ID   S27A5_MOUSE             Reviewed;         689 AA.
AC   Q4LDG0; O88694; Q91VD5;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 2.
DT   16-JUN-2009, entry version 39.
DE   RecName: Full=Bile acyl-CoA synthetase;
DE            Short=BACS;
DE            EC=6.2.1.7;
DE   AltName: Full=Bile acid-CoA ligase;
DE            Short=BA-CoA ligase;
DE            Short=BAL;
DE   AltName: Full=Cholate--CoA ligase;
DE   AltName: Full=Very long-chain acyl-CoA synthetase-related protein;
DE            Short=VLACS-related;
DE            Short=VLACSR;
DE   AltName: Full=Fatty acid transport protein 5;
DE            Short=FATP-5;
DE   AltName: Full=Solute carrier family 27 member 5;
GN   Name=Slc27a5; Synonyms=Acsb, Acsvl6, Fatp5, Vlacsr;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Liver;
RX   MEDLINE=98308102; PubMed=9642112; DOI=10.1006/bbrc.1998.8770;
RA   Berger J., Truppe C., Neumann H., Forss-Petter S.;
RT   "A novel relative of the very-long-chain acyl-CoA synthetase and fatty
RT   acid transporter protein genes with a distinct expression pattern.";
RL   Biochem. Biophys. Res. Commun. 247:255-260(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Salivary gland;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 28-689.
RX   MEDLINE=98337965; PubMed=9671728; DOI=10.1073/pnas.95.15.8625;
RA   Hirsch D., Stahl A., Lodish H.F.;
RT   "A family of fatty acid transporters conserved from mycobacterium to
RT   man.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:8625-8629(1998).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=11980911; DOI=10.1074/jbc.M203295200;
RA   Mihalik S.J., Steinberg S.J., Pei Z., Park J., Kim do G.,
RA   Heinzer A.K., Dacremont G., Wanders R.J., Cuebas D.A., Smith K.D.,
RA   Watkins P.A.;
RT   "Participation of two members of the very long-chain acyl-CoA
RT   synthetase family in bile acid synthesis and recycling.";
RL   J. Biol. Chem. 277:24771-24779(2002).
CC   -!- FUNCTION: Acyl-CoA synthetase involved in bile acid metabolism.
CC       Proposed to catalyze the first step in the conjugation of C24 bile
CC       acids (choloneates) to glycine and taurine before excretion into
CC       bile canaliculi by activating them to their CoA thioesters. Seems
CC       to activate secondary bile acids entering the liver from the
CC       enterohepatic circulation (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + cholate + CoA = AMP + diphosphate +
CC       choloyl-CoA.
CC   -!- CATALYTIC ACTIVITY: ATP + (25R)-3-alpha,7-alpha,12-alpha-
CC       trihydroxy-5-beta-cholestan-26-oate + CoA = AMP + diphosphate +
CC       (25R)-3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein (By similarity).
CC   -!- TISSUE SPECIFICITY: In liver expressed in a periportal
CC       distribution.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
CC       family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AJ223959; CAA11688.1; -; mRNA.
DR   EMBL; BC013335; AAH13335.1; -; mRNA.
DR   EMBL; BC013272; AAH13272.1; -; mRNA.
DR   EMBL; AF072760; AAC40189.1; -; mRNA.
DR   IPI; IPI00313236; -.
DR   PIR; JW0107; JW0107.
DR   RefSeq; NP_033538.1; -.
DR   UniGene; Mm.10984; -.
DR   TCDB; 4.C.1.1.8; proposed fatty acid transporter (FAT) family.
DR   Ensembl; ENSMUSG00000030382; Mus musculus.
DR   GeneID; 26459; -.
DR   KEGG; mmu:26459; -.
DR   MGI; MGI:1347100; Slc27a5.
DR   HOGENOM; Q4LDG0; -.
DR   HOVERGEN; Q4LDG0; -.
DR   OMA; Q4LDG0; TFVDAFE.
DR   BRENDA; 6.2.1.7; 244.
DR   NextBio; 304573; -.
DR   ArrayExpress; Q4LDG0; -.
DR   Bgee; Q4LDG0; -.
DR   GermOnline; ENSMUSG00000030382; Mus musculus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0047747; F:cholate-CoA ligase activity; IEA:EC.
DR   GO; GO:0004467; F:long-chain-fatty-acid-CoA ligase activity; TAS:MGI.
DR   GO; GO:0001676; P:long-chain fatty acid metabolic process; TAS:MGI.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   Pfam; PF00501; AMP-binding; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Endoplasmic reticulum; Fatty acid metabolism; Ligase;
KW   Lipid metabolism; Membrane; Nucleotide-binding; Transmembrane.
FT   CHAIN         1    689       Bile acyl-CoA synthetase.
FT                                /FTId=PRO_0000193214.
FT   TOPO_DOM      1      7       Cytoplasmic (By similarity).
FT   TRANSMEM      8     28       Potential.
FT   TRANSMEM     30     50       Potential.
FT   TRANSMEM     55     75       Potential.
FT   TOPO_DOM     76    689       Cytoplasmic (By similarity).
FT   NP_BIND     292    303       AMP (Potential).
FT   CONFLICT     88     88       K -> I (in Ref. 1; CAA11688).
FT   CONFLICT    408    408       N -> T (in Ref. 3; AAC40189).
FT   CONFLICT    568    568       C -> S (in Ref. 1; CAA11688).
FT   CONFLICT    688    688       N -> K (in Ref. 1; CAA11688).
SQ   SEQUENCE   689 AA;  76203 MW;  1642BBC2CF04FAA3 CRC64;
     MGIWKKLTLL LLLLLLVGLG QPPWPAAMAL ALRWFLGDPT CLVLLGLALL GRPWISSWMP
     HWLSLVGAAL TLFLLPLQPP PGLRWLHKDV AFTFKMLFYG LKFRRRLNKH PPETFVDALE
     RQALAWPDRV ALVCTGSEGS SITNSQLDAR SCQAAWVLKA KLKDAVIQNT RDAAAILVLP
     SKTISALSVF LGLAKLGCPV AWINPHSRGM PLLHSVRSSG ASVLIVDPDL QENLEEVLPK
     LLAENIHCFY LGHSSPTPGV EALGASLDAA PSDPVPASLR ATIKWKSPAI FIFTSGTTGL
     PKPAILSHER VIQVSNVLSF CGCRADDVVY DVLPLYHTIG LVLGFLGCLQ VGATCVLAPK
     FSASRFWAEC RQHGVTVILY VGEILRYLCN VPEQPEDKIH TVRLAMGNGL RANVWKNFQQ
     RFGPIRIWEF YGSTEGNVGL MNYVGHCGAV GRTSCILRML TPFELVQFDI ETAEPLRDKQ
     GFCIPVEPGK PGLLLTKVRK NQPFLGYRGS QAESNRKLVA NVRRVGDLYF NTGDVLTLDQ
     EGFFYFQDRL GDTFRWKGEN VSTGEVECVL SSLDFLEEVN VYGVPVPGCE GKVGMAAVKL
     APGKTFDGQK LYQHVRSWLP AYATPHFIRI QDSLEITNTY KLVKSRLVRE GFDVGIIADP
     LYILDNKAQT FRSLMPDVYQ AVCEGTWNL
//