S27A1_HUMAN
ID S27A1_HUMAN Reviewed; 646 AA.
AC Q6PCB7; A6NIH2; B7Z662;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 160.
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:0000250|UniProtKB:Q60714};
DE AltName: Full=Fatty acid transport protein 1 {ECO:0000303|PubMed:10873384};
DE Short=FATP-1 {ECO:0000303|PubMed:10873384};
DE AltName: Full=Long-chain-fatty-acid--CoA ligase;
DE EC=6.2.1.3 {ECO:0000250|UniProtKB:Q60714};
DE AltName: Full=Solute carrier family 27 member 1 {ECO:0000312|HGNC:HGNC:10995};
DE AltName: Full=Very long-chain acyl-CoA synthetase;
DE EC=6.2.1.- {ECO:0000250|UniProtKB:Q60714};
GN Name=SLC27A1 {ECO:0000312|HGNC:HGNC:10995}; Synonyms=ACSVL5, FATP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 [5]
RP TISSUE SPECIFICITY.
RX PubMed=10873384; DOI=10.1006/geno.2000.6191;
RA Martin G., Nemoto M., Gelman L., Geffroy S., Najib J., Fruchart J.-C.,
RA Roevens P., de Martinville B., Deeb S., Auwerx J.;
RT "The human fatty acid transport protein-1 (SLC27A1; FATP-1) cDNA and gene:
RT organization, chromosomal localization, and expression.";
RL Genomics 66:296-304(2000).
RN [6]
RP FUNCTION, AND TRANSPORT ACTIVITY.
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 [7]
RP FUNCTION, AND TRANSPORT ACTIVITY.
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 FUNCTION, TRANSPORT ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=21395585; DOI=10.1111/j.1471-4159.2011.07245.x;
RA Mitchell R.W., On N.H., Del Bigio M.R., Miller D.W., Hatch G.M.;
RT "Fatty acid transport protein expression in human brain and potential role
RT in fatty acid transport across human brain microvessel endothelial cells.";
RL J. Neurochem. 117:735-746(2011).
RN [9]
RP FUNCTION, AND INTERACTION WITH EPRS1.
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).
RN [10]
RP INTERACTION WITH DGAT2.
RX PubMed=30970241; DOI=10.1016/j.celrep.2019.03.025;
RA Li D., Zhao Y.G., Li D., Zhao H., Huang J., Miao G., Feng D., Liu P.,
RA Li D., Zhang H.;
RT "The ER-Localized Protein DFCP1 Modulates ER-Lipid Droplet Contact
RT Formation.";
RL Cell Rep. 27:343-358(2019).
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:12556534, PubMed:20530735, PubMed:21395585, PubMed:28178239).
CC Also functions as an acyl-CoA ligase catalyzing the ATP-dependent
CC formation of fatty acyl-CoA using LCFA and very-long-chain fatty acids
CC (VLCFA) as substrates, which prevents fatty acid efflux from cells and
CC might drive more fatty acid uptake. May act directly as a bona fide
CC transporter, or alternatively, in a cytoplasmic or membrane-associated
CC multimeric protein complex to trap and draw fatty acids towards
CC accumulation. 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. May be involved in regulation
CC of cholesterol metabolism (By similarity). Probably involved in fatty
CC acid transport across the blood barrier (PubMed:21395585).
CC {ECO:0000250|UniProtKB:Q60714, ECO:0000269|PubMed:12556534,
CC ECO:0000269|PubMed:20530735, ECO:0000269|PubMed:21395585,
CC ECO:0000269|PubMed:28178239}.
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:12556534,
CC ECO:0000269|PubMed:20530735, ECO:0000269|PubMed:21395585};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoate(out) = (9Z)-octadecenoate(in);
CC Xref=Rhea:RHEA:33655, ChEBI:CHEBI:30823;
CC Evidence={ECO:0000269|PubMed:12556534, ECO:0000269|PubMed:21395585};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoate(out) = hexadecanoate(in); Xref=Rhea:RHEA:45256,
CC ChEBI:CHEBI:7896; Evidence={ECO:0000269|PubMed:12556534,
CC ECO:0000269|PubMed:21395585};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate(out) = (9Z,12Z)-
CC octadecadienoate(in); Xref=Rhea:RHEA:45264, ChEBI:CHEBI:30245;
CC Evidence={ECO:0000269|PubMed:12556534};
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:0000250|UniProtKB:Q60714};
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:0000250|UniProtKB:Q60714};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15422;
CC Evidence={ECO:0000250|UniProtKB:Q60714};
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:0000250|UniProtKB:Q60714};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19714;
CC Evidence={ECO:0000250|UniProtKB:Q60714};
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:0000250|UniProtKB:Q60714};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54537;
CC Evidence={ECO:0000250|UniProtKB:Q60714};
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:0000250|UniProtKB:Q60714};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33640;
CC Evidence={ECO:0000250|UniProtKB:Q60714};
CC -!- ACTIVITY REGULATION: Inhibited by Triacsin C.
CC {ECO:0000250|UniProtKB:Q60714}.
CC -!- SUBUNIT: Self-associates. May function as a homodimer (By similarity).
CC Interacts with EPRS1; mediates the translocation of SLC27A1 from the
CC cytoplasm to the plasma membrane thereby increasing the uptake of long-
CC chain fatty acids (PubMed:28178239). Interacts with DGAT2 and this
CC interaction is enhanced in the presence of ZFYVE1 (PubMed:28178239).
CC {ECO:0000250|UniProtKB:Q60714, ECO:0000269|PubMed:28178239,
CC ECO:0000269|PubMed:30970241}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q60714};
CC Single-pass membrane protein {ECO:0000250|UniProtKB:Q60714}.
CC Endomembrane system {ECO:0000250|UniProtKB:Q60714}; Single-pass
CC membrane protein {ECO:0000250|UniProtKB:Q60714}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q60714}. Note=Plasma membrane and intracellular
CC membranes, at least in adipocytes. In adipocytes, but not myocytes,
CC insulin via the mTORC1 signaling pathway induces a rapid translocation
CC of SLC27A1 from intracellular compartments to the plasma membrane,
CC paralleled by increased LCFA uptake. Insulin-dependent translocation
CC from the cytoplasm to the cell membrane is regulated by EPRS1.
CC Predominantly cytoplasmic in myocytes. {ECO:0000250|UniProtKB:Q60714}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6PCB7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6PCB7-2; Sequence=VSP_055806, VSP_055807;
CC -!- TISSUE SPECIFICITY: Highest levels of expression are detected in muscle
CC and adipose tissue small, intermediate levels in small intestine, and
CC barely detectable in liver (PubMed:10873384, PubMed:21395585).
CC Expressed in brain gray matter (PubMed:21395585).
CC {ECO:0000269|PubMed:10873384, ECO:0000269|PubMed:21395585}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AK299852; BAH13148.1; -; mRNA.
DR EMBL; AC010319; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC010618; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471106; EAW84611.1; -; Genomic_DNA.
DR EMBL; BC059399; AAH59399.1; -; mRNA.
DR CCDS; CCDS32953.1; -. [Q6PCB7-1]
DR RefSeq; NP_940982.1; NM_198580.2. [Q6PCB7-1]
DR RefSeq; XP_011526305.1; XM_011528003.2. [Q6PCB7-1]
DR AlphaFoldDB; Q6PCB7; -.
DR SMR; Q6PCB7; -.
DR BioGRID; 132009; 53.
DR IntAct; Q6PCB7; 1.
DR MINT; Q6PCB7; -.
DR STRING; 9606.ENSP00000252595; -.
DR BindingDB; Q6PCB7; -.
DR ChEMBL; CHEMBL2052038; -.
DR GuidetoPHARMACOLOGY; 1108; -.
DR SwissLipids; SLP:000000427; -.
DR TCDB; 4.C.1.1.9; the fatty acid group translocation (fat) family.
DR iPTMnet; Q6PCB7; -.
DR PhosphoSitePlus; Q6PCB7; -.
DR BioMuta; SLC27A1; -.
DR DMDM; 74749156; -.
DR EPD; Q6PCB7; -.
DR jPOST; Q6PCB7; -.
DR MassIVE; Q6PCB7; -.
DR MaxQB; Q6PCB7; -.
DR PaxDb; Q6PCB7; -.
DR PeptideAtlas; Q6PCB7; -.
DR PRIDE; Q6PCB7; -.
DR ProteomicsDB; 67060; -. [Q6PCB7-1]
DR Antibodypedia; 1644; 168 antibodies from 20 providers.
DR DNASU; 376497; -.
DR Ensembl; ENST00000252595.12; ENSP00000252595.6; ENSG00000130304.17. [Q6PCB7-1]
DR Ensembl; ENST00000598424.5; ENSP00000472313.1; ENSG00000130304.17. [Q6PCB7-2]
DR GeneID; 376497; -.
DR KEGG; hsa:376497; -.
DR MANE-Select; ENST00000252595.12; ENSP00000252595.6; NM_198580.3; NP_940982.1.
DR UCSC; uc002ngu.2; human. [Q6PCB7-1]
DR CTD; 376497; -.
DR DisGeNET; 376497; -.
DR GeneCards; SLC27A1; -.
DR HGNC; HGNC:10995; SLC27A1.
DR HPA; ENSG00000130304; Low tissue specificity.
DR MIM; 600691; gene.
DR neXtProt; NX_Q6PCB7; -.
DR OpenTargets; ENSG00000130304; -.
DR PharmGKB; PA35869; -.
DR VEuPathDB; HostDB:ENSG00000130304; -.
DR eggNOG; KOG1179; Eukaryota.
DR GeneTree; ENSGT00940000159323; -.
DR HOGENOM; CLU_000022_46_2_1; -.
DR InParanoid; Q6PCB7; -.
DR OMA; HHGLIMR; -.
DR OrthoDB; 312083at2759; -.
DR PhylomeDB; Q6PCB7; -.
DR TreeFam; TF313430; -.
DR PathwayCommons; Q6PCB7; -.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR Reactome; R-HSA-804914; Transport of fatty acids.
DR SignaLink; Q6PCB7; -.
DR SIGNOR; Q6PCB7; -.
DR BioGRID-ORCS; 376497; 12 hits in 1071 CRISPR screens.
DR ChiTaRS; SLC27A1; human.
DR GeneWiki; SLC27A1; -.
DR GenomeRNAi; 376497; -.
DR Pharos; Q6PCB7; Tchem.
DR PRO; PR:Q6PCB7; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q6PCB7; protein.
DR Bgee; ENSG00000130304; Expressed in apex of heart and 157 other tissues.
DR ExpressionAtlas; Q6PCB7; baseline and differential.
DR Genevisible; Q6PCB7; HS.
DR GO; GO:0009925; C:basal plasma membrane; ISS:ARUK-UCL.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:ARUK-UCL.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0047676; F:arachidonate-CoA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0015225; F:biotin transmembrane transporter activity; IDA:ARUK-UCL.
DR GO; GO:0015562; F:efflux transmembrane transporter activity; IDA:ARUK-UCL.
DR GO; GO:0015245; F:fatty acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0005324; F:long-chain fatty acid transporter activity; IDA:ARUK-UCL.
DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; ISS: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; ISS:ARUK-UCL.
DR GO; GO:0031957; F:very long-chain fatty acid-CoA ligase activity; IEA:Ensembl.
DR GO; GO:0033211; P:adiponectin-activated signaling pathway; IBA:GO_Central.
DR GO; GO:1905135; P:biotin import across plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0015878; P:biotin transport; IDA:ARUK-UCL.
DR GO; GO:0032049; P:cardiolipin biosynthetic process; IMP:UniProtKB.
DR GO; GO:0140115; P:export across plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0044381; P:glucose import in response to insulin stimulus; ISS:ARUK-UCL.
DR GO; GO:1990379; P:lipid transport across blood-brain barrier; IMP:ARUK-UCL.
DR GO; GO:0015911; P:long-chain fatty acid import across plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0044539; P:long-chain fatty acid import into cell; IMP:UniProtKB.
DR GO; GO:0015909; P:long-chain fatty acid transport; IDA:ARUK-UCL.
DR GO; GO:0001579; P:medium-chain fatty acid transport; IBA:GO_Central.
DR GO; GO:0071072; P:negative regulation of phospholipid biosynthetic process; IMP:UniProtKB.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IMP:UniProtKB.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IMP:UniProtKB.
DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; IMP:UniProtKB.
DR GO; GO:0006655; P:phosphatidylglycerol biosynthetic process; IMP:UniProtKB.
DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; IMP:UniProtKB.
DR GO; GO:0006659; P:phosphatidylserine biosynthetic process; IMP:UniProtKB.
DR GO; GO:0031652; P:positive regulation of heat generation; IBA:GO_Central.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; ISS:UniProtKB.
DR GO; GO:0009409; P:response to cold; IBA:GO_Central.
DR GO; GO:0032868; P:response to insulin; IBA:GO_Central.
DR GO; GO:0150104; P:transport across blood-brain barrier; NAS:ARUK-UCL.
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; IPR030308; FATP1.
DR PANTHER; PTHR43107:SF7; PTHR43107:SF7; 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 Alternative splicing; Cell membrane; Cytoplasm; Fatty acid metabolism;
KW Ligase; Lipid metabolism; Lipid transport; Membrane; Nucleotide-binding;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..646
FT /note="Long-chain fatty acid transport protein 1"
FT /id="PRO_0000193201"
FT TOPO_DOM 1..13
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q60714"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..646
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q60714"
FT REGION 191..475
FT /note="Sufficient for oligomerization"
FT /evidence="ECO:0000250|UniProtKB:Q60714"
FT BINDING 246..257
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q60714"
FT VAR_SEQ 1..8
FT /note="MRAPGAGA -> MTHVLGTT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055806"
FT VAR_SEQ 9..187
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055807"
SQ SEQUENCE 646 AA; 71108 MW; 0E1FBA81922567E0 CRC64;
MRAPGAGAAS VVSLALLWLL GLPWTWSAAA ALGVYVGSGG WRFLRIVCKT ARRDLFGLSV
LIRVRLELRR HQRAGHTIPR IFQAVVQRQP ERLALVDAGT GECWTFAQLD AYSNAVANLF
RQLGFAPGDV VAIFLEGRPE FVGLWLGLAK AGMEAALLNV NLRREPLAFC LGTSGAKALI
FGGEMVAAVA EVSGHLGKSL IKFCSGDLGP EGILPDTHLL DPLLKEASTA PLAQIPSKGM
DDRLFYIYTS GTTGLPKAAI VVHSRYYRMA AFGHHAYRMQ AADVLYDCLP LYHSAGNIIG
VGQCLIYGLT VVLRKKFSAS RFWDDCIKYN CTVVQYIGEI CRYLLKQPVR EAERRHRVRL
AVGNGLRPAI WEEFTERFGV RQIGEFYGAT ECNCSIANMD GKVGSCGFNS RILPHVYPIR
LVKVNEDTME LLRDAQGLCI PCQAGEPGLL VGQINQQDPL RRFDGYVSES ATSKKIAHSV
FSKGDSAYLS GDVLVMDELG YMYFRDRSGD TFRWRGENVS TTEVEGVLSR LLGQTDVAVY
GVAVPGVEGK AGMAAVADPH SLLDPNAIYQ ELQKVLAPYA RPIFLRLLPQ VDTTGTFKIQ
KTRLQREGFD PRQTSDRLFF LDLKQGHYLP LNEAVYTRIC SGAFAL
