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Very long-chain acyl-CoA synthetase (VLACS) (VLCS) (EC 6.2.1.-) (Fatty acid transport protein 2) (FATP-2) (Fatty-acid-coenzyme A ligase, very long-chain 1) (Long-chain-fatty-acid--CoA ligase) (EC 6.2.1.3) (Solute carrier family 27 member 2) (THCA-CoA ligase) (Very long-chain-fatty-acid-CoA ligase)

 S27A2_RAT               Reviewed;         620 AA.
P97524;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-MAY-1997, sequence version 1.
23-MAY-2018, entry version 113.
RecName: Full=Very long-chain acyl-CoA synthetase;
Short=VLACS;
Short=VLCS;
EC=6.2.1.-;
AltName: Full=Fatty acid transport protein 2;
Short=FATP-2;
AltName: Full=Fatty-acid-coenzyme A ligase, very long-chain 1;
AltName: Full=Long-chain-fatty-acid--CoA ligase;
EC=6.2.1.3;
AltName: Full=Solute carrier family 27 member 2;
AltName: Full=THCA-CoA ligase;
AltName: Full=Very long-chain-fatty-acid-CoA ligase;
Name=Slc27a2; Synonyms=Acsvl1, Facvl1, Fatp2, Vlacs, Vlcs;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
STRAIN=Wistar; TISSUE=Liver;
PubMed=8939997; DOI=10.1074/jbc.271.48.30360;
Uchiyama A., Aoyama T., Kamijo K., Uchida Y., Kondo N., Orii T.,
Hashimoto T.;
"Molecular cloning of cDNA encoding rat very long-chain acyl-CoA
synthetase.";
J. Biol. Chem. 271:30360-30365(1996).
[2]
SUBCELLULAR LOCATION.
PubMed=10640429; DOI=10.1006/excr.1999.4757;
Smith B.T., Sengupta T.K., Singh I.;
"Intraperoxisomal localization of very-long-chain fatty acyl-CoA
synthetase: implication in X-adrenoleukodystrophy.";
Exp. Cell Res. 254:309-320(2000).
-!- FUNCTION: Acyl-CoA synthetase probably involved in bile acid
metabolism. Proposed to activate C27 precursors of bile acids to
their CoA thioesters derivatives before side chain cleavage via
peroxisomal beta-oxidation occurs. In vitro, activates 3-alpha,7-
alpha,12-alpha-trihydroxy-5-beta-cholestanate (THCA), the C27
precursor of cholic acid deriving from the de novo synthesis from
cholesterol. Does not utilize C24 bile acids as substrates. In
vitro, also activates long- and branched-chain fatty acids and may
have additional roles in fatty acid metabolism. May be involved in
translocation of long-chain fatty acids (LFCA) across membranes
(By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: ATP + a long-chain fatty acid + CoA = AMP +
diphosphate + an acyl-CoA.
-!- CATALYTIC ACTIVITY: ATP + a very-long-chain carboxylic acid + CoA
= AMP + diphosphate + an acyl-CoA.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:10640429}; Multi-pass membrane protein
{ECO:0000269|PubMed:10640429}. Peroxisome membrane
{ECO:0000269|PubMed:10640429}; Multi-pass membrane protein
{ECO:0000269|PubMed:10640429}. Note=Peripheral membrane associated
with the lumenal side of peroxisomes.
-!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
family. {ECO:0000305}.
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EMBL; D85100; BAA12722.1; -; mRNA.
RefSeq; NP_113924.1; NM_031736.1.
UniGene; Rn.3608; -.
ProteinModelPortal; P97524; -.
SMR; P97524; -.
BioGrid; 249304; 1.
iPTMnet; P97524; -.
PhosphoSitePlus; P97524; -.
PRIDE; P97524; -.
GeneID; 65192; -.
KEGG; rno:65192; -.
UCSC; RGD:71103; rat.
CTD; 11001; -.
RGD; 71103; Slc27a2.
HOGENOM; HOG000044189; -.
HOVERGEN; HBG005642; -.
InParanoid; P97524; -.
KO; K08746; -.
PhylomeDB; P97524; -.
PRO; PR:P97524; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005788; C:endoplasmic reticulum lumen; ISS:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0005779; C:integral component of peroxisomal membrane; IDA:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
GO; GO:0005778; C:peroxisomal membrane; IDA:HGNC.
GO; GO:0005777; C:peroxisome; IDA:RGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0102391; F:decanoate-CoA ligase activity; IEA:UniProtKB-EC.
GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IDA:RGD.
GO; GO:0031957; F:very long-chain fatty acid-CoA ligase activity; ISS:UniProtKB.
GO; GO:0015908; P:fatty acid transport; IEA:InterPro.
GO; GO:0001676; P:long-chain fatty acid metabolic process; IMP:UniProtKB.
InterPro; IPR025110; AMP-bd_C.
InterPro; IPR020845; AMP-binding_CS.
InterPro; IPR000873; AMP-dep_Synth/Lig.
InterPro; IPR030305; FATP2.
PANTHER; PTHR43107:SF13; PTHR43107:SF13; 1.
Pfam; PF00501; AMP-binding; 1.
Pfam; PF13193; AMP-binding_C; 1.
PROSITE; PS00455; AMP_BINDING; 1.
1: Evidence at protein level;
Acetylation; ATP-binding; Complete proteome;
Direct protein sequencing; Endoplasmic reticulum;
Fatty acid metabolism; Ligase; Lipid metabolism; Membrane;
Nucleotide-binding; Peroxisome; Phosphoprotein; Reference proteome;
Transmembrane; Transmembrane helix.
CHAIN 1 620 Very long-chain acyl-CoA synthetase.
/FTId=PRO_0000193206.
TOPO_DOM 1 4 Lumenal. {ECO:0000250}.
TRANSMEM 5 27 Helical. {ECO:0000255}.
TOPO_DOM 28 106 Cytoplasmic. {ECO:0000255}.
TRANSMEM 107 127 Helical. {ECO:0000255}.
TOPO_DOM 128 267 Lumenal. {ECO:0000255}.
TRANSMEM 268 288 Helical. {ECO:0000255}.
TOPO_DOM 289 620 Cytoplasmic. {ECO:0000250}.
NP_BIND 222 233 AMP. {ECO:0000255}.
MOD_RES 291 291 N6-acetyllysine.
{ECO:0000250|UniProtKB:O35488}.
MOD_RES 577 577 Phosphothreonine.
{ECO:0000250|UniProtKB:O14975}.
SEQUENCE 620 AA; 70694 MW; 6CF9362DC3805526 CRC64;
MLPVLYTGLA GLLLLPLLLT CCCPYLLQDV RFFLQLANMA RQVRSYRQRR PVRTILHVFL
EQARKTPHKP FLLFRDETLT YAQVDRRSNQ VARALHDHLG LRQGDCVALF MGNEPAYVWL
WLGLLKLGCP MACLNYNIRA KSLLHCFQCC GAKVLLASPE LHEAVEEVLP TLKKEGVSVF
YVSRTSNTNG VDTVLDKVDG VSADPIPESW RSEVTFTTPA VYIYTSGTTG LPKAATINHH
RLWYGTSLAL RSGIKAHDVI YTTMPLYHSA ALMIGLHGCI VVGATFALRS KFSASQFWDD
CRKYNATVIQ YIGELLRYLC NTPQKPNDRD HKVKIALGNG LRGDVWREFI KRFGDIHIYE
FYASTEGNIG FMNYPRKIGA VGRENYLQKK VVRHELIKYD VEKDEPVRDA NGYCIKVPKG
EVGLLICKIT ELTPFFGYAG GKTQTEKKKL RDVFKKGDVY FNSGDLLMID RENFIYFHDR
VGDTFRWKGE NVATTEVADI VGLVDFVEEV NVYGVPVPGH EGRIGMASIK MKENYEFNGK
KLFQHISEYL PSYSRPRFLR IQDTIEITGT FKHRKVTLME EGFNPSVIKD TLYFMDDTEK
TYVPMTEDIY NAIIDKTLKL


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