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Q4LDG0 (S27A5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bile acyl-CoA synthetase

Short name=BACS
EC=6.2.1.7
Alternative name(s):
Bile acid-CoA ligase
Short name=BA-CoA ligase
Short name=BAL
Cholate--CoA ligase
Fatty acid transport protein 5
Short name=FATP-5
Solute carrier family 27 member 5
Very long-chain acyl-CoA synthetase-related protein
Short name=VLACS-related
Short name=VLACSR
Gene names
Name:Slc27a5
Synonyms:Acsb, Acsvl6, Fatp5, Vlacsr
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length689 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Acyl-CoA synthetase involved in bile acid metabolism. Proposed to catalyze the first step in the conjugation of C24 bile acids (choloneates) to glycine and taurine before excretion into bile canaliculi by activating them to their CoA thioesters. Seems to activate secondary bile acids entering the liver from the enterohepatic circulation By similarity.

Catalytic activity

ATP + cholate + CoA = AMP + diphosphate + choloyl-CoA.

ATP + (25R)-3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestan-26-oate + CoA = AMP + diphosphate + (25R)-3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.

Tissue specificity

In liver expressed in a periportal distribution. Ref.4

Sequence similarities

Belongs to the ATP-dependent AMP-binding enzyme family.

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentEndoplasmic reticulum
Membrane
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbile acid biosynthetic process

Inferred from electronic annotation. Source: Ensembl

bile acid metabolic process

Inferred from mutant phenotype PubMed 16618417. Source: MGI

fatty acid transport

Inferred from direct assay Ref.3. Source: MGI

ketone body biosynthetic process

Inferred from mutant phenotype PubMed 16618416. Source: MGI

long-chain fatty acid metabolic process

Traceable author statement PubMed 15464426. Source: MGI

plasma membrane long-chain fatty acid transport

Inferred from mutant phenotype PubMed 16618416. Source: MGI

triglyceride mobilization

Inferred from mutant phenotype PubMed 16618416. Source: MGI

very long-chain fatty acid metabolic process

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentbasal plasma membrane

Inferred from direct assay PubMed 16618416. Source: MGI

endoplasmic reticulum

Traceable author statement PubMed 15464426. Source: MGI

integral component of endoplasmic reticulum membrane

Inferred from electronic annotation. Source: Ensembl

protein complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

cholate-CoA ligase activity

Inferred from electronic annotation. Source: UniProtKB-EC

fatty acid transporter activity

Inferred from direct assay Ref.3. Source: MGI

long-chain fatty acid-CoA ligase activity

Traceable author statement PubMed 15464426. Source: MGI

very long-chain fatty acid-CoA ligase activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 689689Bile acyl-CoA synthetase
PRO_0000193214

Regions

Topological domain1 – 2929Cytoplasmic By similarity
Transmembrane30 – 5021Helical; Potential
Transmembrane55 – 7521Helical; Potential
Topological domain76 – 689614Cytoplasmic By similarity
Nucleotide binding292 – 30312AMP Potential

Experimental info

Sequence conflict881K → I in CAA11688. Ref.1
Sequence conflict4081N → T in AAC40189. Ref.3
Sequence conflict5681C → S in CAA11688. Ref.1
Sequence conflict6881N → K in CAA11688. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q4LDG0 [UniParc].

Last modified November 22, 2005. Version 2.
Checksum: 1642BBC2CF04FAA3

FASTA68976,203
        10         20         30         40         50         60 
MGIWKKLTLL LLLLLLVGLG QPPWPAAMAL ALRWFLGDPT CLVLLGLALL GRPWISSWMP 

        70         80         90        100        110        120 
HWLSLVGAAL TLFLLPLQPP PGLRWLHKDV AFTFKMLFYG LKFRRRLNKH PPETFVDALE 

       130        140        150        160        170        180 
RQALAWPDRV ALVCTGSEGS SITNSQLDAR SCQAAWVLKA KLKDAVIQNT RDAAAILVLP 

       190        200        210        220        230        240 
SKTISALSVF LGLAKLGCPV AWINPHSRGM PLLHSVRSSG ASVLIVDPDL QENLEEVLPK 

       250        260        270        280        290        300 
LLAENIHCFY LGHSSPTPGV EALGASLDAA PSDPVPASLR ATIKWKSPAI FIFTSGTTGL 

       310        320        330        340        350        360 
PKPAILSHER VIQVSNVLSF CGCRADDVVY DVLPLYHTIG LVLGFLGCLQ VGATCVLAPK 

       370        380        390        400        410        420 
FSASRFWAEC RQHGVTVILY VGEILRYLCN VPEQPEDKIH TVRLAMGNGL RANVWKNFQQ 

       430        440        450        460        470        480 
RFGPIRIWEF YGSTEGNVGL MNYVGHCGAV GRTSCILRML TPFELVQFDI ETAEPLRDKQ 

       490        500        510        520        530        540 
GFCIPVEPGK PGLLLTKVRK NQPFLGYRGS QAESNRKLVA NVRRVGDLYF NTGDVLTLDQ 

       550        560        570        580        590        600 
EGFFYFQDRL GDTFRWKGEN VSTGEVECVL SSLDFLEEVN VYGVPVPGCE GKVGMAAVKL 

       610        620        630        640        650        660 
APGKTFDGQK LYQHVRSWLP AYATPHFIRI QDSLEITNTY KLVKSRLVRE GFDVGIIADP 

       670        680 
LYILDNKAQT FRSLMPDVYQ AVCEGTWNL 

« Hide

References

« Hide 'large scale' references
[1]"A novel relative of the very-long-chain acyl-CoA synthetase and fatty acid transporter protein genes with a distinct expression pattern."
Berger J., Truppe C., Neumann H., Forss-Petter S.
Biochem. Biophys. Res. Commun. 247:255-260(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
Tissue: Liver.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Brain and Salivary gland.
[3]"A family of fatty acid transporters conserved from mycobacterium to man."
Hirsch D., Stahl A., Lodish H.F.
Proc. Natl. Acad. Sci. U.S.A. 95:8625-8629(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 28-689.
[4]"Participation of two members of the very long-chain acyl-CoA synthetase family in bile acid synthesis and recycling."
Mihalik S.J., Steinberg S.J., Pei Z., Park J., Kim do G., Heinzer A.K., Dacremont G., Wanders R.J., Cuebas D.A., Smith K.D., Watkins P.A.
J. Biol. Chem. 277:24771-24779(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ223959 mRNA. Translation: CAA11688.1.
BC013335 mRNA. Translation: AAH13335.1.
BC013272 mRNA. Translation: AAH13272.1.
BC145823 mRNA. Translation: AAI45824.1.
BC145825 mRNA. Translation: AAI45826.1.
AF072760 mRNA. Translation: AAC40189.1.
PIRJW0107.
RefSeqNP_033538.2. NM_009512.2.
UniGeneMm.10984.

3D structure databases

ProteinModelPortalQ4LDG0.
SMRQ4LDG0. Positions 111-660.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ4LDG0. 2 interactions.
MINTMINT-1863806.

Protein family/group databases

TCDB4.C.1.1.8. the proposed fatty acid transporter (fat) family.

Proteomic databases

PaxDbQ4LDG0.
PRIDEQ4LDG0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000032539; ENSMUSP00000032539; ENSMUSG00000030382.
GeneID26459.
KEGGmmu:26459.
UCSCuc009fey.3. mouse.

Organism-specific databases

CTD10998.
MGIMGI:1347100. Slc27a5.

Phylogenomic databases

eggNOGCOG0318.
GeneTreeENSGT00550000074420.
HOGENOMHOG000044189.
HOVERGENHBG005642.
InParanoidA6H6C1.
KOK08748.
OMAAWINPHS.
OrthoDBEOG7W6WKB.
PhylomeDBQ4LDG0.
TreeFamTF313430.

Gene expression databases

BgeeQ4LDG0.
GenevestigatorQ4LDG0.

Family and domain databases

InterProIPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSLC27A5. mouse.
NextBio304573.
PROQ4LDG0.
SOURCESearch...

Entry information

Entry nameS27A5_MOUSE
AccessionPrimary (citable) accession number: Q4LDG0
Secondary accession number(s): A6H6C1, O88694, Q91VD5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: November 22, 2005
Last modified: April 16, 2014
This is version 82 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot