ID   S27A3_HUMAN             Reviewed;         683 AA.
AC   Q5K4L6; Q5VUQ7; Q5VUQ8; Q5VUR3; Q6ZV16; Q8N2X7; Q8TEJ0; Q96SW5; Q9BTJ5;
AC   Q9BTY5;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-JAN-2019, sequence version 4.
DT   27-MAR-2024, entry version 162.
DE   RecName: Full=Long-chain fatty acid transport protein 3 {ECO:0000250|UniProtKB:O88561};
DE            Short=FATP-3 {ECO:0000250|UniProtKB:O88561};
DE            Short=Fatty acid transport protein 3 {ECO:0000250|UniProtKB:O88561};
DE   AltName: Full=Arachidonate--CoA ligase {ECO:0000303|PubMed:23936004};
DE            EC=6.2.1.15 {ECO:0000269|PubMed:23936004};
DE   AltName: Full=Long-chain-fatty-acid--CoA ligase;
DE            EC=6.2.1.3 {ECO:0000269|PubMed:23936004};
DE   AltName: Full=Solute carrier family 27 member 3 {ECO:0000312|HGNC:HGNC:10997};
DE   AltName: Full=Very long-chain acyl-CoA synthetase homolog 3 {ECO:0000312|EMBL:CAE12159.1};
DE            Short=VLCS-3 {ECO:0000312|EMBL:CAE12159.1};
DE            EC=6.2.1.- {ECO:0000250|UniProtKB:O88561};
GN   Name=SLC27A3 {ECO:0000312|HGNC:HGNC:10997};
GN   Synonyms=ACSVL3 {ECO:0000303|PubMed:23936004}, FATP3;
GN   ORFNames=PSEC0067, UNQ367/PRO703;
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 [MRNA] (ISOFORM 1).
RC   TISSUE=Liver, and Testis;
RA   Berger J.;
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Spleen;
RA   Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O.;
RT   "The nucleotide sequence of a long cDNA clone isolated from human spleen.";
RL   Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Neuron, Teratocarcinoma, and Tongue;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 250-683 (ISOFORM 2).
RC   TISSUE=Brain, and Lung;
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   [7]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=23936004; DOI=10.1371/journal.pone.0069392;
RA   Pei Z., Fraisl P., Shi X., Gabrielson E., Forss-Petter S., Berger J.,
RA   Watkins P.A.;
RT   "Very long-chain acyl-CoA synthetase 3: overexpression and growth
RT   dependence in lung cancer.";
RL   PLoS ONE 8:E69392-E69392(2013).
CC   -!- FUNCTION: Mainly functions as an acyl-CoA ligase catalyzing the ATP-
CC       dependent formation of fatty acyl-CoA using LCFA and very-long-chain
CC       fatty acids (VLCFA) as substrates (PubMed:23936004). Can mediate the
CC       levels of long-chain fatty acids (LCFA) in the cell by facilitating
CC       their transport across membranes (By similarity).
CC       {ECO:0000250|UniProtKB:O88561, ECO:0000269|PubMed:23936004}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a fatty acid(in) = a fatty acid(out); Xref=Rhea:RHEA:38879,
CC         ChEBI:CHEBI:28868; Evidence={ECO:0000250|UniProtKB:O88561};
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:23936004};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15422;
CC         Evidence={ECO:0000269|PubMed:23936004};
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:0000269|PubMed:23936004};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30752;
CC         Evidence={ECO:0000269|PubMed:23936004};
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:23936004};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33608;
CC         Evidence={ECO:0000269|PubMed:23936004};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z,12Z)-octadecadienoate + ATP + CoA = (9Z,12Z)-
CC         octadecadienoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:33651,
CC         ChEBI:CHEBI:30245, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57383, ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000269|PubMed:23936004};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33652;
CC         Evidence={ECO:0000269|PubMed:23936004};
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:23936004};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19714;
CC         Evidence={ECO:0000269|PubMed:23936004};
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:O88561};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54537;
CC         Evidence={ECO:0000250|UniProtKB:O88561};
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:O88561};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33640;
CC         Evidence={ECO:0000250|UniProtKB:O88561};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC       {ECO:0000269|PubMed:23936004}; Single-pass membrane protein
CC       {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q5K4L6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5K4L6-2; Sequence=VSP_016218;
CC       Name=3;
CC         IsoId=Q5K4L6-3; Sequence=VSP_036534, VSP_036535;
CC   -!- TISSUE SPECIFICITY: Expressed in bronchial and bronchiolar epithelial
CC       cells (at protein level). {ECO:0000269|PubMed:23936004}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH03041.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAH09916.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAH29792.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAQ88775.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAB55156.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAB84960.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAC11578.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAC86050.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAC86050.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=CAE12159.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AJ577572; CAE12159.1; ALT_INIT; mRNA.
DR   EMBL; AK074134; BAB84960.1; ALT_INIT; mRNA.
DR   EMBL; AY358409; AAQ88775.1; ALT_INIT; mRNA.
DR   EMBL; AK027499; BAB55156.1; ALT_INIT; mRNA.
DR   EMBL; AK075377; BAC11578.1; ALT_INIT; mRNA.
DR   EMBL; AK125102; BAC86050.1; ALT_SEQ; mRNA.
DR   EMBL; AL513523; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC003041; AAH03041.1; ALT_INIT; mRNA.
DR   EMBL; BC003654; AAH03654.2; -; mRNA.
DR   EMBL; BC009916; AAH09916.1; ALT_INIT; mRNA.
DR   EMBL; BC029792; AAH29792.1; ALT_INIT; mRNA.
DR   CCDS; CCDS1053.3; -. [Q5K4L6-1]
DR   RefSeq; NP_001304858.2; NM_001317929.2. [Q5K4L6-2]
DR   RefSeq; NP_077306.2; NM_024330.2. [Q5K4L6-1]
DR   AlphaFoldDB; Q5K4L6; -.
DR   SMR; Q5K4L6; -.
DR   BioGRID; 116193; 134.
DR   IntAct; Q5K4L6; 24.
DR   MINT; Q5K4L6; -.
DR   STRING; 9606.ENSP00000271857; -.
DR   SwissLipids; SLP:000001267; -.
DR   TCDB; 4.C.1.1.12; the fatty acid group translocation (fat) family.
DR   GlyGen; Q5K4L6; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q5K4L6; -.
DR   PhosphoSitePlus; Q5K4L6; -.
DR   SwissPalm; Q5K4L6; -.
DR   BioMuta; SLC27A3; -.
DR   DMDM; 215274206; -.
DR   EPD; Q5K4L6; -.
DR   jPOST; Q5K4L6; -.
DR   MassIVE; Q5K4L6; -.
DR   MaxQB; Q5K4L6; -.
DR   PaxDb; 9606-ENSP00000485061; -.
DR   PeptideAtlas; Q5K4L6; -.
DR   ProteomicsDB; 63544; -. [Q5K4L6-1]
DR   ProteomicsDB; 63545; -. [Q5K4L6-2]
DR   ProteomicsDB; 63546; -. [Q5K4L6-3]
DR   Pumba; Q5K4L6; -.
DR   Antibodypedia; 1669; 133 antibodies from 22 providers.
DR   CPTC; Q5K4L6; 4 antibodies.
DR   DNASU; 11000; -.
DR   Ensembl; ENST00000623839.3; ENSP00000485585.1; ENSG00000263163.5.
DR   Ensembl; ENST00000624995.4; ENSP00000485061.2; ENSG00000143554.14. [Q5K4L6-1]
DR   GeneID; 11000; -.
DR   KEGG; hsa:11000; -.
DR   MANE-Select; ENST00000624995.4; ENSP00000485061.2; NM_024330.4; NP_077306.3.
DR   UCSC; uc001fcz.3; human. [Q5K4L6-1]
DR   AGR; HGNC:10997; -.
DR   DisGeNET; 11000; -.
DR   GeneCards; SLC27A3; -.
DR   HGNC; HGNC:10997; SLC27A3.
DR   HPA; ENSG00000143554; Low tissue specificity.
DR   MIM; 604193; gene.
DR   neXtProt; NX_Q5K4L6; -.
DR   OpenTargets; ENSG00000143554; -.
DR   PharmGKB; PA35871; -.
DR   VEuPathDB; HostDB:ENSG00000143554; -.
DR   eggNOG; KOG1179; Eukaryota.
DR   GeneTree; ENSGT00940000161073; -.
DR   HOGENOM; CLU_000022_46_2_1; -.
DR   InParanoid; Q5K4L6; -.
DR   OrthoDB; 1650656at2759; -.
DR   PhylomeDB; Q5K4L6; -.
DR   TreeFam; TF313430; -.
DR   PathwayCommons; Q5K4L6; -.
DR   Reactome; R-HSA-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR   SignaLink; Q5K4L6; -.
DR   SIGNOR; Q5K4L6; -.
DR   BioGRID-ORCS; 11000; 10 hits in 1118 CRISPR screens.
DR   ChiTaRS; SLC27A3; human.
DR   GeneWiki; SLC27A3; -.
DR   GenomeRNAi; 11000; -.
DR   Pharos; Q5K4L6; Tbio.
DR   PRO; PR:Q5K4L6; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q5K4L6; Protein.
DR   Bgee; ENSG00000143554; Expressed in granulocyte and 95 other cell types or tissues.
DR   ExpressionAtlas; Q5K4L6; baseline and differential.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; 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:0005324; F:long-chain fatty acid transporter activity; IBA:GO_Central.
DR   GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IDA:UniProtKB.
DR   GO; GO:0031957; F:very long-chain fatty acid-CoA ligase activity; IDA:UniProtKB.
DR   GO; GO:0015908; P:fatty acid transport; IMP:ARUK-UCL.
DR   GO; GO:0001676; P:long-chain fatty acid metabolic process; IDA:UniProtKB.
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:SF12; SOLUTE CARRIER FAMILY 27 MEMBER 3; 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; Q5K4L6; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Fatty acid metabolism; Ligase;
KW   Lipid metabolism; Lipid transport; Membrane; Mitochondrion;
KW   Nucleotide-binding; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..683
FT                   /note="Long-chain fatty acid transport protein 3"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000193207"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          119..145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         288..292
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT   BINDING         331
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT   BINDING         428
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT   BINDING         528
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT   BINDING         543
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT   BINDING         635
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9SMT7"
FT   VAR_SEQ         223..229
FT                   /note="EFLESLE -> GKAGAPN (in isoform 3)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_036534"
FT   VAR_SEQ         230..683
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_036535"
FT   VAR_SEQ         626..660
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_016218"
FT   VARIANT         63
FT                   /note="G -> A (in dbSNP:rs34527123)"
FT                   /id="VAR_048241"
FT   VARIANT         392
FT                   /note="R -> H (in dbSNP:rs35102232)"
FT                   /id="VAR_048242"
FT   CONFLICT        19
FT                   /note="K -> M (in Ref. 1; CAE12159)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        425
FT                   /note="Y -> F (in Ref. 6; AAH03654)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   683 AA;  73550 MW;  1B18B85D5FF17A94 CRC64;
     MAALLLLPLL LLLPLLLLKL HLWPQLRWLP ADLAFAVRAL CCKRALRARA LAAAAADPEG
     PEGGCSLAWR LAELAQQRAA HTFLIHGSRR FSYSEAERES NRAARAFLRA LGWDWGPDGG
     DSGEGSAGEG ERAAPGAGDA AAGSGAEFAG GDGAARGGGA AAPLSPGATV ALLLPAGPEF
     LWLWFGLAKA GLRTAFVPTA LRRGPLLHCL RSCGARALVL APEFLESLEP DLPALRAMGL
     HLWAAGPGTH PAGISDLLAE VSAEVDGPVP GYLSSPQSIT DTCLYIFTSG TTGLPKAARI
     SHLKILQCQG FYQLCGVHQE DVIYLALPLY HMSGSLLGIV GCMGIGATVV LKSKFSAGQF
     WEDCQQHRVT VFQYIGELCR YLVNQPPSKA ERGHKVRLAV GSGLRPDTWE RFVRRFGPLQ
     VLETYGLTEG NVATINYTGQ RGAVGRASWL YKHIFPFSLI RYDVTTGEPI RDPQGHCMAT
     SPGEPGLLVA PVSQQSPFLG YAGGPELAQG KLLKDVFRPG DVFFNTGDLL VCDDQGFLRF
     HDRTGDTFRW KGENVATTEV AEVFEALDFL QEVNVYGVTV PGHEGRAGMA ALVLRPPHAL
     DLMQLYTHVS ENLPPYARPR FLRLQESLAT TETFKQQKVR MANEGFDPST LSDPLYVLDQ
     AVGAYLPLTT ARYSALLAGN LRI
//