S27A2_MOUSE
ID S27A2_MOUSE Reviewed; 620 AA.
AC O35488; O70550; O88560; Q91WV6;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Long-chain fatty acid transport protein 2 {ECO:0000305};
DE AltName: Full=Arachidonate--CoA ligase;
DE EC=6.2.1.15 {ECO:0000269|PubMed:15699031};
DE AltName: Full=Fatty acid transport protein 2 {ECO:0000303|PubMed:15699031, ECO:0000303|PubMed:20530735, ECO:0000303|PubMed:9671728};
DE Short=FATP-2 {ECO:0000303|PubMed:15699031, ECO:0000303|PubMed:20530735, ECO:0000303|PubMed:9671728};
DE AltName: Full=Fatty-acid-coenzyme A ligase, very long-chain 1;
DE AltName: Full=Long-chain-fatty-acid--CoA ligase;
DE EC=6.2.1.3 {ECO:0000269|PubMed:15699031, ECO:0000269|PubMed:20530735};
DE AltName: Full=Phytanate--CoA ligase;
DE EC=6.2.1.24 {ECO:0000250|UniProtKB:O14975};
DE AltName: Full=Solute carrier family 27 member 2;
DE Short=Slc27a2 {ECO:0000303|PubMed:15699031};
DE AltName: Full=THCA-CoA ligase;
DE EC=6.2.1.7 {ECO:0000250|UniProtKB:O14975};
DE AltName: Full=Very long-chain acyl-CoA synthetase {ECO:0000303|PubMed:20530735};
DE Short=VLACS {ECO:0000303|PubMed:15699031, ECO:0000303|PubMed:20530735};
DE Short=VLCS {ECO:0000303|PubMed:15699031};
DE EC=6.2.1.- {ECO:0000269|PubMed:15699031, ECO:0000269|PubMed:20530735};
DE AltName: Full=Very long-chain-fatty-acid-CoA ligase;
GN Name=Slc27a2; Synonyms=Acsvl1, Facvl1, Fatp2, Vlacs, Vlcs;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=9559670; DOI=10.1016/s0014-5793(98)00255-5;
RA Berger J., Truppe C., Neumann H., Forss-Petter S.;
RT "cDNA cloning and mRNA distribution of a mouse very long-chain acyl-CoA
RT synthetase.";
RL FEBS Lett. 425:305-309(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TRANSPORT
RP ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=9671728; DOI=10.1073/pnas.95.15.8625;
RA Hirsch D., Stahl A., Lodish H.F.;
RT "A family of fatty acid transporters conserved from mycobacterium to man.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:8625-8629(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=11980911; DOI=10.1074/jbc.m203295200;
RA Mihalik S.J., Steinberg S.J., Pei Z., Park J., Kim do G., Heinzer A.K.,
RA Dacremont G., Wanders R.J., Cuebas D.A., Smith K.D., Watkins P.A.;
RT "Participation of two members of the very long-chain acyl-CoA synthetase
RT family in bile acid synthesis and recycling.";
RL J. Biol. Chem. 277:24771-24779(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney, and Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND TRANSPORT ACTIVITY.
RX PubMed=15699031; DOI=10.1074/jbc.m409598200;
RA DiRusso C.C., Li H., Darwis D., Watkins P.A., Berger J., Black P.N.;
RT "Comparative biochemical studies of the murine fatty acid transport
RT proteins (FATP) expressed in yeast.";
RL J. Biol. Chem. 280:16829-16837(2005).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, TRANSPORT ACTIVITY, SUBCELLULAR LOCATION,
RP DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=20530735; DOI=10.1152/ajpendo.00226.2010;
RA Falcon A., Doege H., Fluitt A., Tsang B., Watson N., Kay M.A., Stahl A.;
RT "FATP2 is a hepatic fatty acid transporter and peroxisomal very long-chain
RT acyl-CoA synthetase.";
RL Am. J. Physiol. 299:E384-393(2010).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-577, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, and Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-291, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC -!- FUNCTION: Mediates the import of long-chain fatty acids (LCFA) into the
CC cell by facilitating their transport across cell membranes, playing an
CC important role in hepatic fatty acid uptake (PubMed:9671728,
CC PubMed:15699031, PubMed:20530735). Also functions as an acyl-CoA ligase
CC catalyzing the ATP-dependent formation of fatty acyl-CoA using LCFA and
CC very-long-chain fatty acids (VLCFA) as substrates, which prevents fatty
CC acid efflux from cells and might drive more fatty acid uptake
CC (PubMed:15699031, PubMed:20530735). Plays a pivotal role in regulating
CC available LCFA substrates from exogenous sources in tissues undergoing
CC high levels of beta-oxidation or triglyceride synthesis
CC (PubMed:15699031, PubMed:20530735). Can also activate branched-chain
CC fatty acids such as phytanic acid and pristanic acid (By similarity).
CC May contribute to the synthesis of sphingosine-1-phosphate (By
CC similarity). Does not activate C24 bile acids, cholate and
CC chenodeoxycholate (By similarity). In vitro, activates 3-alpha,7-
CC alpha,12-alpha-trihydroxy-5-beta-cholestanate (THCA), the C27 precursor
CC of cholic acid deriving from the de novo synthesis from cholesterol.
CC However, it is not critical for THCA activation and bile synthesis in
CC vivo (By similarity). {ECO:0000250|UniProtKB:O14975,
CC ECO:0000269|PubMed:15699031, ECO:0000269|PubMed:20530735,
CC ECO:0000269|PubMed:9671728}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a fatty acid(in) = a fatty acid(out); Xref=Rhea:RHEA:38879,
CC ChEBI:CHEBI:28868; Evidence={ECO:0000269|PubMed:15699031,
CC ECO:0000269|PubMed:20530735, ECO:0000269|PubMed:9671728};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoate(out) = (9Z)-octadecenoate(in);
CC Xref=Rhea:RHEA:33655, ChEBI:CHEBI:30823;
CC Evidence={ECO:0000250|UniProtKB:O14975};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-
CC CoA + AMP + diphosphate; Xref=Rhea:RHEA:15421, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57560,
CC ChEBI:CHEBI:83139, ChEBI:CHEBI:456215; EC=6.2.1.3;
CC Evidence={ECO:0000269|PubMed:15699031, ECO:0000305|PubMed:20530735};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15422;
CC Evidence={ECO:0000305|PubMed:15699031, ECO:0000305|PubMed:20530735};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + ATP + CoA =
CC (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + AMP + diphosphate;
CC Xref=Rhea:RHEA:19713, ChEBI:CHEBI:30616, ChEBI:CHEBI:32395,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368,
CC ChEBI:CHEBI:456215; EC=6.2.1.15;
CC Evidence={ECO:0000269|PubMed:15699031};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19714;
CC Evidence={ECO:0000305|PubMed:15699031};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoate + ATP + CoA = (9Z)-octadecenoyl-CoA + AMP +
CC diphosphate; Xref=Rhea:RHEA:33607, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57387, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:15699031};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33608;
CC Evidence={ECO:0000305|PubMed:15699031};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z,15Z)-octadecatrienoate + ATP + CoA = (9Z,12Z,15Z)-
CC octadecatrienoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:44936,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:32387, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:74034, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000250|UniProtKB:O14975};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44937;
CC Evidence={ECO:0000250|UniProtKB:O14975};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + hexadecanoate = AMP + diphosphate + hexadecanoyl-
CC CoA; Xref=Rhea:RHEA:30751, ChEBI:CHEBI:7896, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000305|PubMed:20530735};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30752;
CC Evidence={ECO:0000305|PubMed:20530735};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2,6,10,14-tetramethylpentadecanoate + ATP + CoA = AMP +
CC diphosphate + pristanoyl-CoA; Xref=Rhea:RHEA:47264,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:77250, ChEBI:CHEBI:77268, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000250|UniProtKB:O14975};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47265;
CC Evidence={ECO:0000250|UniProtKB:O14975};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(E)-hexadec-2-enoate + ATP + CoA = (2E)-hexadecenoyl-CoA + AMP
CC + diphosphate; Xref=Rhea:RHEA:36139, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:61526,
CC ChEBI:CHEBI:72745, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000250|UniProtKB:O14975};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36140;
CC Evidence={ECO:0000250|UniProtKB:O14975};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3,7,11,15-tetramethylhexadecanoate + ATP + CoA = AMP +
CC diphosphate + phytanoyl-CoA; Xref=Rhea:RHEA:21380, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37257, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57391, ChEBI:CHEBI:456215; EC=6.2.1.24;
CC Evidence={ECO:0000250|UniProtKB:O14975};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21381;
CC Evidence={ECO:0000250|UniProtKB:O14975};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a very long-chain fatty acid + ATP + CoA = a very long-chain
CC fatty acyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:54536,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:58950, ChEBI:CHEBI:138261, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:15699031, ECO:0000305|PubMed:20530735};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54537;
CC Evidence={ECO:0000305|PubMed:15699031, ECO:0000305|PubMed:20530735};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + tetracosanoate = AMP + diphosphate +
CC tetracosanoyl-CoA; Xref=Rhea:RHEA:33639, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:31014, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:65052, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:15699031, ECO:0000305|PubMed:20530735};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33640;
CC Evidence={ECO:0000305|PubMed:15699031, ECO:0000305|PubMed:20530735};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + ATP + CoA =
CC (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoyl-CoA + AMP + diphosphate;
CC Xref=Rhea:RHEA:44932, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:74298, ChEBI:CHEBI:77016,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:O14975};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44933;
CC Evidence={ECO:0000250|UniProtKB:O14975};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate
CC + ATP + CoA = (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-
CC 26-oyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:22976,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:58677, ChEBI:CHEBI:58734, ChEBI:CHEBI:456215; EC=6.2.1.7;
CC Evidence={ECO:0000250|UniProtKB:O14975};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22977;
CC Evidence={ECO:0000250|UniProtKB:O14975};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:O14975}; Multi-pass membrane protein
CC {ECO:0000255}. Peroxisome membrane {ECO:0000269|PubMed:20530735};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:P97524}. Cell
CC membrane {ECO:0000269|PubMed:20530735}; Multi-pass membrane protein
CC {ECO:0000255}. Microsome {ECO:0000250|UniProtKB:P97524}.
CC -!- TISSUE SPECIFICITY: Strong expression in liver and kidney (at protein
CC level) (PubMed:20530735, PubMed:11980911, PubMed:9671728). Lower
CC expression in brain and testis, no expression in skeletal muscle and
CC spleen (PubMed:11980911). Shows uniform distribution in liver acinus
CC (PubMed:11980911). {ECO:0000269|PubMed:11980911,
CC ECO:0000269|PubMed:20530735, ECO:0000269|PubMed:9671728}.
CC -!- DISRUPTION PHENOTYPE: Conditional knockout in liver results in
CC decreased long-chain fatty acids (LCFA) uptake by hepatocytes and
CC decreased peroxisomal long chain and very long-chain acyl-CoA
CC synthetase (VLACS) activity. {ECO:0000269|PubMed:20530735}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC40186.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ223958; CAA11687.1; -; mRNA.
DR EMBL; AF072757; AAC40186.1; ALT_SEQ; mRNA.
DR EMBL; AF033031; AAB87982.1; -; mRNA.
DR EMBL; AL831764; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL844555; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC013442; AAH13442.1; -; mRNA.
DR EMBL; BC022170; AAH22170.1; -; mRNA.
DR EMBL; BC024735; AAH24735.1; -; mRNA.
DR CCDS; CCDS16683.1; -.
DR RefSeq; NP_036108.2; NM_011978.2.
DR AlphaFoldDB; O35488; -.
DR SMR; O35488; -.
DR BioGRID; 205004; 4.
DR STRING; 10090.ENSMUSP00000057595; -.
DR SwissLipids; SLP:000000430; -.
DR iPTMnet; O35488; -.
DR PhosphoSitePlus; O35488; -.
DR SwissPalm; O35488; -.
DR jPOST; O35488; -.
DR MaxQB; O35488; -.
DR PaxDb; O35488; -.
DR PeptideAtlas; O35488; -.
DR PRIDE; O35488; -.
DR ProteomicsDB; 260899; -.
DR Antibodypedia; 12170; 195 antibodies from 28 providers.
DR DNASU; 26458; -.
DR Ensembl; ENSMUST00000061491; ENSMUSP00000057595; ENSMUSG00000027359.
DR GeneID; 26458; -.
DR KEGG; mmu:26458; -.
DR UCSC; uc008mdq.1; mouse.
DR CTD; 11001; -.
DR MGI; MGI:1347099; Slc27a2.
DR VEuPathDB; HostDB:ENSMUSG00000027359; -.
DR eggNOG; KOG1179; Eukaryota.
DR GeneTree; ENSGT00940000161137; -.
DR HOGENOM; CLU_000022_46_2_1; -.
DR InParanoid; O35488; -.
DR OMA; LRSHETW; -.
DR OrthoDB; 298283at2759; -.
DR PhylomeDB; O35488; -.
DR TreeFam; TF313430; -.
DR Reactome; R-MMU-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
DR Reactome; R-MMU-193775; Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
DR Reactome; R-MMU-389599; Alpha-oxidation of phytanate.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-9033241; Peroxisomal protein import.
DR BioGRID-ORCS; 26458; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Slc27a2; mouse.
DR PRO; PR:O35488; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; O35488; protein.
DR Bgee; ENSMUSG00000027359; Expressed in right kidney and 175 other tissues.
DR ExpressionAtlas; O35488; baseline and differential.
DR Genevisible; O35488; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0005779; C:integral component of peroxisomal membrane; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005778; C:peroxisomal membrane; ISO:MGI.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0047676; F:arachidonate-CoA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0047747; F:cholate-CoA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0015245; F:fatty acid transmembrane transporter activity; IDA:MGI.
DR GO; GO:0005324; F:long-chain fatty acid transporter activity; IDA:UniProtKB.
DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IDA:MGI.
DR GO; GO:0050197; F:phytanate-CoA ligase activity; ISO:MGI.
DR GO; GO:0070251; F:pristanate-CoA ligase activity; ISO:MGI.
DR GO; GO:0031957; F:very long-chain fatty acid-CoA ligase activity; IDA:UniProtKB.
DR GO; GO:0006699; P:bile acid biosynthetic process; ISO:MGI.
DR GO; GO:0001561; P:fatty acid alpha-oxidation; ISO:MGI.
DR GO; GO:0006635; P:fatty acid beta-oxidation; ISO:MGI.
DR GO; GO:0015908; P:fatty acid transport; IDA:MGI.
DR GO; GO:0044539; P:long-chain fatty acid import into cell; ISO:MGI.
DR GO; GO:0001676; P:long-chain fatty acid metabolic process; IDA:MGI.
DR GO; GO:0097089; P:methyl-branched fatty acid metabolic process; ISO:MGI.
DR GO; GO:0042760; P:very long-chain fatty acid catabolic process; IMP:MGI.
DR GO; GO:0000038; P:very long-chain fatty acid metabolic process; IDA:MGI.
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 InterPro; IPR030305; FATP2.
DR PANTHER; PTHR43107:SF13; PTHR43107:SF13; 1.
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 Acetylation; ATP-binding; Cell membrane; Endoplasmic reticulum;
KW Fatty acid metabolism; Ligase; Lipid metabolism; Lipid transport; Membrane;
KW Microsome; Nucleotide-binding; Peroxisome; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..620
FT /note="Long-chain fatty acid transport protein 2"
FT /id="PRO_0000193205"
FT TOPO_DOM 1..4
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:O14975"
FT TRANSMEM 5..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..106
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O14975"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 128..267
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:O14975"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 289..620
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O14975"
FT BINDING 222..233
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255"
FT MOD_RES 291
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 577
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 35
FT /note="R -> Q (in Ref. 3; AAB87982)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="V -> A (in Ref. 1; CAA11687 and 3; AAB87982)"
FT /evidence="ECO:0000305"
FT CONFLICT 234..235
FT /note="AA -> SG (in Ref. 2; AAC40186)"
FT /evidence="ECO:0000305"
FT CONFLICT 243
FT /note="W -> R (in Ref. 2; AAC40186)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="G -> S (in Ref. 2; AAC40186)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="Q -> K (in Ref. 2; AAC40186)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="A -> T (in Ref. 2; AAC40186)"
FT /evidence="ECO:0000305"
SQ 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
