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Q9Y2P5 (S27A5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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
Fatty-acid-coenzyme A ligase, very long-chain 3
Solute carrier family 27 member 5
Very long-chain acyl-CoA synthetase homolog 2
Short name=VLCS-H2
Short name=VLCSH2
Very long-chain acyl-CoA synthetase-related protein
Short name=VLACS-related
Short name=VLACSR
Gene names
Name:SLC27A5
Synonyms:ACSB, ACSVL6, FACVL3, FATP5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length690 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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. In vitro, also activates 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanate (THCA), the C27 precursor of cholic acid deriving from the de novo synthesis from cholesterol. Ref.4 Ref.5

Catalytic activity

ATP + cholate + CoA = AMP + diphosphate + choloyl-CoA. Ref.4 Ref.5

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. Ref.4 Ref.5

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein Ref.1.

Tissue specificity

Predominantly expressed in liver. Ref.1

Sequence similarities

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

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentEndoplasmic reticulum
Membrane
   Coding sequence diversityPolymorphism
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbile acid and bile salt transport

Traceable author statement. Source: Reactome

bile acid biosynthetic process

Inferred from direct assay Ref.5. Source: UniProtKB

bile acid metabolic process

Traceable author statement. Source: Reactome

ketone body biosynthetic process

Inferred from electronic annotation. Source: Ensembl

plasma membrane long-chain fatty acid transport

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

triglyceride mobilization

Inferred from electronic annotation. Source: Ensembl

very long-chain fatty acid metabolic process

Inferred from direct assay Ref.1. Source: UniProtKB

   Cellular_componentbasal plasma membrane

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum

Inferred from direct assay Ref.1. Source: UniProtKB

endoplasmic reticulum membrane

Traceable author statement. Source: Reactome

integral component of endoplasmic reticulum membrane

Inferred from direct assay Ref.5. Source: UniProtKB

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 electronic annotation. Source: Ensembl

very long-chain fatty acid-CoA ligase activity

Inferred from direct assay Ref.1Ref.5. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 690690Bile acyl-CoA synthetase
PRO_0000193213

Regions

Topological domain1 – 3030Cytoplasmic Probable
Transmembrane31 – 5121Helical; Potential
Transmembrane56 – 7621Helical; Potential
Topological domain77 – 690614Cytoplasmic Probable
Nucleotide binding292 – 30312AMP Potential

Natural variations

Natural variant501M → T.
Corresponds to variant rs35350976 [ dbSNP | Ensembl ].
VAR_048243
Natural variant531R → W.
Corresponds to variant rs34415062 [ dbSNP | Ensembl ].
VAR_048244

Sequences

Sequence LengthMass (Da)Tools
Q9Y2P5 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 011313424D794546

FASTA69075,385
        10         20         30         40         50         60 
MGVRQQLALL LLLLLLLWGL GQPVWPVAVA LTLRWLLGDP TCCVLLGLAM LARPWLGPWV 

        70         80         90        100        110        120 
PHGLSLAAAA LALTLLPARL PPGLRWLPAD VIFLAKILHL GLKIRGCLSR QPPDTFVDAF 

       130        140        150        160        170        180 
ERRARAQPGR ALLVWTGPGA GSVTFGELDA RACQAAWALK AELGDPASLC AGEPTALLVL 

       190        200        210        220        230        240 
ASQAVPALCM WLGLAKLGCP TAWINPHGRG MPLAHSVLSS GARVLVVDPD LRESLEEILP 

       250        260        270        280        290        300 
KLQAENIRCF YLSHTSPTPG VGALGAALDA APSHPVPADL RAGITWRSPA LFIYTSGTTG 

       310        320        330        340        350        360 
LPKPAILTHE RVLQMSKMLS LSGATADDVV YTVLPLYHVM GLVVGILGCL DLGATCVLAP 

       370        380        390        400        410        420 
KFSTSCFWDD CRQHGVTVIL YVGELLRYLC NIPQQPEDRT HTVRLAMGNG LRADVWETFQ 

       430        440        450        460        470        480 
QRFGPIRIWE VYGSTEGNMG LVNYVGRCGA LGKMSCLLRM LSPFELVQFD MEAAEPVRDN 

       490        500        510        520        530        540 
QGFCIPVGLG EPGLLLTKVV SQQPFVGYRG PRELSERKLV RNVRQSGDVY YNTGDVLAMD 

       550        560        570        580        590        600 
REGFLYFRDR LGDTFRWKGE NVSTHEVEGV LSQVDFLQQV NVYGVCVPGC EGKVGMAAVQ 

       610        620        630        640        650        660 
LAPGQTFDGE KLYQHVRAWL PAYATPHFIR IQDAMEVTST FKLMKTRLVR EGFNVGIVVD 

       670        680        690 
PLFVLDNRAQ SFRPLTAEMY QAVCEGTWRL 

« Hide

References

« Hide 'large scale' references
[1]"Human liver-specific very-long-chain acyl-coenzyme A synthetase: cDNA cloning and characterization of a second enzymatically active protein."
Steinberg S.J., Wang S.J., McGuinness M.C., Watkins P.A.
Mol. Genet. Metab. 68:32-42(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Liver.
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The human liver-specific homolog of very long-chain acyl-CoA synthetase is cholate:CoA ligase."
Steinberg S.J., Mihalik S.J., Kim D.G., Cuebas D.A., Watkins P.A.
J. Biol. Chem. 275:15605-15608(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY.
[5]"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: FUNCTION, CATALYTIC ACTIVITY, TOPOLOGY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF064255 mRNA. Translation: AAD29444.1.
AK123036 mRNA. Translation: BAG53858.1.
CH471135 Genomic DNA. Translation: EAW72601.1.
RefSeqNP_036386.1. NM_012254.2.
UniGeneHs.292177.

3D structure databases

ProteinModelPortalQ9Y2P5.
SMRQ9Y2P5. Positions 117-651.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116191. 1 interaction.
STRING9606.ENSP00000263093.

Chemistry

ChEMBLCHEMBL5196.

Protein family/group databases

TCDB4.C.1.1.13. the proposed fatty acid transporter (fat) family.

PTM databases

PhosphoSiteQ9Y2P5.

Polymorphism databases

DMDM74739456.

Proteomic databases

PaxDbQ9Y2P5.
PRIDEQ9Y2P5.

Protocols and materials databases

DNASU10998.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263093; ENSP00000263093; ENSG00000083807.
GeneID10998.
KEGGhsa:10998.
UCSCuc002qtc.2. human.

Organism-specific databases

CTD10998.
GeneCardsGC19M058990.
HGNCHGNC:10999. SLC27A5.
HPACAB056160.
HPA007292.
MIM603314. gene.
neXtProtNX_Q9Y2P5.
PharmGKBPA35873.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0318.
HOGENOMHOG000044189.
HOVERGENHBG005642.
InParanoidQ9Y2P5.
KOK08748.
OMASEISAKW.
OrthoDBEOG7W6WKB.
PhylomeDBQ9Y2P5.
TreeFamTF313430.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressQ9Y2P5.
BgeeQ9Y2P5.
CleanExHS_SLC27A5.
GenevestigatorQ9Y2P5.

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

GeneWikiSLC27A5.
GenomeRNAi10998.
NextBio41783.
PROQ9Y2P5.
SOURCESearch...

Entry information

Entry nameS27A5_HUMAN
AccessionPrimary (citable) accession number: Q9Y2P5
Secondary accession number(s): B3KVP6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: November 1, 1999
Last modified: April 16, 2014
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM