S27A3_HUMAN
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 03-AUG-2022, entry version 153.
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; CCDS1053.2; -. [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; 126.
DR IntAct; Q5K4L6; 21.
DR MINT; Q5K4L6; -.
DR STRING; 9606.ENSP00000485061; -.
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; Q5K4L6; -.
DR PeptideAtlas; Q5K4L6; -.
DR PRIDE; Q5K4L6; -.
DR ProteomicsDB; 63544; -. [Q5K4L6-1]
DR ProteomicsDB; 63545; -. [Q5K4L6-2]
DR ProteomicsDB; 63546; -. [Q5K4L6-3]
DR Antibodypedia; 1669; 125 antibodies from 21 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 CTD; 11000; -.
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; 298283at2759; -.
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; 9 hits in 1039 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 93 other tissues.
DR ExpressionAtlas; Q5K4L6; baseline and differential.
DR Genevisible; Q5K4L6; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 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; IPR030307; SLC27A3.
DR PANTHER; PTHR43107:SF12; PTHR43107:SF12; 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; 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
