S27A5_RAT
ID S27A5_RAT Reviewed; 690 AA.
AC Q9ES38;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Long-chain fatty acid transport protein 5 {ECO:0000305};
DE Short=FATP-5 {ECO:0000250|UniProtKB:Q4LDG0};
DE Short=Fatty acid transport protein 5 {ECO:0000250|UniProtKB:Q4LDG0};
DE AltName: Full=Bile acid-CoA ligase {ECO:0000303|PubMed:12454267, ECO:0000303|PubMed:12951368};
DE Short=BA-CoA ligase {ECO:0000303|PubMed:12454267, ECO:0000303|PubMed:12951368};
DE Short=BAL {ECO:0000303|PubMed:12454267, ECO:0000303|PubMed:12951368};
DE AltName: Full=Bile acyl-CoA synthetase {ECO:0000250|UniProtKB:Q9Y2P5};
DE Short=BACS {ECO:0000250|UniProtKB:Q9Y2P5};
DE EC=6.2.1.7 {ECO:0000250|UniProtKB:Q9Y2P5};
DE AltName: Full=Cholate--CoA ligase {ECO:0000250|UniProtKB:Q9Y2P5};
DE AltName: Full=Long-chain-fatty-acid--CoA ligase;
DE EC=6.2.1.3 {ECO:0000250|UniProtKB:Q9Y2P5};
DE AltName: Full=Solute carrier family 27 member 5;
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};
DE EC=6.2.1.- {ECO:0000250|UniProtKB:Q9Y2P5};
GN Name=Slc27a5; Synonyms=Acsb, Fatp5, Vlacsr;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 602-613 AND 651-666,
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND ACTIVITY REGULATION.
RC STRAIN=Sprague-Dawley;
RX PubMed=12454267; DOI=10.1194/jlr.m200260-jlr200;
RA Falany C.N., Xie X., Wheeler J.B., Wang J., Smith M., He D., Barnes S.;
RT "Molecular cloning and expression of rat liver bile acid CoA ligase.";
RL J. Lipid Res. 43:2062-2071(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
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 [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RC TISSUE=Liver;
RX PubMed=12951368; DOI=10.1194/jlr.m300128-jlr200;
RA He D., Barnes S., Falany C.N.;
RT "Rat liver bile acid CoA:amino acid N-acyltransferase: expression,
RT characterization, and peroxisomal localization.";
RL J. Lipid Res. 44:2242-2249(2003).
CC -!- FUNCTION: Mediates the import of long-chain fatty acids (LCFA) by
CC facilitating their transport across cell membranes (By similarity).
CC Also catalyzes the ATP-dependent formation of fatty acyl-CoA using LCFA
CC and very-long-chain fatty acids (VLCFA) as substrates (By similarity).
CC Mainly functions as a bile acyl-CoA synthetase catalyzing the
CC activation of bile acids via formation of bile acid CoA thioesters
CC which is necessary for their subsequent conjugation with glycine or
CC taurine (PubMed:12454267, PubMed:12951368). In particular, catalyzes
CC the activation of the primary bile acid, chenodeoxycholic acid
CC (PubMed:12454267, PubMed:12951368). Primary bile acid cholic acid and
CC secondary bile acids (deoxycholic acid and lithocholic acid) are
CC principal substrates too (By similarity). In vitro, activates 3-
CC alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanate ((25R)-
CC 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oate or THCA), the
CC C27 precursor of cholic acid deriving from the de novo synthesis from
CC cholesterol (By similarity). Plays an important role in hepatic fatty
CC acid uptake and bile acid reconjugation and recycling but not in de
CC novo synthesis of bile acids (By similarity).
CC {ECO:0000250|UniProtKB:Q4LDG0, ECO:0000250|UniProtKB:Q9Y2P5,
CC ECO:0000269|PubMed:12454267, ECO:0000269|PubMed:12951368}.
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:Q9Y2P5};
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:0000250|UniProtKB:Q9Y2P5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23533;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2P5};
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:0000250|UniProtKB:Q9Y2P5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22977;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2P5};
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:12454267, ECO:0000269|PubMed:12951368};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43765;
CC Evidence={ECO:0000305|PubMed:12454267, ECO:0000305|PubMed:12951368};
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:0000250|UniProtKB:Q9Y2P5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47129;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2P5};
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:0000250|UniProtKB:Q9Y2P5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47137;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2P5};
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:Q9Y2P5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54537;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2P5};
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:Q9Y2P5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33640;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2P5};
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:0000250|UniProtKB:Q9Y2P5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43749;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2P5};
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:Q9Y2P5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15422;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2P5};
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:0000250|UniProtKB:Q9Y2P5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33616;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2P5};
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:0000250|UniProtKB:Q9Y2P5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46209;
CC Evidence={ECO:0000250|UniProtKB:Q9Y2P5};
CC -!- ACTIVITY REGULATION: Inhibited by mono-unsaturated fatty acids,
CC palmitoleic acid and oleic acid and nonionic detergents, triton X-100
CC and polyethylene glycol hexadecyl ether (Brij 58).
CC {ECO:0000269|PubMed:12454267}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=32 uM for chenodeoxycholic acid {ECO:0000269|PubMed:12454267};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9Y2P5}; Multi-pass membrane protein
CC {ECO:0000255}. Microsome {ECO:0000269|PubMed:12951368}. Cell membrane
CC {ECO:0000250|UniProtKB:Q4LDG0}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in liver (at protein
CC level). {ECO:0000269|PubMed:12454267}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF242189; AAG09770.1; -; mRNA.
DR EMBL; BC091147; AAH91147.1; -; mRNA.
DR RefSeq; NP_077057.1; NM_024143.2.
DR AlphaFoldDB; Q9ES38; -.
DR SMR; Q9ES38; -.
DR IntAct; Q9ES38; 2.
DR STRING; 10116.ENSRNOP00000026574; -.
DR iPTMnet; Q9ES38; -.
DR PhosphoSitePlus; Q9ES38; -.
DR PaxDb; Q9ES38; -.
DR PRIDE; Q9ES38; -.
DR Ensembl; ENSRNOT00000026575; ENSRNOP00000026574; ENSRNOG00000019626.
DR GeneID; 79111; -.
DR KEGG; rno:79111; -.
DR UCSC; RGD:708535; rat.
DR CTD; 10998; -.
DR RGD; 708535; Slc27a5.
DR eggNOG; KOG1179; Eukaryota.
DR GeneTree; ENSGT00940000157947; -.
DR HOGENOM; CLU_000022_46_2_1; -.
DR InParanoid; Q9ES38; -.
DR OMA; GATFFTY; -.
DR OrthoDB; 298283at2759; -.
DR PhylomeDB; Q9ES38; -.
DR TreeFam; TF313430; -.
DR BioCyc; MetaCyc:MON-14312; -.
DR Reactome; R-RNO-159418; Recycling of bile acids and salts.
DR Reactome; R-RNO-193368; Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
DR Reactome; R-RNO-193775; Synthesis of bile acids and bile salts via 24-hydroxycholesterol.
DR SABIO-RK; Q9ES38; -.
DR PRO; PR:Q9ES38; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000019626; Expressed in liver and 10 other tissues.
DR Genevisible; Q9ES38; RN.
DR GO; GO:0009925; C:basal plasma membrane; ISO:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISO:RGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
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; ISO:RGD.
DR GO; GO:0005324; F:long-chain fatty acid transporter activity; ISS:UniProtKB.
DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0031957; F:very long-chain fatty acid-CoA ligase activity; ISO:RGD.
DR GO; GO:0006699; P:bile acid biosynthetic process; ISO:RGD.
DR GO; GO:0008206; P:bile acid metabolic process; IMP:RGD.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0015908; P:fatty acid transport; ISO:RGD.
DR GO; GO:0046951; P:ketone body biosynthetic process; ISO:RGD.
DR GO; GO:0015911; P:long-chain fatty acid import across plasma membrane; ISO:RGD.
DR GO; GO:0006642; P:triglyceride mobilization; ISO:RGD.
DR GO; GO:0000038; P:very long-chain fatty acid metabolic process; ISO:RGD.
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 ATP-binding; Cell membrane; Direct protein sequencing;
KW Endoplasmic reticulum; Fatty acid metabolism; Ligase; Lipid metabolism;
KW Lipid transport; Membrane; Microsome; Nucleotide-binding;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..690
FT /note="Long-chain fatty acid transport protein 5"
FT /id="PRO_0000193215"
FT TOPO_DOM 1..30
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2P5"
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:0000250|UniProtKB:Q9Y2P5"
FT BINDING 292..303
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000255"
SQ SEQUENCE 690 AA; 76266 MW; D5BEB8317758DA59 CRC64;
MGVWKKLTFL LLSLLLLVGL GQPLWPAATA LALRWFLGDP TCFVLLGLAF LGRPWISSWI
PHWLSLAAAA LTLSLLPPRP PPELRWLHKD VAFAFKLLFY GLNLRRRLNR HPPELFVDAL
EQQAQARPDQ VALVCTGSEG CSITNRELNA KACQAAWALK AKLKEATIQE DKGATAILVL
PSKSISALSV FLGLAKLGCP VAWINPHSRG MPLLHSVQSS GASVLIVDPD LQENLEEVLP
KLLAENIRCF YLGHSSPTPG VEALGAALDA APSDPVPAKL RANIKWKSPA IFIYTSGTTG
LPKPAILSHE RVIQMSNVLS FCGRTADDVV YNVLPLYHSM GLVLGVLGCL QLGATCVLAP
KFSASRYWAE CRQYSVTVVL YVGEVLRYLC NVPGQPEDKK HTVRFALGNG LRADVWENFQ
QRFGPIQIWE LYGSTEGNVG LMNYVGHCGA VGKTSCFIRM LTPLELVQFD IETAEPVRDK
QGFCIPVETG KPGLLLTKIR KNQPFLGYRG SQDETKRKLV ANVRQVGDLY YNTGDVLALD
QEGFFYFRDR LGDTFRWKGE NVSTREVEGV LSILDFLEEV NVYGVTVPGC EGKVGMAAVK
LAPGKTFDGQ KLYQHVRSWL PAYATPHFIR IQDSLEITNT YKLVKSQLAR EGFDVGVIAD
PLYILDNKAE TFRSLMPDVY QAVCEGTWKL
