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Protein

Bile acyl-CoA synthetase

Gene

SLC27A5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

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.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi292 – 30312AMPSequence AnalysisAdd
BLAST

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. cholate-CoA ligase activity Source: UniProtKB-EC
  3. fatty acid transporter activity Source: Ensembl
  4. long-chain fatty acid-CoA ligase activity Source: InterPro
  5. very long-chain fatty acid-CoA ligase activity Source: UniProtKB

GO - Biological processi

  1. bile acid and bile salt transport Source: Reactome
  2. bile acid biosynthetic process Source: UniProtKB
  3. bile acid metabolic process Source: Reactome
  4. ketone body biosynthetic process Source: Ensembl
  5. plasma membrane long-chain fatty acid transport Source: Ensembl
  6. small molecule metabolic process Source: Reactome
  7. triglyceride mobilization Source: Ensembl
  8. very long-chain fatty acid metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_11041. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
REACT_11042. Recycling of bile acids and salts.
REACT_11053. Synthesis of bile acids and bile salts via 24-hydroxycholesterol.

Protein family/group databases

TCDBi4.C.1.1.13. the proposed fatty acid transporter (fat) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Bile acyl-CoA synthetase (EC:6.2.1.7)
Short name:
BACS
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 namesi
Name:SLC27A5
Synonyms:ACSB, ACSVL6, FACVL3, FATP5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:10999. SLC27A5.

Subcellular locationi

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3030Cytoplasmic1 PublicationAdd
BLAST
Transmembranei31 – 5121HelicalSequence AnalysisAdd
BLAST
Transmembranei56 – 7621HelicalSequence AnalysisAdd
BLAST
Topological domaini77 – 690614Cytoplasmic1 PublicationAdd
BLAST

GO - Cellular componenti

  1. basal plasma membrane Source: Ensembl
  2. endoplasmic reticulum Source: UniProtKB
  3. endoplasmic reticulum membrane Source: Reactome
  4. integral component of endoplasmic reticulum membrane Source: UniProtKB
  5. protein complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA35873.

Polymorphism and mutation databases

BioMutaiSLC27A5.
DMDMi74739456.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 690690Bile acyl-CoA synthetasePRO_0000193213Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei501 – 5011Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9Y2P5.
PRIDEiQ9Y2P5.

PTM databases

PhosphoSiteiQ9Y2P5.

Expressioni

Tissue specificityi

Predominantly expressed in liver.1 Publication

Gene expression databases

BgeeiQ9Y2P5.
CleanExiHS_SLC27A5.
ExpressionAtlasiQ9Y2P5. baseline and differential.
GenevestigatoriQ9Y2P5.

Organism-specific databases

HPAiCAB056160.
CAB068239.
HPA007292.

Interactioni

Protein-protein interaction databases

BioGridi116191. 1 interaction.
STRINGi9606.ENSP00000263093.

Structurei

3D structure databases

ProteinModelPortaliQ9Y2P5.
SMRiQ9Y2P5. Positions 117-651.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0318.
GeneTreeiENSGT00550000074420.
HOGENOMiHOG000044189.
HOVERGENiHBG005642.
InParanoidiQ9Y2P5.
KOiK08748.
OMAiSEISAKW.
OrthoDBiEOG7W6WKB.
PhylomeDBiQ9Y2P5.
TreeFamiTF313430.

Family and domain databases

InterProiIPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR030302. FATP5.
[Graphical view]
PANTHERiPTHR24096:SF99. PTHR24096:SF99. 1 hit.
PfamiPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9Y2P5-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGVRQQLALL LLLLLLLWGL GQPVWPVAVA LTLRWLLGDP TCCVLLGLAM
60 70 80 90 100
LARPWLGPWV PHGLSLAAAA LALTLLPARL PPGLRWLPAD VIFLAKILHL
110 120 130 140 150
GLKIRGCLSR QPPDTFVDAF ERRARAQPGR ALLVWTGPGA GSVTFGELDA
160 170 180 190 200
RACQAAWALK AELGDPASLC AGEPTALLVL ASQAVPALCM WLGLAKLGCP
210 220 230 240 250
TAWINPHGRG MPLAHSVLSS GARVLVVDPD LRESLEEILP KLQAENIRCF
260 270 280 290 300
YLSHTSPTPG VGALGAALDA APSHPVPADL RAGITWRSPA LFIYTSGTTG
310 320 330 340 350
LPKPAILTHE RVLQMSKMLS LSGATADDVV YTVLPLYHVM GLVVGILGCL
360 370 380 390 400
DLGATCVLAP KFSTSCFWDD CRQHGVTVIL YVGELLRYLC NIPQQPEDRT
410 420 430 440 450
HTVRLAMGNG LRADVWETFQ QRFGPIRIWE VYGSTEGNMG LVNYVGRCGA
460 470 480 490 500
LGKMSCLLRM LSPFELVQFD MEAAEPVRDN QGFCIPVGLG EPGLLLTKVV
510 520 530 540 550
SQQPFVGYRG PRELSERKLV RNVRQSGDVY YNTGDVLAMD REGFLYFRDR
560 570 580 590 600
LGDTFRWKGE NVSTHEVEGV LSQVDFLQQV NVYGVCVPGC EGKVGMAAVQ
610 620 630 640 650
LAPGQTFDGE KLYQHVRAWL PAYATPHFIR IQDAMEVTST FKLMKTRLVR
660 670 680 690
EGFNVGIVVD PLFVLDNRAQ SFRPLTAEMY QAVCEGTWRL
Length:690
Mass (Da):75,385
Last modified:November 1, 1999 - v1
Checksum:i011313424D794546
GO
Isoform 2 (identifier: Q9Y2P5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     146-229: Missing.

Note: No experimental confirmation available.

Show »
Length:606
Mass (Da):66,846
Checksum:i4A49B281561FF8D6
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti50 – 501M → T.
Corresponds to variant rs35350976 [ dbSNP | Ensembl ].
VAR_048243
Natural varianti53 – 531R → W.
Corresponds to variant rs34415062 [ dbSNP | Ensembl ].
VAR_048244

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei146 – 22984Missing in isoform 2. 1 PublicationVSP_055810Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF064255 mRNA. Translation: AAD29444.1.
AK123036 mRNA. Translation: BAG53858.1.
AK298446 mRNA. Translation: BAG60663.1.
AC012313 Genomic DNA. No translation available.
CH471135 Genomic DNA. Translation: EAW72601.1.
CCDSiCCDS12983.1. [Q9Y2P5-1]
RefSeqiNP_036386.1. NM_012254.2. [Q9Y2P5-1]
UniGeneiHs.292177.

Genome annotation databases

EnsembliENST00000263093; ENSP00000263093; ENSG00000083807. [Q9Y2P5-1]
ENST00000601355; ENSP00000470368; ENSG00000083807. [Q9Y2P5-2]
GeneIDi10998.
KEGGihsa:10998.
UCSCiuc002qtc.2. human. [Q9Y2P5-1]

Polymorphism and mutation databases

BioMutaiSLC27A5.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF064255 mRNA. Translation: AAD29444.1.
AK123036 mRNA. Translation: BAG53858.1.
AK298446 mRNA. Translation: BAG60663.1.
AC012313 Genomic DNA. No translation available.
CH471135 Genomic DNA. Translation: EAW72601.1.
CCDSiCCDS12983.1. [Q9Y2P5-1]
RefSeqiNP_036386.1. NM_012254.2. [Q9Y2P5-1]
UniGeneiHs.292177.

3D structure databases

ProteinModelPortaliQ9Y2P5.
SMRiQ9Y2P5. Positions 117-651.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116191. 1 interaction.
STRINGi9606.ENSP00000263093.

Chemistry

ChEMBLiCHEMBL5196.

Protein family/group databases

TCDBi4.C.1.1.13. the proposed fatty acid transporter (fat) family.

PTM databases

PhosphoSiteiQ9Y2P5.

Polymorphism and mutation databases

BioMutaiSLC27A5.
DMDMi74739456.

Proteomic databases

PaxDbiQ9Y2P5.
PRIDEiQ9Y2P5.

Protocols and materials databases

DNASUi10998.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000263093; ENSP00000263093; ENSG00000083807. [Q9Y2P5-1]
ENST00000601355; ENSP00000470368; ENSG00000083807. [Q9Y2P5-2]
GeneIDi10998.
KEGGihsa:10998.
UCSCiuc002qtc.2. human. [Q9Y2P5-1]

Organism-specific databases

CTDi10998.
GeneCardsiGC19M058990.
HGNCiHGNC:10999. SLC27A5.
HPAiCAB056160.
CAB068239.
HPA007292.
MIMi603314. gene.
neXtProtiNX_Q9Y2P5.
PharmGKBiPA35873.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0318.
GeneTreeiENSGT00550000074420.
HOGENOMiHOG000044189.
HOVERGENiHBG005642.
InParanoidiQ9Y2P5.
KOiK08748.
OMAiSEISAKW.
OrthoDBiEOG7W6WKB.
PhylomeDBiQ9Y2P5.
TreeFamiTF313430.

Enzyme and pathway databases

ReactomeiREACT_11041. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
REACT_11042. Recycling of bile acids and salts.
REACT_11053. Synthesis of bile acids and bile salts via 24-hydroxycholesterol.

Miscellaneous databases

ChiTaRSiSLC27A5. human.
GeneWikiiSLC27A5.
GenomeRNAii10998.
NextBioi35473929.
PROiQ9Y2P5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y2P5.
CleanExiHS_SLC27A5.
ExpressionAtlasiQ9Y2P5. baseline and differential.
GenevestigatoriQ9Y2P5.

Family and domain databases

InterProiIPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR030302. FATP5.
[Graphical view]
PANTHERiPTHR24096:SF99. PTHR24096:SF99. 1 hit.
PfamiPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] (ISOFORM 1), 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.
    , 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] (ISOFORMS 1 AND 2).
    Tissue: Liver.
  3. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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.
  6. "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.
  7. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-501, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiS27A5_HUMAN
AccessioniPrimary (citable) accession number: Q9Y2P5
Secondary accession number(s): B3KVP6, B4DPQ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: November 1, 1999
Last modified: April 29, 2015
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.