S27A1_MOUSE
ID S27A1_MOUSE Reviewed; 646 AA.
AC Q60714;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Long-chain fatty acid transport protein 1 {ECO:0000305};
DE AltName: Full=Arachidonate--CoA ligase;
DE EC=6.2.1.15 {ECO:0000269|PubMed:10593920, ECO:0000269|PubMed:12235169, ECO:0000269|PubMed:12937175};
DE AltName: Full=Fatty acid transport protein {ECO:0000303|PubMed:7954810};
DE AltName: Full=Fatty acid transport protein 1 {ECO:0000303|PubMed:9671728};
DE Short=FATP-1 {ECO:0000303|PubMed:15699031};
DE AltName: Full=Long-chain-fatty-acid--CoA ligase;
DE EC=6.2.1.3 {ECO:0000269|PubMed:10593920, ECO:0000269|PubMed:12235169, ECO:0000269|PubMed:12937175};
DE AltName: Full=Solute carrier family 27 member 1 {ECO:0000312|MGI:MGI:1347098};
DE Short=Vlc27a1 {ECO:0000303|PubMed:15699031};
DE AltName: Full=Very long-chain acyl-CoA synthetase;
DE EC=6.2.1.- {ECO:0000269|PubMed:15699031};
GN Name=Slc27a1 {ECO:0000312|MGI:MGI:1347098};
GN Synonyms=Fatp {ECO:0000303|PubMed:7954810},
GN Fatp1 {ECO:0000303|PubMed:9671728};
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], FUNCTION, CATALYTIC ACTIVITY, TRANSPORT
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TOPOLOGY,
RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC STRAIN=SWR/J;
RX PubMed=7954810; DOI=10.1016/0092-8674(94)90252-6;
RA Schaffer J.E., Lodish H.F.;
RT "Expression cloning and characterization of a novel adipocyte long chain
RT fatty acid transport protein.";
RL Cell 79:427-436(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RX PubMed=9765271; DOI=10.1074/jbc.273.42.27420;
RA Hui T.Y., Frohnert B.I., Smith A.J., Schaffer J.E., Bernlohr D.A.;
RT "Characterization of the murine fatty acid transport protein gene and its
RT insulin response sequence.";
RL J. Biol. Chem. 273:27420-27429(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Retina;
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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, ATP-BINDING, AND MUTAGENESIS OF SER-250.
RX PubMed=9786857; DOI=10.1074/jbc.273.44.28642;
RA Stuhlsatz-Krouper S.M., Bennett N.E., Schaffer J.E.;
RT "Substitution of alanine for serine 250 in the murine fatty acid transport
RT protein inhibits long chain fatty acid transport.";
RL J. Biol. Chem. 273:28642-28650(1998).
RN [5]
RP FUNCTION, TRANSPORT 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 [6]
RP FUNCTION AS AN ACYL-COA LIGASE, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION,
RP AND MUTAGENESIS OF 249-THR--GLY-254.
RX PubMed=10593920; DOI=10.1074/jbc.274.51.36300;
RA Coe N.R., Smith A.J., Frohnert B.I., Watkins P.A., Bernlohr D.A.;
RT "The fatty acid transport protein (FATP1) is a very long chain acyl-CoA
RT synthetase.";
RL J. Biol. Chem. 274:36300-36304(1999).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, ATP-BINDING, MUTAGENESIS OF SER-250 AND
RP THR-252, AND TRANSPORT ACTIVITY.
RX PubMed=10471110; DOI=10.1016/s0952-3278(99)80001-5;
RA Stuhlsatz-Krouper S.M., Bennett N.E., Schaffer J.E.;
RT "Molecular aspects of fatty acid transport: mutations in the IYTSGTTGXPK
RT motif impair fatty acid transport protein function.";
RL Prostaglandins Leukot. Essent. Fatty Acids 60:285-289(1999).
RN [8]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=11470793; DOI=10.1074/jbc.m105556200;
RA Lewis S.E., Listenberger L.L., Ory D.S., Schaffer J.E.;
RT "Membrane topology of the murine fatty acid transport protein 1.";
RL J. Biol. Chem. 276:37042-37050(2001).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=12235169; DOI=10.1194/jlr.m200130-jlr200;
RA Hatch G.M., Smith A.J., Xu F.Y., Hall A.M., Bernlohr D.A.;
RT "FATP1 channels exogenous FA into 1,2,3-triacyl-sn-glycerol and down-
RT regulates sphingomyelin and cholesterol metabolism in growing 293 cells.";
RL J. Lipid Res. 43:1380-1389(2002).
RN [10]
RP SUBUNIT, REGION, AND TRANSPORT ACTIVITY.
RX PubMed=12533547; DOI=10.1074/jbc.m212469200;
RA Richards M.R., Listenberger L.L., Kelly A.A., Lewis S.E., Ory D.S.,
RA Schaffer J.E.;
RT "Oligomerization of the murine fatty acid transport protein 1.";
RL J. Biol. Chem. 278:10477-10483(2003).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11970897; DOI=10.1016/s1534-5807(02)00143-0;
RA Stahl A., Evans J.G., Pattel S., Hirsch D., Lodish H.F.;
RT "Insulin causes fatty acid transport protein translocation and enhanced
RT fatty acid uptake in adipocytes.";
RL Dev. Cell 2:477-488(2002).
RN [12]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12556534; DOI=10.1074/jbc.m211412200;
RA Gimeno R.E., Ortegon A.M., Patel S., Punreddy S., Ge P., Sun Y.,
RA Lodish H.F., Stahl A.;
RT "Characterization of a heart-specific fatty acid transport protein.";
RL J. Biol. Chem. 278:16039-16044(2003).
RN [13]
RP FUNCTION AS AN ACYL-COA LIGASE, AND CATALYTIC ACTIVITY.
RX PubMed=12937175; DOI=10.1074/jbc.m306575200;
RA Hall A.M., Smith A.J., Bernlohr D.A.;
RT "Characterization of the acyl-CoA synthetase activity of purified murine
RT fatty acid transport protein 1.";
RL J. Biol. Chem. 278:43008-43013(2003).
RN [14]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=14991074; DOI=10.1172/jci200418917;
RA Kim J.K., Gimeno R.E., Higashimori T., Kim H.J., Choi H., Punreddy S.,
RA Mozell R.L., Tan G., Stricker-Krongrad A., Hirsch D.J., Fillmore J.J.,
RA Liu Z.X., Dong J., Cline G., Stahl A., Lodish H.F., Shulman G.I.;
RT "Inactivation of fatty acid transport protein 1 prevents fat-induced
RT insulin resistance in skeletal muscle.";
RL J. Clin. Invest. 113:756-763(2004).
RN [15]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15897321; DOI=10.1152/ajpcell.00271.2004;
RA Garcia-Martinez C., Marotta M., Moore-Carrasco R., Guitart M., Camps M.,
RA Busquets S., Montell E., Gomez-Foix A.M.;
RT "Impact on fatty acid metabolism and differential localization of FATP1 and
RT FAT/CD36 proteins delivered in cultured human muscle cells.";
RL Am. J. Physiol. 288:C1264-C1272(2005).
RN [16]
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 [17]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=19527715; DOI=10.1016/j.febslet.2009.06.020;
RA Jain S.S., Chabowski A., Snook L.A., Schwenk R.W., Glatz J.F., Luiken J.J.,
RA Bonen A.;
RT "Additive effects of insulin and muscle contraction on fatty acid transport
RT and fatty acid transporters, FAT/CD36, FABPpm, FATP1, 4 and 6.";
RL FEBS Lett. 583:2294-2300(2009).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, and
RC Testis;
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 [19]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24858472; DOI=10.1371/journal.pone.0098109;
RA Guitart M., Osorio-Conles O., Pentinat T., Cebria J., Garcia-Villoria J.,
RA Sala D., Sebastian D., Zorzano A., Ribes A., Jimenez-Chillaron J.C.,
RA Garcia-Martinez C., Gomez-Foix A.M.;
RT "Fatty acid transport protein 1 (FATP1) localizes in mitochondria in mouse
RT skeletal muscle and regulates lipid and ketone body disposal.";
RL PLoS ONE 9:e98109-e98109(2014).
RN [20]
RP FUNCTION, INTERACTION WITH EPRS1, AND SUBCELLULAR LOCATION.
RX PubMed=28178239; DOI=10.1038/nature21380;
RA Arif A., Terenzi F., Potdar A.A., Jia J., Sacks J., China A., Halawani D.,
RA Vasu K., Li X., Brown J.M., Chen J., Kozma S.C., Thomas G., Fox P.L.;
RT "EPRS is a critical mTORC1-S6K1 effector that influences adiposity in
RT mice.";
RL Nature 542:357-361(2017).
CC -!- FUNCTION: Mediates the import of long-chain fatty acids (LCFA) into the
CC cell by facilitating their transport at the plasma membrane
CC (PubMed:7954810, PubMed:9786857, PubMed:9671728, PubMed:10471110,
CC PubMed:12235169, PubMed:11970897, PubMed:15699031, PubMed:28178239,
CC PubMed:24858472, PubMed:19527715) (Probable). Also functions as an
CC acyl-CoA ligase catalyzing the ATP-dependent formation of fatty acyl-
CC CoA using LCFA and very-long-chain fatty acids (VLCFA) as substrates,
CC which prevents fatty acid efflux from cells and might drive more fatty
CC acid uptake (PubMed:10593920, PubMed:12235169, PubMed:12937175). May
CC act directly as a bona fide transporter, or alternatively, in a
CC cytoplasmic or membrane-associated multimeric protein complex to trap
CC and draw fatty acids towards accumulation (PubMed:14991074,
CC PubMed:15897321). Plays a pivotal role in regulating available LCFA
CC substrates from exogenous sources in tissues undergoing high levels of
CC beta-oxidation or triglyceride synthesis (PubMed:12235169). May be
CC involved in regulation of cholesterol metabolism (PubMed:12235169).
CC Probably involved in fatty acid transport across the blood barrier (By
CC similarity). {ECO:0000250|UniProtKB:Q6PCB7,
CC ECO:0000269|PubMed:10471110, ECO:0000269|PubMed:10593920,
CC ECO:0000269|PubMed:11970897, ECO:0000269|PubMed:12235169,
CC ECO:0000269|PubMed:12937175, ECO:0000269|PubMed:14991074,
CC ECO:0000269|PubMed:15699031, ECO:0000269|PubMed:15897321,
CC ECO:0000269|PubMed:19527715, ECO:0000269|PubMed:24858472,
CC ECO:0000269|PubMed:28178239, ECO:0000269|PubMed:7954810,
CC ECO:0000269|PubMed:9671728, ECO:0000269|PubMed:9786857,
CC ECO:0000305|PubMed:12556534}.
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:10471110,
CC ECO:0000269|PubMed:12533547, ECO:0000269|PubMed:15699031,
CC ECO:0000269|PubMed:7954810, 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:0000269|PubMed:7954810};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoate(out) = hexadecanoate(in); Xref=Rhea:RHEA:45256,
CC ChEBI:CHEBI:7896; Evidence={ECO:0000269|PubMed:7954810};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate(out) = (5Z,8Z,11Z,14Z)-
CC eicosatetraenoate(in); Xref=Rhea:RHEA:71395, ChEBI:CHEBI:32395;
CC Evidence={ECO:0000269|PubMed:7954810};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate(out) = (9Z,12Z)-
CC octadecadienoate(in); Xref=Rhea:RHEA:45264, ChEBI:CHEBI:30245;
CC Evidence={ECO:0000250|UniProtKB:Q6PCB7};
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};
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:0000269|PubMed:15699031};
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};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54537;
CC Evidence={ECO:0000269|PubMed:15699031};
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};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33640;
CC Evidence={ECO:0000269|PubMed:15699031};
CC -!- ACTIVITY REGULATION: Inhibited by Triacsin C (PubMed:12235169). Both
CC insulin and muscle contraction stimulate translocation to the plasma
CC membrane in muscle, increasing fatty acid transport activity
CC (PubMed:19527715). {ECO:0000269|PubMed:12235169,
CC ECO:0000269|PubMed:19527715}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.2 uM for (9Z)-octadecenoate (oleate)
CC {ECO:0000269|PubMed:7954810};
CC -!- SUBUNIT: Self-associates. May function as a homodimer
CC (PubMed:12533547). Interacts with EPRS1; mediates the translocation of
CC SLC27A1 from the cytoplasm to the plasma membrane thereby increasing
CC the uptake of long-chain fatty acids (PubMed:28178239). Interacts with
CC DGAT2 and this interaction is enhanced in the presence of ZFYVE1 (By
CC similarity). {ECO:0000250|UniProtKB:Q6PCB7,
CC ECO:0000269|PubMed:12533547, ECO:0000269|PubMed:28178239}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10471110,
CC ECO:0000269|PubMed:10593920, ECO:0000269|PubMed:11470793,
CC ECO:0000269|PubMed:11970897, ECO:0000269|PubMed:24858472,
CC ECO:0000269|PubMed:28178239, ECO:0000269|PubMed:7954810,
CC ECO:0000269|PubMed:9786857}; Single-pass membrane protein
CC {ECO:0000269|PubMed:11470793, ECO:0000269|PubMed:7954810}.
CC Mitochondrion outer membrane {ECO:0000269|PubMed:24858472}.
CC Endomembrane system {ECO:0000269|PubMed:10593920,
CC ECO:0000269|PubMed:15897321}; Single-pass membrane protein
CC {ECO:0000269|PubMed:11470793, ECO:0000269|PubMed:7954810}. Cytoplasm
CC {ECO:0000269|PubMed:10593920, ECO:0000269|PubMed:15897321}. Note=Plasma
CC membrane and intracellular membranes, at least in adipocytes
CC (PubMed:10593920, PubMed:11970897, PubMed:28178239). In adipocytes, but
CC not myocytes, insulin via the mTORC1 signaling pathway induces a rapid
CC translocation of SLC27A1 from intracellular compartments to the plasma
CC membrane, paralleled by increased LCFA uptake (PubMed:11970897,
CC PubMed:28178239). Insulin-dependent translocation from the cytoplasm to
CC the cell membrane is regulated by EPRS1 (PubMed:11970897,
CC PubMed:28178239). Predominantly cytoplasmic in myocytes
CC (PubMed:15897321). {ECO:0000269|PubMed:15897321}.
CC -!- TISSUE SPECIFICITY: Higher expression in white adipose tissue than in
CC heart (PubMed:12556534). Highest expression in skeletal muscle, heart
CC and fat. Lower levels in brain, kidney, lung, liver and testis. No
CC expression in spleen or intestine. {ECO:0000269|PubMed:12556534,
CC ECO:0000269|PubMed:7954810, ECO:0000269|PubMed:9671728}.
CC -!- DEVELOPMENTAL STAGE: Higher expression in differentiated adipocytes
CC compared to preadipocytes. {ECO:0000269|PubMed:7954810}.
CC -!- INDUCTION: Expression is down-regulated by insulin.
CC {ECO:0000269|PubMed:9765271}.
CC -!- DISRUPTION PHENOTYPE: Mice deficient for Slc27a1 are viable and do not
CC display overt developmental phenotype or alteration in whole-body
CC adiposity. However, they are protected from fat-induced accumulation of
CC intramuscular fatty acyl-CoA and insulin resistance in skeletal muscle.
CC {ECO:0000269|PubMed:14991074}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; U15976; AAC71060.1; -; mRNA.
DR EMBL; AF023258; AAC69640.1; -; Genomic_DNA.
DR EMBL; AF023256; AAC69640.1; JOINED; Genomic_DNA.
DR EMBL; AF023257; AAC69640.1; JOINED; Genomic_DNA.
DR EMBL; BC028937; AAH28937.1; -; mRNA.
DR CCDS; CCDS40386.1; -.
DR PIR; A55093; A55093.
DR RefSeq; NP_036107.1; NM_011977.3.
DR RefSeq; XP_006509736.1; XM_006509673.2.
DR RefSeq; XP_006509737.1; XM_006509674.3.
DR RefSeq; XP_006509738.1; XM_006509675.3.
DR RefSeq; XP_006509739.1; XM_006509676.3.
DR AlphaFoldDB; Q60714; -.
DR SMR; Q60714; -.
DR BioGRID; 205003; 1.
DR STRING; 10090.ENSMUSP00000034267; -.
DR BindingDB; Q60714; -.
DR ChEMBL; CHEMBL2052039; -.
DR SwissLipids; SLP:000000426; -.
DR iPTMnet; Q60714; -.
DR PhosphoSitePlus; Q60714; -.
DR SwissPalm; Q60714; -.
DR jPOST; Q60714; -.
DR MaxQB; Q60714; -.
DR PaxDb; Q60714; -.
DR PRIDE; Q60714; -.
DR ProteomicsDB; 256872; -.
DR Antibodypedia; 1644; 168 antibodies from 20 providers.
DR DNASU; 26457; -.
DR Ensembl; ENSMUST00000034267; ENSMUSP00000034267; ENSMUSG00000031808.
DR Ensembl; ENSMUST00000212889; ENSMUSP00000148768; ENSMUSG00000031808.
DR GeneID; 26457; -.
DR KEGG; mmu:26457; -.
DR UCSC; uc009mdw.1; mouse.
DR CTD; 376497; -.
DR MGI; MGI:1347098; Slc27a1.
DR VEuPathDB; HostDB:ENSMUSG00000031808; -.
DR eggNOG; KOG1179; Eukaryota.
DR GeneTree; ENSGT00940000159323; -.
DR HOGENOM; CLU_000022_46_2_1; -.
DR InParanoid; Q60714; -.
DR OMA; HHGLIMR; -.
DR OrthoDB; 312083at2759; -.
DR PhylomeDB; Q60714; -.
DR TreeFam; TF313430; -.
DR Reactome; R-MMU-804914; Transport of fatty acids.
DR BioGRID-ORCS; 26457; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Slc27a1; mouse.
DR PRO; PR:Q60714; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q60714; protein.
DR Bgee; ENSMUSG00000031808; Expressed in retinal neural layer and 263 other tissues.
DR ExpressionAtlas; Q60714; baseline and differential.
DR Genevisible; Q60714; MM.
DR GO; GO:0009925; C:basal plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0005901; C:caveola; ISO:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; TAS:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0047676; F:arachidonate-CoA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0015225; F:biotin transmembrane transporter activity; ISO:MGI.
DR GO; GO:0015562; F:efflux transmembrane transporter activity; ISO:MGI.
DR GO; GO:0015245; F:fatty acid transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0005324; F:long-chain fatty acid transporter activity; ISO:MGI.
DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IDA:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:1901480; F:oleate transmembrane transporter activity; IEA:RHEA.
DR GO; GO:0090434; F:oleoyl-CoA ligase activity; IMP:ARUK-UCL.
DR GO; GO:0031957; F:very long-chain fatty acid-CoA ligase activity; IDA:MGI.
DR GO; GO:0033211; P:adiponectin-activated signaling pathway; IMP:MGI.
DR GO; GO:1905135; P:biotin import across plasma membrane; ISO:MGI.
DR GO; GO:0015878; P:biotin transport; ISO:MGI.
DR GO; GO:0032049; P:cardiolipin biosynthetic process; ISO:MGI.
DR GO; GO:0140115; P:export across plasma membrane; ISO:MGI.
DR GO; GO:0015908; P:fatty acid transport; IDA:MGI.
DR GO; GO:0044381; P:glucose import in response to insulin stimulus; IMP:ARUK-UCL.
DR GO; GO:1990379; P:lipid transport across blood-brain barrier; ISO:MGI.
DR GO; GO:0015911; P:long-chain fatty acid import across plasma membrane; ISO:MGI.
DR GO; GO:0044539; P:long-chain fatty acid import into cell; IDA:UniProtKB.
DR GO; GO:0001676; P:long-chain fatty acid metabolic process; TAS:MGI.
DR GO; GO:0015909; P:long-chain fatty acid transport; IMP:MGI.
DR GO; GO:0001579; P:medium-chain fatty acid transport; IGI:MGI.
DR GO; GO:0071072; P:negative regulation of phospholipid biosynthetic process; ISO:MGI.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; ISO:MGI.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; ISO:MGI.
DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; ISO:MGI.
DR GO; GO:0006655; P:phosphatidylglycerol biosynthetic process; ISO:MGI.
DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; ISO:MGI.
DR GO; GO:0006659; P:phosphatidylserine biosynthetic process; ISO:MGI.
DR GO; GO:0031652; P:positive regulation of heat generation; IMP:MGI.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IMP:MGI.
DR GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; IDA:UniProtKB.
DR GO; GO:0009409; P:response to cold; IMP:MGI.
DR GO; GO:0032868; P:response to insulin; IMP:MGI.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
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; IPR030308; FATP1.
DR PANTHER; PTHR43107:SF7; PTHR43107:SF7; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Fatty acid metabolism; Ligase; Lipid metabolism;
KW Lipid transport; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW Nucleotide-binding; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..646
FT /note="Long-chain fatty acid transport protein 1"
FT /id="PRO_0000193202"
FT TOPO_DOM 1..13
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:11470793"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..646
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:11470793"
FT REGION 191..475
FT /note="Sufficient for oligomerization"
FT /evidence="ECO:0000269|PubMed:12533547"
FT BINDING 246..257
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:10471110,
FT ECO:0000269|PubMed:10593920, ECO:0000269|PubMed:9786857"
FT MUTAGEN 249..254
FT /note="TSGTTG->LEAAA: Abolishes very-long-chain acyl-CoA
FT synthetase activity."
FT /evidence="ECO:0000269|PubMed:10593920"
FT MUTAGEN 250
FT /note="S->A: Diminishes LCFA import and decreases
FT nucleotide binding. No effect on localization to the cell
FT membrane."
FT /evidence="ECO:0000269|PubMed:10471110,
FT ECO:0000269|PubMed:9786857"
FT MUTAGEN 252
FT /note="T->A: Diminishes LCFA import and decreases
FT nucleotide binding. No effect on localization to the cell
FT membrane."
FT /evidence="ECO:0000269|PubMed:10471110"
SQ SEQUENCE 646 AA; 71276 MW; 910B92BA8D985B4C CRC64;
MRAPGAGTAS VASLALLWFL GLPWTWSAAA AFCVYVGGGG WRFLRIVCKT ARRDLFGLSV
LIRVRLELRR HRRAGDTIPC IFQAVARRQP ERLALVDASS GICWTFAQLD TYSNAVANLF
RQLGFAPGDV VAVFLEGRPE FVGLWLGLAK AGVVAALLNV NLRREPLAFC LGTSAAKALI
YGGEMAAAVA EVSEQLGKSL LKFCSGDLGP ESILPDTQLL DPMLAEAPTT PLAQAPGKGM
DDRLFYIYTS GTTGLPKAAI VVHSRYYRIA AFGHHSYSMR AADVLYDCLP LYHSAGNIMG
VGQCVIYGLT VVLRKKFSAS RFWDDCVKYN CTVVQYIGEI CRYLLRQPVR DVEQRHRVRL
AVGNGLRPAI WEEFTQRFGV PQIGEFYGAT ECNCSIANMD GKVGSCGFNS RILTHVYPIR
LVKVNEDTME PLRDSEGLCI PCQPGEPGLL VGQINQQDPL RRFDGYVSDS ATNKKIAHSV
FRKGDSAYLS GDVLVMDELG YMYFRDRSGD TFRWRGENVS TTEVEAVLSR LLGQTDVAVY
GVAVPGVEGK AGMAAIADPH SQLDPNSMYQ ELQKVLASYA RPIFLRLLPQ VDTTGTFKIQ
KTRLQREGFD PRQTSDRLFF LDLKQGRYVP LDERVHARIC AGDFSL
