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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_MOUSE             Reviewed;         620 AA.
O35488; O70550; O88560; Q91WV6;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
20-JUN-2018, entry version 142.
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;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ; TISSUE=Liver;
PubMed=9559670; DOI=10.1016/S0014-5793(98)00255-5;
Berger J., Truppe C., Neumann H., Forss-Petter S.;
"cDNA cloning and mRNA distribution of a mouse very long-chain acyl-
CoA synthetase.";
FEBS Lett. 425:305-309(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9671728; DOI=10.1073/pnas.95.15.8625;
Hirsch D., Stahl A., Lodish H.F.;
"A family of fatty acid transporters conserved from mycobacterium to
man.";
Proc. Natl. Acad. Sci. U.S.A. 95:8625-8629(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
STRAIN=C57BL/6J; TISSUE=Liver;
PubMed=11980911; DOI=10.1074/jbc.M203295200;
Mihalik S.J., Steinberg S.J., Pei Z., Park J., Kim do G.,
Heinzer A.K., Dacremont G., Wanders R.J., Cuebas D.A., Smith K.D.,
Watkins P.A.;
"Participation of two members of the very long-chain acyl-CoA
synthetase family in bile acid synthesis and recycling.";
J. Biol. Chem. 277:24771-24779(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Kidney, and Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
FUNCTION IN FATTY ACID TRANSPORT.
PubMed=15699031; DOI=10.1074/jbc.M409598200;
DiRusso C.C., Li H., Darwis D., Watkins P.A., Berger J., Black P.N.;
"Comparative biochemical studies of the murine fatty acid transport
proteins (FATP) expressed in yeast.";
J. Biol. Chem. 280:16829-16837(2005).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-577, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Kidney, and Liver;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[8]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-291, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=23576753; DOI=10.1073/pnas.1302961110;
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J.,
Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
"Label-free quantitative proteomics of the lysine acetylome in
mitochondria identifies substrates of SIRT3 in metabolic pathways.";
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
-!- 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 (By similarity).
May be involved in translocation of long-chain fatty acids (LFCA)
across membranes. {ECO:0000250, ECO:0000269|PubMed:15699031}.
-!- 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:0000250}; Multi-pass membrane protein {ECO:0000250}.
Peroxisome membrane {ECO:0000250}; Multi-pass membrane protein
{ECO:0000250}. Note=Peripheral membrane associated with the
lumenal side of peroxisomes. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Strong expression in liver and kidney, low
expression in brain and testis, no expression in skeletal muscle
and spleen. Shows uniform distribution in liver acinus.
{ECO:0000269|PubMed:11980911}.
-!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC40186.1; Type=Frameshift; Positions=253, 263, 267, 281, 289, 293, 299, 301, 307; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AJ223958; CAA11687.1; -; mRNA.
EMBL; AF072757; AAC40186.1; ALT_SEQ; mRNA.
EMBL; AF033031; AAB87982.1; -; mRNA.
EMBL; AL831764; CAM17405.1; -; Genomic_DNA.
EMBL; AL844555; CAM17405.1; JOINED; Genomic_DNA.
EMBL; AL844555; CAM18704.1; -; Genomic_DNA.
EMBL; AL831764; CAM18704.1; JOINED; Genomic_DNA.
EMBL; BC013442; AAH13442.1; -; mRNA.
EMBL; BC022170; AAH22170.1; -; mRNA.
EMBL; BC024735; AAH24735.1; -; mRNA.
CCDS; CCDS16683.1; -.
RefSeq; NP_036108.2; NM_011978.2.
UniGene; Mm.290044; -.
ProteinModelPortal; O35488; -.
SMR; O35488; -.
IntAct; O35488; 4.
MINT; O35488; -.
STRING; 10090.ENSMUSP00000057595; -.
SwissLipids; SLP:000000430; -.
iPTMnet; O35488; -.
PhosphoSitePlus; O35488; -.
SwissPalm; O35488; -.
MaxQB; O35488; -.
PaxDb; O35488; -.
PeptideAtlas; O35488; -.
PRIDE; O35488; -.
Ensembl; ENSMUST00000061491; ENSMUSP00000057595; ENSMUSG00000027359.
GeneID; 26458; -.
KEGG; mmu:26458; -.
UCSC; uc008mdq.1; mouse.
CTD; 11001; -.
MGI; MGI:1347099; Slc27a2.
eggNOG; KOG1179; Eukaryota.
eggNOG; ENOG410XQ8T; LUCA.
GeneTree; ENSGT00550000074420; -.
HOGENOM; HOG000044189; -.
HOVERGEN; HBG005642; -.
InParanoid; O35488; -.
KO; K08746; -.
OMA; VGLHGCI; -.
OrthoDB; EOG091G0B76; -.
TreeFam; TF313430; -.
Reactome; R-MMU-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
Reactome; R-MMU-193775; Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
Reactome; R-MMU-389599; Alpha-oxidation of phytanate.
Reactome; R-MMU-6798695; Neutrophil degranulation.
Reactome; R-MMU-9033241; Peroxisomal protein import.
ChiTaRS; Slc27a2; mouse.
PRO; PR:O35488; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000027359; -.
ExpressionAtlas; O35488; baseline and differential.
Genevisible; O35488; MM.
GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
GO; GO:0005788; C:endoplasmic reticulum lumen; ISS:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISO:MGI.
GO; GO:0005779; C:integral component of peroxisomal membrane; ISS:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0005739; C:mitochondrion; HDA:MGI.
GO; GO:0005778; C:peroxisomal membrane; ISO:MGI.
GO; GO:0005777; C:peroxisome; IDA:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0102391; F:decanoate-CoA ligase activity; IEA:UniProtKB-EC.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0015245; F:fatty acid transmembrane transporter activity; IDA:MGI.
GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IDA:MGI.
GO; GO:0050197; F:phytanate-CoA ligase activity; ISO:MGI.
GO; GO:0070251; F:pristanate-CoA ligase activity; ISO:MGI.
GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
GO; GO:0031957; F:very long-chain fatty acid-CoA ligase activity; IDA:MGI.
GO; GO:0006699; P:bile acid biosynthetic process; ISO:MGI.
GO; GO:0001561; P:fatty acid alpha-oxidation; ISO:MGI.
GO; GO:0006635; P:fatty acid beta-oxidation; ISO:MGI.
GO; GO:0015908; P:fatty acid transport; IDA:MGI.
GO; GO:0044539; P:long-chain fatty acid import; ISO:MGI.
GO; GO:0001676; P:long-chain fatty acid metabolic process; IDA:MGI.
GO; GO:0097089; P:methyl-branched fatty acid metabolic process; ISO:MGI.
GO; GO:0042760; P:very long-chain fatty acid catabolic process; IMP:MGI.
GO; GO:0000038; P:very long-chain fatty acid metabolic process; IDA:MGI.
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; 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_0000193205.
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:0000244|PubMed:23576753}.
MOD_RES 577 577 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
CONFLICT 35 35 R -> Q (in Ref. 3; AAB87982).
{ECO:0000305}.
CONFLICT 168 168 V -> A (in Ref. 1; CAA11687 and 3;
AAB87982). {ECO:0000305}.
CONFLICT 234 235 AA -> SG (in Ref. 2; AAC40186).
{ECO:0000305}.
CONFLICT 243 243 W -> R (in Ref. 2; AAC40186).
{ECO:0000305}.
CONFLICT 247 247 G -> S (in Ref. 2; AAC40186).
{ECO:0000305}.
CONFLICT 257 257 Q -> K (in Ref. 2; AAC40186).
{ECO:0000305}.
CONFLICT 271 271 A -> T (in Ref. 2; AAC40186).
{ECO:0000305}.
SEQUENCE 620 AA; 70423 MW; 62994BDB1D828B37 CRC64;
MLPVLYTGLA GLLLLPLLLT CCCPYLLQDV RYFLRLANMA RRVRSYRQRR PVRTILRAFL
EQARKTPHKP FLLFRDETLT YAQVDRRSNQ VARALHDQLG LRQGDCVALF MGNEPAYVWI
WLGLLKLGCP MACLNYNIRA KSLLHCFQCC GAKVLLASPD LQEAVEEVLP TLKKDAVSVF
YVSRTSNTNG VDTILDKVDG VSAEPTPESW RSEVTFTTPA VYIYTSGTTG LPKAATINHH
RLWYGTGLAM SSGITAQDVI YTTMPLYHSA ALMIGLHGCI VVGATLALRS KFSASQFWDD
CRKYNVTVIQ YIGELLRYLC NTPQKPNDRD HKVKKALGNG LRGDVWREFI KRFGDIHVYE
FYASTEGNIG FVNYPRKIGA VGRANYLQRK VARYELIKYD VEKDEPVRDA NGYCIKVPKG
EVGLLVCKIT QLTPFIGYAG GKTQTEKKKL RDVFKKGDIY FNSGDLLMID RENFVYFHDR
VGDTFRWKGE NVATTEVADI VGLVDFVEEV NVYGVPVPGH EGRIGMASLK IKENYEFNGK
KLFQHIAEYL PSYARPRFLR IQDTIEITGT FKHRKVTLME EGFNPTVIKD TLYFMDDAEK
TFVPMTENIY NAIIDKTLKL


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