Q9Y2P5 (S27A5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	690 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Fatty acid metabolism Lipid metabolism
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Polymorphism
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	bile acid and bile salt transport Traceable author statement. Source: Reactome bile acid biosynthetic process Inferred from direct assay Ref.5. Source: UniProtKB ketone body biosynthetic process Inferred from electronic annotation. Source: Compara plasma membrane long-chain fatty acid transport Inferred from electronic annotation. Source: Compara triglyceride mobilization Inferred from electronic annotation. Source: Compara very long-chain fatty acid metabolic process Inferred from direct assay Ref.1. Source: UniProtKB
Cellular_component	basal plasma membrane Inferred from electronic annotation. Source: Compara integral to endoplasmic reticulum membrane Inferred from direct assay Ref.5. Source: UniProtKB protein complex Inferred from electronic annotation. Source: Compara
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW cholate-CoA ligase activity Inferred from electronic annotation. Source: EC fatty acid transporter activity Inferred from electronic annotation. Source: Compara very long-chain fatty acid-CoA ligase activity Inferred from direct assay Ref.1Ref.5. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 690	690	Bile acyl-CoA synthetase		PRO_0000193213
Regions
	Topological domain	1 – 30	30	Cytoplasmic Probable
	Transmembrane	31 – 51	21	Helical; Potential
	Transmembrane	56 – 76	21	Helical; Potential
	Topological domain	77 – 690	614	Cytoplasmic Probable
	Nucleotide binding	292 – 303	12	AMP Potential
Natural variations
	Natural variant	50	1	M → T. Corresponds to variant rs35350976 [ dbSNP | Ensembl ].		VAR_048243
	Natural variant	53	1	R → W. Corresponds to variant rs34415062 [ dbSNP | Ensembl ].		VAR_048244

Sequences

	Sequence		Length	Mass (Da)
	Q9Y2P5 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 011313424D794546	FASTA	690	75,385
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
IPI	IPI00016827.
RefSeq	NP_036386.1. NM_012254.2.
UniGene	Hs.292177.
3D structure databases
ProteinModelPortal	Q9Y2P5.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000263093.
PTM databases
PhosphoSite	Q9Y2P5.
Polymorphism databases
DMDM	74739456.
Proteomic databases
PaxDb	Q9Y2P5.
PRIDE	Q9Y2P5.
Protocols and materials databases
DNASU	10998.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000263093; ENSP00000263093; ENSG00000083807.
GeneID	10998.
KEGG	hsa:10998.
UCSC	uc002qtc.2. human.
Organism-specific databases
CTD	10998.
GeneCards	GC19M059009.
HGNC	HGNC:10999. SLC27A5.
HPA	CAB056160. HPA007292.
MIM	603314. gene.
neXtProt	NX_Q9Y2P5.
PharmGKB	PA35873.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0318.
HOGENOM	HOG000044189.
HOVERGEN	HBG005642.
InParanoid	Q9Y2P5.
KO	K08748.
OMA	FYASSEG.
OrthoDB	EOG41ZF9B.
PhylomeDB	Q9Y2P5.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism.
Gene expression databases
Bgee	Q9Y2P5.
CleanEx	HS_SLC27A5.
Genevestigator	Q9Y2P5.
GermOnline	ENSG00000083807. Homo sapiens.
Family and domain databases
InterPro	IPR020845. AMP-binding_CS. IPR000873. AMP-dep_Synth/Lig. [Graphical view]
Pfam	PF00501. AMP-binding. 1 hit. [Graphical view]
PROSITE	PS00455. AMP_BINDING. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChEMBL	CHEMBL5196.
GenomeRNAi	10998.
NextBio	41783.
SOURCE	Search...

Entry information

Entry name

S27A5_HUMAN

Accession

Primary (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 3, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.