UniProt Accession

 S27A2_HUMAN; O14975; A8K2J7; Q53FY6; Q6PF09 

Genbank Protein ID

 D88308; AF096290; AK223145; AK290262; AC009753; CH471082; BC057770 

Genbank Nucleotide ID

 BAA23644.1; AAC64973.1; BAD96865.1; BAF82951.1; EAW77386.1; AAH57770.1 

Protein Name

 Very long-chain acyl-CoA synthetase 

Protein Synonyms/Alias

 VLACS; VLCS; Fatty acid transport protein 2; FATP-2; Fatty-acid-coenzyme A ligase, very long-chain 1; Long-chain-fatty-acid--CoA ligase; Solute carrier family 27 member 2; THCA-CoA ligase; Very long-chain-fatty-acid-CoA ligase 

Gene Name

 SLC27A2 

Gene Synonyms/Alias

 ACSVL1; FACVL1; FATP2; VLACS 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
398	IITYDLIKYDVEKDE	ubiquitination	[1, 2, 3]
442	FNGYAGAKAQTEKKK	ubiquitination	[3]

Reference

 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661] 

Functional Description

 Acyl-CoA synthetase probably involved in bile acid metabolism. Proposed to activate C27 precurors of bile acids to their CoA thioesters derivatives before side chain cleavage via peroxisomal beta-oxidation occurs. In vitro, 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. Does not utilize C24 bile acids as substrates. In vitro, also activates long- and branched-chain fatty acids and may have additional roles in fatty acid metabolism. May be involved in translocation of long-chain fatty acids (LFCA) across membranes (By similarity). 

Sequence Annotation

 NP_BIND 222 233 AMP (Potential).
 MOD_RES 291 291 N6-acetyllysine (By similarity).
 MOD_RES 325 325 N6-acetyllysine (By similarity).
 MOD_RES 577 577 Phosphothreonine.  

Keyword

 Acetylation; Alternative splicing; ATP-binding; Complete proteome; Endoplasmic reticulum; Fatty acid metabolism; Ligase; Lipid metabolism; Membrane; Nucleotide-binding; Peroxisome; Phosphoprotein; Polymorphism; Reference proteome; Transmembrane; Transmembrane helix. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 620 AA 

Protein Sequence

Gene Ontology

 GO:0005788; C:endoplasmic reticulum lumen; IDA:UniProtKB.
 GO:0030176; C:integral to endoplasmic reticulum membrane; IDA:UniProtKB.
 GO:0005779; C:integral to peroxisomal membrane; IDA:UniProtKB.
 GO:0005739; C:mitochondrion; IEA:Compara.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0015245; F:fatty acid transporter activity; IEA:Compara.
 GO:0004467; F:long-chain fatty acid-CoA ligase activity; IDA:UniProtKB.
 GO:0050197; F:phytanate-CoA ligase activity; IDA:UniProtKB.
 GO:0070251; F:pristanate-CoA ligase activity; IDA:UniProtKB.
 GO:0031957; F:very long-chain fatty acid-CoA ligase activity; IDA:UniProtKB.
 GO:0006699; P:bile acid biosynthetic process; IDA:UniProtKB.
 GO:0001561; P:fatty acid alpha-oxidation; IDA:UniProtKB.
 GO:0006635; P:fatty acid beta-oxidation; IDA:UniProtKB.
 GO:0044539; P:long-chain fatty acid import; IDA:UniProtKB.
 GO:0097089; P:methyl-branched fatty acid metabolic process; IDA:UniProtKB.
 GO:0042760; P:very long-chain fatty acid catabolic process; IEA:Compara. 

Interpro

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

Pfam

 PF00501; AMP-binding 

SMART

  

PROSITE

 PS00455; AMP_BINDING 

PRINTS