ACSM4_RAT
ID ACSM4_RAT Reviewed; 580 AA.
AC Q7TN78;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Acyl-coenzyme A synthetase ACSM4, mitochondrial;
DE EC=6.2.1.2 {ECO:0000269|PubMed:12709059};
DE AltName: Full=Olfactory specific medium-chain acyl CoA synthetase {ECO:0000303|PubMed:12709059};
DE Short=O-MACS {ECO:0000303|PubMed:12709059};
DE Flags: Precursor;
GN Name=Acsm4; Synonyms=Omacs {ECO:0000303|PubMed:12709059};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC STRAIN=Wistar; TISSUE=Olfactory epithelium;
RX PubMed=12709059; DOI=10.1046/j.1432-1033.2003.03571.x;
RA Oka Y., Kobayakawa K., Nishizumi H., Miyamichi K., Hirose S., Tsuboi A.,
RA Sakano H.;
RT "O-MACS, a novel member of the medium-chain acyl-CoA synthetase family,
RT specifically expressed in the olfactory epithelium in a zone-specific
RT manner.";
RL Eur. J. Biochem. 270:1995-2004(2003).
CC -!- FUNCTION: Catalyzes the activation of fatty acids by CoA to produce an
CC acyl-CoA, the first step in fatty acid metabolism (PubMed:12709059).
CC Capable of activating medium-chain fatty acids with a preference for
CC C6-12 fatty acids (PubMed:12709059). {ECO:0000269|PubMed:12709059}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a medium chain fatty acid + ATP + CoA = a medium-chain fatty
CC acyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:48340,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:59558, ChEBI:CHEBI:90546, ChEBI:CHEBI:456215; EC=6.2.1.2;
CC Evidence={ECO:0000269|PubMed:12709059};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48341;
CC Evidence={ECO:0000305|PubMed:12709059};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + hexanoate = AMP + diphosphate + hexanoyl-CoA;
CC Xref=Rhea:RHEA:43740, ChEBI:CHEBI:17120, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:62620,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:12709059};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43741;
CC Evidence={ECO:0000305|PubMed:12709059};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + octanoate = AMP + diphosphate + octanoyl-CoA;
CC Xref=Rhea:RHEA:33631, ChEBI:CHEBI:25646, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57386,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:12709059};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33632;
CC Evidence={ECO:0000305|PubMed:12709059};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + decanoate = AMP + decanoyl-CoA + diphosphate;
CC Xref=Rhea:RHEA:33627, ChEBI:CHEBI:27689, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:61430,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:12709059};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33628;
CC Evidence={ECO:0000305|PubMed:12709059};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + dodecanoate = AMP + diphosphate + dodecanoyl-CoA;
CC Xref=Rhea:RHEA:33623, ChEBI:CHEBI:18262, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:12709059};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33624;
CC Evidence={ECO:0000305|PubMed:12709059};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q08AH1};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q08AH1};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:12709059}.
CC -!- TISSUE SPECIFICITY: Detected in adult olfactory epithelium.
CC {ECO:0000269|PubMed:12709059}.
CC -!- DEVELOPMENTAL STAGE: Detected in all cell layers of the dorso-medial
CC part of the embryonic olfactory placode and olfactory epithelium. First
CC detected in olfactory placode on embryonic day 11.5. Detected in
CC olfactory placode on embryonic day 12, 14, 16 and 18.
CC {ECO:0000269|PubMed:12709059}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AB096688; BAC77614.1; -; mRNA.
DR RefSeq; NP_859046.1; NM_181695.1.
DR RefSeq; XP_017444802.1; XM_017589313.1.
DR AlphaFoldDB; Q7TN78; -.
DR SMR; Q7TN78; -.
DR STRING; 10116.ENSRNOP00000031354; -.
DR SwissLipids; SLP:000001211; -.
DR PaxDb; Q7TN78; -.
DR PRIDE; Q7TN78; -.
DR Ensembl; ENSRNOT00000034610; ENSRNOP00000031354; ENSRNOG00000014726.
DR GeneID; 353317; -.
DR KEGG; rno:353317; -.
DR UCSC; RGD:727928; rat.
DR CTD; 341392; -.
DR RGD; 727928; Acsm4.
DR eggNOG; KOG1175; Eukaryota.
DR GeneTree; ENSGT00940000162316; -.
DR HOGENOM; CLU_000022_59_10_1; -.
DR InParanoid; Q7TN78; -.
DR OMA; GPVGCRY; -.
DR OrthoDB; 683933at2759; -.
DR PhylomeDB; Q7TN78; -.
DR TreeFam; TF354287; -.
DR Reactome; R-RNO-177128; Conjugation of salicylate with glycine.
DR Reactome; R-RNO-9749641; Aspirin ADME.
DR PRO; PR:Q7TN78; -.
DR Proteomes; UP000002494; Chromosome 1.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0047760; F:butyrate-CoA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0102391; F:decanoate-CoA ligase activity; IDA:UniProtKB.
DR GO; GO:0015645; F:fatty acid ligase activity; IDA:UniProtKB.
DR GO; GO:0004321; F:fatty-acyl-CoA synthase activity; IDA:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005549; F:odorant binding; NAS:RGD.
DR GO; GO:0006637; P:acyl-CoA metabolic process; IDA:RGD.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0007608; P:sensory perception of smell; NAS:RGD.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Fatty acid metabolism; Ligase; Lipid metabolism; Magnesium;
KW Metal-binding; Mitochondrion; Nucleotide-binding; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..22
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 23..580
FT /note="Acyl-coenzyme A synthetase ACSM4, mitochondrial"
FT /id="PRO_0000306105"
FT BINDING 229..237
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 368..373
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 455
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 470
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 566
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 580 AA; 65317 MW; D9556CB46AAAB7C0 CRC64;
MKVLLRCQRL RFIWLAKPAG RHFHRDPQLW APLTLDDFEA INRCEKPLPK NFNFAADVLD
QWSLKEKSGE RPANPALWWV NGKGDEVKWS FQELGSLSRK AANVLTKPCG LQRGDRVAVI
LPRIPEWWLI NVACMRTGLV FMPGTIQLTR KDILYRLQAS KAKCIVASEE VAPAVDSIAS
ECPNLKTKLL VSPHRWDGWL SFQELLQSAS EEHNCVQTGS QEPMAIYFTS GTTGSPKMAQ
HSQSSLGIGY ALCGRYWLDL TSSDIMWNMS DTGWIKAAIG SVFSTWLRGA CVFVHRMAQF
NTDTFLDTLT SYPITTLCSA PTVYRMLVQQ DLKRYQFKRL RHCLTGGEPL NPEVLEQWKA
QTGLELYEGY GQTEVGIICA NRKGEEIKPG SMGKGVVPYD VQIIDEHGNI LPSGKEGEIA
LRLGSDRPFC FFSEYVDNPE KTDATIRRNF YITGDRGVMD DDGYLWFVGR ADDVIISSGY
RIGPFEVESA LIEHPAVVES AVVSSPDPIR GEVVKAFIVL AAPFKSSNRE KLTAELQDHV
KNSTAPYKYP RKVEFVQELP KTITGKIKRN VLRDQEWGRA
