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   27-MAR-2024, entry version 173.
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; 10090-ENSMUSP00000057595; -.
DR   PeptideAtlas; O35488; -.
DR   ProteomicsDB; 260899; -.
DR   Antibodypedia; 12170; 217 antibodies from 28 providers.
DR   DNASU; 26458; -.
DR   Ensembl; ENSMUST00000061491.14; ENSMUSP00000057595.8; ENSMUSG00000027359.17.
DR   GeneID; 26458; -.
DR   KEGG; mmu:26458; -.
DR   UCSC; uc008mdq.1; mouse.
DR   AGR; MGI:1347099; -.
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; IIHELYA; -.
DR   OrthoDB; 1650656at2759; -.
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-75105; Fatty acyl-CoA biosynthesis.
DR   Reactome; R-MMU-9033241; Peroxisomal protein import.
DR   BioGRID-ORCS; 26458; 2 hits in 78 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 177 other cell types or tissues.
DR   ExpressionAtlas; O35488; baseline and differential.
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:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0005778; C:peroxisomal membrane; ISS:UniProtKB.
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:1901480; F:oleate transmembrane transporter activity; IEA:RHEA.
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   CDD; cd05938; hsFATP2a_ACSVL_like; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 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_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   PANTHER; PTHR43107; LONG-CHAIN FATTY ACID TRANSPORT PROTEIN; 1.
DR   PANTHER; PTHR43107:SF13; VERY LONG-CHAIN ACYL-COA SYNTHETASE; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   Genevisible; O35488; MM.
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
//