ID   S27A5_HUMAN             Reviewed;         690 AA.
AC   Q9Y2P5; B3KVP6; B4DPQ1;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   10-JUN-2026, entry version 168.
DE   RecName: Full=Long-chain fatty acid transport protein 5 {ECO:0000305};
DE            Short=FATP-5 {ECO:0000303|PubMed:20448275, ECO:0000303|PubMed:20530735};
DE            Short=Fatty acid transport protein 5 {ECO:0000303|PubMed:20530735};
DE   AltName: Full=Bile acid-CoA ligase {ECO:0000250|UniProtKB:Q9ES38};
DE            Short=BA-CoA ligase {ECO:0000250|UniProtKB:Q9ES38};
DE            Short=BAL {ECO:0000250|UniProtKB:Q9ES38};
DE   AltName: Full=Bile acyl-CoA synthetase {ECO:0000303|PubMed:11980911};
DE            Short=BACS {ECO:0000303|PubMed:11980911};
DE            EC=6.2.1.7 {ECO:0000269|PubMed:10479480, ECO:0000269|PubMed:10749848, ECO:0000269|PubMed:11980911};
DE   AltName: Full=Cholate--CoA ligase {ECO:0000303|PubMed:10749848};
DE   AltName: Full=Fatty-acid-coenzyme A ligase, very long-chain 3;
DE   AltName: Full=Long-chain-fatty-acid--CoA ligase;
DE            EC=6.2.1.3 {ECO:0000269|PubMed:10479480};
DE   AltName: Full=Solute carrier family 27 member 5;
DE   AltName: Full=Very long-chain acyl-CoA synthetase homolog 2 {ECO:0000303|PubMed:10479480, ECO:0000303|PubMed:10749848};
DE            Short=VLCS-H2 {ECO:0000303|PubMed:10479480, ECO:0000303|PubMed:10749848, ECO:0000303|PubMed:11980911};
DE            Short=VLCSH2 {ECO:0000303|PubMed:10479480, ECO:0000303|PubMed:10749848, ECO:0000303|PubMed:11980911};
DE            EC=6.2.1.- {ECO:0000269|PubMed:10479480};
DE   AltName: Full=Very long-chain acyl-CoA synthetase-related protein {ECO:0000250|UniProtKB:Q4LDG0};
DE            Short=VLACS-related {ECO:0000250|UniProtKB:Q4LDG0};
DE            Short=VLACSR {ECO:0000250|UniProtKB:Q4LDG0};
GN   Name=SLC27A5; Synonyms=ACSB, ACSVL6, FACVL3, FATP5;
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), FUNCTION, CATALYTIC ACTIVITY,
RP   TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=10479480; DOI=10.1006/mgme.1999.2883;
RA   Steinberg S.J., Wang S.J., McGuinness M.C., Watkins P.A.;
RT   "Human liver-specific very-long-chain acyl-coenzyme A synthetase: cDNA
RT   cloning and characterization of a second enzymatically active protein.";
RL   Mol. Genet. Metab. 68:32-42(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Liver;
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   [3]
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   [4]
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   [5]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=10749848; DOI=10.1074/jbc.c000015200;
RA   Steinberg S.J., Mihalik S.J., Kim D.G., Cuebas D.A., Watkins P.A.;
RT   "The human liver-specific homolog of very long-chain acyl-CoA synthetase is
RT   cholate:CoA ligase.";
RL   J. Biol. Chem. 275:15605-15608(2000).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, TOPOLOGY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   ACTIVITY REGULATION.
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   [7]
RP   FUNCTION, AND TRANSPORT ACTIVITY.
RX   PubMed=20448275; DOI=10.1177/1087057110369700;
RA   Zhou W., Madrid P., Fluitt A., Stahl A., Xie X.S.;
RT   "Development and validation of a high-throughput screening assay for human
RT   long-chain fatty acid transport proteins 4 and 5.";
RL   J. Biomol. Screen. 15:488-497(2010).
RN   [8]
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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-501, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- FUNCTION: May mediate the import of long-chain fatty acids (LCFA) by
CC       facilitating their transport across cell membranes (PubMed:20448275,
CC       PubMed:20530735). Also catalyzes the ATP-dependent formation of fatty
CC       acyl-CoA using LCFA and very-long-chain fatty acids (VLCFA) as
CC       substrates (PubMed:10479480). Mainly functions as a bile acyl-CoA
CC       synthetase catalyzing the activation of bile acids via ATP-dependent
CC       formation of bile acid CoA thioesters which is necessary for their
CC       subsequent conjugation with glycine or taurine (PubMed:10749848,
CC       PubMed:11980911). Both primary bile acids (cholic acid and
CC       chenodeoxycholic acid) and secondary bile acids (deoxycholic acid and
CC       lithocholic acid) are the principal substrates (PubMed:10749848,
CC       PubMed:11980911). In vitro, activates 3-alpha,7-alpha,12-alpha-
CC       trihydroxy-5-beta-cholestanate ((25R)-3alpha,7alpha,12alpha-trihydroxy-
CC       5beta-cholestan-26-oate or THCA), the C27 precursor of cholic acid
CC       deriving from the de novo synthesis from cholesterol (PubMed:11980911).
CC       Plays an important role in hepatic fatty acid uptake and bile acid
CC       reconjugation and recycling but not in de novo synthesis of bile acids
CC       (By similarity). {ECO:0000250|UniProtKB:Q4LDG0,
CC       ECO:0000269|PubMed:10479480, ECO:0000269|PubMed:10749848,
CC       ECO:0000269|PubMed:11980911, ECO:0000269|PubMed:20448275,
CC       ECO:0000269|PubMed:20530735}.
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:20448275,
CC         ECO:0000269|PubMed:20530735};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cholate + ATP + CoA = choloyl-CoA + AMP + diphosphate;
CC         Xref=Rhea:RHEA:23532, ChEBI:CHEBI:29747, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57373,
CC         ChEBI:CHEBI:456215; EC=6.2.1.7;
CC         Evidence={ECO:0000269|PubMed:10479480, ECO:0000269|PubMed:10749848,
CC         ECO:0000269|PubMed:11980911};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23533;
CC         Evidence={ECO:0000305|PubMed:10479480, ECO:0000305|PubMed:10749848,
CC         ECO:0000305|PubMed:11980911};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chenodeoxycholate + ATP + CoA = chenodeoxycholoyl-CoA + AMP +
CC         diphosphate; Xref=Rhea:RHEA:43764, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:36234, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:62989, ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000269|PubMed:11980911};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43765;
CC         Evidence={ECO:0000305|PubMed:11980911};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=deoxycholate + ATP + CoA = deoxycholoyl-CoA + AMP +
CC         diphosphate; Xref=Rhea:RHEA:47128, ChEBI:CHEBI:23614,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:58810, ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000269|PubMed:11980911};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47129;
CC         Evidence={ECO:0000305|PubMed:11980911};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=lithocholate + ATP + CoA = lithocholoyl-CoA + AMP +
CC         diphosphate; Xref=Rhea:RHEA:47136, ChEBI:CHEBI:29744,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:87438, ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000269|PubMed:11980911};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47137;
CC         Evidence={ECO:0000305|PubMed:11980911};
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:0000269|PubMed:11980911};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22977;
CC         Evidence={ECO:0000305|PubMed:11980911};
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:10479480};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54537;
CC         Evidence={ECO:0000305|PubMed:10479480};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=tetracosanoate + ATP + CoA = tetracosanoyl-CoA + AMP +
CC         diphosphate; 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:10479480};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33640;
CC         Evidence={ECO:0000305|PubMed:10479480};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hexacosanoate + ATP + CoA = hexacosanoyl-CoA + AMP +
CC         diphosphate; Xref=Rhea:RHEA:43748, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:31013, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:64868, ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000269|PubMed:10479480};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43749;
CC         Evidence={ECO:0000305|PubMed:10479480};
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:10479480};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15422;
CC         Evidence={ECO:0000305|PubMed:10479480};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=octadecanoate + ATP + CoA = octadecanoyl-CoA + AMP +
CC         diphosphate; Xref=Rhea:RHEA:33615, ChEBI:CHEBI:25629,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57394, ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000269|PubMed:10479480};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33616;
CC         Evidence={ECO:0000305|PubMed:10479480};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=eicosanoate + ATP + CoA = eicosanoyl-CoA + AMP + diphosphate;
CC         Xref=Rhea:RHEA:46208, ChEBI:CHEBI:30616, ChEBI:CHEBI:32360,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57380,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:10479480};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46209;
CC         Evidence={ECO:0000305|PubMed:10479480};
CC   -!- ACTIVITY REGULATION: 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-
CC       cholestanate (THCA) inhibits the activation of cholate.
CC       {ECO:0000269|PubMed:11980911}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.8 uM for cholate {ECO:0000269|PubMed:11980911};
CC         Vmax=3.8 nmol/min/mg enzyme with cholate as substrate for bile
CC         acyl-CoA synthetase activity {ECO:0000269|PubMed:11980911};
CC   -!- INTERACTION:
CC       Q9Y2P5; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-12176609, EBI-16439278;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:10479480}; Multi-pass membrane protein
CC       {ECO:0000255}. Microsome {ECO:0000250|UniProtKB:Q9ES38}. Cell membrane
CC       {ECO:0000250|UniProtKB:Q4LDG0}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9Y2P5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9Y2P5-2; Sequence=VSP_055810;
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in liver.
CC       {ECO:0000269|PubMed:10479480}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; AF064255; AAD29444.1; -; mRNA.
DR   EMBL; AK123036; BAG53858.1; -; mRNA.
DR   EMBL; AK298446; BAG60663.1; -; mRNA.
DR   EMBL; AC012313; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471135; EAW72601.1; -; Genomic_DNA.
DR   CCDS; CCDS12983.1; -. [Q9Y2P5-1]
DR   CCDS; CCDS82415.1; -. [Q9Y2P5-2]
DR   RefSeq; NP_001308125.1; NM_001321196.2. [Q9Y2P5-2]
DR   RefSeq; NP_036386.1; NM_012254.3. [Q9Y2P5-1]
DR   AlphaFoldDB; Q9Y2P5; -.
DR   SMR; Q9Y2P5; -.
DR   BioGRID; 116191; 103.
DR   FunCoup; Q9Y2P5; 264.
DR   IntAct; Q9Y2P5; 98.
DR   NDEx; IQUERY-CP-SLC27A5; 7 NDEx IQuery Curated Pathways.
DR   STRING; 9606.ENSP00000263093; -.
DR   ChEMBL; CHEMBL5196; -.
DR   SwissLipids; SLP:000000429; -.
DR   SwissLipids; SLP:000001315; -. [Q9Y2P5-1]
DR   TCDB; 4.C.1.1.13; the fatty acid group translocation (fat) family.
DR   GlyGen; Q9Y2P5; 1 site.
DR   iPTMnet; Q9Y2P5; -.
DR   PhosphoSitePlus; Q9Y2P5; -.
DR   BioMuta; SLC27A5; -.
DR   DMDM; 74739456; -.
DR   jPOST; Q9Y2P5; -.
DR   MassIVE; Q9Y2P5; -.
DR   PaxDb; 9606-ENSP00000263093; -.
DR   PeptideAtlas; Q9Y2P5; -.
DR   ProteomicsDB; 85854; -. [Q9Y2P5-1]
DR   Antibodypedia; 1943; 305 antibodies from 27 providers.
DR   DNASU; 10998; -.
DR   Ensembl; ENST00000263093.7; ENSP00000263093.2; ENSG00000083807.11. [Q9Y2P5-1]
DR   Ensembl; ENST00000601355.1; ENSP00000470368.1; ENSG00000083807.11. [Q9Y2P5-2]
DR   Ensembl; ENST00000864562.1; ENSP00000534621.1; ENSG00000083807.11. [Q9Y2P5-1]
DR   Ensembl; ENST00000864563.1; ENSP00000534622.1; ENSG00000083807.11. [Q9Y2P5-1]
DR   Ensembl; ENST00000864564.1; ENSP00000534623.1; ENSG00000083807.11. [Q9Y2P5-1]
DR   Ensembl; ENST00000864565.1; ENSP00000534624.1; ENSG00000083807.11. [Q9Y2P5-2]
DR   Ensembl; ENST00000864566.1; ENSP00000534625.1; ENSG00000083807.11. [Q9Y2P5-1]
DR   GeneID; 10998; -.
DR   KEGG; hsa:10998; -.
DR   MANE-Select; ENST00000263093.7; ENSP00000263093.2; NM_012254.3; NP_036386.1.
DR   UCSC; uc002qtc.3; human. [Q9Y2P5-1]
DR   AGR; HGNC:10999; -.
DR   ClinPGx; PA35873; -.
DR   CTD; 10998; -.
DR   DisGeNET; 10998; -.
DR   GeneCards; SLC27A5; -.
DR   HGNC; HGNC:10999; SLC27A5.
DR   HPA; ENSG00000083807; Tissue enriched (liver).
DR   MalaCards; SLC27A5; -.
DR   MIM; 603314; gene.
DR   OpenTargets; ENSG00000083807; -.
DR   VEuPathDB; HostDB:ENSG00000083807; -.
DR   eggNOG; KOG1179; Eukaryota.
DR   GeneTree; ENSGT00940000157947; -.
DR   HOGENOM; CLU_000022_46_2_1; -.
DR   InParanoid; Q9Y2P5; -.
DR   OMA; ATFFTYV; -.
DR   OrthoDB; 288590at2759; -.
DR   PAN-GO; Q9Y2P5; 7 GO annotations based on evolutionary models.
DR   PhylomeDB; Q9Y2P5; -.
DR   PathwayCommons; Q9Y2P5; -.
DR   Reactome; R-HSA-159418; Recycling of bile acids and salts.
DR   Reactome; R-HSA-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
DR   Reactome; R-HSA-193775; Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
DR   SignaLink; Q9Y2P5; -.
DR   SIGNOR; Q9Y2P5; -.
DR   Agora; ENSG00000083807; -.
DR   BioGRID-ORCS; 10998; 25 hits in 1158 CRISPR screens.
DR   ChiTaRS; SLC27A5; human.
DR   GeneWiki; SLC27A5; -.
DR   GenomeRNAi; 10998; -.
DR   Pharos; Q9Y2P5; Tbio.
DR   PRO; PR:Q9Y2P5; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; Q9Y2P5; protein.
DR   Bgee; ENSG00000083807; Expressed in right lobe of liver and 128 other cell types or tissues.
DR   ExpressionAtlas; Q9Y2P5; baseline and differential.
DR   GO; GO:0009925; C:basal plasma membrane; IEA:Ensembl.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0047747; F:cholate-CoA ligase activity; IDA:UniProtKB.
DR   GO; GO:0005324; F:long-chain fatty acid transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IBA:GO_Central.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR   GO; GO:0031957; F:very long-chain fatty acid-CoA ligase activity; IDA:UniProtKB.
DR   GO; GO:0015721; P:bile acid and bile salt transport; TAS:Reactome.
DR   GO; GO:0006699; P:bile acid biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0008206; P:bile acid metabolic process; IBA:GO_Central.
DR   GO; GO:0044539; P:long-chain fatty acid import into cell; IBA:GO_Central.
DR   GO; GO:0001676; P:long-chain fatty acid metabolic process; IBA:GO_Central.
DR   GO; GO:0000038; P:very long-chain fatty acid metabolic process; IDA:UniProtKB.
DR   CDD; cd05938; hsFATP2a_ACSVL_like; 1.
DR   FunFam; 3.30.300.30:FF:000002; Long-chain fatty acid transport protein 1; 1.
DR   FunFam; 3.40.50.12780:FF:000005; Solute carrier family 27 member 6; 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_dom.
DR   InterPro; IPR042099; ANL_N_sf.
DR   PANTHER; PTHR43107; LONG-CHAIN FATTY ACID TRANSPORT PROTEIN; 1.
DR   PANTHER; PTHR43107:SF25; LONG-CHAIN FATTY ACID TRANSPORT PROTEIN 5; 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.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Cell membrane; Endoplasmic reticulum;
KW   Fatty acid metabolism; Ligase; Lipid metabolism; Lipid transport; Membrane;
KW   Microsome; Nucleotide-binding; Oxidoreductase; Phosphoprotein;
KW   Proteomics identification; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..690
FT                   /note="Long-chain fatty acid transport protein 5"
FT                   /id="PRO_0000193213"
FT   TOPO_DOM        1..30
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:11980911"
FT   TRANSMEM        31..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        56..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        77..690
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:11980911"
FT   BINDING         292..303
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         501
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   VAR_SEQ         146..229
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_055810"
FT   VARIANT         50
FT                   /note="M -> T (in dbSNP:rs35350976)"
FT                   /id="VAR_048243"
FT   VARIANT         53
FT                   /note="R -> W (in dbSNP:rs34415062)"
FT                   /id="VAR_048244"
SQ   SEQUENCE   690 AA;  75385 MW;  011313424D794546 CRC64;
     MGVRQQLALL LLLLLLLWGL GQPVWPVAVA LTLRWLLGDP TCCVLLGLAM LARPWLGPWV
     PHGLSLAAAA LALTLLPARL PPGLRWLPAD VIFLAKILHL GLKIRGCLSR QPPDTFVDAF
     ERRARAQPGR ALLVWTGPGA GSVTFGELDA RACQAAWALK AELGDPASLC AGEPTALLVL
     ASQAVPALCM WLGLAKLGCP TAWINPHGRG MPLAHSVLSS GARVLVVDPD LRESLEEILP
     KLQAENIRCF YLSHTSPTPG VGALGAALDA APSHPVPADL RAGITWRSPA LFIYTSGTTG
     LPKPAILTHE RVLQMSKMLS LSGATADDVV YTVLPLYHVM GLVVGILGCL DLGATCVLAP
     KFSTSCFWDD CRQHGVTVIL YVGELLRYLC NIPQQPEDRT HTVRLAMGNG LRADVWETFQ
     QRFGPIRIWE VYGSTEGNMG LVNYVGRCGA LGKMSCLLRM LSPFELVQFD MEAAEPVRDN
     QGFCIPVGLG EPGLLLTKVV SQQPFVGYRG PRELSERKLV RNVRQSGDVY YNTGDVLAMD
     REGFLYFRDR LGDTFRWKGE NVSTHEVEGV LSQVDFLQQV NVYGVCVPGC EGKVGMAAVQ
     LAPGQTFDGE KLYQHVRAWL PAYATPHFIR IQDAMEVTST FKLMKTRLVR EGFNVGIVVD
     PLFVLDNRAQ SFRPLTAEMY QAVCEGTWRL
//