S27A5_HUMAN
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 03-AUG-2022, entry version 151.
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=ATP + cholate + CoA = AMP + choloyl-CoA + 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=ATP + chenodeoxycholate + CoA = AMP + chenodeoxycholoyl-CoA +
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=ATP + CoA + deoxycholate = AMP + deoxycholoyl-CoA +
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=ATP + CoA + lithocholate = AMP + diphosphate + lithocholoyl-
CC CoA; Xref=Rhea:RHEA:47136, ChEBI:CHEBI:29744, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:87438,
CC ChEBI:CHEBI:456215; 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=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:10479480};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33640;
CC Evidence={ECO:0000305|PubMed:10479480};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + CoA + hexacosanoate = AMP + diphosphate + hexacosanoyl-
CC CoA; Xref=Rhea:RHEA:43748, ChEBI:CHEBI:30616, ChEBI:CHEBI:31013,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:64868,
CC ChEBI:CHEBI:456215; 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=ATP + CoA + octadecanoate = AMP + diphosphate + octadecanoyl-
CC CoA; Xref=Rhea:RHEA:33615, ChEBI:CHEBI:25629, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394,
CC ChEBI:CHEBI:456215; 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=ATP + CoA + eicosanoate = AMP + diphosphate + eicosanoyl-CoA;
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 acyl-
CC 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_001321196.1. [Q9Y2P5-2]
DR RefSeq; NP_036386.1; NM_012254.2. [Q9Y2P5-1]
DR AlphaFoldDB; Q9Y2P5; -.
DR SMR; Q9Y2P5; -.
DR BioGRID; 116191; 9.
DR IntAct; Q9Y2P5; 1.
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 iPTMnet; Q9Y2P5; -.
DR PhosphoSitePlus; Q9Y2P5; -.
DR BioMuta; SLC27A5; -.
DR DMDM; 74739456; -.
DR jPOST; Q9Y2P5; -.
DR MassIVE; Q9Y2P5; -.
DR PaxDb; Q9Y2P5; -.
DR PeptideAtlas; Q9Y2P5; -.
DR PRIDE; Q9Y2P5; -.
DR ProteomicsDB; 85854; -. [Q9Y2P5-1]
DR Antibodypedia; 1943; 310 antibodies from 26 providers.
DR DNASU; 10998; -.
DR Ensembl; ENST00000263093.7; ENSP00000263093.2; ENSG00000083807.10. [Q9Y2P5-1]
DR Ensembl; ENST00000601355.1; ENSP00000470368.1; ENSG00000083807.10. [Q9Y2P5-2]
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 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 neXtProt; NX_Q9Y2P5; -.
DR OpenTargets; ENSG00000083807; -.
DR Orphanet; 276066; Bile acid CoA ligase deficiency and defective amidation.
DR PharmGKB; PA35873; -.
DR VEuPathDB; HostDB:ENSG00000083807; -.
DR eggNOG; KOG1179; Eukaryota.
DR GeneTree; ENSGT00940000157947; -.
DR HOGENOM; CLU_000022_46_2_1; -.
DR InParanoid; Q9Y2P5; -.
DR OMA; GATFFTY; -.
DR OrthoDB; 298283at2759; -.
DR PhylomeDB; Q9Y2P5; -.
DR TreeFam; TF313430; -.
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 BioGRID-ORCS; 10998; 24 hits in 1078 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 126 other tissues.
DR ExpressionAtlas; Q9Y2P5; baseline and differential.
DR Genevisible; Q9Y2P5; HS.
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; TAS:Reactome.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:UniProtKB.
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:0015245; F:fatty acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005324; F:long-chain fatty acid 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:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0046951; P:ketone body biosynthetic process; IBA:GO_Central.
DR GO; GO:0015911; P:long-chain fatty acid import across plasma membrane; IBA:GO_Central.
DR GO; GO:0006642; P:triglyceride mobilization; IBA:GO_Central.
DR GO; GO:0000038; P:very 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; IPR030302; FATP5.
DR PANTHER; PTHR43107:SF4; PTHR43107:SF4; 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; Cell membrane; Endoplasmic reticulum;
KW Fatty acid metabolism; Ligase; Lipid metabolism; Lipid transport; Membrane;
KW Microsome; Nucleotide-binding; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Transmembrane; 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
