UniProt Accession

 S27A5_MOUSE; Q4LDG0; A6H6C1; O88694; Q91VD5 

Genbank Protein ID

 AJ223959; BC013335; BC013272; BC145823; BC145825; AF072760 

Genbank Nucleotide ID

 CAA11688.1; AAH13335.1; AAH13272.1; AAI45824.1; AAI45826.1; AAC40189.1 

Protein Name

 Bile acyl-CoA synthetase 

Protein Synonyms/Alias

 BACS; Bile acid-CoA ligase; BA-CoA ligase; BAL; Cholate--CoA ligase; Fatty acid transport protein 5; FATP-5; Solute carrier family 27 member 5; Very long-chain acyl-CoA synthetase-related protein; VLACS-related; VLACSR 

Gene Name

 Slc27a5 

Gene Synonyms/Alias

 Acsb; Acsvl6; Fatp5; Vlacsr 

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
159	CQAAWVLKAKLKDAV	acetylation	[1]
159	CQAAWVLKAKLKDAV	ubiquitination	[2]
163	WVLKAKLKDAVIQNT	ubiquitination	[2]
302	SGTTGLPKPAILSHE	ubiquitination	[2]
398	VPEQPEDKIHTVRLA	ubiquitination	[2]
416	GLRANVWKNFQQRFG	acetylation	[1, 3]
416	GLRANVWKNFQQRFG	ubiquitination	[2]
479	TAEPLRDKQGFCIPV	ubiquitination	[2]
490	CIPVEPGKPGLLLTK	ubiquitination	[2]
500	LLLTKVRKNQPFLGY	ubiquitination	[2]
517	SQAESNRKLVANVRR	ubiquitination	[2]
599	KVGMAAVKLAPGKTF	ubiquitination	[2]
604	AVKLAPGKTFDGQKL	ubiquitination	[2]
610	GKTFDGQKLYQHVRS	ubiquitination	[2]
641	LEITNTYKLVKSRLV	ubiquitination	[2]
644	TNTYKLVKSRLVREG	ubiquitination	[2]
667	PLYILDNKAQTFRSL	ubiquitination	[2]

Reference

 [1] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [2] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [3] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654] 

Functional Description

 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). 

Sequence Annotation

 NP_BIND 292 303 AMP (Potential).  

Keyword

 ATP-binding; Complete proteome; Endoplasmic reticulum; Fatty acid metabolism; Ligase; Lipid metabolism; Membrane; Nucleotide-binding; Reference proteome; Transmembrane; Transmembrane helix. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 689 AA 

Protein Sequence

Gene Ontology

 GO:0009925; C:basal plasma membrane; IDA:MGI.
 GO:0005783; C:endoplasmic reticulum; TAS:MGI.
 GO:0030176; C:integral to endoplasmic reticulum membrane; IEA:Compara.
 GO:0043234; C:protein complex; IEA:Compara.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0047747; F:cholate-CoA ligase activity; IEA:EC.
 GO:0015245; F:fatty acid transporter activity; IDA:MGI.
 GO:0004467; F:long-chain fatty acid-CoA ligase activity; TAS:MGI.
 GO:0031957; F:very long-chain fatty acid-CoA ligase activity; IEA:Compara.
 GO:0006699; P:bile acid biosynthetic process; IEA:Compara.
 GO:0008206; P:bile acid metabolic process; IMP:MGI.
 GO:0046951; P:ketone body biosynthetic process; IMP:MGI.
 GO:0015911; P:plasma membrane long-chain fatty acid transport; IMP:MGI.
 GO:0006642; P:triglyceride mobilization; IMP:MGI.
 GO:0000038; P:very long-chain fatty acid metabolic process; IEA:Compara. 

Interpro

 IPR020845; AMP-binding_CS.
 IPR000873; AMP-dep_Synth/Lig. 

Pfam

 PF00501; AMP-binding 

SMART

  

PROSITE

 PS00455; AMP_BINDING 

PRINTS