCRIYSLVRTRSRRLTFRKNISKASRSSEKSLALLKTVIIVLSVFIACWAPLFILLLLDVGCKAKTCDILYKAEYFLVLAVLNSGTNPIIYTLTNKEMRRAFIRIVSCCKCPNGDSAGKFKRPIIPGMEFSRSKSDNSSHPQKDDGDNPETIMSSGNVNSSS
null
null
actin cytoskeleton organization [GO:0030036]; adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway [GO:0007193]; angiogenesis [GO:0001525]; blood vessel maturation [GO:0001955]; brain development [GO:0007420]; cardiac muscle tissue growth involved in heart morphogenesis [GO:0003245]; cell migration [GO:0016477]; cell population proliferation [GO:0008283]; chemotaxis [GO:0006935]; endothelial cell differentiation [GO:0045446]; G protein-coupled receptor signaling pathway [GO:0007186]; heart trabecula morphogenesis [GO:0061384]; lamellipodium assembly [GO:0030032]; leukocyte chemotaxis [GO:0030595]; negative regulation of stress fiber assembly [GO:0051497]; neuron differentiation [GO:0030182]; phospholipase C-activating G protein-coupled receptor signaling pathway [GO:0007200]; positive regulation of cell migration [GO:0030335]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of positive chemotaxis [GO:0050927]; positive regulation of smooth muscle cell proliferation [GO:0048661]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of bone mineralization [GO:0030500]; regulation of bone resorption [GO:0045124]; regulation of cell adhesion [GO:0030155]; regulation of metabolic process [GO:0019222]; sphingosine-1-phosphate receptor signaling pathway [GO:0003376]; T cell migration [GO:0072678]; transmission of nerve impulse [GO:0019226]
caveola [GO:0005901]; cytoplasm [GO:0005737]; endosome [GO:0005768]; external side of plasma membrane [GO:0009897]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]
G protein-coupled receptor activity [GO:0004930]; G protein-coupled receptor binding [GO:0001664]; sphingolipid binding [GO:0046625]; sphingosine-1-phosphate receptor activity [GO:0038036]
PF00001;
1.20.1070.10;
G-protein coupled receptor 1 family
PTM: Palmitoylated by ZDHHC5. Palmitoylation is required for targeting to plasma membrane, enabling G(i) coupling. {ECO:0000250|UniProtKB:P21453}.
SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Endosome {ECO:0000250}. Membrane, caveola {ECO:0000250}. Note=Recruited to caveolin-enriched plasma membrane microdomains in response to oxidized 1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphocholine. Ligand binding leads to receptor internalization (By similarity). {ECO:0000250}.
null
null
null
null
null
FUNCTION: G-protein coupled receptor for the bioactive lysosphingolipid sphingosine 1-phosphate (S1P) that seems to be coupled to the G(i) subclass of heteromeric G proteins. Signaling leads to the activation of RAC1, SRC, PTK2/FAK1 and MAP kinases. Plays an important role in cell migration, probably via its role in the reorganization of the actin cytoskeleton and the formation of lamellipodia in response to stimuli that increase the activity of the sphingosine kinase SPHK1. Required for normal chemotaxis toward sphingosine 1-phosphate. Required for normal embryonic heart development and normal cardiac morphogenesis. Plays an important role in the regulation of sprouting angiogenesis and vascular maturation. Inhibits sprouting angiogenesis to prevent excessive sprouting during blood vessel development. Required for normal egress of mature T-cells from the thymus into the blood stream and into peripheral lymphoid organs. Plays a role in the migration of osteoclast precursor cells, the regulation of bone mineralization and bone homeostasis. Plays a role in responses to oxidized 1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphocholine by pulmonary endothelial cells and in the protection against ventilator-induced lung injury. {ECO:0000269|PubMed:11032855, ECO:0000269|PubMed:11230698, ECO:0000269|PubMed:11726541, ECO:0000269|PubMed:12869509, ECO:0000269|PubMed:14732704, ECO:0000269|PubMed:14737169, ECO:0000269|PubMed:19204730, ECO:0000269|PubMed:19286607, ECO:0000269|PubMed:21668976, ECO:0000269|PubMed:22951644}.
Mus musculus (Mouse)
O08532
CA2D1_MOUSE
MAAGCLLALTLTLFQSGLIGPSSEEPFPSPVTIKSWVDKMQEDLVTLAKTASGVTQLADIYEKYQDLYTVEPNNARQLVEIAARDIEKLLSNRSKALVRLAMEAEKVQAAHQWREDFASNEVVYYNAKDDLDPERNESEPGSQRIKPVFIEDANFGRQISYQHAAVHIPTDIYEGSTIVLNELNWTSALDEVFKRNRDEDPTLLWQVFGSATGLARYYPASPWVDNSRTPNKIDLYDVRRRPWYIQGAASPKDMLILVDVSGSVSGLTLKLIRTSVSEMLETLSDDDFVNVASFNSNAQDVSCFQHLVQANVRNKKVLKDAVNNITAKGITDYKKGFSFAFEQLLNYNVSRANCNKIIMLFTDGGEERAQEIFAKYNKDKKVRVFTFSVGQHNYDRGPIQWMACENKGYYYEIPSIGAIRINTQEYLDVLGRPMVLAGDKAKQVQWTNVYLDALELGLVITGTLPVFNVTGQSENKTNLKNQLILGVMGVDVSLEDIKRLTPRFTLCPNGYYFAIDPNGYVLLHPNLQPKPIGVGIPTINLRKRRPNVQNPKSQEPVTLDFLDAELENEIKVEIRNKMIDGESGEKTFRTLVKSQDERYIDKGNRTYTWTPVNGTDYSLALVLPTYSFYYIKAKLEETITQARYSETLKPDNFEESGYTFIAPREYCNDLKPSDNNTEFLLNFNEFIDRKTPNNPSCNTDLINRILLDAGFTNELVQNYWSKQKNIKGVKARFVVTDGGITRVYPKEAGENWQENPETYEDSFYKRSLDNDNYVFTAPYFNKSGPGAYESGIMVSKAVELYIQGKLLKPAVVGIKIDVNSWIENFTKTSIRDPCAGPVCDCKRNSDVMDCVILDDGGFLLMANHDDYTNQIGRFFGEIDPSMMRHLVNISLYAFNKSYDYQSVCDPGAAPKQGAGHRSAYVPSIADILQIGWWATAAAWSILQQLLLSLTFPRLLEAVEMEEDDFTASLSKQSCITEQTQYFFKNDTKSFSGLLDCGNCSRIFHVEKLMNTNLVFIMVESKGTCPCDTRLLMQAEQTSDGPDPCDMVKQPRYRKGPDVCFDNNVLEDYTDCGGVSGLNPSLWSIFGLQFILLWLVSGSRHYLL
null
null
calcium ion transmembrane transport [GO:0070588]; calcium ion transmembrane transport via high voltage-gated calcium channel [GO:0061577]; calcium ion transport into cytosol [GO:0060402]; cardiac muscle cell action potential involved in contraction [GO:0086002]; cellular response to amyloid-beta [GO:1904646]; positive regulation of high voltage-gated calcium channel activity [GO:1901843]; regulation of calcium ion transmembrane transport via high voltage-gated calcium channel [GO:1902514]; regulation of calcium ion transport [GO:0051924]; regulation of heart rate by cardiac conduction [GO:0086091]; regulation of membrane repolarization during action potential [GO:0098903]; regulation of ventricular cardiac muscle cell membrane repolarization [GO:0060307]
glutamatergic synapse [GO:0098978]; L-type voltage-gated calcium channel complex [GO:1990454]; neuronal dense core vesicle [GO:0098992]; postsynaptic membrane [GO:0045211]; presynaptic active zone membrane [GO:0048787]; sarcoplasmic reticulum [GO:0016529]; T-tubule [GO:0030315]; voltage-gated calcium channel complex [GO:0005891]
metal ion binding [GO:0046872]; voltage-gated calcium channel activity [GO:0005245]; voltage-gated calcium channel activity involved in bundle of His cell action potential [GO:0086057]
PF08473;PF00092;PF08399;
3.30.450.20;3.40.50.410;
Calcium channel subunit alpha-2/delta family
PTM: Proteolytically processed into subunits alpha-2-1 and delta-1 that are disulfide-linked. {ECO:0000250}.
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Cell membrane {ECO:0000250|UniProtKB:P54289}.
null
null
null
null
null
FUNCTION: The alpha-2/delta subunit of voltage-dependent calcium channels regulates calcium current density and activation/inactivation kinetics of the calcium channel (By similarity). Plays an important role in excitation-contraction coupling (By similarity). {ECO:0000250|UniProtKB:P54289}.
Mus musculus (Mouse)
O08537
ESR2_MOUSE
MEIKNSPSSLTSPASYNCSQSILPLEHGPIYIPSSYVESRHEYSAMTFYSPAVMNYSVPSSTGNLEGGPVRQTASPNVLWPTSGHLSPLATHCQSSLLYAEPQKSPWCEARSLEHTLPVNRETLKRKLGGSGCASPVTSPSAKRDAHFCAVCSDYASGYHYGVWSCEGCKAFFKRSIQGHNDYICPATNQCTIDKNRRKSCQACRLRKCYEVGMVKCGSRRERCGYRIVRRQRSASEQVHCLNKAKRTSGHTPRVKELLLNSLSPEQLVLTLLEAEPPNVLVSRPSMPFTEASMMMSLTKLADKELVHMIGWAKKIPGFVELSLLDQVRLLESCWMEVLMVGLMWRSIDHPGKLIFAPDLVLDRDEGKCVEGILEIFDMLLATTARFRELKLQHKEYLCVKAMILLNSSMYPLATASQEAESSRKLTHLLNAVTDALVWVISKSGISSQQQSVRLANLLMLLSHVRHISNKGMEHLLSMKCKNVVPVYDLLLEMLNAHTLRGYKSSISGSECCSTEDSKSKEGSQNLQSQ
null
null
androgen receptor signaling pathway [GO:0030521]; behavioral fear response [GO:0001662]; brain development [GO:0007420]; cell population proliferation [GO:0008283]; cellular response to estradiol stimulus [GO:0071392]; cellular response to estrogen stimulus [GO:0071391]; cellular response to lipopolysaccharide [GO:0071222]; epithelial cell maturation involved in prostate gland development [GO:0060743]; epithelial cell proliferation [GO:0050673]; estrous cycle [GO:0044849]; hormone-mediated apoptotic signaling pathway [GO:0008628]; intracellular estrogen receptor signaling pathway [GO:0030520]; intracellular steroid hormone receptor signaling pathway [GO:0030518]; learning or memory [GO:0007611]; negative regulation of androgen receptor signaling pathway [GO:0060766]; negative regulation of behavior [GO:0048521]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of epithelial cell proliferation [GO:0050680]; negative regulation of feeding behavior [GO:2000252]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of reactive oxygen species metabolic process [GO:2000378]; negative regulation of smooth muscle cell proliferation [GO:0048662]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neuron migration [GO:0001764]; ovarian follicle development [GO:0001541]; positive regulation of apoptotic process [GO:0043065]; positive regulation of DNA-binding transcription factor activity [GO:0051091]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of epidermal growth factor receptor signaling pathway [GO:0045742]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of transcription by RNA polymerase II [GO:0045944]; prostate gland epithelium morphogenesis [GO:0060740]; regulation of cell population proliferation [GO:0042127]; regulation of transcription by RNA polymerase II [GO:0006357]; response to testosterone [GO:0033574]; Sertoli cell proliferation [GO:0060011]; uterus development [GO:0060065]; vagina development [GO:0060068]; vasodilation [GO:0042311]
cytoplasm [GO:0005737]; mitochondrion [GO:0005739]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; perikaryon [GO:0043204]; perinuclear region of cytoplasm [GO:0048471]; protein-DNA complex [GO:0032993]
DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; enzyme binding [GO:0019899]; estradiol binding [GO:1903924]; estrogen binding [GO:0099130]; estrogen response element binding [GO:0034056]; heterocyclic compound binding [GO:1901363]; hormone binding [GO:0042562]; nuclear estrogen receptor activity [GO:0030284]; nuclear receptor activity [GO:0004879]; nuclear steroid receptor activity [GO:0003707]; organic cyclic compound binding [GO:0097159]; peroxisome proliferator activated receptor binding [GO:0042975]; promoter-specific chromatin binding [GO:1990841]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]; steroid binding [GO:0005496]; steroid hormone binding [GO:1990239]; zinc ion binding [GO:0008270]
PF12497;PF00104;PF00105;
3.30.50.10;1.10.565.10;
Nuclear hormone receptor family, NR3 subfamily
PTM: Phosphorylation at Ser-87 and Ser-105 recruits NCOA1. {ECO:0000269|PubMed:10230404, ECO:0000269|PubMed:10995228}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92731}.
null
null
null
null
null
FUNCTION: Nuclear hormone receptor. Binds estrogens with an affinity similar to that of ESR1/ER-alpha, and activates expression of reporter genes containing estrogen response elements (ERE) in an estrogen-dependent manner. {ECO:0000250|UniProtKB:Q92731}.
Mus musculus (Mouse)
O08538
ANGP1_MOUSE
MTVFLSFAFFAAILTHIGCSNQRRNPENGGRRYNRIQHGQCAYTFILPEHDGNCRESATEQYNTNALQRDAPHVEPDFSSQKLQHLEHVMENYTQWLQKLENYIVENMKSEMAQIQQNAVQNHTATMLEIGTSLLSQTAEQTRKLTDVETQVLNQTSRLEIQLLENSLSTYKLEKQLLQQTNEILKIHEKNSLLEHKILEMEGKHKEELDTLKEEKENLQGLVSRQTFIIQELEKQLSRATNNNSILQKQQLELMDTVHNLISLCTKEGVLLKGGKREEEKPFRDCADVYQAGFNKSGIYTIYFNNMPEPKKVFCNMDVNGGGWTVIQHREDGSLDFQRGWKEYKMGFGNPSGEYWLGNEFIFAITSQRQYMLRIELMDWEGNRAYSQYDRFHIGNEKQNYRLYLKGHTGTAGKQSSLILHGADFSTKDADNDNCMCKCALMLTGGWWFDACGPSNLNGMFYTAGQNHGKLNGIKWHYFKGPSYSLRSTTMMIRPLDF
null
null
angiogenesis [GO:0001525]; branching involved in blood vessel morphogenesis [GO:0001569]; cardiac muscle tissue morphogenesis [GO:0055008]; cell-substrate adhesion [GO:0031589]; endocardium morphogenesis [GO:0003160]; endoderm development [GO:0007492]; glomerulus vasculature development [GO:0072012]; hemopoiesis [GO:0030097]; heparin biosynthetic process [GO:0030210]; in utero embryonic development [GO:0001701]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell adhesion [GO:0007162]; negative regulation of cytokine production involved in immune response [GO:0002719]; negative regulation of endothelial cell apoptotic process [GO:2000352]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of protein import into nucleus [GO:0042308]; negative regulation of protein phosphorylation [GO:0001933]; negative regulation of vascular permeability [GO:0043116]; neuron apoptotic process [GO:0051402]; ovarian follicle development [GO:0001541]; positive chemotaxis [GO:0050918]; positive regulation of blood vessel endothelial cell migration [GO:0043536]; positive regulation of blood-brain barrier permeability [GO:1905605]; positive regulation of cell adhesion [GO:0045785]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of gene expression [GO:0010628]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of protein ubiquitination [GO:0031398]; positive regulation of receptor internalization [GO:0002092]; positive regulation of vascular endothelial growth factor receptor signaling pathway [GO:0030949]; protein localization to cell surface [GO:0034394]; regulation of canonical NF-kappaB signal transduction [GO:0043122]; regulation of macrophage migration inhibitory factor signaling pathway [GO:2000446]; regulation of skeletal muscle satellite cell proliferation [GO:0014842]; regulation of tumor necrosis factor production [GO:0032680]; sprouting angiogenesis [GO:0002040]; Tie signaling pathway [GO:0048014]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]; vasculogenesis [GO:0001570]; vasculogenesis involved in coronary vascular morphogenesis [GO:0060979]
collagen-containing extracellular matrix [GO:0062023]; extracellular space [GO:0005615]; membrane raft [GO:0045121]; microvillus [GO:0005902]; plasma membrane [GO:0005886]
identical protein binding [GO:0042802]; receptor tyrosine kinase binding [GO:0030971]; signaling receptor binding [GO:0005102]; vascular endothelial growth factor receptor binding [GO:0005172]
PF00147;
3.90.215.10;4.10.530.10;
null
null
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8980223}.
null
null
null
null
null
FUNCTION: Binds and activates TEK/TIE2 receptor by inducing its dimerization and tyrosine phosphorylation. Plays an important role in the regulation of angiogenesis, endothelial cell survival, proliferation, migration, adhesion and cell spreading, reorganization of the actin cytoskeleton, but also maintenance of vascular quiescence. Required for normal angiogenesis and heart development during embryogenesis. After birth, activates or inhibits angiogenesis, depending on the context. Inhibits angiogenesis and promotes vascular stability in quiescent vessels, where endothelial cells have tight contacts. In quiescent vessels, ANGPT1 oligomers recruit TEK to cell-cell contacts, forming complexes with TEK molecules from adjoining cells, and this leads to preferential activation of phosphatidylinositol 3-kinase and the AKT1 signaling cascades. In migrating endothelial cells that lack cell-cell adhesions, ANGT1 recruits TEK to contacts with the extracellular matrix, leading to the formation of focal adhesion complexes, activation of PTK2/FAK and of the downstream kinases MAPK1/ERK2 and MAPK3/ERK1, and ultimately to the stimulation of sprouting angiogenesis. Mediates blood vessel maturation/stability. Implicated in endothelial developmental processes later and distinct from that of VEGF. Appears to play a crucial role in mediating reciprocal interactions between the endothelium and surrounding matrix and mesenchyme (By similarity). {ECO:0000250}.
Mus musculus (Mouse)
O08539
BIN1_MOUSE
MAEMGSKGVTAGKIASNVQKKLTRAQEKVLQKLGKADETKDEQFEQCVQNFNKQLTEGTRLQKDLRTYLASVKAMHEASKKLSECLQEVYEPEWPGRDEANKIAENNDLLWMDYHQKLVDQALLTMDTYLGQFPDIKSRIAKRGRKLVDYDSARHHYESLQTAKKKDEAKIAKPVSLLEKAAPQWCQGKLQAHLVAQTNLLRNQAEEELIKAQKVFEEMNVDLQEELPSLWNSRVGFYVNTFQSIAGLEENFHKEMSKLNQNLNDVLVSLEKQHGSNTFTVKAQPSDNAPEKGNKSPSPPPDGSPAATPEIRVNHEPEPASGASPGATIPKSPSQLRKGPPVPPPPKHTPSKEMKQEQILSLFDDAFVPEISVTTPSQFEAPGPFSEQASLLDLDFEPLPPVASPVKAPTPSGQSIPWDLWEPTESQAGILPSGEPSSAEGSFAVAWPSQTAEPGPAQPAEASEVVGGAQEPGETAASEATSSSLPAVVVETFSATVNGAVEGSAGTGRLDLPPGFMFKVQAQHDYTATDTDELQLKAGDVVLVIPFQNPEEQDEGWLMGVKESDWNQHKELEKCRGVFPENFTERVQ
null
null
endosome to lysosome transport [GO:0008333]; lipid tube assembly [GO:0060988]; muscle cell differentiation [GO:0042692]; negative regulation of amyloid-beta formation [GO:1902430]; negative regulation of aspartic-type endopeptidase activity involved in amyloid precursor protein catabolic process [GO:1902960]; negative regulation of calcium ion transmembrane transport via high voltage-gated calcium channel [GO:1904878]; negative regulation of potassium ion transmembrane transport [GO:1901380]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of ventricular cardiac muscle cell action potential [GO:1903946]; nucleus localization [GO:0051647]; nucleus organization [GO:0006997]; positive regulation of actin filament polymerization [GO:0030838]; positive regulation of apoptotic process [GO:0043065]; positive regulation of astrocyte differentiation [GO:0048711]; positive regulation of endocytosis [GO:0045807]; regulation of cell cycle process [GO:0010564]; regulation of heart rate by cardiac conduction [GO:0086091]; regulation of neuron differentiation [GO:0045664]; synaptic vesicle endocytosis [GO:0048488]; T-tubule organization [GO:0033292]
axon [GO:0030424]; axon initial segment [GO:0043194]; axon terminus [GO:0043679]; cerebellar mossy fiber [GO:0044300]; cytosol [GO:0005829]; dendrite [GO:0030425]; endosome [GO:0005768]; extrinsic component of synaptic vesicle membrane [GO:0098850]; glutamatergic synapse [GO:0098978]; I band [GO:0031674]; lipid tube [GO:0060987]; microtubule [GO:0005874]; node of Ranvier [GO:0033268]; nuclear envelope [GO:0005635]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; RNA polymerase II transcription repressor complex [GO:0090571]; synapse [GO:0045202]; synaptic vesicle [GO:0008021]; T-tubule [GO:0030315]; varicosity [GO:0043196]; vesicle [GO:0031982]; Z disc [GO:0030018]
actin filament binding [GO:0051015]; aspartic-type endopeptidase inhibitor activity [GO:0019828]; GTPase binding [GO:0051020]; identical protein binding [GO:0042802]; phospholipid binding [GO:0005543]; protease binding [GO:0002020]; protein-containing complex binding [GO:0044877]; protein-folding chaperone binding [GO:0051087]; RNA polymerase binding [GO:0070063]; tau protein binding [GO:0048156]
PF03114;PF14604;
1.20.1270.60;2.30.30.40;
null
PTM: Phosphorylated by protein kinase C. {ECO:0000250}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O00499}. Cytoplasm {ECO:0000269|PubMed:12668730}. Endosome {ECO:0000269|PubMed:12668730}. Cell membrane, sarcolemma, T-tubule {ECO:0000250|UniProtKB:O08839}.
null
null
null
null
null
FUNCTION: Is a key player in the control of plasma membrane curvature, and membrane shaping and remodeling. Required in muscle cells for the formation of T-tubules, tubular invaginations of the plasma membrane that function in depolarization-contraction coupling. Required in muscle cells for the formation of T-tubules, tubular invaginations of the plasma membrane that function in depolarization-contraction coupling (PubMed:12183633). Is a negative regulator of endocytosis (By similarity). Is also involved in the regulation of intracellular vesicles sorting, modulation of BACE1 trafficking and the control of amyloid-beta production (PubMed:12668730, PubMed:27179792). In neuronal circuits, endocytosis regulation may influence the internalization of PHF-tau aggregates (By similarity). May be involved in the regulation of MYC activity and the control cell proliferation (By similarity). {ECO:0000250|UniProtKB:O00499, ECO:0000250|UniProtKB:O08839, ECO:0000269|PubMed:12183633, ECO:0000269|PubMed:12668730, ECO:0000269|PubMed:27179792}.
Mus musculus (Mouse)
O08543
EFNA5_MOUSE
MLHVEMLTLLFLVLWMCVFSQDPGSKVVADRYAVYWNSSNPRFQRGDYHIDVCINDYLDVFCPHYEDSVPEDKTERYVLYMVNFDGYSACDHTSKGFKRWECNRPHSPNGPLKFSEKFQLFTPFSLGFEFRPGREYFYISSAIPDNGRRSCLKLKVFVRPTNSCMKTIGVHDRVFDVNDKVENSLEPADDTVHESAEPSRGENAAQTPRIPSRLLAILLFLLAMLLTL
null
null
axon guidance [GO:0007411]; cellular response to follicle-stimulating hormone stimulus [GO:0071372]; cellular response to forskolin [GO:1904322]; collateral sprouting [GO:0048668]; ephrin receptor signaling pathway [GO:0048013]; negative regulation of substrate adhesion-dependent cell spreading [GO:1900025]; positive regulation of collateral sprouting [GO:0048672]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of synapse assembly [GO:0051965]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of cell morphogenesis [GO:0022604]; regulation of cell-cell adhesion [GO:0022407]; regulation of focal adhesion assembly [GO:0051893]; regulation of GTPase activity [GO:0043087]; regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0061178]; regulation of microtubule cytoskeleton organization [GO:0070507]; retinal ganglion cell axon guidance [GO:0031290]; synaptic membrane adhesion [GO:0099560]
adherens junction [GO:0005912]; basement membrane [GO:0005604]; caveola [GO:0005901]; cell periphery [GO:0071944]; external side of plasma membrane [GO:0009897]; GABA-ergic synapse [GO:0098982]; plasma membrane [GO:0005886]
chemorepellent activity [GO:0045499]; ephrin receptor binding [GO:0046875]; neurotrophin TRKB receptor binding [GO:0005169]
PF00812;
2.60.40.420;
Ephrin family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. Membrane, caveola {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. Note=Compartmentalized in discrete caveolae-like membrane microdomains. {ECO:0000250}.
null
null
null
null
null
FUNCTION: Cell surface GPI-bound ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Induces compartmentalized signaling within a caveolae-like membrane microdomain when bound to the extracellular domain of its cognate receptor. This signaling event requires the activity of the Fyn tyrosine kinase. Activates the EPHA3 receptor to regulate cell-cell adhesion and cytoskeletal organization. With the receptor EPHA2 may regulate lens fiber cells shape and interactions and be important for lens transparency maintenance. May function actively to stimulate axon fasciculation. The interaction of EFNA5 with EPHA5 also mediates communication between pancreatic islet cells to regulate glucose-stimulated insulin secretion. Cognate/functional ligand for EPHA7, their interaction regulates brain development modulating cell-cell adhesion and repulsion. {ECO:0000269|PubMed:11089974, ECO:0000269|PubMed:17448994, ECO:0000269|PubMed:18948590, ECO:0000269|PubMed:9053851}.
Mus musculus (Mouse)
O08545
EFNA3_MOUSE
MAAAPLLLLLLLVPVPLLPLLAQGPGGALGNRHAVYWNSSNQHLRREGYTVQVNVNDYLDIYCPHYNSSGPGGGAEQYVLYMVNLSGYRTCNASQGSKRWECNRQHASHSPIKFSEKFQRYSAFSLGYEFHAGQEYYYISTPTHNLHWKCLRMKVFVCCASTSHSGEKPVPTLPQFTMGPNVKINVLEDFEGENPQVPKLEKSISGTSPKREHLPLAVGIAFFLMTLLAS
null
null
axon guidance [GO:0007411]; ephrin receptor signaling pathway [GO:0048013]; negative regulation of angiogenesis [GO:0016525]; regulation of neuron differentiation [GO:0045664]
plasma membrane [GO:0005886]; side of membrane [GO:0098552]
ephrin receptor binding [GO:0046875]
PF00812;
2.60.40.420;
Ephrin family
null
SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
null
null
null
null
null
FUNCTION: Cell surface GPI-bound ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. {ECO:0000269|PubMed:9053851}.
Mus musculus (Mouse)
O08547
SC22B_MOUSE
MVLLTMIARVADGLPLAASMQEDEQSGRDLQQYQSQAKQLFRKLNEQSPTRCTLEAGAMTFHYIIEQGVCYLVLCEAAFPKKLAFAYLEDLHSEFDEQHGKKVPTVSRPYSFIEFDTFIQKTKKLYIDSRARRNLGSINTELQDVQRIMVANIEEVLQRGEALSALDSKANNLSSLSKKYRQDAKYLNMRSTYAKLAAVAVFFIMLIVYVRFWWL
null
null
endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; negative regulation of autophagosome assembly [GO:1902902]; positive regulation of protein catabolic process [GO:0045732]; protein transport [GO:0015031]; retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum [GO:0006890]; vesicle fusion with Golgi apparatus [GO:0048280]; vesicle-mediated transport [GO:0016192]
COPI-coated vesicle [GO:0030137]; endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; ER to Golgi transport vesicle membrane [GO:0012507]; Golgi membrane [GO:0000139]; melanosome [GO:0042470]; SNARE complex [GO:0031201]; synaptic vesicle [GO:0008021]
SNAP receptor activity [GO:0005484]; syntaxin binding [GO:0019905]
PF13774;PF00957;
1.20.5.110;3.30.450.50;
Synaptobrevin family
null
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q4KM74}; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:Q4KM74}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:Q4KM74}. Golgi apparatus, cis-Golgi network membrane {ECO:0000250|UniProtKB:Q4KM74}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q4KM74}. Melanosome {ECO:0000250|UniProtKB:O75396}. Note=Concentrated most in the intermediate compartment/cis-Golgi network and the cis-Golgi cisternae 1 and 2. Greatly reduced in concentration at the trans end of the Golgi apparatus. {ECO:0000250|UniProtKB:Q4KM74}.
null
null
null
null
null
FUNCTION: SNARE involved in targeting and fusion of ER-derived transport vesicles with the Golgi complex as well as Golgi-derived retrograde transport vesicles with the ER.
Mus musculus (Mouse)
O08550
KMT2B_MOUSE
MAAAAGGGSCPGPGSARGRFPGRPRGSGGGGGRGGRGNGAERVRVALRRGGGAAGPGGAEPGEDTALLRLLGLRRGLRRLRRLWAGARVQRGRGRGRGRGWGPNRGCMPEEESSDGESEEEEFQGFHSDEDVAPSSLRSALRSQRGRAPRGRGRKHKTTPLPPRLADVTPVPPKAPTRKRGEEGTERMVQALTELLRRSQAPQPPRSRARAREPSTPRRSRGRPPGRPAGPCRKKQQAVVLAEAAVTIPKPEPPPPVVPVKNKAGSWKCKEGPGPGPGTPKRGGQPGRGGRGGRGRGRGGLPLMIKFVSKAKKVKMGQLSQELESGQGHGQRGESWQDAPQRKDGDEPERGSCRKKQEQKLEEEEEEEEKEGEEKEEKDDNEDNNKQEEEEETERAVAEEEAMLAKEKEEAKLPSPPLTPPVPSPPPPLPPPSTSPPPPASPLPPPVSPPPPLSPPPYPAPEKQEESPPLVPATCSRKRGRPPLTPSQRAEREAARSGPEGTLSPTPNPSTTTGSPLEDSPTVVPKSTTFLKNIRQFIMPVVSARSSRVIKTPRRFMDEDPPKPPKVEASIVRPPVATSPPAPQEPVPVSSPPRVPTPPSTPVPLPEKRRSILREPTFRWTSLTRELPPPPPAPPPAPSPPPAPATPSRRPLLLRAPQFTPSEAHLKIYESVLTPPPLGALETPEPELPPADDSPAEPEPRAVGRTNHLSLPRFVPVVTSPVKVEVPPHGAPALSEGQQLQLQQPPQALQTQLLPQALPPQQPQAQPPPSPQHTPPLEKARVASLGSLPLSGVEEKMFSLLKRAKVQLFKIDQQQQQKVAASMPLSPAVQTEEAVGTVKQTPDRGCVRSEDESMEAKRDRASGPESPLQGPRIKHVCRHAAVALGQARAMVPEDVPRLSALPLRDRQDLATEDTSSASETESVPSRSQREKVESAGPGGDSEPTGSTGALAHTPRRSLPSHHGKKMRMARCGHCRGCLRVQDCGSCVNCLDKPKFGGPNTKKQCCVYRKCDKIEARKMERLAKKGRTIVKTLLPWDSDESPEASPGPPGPRRGAGAGGSREEVGATPGPEEQDSLLLQRKSARRCVKQRPSYDVFEDSDDSEPGGPPAPRRRTPREHELPVLEPEEQSRPRKPTLQPVLQLKARRRLDKDALAPGPFASFPNGWTGKQKSPDGVHRVRVDFKEDCDLENVWLMGGLSVLTSVPGGPPMVCLLCASKGLHELVFCQVCCDPFHPFCLEEAERPSPQHRDTWCCRRCKFCHVCGRKGRGSKHLLECERCRHAYHPACLGPSYPTRATRRRRHWICSACVRCKSCGATPGKNWDVEWSGDYSLCPRCTELYEKGNYCPICTRCYEDNDYESKMMQCAQCDHWVHAKCEGLSDEDYEILSGLPDSVLYTCGPCAGATQPRWREALSGALQGGLRQVLQGLLSSKVAGPLLLCTQCGQDGKQLHPGPCDLQAVGKRFEEGLYKSVHSFMEDVVAILMRHSEEGETPERRAGSQMKGLLLKLLESAFCWFDAHDPKYWRRSTRLPNGVLPNAVLPPSLDHVYAQWRQQESETPESGQPPGDPSAAFQSKDPAAFSHLDDPRQCALCLKYGDADSKEAGRLLYIGQNEWTHVNCAIWSAEVFEENDGSLKNVHAAVARGRQMRCELCLKPGATVGCCLSSCLSNFHFMCARASYCIFQDDKKVFCQKHTDLLDGKEIVTPDGFDVLRRVYVDFEGINFKRKFLTGLEPDVINVLIGSIRINSLGTLSDLSDCEGRLFPIGYQCSRLYWSTVDARRRCWYRCRILEYRPWGPREEPVHLEAAEENQTIVHSPTPSSDTDSLIPGDPVHHSPIQNLDPPLRTDSSNGPPPTPRSFSGARIKVPNYSPSRRPLGGVSFGPLPSPGSPSSLTHHIPTVGDSDFPAPPRRSRRPSPLATRPPPSRRTSSPLRTSPQLRVPLSTSVTALTPTSGELAPPDLAPSPLPPSEDLGPDFEDMEVVSGLSAADLDFAASLLGTEPFQEEIVAAGAVGSSQGGPGDSSEEEASPTTHYVHFPVTVVSGPALAPSSLAGAPRIEQLDGVDDGTDSEAEAVQQPRGQGTPPSGPGVGRGGVLGAAGDRAQPPEDLPSEIVDFVLKNLGGPGEGAAGPREDSLPSAPPLANGSQPPQSLSTSPADPTRTFAWLPGAPGVRVLSLGPAPEPPKPATSKIILVNKLGQVFVKMAGEGEPVAPPVKQPPLPPIIPPTAPTSWTLPPGPLLSVLPVVGVGVVRPAPPPPPPPLTLVFSSGPPSPPRQAIRVKRVSTFSGRSPPVPPPNKTPRLDEDGESLEDAHHVPGISGSGFSRVRMKTPTVRGVLDLNNPGEQPEEESPGRPQDRCPLLPLAEAPSQALDGSSDLLFESQWHHYSAGEASSSEEEPPSPEDKENQVPKRVGPHLRFEISSDDGFSVEAESLEVAWRTLIEKVQEARGHARLRHLSFSGMSGARLLGIHHDAVIFLAEQLPGAQRCQHYKFRYHQQGEGQEEPPLNPHGAARAEVYLRKCTFDMFNFLASQHRVLPEGATCDEEEDEVQLRSTRRATSLELPMAMRFRHLKKTSKEAVGVYRSAIHGRGLFCKRNIDAGEMVIEYSGIVIRSVLTDKREKFYDGKGIGCYMFRMDDFDVVDATMHGNAARFINHSCEPNCFSRVIHVEGQKHIVIFALRRILRGEELTYDYKFPIEDASNKLPCNCGAKRCRRFLN
2.1.1.364
null
DNA methylation-dependent heterochromatin formation [GO:0006346]; maternal-to-zygotic transition of gene expression [GO:0160021]; methylation [GO:0032259]; oocyte development [GO:0048599]; ovarian follicle development [GO:0001541]; ovulation [GO:0030728]; positive regulation of DNA-templated transcription [GO:0045893]
cytosol [GO:0005829]; histone methyltransferase complex [GO:0035097]; nucleus [GO:0005634]
histone H3K4 methyltransferase activity [GO:0042800]; histone H3K4 monomethyltransferase activity [GO:0140945]; histone H3K4 trimethyltransferase activity [GO:0140999]; unmethylated CpG binding [GO:0045322]; zinc ion binding [GO:0008270]
PF05965;PF05964;PF00628;PF00856;PF02008;PF13771;
3.30.160.360;1.20.920.10;2.170.270.10;3.30.40.10;
Class V-like SAM-binding methyltransferase superfamily, Histone-lysine methyltransferase family, TRX/MLL subfamily
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UMN6}.
CATALYTIC ACTIVITY: Reaction=L-lysyl(4)-[histone H3] + S-adenosyl-L-methionine = H(+) + N(6)-methyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60264, Rhea:RHEA-COMP:15543, Rhea:RHEA-COMP:15547, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.364; Evidence={ECO:0000250|UniProtKB:Q9UMN6}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60265; Evidence={ECO:0000250|UniProtKB:Q9UMN6}; CATALYTIC ACTIVITY: Reaction=N(6)-methyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-methionine = H(+) + N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60268, Rhea:RHEA-COMP:15540, Rhea:RHEA-COMP:15543, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61929, ChEBI:CHEBI:61976; Evidence={ECO:0000250|UniProtKB:Q9UMN6}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60269; Evidence={ECO:0000250|UniProtKB:Q9UMN6};
null
null
null
null
FUNCTION: Histone methyltransferase that catalyzes methyl group transfer from S-adenosyl-L-methionine to the epsilon-amino group of 'Lys-4' of histone H3 (H3K4) via a non-processive mechanism. Part of chromatin remodeling machinery predominantly forms H3K4me1 and H3K4me2 methylation marks at active chromatin sites where transcription and DNA repair take place (By similarity). Likely plays a redundant role with KMT2C in enriching H3K4me1 marks on primed and active enhancer elements (By similarity). Plays a central role in beta-globin locus transcription regulation by being recruited by NFE2 (By similarity). Plays an important role in controlling bulk H3K4me during oocyte growth and preimplantation development (PubMed:20808952). Required during the transcriptionally active period of oocyte growth for the establishment and/or maintenance of bulk H3K4 trimethylation (H3K4me3), global transcriptional silencing that preceeds resumption of meiosis, oocyte survival and normal zygotic genome activation (PubMed:20808952). {ECO:0000250|UniProtKB:Q9UMN6, ECO:0000269|PubMed:20808952}.
Mus musculus (Mouse)
O08553
DPYL2_MOUSE
MSYQGKKNIPRITSDRLLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPDQGMTSADDFFQGTKAALAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDITEWHKGIQEEMEALVKDHGVNSFLVYMAFKDRFQLTDSQIYEVLSVIRDIGAIAQVHAENGDIIAEEQQRILDLGITGPEGHVLSRPEEVEAEAVNRSITIANQTNCPLYVTKVMSKSAAEVIAQARKKGTVVYGEPITASLGTDGSHYWSKNWAKAAAFVTSPPLSPDPTTPDFLNSLLSCGDLQVTGSAHCTFNTAQKAVGKDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPRKGRISVGSDADLVIWDPDSVKTISAKTHNSALEYNIFEGMECRGSPLVVISQGKIVLEDGTLHVTEGSGRYIPRKPFPDFVYKRIKARSRLAELRGVPRGLYDGPVCEVSVTPKTVTPASSAKTSPAKQQAPPVRNLHQSGFSLSGAQIDDNIPRRTTQRIVAPPGGRANITSLG
null
null
cell differentiation [GO:0030154]; cytoskeleton organization [GO:0007010]; endocytosis [GO:0006897]; nervous system development [GO:0007399]; positive regulation of glutamate secretion [GO:0014049]; regulation of neuron differentiation [GO:0045664]; regulation of neuron projection development [GO:0010975]; synaptic vesicle transport [GO:0048489]
axon [GO:0030424]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; dendrite [GO:0030425]; growth cone [GO:0030426]; membrane [GO:0016020]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209]; neuronal cell body [GO:0043025]; presynapse [GO:0098793]; protein-containing complex [GO:0032991]; synapse [GO:0045202]
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides [GO:0016812]; protein kinase binding [GO:0019901]
PF01979;
3.20.20.140;2.30.40.10;
Metallo-dependent hydrolases superfamily, Hydantoinase/dihydropyrimidinase family
PTM: Phosphorylation by DYRK2 at Ser-522 is required for subsequent phosphorylation by GSK3B (By similarity). Phosphorylation at Thr-514 by GSK3B abolishes tubulin-binding leading to destabilization of microtubule assembly in axons and neurodegeneration. {ECO:0000250, ECO:0000269|PubMed:22057101}.
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Membrane {ECO:0000250}. Note=Tightly but non-covalently associated with membranes. {ECO:0000250}.
null
null
null
null
null
FUNCTION: Plays a role in neuronal development and polarity, as well as in axon growth and guidance, neuronal growth cone collapse and cell migration. Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. May play a role in endocytosis. {ECO:0000269|PubMed:22057101}.
Mus musculus (Mouse)
O08556
CCR5_RAT
MDFQGSIPTYIYDIDYSMSAPCQKVNVKQIAAQLLPPLYSLVFIFGFVGNMMVFLILISCKKLKSMTDIYLFNLAISDLLFLLTLPFWAHYAANEWVFGNIMCKLFTGIYHIGYFGGIFFIILLTIDRYLAIVHAVFAIKARTVNFGVITSVVTWVVAVFVSLPEIIFMRSQKEGSHYTCSPHFLHIQYRFWKHFQTLKMVILSLILPLLVMVICYSGILNTLFRCRNEKKRHRAVRLIFAIMIVYFLFWTPYNIVLLLTTFQEYFGLNNCSSSNRLDQAMQVTETLGMTHCCLNPVIYAFVGEKFRNYLSVFFRKHIVKRFCKHCSIFQQVNPDRVSSVYTRSTGEQEVSTGL
null
null
calcium ion transport [GO:0006816]; calcium-mediated signaling [GO:0019722]; cell chemotaxis [GO:0060326]; cell-cell signaling [GO:0007267]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to transforming growth factor beta stimulus [GO:0071560]; cellular response to tumor necrosis factor [GO:0071356]; defense response [GO:0006952]; defense response to bacterium [GO:0042742]; fat cell differentiation [GO:0045444]; forebrain development [GO:0030900]; G protein-coupled receptor signaling pathway [GO:0007186]; immune response [GO:0006955]; inflammatory response [GO:0006954]; inflammatory response to antigenic stimulus [GO:0002437]; leukocyte migration [GO:0050900]; MAPK cascade [GO:0000165]; negative regulation of axon extension [GO:0030517]; negative regulation of macrophage apoptotic process [GO:2000110]; negative regulation of neural precursor cell proliferation [GO:2000178]; positive regulation of cell killing [GO:0031343]; positive regulation of cell-cell adhesion [GO:0022409]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of fever generation [GO:0031622]; positive regulation of gene expression [GO:0010628]; positive regulation of interleukin-1 beta production [GO:0032731]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of neuron differentiation [GO:0045666]; positive regulation of tumor necrosis factor production [GO:0032760]; regulation of cell migration [GO:0030334]; release of sequestered calcium ion into cytosol by sarcoplasmic reticulum [GO:0014808]; response to cholesterol [GO:0070723]; response to ionizing radiation [GO:0010212]; response to lipopolysaccharide [GO:0032496]; signaling [GO:0023052]
cell surface [GO:0009986]; cytoplasm [GO:0005737]; endosome [GO:0005768]; external side of plasma membrane [GO:0009897]
actin binding [GO:0003779]; C-C chemokine binding [GO:0019957]; C-C chemokine receptor activity [GO:0016493]; chemokine (C-C motif) ligand 5 binding [GO:0071791]; identical protein binding [GO:0042802]; protein kinase binding [GO:0019901]
PF00001;
1.20.1070.10;
G-protein coupled receptor 1 family
PTM: Sulfated on at least 2 of the N-terminal tyrosines. Sulfation is required for efficient binding of the chemokines, CCL3 and CCL4 (By similarity). {ECO:0000250|UniProtKB:P51681}.; PTM: O-glycosylated, but not N-glycosylated. Ser-6 appears to be the major site. Also sialylated glycans present which contribute to chemokine binding. Ser-17 may also be glycosylated and, if so, with small moieties such as a T-antigen (By similarity). {ECO:0000250|UniProtKB:P51681}.; PTM: Palmitoylation in the C-terminal is important for cell surface expression. {ECO:0000250|UniProtKB:P51681}.; PTM: Phosphorylation on serine residues in the C-terminal is stimulated by binding CC chemokines especially by APO-RANTES. {ECO:0000250|UniProtKB:P51681}.
SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
null
null
null
null
null
FUNCTION: Receptor for a number of inflammatory CC-chemokines including CCL3/MIP-1-alpha, CCL4/MIP-1-beta and RANTES and subsequently transduces a signal by increasing the intracellular calcium ion level. May play a role in the control of granulocytic lineage proliferation or differentiation. Participates in T-lymphocyte migration to the infection site by acting as a chemotactic receptor. {ECO:0000250|UniProtKB:P51681}.
Rattus norvegicus (Rat)
O08557
DDAH1_RAT
MAGLSHPSVFGRATHAVVRAPPESLCRHALRRSQGEEVDFARAERQHQLYVGVLGSKLGLQVVQLPADESLPDCVFVEDVAVVCEETALITRPGAPSRRKEVDMMKEALEKLQLNIVEMKDENATLDGGDVLFTGREFFVGLSKRTNQRGAEILADTFKDYAVSTVPVADSLHLKSFCSMAGPNLIAIGSSESAQKALKIMQQMSDHRYDKLTVPDDMAANCIYLNIPSKGHVLLHRTPEEYPESAKVYEKLKDHLLIPVSNSEMEKVDGLLTCCSVFINKKTDS
3.5.3.18
null
arginine catabolic process [GO:0006527]; arginine metabolic process [GO:0006525]; citrulline metabolic process [GO:0000052]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of cellular response to hypoxia [GO:1900038]; negative regulation of vascular permeability [GO:0043116]; positive regulation of angiogenesis [GO:0045766]; positive regulation of nitric oxide biosynthetic process [GO:0045429]; regulation of systemic arterial blood pressure [GO:0003073]
null
amino acid binding [GO:0016597]; dimethylargininase activity [GO:0016403]; metal ion binding [GO:0046872]
PF19420;
null
DDAH family
null
null
CATALYTIC ACTIVITY: Reaction=H2O + N(omega),N(omega)-dimethyl-L-arginine = dimethylamine + L-citrulline; Xref=Rhea:RHEA:17305, ChEBI:CHEBI:15377, ChEBI:CHEBI:57743, ChEBI:CHEBI:58040, ChEBI:CHEBI:58326; EC=3.5.3.18; CATALYTIC ACTIVITY: Reaction=H2O + N(omega)-methyl-L-arginine = L-citrulline + methylamine; Xref=Rhea:RHEA:25173, ChEBI:CHEBI:15377, ChEBI:CHEBI:57743, ChEBI:CHEBI:59338, ChEBI:CHEBI:114953; EC=3.5.3.18; Evidence={ECO:0000250|UniProtKB:O94760};
null
null
null
null
FUNCTION: Hydrolyzes N(G),N(G)-dimethyl-L-arginine (ADMA) and N(G)-monomethyl-L-arginine (MMA) which act as inhibitors of NOS. Has therefore a role in the regulation of nitric oxide generation. {ECO:0000269|PubMed:16632550}.
Rattus norvegicus (Rat)
O08560
DGKZ_RAT
MEPRDPSPEARSSDSESASASSSGSERDADPEPDKAPRRLTKRRFPGLRLFGHRKAITKSGLQHLAPPPPTPGAPCGESERQIRSTVDWSESAAYGEHIWFETNVSGDFCYVGEQYCVAKMLPKSAPRRKCAACKIVVHTPCIGQLEKINFRCKPSFRESGSRNVREPTFVRHHWVHRRRQDGKCRHCGKGFQQKFTFHSKEIVAISCSWCKQAYHSKVSCFMLQQIEEPCSLGVHAAVVIPPTWILRARRPQNTLKASKKKKRASFKRRSSKKGPEEGRWRPFIIRPTPSPLMKPLLVFVNPKSGGNQGAKIIQSFLWYLNPRQVFDLSQGGPREALEMYRKVHNLRILACGGDGTVGWILSTLDQLRLKPPPPVAILPLGTGNDLARTLNWGGGYTDEPVSKILSHVEEGNVVQLDRWDLRAEPNPEAGPEERDDGATDRLPLDVFNNYFSLGFDAHVTLEFHESREANPEKFNSRFRNKMFYAGTAFSDFLMGSSKDLAKHIRVVCDGMDLTPKIQDLKPQCIVFLNIPRYCAGTMPWGHPGEHHDFEPQRHDDGYLEVIGFTMTSLAALQVGGHGERLTQCREVLLTTAKAIPVQVDGEPCKLAASRIRIALRNQATMVQKAKRRSTAPLHSDQQPVPEQLRIQVSRVSMHDYEALHYDKEQLKEASVPLGTVVVPGDSDLELCRAHIERLQQEPDGAGAKSPMCHPLSSKWCFLDATTASRFYRIDRAQEHLNYVTEIAQDEIYILDPELLGASARPDLPTPTSPLPASPCSPTPGSLQGDAALPQGEELIEAAKRNDFCKLQELHRAGGDLMHRDHQSRTLLHHAVSTGSKEVVRYLLDHAPPEILDAVEENGETCLHQAAALGQRTICHYIVEAGASLMKTDQQGDTPRQRAEKAQDTELAAYLENRQHYQMIQREDQETAV
2.7.1.107; 2.7.1.93
null
diacylglycerol metabolic process [GO:0046339]; glycerolipid metabolic process [GO:0046486]; intracellular signal transduction [GO:0035556]; lipid phosphorylation [GO:0046834]; maintenance of postsynaptic density structure [GO:0099562]; negative regulation of Ras protein signal transduction [GO:0046580]; negative regulation of T cell receptor signaling pathway [GO:0050860]; phosphatidic acid biosynthetic process [GO:0006654]; protein kinase C-activating G protein-coupled receptor signaling pathway [GO:0007205]; Ras protein signal transduction [GO:0007265]; regulation of synaptic transmission, glutamatergic [GO:0051966]
cytosol [GO:0005829]; glutamatergic synapse [GO:0098978]; lamellipodium [GO:0030027]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; Schaffer collateral - CA1 synapse [GO:0098685]
alkylglycerol kinase activity [GO:0047649]; ATP binding [GO:0005524]; ATP-dependent diacylglycerol kinase activity [GO:0004143]; enzyme inhibitor activity [GO:0004857]; kinase activity [GO:0016301]; metal ion binding [GO:0046872]
PF12796;PF00130;PF00609;PF00781;
2.60.200.40;1.25.40.20;
Eukaryotic diacylglycerol kinase family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8855332}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q13574}. Cell membrane {ECO:0000250|UniProtKB:Q13574}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q13574}.
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycerol + ATP = a 1,2-diacyl-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:10272, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:30616, ChEBI:CHEBI:58608, ChEBI:CHEBI:456216; EC=2.7.1.107; Evidence={ECO:0000250|UniProtKB:Q13574}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10273; Evidence={ECO:0000250|UniProtKB:Q13574}; CATALYTIC ACTIVITY: Reaction=1-O-alkyl-sn-glycerol + ATP = 1-O-alkyl-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:16937, ChEBI:CHEBI:15378, ChEBI:CHEBI:15850, ChEBI:CHEBI:30616, ChEBI:CHEBI:58014, ChEBI:CHEBI:456216; EC=2.7.1.93; Evidence={ECO:0000250|UniProtKB:Q13574}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16938; Evidence={ECO:0000250|UniProtKB:Q13574}; CATALYTIC ACTIVITY: Reaction=1-O-alkyl-2-acyl-sn-glycerol + ATP = 1-O-alkyl-2-acyl-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:44072, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:52595, ChEBI:CHEBI:73332, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q13574}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44073; Evidence={ECO:0000250|UniProtKB:Q13574}; CATALYTIC ACTIVITY: Reaction=1,2-didecanoyl-sn-glycerol + ATP = 1,2-didecanoyl-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:43428, ChEBI:CHEBI:15378, ChEBI:CHEBI:18155, ChEBI:CHEBI:30616, ChEBI:CHEBI:78227, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q13574}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43429; Evidence={ECO:0000250|UniProtKB:Q13574}; CATALYTIC ACTIVITY: Reaction=1,2-ditetradecanoyl-sn-glycerol + ATP = 1,2-ditetradecanoyl-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:43444, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:80651, ChEBI:CHEBI:83550, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q13574}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43445; Evidence={ECO:0000250|UniProtKB:Q13574}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + ATP = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:43416, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:64839, ChEBI:CHEBI:75466, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q13574}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43417; Evidence={ECO:0000250|UniProtKB:Q13574}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol + ATP = 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:40335, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:72864, ChEBI:CHEBI:77096, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q13574}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40336; Evidence={ECO:0000250|UniProtKB:Q13574}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + ATP = 1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:43424, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:74560, ChEBI:CHEBI:75468, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q13574}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43425; Evidence={ECO:0000250|UniProtKB:Q13574}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol + ATP = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:40323, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:75728, ChEBI:CHEBI:77091, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q13574}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40324; Evidence={ECO:0000250|UniProtKB:Q13574}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycerol + ATP = 1-octadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:40359, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:77129, ChEBI:CHEBI:77130, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q13574}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40360; Evidence={ECO:0000250|UniProtKB:Q13574}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + ATP = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:40327, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:52333, ChEBI:CHEBI:74546, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q13574}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40328; Evidence={ECO:0000250|UniProtKB:Q13574}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-2-hexadecanoyl-sn-glycerol + ATP = 1-(9Z)-octadecenoyl-2-hexadecanoyl-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:43420, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:74551, ChEBI:CHEBI:75447, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q13574}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43421; Evidence={ECO:0000250|UniProtKB:Q13574}; CATALYTIC ACTIVITY: Reaction=1-eicosanoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycerol + ATP = 1-eicosanoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:40331, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:77094, ChEBI:CHEBI:87223, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q13574}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40332; Evidence={ECO:0000250|UniProtKB:Q13574}; CATALYTIC ACTIVITY: Reaction=1,2-di-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycerol + ATP = 1,2-di-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:40351, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:77125, ChEBI:CHEBI:77126, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q13574}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40352; Evidence={ECO:0000250|UniProtKB:Q13574}; CATALYTIC ACTIVITY: Reaction=1-O-hexadecyl-2-acetyl-sn-glycerol + ATP = 1-O-hexadecyl-2-acetyl-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:41676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:75936, ChEBI:CHEBI:78385, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q13574}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41677; Evidence={ECO:0000250|UniProtKB:Q13574}; CATALYTIC ACTIVITY: Reaction=1-O-hexadecyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol + ATP = 1-O-hexadecyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:40403, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:77184, ChEBI:CHEBI:77186, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q13574}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40404; Evidence={ECO:0000250|UniProtKB:Q13574}; CATALYTIC ACTIVITY: Reaction=1-O-hexadecyl-2-(9Z-octadecenoyl)-sn-glycerol + ATP = 1-O-hexadecyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:40407, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:77185, ChEBI:CHEBI:77187, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q13574}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40408; Evidence={ECO:0000250|UniProtKB:Q13574}; CATALYTIC ACTIVITY: Reaction=1-O-hexadecyl-sn-glycerol + ATP = 1-O-hexadecyl-sn-glycero-3-phosphate + ADP + H(+); Xref=Rhea:RHEA:41672, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:34115, ChEBI:CHEBI:77580, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q13574}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41673; Evidence={ECO:0000250|UniProtKB:Q13574};
null
PATHWAY: Lipid metabolism; glycerolipid metabolism. {ECO:0000250|UniProtKB:Q13574}.
null
null
FUNCTION: Diacylglycerol kinase that converts diacylglycerol/DAG into phosphatidic acid/phosphatidate/PA and regulates the respective levels of these two bioactive lipids. Thereby, acts as a central switch between the signaling pathways activated by these second messengers with different cellular targets and opposite effects in numerous biological processes. Also plays an important role in the biosynthesis of complex lipids. Does not exhibit an acyl chain-dependent substrate specificity among diacylglycerol species. Can also phosphorylate 1-alkyl-2-acylglycerol in vitro but less efficiently and with a preference for alkylacylglycerols containing an arachidonoyl group (By similarity). The biological processes it is involved in include T cell activation since it negatively regulates T-cell receptor signaling which is in part mediated by diacylglycerol (By similarity). By generating phosphatidic acid, stimulates PIP5KIA activity which regulates actin polymerization (By similarity). Through the same mechanism could also positively regulate insulin-induced translocation of SLC2A4 to the cell membrane (By similarity). Regulates RASGRP1 activity (By similarity). {ECO:0000250|UniProtKB:Q13574, ECO:0000250|UniProtKB:Q80UP3}.
Rattus norvegicus (Rat)
O08561
PI4KB_RAT
MGDMVVEPATLKPTSEPTPSPSGNNGGSLLSVITEGVGELSVIDPEVAQKACQEVLEKVKLLHGGVAISSKGSPLELVNGDGVDNEIRCLDDPPTEIREEEDEMEPGVVSGTAKGTRRRRQNNSAKQSWLLRLFESKLFDISMAISYLYNSKEPGVQAYIGNRLFCFRNEDVDFYLPQLLNMYIHMDEDVGDAIKPYIVHRCRQSINFSLQCALLLGAYSSDMHISTQRHSRGTKLRKLILSDELKPAHRKRELPTLSPAPDTGLSPSKRTHQRSKSDATASISLSSNLKRTASNPKVENEDEELSSSTESIDNSFSSPVRLAPEREFIKSLMAIGKRLATLPTKEQKTQRLISELSLLNHKLPARVWLPTAGFDHHVVRVPHTQAVVLNSKDKAPYLIYVEVLECENFDTTNVPARIPENRIRSTRSVENLPECGITHEQRAGSFSTVPNYDNDDEAWSVDDIGELQVELPEVHTNSCDNISQFSVDSITSQESKEPVFIAAGDIRRRLSEQLAHTPTAFKRDPEDPSAVALKEPWQEKVRRIREGSPYGHLPNWRLLSVIVKCGDDLRQELLAFQVLKQLQSIWEQERVPLWIKPYKILVISADSGMIEPVVNAVSIHQVKKQSQLSLLDYFLQEHGSYTTEAFLSAQRNFVQSCAGYCLVCYLLQVKDRHNGNILLDAEGHIIHIDFGFILSSSPRNLGFETSAFKLTTEFVDVMGGLNGDMFNYYKMLMLQGLIAARKHMDKVVQIVEIMQQGSQLPCFHGSSTIRNLKERFHMSMTEEQLQLLVEQMVDGSMRSITTKLYDGFQYLTNGIM
2.7.1.67
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9UBF8}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q9UBF8};
inner ear development [GO:0048839]; lysosome organization [GO:0007040]; phosphatidylinositol phosphate biosynthetic process [GO:0046854]; phosphatidylinositol-mediated signaling [GO:0048015]; phosphorylation [GO:0016310]
cytoplasm [GO:0005737]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; membrane [GO:0016020]; mitochondrial outer membrane [GO:0005741]; rough endoplasmic reticulum membrane [GO:0030867]
1-phosphatidylinositol 4-kinase activity [GO:0004430]; 14-3-3 protein binding [GO:0071889]; ATP binding [GO:0005524]
PF00454;PF21245;
1.10.1070.11;
PI3/PI4-kinase family, Type III PI4K subfamily
null
SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:11526106, ECO:0000269|PubMed:19458041, ECO:0000269|PubMed:8973579}. Endomembrane system {ECO:0000250}. Mitochondrion outer membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Rough endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9UBF8}. Note=Found in the outer membrane of mitochondria and membranes of the rough endoplasmic reticulum. Recruited to the Golgi complex by the small GTPase ARF to stimulate the synthesis of phosphatidylinositol 4,5-bisphosphate (PIP2) on the Golgi complex. Recruited to the Golgi apparatus membrane by ACBD3, GGA2 is also involved in the recruitment. {ECO:0000250|UniProtKB:Q9UBF8}.
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ADP + H(+); Xref=Rhea:RHEA:19877, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57880, ChEBI:CHEBI:58178, ChEBI:CHEBI:456216; EC=2.7.1.67; Evidence={ECO:0000269|PubMed:8973579}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19878; Evidence={ECO:0000305|PubMed:8973579};
null
null
null
null
FUNCTION: Phosphorylates phosphatidylinositol (PI) in the first committed step in the production of the second messenger inositol-1,4,5,-trisphosphate (PIP) (PubMed:8973579). May regulate Golgi disintegration/reorganization during mitosis, possibly via its phosphorylation (By similarity). Involved in Golgi-to-plasma membrane trafficking (PubMed:8973579). May play an important role in the inner ear development. {ECO:0000250|UniProtKB:Q9UBF8, ECO:0000269|PubMed:8973579}.
Rattus norvegicus (Rat)
O08562
SCN9A_RAT
MAMLPPPGPQSFVHFTKQSLALIEQRISEEKAKEHKDEKKDDEEEGPKPSSDLEAGKQLPFIYGDIPPGMVSEPLEDLDPYYADKKTFIVLNKGKAIFRFNATPALYMLSPFSPLRRISIKILVHSLFSMLIMCTILTNCIFMTLSNPPEWTKNVEYTFTGIYTFESLIKILARGFCVGEFTFLRDPWNWLDFVVIVFAYLTEFVNLGNVSALRTFRVLRALKTISVIPGLKTIVGALIQSVKKLSDVMILTVFCLSVFALIGLQLFMGNLKHKCFRKELEENETLESIMNTAESEEELKKYFYYLEGSKDALLCGFSTDSGQCPEGYICVKAGRNPDYGYTSFDTFSWAFLALFRLMTQDYWENLYQQTLRAAGKTYMIFFVVVIFLGSFYLINLILAVVAMAYEEQNQANIEEAKQKELEFQQMLDRLKKEQEEAEAIAAAAAEFTSIGRSRIMGLSESSSETSRLSSKSAKERRNRRKKKKQKMSSGEEKGDDEKLSKSGSEESIRKKSFHLGVEGHHRTREKRLSTPNQSPLSIRGSLFSARRSSRTSLFSFKGRGRDLGSETEFADDEHSIFGDNESRRGSLFVPHRPRERRSSNISQASRSPPVLPVNGKMHSAVDCNGVVSLVDGPSALMLPNGQLLPEVIIDKATSDDSGTTNQMRKKRLSSSYFLSEDMLNDPHLRQRAMSRASILTNTVEELEESRQKCPPWWYRFAHTFLIWNCSPYWIKFKKLIYFIVMDPFVDLAITICIVLNTLFMAMEHHPMTEEFKNVLAVGNLIFTGIFAAEMVLKLIAMDPYEYFQVGWNIFDSLIVTLSLIELFLADVEGLSVLRSFRLLRVFKLAKSWPTLNMLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKSYKECVCKINVDCKLPRWHMNDFFHSFLIVFRVLCGEWIETMWDCMEVAGQTMCLIVYMMVMVIGNLVVLNLFLALLLSSFSSDNLTAIEEDTDANNLQIAVARIKRGINYVKQTLREFILKSFSKKPKGSKDTKRTADPNNKKENYISNRTLAEMSKDHNFLKEKDRISGYGSSLDKSFMDENDYQSFIHNPSLTVTVPIAPGESDLEIMNTEELSSDSDSDYSKEKRNRSSSSECSTVDNPLPGEEEAEAEPVNADEPEACFTDGCVRRFPCCQVNVDSGKGKVWWTIRKTCYRIVEHSWFESFIVLMILLSSGALAFEDIYIEKKKTIKIILEYADKIFTYIFILEMLLKWVAYGYKTYFTNAWCWLDFLIVDVSLVTLVANTLGYSDLGPIKSLRTLRALRPLRALSRFEGMRVVVNALIGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKFYECVNTTDGSRFPTSQVANRSECFALMNVSGNVRWKNLKVNFDNVGLGYLSLLQVATFKGWMDIMYAAVDSVNVNEQPKYEYSLYMYIYFVIFIIFGSFFTLNLFIGVIIDNFNQQKKKLGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPGNKFQGCIFDLVTNQAFDITIMVLICLNMVTMMVEKEGQTEYMDYVLHWINMVFIILFTGECVLKLISLRHYYFTVGWNIFDFVVVILSIVGMFLAEMIEKYFVSPTLFRVIRLARIGRILRLIKGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYAIFGMSNFAYVKKEAGINDMFNFETFGNSMICLFQITTSAGWDGLLAPILNSAPPDCDPKKVHPGSSVEGDCGNPSVGIFYFVSYIIISFLVVVNMYIAVILENFSVATEESTEPLSEDDFEMFYEVWEKFDPDATQFIEFCKLSDFAAALDPPLLIAKPNKVQLIAMDLPMVSGDRIHCLDILFAFTKRVLGEGGEMDSLRSQMEERFMSANPSKVSYEPITTTLKRKQEEVSATIIQRAYRRYRLRQHVKNISSIYIKDGDRDDDLPNKEDTVFDNVNENSSPEKTDVTASTISPPSYDSVTKPDQEKYETDKTEKEDKEKDESRK
null
null
behavioral response to formalin induced pain [GO:0061368]; behavioral response to pain [GO:0048266]; circadian rhythm [GO:0007623]; detection of mechanical stimulus involved in sensory perception [GO:0050974]; detection of temperature stimulus involved in sensory perception of pain [GO:0050965]; inflammatory response [GO:0006954]; membrane depolarization during action potential [GO:0086010]; negative regulation of action potential [GO:0045759]; neuronal action potential [GO:0019228]; post-embryonic development [GO:0009791]; response to toxic substance [GO:0009636]; rhythmic excitation [GO:0043179]; sensory perception of pain [GO:0019233]; sodium ion transmembrane transport [GO:0035725]
axon [GO:0030424]; plasma membrane [GO:0005886]; voltage-gated sodium channel complex [GO:0001518]
sodium ion binding [GO:0031402]; voltage-gated sodium channel activity [GO:0005248]
PF00520;PF06512;PF11933;
1.10.287.70;1.10.238.10;1.20.5.1190;1.20.120.350;
Sodium channel (TC 1.A.1.10) family, Nav1.7/SCN9A subfamily
PTM: Phosphorylation at Ser-1488 by PKC in a highly conserved cytoplasmic loop increases peak sodium currents. {ECO:0000250|UniProtKB:Q15858}.; PTM: Ubiquitinated by NEDD4L; which may promote its endocytosis. Does not seem to be ubiquitinated by NEDD4. {ECO:0000250|UniProtKB:Q62205}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q15858}; Multi-pass membrane protein {ECO:0000250|UniProtKB:D0E0C2}. Cell projection, neuron projection {ECO:0000269|PubMed:9037087}. Note=In neurite terminals. {ECO:0000269|PubMed:9037087}.
null
null
null
null
null
FUNCTION: Mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient. It is a tetrodotoxin-sensitive Na(+) channel isoform. Plays a role in pain mechanisms, especially in the development of inflammatory pain. {ECO:0000250|UniProtKB:Q15858}.
Rattus norvegicus (Rat)
O08564
PLPP1_RAT
MFDKPRLPYVVLDVICVLLAGLPFIILTSRHTPFQRGVFCTDESIKYPYREDTIPYALLGGIVIPFCIIVMITGETLSVYFNVLHSNSFVSNHYIATIYKAVGAFLFGASASQSLTDIAKYSIGRLRPHFLAVCNPDWSKINCSDGYIENFVCQGNEQKVREGRLSFYSGHSSFSMYCMLFVALYLQARMKGDWARLLRPMLQFGLVALSIYVGLSRVSDYKHHWSDVLIGLIQGAVVAILVVLYVTDFFKTTESNKERKEDSHTTLHETTNRQSYARNHEP
3.1.3.-; 3.1.3.106; 3.1.3.4; 3.6.1.75
null
ceramide metabolic process [GO:0006672]; phospholipid dephosphorylation [GO:0046839]; phospholipid metabolic process [GO:0006644]; signal transduction [GO:0007165]; sphingosine metabolic process [GO:0006670]
apical plasma membrane [GO:0016324]; caveola [GO:0005901]; membrane [GO:0016020]; membrane raft [GO:0045121]; plasma membrane [GO:0005886]
ceramide-1-phosphate phosphatase activity [GO:0106235]; diacylglycerol diphosphate phosphatase activity [GO:0000810]; lipid phosphatase activity [GO:0042577]; lysophosphatidic acid phosphatase activity [GO:0052642]; phosphatidate phosphatase activity [GO:0008195]; sphingosine-1-phosphate phosphatase activity [GO:0042392]
PF01569;
1.20.144.10;
PA-phosphatase related phosphoesterase family
PTM: N-glycosylated. N-linked sugars are of the complex type. N-glycosylation is not required for the phosphatase activity. {ECO:0000250|UniProtKB:Q61469}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8663293}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:O14494}; Multi-pass membrane protein {ECO:0000255}. Membrane raft {ECO:0000250|UniProtKB:O14494}; Multi-pass membrane protein {ECO:0000255}. Membrane, caveola {ECO:0000250|UniProtKB:Q61469}; Multi-pass membrane protein {ECO:0000255}.
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + H2O = a 1,2-diacyl-sn-glycerol + phosphate; Xref=Rhea:RHEA:27429, ChEBI:CHEBI:15377, ChEBI:CHEBI:17815, ChEBI:CHEBI:43474, ChEBI:CHEBI:58608; EC=3.1.3.4; Evidence={ECO:0000269|PubMed:10359651, ECO:0000269|PubMed:8663293}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27430; Evidence={ECO:0000305|PubMed:10359651}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphate + H2O = 1,2-dihexadecanoyl-sn-glycerol + phosphate; Xref=Rhea:RHEA:43236, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:72859, ChEBI:CHEBI:82929; Evidence={ECO:0000250|UniProtKB:O14494}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43237; Evidence={ECO:0000250|UniProtKB:O14494}; CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 1,2-di-(9Z-octadecenoyl)-sn-glycerol + phosphate; Xref=Rhea:RHEA:43244, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:52333, ChEBI:CHEBI:74546; Evidence={ECO:0000269|PubMed:8663293}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43245; Evidence={ECO:0000305|PubMed:8663293}; CATALYTIC ACTIVITY: Reaction=H2O + monoacyl-sn-glycero-3-phosphate = a monoacylglycerol + phosphate; Xref=Rhea:RHEA:46736, ChEBI:CHEBI:15377, ChEBI:CHEBI:17408, ChEBI:CHEBI:43474, ChEBI:CHEBI:77589; Evidence={ECO:0000269|PubMed:10359651, ECO:0000269|PubMed:8663293}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46737; Evidence={ECO:0000269|PubMed:10359651}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-sn-glycero-3-phosphate + H2O = (9Z-octadecenoyl)-glycerol + phosphate; Xref=Rhea:RHEA:50884, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:75937, ChEBI:CHEBI:84973; Evidence={ECO:0000269|PubMed:8663293}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50885; Evidence={ECO:0000305|PubMed:8663293}; CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphate + H2O = a 1-acyl-sn-glycerol + phosphate; Xref=Rhea:RHEA:33155, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57970, ChEBI:CHEBI:64683; EC=3.1.3.106; Evidence={ECO:0000269|PubMed:8663293}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33156; Evidence={ECO:0000305|PubMed:8663293}; CATALYTIC ACTIVITY: Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 1-(9Z-octadecenoyl)-sn-glycerol + phosphate; Xref=Rhea:RHEA:39835, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:74544, ChEBI:CHEBI:75757; Evidence={ECO:0000250|UniProtKB:Q61469}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39836; Evidence={ECO:0000250|UniProtKB:Q61469}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycerol 3-diphosphate + H2O = a 1,2-diacyl-sn-glycero-3-phosphate + H(+) + phosphate; Xref=Rhea:RHEA:27449, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58608, ChEBI:CHEBI:59996; EC=3.6.1.75; Evidence={ECO:0000269|PubMed:10359651}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27450; Evidence={ECO:0000305|PubMed:10359651}; CATALYTIC ACTIVITY: Reaction=H2O + sphing-4-enine 1-phosphate = phosphate + sphing-4-enine; Xref=Rhea:RHEA:27518, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57756, ChEBI:CHEBI:60119; Evidence={ECO:0000269|PubMed:10359651, ECO:0000269|PubMed:8663293}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27519; Evidence={ECO:0000305|PubMed:10359651}; CATALYTIC ACTIVITY: Reaction=an N-acylsphing-4-enine 1-phosphate + H2O = an N-acylsphing-4-enine + phosphate; Xref=Rhea:RHEA:33743, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:52639, ChEBI:CHEBI:57674; Evidence={ECO:0000269|PubMed:10359651, ECO:0000269|PubMed:8663293}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33744; Evidence={ECO:0000305|PubMed:10359651}; CATALYTIC ACTIVITY: Reaction=H2O + N-(octanoyl)-sphing-4-enine-1-phosphate = N-octanoylsphing-4-enine + phosphate; Xref=Rhea:RHEA:62040, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:45815, ChEBI:CHEBI:85376; Evidence={ECO:0000250|UniProtKB:O14494}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62041; Evidence={ECO:0000250|UniProtKB:O14494}; CATALYTIC ACTIVITY: Reaction=H2O + N-(9Z-octadecenoyl)-ethanolamine phosphate = N-(9Z-octadecenoyl) ethanolamine + phosphate; Xref=Rhea:RHEA:62160, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:71466, ChEBI:CHEBI:145465; Evidence={ECO:0000250|UniProtKB:O14494}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62161; Evidence={ECO:0000250|UniProtKB:O14494}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + phosphate; Xref=Rhea:RHEA:41255, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:64839, ChEBI:CHEBI:75466; Evidence={ECO:0000269|PubMed:10359651}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41256; Evidence={ECO:0000305|PubMed:10359651};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.5 uM for 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate (at pH 6.5 and 37 degrees Celsius) {ECO:0000269|PubMed:8663293}; KM=0.4 uM for (9Z)-octadecenoyl-sn-glycero-3-phosphate (at pH 6.5 and 37 degrees Celsius) {ECO:0000269|PubMed:8663293}; KM=1.9 uM for N-acylsphing-4-enine 1-phosphate (at pH 6.5 and 37 degrees Celsius) {ECO:0000269|PubMed:8663293}; KM=4 uM for sphing-4-enine 1-phosphate (at pH 6.5 and 37 degrees Celsius) {ECO:0000269|PubMed:8663293}; Vmax=0.55 umol/min/mg enzyme with 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate as substrate {ECO:0000269|PubMed:8663293}; Vmax=0.19 umol/min/mg enzyme with (9Z)-octadecenoyl-sn-glycero-3-phosphate as substrate {ECO:0000269|PubMed:8663293}; Vmax=0.26 umol/min/mg enzyme with N-acylsphing-4-enine 1-phosphate as substrate {ECO:0000269|PubMed:8663293}; Vmax=0.15 umol/min/mg enzyme with sphing-4-enine 1-phosphate as substrate {ECO:0000269|PubMed:8663293};
PATHWAY: Lipid metabolism; phospholipid metabolism. {ECO:0000269|PubMed:10359651, ECO:0000269|PubMed:8663293}.
null
null
FUNCTION: Magnesium-independent phospholipid phosphatase of the plasma membrane that catalyzes the dephosphorylation of a variety of glycerolipid and sphingolipid phosphate esters including phosphatidate/PA, lysophosphatidate/LPA, diacylglycerol pyrophosphate/DGPP, sphingosine 1-phosphate/S1P and ceramide 1-phosphate/C1P (PubMed:10359651, PubMed:8663293). Also acts on N-oleoyl ethanolamine phosphate/N-(9Z-octadecenoyl)-ethanolamine phosphate, a potential physiological compound (By similarity). Through its extracellular phosphatase activity allows both the hydrolysis and the cellular uptake of these bioactive lipid mediators from the milieu, regulating signal transduction in different cellular processes (PubMed:10359651). It is for instance essential for the extracellular hydrolysis of S1P and subsequent conversion into intracellular S1P (By similarity). Involved in the regulation of inflammation, platelets activation, cell proliferation and migration among other processes (By similarity). May also have an intracellular activity to regulate phospholipid-mediated signaling pathways (PubMed:17057224). {ECO:0000250|UniProtKB:O14494, ECO:0000269|PubMed:10359651, ECO:0000269|PubMed:17057224, ECO:0000269|PubMed:8663293}.
Rattus norvegicus (Rat)
O08565
CXCR4_RAT
MEIYTSDNYSEEVGSGDYDSNKEPCFRDENENFNRIFLPTIYFIIFLTGIVGNGLVILVMGYQKKLRSMTDKYRLHLSVADLLFVITLPFWAVDAMADWYFGKFLCKAVHIIYTVNLYSSVLILAFISLDRYLAIVHATNSQRPRKLLAEKAVYVGVWIPALLLTIPDIIFADVSQGDGRYICDRLYPDSLWMVVFQFQHIMVGLILPGIVILSCYCIIISKLSHSKGHQKRKALKTTVILILAFFACWLPYYVGISIDSFILLEVIKQGCEFESVVHKWISITEALAFFHCCLNPILYAFLGAKFKSSAQHALNSMSRGSSLKILSKGKRGGHSSVSTESESSSFHSS
null
null
aorta development [GO:0035904]; blood vessel endothelial cell migration [GO:0043534]; brain development [GO:0007420]; branching involved in blood vessel morphogenesis [GO:0001569]; calcium-mediated signaling [GO:0019722]; cardiac muscle contraction [GO:0060048]; cell chemotaxis [GO:0060326]; cell migration [GO:0016477]; cellular response to cytokine stimulus [GO:0071345]; cellular response to organonitrogen compound [GO:0071417]; cellular response to xenobiotic stimulus [GO:0071466]; CXCL12-activated CXCR4 signaling pathway [GO:0038160]; detection of mechanical stimulus involved in sensory perception of pain [GO:0050966]; detection of temperature stimulus involved in sensory perception of pain [GO:0050965]; endothelial cell differentiation [GO:0045446]; endothelial tube morphogenesis [GO:0061154]; epithelial cell development [GO:0002064]; G protein-coupled receptor signaling pathway [GO:0007186]; generation of neurons [GO:0048699]; germ cell development [GO:0007281]; germ cell migration [GO:0008354]; hematopoietic stem cell migration [GO:0035701]; immune response [GO:0006955]; kidney development [GO:0001822]; motor neuron axon guidance [GO:0008045]; myelin maintenance [GO:0043217]; neural precursor cell proliferation [GO:0061351]; neurogenesis [GO:0022008]; neuron migration [GO:0001764]; neuron recognition [GO:0008038]; osteoclast differentiation [GO:0030316]; positive regulation of calcium ion import [GO:0090280]; positive regulation of cell migration [GO:0030335]; positive regulation of chemotaxis [GO:0050921]; positive regulation of cold-induced thermogenesis [GO:0120162]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of dendrite extension [GO:1903861]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of macrophage migration inhibitory factor signaling pathway [GO:2000448]; positive regulation of mesenchymal stem cell migration [GO:1905322]; positive regulation of neurogenesis [GO:0050769]; positive regulation of oligodendrocyte differentiation [GO:0048714]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of vascular wound healing [GO:0035470]; positive regulation of vasculature development [GO:1904018]; regulation of calcium ion transport [GO:0051924]; regulation of cell adhesion [GO:0030155]; regulation of cell migration [GO:0030334]; regulation of chemotaxis [GO:0050920]; regulation of neuron migration [GO:2001222]; regulation of programmed cell death [GO:0043067]; regulation of viral process [GO:0050792]; response to activity [GO:0014823]; response to hypoxia [GO:0001666]; response to organic cyclic compound [GO:0014070]; response to tacrolimus [GO:1901327]; response to ultrasound [GO:1990478]; T cell proliferation [GO:0042098]; telencephalon cell migration [GO:0022029]; ventricular septum development [GO:0003281]
cell leading edge [GO:0031252]; cell surface [GO:0009986]; cell-cell junction [GO:0005911]; cytoplasmic vesicle [GO:0031410]; early endosome [GO:0005769]; endosome [GO:0005768]; external side of plasma membrane [GO:0009897]; growth cone [GO:0030426]; late endosome [GO:0005770]; lysosome [GO:0005764]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]
actin binding [GO:0003779]; C-C chemokine binding [GO:0019957]; C-C chemokine receptor activity [GO:0016493]; C-X-C chemokine receptor activity [GO:0016494]; C-X-C motif chemokine 12 receptor activity [GO:0038147]; myosin light chain binding [GO:0032027]; small molecule binding [GO:0036094]; ubiquitin binding [GO:0043130]; ubiquitin protein ligase binding [GO:0031625]
PF00001;PF12109;
1.20.1070.10;
G-protein coupled receptor 1 family
PTM: Phosphorylated on agonist stimulation. Rapidly phosphorylated on serine and threonine residues in the C-terminal. Phosphorylation at Ser-321 and Ser-322 leads to recruitment of ITCH, ubiquitination and protein degradation. {ECO:0000250|UniProtKB:P61073}.; PTM: Ubiquitinated after ligand binding, leading to its degradation. Ubiquitinated by ITCH at the cell membrane on agonist stimulation. The ubiquitin-dependent mechanism, endosomal sorting complex required for transport (ESCRT), then targets CXCR4 for lysosomal degradation. This process is dependent also on prior Ser-/Thr-phosphorylation in the C-terminal of CXCR4. Also binding of ARRB1 to STAM negatively regulates CXCR4 sorting to lysosomes though modulating ubiquitination of SFR5S. {ECO:0000250|UniProtKB:P61073}.; PTM: Sulfation is required for efficient binding of CXCL12/SDF-1alpha and promotes its dimerization. {ECO:0000250|UniProtKB:P61073}.; PTM: O- and N-glycosylated. N-glycosylation can mask coreceptor function. The O-glycosylation chondroitin sulfate attachment does not affect interaction with CXCL12/SDF-1alpha nor its coreceptor activity. {ECO:0000250|UniProtKB:P61073}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P61073}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P61073}. Cell junction {ECO:0000250}. Early endosome {ECO:0000250}. Late endosome {ECO:0000250}. Lysosome {ECO:0000250}. Note=In unstimulated cells, diffuse pattern on plasma membrane. On agonist stimulation, colocalizes with ITCH at the plasma membrane where it becomes ubiquitinated (By similarity). In the presence of antigen, distributes to the immunological synapse forming at the T-cell-APC contact area, where it localizes at the peripheral and distal supramolecular activation cluster (SMAC) (By similarity). {ECO:0000250}.
null
null
null
null
null
FUNCTION: Receptor for the C-X-C chemokine CXCL12/SDF-1 that transduces a signal by increasing intracellular calcium ion levels and enhancing MAPK1/MAPK3 activation. Involved in the AKT signaling cascade (By similarity). Plays a role in regulation of cell migration, e.g. during wound healing. Acts as a receptor for extracellular ubiquitin; leading to enhanced intracellular calcium ions and reduced cellular cAMP levels. Binds bacterial lipopolysaccharide (LPS) et mediates LPS-induced inflammatory response, including TNF secretion by monocytes (By similarity). Involved in hematopoiesis and in cardiac ventricular septum formation. Also plays an essential role in vascularization of the gastrointestinal tract, probably by regulating vascular branching and/or remodeling processes in endothelial cells. Involved in cerebellar development. In the CNS, could mediate hippocampal-neuron survival (By similarity). {ECO:0000250|UniProtKB:P61073, ECO:0000250|UniProtKB:P70658}.
Rattus norvegicus (Rat)
O08573
LEG9_MOUSE
MALFSAQSPYINPIIPFTGPIQGGLQEGLQVTLQGTTKSFAQRFVVNFQNSFNGNDIAFHFNPRFEEGGYVVCNTKQNGQWGPEERKMQMPFQKGMPFELCFLVQRSEFKVMVNKKFFVQYQHRVPYHLVDTIAVSGCLKLSFITFQNSAAPVQHVFSTLQFSQPVQFPRTPKGRKQKTQNFRPAHQAPMAQTTIHMVHSTPGQMFSTPGIPPVVYPTPAYTIPFYTPIPNGLYPSKSIMISGNVLPDATRFHINLRCGGDIAFHLNPRFNENAVVRNTQINNSWGQEERSLLGRMPFSRGQSFSVWIICEGHCFKVAVNGQHMCEYYHRLKNLQDINTLEVAGDIQLTHVQT
null
null
cellular response to virus [GO:0098586]; chemotaxis [GO:0006935]; female pregnancy [GO:0007565]; heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0007157]; immune system process [GO:0002376]; maintenance of protein location [GO:0045185]; negative regulation of CD4-positive, alpha-beta T cell proliferation [GO:2000562]; negative regulation of gene expression [GO:0010629]; negative regulation of inflammatory response [GO:0050728]; negative regulation of natural killer cell activation [GO:0032815]; negative regulation of natural killer cell degranulation [GO:0043322]; negative regulation of type II interferon production [GO:0032689]; positive regulation of chemokine production [GO:0032722]; positive regulation of cytokine production [GO:0001819]; positive regulation of defense response to bacterium [GO:1900426]; positive regulation of gene expression [GO:0010628]; positive regulation of innate immune response [GO:0045089]; positive regulation of interleukin-1 production [GO:0032732]; positive regulation of interleukin-10 production [GO:0032733]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of macrophage activation [GO:0043032]; positive regulation of oxidoreductase activity [GO:0051353]; positive regulation of regulatory T cell differentiation [GO:0045591]; positive regulation of SMAD protein signal transduction [GO:0060391]; positive regulation of T cell migration [GO:2000406]; positive regulation of tumor necrosis factor production [GO:0032760]; receptor clustering [GO:0043113]; regulation of natural killer cell differentiation [GO:0032823]; response to lipopolysaccharide [GO:0032496]; transforming growth factor beta receptor signaling pathway [GO:0007179]
collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular region [GO:0005576]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
carbohydrate binding [GO:0030246]; enzyme binding [GO:0019899]; galactoside binding [GO:0016936]; protein serine/threonine kinase activator activity [GO:0043539]; signaling receptor binding [GO:0005102]
PF00337;
2.60.120.200;
null
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23242525}. Nucleus {ECO:0000269|PubMed:23242525}. Secreted {ECO:0000250|UniProtKB:O00182}. Note=May also be secreted by a non-classical secretory pathway (PubMed:9038233). Secreted by mesenchymal stromal cells upon IFNG stimulation (By similarity). {ECO:0000250|UniProtKB:O00182, ECO:0000269|PubMed:9038233}.
null
null
null
null
null
FUNCTION: Binds galactosides (By similarity). Has high affinity for the Forssman pentasaccharide (By similarity). Ligand for HAVCR2/TIM3 (By similarity). Binding to HAVCR2 induces T-helper type 1 lymphocyte (Th1) death (By similarity). Also stimulates bactericidal activity in infected macrophages by causing macrophage activation and IL1B secretion which restricts intracellular bacterial growth (PubMed:20937702). Ligand for P4HB; the interaction retains P4HB at the cell surface of Th2 T-helper cells, increasing disulfide reductase activity at the plasma membrane, altering the plasma membrane redox state and enhancing cell migration (PubMed:21670307). Ligand for CD44; the interaction enhances binding of SMAD3 to the FOXP3 promoter, leading to up-regulation of FOXP3 expression and increased induced regulatory T (iTreg) cell stability and suppressive function (PubMed:25065622). Promotes ability of mesenchymal stromal cells to suppress T-cell proliferation (By similarity). Expands regulatory T-cells and induces cytotoxic T-cell apoptosis following virus infection (By similarity). Activates ERK1/2 phosphorylation inducing cytokine (IL-6, IL-8, IL-12) and chemokine (CCL2) production in mast and dendritic cells (By similarity). Inhibits degranulation and induces apoptosis of mast cells (By similarity). Induces maturation and migration of dendritic cells (By similarity). Inhibits natural killer (NK) cell function (PubMed:23408620). Can transform NK cell phenotype from peripheral to decidual during pregnancy (By similarity). Astrocyte derived galectin-9 enhances microglial TNF production (PubMed:25158758). May play a role in thymocyte-epithelial interactions relevant to the biology of the thymus. May provide the molecular basis for urate flux across cell membranes, allowing urate that is formed during purine metabolism to efflux from cells and serving as an electrogenic transporter that plays an important role in renal and gastrointestinal urate excretion (By similarity). Highly selective to the anion urate (By similarity). {ECO:0000250|UniProtKB:O00182, ECO:0000250|UniProtKB:P97840, ECO:0000269|PubMed:20937702, ECO:0000269|PubMed:21670307, ECO:0000269|PubMed:23408620, ECO:0000269|PubMed:25065622, ECO:0000269|PubMed:25158758}.; FUNCTION: [Isoform 2]: Acts as an eosinophil chemoattractant (By similarity). It also inhibits angiogenesis (By similarity). Suppresses IFNG production by natural killer cells. {ECO:0000250|UniProtKB:O00182, ECO:0000269|PubMed:23242525}.
Mus musculus (Mouse)
O08574
MESP2_MOUSE
MAQSSPPQSLQGLVPLGLLPGLGLGSAIGLHVSGLVLRFVRFLPFYATRRPSQPAGPARSTRTTQATAPRRTRPAPAGGQRQSASEREKLRMRTLARALQELRRFLPPSVAPAGQSLTKIETLRLAIRYIGHLSALLGLSEDSLRRRRRRSADAAFSHRCPQCPDGGSPSQAQMLGPSLGSAMSSGVSWGCPPACPGPLISPENLGNRISNVDPRVTPPYCPQIQSPLHQSLERAADSSPWAPPQACPGMQMSPEPRNKTGHWTQSTEPAELTKVYQSLSVSPEPRLSLGSPLLLPRPSCQRLQPQPQPQPQWGCWGHDAEVLSTSEDQGSSPALQLPVASPTPSSGLQLSGCPELWQEDLEGPPLNIFY
null
null
heart morphogenesis [GO:0003007]; mesoderm formation [GO:0001707]; mesodermal cell migration [GO:0008078]; Notch signaling pathway [GO:0007219]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]; signal transduction involved in regulation of gene expression [GO:0023019]; somite rostral/caudal axis specification [GO:0032525]; somitogenesis [GO:0001756]
nucleoplasm [GO:0005654]; 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 dimerization activity [GO:0046983]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
PF00010;
4.10.280.10;
null
PTM: Degraded by the proteasome.; PTM: Phosphorylated. {ECO:0000269|PubMed:16996494}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:15902259, ECO:0000269|PubMed:16996494}.
null
null
null
null
null
FUNCTION: Transcription factor with important role in somitogenesis. Defines the rostrocaudal patterning of the somite by participating in distinct Notch pathways. Regulates also the FGF signaling pathway. Specifies the rostral half of the somites. Generates rostro-caudal polarity of somites by down-regulating in the presumptive rostral domain DLL1, a Notch ligand. Participates in the segment border formation by activating in the anterior presomitic mesoderm LFNG, a negative regulator of DLL1-Notch signaling. Acts as a strong suppressor of Notch activity. Together with MESP1 is involved in the epithelialization of somitic mesoderm and in the development of cardiac mesoderm. May play a role with Tcf15 in the differentiation of myotomal and sclerotomal cells by regulating Pax family genes. Controls also the expression of the protocadherin PCDH8/PAPC, EPHA4, RIPPLY2, NOTCH2, FGFR1, and CER1. Binds to the E-boxes within the EPH4A and RIPPLY2 enhancers. {ECO:0000269|PubMed:10887078, ECO:0000269|PubMed:10932180, ECO:0000269|PubMed:12591245, ECO:0000269|PubMed:12900443, ECO:0000269|PubMed:15677726, ECO:0000269|PubMed:15902259, ECO:0000269|PubMed:16728472, ECO:0000269|PubMed:17306789, ECO:0000269|PubMed:17477400, ECO:0000269|PubMed:9242490}.
Mus musculus (Mouse)
O08575
EYA2_MOUSE
MLEVVTSPSLATSSDWSEHGAAVGTLSDREGIAKSAALSVPQLFVKSHPRVPPGQSSTAMAAYGQTQYSTGIQQAPPYTAYPTPAQAYGIPPYSIKTEDSLNHSPSQSGFLSYGPSFSTAPAGQSPYTYPVHSTAGLYQGANGLTNTAGFGSVHQDYPSYPSFSQNQYPQYFSPSYNPPYVPASSLCSSPLSTSTYVLQEAPHNVPSQSSESLAGDYNTHNGPSTPAKEGDTERPHRASDGKLRGRSKRNSDPSPAGDNEIERVFVWDLDETIIIFHSLLTGTFASRYGKDTTTSVRIGLMMEEMIFNLADTHLFFNDLEDCDQIHVDDVSSDDNGQDLSTYNFSTDGFHSTAPGASLCLGTGVHGGVDWMRKLAFRYRRVKEMYNTYRNNVGGLIGAPKRETWLQLRAELEALTDLWLTHSLKALNLINSRPNCVNVLVTTTQLIPALAKVLLYGLGSVFPIENIYSATKTGKESCFERIMQRFGRKAVYIVIGDGVEEEQGAKKHNMPFWRISCHADLEALRHALELEYL
3.1.3.48
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O00167}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:O00167};
cell differentiation [GO:0030154]; DNA repair [GO:0006281]; extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; mitochondrial outer membrane permeabilization [GO:0097345]; negative regulation of extrinsic apoptotic signaling pathway in absence of ligand [GO:2001240]; positive regulation of DNA repair [GO:0045739]; striated muscle tissue development [GO:0014706]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleus [GO:0005634]
histone H2AXY142 phosphatase activity [GO:0140793]; magnesium ion binding [GO:0000287]; protein tyrosine phosphatase activity [GO:0004725]
PF00702;
3.40.50.12350;
HAD-like hydrolase superfamily, EYA family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10490620}. Nucleus {ECO:0000269|PubMed:10490620}. Note=Retained in the cytoplasm via interaction with GNAZ and GNAI2 (By similarity). Interaction with SIX1, SIX2, SIX4 or SIX5 is required for translocation to the nucleus. {ECO:0000250|UniProtKB:O00167}.
CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000269|PubMed:14628052};
null
null
null
null
FUNCTION: Functions both as protein phosphatase and as transcriptional coactivator for SIX1, and probably also for SIX2, SIX4 and SIX5 (PubMed:10490620, PubMed:17098221). Tyrosine phosphatase that dephosphorylates 'Tyr-142' of histone H2AX (H2AXY142ph) and promotes efficient DNA repair via the recruitment of DNA repair complexes containing MDC1. 'Tyr-142' phosphorylation of histone H2AX plays a central role in DNA repair and acts as a mark that distinguishes between apoptotic and repair responses to genotoxic stress. Its function as histone phosphatase may contribute to its function in transcription regulation during organogenesis (By similarity). Plays an important role in hypaxial muscle development together with SIX1 and DACH2; in this it is functionally redundant with EYA1 (By similarity). {ECO:0000250|UniProtKB:O00167, ECO:0000269|PubMed:10490620, ECO:0000269|PubMed:17098221}.
Mus musculus (Mouse)
O08579
EMD_MOUSE
MDDYAVLSDTELAAVLRQYNIPHGPIVGSTRKLYEKKIFEYETQRRRLLPPNSSSSSFSYQFSDLDSAAVDSDMYDLPKKEDALLYQSKDYNDDYYEESYLTTKTYGEPESVGMSKSFRQPGTSLVDADTFHHQVRDDIFSSLEEEGKDRERLIYGQDSAYQSIAHYRPISNVSRSSLGLSYYPTSSTSSVSSSSSSPSSWLTRRAIRPEKQAPAAALGQDRQVPLWGQLLLFLVFAAFLLFVYYSIQAEEGNPFWMDP
null
null
cellular response to growth factor stimulus [GO:0071363]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of fibroblast proliferation [GO:0048147]; nuclear membrane organization [GO:0071763]; positive regulation of protein export from nucleus [GO:0046827]; skeletal muscle cell differentiation [GO:0035914]
cortical endoplasmic reticulum [GO:0032541]; microtubule [GO:0005874]; nuclear envelope [GO:0005635]; nuclear inner membrane [GO:0005637]; nuclear lamina [GO:0005652]; nuclear membrane [GO:0031965]; nuclear outer membrane [GO:0005640]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spindle [GO:0005819]; spindle pole centrosome [GO:0031616]; TMEM240-body [GO:0160045]
actin binding [GO:0003779]; beta-tubulin binding [GO:0048487]; cadherin binding [GO:0045296]
PF03020;
1.10.720.40;
null
null
SUBCELLULAR LOCATION: Nucleus inner membrane {ECO:0000250|UniProtKB:P50402}; Single-pass membrane protein; Nucleoplasmic side {ECO:0000250|UniProtKB:P50402}. Nucleus outer membrane. Note=Colocalized with BANF1 at the central region of the assembling nuclear rim, near spindle-attachment sites. The accumulation of different intermediates of prelamin-A/C (non-farnesylated or carboxymethylated farnesylated prelamin-A/C) in fibroblasts modify its localization in the nucleus (By similarity). {ECO:0000250}.
null
null
null
null
null
FUNCTION: Stabilizes and promotes the formation of a nuclear actin cortical network. Stimulates actin polymerization in vitro by binding and stabilizing the pointed end of growing filaments. Inhibits beta-catenin activity by preventing its accumulation in the nucleus. Acts by influencing the nuclear accumulation of beta-catenin through a CRM1-dependent export pathway. Links centrosomes to the nuclear envelope via a microtubule association. Required for proper localization of non-farnesylated prelamin-A/C. Together with NEMP1, contributes to nuclear envelope stiffness in germ cells. {ECO:0000250|UniProtKB:P50402}.
Mus musculus (Mouse)
O08580
ERR1_MOUSE
MSSQVVGIEPLYIKAEPASPDSPKGSSETETEPPVTLASGPAPARCLPGHKEEEDGEGAGSGEQGSGKLVLSSLPKRLCLVCGDVASGYHYGVASCEACKAFFKRTIQGSIEYSCPASNECEITKRRRKACQACRFTKCLRVGMLKEGVRLDRVRGGRQKYKRRPEVDPLPFPGPFPAGPLAVAGGPRKTAPVNALVSHLLVVEPEKLYAMPDPASPDGHLPAVATLCDLFDREIVVTISWAKSIPGFSSLSLSDQMSVLQSVWMEVLVLGVAQRSLPLQDELAFAEDLVLDEEGARAAGLGDLGAALLQLVRRLQALRLEREEYVLLKALALANSDSVHIEDAEAVEQLREALHEALLEYEAGRAGPGGGAERRRAGRLLLTLPLLRQTAGKVLAHFYGVKLEGKVPMHKLFLEMLEAMMD
null
null
cartilage development [GO:0051216]; intracellular steroid hormone receptor signaling pathway [GO:0030518]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of cellular response to insulin stimulus [GO:1900078]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of cell population proliferation [GO:0042127]; regulation of DNA-templated transcription [GO:0006355]; regulation of ossification [GO:0030278]; regulation of osteoblast differentiation [GO:0045667]; regulation of osteoclast differentiation [GO:0045670]; regulation of transcription by RNA polymerase II [GO:0006357]
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 repressor activity, RNA polymerase II-specific [GO:0001227]; estrogen response element binding [GO:0034056]; nuclear receptor activity [GO:0004879]; nuclear steroid receptor activity [GO:0003707]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]; steroid binding [GO:0005496]; zinc ion binding [GO:0008270]
PF00104;PF00105;
3.30.50.10;1.10.565.10;
Nuclear hormone receptor family, NR3 subfamily
PTM: Phosphorylation on Ser-19 enhances sumoylation on Lys-14 increasing repression of transcriptional activity. {ECO:0000250}.; PTM: Sumoylated with SUMO2. Main site is Lys-14 which is enhanced by phosphorylation on Ser-19, cofactor activation, and by interaction with PIAS4. Sumoylation enhances repression of transcriptional activity, but has no effect on subcellular location nor on DNA binding (By similarity). {ECO:0000250}.; PTM: Reversibly acetylated. Acetylation by PCAF/KAT2 at Lys-129, Lys-138, Lys-160 and Lys-162 and PCAF/KAT2 decreases transcriptional activity probably by inhibiting DNA-binding activity; deacetylation involves SIRT1 and HDAC8 and increases DNA-binding (By similarity). {ECO:0000250}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P11474, ECO:0000255|PROSITE-ProRule:PRU00407}. Cytoplasm {ECO:0000250|UniProtKB:P11474}. Note=Co-localizes to the cytoplasm only in presence of MAPK15. {ECO:0000250|UniProtKB:P11474}.
null
null
null
null
null
FUNCTION: Binds to an ERR-alpha response element (ERRE) containing a single consensus half-site, 5'-TNAAGGTCA-3'. Can bind to the medium-chain acyl coenzyme A dehydrogenase (MCAD) response element NRRE-1 and may act as an important regulator of MCAD promoter. Binds to the C1 region of the lactoferrin gene promoter. Requires dimerization and the coactivator, PGC-1A, for full activity. The ERRalpha/PGC1alpha complex is a regulator of energy metabolism. Induces the expression of PERM1 in the skeletal muscle (By similarity). {ECO:0000250}.
Mus musculus (Mouse)
O08581
KCNK1_MOUSE
MLQSLAGSSCVRLVERHRSAWCFGFLVLGYLLYLVFGAVVFSSVELPYEDLLRQELRKLKRRFLEEHECLSEPQLEQFLGRVLEASNYGVSVLSNASGNWNWDFTSALFFASTVLSTTGYGHTVPLSDGGKAFCIIYSVIGIPFTLLFLTAVVQRVTVHVTRRPVLYFHIRWGFSKQVVAIVHAVLLGFVTVSCFFFIPAAVFSVLEDDWNFLESFYFCFISLSTIGLGDYVPGEGYNQKFRELYKIGITCYLLLGLIAMLVVLETFCELHELKKFRKMFYVKKDKDEDLVHIMEHDQLSFSSVTEQVAGLKEEQKQSEPFVASQSPPYEDGSADH
null
null
potassium ion transmembrane transport [GO:0071805]; potassium ion transport [GO:0006813]; regulation of resting membrane potential [GO:0060075]; response to nicotine [GO:0035094]; sodium ion transmembrane transport [GO:0035725]; stabilization of membrane potential [GO:0030322]
apical plasma membrane [GO:0016324]; brush border membrane [GO:0031526]; dendrite [GO:0030425]; endosome [GO:0005768]; inward rectifier potassium channel complex [GO:1902937]; membrane [GO:0016020]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; potassium channel complex [GO:0034705]; recycling endosome [GO:0055037]; synaptic membrane [GO:0097060]
identical protein binding [GO:0042802]; inward rectifier potassium channel activity [GO:0005242]; outward rectifier potassium channel activity [GO:0015271]; potassium channel activity [GO:0005267]; potassium ion leak channel activity [GO:0022841]; sodium channel activity [GO:0005272]
PF07885;
1.10.287.70;
Two pore domain potassium channel (TC 1.A.1.8) family
PTM: Sumoylation is controversial. Sumoylated by UBE2I. Not sumoylated when expressed in xenopus oocytes or mammalian cells. Sumoylation inactivates the channel, but does not interfere with expression at the cell membrane. Sumoylation of a single subunit is sufficient to silence the dimeric channel. Sumoylation of KCNK1 is sufficient to silence heterodimeric channels formed by KCNK1 and KCNK3 or KCNK9. Desumoylated by SENP1; this activates the channel. Desumoylated by SENP1; this strongly increases halothane-mediated activation of heterodimeric channels formed with KCNK9. SENP1 treatment has no effect. {ECO:0000250|UniProtKB:O00180}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15540117, ECO:0000269|PubMed:19959478, ECO:0000269|PubMed:24368895, ECO:0000269|PubMed:24496152, ECO:0000269|PubMed:9013852}; Multi-pass membrane protein {ECO:0000305}. Recycling endosome {ECO:0000269|PubMed:15540117}. Apical cell membrane {ECO:0000269|PubMed:12855359, ECO:0000305|PubMed:16025300}. Cytoplasmic vesicle {ECO:0000269|PubMed:16025300, ECO:0000269|PubMed:24368895}. Perikaryon {ECO:0000269|PubMed:12855359, ECO:0000269|PubMed:17079103, ECO:0000269|PubMed:25406588}. Cell projection, dendrite {ECO:0000269|PubMed:25406588}. Cell projection {ECO:0000269|PubMed:17079103}. Synaptic cell membrane {ECO:0000250|UniProtKB:Q9Z2T2}. Note=The heterodimer with KCNK2 is detected at the astrocyte cell membrane (PubMed:24496152). Not detected at the astrocyte cell membrane when KCNK2 is absent (PubMed:24496152). Detected on neuronal cell bodies, and to a lesser degree on neuronal cell projections (PubMed:12855359, PubMed:17079103). Detected on hippocampus dentate gyrus granule cell bodies and to a lesser degree on proximal dendrites (PubMed:25406588). Detected at the apical cell membrane in stria vascularis in the cochlea (By similarity). Detected at the apical cell membrane of vestibular dark cells situated between the crista and the utricle in the inner ear (PubMed:12855359). Detected at the apical cell membrane in stria vascularis in the cochlea (PubMed:12855359). Detected at the apical cell membrane in kidney proximal tubule segment S1 and in subapical compartments in segments S1, S2 and S3 (PubMed:16025300). Predominantly in cytoplasmic structures in kidney distal convoluted tubules and collecting ducts (PubMed:16025300). Predominantly in cytoplasmic structures in hippocampus astrocytes; only a minor proportion of the protein is present at the cell membrane (PubMed:24368895). {ECO:0000250|UniProtKB:Q9Z2T2, ECO:0000269|PubMed:16025300, ECO:0000269|PubMed:17079103, ECO:0000269|PubMed:24368895, ECO:0000269|PubMed:24496152, ECO:0000269|PubMed:25406588}.
null
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Note=Both activation and channel closure are very rapid. Is not voltage-gated (PubMed:22431633, PubMed:24496152). The relationship between voltage and current is nearly linear (PubMed:22431633, PubMed:24496152). {ECO:0000269|PubMed:22431633, ECO:0000269|PubMed:24496152, ECO:0000305};
null
null
null
FUNCTION: Ion channel that contributes to passive transmembrane potassium transport and to the regulation of the resting membrane potential in brain astrocytes, but also in kidney and in other tissues (PubMed:16847696, PubMed:22431633, PubMed:24368895). Forms dimeric channels through which potassium ions pass in accordance with their electrochemical gradient. The channel is selective for K(+) ions at physiological potassium concentrations and at neutral pH, but becomes permeable to Na(+) at subphysiological K(+) levels and upon acidification of the extracellular medium. The homodimer has very low potassium channel activity, when expressed in heterologous systems, and can function as weakly inward rectifying potassium channel (PubMed:24496152, PubMed:9013852). Channel activity is modulated by activation of serotonin receptors (PubMed:24368895). Heterodimeric channels containing KCNK1 and KCNK2 have much higher activity, and may represent the predominant form in astrocytes (PubMed:24496152). Heterodimeric channels containing KCNK1 and KCNK3 or KCNK9 have much higher activity. Heterodimeric channels formed by KCNK1 and KCNK9 may contribute to halothane-sensitive currents (By similarity). Mediates outward rectifying potassium currents in dentate gyrus granule cells and contributes to the regulation of their resting membrane potential (PubMed:25406588). Contributes to the regulation of action potential firing in dentate gyrus granule cells and down-regulates their intrinsic excitability (PubMed:25406588). In astrocytes, the heterodimer formed by KCNK1 and KCNK2 is required for rapid glutamate release in response to activation of G-protein coupled receptors, such as F2R and CNR1 (PubMed:24496152). Required for normal ion and water transport in the kidney (PubMed:16025300). Contributes to the regulation of the resting membrane potential of pancreatic beta cells (PubMed:22431633). The low channel activity of homodimeric KCNK1 may be due to sumoylation. The low channel activity may be due to rapid internalization from the cell membrane and retention in recycling endosomes (PubMed:15540117). {ECO:0000250|UniProtKB:O00180, ECO:0000250|UniProtKB:Q9Z2T2, ECO:0000269|PubMed:15540117, ECO:0000269|PubMed:16025300, ECO:0000269|PubMed:16847696, ECO:0000269|PubMed:22431633, ECO:0000269|PubMed:24368895, ECO:0000269|PubMed:24496152, ECO:0000269|PubMed:9013852}.
Mus musculus (Mouse)
O08583
THOC4_MOUSE
MADKMDMSLDDIIKLNRSQRGGRGGGRGRGRAGSQGGRGGAVQAAARVNRGGGPMRNRPAIARGAAGGGRNRPAPYSRPKQLPDKWQHDLFDSGFGGGAGVETGGKLLVSNLDFGVSDADIQELFAEFGTLKKAAVHYDRSGRSLGTADVHFERKADALKAMKQYNGVPLDGRPMNIQLVTSQIDTQRRPAQSINRGGMTRNRGSGGFGGGGTRRGTRGGSRGRGRGTGRNSKQQLSAEELDAQLDAYNARMDTS
null
null
mRNA export from nucleus [GO:0006406]; mRNA processing [GO:0006397]; RNA export from nucleus [GO:0006405]; RNA splicing [GO:0008380]
cytoplasm [GO:0005737]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; spliceosomal complex [GO:0005681]
C5-methylcytidine-containing RNA reader activity [GO:0062153]; molecular adaptor activity [GO:0060090]; mRNA binding [GO:0003729]; RNA binding [GO:0003723]; RNA folding chaperone [GO:0140691]; single-stranded DNA binding [GO:0003697]
PF13865;PF00076;
3.30.70.330;
THOC4 family
PTM: Arg-50 and Arg-203 are dimethylated, probably to asymmetric dimethylarginine. Arginine methylation reduces RNA binding (By similarity). {ECO:0000250}.; PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9119228}. Nucleus speckle {ECO:0000250|UniProtKB:Q86V81}. Cytoplasm {ECO:0000269|PubMed:9119228}. Note=Colocalizes with the core EJC, ALYREF/THOC4, NXF1 and DDX39B in the nucleus and nuclear speckles. Localizes to regions surrounding nuclear speckles known as perispeckles in which TREX complex assembly seems to occur. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. {ECO:0000250|UniProtKB:Q86V81}.
null
null
null
null
null
FUNCTION: Export adapter involved in nuclear export of spliced and unspliced mRNA. Binds mRNA which is thought to be transferred to the NXF1-NXT1 heterodimer for export (TAP/NFX1 pathway) (PubMed:10786854, PubMed:11158589, PubMed:9119228). Component of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and specifically associates with spliced mRNA and not with unspliced pre-mRNA. TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm. TREX recruitment occurs via an interaction between ALYREF/THOC4 and the cap-binding protein NCBP1. The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production; ALYREF/THOC4 mediates the recruitment of the TREX complex to the intronless viral mRNA. Required for TREX complex assembly and for linking DDX39B to the cap-binding complex (CBC). In conjunction with THOC5 functions in NXF1-NXT1 mediated nuclear export of HSP70 mRNA; both proteins enhance the RNA binding activity of NXF1 and are required for NXF1 localization to the nuclear rim. Involved in the nuclear export of intronless mRNA; proposed to be recruited to intronless mRNA by ATP-bound DDX39B. Involved in transcription elongation and genome stability. Involved in mRNA export of C5-methylcytosine (m5C)-containing mRNAs: specifically recognizes and binds m5C mRNAs and mediates their nucleo-cytoplasmic shuttling (By similarity). {ECO:0000250|UniProtKB:Q86V81, ECO:0000269|PubMed:10786854, ECO:0000269|PubMed:11158589, ECO:0000269|PubMed:9119228}.; FUNCTION: Acts as a chaperone and promotes the dimerization of transcription factors containing basic leucine zipper (bZIP) domains and thereby promotes transcriptional activation. {ECO:0000250|UniProtKB:Q86V81}.
Mus musculus (Mouse)
O08584
KLF6_MOUSE
MDVLPMCSIFQELQIVHETGYFSALPSLEEYWQQTCLELERYLQSEPCYVSASEIKFDSQEDLWTKFILAREKKEESELKISSSPPEDSLISSSFNYNLETNSLNSDVSSESSDSSEELSPTTKFTSDPIGEVLVNSGNLSSSVISTPPSSPEVNRESSQLWGCGPGDLPSPGKVRSGTSGKSGDKGNGDASPDGRRRVHRCHFNGCRKVYTKSSHLKAHQRTHTGEKPYRCSWEGCEWRFARSDELTRHFRKHTGAKPFKCSHCDRCFSRSDHLALHMKRHL
null
null
cytokine-mediated signaling pathway [GO:0019221]; positive regulation of connective tissue replacement [GO:1905205]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]
cytoplasm [GO:0005737]; nucleus [GO:0005634]
DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; double-stranded DNA binding [GO:0003690]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
PF00096;
3.30.160.60;
Krueppel C2H2-type zinc-finger protein family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
null
null
null
null
null
FUNCTION: Transcriptional activator. Binds a GC box motif. Could play a role in B-cell growth and development (By similarity). {ECO:0000250}.
Mus musculus (Mouse)
O08585
CLCA_MOUSE
MAELDPFGAPAGAPGGPALGNGVAGAGEEDPAAAFLAQQESEIAGIENDEAFAILDGGAPGRATRRAAGGPDAVDGVMNGEYYQESNGPTDSYAAISEVDRLQSEPESIRKWREEQTERLEALDANSRKQEAEWKEKAIKELEEWYARQDEQLQKTKANNRVADEAFYKQPFADLIGYVAAEEAFVNDIDESSPGTEWERVARLCDFNPKSSKQAKDVSRMRSVLISLKQAPLVH
null
null
cell cycle [GO:0007049]; cell division [GO:0051301]; clathrin-dependent endocytosis [GO:0072583]; intracellular protein transport [GO:0006886]
clathrin coat [GO:0030118]; clathrin coat of coated pit [GO:0030132]; clathrin coat of trans-Golgi network vesicle [GO:0030130]; clathrin vesicle coat [GO:0030125]; clathrin-coated pit [GO:0005905]; clathrin-coated vesicle [GO:0030136]; cytoplasmic vesicle [GO:0031410]; glutamatergic synapse [GO:0098978]; plasma membrane [GO:0005886]; postsynaptic endocytic zone [GO:0098843]; postsynaptic endocytic zone cytoplasmic component [GO:0099631]; presynaptic endocytic zone membrane [GO:0098835]; spindle [GO:0005819]; synaptic vesicle membrane [GO:0030672]
clathrin heavy chain binding [GO:0032050]; GTPase binding [GO:0051020]; peptide binding [GO:0042277]; protein-containing complex binding [GO:0044877]; structural molecule activity [GO:0005198]
PF01086;
null
Clathrin light chain family
null
SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Membrane, coated pit; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P09496}. Note=Cytoplasmic face of coated pits and vesicles.In complex with TACC3 and CKAP5 (forming the TACC3/ch-TOG/clathrin complex) localized to inter-microtubule bridges in mitotic spindles. {ECO:0000250|UniProtKB:P09496}.
null
null
null
null
null
FUNCTION: Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. Acts as a component of the TACC3/ch-TOG/clathrin complex proposed to contribute to stabilization of kinetochore fibers of the mitotic spindle by acting as inter-microtubule bridge (By similarity). {ECO:0000250|UniProtKB:P09496}.
Mus musculus (Mouse)
O08586
PTEN_MOUSE
MTAIIKEIVSRNKRRYQEDGFDLDLTYIYPNIIAMGFPAERLEGVYRNNIDDVVRFLDSKHKNHYKIYNLCAERHYDTAKFNCRVAQYPFEDHNPPQLELIKPFCEDLDQWLSEDDNHVAAIHCKAGKGRTGVMICAYLLHRGKFLKAQEALDFYGEVRTRDKKGVTIPSQRRYVYYYSYLLKNHLDYRPVALLFHKMMFETIPMFSGGTCNPQFVVCQLKVKIYSSNSGPTRREDKFMYFEFPQPLPVCGDIKVEFFHKQNKMLKKDKMFHFWVNTFFIPGPEETSEKVENGSLCDQEIDSICSIERADNDKEYLVLTLTKNDLDKANKDKANRYFSPNFKVKLYFTKTVEEPSNPEASSSTSVTPDVSDNEPDHYRYSDTTDSDPENEPFDEDQHSQITKV
3.1.3.-; 3.1.3.16; 3.1.3.48; 3.1.3.67
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
adult behavior [GO:0030534]; angiogenesis [GO:0001525]; apoptotic process [GO:0006915]; B cell proliferation [GO:0042100]; brain morphogenesis [GO:0048854]; cardiac muscle tissue development [GO:0048738]; cell migration [GO:0016477]; cell motility [GO:0048870]; cell population proliferation [GO:0008283]; cellular response to decreased oxygen levels [GO:0036294]; cellular response to ethanol [GO:0071361]; cellular response to hypoxia [GO:0071456]; cellular response to insulin stimulus [GO:0032869]; cellular response to insulin-like growth factor stimulus [GO:1990314]; cellular response to leptin stimulus [GO:0044320]; central nervous system development [GO:0007417]; central nervous system myelin maintenance [GO:0032286]; central nervous system neuron axonogenesis [GO:0021955]; dendritic spine morphogenesis [GO:0060997]; dentate gyrus development [GO:0021542]; endothelial cell migration [GO:0043542]; forebrain morphogenesis [GO:0048853]; gene expression [GO:0010467]; heart development [GO:0007507]; inositol phosphate catabolic process [GO:0071545]; learning or memory [GO:0007611]; locomotor rhythm [GO:0045475]; locomotory behavior [GO:0007626]; long-term synaptic depression [GO:0060292]; long-term synaptic potentiation [GO:0060291]; male mating behavior [GO:0060179]; maternal behavior [GO:0042711]; memory [GO:0007613]; multicellular organismal response to stress [GO:0033555]; myelination [GO:0042552]; negative regulation of apoptotic process [GO:0043066]; negative regulation of axon regeneration [GO:0048681]; negative regulation of axonogenesis [GO:0050771]; negative regulation of B cell proliferation [GO:0030889]; negative regulation of cardiac muscle cell proliferation [GO:0060044]; negative regulation of cell cycle [GO:0045786]; negative regulation of cell migration [GO:0030336]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of cell size [GO:0045792]; negative regulation of cellular senescence [GO:2000773]; negative regulation of defense response to bacterium [GO:1900425]; negative regulation of dendrite extension [GO:1903860]; negative regulation of dendritic spine morphogenesis [GO:0061002]; negative regulation of epithelial cell proliferation [GO:0050680]; negative regulation of excitatory postsynaptic potential [GO:0090394]; negative regulation of Fc-gamma receptor signaling pathway involved in phagocytosis [GO:1905450]; negative regulation of focal adhesion assembly [GO:0051895]; negative regulation of myelination [GO:0031642]; negative regulation of neuron projection development [GO:0010977]; negative regulation of organ growth [GO:0046621]; negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051898]; negative regulation of protein phosphorylation [GO:0001933]; negative regulation of ribosome biogenesis [GO:0090071]; negative regulation of synaptic vesicle clustering [GO:2000808]; negative regulation of T cell proliferation [GO:0042130]; neuron projection development [GO:0031175]; neuron-neuron synaptic transmission [GO:0007270]; phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0043491]; phosphatidylinositol dephosphorylation [GO:0046856]; platelet-derived growth factor receptor signaling pathway [GO:0048008]; positive regulation of apoptotic process [GO:0043065]; positive regulation of apoptotic signaling pathway [GO:2001235]; positive regulation of cardiac muscle cell apoptotic process [GO:0010666]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of excitatory postsynaptic potential [GO:2000463]; positive regulation of gene expression [GO:0010628]; positive regulation of interleukin-6 production [GO:0032755]; positive regulation of neuron differentiation [GO:0045666]; positive regulation of tumor necrosis factor production [GO:0032760]; positive regulation of ubiquitin protein ligase activity [GO:1904668]; postsynaptic density assembly [GO:0097107]; prepulse inhibition [GO:0060134]; presynaptic membrane assembly [GO:0097105]; prostate gland growth [GO:0060736]; protein dephosphorylation [GO:0006470]; regulation of axon regeneration [GO:0048679]; regulation of B cell apoptotic process [GO:0002902]; regulation of cell cycle [GO:0051726]; regulation of cellular component size [GO:0032535]; regulation of cellular localization [GO:0060341]; regulation of macrophage apoptotic process [GO:2000109]; regulation of neuron projection development [GO:0010975]; regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051896]; regulation of protein stability [GO:0031647]; regulation of synaptic transmission, GABAergic [GO:0032228]; rhythmic synaptic transmission [GO:0060024]; social behavior [GO:0035176]; synapse assembly [GO:0007416]; synapse maturation [GO:0060074]; T cell proliferation [GO:0042098]
cell projection [GO:0042995]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendritic spine [GO:0043197]; myelin sheath adaxonal region [GO:0035749]; neuron projection [GO:0043005]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; PML body [GO:0016605]; postsynaptic cytosol [GO:0099524]; postsynaptic density [GO:0014069]; postsynaptic membrane [GO:0045211]; Schmidt-Lanterman incisure [GO:0043220]
inositol-1,3,4,5,6-pentakisphosphate 3-phosphatase activity [GO:0030351]; inositol-1,3,4,5-tetrakisphosphate 3-phosphatase activity [GO:0051717]; ionotropic glutamate receptor binding [GO:0035255]; myosin phosphatase activity [GO:0017018]; PDZ domain binding [GO:0030165]; phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase activity [GO:0016314]; phosphatidylinositol-3,4-bisphosphate 3-phosphatase activity [GO:0051800]; phosphatidylinositol-3-phosphate phosphatase activity [GO:0004438]; platelet-derived growth factor receptor binding [GO:0005161]; protein kinase binding [GO:0019901]; protein serine/threonine phosphatase activity [GO:0004722]; protein tyrosine kinase binding [GO:1990782]; protein tyrosine phosphatase activity [GO:0004725]; ubiquitin-specific protease binding [GO:1990381]
PF10409;PF00102;
2.60.40.1110;3.90.190.10;
PTEN phosphatase protein family
PTM: Constitutively phosphorylated by CK2 under normal conditions. Phosphorylation results in an inhibited activity towards PIP3. Phosphorylation can both inhibit or promote PDZ-binding. Phosphorylation at Tyr-336 by FRK/PTK5 protects this protein from ubiquitin-mediated degradation probably by inhibiting its binding to NEDD4 (By similarity). Phosphorylation by PLK3 promotes its stability and prevents its degradation by the proteasome. Phosphorylation by ROCK1 is essential for its stability and activity. Phosphorylated on Thr-319 and Thr-321 in the C2-type tensin domain following EGF stimulation which changes its binding preference from the p85 regulatory subunit of the PI3K kinase complex to DLC1 (By similarity). {ECO:0000250|UniProtKB:P60484, ECO:0000269|PubMed:19473982, ECO:0000269|PubMed:20008297, ECO:0000269|PubMed:20940307}.; PTM: Monoubiquitinated; monoubiquitination is increased in presence of retinoic acid. Deubiquitinated by USP7; leading to its nuclear exclusion. Monoubiquitination of one of either Lys-13 and Lys-289 amino acid is sufficient to modulate PTEN compartmentalization (By similarity). Ubiquitinated by XIAP/BIRC4. {ECO:0000250, ECO:0000269|PubMed:19473982}.; PTM: Ubiquitinated by the DCX(DCAF13) E3 ubiquitin ligase complex, leading to its degradation. {ECO:0000269|PubMed:31492966}.; PTM: ISGylated. ISGylation promotes PTEN degradation. {ECO:0000250|UniProtKB:P60484}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19473982, ECO:0000269|PubMed:25801959}. Nucleus {ECO:0000269|PubMed:19473982, ECO:0000269|PubMed:25801959}. Nucleus, PML body {ECO:0000250|UniProtKB:P60484}. Cell projection, dendritic spine {ECO:0000269|PubMed:33428810}. Postsynaptic density {ECO:0000250|UniProtKB:O54857}. Note=Monoubiquitinated form is nuclear (By similarity). Nonubiquitinated form is cytoplasmic (By similarity). Colocalized with PML and USP7 in PML nuclear bodies (By similarity). XIAP/BIRC4 promotes its nuclear localization (PubMed:19473982). Associares with the postsynaptic density in response to NMDAR activation (By similarity). {ECO:0000250|UniProtKB:O54857, ECO:0000250|UniProtKB:P60484, ECO:0000269|PubMed:19473982}.
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-trisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + phosphate; Xref=Rhea:RHEA:25017, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57836, ChEBI:CHEBI:58456; EC=3.1.3.67; Evidence={ECO:0000250|UniProtKB:P60484}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25018; Evidence={ECO:0000250|UniProtKB:P60484}; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; Evidence={ECO:0000250|UniProtKB:P60484}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20630; Evidence={ECO:0000250|UniProtKB:P60484}; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; Evidence={ECO:0000250|UniProtKB:P60484}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47005; Evidence={ECO:0000250|UniProtKB:P60484}; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000250|UniProtKB:P60484}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10685; Evidence={ECO:0000250|UniProtKB:P60484}; CATALYTIC ACTIVITY: Reaction=1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-trisphosphate) + H2O = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + phosphate; Xref=Rhea:RHEA:43552, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:83416, ChEBI:CHEBI:83419; Evidence={ECO:0000250|UniProtKB:P60484}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43553; Evidence={ECO:0000250|UniProtKB:P60484}; CATALYTIC ACTIVITY: Reaction=1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-trisphosphate) + H2O = 1,2-dihexadecanoyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + phosphate; Xref=Rhea:RHEA:43560, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:83420, ChEBI:CHEBI:83423; Evidence={ECO:0000250|UniProtKB:P60484}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43561; Evidence={ECO:0000250|UniProtKB:P60484}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,3,4,5,6-pentakisphosphate + H2O = 1D-myo-inositol 1,4,5,6-tetrakisphosphate + phosphate; Xref=Rhea:RHEA:77143, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57627, ChEBI:CHEBI:57733; Evidence={ECO:0000250|UniProtKB:P60484}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77144; Evidence={ECO:0000250|UniProtKB:P60484}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + phosphate; Xref=Rhea:RHEA:77155, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57895, ChEBI:CHEBI:203600; Evidence={ECO:0000250|UniProtKB:P60484}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77156; Evidence={ECO:0000250|UniProtKB:P60484};
null
null
null
null
FUNCTION: Dual-specificity protein phosphatase, dephosphorylating tyrosine-, serine- and threonine-phosphorylated proteins. Also functions as a lipid phosphatase, removing the phosphate in the D3 position of the inositol ring of PtdIns(3,4,5)P3/phosphatidylinositol 3,4,5-trisphosphate, PtdIns(3,4)P2/phosphatidylinositol 3,4-diphosphate and PtdIns3P/phosphatidylinositol 3-phosphate with a preference for PtdIns(3,4,5)P3. Furthermore, this enzyme can also act as a cytosolic inositol 3-phosphatase acting on Ins(1,3,4,5,6)P5/inositol 1,3,4,5,6 pentakisphosphate and possibly Ins(1,3,4,5)P4/1D-myo-inositol 1,3,4,5-tetrakisphosphate (By similarity). Antagonizes the PI3K-AKT/PKB signaling pathway by dephosphorylating phosphoinositides and thereby modulating cell cycle progression and cell survival (PubMed:10339565, PubMed:19778506, PubMed:31492966). The unphosphorylated form cooperates with MAGI2 to suppress AKT1 activation. In motile cells, suppresses the formation of lateral pseudopods and thereby promotes cell polarization and directed movement. Dephosphorylates tyrosine-phosphorylated focal adhesion kinase and inhibits cell migration and integrin-mediated cell spreading and focal adhesion formation (By similarity). Required for growth factor-induced epithelial cell migration; growth factor stimulation induces PTEN phosphorylation which changes its binding preference from the p85 regulatory subunit of the PI3K kinase complex to DLC1 and results in translocation of the PTEN-DLC1 complex to the posterior of migrating cells to promote RHOA activation (By similarity). Meanwhile, TNS3 switches binding preference from DLC1 to p85 and the TNS3-p85 complex translocates to the leading edge of migrating cells to activate RAC1 activation (By similarity). Plays a role as a key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation (PubMed:10339565, PubMed:19778506). Involved in the regulation of synaptic function in excitatory hippocampal synapses. Recruited to the postsynaptic membrane upon NMDA receptor activation, is required for the modulation of synaptic activity during plasticity. Enhancement of lipid phosphatase activity is able to drive depression of AMPA receptor-mediated synaptic responses, activity required for NMDA receptor-dependent long-term depression (LTD) (By similarity). May be a negative regulator of insulin signaling and glucose metabolism in adipose tissue. The nuclear monoubiquitinated form possesses greater apoptotic potential, whereas the cytoplasmic nonubiquitinated form induces less tumor suppressive ability (By similarity). {ECO:0000250|UniProtKB:O54857, ECO:0000250|UniProtKB:P60484, ECO:0000269|PubMed:10339565, ECO:0000269|PubMed:19778506, ECO:0000269|PubMed:31492966}.
Mus musculus (Mouse)
O08589
PLM_RAT
MASPGHILIVCVCLLSMASAEAPQEPDPFTYDYHTLRIGGLTIAGILFILGILIILSKRCRCKFNQQQRTGEPDEEEGTFRSSIRRLSTRRR
null
null
negative regulation of protein glutathionylation [GO:0010734]; positive regulation of inorganic anion transmembrane transport [GO:1903797]; positive regulation of organic acid transport [GO:0032892]; positive regulation of sodium ion export across plasma membrane [GO:1903278]; potassium ion transport [GO:0006813]; regulation of cardiac muscle cell contraction [GO:0086004]; regulation of cardiac muscle cell membrane potential [GO:0086036]; regulation of cytosolic calcium ion concentration [GO:0051480]; sodium ion transport [GO:0006814]
apical plasma membrane [GO:0016324]; caveola [GO:0005901]; intercalated disc [GO:0014704]; sarcolemma [GO:0042383]; sodium:potassium-exchanging ATPase complex [GO:0005890]; T-tubule [GO:0030315]
ATPase binding [GO:0051117]; myosin binding [GO:0017022]; sodium channel regulator activity [GO:0017080]
PF02038;
1.20.5.780;
FXYD family
PTM: Major plasma membrane substrate for cAMP-dependent protein kinase (PKA) and protein kinase C (PKC) in several different tissues (By similarity). Phosphorylated in response to insulin and adrenergic stimulation (By similarity). Phosphorylation at Ser-88 stimulates sodium/potassium-transporting ATPase activity while the unphosphorylated form inhibits sodium/potassium-transporting ATPase activity (PubMed:17283221). Phosphorylation increases tetramerization, decreases binding to ATP1A1 and reduces inhibition of ATP1A1 activity (By similarity). Phosphorylation at Ser-83 leads to greatly reduced interaction with ATP1A1, ATP1A2 and ATP1A3 (PubMed:23532852). May be phosphorylated by DMPK (By similarity). {ECO:0000250|UniProtKB:O00168, ECO:0000250|UniProtKB:P56513, ECO:0000269|PubMed:17283221, ECO:0000269|PubMed:23532852}.; PTM: Palmitoylation increases half-life and stability and is enhanced upon phosphorylation at Ser-88 by PKA. {ECO:0000250|UniProtKB:O00168}.
SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000269|PubMed:23532852}; Single-pass type I membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:12657675}; Single-pass type I membrane protein {ECO:0000255}. Membrane, caveola {ECO:0000269|PubMed:23532852}. Cell membrane, sarcolemma, T-tubule {ECO:0000269|PubMed:23532852}. Note=Detected in the apical cell membrane in brain (PubMed:12657675). In myocytes, localizes to sarcolemma, t-tubules and intercalated disks (PubMed:23532852). {ECO:0000269|PubMed:12657675, ECO:0000269|PubMed:23532852}.
null
null
null
null
null
FUNCTION: Associates with and regulates the activity of the sodium/potassium-transporting ATPase (NKA) which transports Na(+) out of the cell and K(+) into the cell (By similarity). Inhibits NKA activity in its unphosphorylated state and stimulates activity when phosphorylated (PubMed:17283221). Reduces glutathionylation of the NKA beta-1 subunit ATP1B1, thus reversing glutathionylation-mediated inhibition of ATP1B1 (By similarity). Contributes to female sexual development by maintaining the excitability of neurons which secrete gonadotropin-releasing hormone (By similarity). {ECO:0000250|UniProtKB:P56513, ECO:0000250|UniProtKB:Q9Z239, ECO:0000269|PubMed:17283221}.
Rattus norvegicus (Rat)
O08590
AOC3_RAT
MTQKTTLVLLALAVITIFALVCVLLAGRSGDGGRLSQPLHCPSVLPSVQPQTHPGQSQPFADLSPEELTAVMSFLIKHLGPGLVDAAQARPSDNCVFSVELQLPAKAAALAHLDRGGPPPVREALAIIFFGGQPKPNVSELVVGPLPHPSYMRDVTVERHGGPLPYYRRPVLTREYQDIQEMIFHRELPQASGLLHHCCFYKRQGHNLLKMTTAPRGLQSGDRATWFGIYYNLSGAGFYPHPIGLELLVDHKALDPALWTIQKVFYQGRYYESLTQLEDMFEAGLVNVVLVPDNGTGGSWSLKSSVPPGRAPPLQFHPEGPRFSVQGSQVRSSLWAFSFGLGAFSGPRIFDIRFQGERVAYEISVQEAIALYGGNSPASMSTCYMDGSFGIGKYSTPLTRGVDCPYLATYVDWHFLLESQTPKTLRDAFCVFEQNQGLPLRRHHSDFYSHYFGGVVETVLVVRSVATLLNYDYVWDMVFHSNGAIEVKFHATGYITSAFFFGAGEKFGNRVAEHTLGTVHTHNAHFKVDLDVAGLKNWAWAEDLAFVPMNVPWQPEFQMQRLQVTRKLLETEEEAAFPLGNATPRYLYLASNHSNKWGHRRGYRIQILSFAGKPLPQESPIEKAFTWGRYHLAVTQRKEEEPSSSSIYNQNDPWTPTVDFTDFISNETIAGEDLVAWVTAGFLHIPHAEDIPNTVTVGNGVGFFLRPYNFFDEDPSFYSPDSIYFRKDQDVTDCEVNSLACLSQTANCVPDLPAFSHGGFTYK
1.4.3.21
COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000250|UniProtKB:Q16853}; Note=Binds 1 copper ion per subunit. {ECO:0000250|UniProtKB:Q16853}; COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:Q16853}; Note=Binds 2 calcium ions per subunit. {ECO:0000250|UniProtKB:Q16853}; COFACTOR: Name=L-topaquinone; Xref=ChEBI:CHEBI:79027; Evidence={ECO:0000250|UniProtKB:Q16853}; Note=Contains 1 topaquinone per subunit. {ECO:0000250|UniProtKB:Q16853};
amine metabolic process [GO:0009308]; cell adhesion [GO:0007155]; eating behavior [GO:0042755]; leukocyte migration involved in inflammatory response [GO:0002523]; positive regulation of acute inflammatory response [GO:0002675]; positive regulation of glucose transmembrane transport [GO:0010828]; positive regulation of leukocyte migration [GO:0002687]; regulation of blood pressure [GO:0008217]; response to antibiotic [GO:0046677]; response to immobilization stress [GO:0035902]
cell surface [GO:0009986]; cytoplasm [GO:0005737]; early endosome [GO:0005769]; endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; microvillus [GO:0005902]; plasma membrane [GO:0005886]
aliphatic amine oxidase activity [GO:0052595]; calcium ion binding [GO:0005509]; copper ion binding [GO:0005507]; identical protein binding [GO:0042802]; primary amine oxidase activity [GO:0008131]; protein heterodimerization activity [GO:0046982]; quinone binding [GO:0048038]
PF01179;PF02727;PF02728;
3.10.450.40;2.70.98.20;
Copper/topaquinone oxidase family
PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue. {ECO:0000250|UniProtKB:Q16853}.; PTM: N- and O-glycosylated. {ECO:0000250|UniProtKB:Q16853}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8520629, ECO:0000269|PubMed:9083076}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q16853}.
CATALYTIC ACTIVITY: Reaction=H2O + methylamine + O2 = formaldehyde + H2O2 + NH4(+); Xref=Rhea:RHEA:59420, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16842, ChEBI:CHEBI:28938, ChEBI:CHEBI:59338; Evidence={ECO:0000250|UniProtKB:Q16853}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59421; Evidence={ECO:0000250|UniProtKB:Q16853}; CATALYTIC ACTIVITY: Reaction=benzylamine + H2O + O2 = benzaldehyde + H2O2 + NH4(+); Xref=Rhea:RHEA:59424, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17169, ChEBI:CHEBI:28938, ChEBI:CHEBI:225238; Evidence={ECO:0000269|PubMed:15744061}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59425; Evidence={ECO:0000250|UniProtKB:Q16853}; CATALYTIC ACTIVITY: Reaction=2-phenylethylamine + H2O + O2 = 2-phenylacetaldehyde + H2O2 + NH4(+); Xref=Rhea:RHEA:25265, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16424, ChEBI:CHEBI:28938, ChEBI:CHEBI:225237; EC=1.4.3.21; Evidence={ECO:0000250|UniProtKB:Q16853}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25266; Evidence={ECO:0000250|UniProtKB:Q16853};
null
null
null
null
FUNCTION: Catalyzes the oxidative deamination of primary amines to the corresponding aldehydes with the concomitant production of hydrogen peroxide and ammonia. Has a preference for the primary monoamines methylamine and benzylamine (PubMed:15744061). Could also act on 2-phenylethylamine but much less efficiently. At endothelial cells surface can also function as a cell adhesion protein that participates in lymphocyte extravasation and recirculation by mediating the binding of lymphocytes to peripheral lymph node vascular endothelial cells in an L-selectin-independent fashion (By similarity). {ECO:0000250|UniProtKB:Q16853, ECO:0000269|PubMed:15744061}.
Rattus norvegicus (Rat)
O08599
STXB1_MOUSE
MAPIGLKAVVGEKIMHDVIKKVKKKGEWKVLVVDQLSMRMLSSCCKMTDIMTEGITIVEDINKRREPLPSLEAVYLITPSEKSVHSLISDFKDPPTAKYRAAHVFFTDSCPDALFNELVKSRAAKVIKTLTEINIAFLPYESQVYSLDSADSFQSFYSPHKAQMKNPILERLAEQIATLCATLKEYPAVRYRGEYKDNALLAQLIQDKLDAYKADDPTMGEGPDKARSQLLILDRGFDPSSPVLHELTFQAMSYDLLPIENDVYKYETSGIGEARVKEVLLDEDDDLWIALRHKHIAEVSQEVTRSLKDFSSSKRMNTGEKTTMRDLSQMLKKMPQYQKELSKYSTHLHLAEDCMKHYQGTVDKLCRVEQDLAMGTDAEGEKIKDPMRAIVPILLDANVSTYDKIRIILLYIFLKNGITEENLNKLIQHAQIPPEDSEIITNMAHLGVPIVTDSTLRRRSKPERKERISEQTYQLSRWTPIIKDIMEDTIEDKLDTKHYPYISTRSSASFSTTAVSARYGHWHKNKAPGEYRSGPRLIIFILGGVSLNEMRCAYEVTQANGKWEVLIGSTHILTPQKLLDTLKKLNKTDEEISS
null
null
axon target recognition [GO:0007412]; cellular response to type II interferon [GO:0071346]; developmental process involved in reproduction [GO:0003006]; establishment of localization in cell [GO:0051649]; exocytosis [GO:0006887]; intracellular protein transport [GO:0006886]; long-term synaptic depression [GO:0060292]; negative regulation of neuron apoptotic process [GO:0043524]; negative regulation of protein-containing complex assembly [GO:0031333]; negative regulation of synaptic transmission, GABAergic [GO:0032229]; neuromuscular synaptic transmission [GO:0007274]; neuron apoptotic process [GO:0051402]; neurotransmitter secretion [GO:0007269]; platelet aggregation [GO:0070527]; platelet degranulation [GO:0002576]; positive regulation of calcium ion-dependent exocytosis [GO:0045956]; positive regulation of exocytosis [GO:0045921]; positive regulation of glutamate secretion, neurotransmission [GO:1903296]; positive regulation of mast cell degranulation [GO:0043306]; positive regulation of vesicle docking [GO:0106022]; presynaptic dense core vesicle exocytosis [GO:0099525]; protein localization to plasma membrane [GO:0072659]; protein stabilization [GO:0050821]; regulation of acrosomal vesicle exocytosis [GO:2000367]; regulation of synaptic vesicle priming [GO:0010807]; regulation of vesicle fusion [GO:0031338]; response to estradiol [GO:0032355]; SNARE complex assembly [GO:0035493]; synaptic vesicle fusion to presynaptic active zone membrane [GO:0031629]; synaptic vesicle maturation [GO:0016188]; synaptic vesicle priming [GO:0016082]; vesicle docking involved in exocytosis [GO:0006904]; vesicle-mediated transport [GO:0016192]
axon [GO:0030424]; cytoplasm [GO:0005737]; extrinsic component of presynaptic active zone membrane [GO:0098891]; extrinsic component of presynaptic membrane [GO:0098888]; glutamatergic synapse [GO:0098978]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209]; nucleoplasm [GO:0005654]; parallel fiber to Purkinje cell synapse [GO:0098688]; perinuclear region of cytoplasm [GO:0048471]; phagocytic vesicle [GO:0045335]; plasma membrane [GO:0005886]; platelet alpha granule [GO:0031091]; postsynapse [GO:0098794]; presynapse [GO:0098793]; presynaptic active zone cytoplasmic component [GO:0098831]; presynaptic active zone membrane [GO:0048787]; presynaptic cytosol [GO:0099523]; protein-containing complex [GO:0032991]; secretory granule [GO:0030141]
identical protein binding [GO:0042802]; molecular adaptor activity [GO:0060090]; phospholipase binding [GO:0043274]; protein domain specific binding [GO:0019904]; protein kinase binding [GO:0019901]; SNARE binding [GO:0000149]; syntaxin binding [GO:0019905]; syntaxin-1 binding [GO:0017075]
PF00995;
1.25.40.60;3.40.50.1910;3.40.50.2060;
STXBP/unc-18/SEC1 family
null
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P61764}. Membrane; Peripheral membrane protein.
null
null
null
null
null
FUNCTION: Participates in the regulation of synaptic vesicle docking and fusion through interaction with GTP-binding proteins (By similarity). Essential for neurotransmission and binds syntaxin, a component of the synaptic vesicle fusion machinery probably in a 1:1 ratio. Can interact with syntaxins 1, 2, and 3 but not syntaxin 4. Involved in the release of neurotransmitters from neurons through interacting with SNARE complex component STX1A and mediating the assembly of the SNARE complex at synaptic membranes (PubMed:21445306, PubMed:28821673). May play a role in determining the specificity of intracellular fusion reactions (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P61765, ECO:0000269|PubMed:21445306, ECO:0000269|PubMed:28821673}.
Mus musculus (Mouse)
O08600
NUCG_MOUSE
MRALRAGLTLALGAGLGAAAEHWRRREGKAPGLLGRVPLLPVVAADLPALPGGPAGGTGELAKYGLPGVAQLRSRESYVLSYDPRTRGALWVLEQLRPERLRGDGDRSACDFREDDSVHAYHRATNADYRGSGFDRGHLAAAANHRWSQRAMDDTFYLSNVAPQVPHLNQNAWNNLERYSRSLTRTYQNVYVCTGPLFLPRTEADGKSYVKYQVIGKNHVAVPTHFFKVLILEAAGGQIELRSYVMPNAPVDETIPLERFLVPIESIERASGLLFVPNILARAGNLKAITAGSK
3.1.30.-
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:32095813, ECO:0000269|PubMed:32192768};
apoptotic DNA fragmentation [GO:0006309]; DNA catabolic process [GO:0006308]; DNA damage response [GO:0006974]; in utero embryonic development [GO:0001701]; mitochondrial DNA catabolic process [GO:0032043]; negative regulation of TOR signaling [GO:0032007]; positive regulation of apoptotic DNA fragmentation [GO:1902512]; positive regulation of apoptotic process [GO:0043065]; positive regulation of autophagy [GO:0010508]; positive regulation of hydrogen peroxide-mediated programmed cell death [GO:1901300]; positive regulation of mitochondrial DNA replication [GO:0090297]; response to antibiotic [GO:0046677]; response to tumor necrosis factor [GO:0034612]
mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; perikaryon [GO:0043204]; perinuclear region of cytoplasm [GO:0048471]
DNA endonuclease activity [GO:0004520]; DNA nuclease activity [GO:0004536]; magnesium ion binding [GO:0000287]; nucleic acid binding [GO:0003676]; protein homodimerization activity [GO:0042803]; RNA endonuclease activity [GO:0004521]; single-stranded DNA endodeoxyribonuclease activity [GO:0000014]
PF01223;
3.40.570.10;
DNA/RNA non-specific endonuclease family
PTM: GSK3-beta-mediated phosphorylation at Thr-125 is necessary for its interaction with YWHAG and the induction of autophagy. {ECO:0000250|UniProtKB:Q14249}.
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q14249}.
null
null
null
null
null
FUNCTION: Endonuclease that preferentially catalyzes the cleavage of double-stranded 5-hydroxymethylcytosine (5hmC)-modified DNA (PubMed:25355512, PubMed:32095813). The 5hmC-modified nucleotide does not increase the binding affinity, but instead increases the efficiency of cutting and specifies the site of cleavage for the modified DNAs (PubMed:32095813). Shows significantly higher affinity for four-stranded Holliday junction over duplex and single-stranded DNAs (PubMed:32095813). Promotes conservative recombination when the DNA is 5hmC-modified (PubMed:25355512). Promotes autophagy through the suppression of mTOR by its phosphorylation-mediated interaction with YWHAG and its endonuclease activity-mediated DNA damage response (PubMed:33473107). GSK3-beta mediated phosphorylation of ENDOG enhances its interaction with YWHAG, leading to the release of TSC2 and PIK3C3 from YWHAG resulting in mTOR pathway suppression and autophagy initiation (By similarity). Promotes cleavage of mtDNA in response to oxidative and nitrosative stress, in turn inducing compensatory mtDNA replication (By similarity). {ECO:0000250|UniProtKB:Q14249, ECO:0000269|PubMed:25355512, ECO:0000269|PubMed:32095813, ECO:0000269|PubMed:33473107}.
Mus musculus (Mouse)
O08601
MTP_MOUSE
MILLAVLFLCFFSSYSASVKGHTTGLSLNNERLYKLTYSTEVFLDGGKGKPQDSVGYKISSDVDVVLLWRNPDGDDDQVIQVTITAVNVENAGQQRGEKSIFQGKSTPKIIGKDNLEALQRPMLLHLVRGKVKEFYSYENEPVGIENLKRGLASLFQMQLSSGTTNEVDISGDCKVTYQAQQDKVVKIKALDTCKIERSGFTTANQVLGVSSKATSVTTYKIEDSFVTAVLAEETRAFALNFQQTIAGKIVSKQKLELKTTEAGPRMIPGKQVAGVIKAVDSKYKAIPIVGQVLERVCKGCPSLAEHWKSIRKNLEPENLSKAEAVQSFLAFIQHLRTSRREEILQILKAEKKEVLPQLVDAVTSAQTPDSLEAILDFLDFKSDSSIILQERFLYACGFATHPDEELLRALLSKFKGSFASNDIRESVMIIIGALVRKLCQNEGCKLKAVVEAKKLILGGLEKPEKKEDTTMYLLALKNALLPEGIPLLLKYAEAGEGPVSHLATTVLQRYDVSFITDEVKKTLNRIYHQNRKVHEKTVRTTAAAVILKNPSYMDVKNILLSIGELPKEMNKYMLTVVQDILHFEMPASKMIRRVLKEMAVHNYDRFSKSGSSSAYTGYVERSPRAASTYSLDILYSGSGILRRSNLNIFQYIGKAELHGSQVVIEAQGLEGLIAATPDEGEENLDSYAGMSAILFDVQLRPVTFFNGYSDLMSKMLSASGDPVSVVKGLILLIDHSQDIQLQSGLKANMEIQGGLAIDISGSMEFSLWYRESKTRVKNRVAVVITSDVTVDASFVKAGVESRAETEAGLEFISTVQFSQYPFLVCMQMDKAEAPLRQFETKYERLSTGRGYVSRRRKESLVAGCELPLHQENSEMCNVVFPPQPESDNSGGWF
null
null
cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; circadian rhythm [GO:0007623]; establishment of localization in cell [GO:0051649]; lipid metabolic process [GO:0006629]; lipid transport [GO:0006869]; lipoprotein metabolic process [GO:0042157]; lipoprotein transport [GO:0042953]; low-density lipoprotein particle remodeling [GO:0034374]; phospholipid transport [GO:0015914]; plasma lipoprotein particle assembly [GO:0034377]; protein secretion [GO:0009306]; response to calcium ion [GO:0051592]; triglyceride metabolic process [GO:0006641]; triglyceride transport [GO:0034197]
basolateral plasma membrane [GO:0016323]; brush border membrane [GO:0031526]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; microvillus membrane [GO:0031528]; receptor complex [GO:0043235]; vesicle [GO:0031982]
apolipoprotein binding [GO:0034185]; ceramide 1-phosphate transfer activity [GO:1902388]; cholesterol transfer activity [GO:0120020]; lipid binding [GO:0008289]; lipid transporter activity [GO:0005319]; phosphatidylcholine transfer activity [GO:0120019]; phosphatidylethanolamine transfer activity [GO:1904121]; phospholipid transfer activity [GO:0120014]; phospholipid transporter activity [GO:0005548]; protein heterodimerization activity [GO:0046982]; protein-containing complex binding [GO:0044877]; triglyceride transfer activity [GO:0140344]
PF19444;PF01347;
1.25.10.20;
null
PTM: [Isoform 2]: Cleaved by signal peptidase between residues Gln-33 and Asn-34. {ECO:0000269|PubMed:17312007, ECO:0000269|PubMed:17635917}.
SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:33168624}.; SUBCELLULAR LOCATION: [Isoform 1]: Endoplasmic reticulum {ECO:0000269|PubMed:17312007, ECO:0000269|PubMed:17635917}. Golgi apparatus {ECO:0000250|UniProtKB:P55157}. Note=Colocalizes with P4HB/PDI in the endoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:P55157}.; SUBCELLULAR LOCATION: [Isoform 2]: Endoplasmic reticulum {ECO:0000269|PubMed:17312007}. Golgi apparatus {ECO:0000269|PubMed:17635917}.
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(in) = a 1,2-diacyl-sn-glycero-3-phosphocholine(out); Xref=Rhea:RHEA:38571, ChEBI:CHEBI:57643; Evidence={ECO:0000250|UniProtKB:P55157}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38572; Evidence={ECO:0000250|UniProtKB:P55157}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out); Xref=Rhea:RHEA:38895, ChEBI:CHEBI:64612; Evidence={ECO:0000269|PubMed:15897609}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38896; Evidence={ECO:0000305|PubMed:15897609}; CATALYTIC ACTIVITY: Reaction=a cholesterol ester(in) = a cholesterol ester(out); Xref=Rhea:RHEA:39007, ChEBI:CHEBI:17002; Evidence={ECO:0000269|PubMed:15897609, ECO:0000269|PubMed:18502767}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39008; Evidence={ECO:0000305|PubMed:15897609}; CATALYTIC ACTIVITY: Reaction=a triacyl-sn-glycerol(in) = a triacyl-sn-glycerol(out); Xref=Rhea:RHEA:39011, ChEBI:CHEBI:64615; Evidence={ECO:0000269|PubMed:15897609, ECO:0000269|PubMed:16478722, ECO:0000269|PubMed:18502767, ECO:0000269|PubMed:33168624}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39012; Evidence={ECO:0000305|PubMed:16478722};
null
null
null
null
FUNCTION: Catalyzes the transport of triglyceride, cholesteryl ester, and phospholipid between phospholipid surfaces (PubMed:15897609, PubMed:16478722, PubMed:18502767, PubMed:33168624). Required for the assembly and secretion of plasma lipoproteins that contain apolipoprotein B (PubMed:10713055, PubMed:17635917, PubMed:18502767, PubMed:33168624, PubMed:9502759). May be involved in regulating cholesteryl ester biosynthesis in cells that produce lipoproteins (PubMed:18502767). {ECO:0000269|PubMed:10713055, ECO:0000269|PubMed:15897609, ECO:0000269|PubMed:16478722, ECO:0000269|PubMed:17635917, ECO:0000269|PubMed:18502767, ECO:0000269|PubMed:33168624, ECO:0000269|PubMed:9502759}.; FUNCTION: [Isoform 2]: Critical for the development of natural killer T (NKT) cells (PubMed:17312007). Required for the assembly and secretion of plasma lipoproteins that contain apolipoprotein B (PubMed:17635917). {ECO:0000269|PubMed:17312007, ECO:0000269|PubMed:17635917}.
Mus musculus (Mouse)
O08602
RAE1A_MOUSE
MAKAAVTKRHHFMIQKLLILLSYGYTNGLDDAHSLRCNLTIKDPTPADPLWYEAKCLVDEILILHLSNINKTMTSGDPGETANATEVGECLTQPLKDLCQKLRNKVSNTKVDTHKTNGYPHLQVTMIYLQSQGQIPSATWEFNISDSYFFTFYTENMSWRSANDESGVIMNKWKDDGEFVKRLKFLIPECRQEVDEFLKQPKEKPRSTSRSPSITQLTSTSPLPPPSHSTSKKGFISVGLIFISLLFAFAFAM
null
null
antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent [GO:0002486]; antigen processing and presentation of endogenous peptide antigen via MHC class Ib [GO:0002476]; cellular response to exogenous dsRNA [GO:0071360]; cellular response to lipopolysaccharide [GO:0071222]; defense response to bacterium [GO:0042742]; immune response [GO:0006955]; positive regulation of T cell mediated cytotoxicity [GO:0001916]
external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]
natural killer cell lectin-like receptor binding [GO:0046703]
PF14586;
3.30.500.10;
NKG2D ligand family
PTM: Glycosylated. {ECO:0000269|PubMed:8982867}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10894171, ECO:0000269|PubMed:8982867}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:10894171, ECO:0000269|PubMed:8982867}.
null
null
null
null
null
FUNCTION: Acts as a ligand for KLRK1. {ECO:0000269|PubMed:10894171}.
Mus musculus (Mouse)
O08603
RAE1B_MOUSE
MAKAAVTKRHHFMIQKLLILLSYGYTNGLDDAHSLRCNLTIKDPTPADPLWYEAKCFVGEILILHLSNINKTMTSGDPGETANATEVKKCLTQPLKNLCQKLRNKVSNTKVDTHKTNGYPHLQVTMIYPQSQGRTPSATWEFNISDSYFFTFYTENMSWRSANDESGVIMNKWKDDGEFVKQLKFLIHECSQKMDEFLKQSKEKPRSTSRSPSITQLTSTSPLPPPSHSTSKKGFISVGLIFISLLFAFAFAM
null
null
antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent [GO:0002486]; antigen processing and presentation of endogenous peptide antigen via MHC class Ib [GO:0002476]; cellular response to exogenous dsRNA [GO:0071360]; cellular response to lipopolysaccharide [GO:0071222]; defense response to bacterium [GO:0042742]; immune response [GO:0006955]; positive regulation of immune response to tumor cell [GO:0002839]; positive regulation of macrophage activation [GO:0043032]; positive regulation of natural killer cell activation [GO:0032816]; positive regulation of nitric oxide biosynthetic process [GO:0045429]; positive regulation of T cell mediated cytotoxicity [GO:0001916]; positive regulation of type II interferon production [GO:0032729]; susceptibility to natural killer cell mediated cytotoxicity [GO:0042271]
external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]
natural killer cell lectin-like receptor binding [GO:0046703]
PF14586;
3.30.500.10;
NKG2D ligand family
PTM: Glycosylated. {ECO:0000269|PubMed:8982867}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10894171, ECO:0000269|PubMed:8982867}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:10894171, ECO:0000269|PubMed:8982867}.
null
null
null
null
null
FUNCTION: Acts as a ligand for KLRK1. {ECO:0000269|PubMed:10894171, ECO:0000269|PubMed:11248803, ECO:0000269|PubMed:11557981}.
Mus musculus (Mouse)
O08604
RAE1C_MOUSE
MAKAAVTKRHHFMIQKLLILLSYGYTNGLDDAHSLRCNLTIKAPTPADPLWYEAKCLVDEILILHLSNINKTMTSGDPGETANATEVGECLTQPVNDLCQKLRDKVSNTKVDTHKTNGYPHLQVTMIYPQSQGQTPSATWEFNISDSYFFTFYTENMSWRSANDESGVIMNKWNDDGDLVQRLKYFIPECRQKIDEFLKQSKEKPRSTSRSPSITQLTSTSPLPPPSHSTSKKGFISVGLIFISLLFAFAFAM
null
null
antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent [GO:0002486]; antigen processing and presentation of endogenous peptide antigen via MHC class Ib [GO:0002476]; cellular response to exogenous dsRNA [GO:0071360]; cellular response to lipopolysaccharide [GO:0071222]; defense response to bacterium [GO:0042742]; immune response [GO:0006955]; positive regulation of T cell mediated cytotoxicity [GO:0001916]
external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]
natural killer cell lectin-like receptor binding [GO:0046703]
PF14586;
3.30.500.10;
NKG2D ligand family
PTM: Glycosylated. {ECO:0000269|PubMed:8982867}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10894171, ECO:0000269|PubMed:8982867}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:10894171, ECO:0000269|PubMed:8982867}.
null
null
null
null
null
FUNCTION: Acts as a ligand for KLRK1. {ECO:0000269|PubMed:10894171}.
Mus musculus (Mouse)
O08605
MKNK1_MOUSE
MVSSQKLEKPIEMGSSEPLPIVDSDKRRKKKRKTRATDSLPGKFEDVYQLTSELLGEGAYAKVQGAVNLQSGKEYAVKIIEKQAGHSRSRVFREVETLYQCQGNRNILELIEFFEDDTRFYLVFEKLQGGSILAHIQKRKHFNEREASRVVRDVATALDFLHTKGIAHRDLKPENILCESPEKVSPVKICDFDLGSGVKLNNSCTPITTPELTTPCGSAEYMAPEVVEVFRDEATFYDKRCDLWSLGVVLYIMLSGYPPFVGHCGADCGWDRGEVCRMCQNKLFESIQEGKYEFPDKDWAHISNEAKDLISKLLVRDAKQRLSAAQVLQHPWVQGQAPERGLPTPQVLQRNSSTMDLTLFAAEAIALNRQLSQHEENELAEEQEALAEGLCSMKLSPPSKSRLARRRALAQAGRSRDANPCLTPAGL
2.7.11.1
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:9155017};
extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; intracellular signal transduction [GO:0035556]; protein phosphorylation [GO:0006468]; regulation of translational initiation [GO:0006446]; response to salt stress [GO:0009651]
cytoplasm [GO:0005737]; nucleus [GO:0005634]
ATP binding [GO:0005524]; calcium-dependent protein serine/threonine kinase activity [GO:0009931]; calmodulin binding [GO:0005516]; calmodulin-dependent protein kinase activity [GO:0004683]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
PF00069;
1.10.510.10;
Protein kinase superfamily, CAMK Ser/Thr protein kinase family
PTM: Dual phosphorylation of Thr-209 and Thr-214 activates the kinase. Phosphorylation of Thr-344 activates the kinase. MAPK3/ERK1 is one of the kinases which activate MKNK1/MNK1. Phosphorylation by PAK2 leads to a reduced phosphorylation of EIF4G1 (By similarity). {ECO:0000250}.
null
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:9155017}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:9155017};
null
null
null
null
FUNCTION: May play a role in the response to environmental stress and cytokines. Appears to regulate translation by phosphorylating EIF4E, thus increasing the affinity of this protein for the 7-methylguanosine-containing mRNA cap. {ECO:0000269|PubMed:9155017}.
Mus musculus (Mouse)
O08608
OAZ2_MOUSE
MINTQDSSILPLSKCPQLQCCRHIVPGPLWCSDAPHPLSKIPGGRGGGRDPSLSALIYKDEKLTVTQDLPVNDGKPHIVHFQYEVTEVKVSSWDAVLSSQSLFVEIPDGLLADGSKEGLLALLEFAEEKMKVNYVFICFRKGREDRAPLLKTFSFLGFEIVRPGHPCVPSRPDVMFMVYPLDQNLSDED
null
null
negative regulation of polyamine transmembrane transport [GO:1902268]; polyamine biosynthetic process [GO:0006596]; polyamine metabolic process [GO:0006595]; positive regulation of intracellular protein transport [GO:0090316]; positive regulation of protein catabolic process [GO:0045732]
cytoplasm [GO:0005737]; nucleus [GO:0005634]
ornithine decarboxylase inhibitor activity [GO:0008073]
PF02100;
3.40.630.60;
ODC antizyme family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19725046}.
null
null
null
null
null
FUNCTION: Ornithine decarboxylase (ODC) antizyme protein that negatively regulates ODC activity and intracellular polyamine biosynthesis and uptake in response to increased intracellular polyamine levels. Binds to ODC monomers, inhibiting the assembly of the functional ODC homodimers. Does not target the ODC monomers for degradation, which allows a protein synthesis-independent restoration of ODC activity (PubMed:16916800, PubMed:18508777, PubMed:24967154). Involved in the translocation of AZIN2 from ER-Golgi intermediate compartment (ERGIC) to the cytosol (PubMed:19449338). {ECO:0000269|PubMed:16916800, ECO:0000269|PubMed:18508777, ECO:0000269|PubMed:19449338, ECO:0000269|PubMed:24967154}.
Mus musculus (Mouse)
O08609
MLX_MOUSE
MTEPGASPEDPWVKASFADAHAGEGRAGRARARRGSGRRGAPQLSPESPLLSGARGCREDSSHPACAKVEYAYSDNSLDPGLFVESTHKGSVVSRANSIGSTSASSVPNTDDEDSDYQQEAYKESYKDRRRRAHTQAEQKRRDAIKRGYDDLQTIVPTCQQQDFSIGSQKLSKAIVLQKTIDYIQFLHKEKKKQEEEVSTLRKDVTALKIMKVNYEQIVKAHQDNPHEGEDQVSDQVKFNVFQGIMDSLFQSFNASISVASFQELSACVFSWIEEHCEPQTLREIVIGVLHQLKNQLY
null
null
nucleocytoplasmic transport [GO:0006913]; positive regulation of glycolytic process [GO:0045821]; positive regulation of lipid biosynthetic process [GO:0046889]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of transcription from RNA polymerase II promoter by glucose [GO:0000432]
cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575]
DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; protein dimerization activity [GO:0046983]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]
PF00010;
4.10.280.10;
null
null
SUBCELLULAR LOCATION: [Isoform Alpha]: Cytoplasm {ECO:0000250|UniProtKB:Q9UH92}. Note=Found predominantly in the cytoplasm. {ECO:0000250|UniProtKB:Q9UH92}.; SUBCELLULAR LOCATION: [Isoform Beta]: Cytoplasm {ECO:0000250|UniProtKB:Q9UH92}. Note=Found predominantly in the cytoplasm. {ECO:0000250|UniProtKB:Q9UH92}.; SUBCELLULAR LOCATION: [Isoform Gamma]: Nucleus {ECO:0000250|UniProtKB:Q9UH92}. Note=Found predominantly in the nucleus. {ECO:0000250|UniProtKB:Q9UH92}.
null
null
null
null
null
FUNCTION: Transcription regulator. Forms a sequence-specific DNA-binding protein complex with MAD1, MAD4, MNT, WBSCR14 and MLXIP which recognizes the core sequence 5'-CACGTG-3'. The TCFL4-MAD1, TCFL4-MAD4, TCFL4-WBSCR14 complexes are transcriptional repressors. Plays a role in transcriptional activation of glycolytic target genes. Involved in glucose-responsive gene regulation. {ECO:0000269|PubMed:10593926, ECO:0000269|PubMed:11073985, ECO:0000269|PubMed:16644671}.
Mus musculus (Mouse)
O08615
OXLA_MUSSP
AFKDLKALGCKKAMNKFNKHTLLEYLLEEGNLSRPAVQLLGDVMSE
1.4.3.2; 1.4.3.25
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:O09046};
adaptive immune response [GO:0002250]; amino acid catabolic process [GO:0009063]; L-phenylalanine catabolic process [GO:0006559]; negative regulation of T cell activation [GO:0050868]; negative regulation of T cell mediated immune response to tumor cell [GO:0002841]; negative regulation of T cell proliferation [GO:0042130]; positive regulation of regulatory T cell differentiation [GO:0045591]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of adaptive immune response [GO:0002819]; regulation of B cell differentiation [GO:0045577]; tryptophan catabolic process [GO:0006569]; tryptophan catabolic process to indole-3-acetate [GO:0019440]; tyrosine catabolic process [GO:0006572]
acrosomal vesicle [GO:0001669]; extracellular region [GO:0005576]; immunological synapse [GO:0001772]; lysosome [GO:0005764]; sperm midpiece [GO:0097225]
L-amino-acid oxidase activity [GO:0001716]; L-phenylalaine oxidase activity [GO:0106329]; polyamine oxidase activity [GO:0046592]
null
1.10.405.10;
Flavin monoamine oxidase family, FIG1 subfamily
null
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q96RQ9}. Lysosome {ECO:0000250|UniProtKB:O09046}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250|UniProtKB:Q96RQ9}. Note=Secreted at the immunological synapse. {ECO:0000250|UniProtKB:Q96RQ9}.
CATALYTIC ACTIVITY: Reaction=an L-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 + NH4(+); Xref=Rhea:RHEA:13781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179, ChEBI:CHEBI:59869; EC=1.4.3.2; Evidence={ECO:0000250|UniProtKB:Q96RQ9}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13782; Evidence={ECO:0000250|UniProtKB:Q96RQ9}; CATALYTIC ACTIVITY: Reaction=H2O + L-tryptophan + O2 = H2O2 + indole-3-pyruvate + NH4(+); Xref=Rhea:RHEA:61244, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17640, ChEBI:CHEBI:28938, ChEBI:CHEBI:57912; Evidence={ECO:0000250|UniProtKB:Q96RQ9}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61245; Evidence={ECO:0000250|UniProtKB:Q96RQ9}; CATALYTIC ACTIVITY: Reaction=H2O + L-phenylalanine + O2 = 3-phenylpyruvate + H2O2 + NH4(+); Xref=Rhea:RHEA:61240, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:18005, ChEBI:CHEBI:28938, ChEBI:CHEBI:58095; Evidence={ECO:0000250|UniProtKB:Q96RQ9}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61241; Evidence={ECO:0000250|UniProtKB:Q96RQ9}; CATALYTIC ACTIVITY: Reaction=H2O + L-tyrosine + O2 = 3-(4-hydroxyphenyl)pyruvate + H2O2 + NH4(+); Xref=Rhea:RHEA:61248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:36242, ChEBI:CHEBI:58315; Evidence={ECO:0000250|UniProtKB:Q96RQ9}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61249; Evidence={ECO:0000250|UniProtKB:Q96RQ9}; CATALYTIC ACTIVITY: Reaction=H2O + L-arginine + O2 = 5-guanidino-2-oxopentanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:51404, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:32682, ChEBI:CHEBI:58489; EC=1.4.3.25; Evidence={ECO:0000250|UniProtKB:Q96RQ9}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51405; Evidence={ECO:0000250|UniProtKB:Q96RQ9};
null
PATHWAY: Amino-acid degradation; L-tryptophan degradation via pyruvate pathway. {ECO:0000250|UniProtKB:Q96RQ9}.
null
null
FUNCTION: Secreted L-amino-acid oxidase that acts as a key immunoregulator. Has preference for L-aromatic amino acids: converts phenylalanine (Phe), tyrosine (Tyr) and tryptophan (Trp) to phenylpyruvic acid (PP), hydroxyphenylpyruvic acid (HPP), and indole-3-pyruvic acid (I3P), respectively. Also has weak L-arginine oxidase activity. Acts as a negative regulator of anti-tumor immunity by mediating Trp degradation via an indole pyruvate pathway that activates the transcription factor AHR. IL4I1-mediated Trp catabolism generates I3P, giving rise to indole metabolites (indole-3-acetic acid (IAA) and indole-3-aldehyde (I3A)) and kynurenic acid, which act as ligands for AHR, a ligand-activated transcription factor that plays important roles in immunity and cancer. AHR activation by indoles following IL4I1-mediated Trp degradation enhances tumor progression by promoting cancer cell motility and suppressing adaptive immunity. Also has an immunoregulatory function in some immune cells, probably by mediating Trp degradation and promoting downstream AHR activation: inhibits T-cell activation and proliferation, promotes the differentiation of naive CD4(+) T-cells into FOXP3(+) regulatory T-cells (Treg) and regulates the development and function of B-cells (By similarity). Also regulates M2 macrophage polarization by inhibiting T-cell activation (By similarity). Also has antibacterial properties by inhibiting growth of Gram negative and Gram positive bacteria through the production of NH4(+) and H2O2 (By similarity). {ECO:0000250|UniProtKB:O09046, ECO:0000250|UniProtKB:Q96RQ9}.
Mus spretus (Western Mediterranean mouse) (Algerian mouse)
O08617
PTPRR_RAT
MRRAVGFPALCLLLNLHAAGCFSRNNDHFLAIRQKKSWKPMFIYDHSQDIKKSLDIAQEAYKHNYPAPSEVQISKRHQIVDSAFPRPAYDPSLNLLAASGQDLEIENLPIPAANVIVVTLQMDIDKLNITLLRIFRQGVAAALGLLPQQVHINRLIEKKSQIELFVSPGNRKPGEPQALQAEEVLRSLNVDVLRQSLPQFGSIDVSPEKNVLQGQHEADKIWSKEGFYAVVIFLSIFIIIVTCLMIIYRLKERLQLSFRQDKEKNQEIHLSPIALQQAQSEAKAAHSMVQPDQAPKVLNVVVDPQGQCTPEIRNTASTSVCPSPFRMKPIGLQERRGSNVSLTLDMSSLGNVEPFVAVSTPREKVAMEYLQSASRVLTSPQLRDVVASSHLLQSEFMEIPMNFVDPKEIDIPRHGTKNRYKTILPNPLSRVCLRPKNITDPLSTYINANYIRGYSGKEKAFIATQGPMINTVNDFWQMVWQEDSPVIVMITKLKEKNEKCVLYWPEKRGIYGKVEVLVIGVNECDNYTIRNLVLKRGSHTQHVKHYWYTSWPDHKTPDSAQPLLQLMLDVEEDRLASEGRGPVVVHCSAGIGRTGCFIATSIGCQQLKEEGVVDALSIVCQLRVDRGGMVQTSEQYEFVHHALCLFESRLSPETVQ
3.1.3.48
null
dephosphorylation [GO:0016311]; ERBB2 signaling pathway [GO:0038128]; in utero embryonic development [GO:0001701]; negative regulation of epithelial cell migration [GO:0010633]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; nervous system development [GO:0007399]; neuron differentiation [GO:0030182]; signal transduction [GO:0007165]
cell junction [GO:0030054]; cytosol [GO:0005829]; plasma membrane [GO:0005886]
protein kinase binding [GO:0019901]; protein tyrosine phosphatase activity [GO:0004725]
PF00102;
3.90.190.10;
Protein-tyrosine phosphatase family, Receptor class 7 subfamily
null
SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform 4]: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU10044};
null
null
null
null
FUNCTION: Sequesters mitogen-activated protein kinases (MAPKs) such as MAPK1, MAPK3 and MAPK14 in the cytoplasm in an inactive form. The MAPKs bind to a dephosphorylated kinase interacting motif, phosphorylation of which by the protein kinase A complex releases the MAPKs for activation and translocation into the nucleus (By similarity). {ECO:0000250}.
Rattus norvegicus (Rat)
O08623
SQSTM_RAT
MASLTVKAYLLGKEEAAREIRRFSFCFSPEPEAEAAAGPGPCERLLSRVAVLFPALRPGGFQAHYRDEDGDLVAFSSDEELTMAMSYVKDDIFRIYIKEKKECRREHRPPCAQEARSMVHPNVICDGCNGPVVGTRYKCSVCPDYDLCSVCEGKGLHREHSKLIFPNPFGHLSDSFSHSRWLRKLKHGHFGWPGWEMGPPGNWSPRPPRAGDGRPCPTAESASAPSEDPNVNFLKNVGESVAAALSPLGIEVDIDVEHGGKRSRLTPTSAESSSTGTEDKSGTQPSSCSSEVSKPDGAGEGPAQSLTEQMKKIALESVGQPEELMESDNCSGGDDDWTHLSSKEVDPSTGELQSLQMPESEGPSSLDPSQEGPTGLKEAALYPHLPPEADPRLIESLSQMLSMGFSDEGGWLTRLLQTKNYDIGAALDTIQYSKHPPPL
null
null
aggrephagy [GO:0035973]; apoptotic process [GO:0006915]; autophagy [GO:0006914]; brown fat cell proliferation [GO:0070342]; cell differentiation [GO:0030154]; endosome organization [GO:0007032]; energy homeostasis [GO:0097009]; immune system process [GO:0002376]; macroautophagy [GO:0016236]; mitophagy [GO:0000423]; negative regulation of protein ubiquitination [GO:0031397]; negative regulation of toll-like receptor 4 signaling pathway [GO:0034144]; negative regulation of transcription by RNA polymerase II [GO:0000122]; non-membrane-bounded organelle assembly [GO:0140694]; pexophagy [GO:0000425]; positive regulation of autophagy [GO:0010508]; positive regulation of long-term synaptic potentiation [GO:1900273]; positive regulation of protein localization to plasma membrane [GO:1903078]; positive regulation of protein phosphorylation [GO:0001934]; protein catabolic process [GO:0030163]; protein import into nucleus [GO:0006606]; protein localization to perinuclear region of cytoplasm [GO:1905719]; protein targeting to vacuole involved in autophagy [GO:0071211]; regulation of canonical NF-kappaB signal transduction [GO:0043122]; regulation of protein complex stability [GO:0061635]; response to ischemia [GO:0002931]; response to mitochondrial depolarisation [GO:0098780]; temperature homeostasis [GO:0001659]; transcription by RNA polymerase II [GO:0006366]
aggresome [GO:0016235]; amphisome [GO:0044753]; autolysosome [GO:0044754]; autophagosome [GO:0005776]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; inclusion body [GO:0016234]; intracellular non-membrane-bounded organelle [GO:0043232]; late endosome [GO:0005770]; Lewy body [GO:0097413]; mitochondrion [GO:0005739]; P-body [GO:0000932]; phagophore assembly site [GO:0000407]; PML body [GO:0016605]; sarcomere [GO:0030017]; sperm midpiece [GO:0097225]
enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; ionotropic glutamate receptor binding [GO:0035255]; K63-linked polyubiquitin modification-dependent protein binding [GO:0070530]; molecular condensate scaffold activity [GO:0140693]; molecular sequestering activity [GO:0140313]; protein kinase binding [GO:0019901]; protein kinase C binding [GO:0005080]; protein sequestering activity [GO:0140311]; protein-containing complex binding [GO:0044877]; protein-macromolecule adaptor activity [GO:0030674]; SH2 domain binding [GO:0042169]; signaling adaptor activity [GO:0035591]; signaling receptor activity [GO:0038023]; ubiquitin binding [GO:0043130]; ubiquitin protein ligase binding [GO:0031625]; ubiquitin-dependent protein binding [GO:0140036]; zinc ion binding [GO:0008270]
PF00564;PF16577;PF00569;
3.30.60.90;1.10.8.10;
null
PTM: Phosphorylated (PubMed:9177193). Phosphorylation at Ser-406 by ULK1 destabilizes the UBA dimer interface and increases binding affinity to ubiquitinated proteins. Phosphorylation at Ser-406 also primes for subsequent phosphorylation at Ser-402 (By similarity). Phosphorylation at Ser-402 by CK2 or ULK1 promotes binding to ubiquitinated proteins by increasing the affinity between the UBA domain and polyubiquitin chains. Phosphorylation at Ser-402 by ULK1 is stimulated by SESN2. Phosphorylated at Ser-402 by TBK1, leading to promote relocalization of 'Lys-63'-linked ubiquitinated STING1 to autophagosomes. Phosphorylation at Ser-348 by ULK1 promotes interaction with KEAP1 and inactivation of the BCR(KEAP1) complex, promoting NFE2L2/NRF2 nuclear accumulation and expression of phase II detoxifying enzymes. Phosphorylated in vitro by TTN (By similarity). {ECO:0000250|UniProtKB:Q13501, ECO:0000250|UniProtKB:Q64337, ECO:0000269|PubMed:9177193}.; PTM: Ubiquitinated by UBE2J1 and RNF26 at Lys-434: ubiquitinated SQSTM1 attracts specific vesicle-associated adapters, forming a molecular bridge that restrains cognate vesicles in the perinuclear region and organizes the endosomal pathway for efficient cargo transport. Ubiquitination by UBE2D2 and UBE2D3 increases its ability to bind polyubiquitin chains by destabilizing the UBA dimer interface. Deubiquitination by USP15 releases target vesicles for fast transport into the cell periphery. Ubiquitinated by the BCR(KEAP1) complex at Lys-419, increasing SQSTM1 sequestering activity and promoting its degradation. Ubiquitinated via 'Lys-29' and 'Lys-33'-linked polyubiquitination leading to xenophagic targeting of bacteria and inhibition of their replication. {ECO:0000250|UniProtKB:Q13501}.; PTM: Acetylated at Lys-419 and Lys-434 by KAT5/TIP60, promotes activity by destabilizing the UBA dimer interface and increases binding affinity to ubiquitinated proteins. Deacetylated by HDAC6. {ECO:0000250|UniProtKB:Q13501}.; PTM: Palmitoylation at Cys-288 by ZDHHC19 is required for efficient autophagic degradation of SQSTM1-cargo complexes by promoting affinity for ATG8 proteins and recruitment of p62 bodies to autophagosomes. Dealmitoylated at Cys-288 by LYPLA1. {ECO:0000250|UniProtKB:Q13501}.
SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome {ECO:0000250|UniProtKB:Q13501}. Preautophagosomal structure {ECO:0000250|UniProtKB:Q13501}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q64337}. Nucleus, PML body {ECO:0000250|UniProtKB:Q13501}. Late endosome {ECO:0000250|UniProtKB:Q13501}. Lysosome {ECO:0000250|UniProtKB:Q13501}. Nucleus {ECO:0000250|UniProtKB:Q64337}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q13501}. Cytoplasm, myofibril, sarcomere {ECO:0000269|PubMed:15802564}. Note=In cardiac muscle, localizes to the sarcomeric band (PubMed:15802564). Localizes to cytoplasmic membraneless inclusion bodies, known as p62 bodies, containing polyubiquitinated protein aggregates (By similarity). In protein aggregate diseases of the liver, found in large amounts in Mallory bodies of alcoholic and nonalcoholic steatohepatitis, hyaline bodies in hepatocellular carcinoma, and in SERPINA1 aggregates. Enriched in Rosenthal fibers of pilocytic astrocytoma. In the cytoplasm, observed in both membrane-free ubiquitin-containing protein aggregates (sequestosomes) and membrane-surrounded autophagosomes. Colocalizes with TRIM13 in the perinuclear endoplasmic reticulum. Co-localizes with TRIM5 in cytoplasmic bodies. When nuclear export is blocked by treatment with leptomycin B, accumulates in PML bodies (By similarity). {ECO:0000250|UniProtKB:Q13501, ECO:0000250|UniProtKB:Q64337, ECO:0000269|PubMed:15802564}.
null
null
null
null
null
FUNCTION: Molecular adapter required for selective macroautophagy (aggrephagy) by acting as a a bridge between polyubiquitinated proteins and autophagosomes (By similarity). Promotes the recruitment of ubiquitinated cargo proteins to autophagosomes via multiple domains that bridge proteins and organelles in different steps (By similarity). SQSTM1 first mediates the assembly and removal of ubiquitinated proteins by undergoing liquid-liquid phase separation upon binding to ubiquitinated proteins via its UBA domain, leading to the formation of insoluble cytoplasmic inclusions, known as p62 bodies (By similarity). SQSTM1 then interacts with ATG8 family proteins on autophagosomes via its LIR motif, leading to p62 body recruitment to autophagosomes, followed by autophagic clearance of ubiquitinated proteins (By similarity). SQSTM1 is itself degraded along with its ubiquitinated cargos (By similarity). Also required to recruit ubiquitinated proteins to PML bodies in the nucleus (By similarity). Also involved in autophagy of peroxisomes (pexophagy) in response to reactive oxygen species (ROS) by acting as a bridge between ubiquitinated PEX5 receptor and autophagosomes (By similarity). Acts as an activator of the NFE2L2/NRF2 pathway via interaction with KEAP1: interaction inactivates the BCR(KEAP1) complex by sequestering the complex in inclusion bodies, promoting nuclear accumulation of NFE2L2/NRF2 and subsequent expression of cytoprotective genes (By similarity). Promotes relocalization of 'Lys-63'-linked ubiquitinated STING1 to autophagosomes (By similarity). Involved in endosome organization by retaining vesicles in the perinuclear cloud: following ubiquitination by RNF26, attracts specific vesicle-associated adapters, forming a molecular bridge that restrains cognate vesicles in the perinuclear region and organizes the endosomal pathway for efficient cargo transport (By similarity). Sequesters tensin TNS2 into cytoplasmic puncta, promoting TNS2 ubiquitination and proteasomal degradation (By similarity). May regulate the activation of NFKB1 by TNF-alpha, nerve growth factor (NGF) and interleukin-1 (PubMed:11244088, PubMed:11500922). May play a role in titin/TTN downstream signaling in muscle cells (By similarity). Adapter that mediates the interaction between TRAF6 and CYLD (By similarity). {ECO:0000250|UniProtKB:Q13501, ECO:0000250|UniProtKB:Q64337, ECO:0000269|PubMed:11244088, ECO:0000269|PubMed:11500922}.; FUNCTION: [Isoform 1]: More potent than isoform 2 to stimulate PRKCZ-dependent phosphorylation of KCNAB2. {ECO:0000269|PubMed:10477520}.
Rattus norvegicus (Rat)
O08625
SYT10_RAT
MSFRKEDGVSSLCQKALHIITELCFAGQVEWDKCSGIFPADRSGQGGGGTDISVSLLAVVVSFCGLALLVVSLFVFWKLCWPCWKSKLVAPNVSTLPQSISSAPTEVFETEEKKEVEENEKPAPKAIEPAIKISHTSPDIPAEVQTALKEHLIKHARVQRQTTDPTSSSRHNSFRRHLPRQMNVSSVDFSMGTEPVLQRGETRTSIGRIKPELYKQKSVDSEGNRKDDVKTCGKLNFALQYDYENELLVVKIIKALDLPAKDFTGTSDPYVKIYLLPDRKKKFQTRVHRKTLNPLFDELFQFPVVYDQLSNRKLHFSIYDFDRFSRHDMIGEVILDNLFEVSDLSREATVWKDIHCATTESIDLGEIMFSLCYLPTAGRMTLTVIKCRNLKAMDITGSSDPYVKVSLMCEGRRLKKRKTTTKKNTLNPVYNEAIIFDIPPENVDQVSLCIAVMDYDRVGHNEVIGVCRTGLDAEGLGRDHWNEMLAYHRKPITHWHPLLELPGRATSFDSQGSCSSPRPPSTP
null
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00041, ECO:0000269|PubMed:11823420}; Note=Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2 domains. {ECO:0000250|UniProtKB:P40748};
calcium-ion regulated exocytosis [GO:0017156]; cellular response to calcium ion [GO:0071277]; chemical synaptic transmission [GO:0007268]; positive regulation of calcium ion-dependent exocytosis [GO:0045956]; presynaptic dense core vesicle exocytosis [GO:0099525]; regulation of calcium ion-dependent exocytosis [GO:0017158]; regulation of dopamine secretion [GO:0014059]; sensory perception of smell [GO:0007608]
exocytic vesicle [GO:0070382]; glutamatergic synapse [GO:0098978]; plasma membrane [GO:0005886]; presynapse [GO:0098793]; synaptic vesicle membrane [GO:0030672]
calcium ion binding [GO:0005509]; calcium-dependent phospholipid binding [GO:0005544]; clathrin binding [GO:0030276]; identical protein binding [GO:0042802]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; phosphatidylserine binding [GO:0001786]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; SNARE binding [GO:0000149]; syntaxin binding [GO:0019905]
PF00168;
2.60.40.150;
Synaptotagmin family
null
SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250|UniProtKB:Q9R0N4}; Single-pass membrane protein {ECO:0000255}. Note=Localizes to neuronal vesicles containing IGF1 that are not enriched at synapses. Does not colocalize with synaptic vesicles or with the Golgi apparatus. {ECO:0000250|UniProtKB:Q9R0N4}.
null
null
null
null
null
FUNCTION: Ca(2+) sensor specifically required for the Ca(2+)-dependent exocytosis of secretory vesicles containing IGF1 in neurons of the olfactory bulb. Exocytosis of IGF1 is required for sensory perception of smell. Not involved in Ca(2+)-dependent synaptic vesicle exocytosis (By similarity). Acts through Ca(2+) and phospholipid binding to the C2 domain: Ca(2+) induces binding of the C2-domains to phospholipid membranes and to assembled SNARE-complexes; both actions contribute to triggering exocytosis (PubMed:18508778). {ECO:0000250|UniProtKB:Q9R0N4, ECO:0000269|PubMed:18508778}.
Rattus norvegicus (Rat)
O08629
TIF1B_RAT
MAASAAAATAAASAATAASAASGSPGSGEGSAGGEKRPAASSAAAASASASSPAGGGGEAQELLEHCGVCRERLRPERDPRLLPCLHSACSACLGPATPAAANNSGDGGSAGDGAMVDCPVCKQQCYSKDIVENYFMRDSGSKASSDSQDANQCCTSCEDNAPATSYCVECSEPLCETCVEAHQRVKYTKDHTVRSTGPAKTRDGERTVYCNVHKHEPLVLFCESCDTLTCRDCQLNAHKDHQYQFLEDAVRNQRKLLASLVKRLGDKHATLQKNTKEVRSSIRQVSDVQKRVQVDVKMAILQIMKELNKRGRVLVNDAQKVTEGQQERLERQHWTMTKIQKHQEHILRFASWALESDNNTALLLSKKLIYFQLHRALKMIVDPVEPHGEMKFQWDLNAWTKSAEAFGKIVAERPGTNSTGPGPMAPPRAPGPLSKQGSGSSQPMEVQEGYGFGTDDPYSSAEPHVSGMKRSRSGEGEVSGLMRKVPRVSLERLDLDLTSDSQPPVFKVFPGSTTEDYNLIVIERGAAAAAAGQAGTVPPGAPGAPPLPGMAIVKEEETEAAIGAPPAAPEGPETKPVLMALTEGPGAEGPRLASPSGSTSSGLEVVAPEVTSAPVSGPGILDDSATICRVCQKPGDLVMCNQCEFCFHLDCHLPSLQDVPGEEWSCSLCHVLPDLKEEDGSLSLDGADSTGVVAKLSPANQRKCERVLLALFCHEPCRPLHQLATDSTFSMEQPGGTLDLTLIRARLQEKLSPPYSSPQEFAQDVGRMFKQFNKLTEDKADVQSIIGLQRFFETRMNDAFGDTKFSAVLVEPPPLNLPSAGLSSQELSGPGDGP
2.3.2.27
null
chromatin organization [GO:0006325]; convergent extension involved in axis elongation [GO:0060028]; DNA repair [GO:0006281]; embryo implantation [GO:0007566]; embryonic placenta morphogenesis [GO:0060669]; epithelial to mesenchymal transition [GO:0001837]; genomic imprinting [GO:0071514]; in utero embryonic development [GO:0001701]; innate immune response [GO:0045087]; negative regulation of DNA demethylation [GO:1901536]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of single stranded viral RNA replication via double stranded DNA intermediate [GO:0045869]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of DNA methylation-dependent heterochromatin formation [GO:0090309]; positive regulation of DNA repair [GO:0045739]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of protein import into nucleus [GO:0042307]; post-fertilization epigenetic regulation of gene expression [GO:0043045]; protein sumoylation [GO:0016925]; suppression of viral release by host [GO:0044790]
chromatin [GO:0000785]; euchromatin [GO:0000791]; heterochromatin [GO:0000792]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; RNA polymerase II transcription regulator complex [GO:0090575]
chromatin binding [GO:0003682]; chromo shadow domain binding [GO:0070087]; DNA binding [GO:0003677]; Krueppel-associated box domain binding [GO:0035851]; promoter-specific chromatin binding [GO:1990841]; protein kinase activity [GO:0004672]; SUMO transferase activity [GO:0019789]; transcription coactivator activity [GO:0003713]; transcription corepressor activity [GO:0003714]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin protein ligase binding [GO:0031625]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270]
PF00628;PF00643;PF14634;
1.20.920.10;3.30.160.60;3.30.40.10;
TRIM/RBCC family
PTM: ATM-induced phosphorylation on Ser-825 represses sumoylation leading to the de-repression of expression of a subset of genes involved in cell cycle control and apoptosis in response to genotoxic stress. Dephosphorylation by the phosphatases, PPP1CA and PP1CB forms, allows sumoylation and expression of TRIM28 target genes. {ECO:0000250|UniProtKB:Q13263}.; PTM: Sumoylation/desumoylation events regulate TRIM28-mediated transcriptional repression. Sumoylation is required for interaction with CHD3 and SETDB1 and the corepressor activity. Represses and is repressed by Ser-824 phosphorylation. Enhances the TRIM28 corepressor activity, inhibiting transcriptional activity of a number of genes including GADD45A and CDKN1A/p21. Lys-555, Lys-780 and Lys-805 are the major sites of sumoylation. In response to Dox-induced DNA damage, enhanced phosphorylation on Ser-825 prevents sumoylation and allows de-repression of CDKN1A/p21. {ECO:0000250|UniProtKB:Q13263}.; PTM: Auto-ubiquitinated; enhanced by MAGEA2 and MAGEC2. {ECO:0000250|UniProtKB:Q13263}.; PTM: Citrullinated by PADI4. {ECO:0000250|UniProtKB:Q62318}.; PTM: ADP-ribosylated by SIRT6, promoting TRIM28/KAP1 interaction with CBX5, thereby contributing to the packaging of LINE-1 retrotransposon elements into transcriptionally repressive heterochromatin. {ECO:0000250|UniProtKB:Q62318}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q62318}. Note=Associated with centromeric heterochromatin during cell differentiation through CBX1 (By similarity). Localizes to sites of DNA damage (By similarity). {ECO:0000250|UniProtKB:Q13263, ECO:0000250|UniProtKB:Q62318}.
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27;
null
PATHWAY: Protein modification; protein sumoylation.
null
null
FUNCTION: Nuclear corepressor for KRAB domain-containing zinc finger proteins (KRAB-ZFPs). Mediates gene silencing by recruiting CHD3, a subunit of the nucleosome remodeling and deacetylation (NuRD) complex, and SETDB1 (which specifically methylates histone H3 at 'Lys-9' (H3K9me)) to the promoter regions of KRAB target genes. Enhances transcriptional repression by coordinating the increase in H3K9me, the decrease in histone H3 'Lys-9 and 'Lys-14' acetylation (H3K9ac and H3K14ac, respectively) and the disposition of HP1 proteins to silence gene expression. Recruitment of SETDB1 induces heterochromatinization. May play a role as a coactivator for CEBPB and NR3C1 in the transcriptional activation of ORM1. Also a corepressor for ERBB4. Inhibits E2F1 activity by stimulating E2F1-HDAC1 complex formation and inhibiting E2F1 acetylation. May serve as a partial backup to prevent E2F1-mediated apoptosis in the absence of RB1. Important regulator of CDKN1A/p21(CIP1). Has E3 SUMO-protein ligase activity toward itself via its PHD-type zinc finger. Also specifically sumoylates IRF7, thereby inhibiting its transactivation activity. Ubiquitinates p53/TP53 leading to its proteasomal degradation; the function is enhanced by MAGEC2 and MAGEA2, and possibly MAGEA3 and MAGEA6. Mediates the nuclear localization of KOX1, ZNF268 and ZNF300 transcription factors. In association with isoform 2 of ZFP90, is required for the transcriptional repressor activity of FOXP3 and the suppressive function of regulatory T-cells (Treg). Probably forms a corepressor complex required for activated KRAS-mediated promoter hypermethylation and transcriptional silencing of tumor suppressor genes (TSGs) or other tumor-related genes in colorectal cancer (CRC) cells. Required to maintain a transcriptionally repressive state of genes in undifferentiated embryonic stem cells (ESCs). In ESCs, in collaboration with SETDB1, is also required for H3K9me3 and silencing of endogenous and introduced retroviruses in a DNA-methylation independent-pathway. Associates at promoter regions of tumor suppressor genes (TSGs) leading to their gene silencing. The SETDB1-TRIM28-ZNF274 complex may play a role in recruiting ATRX to the 3'-exons of zinc finger genes with atypical chromatin signatures to establish or maintain/protect H3K9me3 at these transcriptionally active regions. {ECO:0000250|UniProtKB:Q13263, ECO:0000250|UniProtKB:Q62318}.
Rattus norvegicus (Rat)
O08638
MYH11_MOUSE
MAQKGQLSDDEKFLFVDKNFMNSPMAQADWVAKKLVWVPSEKQGFEAASIKEEKGDEVVVELVENGKKVTVGKDDIQKMNPPKFSKVEDMAELTCLNEASVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGESGAGKTENTQKVIQYLAVVASSHKGKKDSSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMKSDLLLESFNSYTFLSNGFVPIPAAQDDEMFQETLEAMSIMGFNEEEQLAILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLVGINVTDFTRAILTPRIKVGRDVVQKAQTKEQADFAIEALAKATYERLFRWILSRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPSIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCSEQGNHPKFQKPKQLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSLPSASKTKKGMFRTVGQLYKEQLGKLMATLRNTTANFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFRTGVLAHLEEERDLKITDVIMAFQAMCRGYLARKAFTKRQQQLTAMKVIQRNCAAYLKLRNWQWWRLFTKVKPLLQVTRQEEEMQAKEEEMQKITERQQKAETELKELEQKHTQLAEEKTLLQEQLQAETELYAESEEMRVRLAAKKQELEEILHEMEARLEEEEDRRQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDILVMDDQNSKLSKERKLLEERVSDLTTNLAEEEEKAKNLTKLKSKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDEEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQEVTVLKKALDEETRSHEAQVQEMRQKHTQAVEELTEQLEQFKRAKANLDKSKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEVQLQDLQSKCSDGERARAELSDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQKLNVSTKLRQLEDERNSLQDQLDEEMEAKQNLERHVSTLNIQLSDSKKKLQDFASTIEVMEEGKKRLQKEMEGLSQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEESEDDVQATEDAKLRLEVNMQALKGQFERDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELDDARASRDEIFATSKENEKKAKSLEADLMQLQEDLAAAERARKQADLEKEELAEELASSLSGRNTLQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATLQAEQLSNELATERSTAQKNESARQQLERQNKELRSKLQEVEGAVKAKLKSTVAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEVLLQVEDERKMAEQYKEQAEKGNTKVKQLKRQLEEAEEESQCINANRRKLQRELDEATESNEAMGREVNALKSKLRRGNEASFVPSRRAGGRRVIENTDGSEEEMDARDSDFNGTKASE
null
null
actomyosin structure organization [GO:0031032]; cardiac muscle cell development [GO:0055013]; elastic fiber assembly [GO:0048251]; skeletal muscle myosin thick filament assembly [GO:0030241]; smooth muscle contraction [GO:0006939]
brush border [GO:0005903]; cytoplasm [GO:0005737]; melanosome [GO:0042470]; muscle myosin complex [GO:0005859]; myofibril [GO:0030016]; myosin complex [GO:0016459]; myosin filament [GO:0032982]; myosin II complex [GO:0016460]; smooth muscle contractile fiber [GO:0030485]; stress fiber [GO:0001725]
actin filament binding [GO:0051015]; ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; cytoskeletal motor activity [GO:0003774]; microfilament motor activity [GO:0000146]; structural constituent of muscle [GO:0008307]
PF00063;PF02736;PF01576;
1.10.10.820;1.20.5.170;1.20.5.340;1.20.58.530;3.30.70.1590;6.10.250.2420;3.40.850.10;2.30.30.360;1.20.120.720;4.10.270.10;
TRAFAC class myosin-kinesin ATPase superfamily, Myosin family
null
SUBCELLULAR LOCATION: Melanosome {ECO:0000250}. Cytoplasm, myofibril. Note=Thick filaments of the myofibrils.
null
null
null
null
null
FUNCTION: Muscle contraction.
Mus musculus (Mouse)
O08644
EPHB6_MOUSE
MATEGTTGSGSRVVAGMVCSLWLLVLGSSVLALEEVLLDTTGETSEIGWLTYPPGGWDEVSVLDDQRRLTRTFEACHVAGLPPGSGQDNWLQTHFVERRGAQRAHIRLHFSVRACSSLGVSGGTCRETFTLYYRQADEPDGPDSIAAWHLKRWTKVDTIAADESFPASSSSSSWAVGPHRTGQRVGLQLNVKERSFGPLTQRGFYVAFQDTGACLALVAVKLFSYTCPSVLRAFASFPETQASGAGGASLVAAVGTCVAHAEPEEDGVGGQAGGSPPRLHCNGEGRWMVAVGGCRCQPGHQPARGDKLCQACPEGSYKALAGNVPCSPCPARSHSPDPAAPVCPCLQGFYRASSDPPEAPCTGPPSAPRELWFEVQGSALMLHWRLPQELGGRGDLLFNVVCKECGGHGEPSSGGMCRRCRDEVHFDPRQRGLTESRVLVGGLRAHVPYILEVQAVNGVSELSPDPPQAAAINVSTSHEVPSAVPVMHQVSRAANSITVSWPQPEQTNGNILDYQLRYYDQAEDESHSFTMTSETNTATVTRLSPGHIYGFQVRARTAAGHGPYGGKVYFQTLPQGELSSQLPEKLSLVIGSILGALAFLLLAAITVLAVIFQRKRRGTGYTEQLQQYSSPGLGVKYYIDPSTYDDPCQAIRELAREVDPTYIKIEEVIGAGSFGEVRRGRLQPRGRREQAVAIQALWAGGAESLKMTFLGRAALLGQFQHPNILRLEGVVTKSRPVMVLTELMELGPLDSFLRQREGQFSSLQLVAMQRGVAAAMQYLSSFAFVHRALSARSVLVNSHLVCKVARLGHSPQGSSSLLRWAAPEVITHGKYTTSSDVWSFGILMWEVMSYGERPYWDMNEQEVLNAIEQEFRLPPPPGCPPGLHLLMLDTWQKDRARRPHFDQLVAAFDKMIRKPDTLQAEGGSGDRPSQALLNPVALDFPCLDSPQAWLSAIGLECYQDNFSKFGLSTFSDVAQLSLEDLPGLGITLAGHQKKLLHNIQLLQQHLRQPGSVEV
null
null
activated T cell proliferation [GO:0050798]; axon guidance [GO:0007411]; ephrin receptor signaling pathway [GO:0048013]; positive regulation of T cell costimulation [GO:2000525]; T cell mediated immunity [GO:0002456]; type IV hypersensitivity [GO:0001806]
cell surface [GO:0009986]; dendrite [GO:0030425]; extracellular region [GO:0005576]; plasma membrane [GO:0005886]
ATP binding [GO:0005524]; transmembrane-ephrin receptor activity [GO:0005005]
PF14575;PF01404;PF07699;PF00041;PF07714;PF07647;
2.60.40.1770;2.60.120.260;2.60.40.10;1.10.150.50;1.10.510.10;2.10.50.10;
Protein kinase superfamily, Tyr protein kinase family, Ephrin receptor subfamily
PTM: Ligand-binding increases phosphorylation on tyrosine residues. Phosphorylation on tyrosine residues is mediated by transphosphorylation by the catalytically active EPHB1 in a ligand-independent manner. Tyrosine phosphorylation of the receptor may act as a switch on the functional transition from cell adhesion/attraction to de-adhesion/repulsion (By similarity). {ECO:0000250}.
SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted.; SUBCELLULAR LOCATION: [Isoform 3]: Secreted.
null
null
null
null
null
FUNCTION: Kinase-defective receptor for members of the ephrin-B family. Binds to ephrin-B1 and ephrin-B2. Modulates cell adhesion and migration by exerting both positive and negative effects upon stimulation with ephrin-B2. Inhibits JNK activation, T-cell receptor-induced IL-2 secretion and CD25 expression upon stimulation with ephrin-B2 (By similarity). {ECO:0000250}.
Mus musculus (Mouse)
O08648
M3K4_MOUSE
MRDAIAEPVPPPALADTPAAAMEELRPAPPPQPEPDPECCPAARQECMLGESARKSMESDPEDFSDETNTETLYGTSPPSTPRQMKRLSAKHQRNSAGRPASRSNLKEKMNTPSQSPHKDLGKGVETVEEYSYKQEKKIRATLRTTERDHKKNAQCSFMLDSVAGSLPKKSIPDVDLNKPYLSLGCSNAKLPVSMPMPIARTARQTSRTDCPADRLKFFETLRLLLKLTSVSKKKDREQRGQENTAAFWFNRSNELIWLELQAWHAGRTINDQDLFLYTARQAIPDIINEILTFKVNYGSIAFSSNGAGFNGPLVEGQCRTPQETNRVGCSSYHEHLQRQRVSFEQVKRIMELLEYMEALYPSLQALQKDYERYAAKDFEDRVQALCLWLNITKDLNQKLRIMGTVLGIKNLSDIGWPVFEIPSPRPSKGYEPEDEVEDTEVELRELESGTEESDEEPTPSPRVPELRLSTDAILDSRSQGCVSRKLERLESEEDSIGWGTADCGPEASRHCLTSIYRPFVDKALKQMGLRKLILRLHKLMNGSLQRARVALVKDDRPVEFSDFPGPMWGSDYVQLSGTPPSSEQKCSAVSWEELRAMDLPSFEPAFLVLCRVLLNVIHECLKLRLEQRPAGEPSLLSIKQLVRECKEVLKGGLLMKQYYQFMLQEVLGGLEKTDCNMDAFEEDLQKMLMVYFDYMRSWIQMLQQLPQASHSLKNLLEEEWNFTKEITHYIRGGEAQAGKLFCDIAGMLLKSTGSFLESGLQESCAELWTSADDNGAADELRRSVIEISRALKELFHEARERASKALGFAKMLRKDLEIAAEFVLSASARELLDALKAKQYVKVQIPGLENLHVFVPDSLAEEKKIILQLLNAATGKDCSKDPDDVFMDAFLLLTKHGDRARDSEDGWGTWEARAVKIVPQVETVDTLRSMQVDNLLLVVMESAHLVLQRKAFQQSIEGLMTVRHEQTSSQPIIAKGLQQLKNDALELCNRISDAIDRVDHMFTLEFDAEVEESESATLQQYYREAMIQGYNFGFEYHKEVVRLMSGEFRQKIGDKYISFAQKWMNYVLTKCESGRGTRPRWATQGFDFLQAIEPAFISALPEDDFLSLQALMNECIGHVIGKPHSPVTAIHRNSPRPVKVPRCHSDPPNPHLIIPTPEGFSTRSVPSDARTHGNSVAAAAAVAAAATTAAGRPGPGGGDSVPAKPVNTAPDTRGSSVPENDRLASIAAELQFRSLSRHSSPTEERDEPAYPRSDSSGSTRRSWELRTLISQTKDSASKQGPIEAIQKSVRLFEERRYREMRRKNIIGQVCDTPKSYDNVMHVGLRKVTFKWQRGNKIGEGQYGKVYTCISVDTGELMAMKEIRFQPNDHKTIKETADELKIFEGIKHPNLVRYFGVELHREEMYIFMEYCDEGTLEEVSRLGLQEHVIRLYTKQITVAINVLHEHGIVHRDIKGANIFLTSSGLIKLGDFGCSVKLKNNAQTMPGEVNSTLGTAAYMAPEVITRAKGEGHGRAADIWSLGCVVIEMVTGKRPWHEYEHNFQIMYKVGMGHKPPIPERLSPEGKAFLSHCLESDPKIRWTASQLLDHAFVKVCTDEE
2.7.11.25
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
chorionic trophoblast cell differentiation [GO:0060718]; intracellular signal transduction [GO:0035556]; male germ-line sex determination [GO:0019100]; p38MAPK cascade [GO:0038066]; phosphorylation [GO:0016310]; placenta development [GO:0001890]; positive regulation of JUN kinase activity [GO:0043507]; positive regulation of p38MAPK cascade [GO:1900745]; positive regulation of telomere capping [GO:1904355]; positive regulation of telomere maintenance via telomerase [GO:0032212]; regulation of gene expression [GO:0010468]; response to UV-C [GO:0010225]
cytoplasm [GO:0005737]; perinuclear region of cytoplasm [GO:0048471]
ATP binding [GO:0005524]; MAP kinase kinase kinase activity [GO:0004709]; metal ion binding [GO:0046872]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]
PF19431;PF00069;
1.10.510.10;
Protein kinase superfamily, STE Ser/Thr protein kinase family, MAP kinase kinase kinase subfamily
null
SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:16157600}. Note=Localized in perinuclear vesicular-like structures, probably Golgi-associated vesicles.
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.25; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.25;
null
null
null
null
FUNCTION: Component of a protein kinase signal transduction cascade. Activates the CSBP2, P38 and JNK MAPK pathways, but not the ERK pathway. Specifically phosphorylates and activates MAP2K4 and MAP2K6. {ECO:0000269|PubMed:16157600, ECO:0000269|PubMed:9079650}.
Mus musculus (Mouse)
O08650
HYAS3_MOUSE
MPVQLTTALRVVGTSLFALVVLGGILAAYVTGYQFIHTEKHYLSFGLYGAILGLHLLIQSLFAFLEHRRMRRAGRPLKLHCSQRPRSVALCIAAYQEDPEYLRKCLRSAQRIAFPNLKVVMVVDGNRQEDTYMLDIFHEVLGGTEQAGFFVWRSNFHEAGEGETEASLQEGMERVRAVVWASTFSCIMQKWGGKREVMYTAFKALGNSVDYIQVCDSDTVLDPACTIEMLRVLEEDPQVGGVGGDVQILNKYDSWISFLSSVRYWMAFNVERACQSYFGCVQCISGPLGMYRNSLLQQFLEDWYHQKFLGSKCSFGDDRHLTNRVLSLGYRTKYTARSKCLTETPTRYLRWLNQQTRWSKSYFREWLYNSLWFHKHHLWMTYESVVTGFFPFFLIATVIQLFYRGRIWNILLFLLTVQLVGIIKATYACFLRGNAEMIFMSLYSLLYMSSLLPAKIFAIATINKSGWGTSGRKTIVVNFIGLIPVSIWVAVLLGGLAYTAYCQDLFSETELAFLVSGAILYGCYWVALLMLYLAIIARRCGKKPEQYSLAFAEV
2.4.1.212
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
extracellular matrix assembly [GO:0085029]; extracellular polysaccharide biosynthetic process [GO:0045226]; hyaluronan biosynthetic process [GO:0030213]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of hyaluranon cable assembly [GO:1900106]
cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; Golgi membrane [GO:0000139]; hyaluranon cable [GO:0036117]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
hyaluronan synthase activity [GO:0050501]; identical protein binding [GO:0042802]
PF13641;
null
NodC/HAS family
PTM: O-GlcNAcylation increases the hyaluronan synthase activity, HAS3 stability and its plasma membrane residence. The concentration of UDP-GlcNAc controls the level of O-GlcNAc modification. {ECO:0000250|UniProtKB:O00219}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10455188, ECO:0000269|PubMed:16014622}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:16014622}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:16014622}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle {ECO:0000269|PubMed:16014622}. Note=Travels through endoplasmic reticulum (ER), Golgi, plasma membrane, and endocytic vesicles (PubMed:16014622). Actives only when present in plasma membrane (PubMed:16014622). O-GlcNAcylation controls its membrane localization (By similarity). A rapid recycling of HAS3 between plasma membrane and endosomes is controlled by the cytosolic levels of UDP-GlcUA and UDP-GlcNAc (By similarity). {ECO:0000250|UniProtKB:O00219, ECO:0000269|PubMed:16014622}.
CATALYTIC ACTIVITY: Reaction=[hyaluronan](n) + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N-acetyl-beta-D-glucosaminyl-(1->4)-[hyaluronan](n) + UDP; Xref=Rhea:RHEA:20465, Rhea:RHEA-COMP:12583, Rhea:RHEA-COMP:12585, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:132153, ChEBI:CHEBI:132154; EC=2.4.1.212; Evidence={ECO:0000269|PubMed:10455188, ECO:0000269|PubMed:16014622}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20466; Evidence={ECO:0000269|PubMed:10455188}; CATALYTIC ACTIVITY: Reaction=N-acetyl-beta-D-glucosaminyl-(1->4)-[hyaluronan](n) + UDP-alpha-D-glucuronate = [hyaluronan](n+1) + H(+) + UDP; Xref=Rhea:RHEA:12528, Rhea:RHEA-COMP:12585, Rhea:RHEA-COMP:12587, ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:132153, ChEBI:CHEBI:132154; EC=2.4.1.212; Evidence={ECO:0000269|PubMed:10455188, ECO:0000269|PubMed:16014622}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12529; Evidence={ECO:0000269|PubMed:10455188};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.2 mM for UDP-Glc-NAc (at pH 7.1 and 37 degrees Celsius, in the presence of 15 mM MgCl2) {ECO:0000269|PubMed:10455188}; KM=0.3 mM for UDP-Glc-UA (at pH 7.1 and 37 degrees Celsius, in the presence of 15 mM MgCl2) {ECO:0000269|PubMed:10455188};
PATHWAY: Glycan biosynthesis; hyaluronan biosynthesis. {ECO:0000269|PubMed:10455188, ECO:0000269|PubMed:16014622}.
null
null
FUNCTION: Catalyzes the addition of GlcNAc or GlcUA monosaccharides to the nascent hyaluronan polymer. Therefore, it is essential to hyaluronan synthesis a major component of most extracellular matrices that has a structural role in tissues architectures and regulates cell adhesion, migration and differentiation. This is one of three isoenzymes responsible for cellular hyaluronan synthesis. {ECO:0000269|PubMed:10455188, ECO:0000269|PubMed:16014622}.
Mus musculus (Mouse)
O08651
SERA_RAT
MAFANLRKILISDSLDPCCRKILQDGGLQVVEKQNLSKEELIAELQDCEGLIVRSATKVTADVINAAEKLQVVGRAGTGVDNVDLEAATRKGVLVMNTPNGNSLSAAELTCGMLMCLARQIPQATASMKDGKWDRKKFMGTELNGKTLGILGLGRIGREVAARMQAFGMKTVGYDPIISPEVAASFGVQQLPLEEIWPLCDFITVHTPLLPSTTGLLNDSTFAQCKKGVRVVNCARGGIVDEGALLRALQSGQCAGAALDVFTEEPPRDRALVDHENVISCPHLGASTKEAQSRCGEEIAVQFVDMVKGKSLTGVVNAQALTSAFSPHTKPWIGLAEALGTLMHAWAGSPKGTIQVVTQGTSLKNAGTCLSPAVIVGLLREASKQADVNLVNAKLLVKEAGLNVTTSHSPGVPGEQGIGECLLTVALAGAPYQAVGLVQGTTPMLQMLNGAVFRPEVPLRRGQPLLLFRAQPSDPVMLPTMIGLLAEAGVQLLSYQTSKVSDGDTWHVMGLSSLLPSLDAWKQHVSEAFQFCF
1.1.1.95
null
G1 to G0 transition [GO:0070314]; gamma-aminobutyric acid metabolic process [GO:0009448]; glial cell development [GO:0021782]; glutamine metabolic process [GO:0006541]; glycine metabolic process [GO:0006544]; L-serine biosynthetic process [GO:0006564]; L-serine metabolic process [GO:0006563]; neural tube development [GO:0021915]; neurogenesis [GO:0022008]; neuron projection development [GO:0031175]; regulation of gene expression [GO:0010468]; serine family amino acid biosynthetic process [GO:0009070]; spinal cord development [GO:0021510]; taurine metabolic process [GO:0019530]; threonine metabolic process [GO:0006566]
null
NAD binding [GO:0051287]; phosphoglycerate dehydrogenase activity [GO:0004617]
PF00389;PF02826;PF19304;
3.40.50.720;
D-isomer specific 2-hydroxyacid dehydrogenase family
null
null
CATALYTIC ACTIVITY: Reaction=(2R)-3-phosphoglycerate + NAD(+) = 3-phosphooxypyruvate + H(+) + NADH; Xref=Rhea:RHEA:12641, ChEBI:CHEBI:15378, ChEBI:CHEBI:18110, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58272; EC=1.1.1.95; Evidence={ECO:0000269|PubMed:9163325};
null
PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 1/3. {ECO:0000269|PubMed:9163325}.
null
null
FUNCTION: Catalyzes the reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L-serine biosynthesis pathway. Does not catalyze the reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate and the reversible oxidation of (S)-malate to oxaloacetate. {ECO:0000269|PubMed:9163325}.
Rattus norvegicus (Rat)
O08656
HXA1_RAT
MDNARLNSFLEYPILGSGDSGTCSARVYSSDHGITTFQSCAVSANSCGGDDRFLGGRGVQITSPHHHHHHHHHPQPATYQTSGNLGVSYSHSSCGPSYGAQNFSAPYGPYGLNQEADVSGGYPPCAPAVYSGNLSSPMVQHHHHHQGYAGGTVGSPQYIHHSYGQEHQSLALATYNNSLSPLHASHQEACRSPASETSSPAQTFDWMKVKRNPPKTGKVGEYGYVGQPNAVRTNFTTKQLTELEKEFHFNKYLTRARSEIAASLQLNETQVKIWFQNRRMKQKKREKEGLLPMSPATPPGSDEKTEESSEKSSSSPSAPSPASSTSDTLTTSH
null
null
abducens nerve formation [GO:0021599]; anatomical structure formation involved in morphogenesis [GO:0048646]; anatomical structure morphogenesis [GO:0009653]; anterior/posterior pattern specification [GO:0009952]; artery development [GO:0060840]; artery morphogenesis [GO:0048844]; cellular response to ethanol [GO:0071361]; cellular response to retinoic acid [GO:0071300]; central nervous system neuron differentiation [GO:0021953]; cochlea development [GO:0090102]; cochlea morphogenesis [GO:0090103]; cognition [GO:0050890]; embryonic neurocranium morphogenesis [GO:0048702]; facial nerve structural organization [GO:0021612]; facial nucleus development [GO:0021754]; hindbrain development [GO:0030902]; inner ear development [GO:0048839]; inner ear morphogenesis [GO:0042472]; motor neuron axon guidance [GO:0008045]; nervous system development [GO:0007399]; neuromuscular process [GO:0050905]; optokinetic behavior [GO:0007634]; outer ear morphogenesis [GO:0042473]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of behavior [GO:0050795]; regulation of transcription by RNA polymerase II [GO:0006357]; rhombomere 3 development [GO:0021569]; rhombomere 4 development [GO:0021570]; rhombomere 5 development [GO:0021571]; semicircular canal formation [GO:0060876]; sensory perception of sound [GO:0007605]
nucleus [GO:0005634]
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; identical protein binding [GO:0042802]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]; sequence-specific double-stranded DNA binding [GO:1990837]
PF00046;
1.10.10.60;
Antp homeobox family, Labial subfamily
PTM: Glycosylated by OGT. {ECO:0000250|UniProtKB:P09022}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
null
null
null
null
null
FUNCTION: Sequence-specific transcription factor (By similarity). Regulates multiple developmental processes including brainstem, inner and outer ear, abducens nerve and cardiovascular development and morphogenesis as well as cognition and behavior (By similarity). Also part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Acts on the anterior body structures. Seems to act in the maintenance and/or generation of hindbrain segments (By similarity). Activates transcription in the presence of PBX1A and PKNOX1 (By similarity). {ECO:0000250|UniProtKB:P09022, ECO:0000250|UniProtKB:P49639, ECO:0000250|UniProtKB:Q90423}.
Rattus norvegicus (Rat)
O08662
PI4KA_RAT
MAAAGARGTGGSGSSSGSSTSRGFYFNTVLSLARSLAVQRPASLEKVQKLLCMCPVDFHGIFQLDERRRDAVIALGIFLIESDLQHKDCIVPYLLRLLRGLPKVYWVEESTARKGRGNLPVAESFSFCLVTLLSDVACRDPSLRDEILEALLQVLHVLLGMCQALEIQEKEYLCKYAIPCLIGISRSFGRYSNSEESLLSKLFPKVPPHSLRIPEELEGVRRRSFNDFRSILPSNLLTVCQEGTLKRKTSSVSSISQVSPERGMPPPSSPGGSAFHYFEASCLPDGTTLEPEYYFSTISSSFSVSPLFNGITYKEFYIPLEMLRELLNLVKKIVEEPVLKSLDAAVARVMEANPSADLYYTTFSDPVYLTMFKMLRDTLYYMKDLPTSFVKEIHDFVLEQFNMSQGELQKILHDADRIHSEMSPLKLRCQANAACVDLMVWAVKDEQGAENLCIKLSEKLQSKTSSKVIIAHLPLLICCLQGLGRLCERFPVVVHSVTPSLRDFLVIPSPVLVKLYKYHSQYHTVAGSDIKISVTNEHSESTLNVLPGKKNQPSMYEQLRDIAIDNICRCLKAGLTVDPVIVEAFLASLSNRLYISQESDKDAHLIPDHTIRALGHIAVALRDTPKVMEPILQILQQKFCQPPSPLDVLIIDQLGCLVITGNQYIYQEVWNLFQQISVKASSVVYSATKDYKDHGYRHCSLAVINALANIAANIQEEHLVDELLMNLLELFVQLGLEGKRASERASEKGPALKASSSAGNLGVLIPVIAVLTRRLPPIKEAKPRLQKLFRDFWLYSVLMGFAVEGSGLWPEEWYEGVCEIATKSPLLTFPSKEPLRSVLQYNSAMKNDTVTPAELNELRSTIINLLDPPPEVSALINKLDFAMSTYLLSVYRLEYMRVLRSTDPDRFQVMFCYFEDKAIQKDKSGMMQCVIAVADKVFDAFLNMMAEKAKTKENEEELERHAQFLLVNFNHIHKRIRRVADKYLSGLVDKFPHLLWSGTVLKTMLDILQTLSLSLSADIHKDQPYYDIPDAPYRITVPDTYEARESIVKDFAARCGMILQEAMKWAPTVTKSHLQEYLNKHQNWVSGLSQHTGLAMATESILHFAGYNKQNTTLGVTQLTERPACVKKDYSNFMASLNLRNRYAGEVHGMIRFSGATGQMSDLNKMMVQDLITALDHSHPQHYTQAMFKLTAMLISSKDCDPQLLHHLCWGPLRMFNEHGMETALACWEWLLAGKNGVEVPFMREMAGAWHMTVEQKFGLFSAETKEADPLAASEASQPRPCPPEVTPHYIWIDFLVQRFEIAKYCSSDQVEIFSSLLQRSMSLHIGGARGSMNRHVAAIGPRFKLLTLGLSLLHADVVPNATIRNVLREKIYSTAFDYFSCPPKFPTQGEKRLREDISIMIKFWTAMFSDKKYLTASQLVPPDNQDTRSNLDITVGSRQQATQGWINTYPLSSGMSTISKKSGMSKKTNRGSQLHKYYMKRRTLLLSLLATEIERLITWYNPLSAPELELDQAGENSVANWRSKYISLSEKQWKDNVNLAWTISPYLAVQLPARFKNTEAIGNEVTRLVRLDPGAVSDVPEAIKFLVTWHTIDADAPELSHVLCWAPTDPPTGLSYFSSMYPPHPLTAQYGVKVLRSFPPDAILFYIPQIVQALRYDKMGYVREYILWAAAKSQLLAHQFIWNMKTNIYLDEEGHQKDPDIGDLLEQLVEEITGSLSGPAKDFYQREFDFFNKITNVSAIIKPYPKGDERKKACLSALSEVKVQPGCYLPSNPEAIVLDIDYKSGTPMQSAAKAPYLAKFKVKRCGVSELEKEGLQCRSDTEDECRRQEADGKKICWQAAIFKVGDDCRQDMLALQIIDLFKNIFQLVGLDLFVFPYRVVATAPGCGVIECIPDCTSRDQLGRQTDFGMYDYFTRQYGDESTLAFQQARYNFIRSMAAYSLLLFLLQIKDRHNGNIMLDKKGHIIHIDFGFMFESSPGGNLGWEPDIKLTDEMVMIMGGKMEATPFKWFMEMCVRGYLAVRPYMDAVVSLVTLMLDTGLPCFRGQTIKLLKHRFSPNMTEREAANFIMKIIQNCFLSNRSRTYDMIQYYQNDIPY
2.7.1.67
null
modulation by host of viral process [GO:0044788]; phosphatidylinositol phosphate biosynthetic process [GO:0046854]; phosphatidylinositol-mediated signaling [GO:0048015]; phosphorylation [GO:0016310]; reorganization of cellular membranes to establish viral sites of replication [GO:0140754]
cytoplasm [GO:0005737]; Golgi-associated vesicle membrane [GO:0030660]; plasma membrane [GO:0005886]
1-phosphatidylinositol 4-kinase activity [GO:0004430]; ATP binding [GO:0005524]; kinase activity [GO:0016301]
PF00454;PF00613;PF19274;
1.10.1070.11;1.25.40.70;
PI3/PI4-kinase family, Type III PI4K subfamily
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P42356}. Cell membrane {ECO:0000250|UniProtKB:P42356}. Note=Localization to the plasma membrane is mediated by the PI4K complex and association with EFR3 (EFR3A or EFR3B), TTC7 (TTC7A or TTC7B) and HYCC (HYCC1 or HYCC2). Localization to the plasma membrane is regulated by TMEM150A. {ECO:0000250|UniProtKB:P42356}.
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ADP + H(+); Xref=Rhea:RHEA:19877, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57880, ChEBI:CHEBI:58178, ChEBI:CHEBI:456216; EC=2.7.1.67; Evidence={ECO:0000269|PubMed:8662589};
null
null
null
null
FUNCTION: Acts on phosphatidylinositol (PtdIns) in the first committed step in the production of the second messenger inositol-1,4,5,-trisphosphate. {ECO:0000269|PubMed:8662589}.
Rattus norvegicus (Rat)
O08663
MAP2_MOUSE
MAGVEQAASFGGHLNGDLDPDDREEGTSSTAEEAAKKKRRKKKKGKGAVSAVQQELDKESGALVDEVAKQLESQALEEKERDDDDEDGDGDADGATGKKKKKKKKKRGPKVQTDPPSVPICDLYPNGVFPKGQECEYPPTQDGRTAAWRTTSEEKKALDQASEEIWNDFREAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDCSRKLIKENGLNAGLAFPTGCSLNNCAAHYTPNAGDTTVLQYDDICKIDFGTHISGRIIDCAFTVTFNPKYDILLTAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYEVEIDGKTYQVKPIRNLNGHSIGPYRIHAGKTVPIVKGGEATRMEEGEVYAIETFGSTGKGVVHDDMECSHYMKNFDVGHVPIRLPRTKHLLNVINENFGTLAFCRRWLDRLGESKYLMALKNLCDLGIVDPYPPLCDIKGSYTAQFEHTILLRPTCKEVVSRGDDY
3.4.11.18
COFACTOR: Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000255|HAMAP-Rule:MF_03175}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_03175}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP-Rule:MF_03175}; Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000255|HAMAP-Rule:MF_03175}; Note=Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site. {ECO:0000255|HAMAP-Rule:MF_03175};
N-terminal protein amino acid modification [GO:0031365]; peptidyl-methionine modification [GO:0018206]; protein processing [GO:0016485]
cytoplasm [GO:0005737]
aminopeptidase activity [GO:0004177]; initiator methionyl aminopeptidase activity [GO:0004239]; metal ion binding [GO:0046872]; metalloaminopeptidase activity [GO:0070006]; metalloexopeptidase activity [GO:0008235]
PF00557;
3.90.230.10;1.10.10.10;
Peptidase M24A family, Methionine aminopeptidase eukaryotic type 2 subfamily
PTM: Contains approximately 12 O-linked N-acetylglucosamine (GlcNAc) residues. O-glycosylation is required for EIF2S1 binding. {ECO:0000255|HAMAP-Rule:MF_03175}.
SUBCELLULAR LOCATION: Cytoplasm. Note=About 30% of expressed METAP2 associates with polysomes. {ECO:0000255|HAMAP-Rule:MF_03175}.
CATALYTIC ACTIVITY: Reaction=Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.; EC=3.4.11.18; Evidence={ECO:0000255|HAMAP-Rule:MF_03175};
null
null
null
null
FUNCTION: Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). {ECO:0000255|HAMAP-Rule:MF_03175}.; FUNCTION: Protects eukaryotic initiation factor EIF2S1 from translation-inhibiting phosphorylation by inhibitory kinases such as EIF2AK2/PKR and EIF2AK1/HCR. Plays a critical role in the regulation of protein synthesis. {ECO:0000255|HAMAP-Rule:MF_03175}.
Mus musculus (Mouse)
O08665
SEM3A_MOUSE
MGWFTGIACLFWGVLLTARANYANGKNNVPRLKLSYKEMLESNNVITFNGLANSSSYHTFLLDEERSRLYVGAKDHIFSFNLVNIKDFQKIVWPVSYTRRDECKWAGKDILKECANFIKVLEAYNQTHLYACGTGAFHPICTYIEVGHHPEDNIFKLQDSHFENGRGKSPYDPKLLTASLLIDGELYSGTAADFMGRDFAIFRTLGHHHPIRTEQHDSRWLNDPRFISAHLIPESDNPEDDKVYFFFRENAIDGEHSGKATHARIGQICKNDFGGHRSLVNKWTTFLKARLICSVPGPNGIDTHFDELQDVFLMNSKDPKNPIVYGVFTTSSNIFKGSAVCMYSMSDVRRVFLGPYAHRDGPNYQWVPYQGRVPYPRPGTCPSKTFGGFDSTKDLPDDVITFARSHPAMYNPVFPINNRPIMIKTDVNYQFTQIVVDRVDAEDGQYDVMFIGTDVGTVLKVVSVPKETWHDLEEILLEEMTVFREPTTISAMELSTKQQQLYIGSTAGVAQLPLHRCDIYGKACAECCLARDPYCAWDGSSCSRYFPTAKRRTRRQDIRNGDPLTHCSDLQHHDNHHGPSLEERIIYGVENSSTFLECSPKSQRALVYWQFQRRNEDRKEEIRMGDHIIRTEQGLLLRSLQKKDSGNYLCHAVEHGFMQTLLKVTLEVIDTEHLEELLHKDDDGDGSKIKEMSSSMTPSQKVWYRDFMQLINHPNLNTMDEFCEQVWKRDRKQRRQRPGHSQGSSNKWKHMQESKKGRNRRTHEFERAPRSV
null
null
axon extension [GO:0048675]; axon extension involved in axon guidance [GO:0048846]; axon guidance [GO:0007411]; axonal fasciculation [GO:0007413]; axonogenesis involved in innervation [GO:0060385]; basal dendrite arborization [GO:0150020]; branchiomotor neuron axon guidance [GO:0021785]; dendrite morphogenesis [GO:0048813]; dichotomous subdivision of terminal units involved in salivary gland branching [GO:0060666]; epithelial cell migration [GO:0010631]; facial nerve structural organization [GO:0021612]; facioacoustic ganglion development [GO:1903375]; gonadotrophin-releasing hormone neuronal migration to the hypothalamus [GO:0021828]; maintenance of synapse structure [GO:0099558]; motor neuron axon guidance [GO:0008045]; negative chemotaxis [GO:0050919]; negative regulation of axon extension [GO:0030517]; negative regulation of axon extension involved in axon guidance [GO:0048843]; negative regulation of epithelial cell migration [GO:0010633]; nerve development [GO:0021675]; nervous system development [GO:0007399]; neural crest cell migration [GO:0001755]; neural crest cell migration involved in autonomic nervous system development [GO:1901166]; neural crest cell migration involved in sympathetic nervous system development [GO:1903045]; neuron migration [GO:0001764]; olfactory bulb development [GO:0021772]; positive regulation of male gonad development [GO:2000020]; positive regulation of neuron migration [GO:2001224]; regulation of axon extension involved in axon guidance [GO:0048841]; regulation of heart rate [GO:0002027]; semaphorin-plexin signaling pathway [GO:0071526]; sympathetic ganglion development [GO:0061549]; sympathetic neuron projection extension [GO:0097490]; sympathetic neuron projection guidance [GO:0097491]; synaptic target recognition [GO:0008039]; trigeminal ganglion development [GO:0061551]; trigeminal nerve structural organization [GO:0021637]; ventral trunk neural crest cell migration [GO:0036486]
axon [GO:0030424]; cerebellar climbing fiber to Purkinje cell synapse [GO:0150053]; dendrite [GO:0030425]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; glutamatergic synapse [GO:0098978]; plasma membrane [GO:0005886]
chemorepellent activity [GO:0045499]; neuropilin binding [GO:0038191]; semaphorin receptor binding [GO:0030215]
PF18452;PF01403;
2.60.40.10;3.30.1680.10;2.130.10.10;
Semaphorin family
null
SUBCELLULAR LOCATION: Secreted.
null
null
null
null
null
FUNCTION: Plays a role in growth cones guidance. May function to pattern sensory projections by selectively repelling axons that normally terminate dorsally. Involved in the development of the olfactory system and in neuronal control of puberty (By similarity). {ECO:0000250}.
Mus musculus (Mouse)
O08674
RBPJL_MOUSE
MDPRETTDPSLPPGPLTHLSLPDSSEVRLQSDGPSLLGSWTRSPPEHAIILREGVRTCLQQRCEQTVWILHAKVAQKSYGNEKRFFCPPPCVYLAGPGWRVKPMQDQALQSAETGPTVCGYMGLDGASGSAPETQKLNFEEQPDSREFGCAKTLYISDADKRKHFRLVLRLVLRGGQELGTFHSRLIKVISKPSQKKQSLKNTDLCISSGSKVSLFNRLRSQTVSTRYLSVEDGAFVASARQWAAFTLHLADGHCSQGDFPPQEGYIRYGSLVQLVCTVTGITLPPMIIRKVAKQCALLDVDEPISQLHKCAFQFPSDTPGGAGTYLCLATEKVVRFQASLCPKEANRALLNDSSCWTIIGTESVEFTFSTSLACTREPVTPVPLISTLELSGGGDVATLELHGENFHAGLKVWFGDVEAETMYRSPRSLVCVVPDVAAFGSDWRWLRTPITVPVSLLRADALFYPSPFSFTYTPEYSALPRLPNAQEPAPDADTLLESIHHEFTRTNFHLFCPT
null
null
positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription by RNA polymerase II [GO:0045944]
nucleus [GO:0005634]; transcription regulator complex [GO:0005667]
chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]
PF09270;PF09271;PF20144;
2.80.10.50;2.60.40.10;2.60.40.1450;
Su(H) family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9111338}.
null
null
null
null
null
FUNCTION: Putative transcription factor, which cooperates with EBNA2 to activate transcription.
Mus musculus (Mouse)