Reviewed, UniProtKB/Swiss-Prot P97524 (S27A2_RAT)

Names and origin

Protein names

Recommended name:
    Very long-chain acyl-CoA synthetase
      Short name=VLACS
      Short name=VLCS
    EC=6.2.1.-
Alternative name(s):
    Very long-chain-fatty-acid-CoA ligase
    THCA-CoA ligase
    Fatty-acid-coenzyme A ligase, very long-chain 1
    Long-chain-fatty-acid--CoA ligase
    EC=6.2.1.3
    Fatty acid transport protein 2
      Short name=FATP-2
    Solute carrier family 27 member 2

Gene names

Name:	Slc27a2
Synonyms:	Acsvl1, Facvl1, Fatp2, Vlacs, Vlcs

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	620 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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.
Catalytic activity	ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA. ATP + a very-long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein. Peroxisome membrane; Multi-pass membrane protein. Note: Peripheral membrane associated with the lumenal side of peroxisomes. Ref.2
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 Peroxisome
Domain	Transmembrane
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
PTM	Acetylation Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	fatty acid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-KW integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell microsome Ref.1 Inferred from mutant phenotype. Source: RGD peroxisomal membrane Inferred from direct assay. Source: HGNC
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW long-chain-fatty-acid-CoA ligase activity Ref.1 Inferred from mutant phenotype. Source: RGD protein binding Inferred from physical interaction. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 620	620	Very long-chain acyl-CoA synthetase		PRO_0000193206
Regions
	Topological domain	1 – 4	4	Lumenal By similarity
	Transmembrane	5 – 27	23	Potential
	Topological domain	28 – 106	79	Cytoplasmic Potential
	Transmembrane	107 – 127	21	Potential
	Topological domain	128 – 267	140	Lumenal Potential
	Transmembrane	268 – 288	21	Potential
	Topological domain	289 – 620	332	Cytoplasmic By similarity
	Nucleotide binding	222 – 233	12	AMP Potential
Amino acid modifications
	Modified residue	291	1	N6-acetyllysine By similarity
	Modified residue	325	1	N6-acetyllysine By similarity
	Modified residue	577	1	Phosphothreonine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P97524-1 [UniParc]. Last modified May 1, 1997. Version 1. Checksum: 6CF9362DC3805526	FASTA	620	70,694
	10 20 30 40 50 60 MLPVLYTGLA GLLLLPLLLT CCCPYLLQDV RFFLQLANMA RQVRSYRQRR PVRTILHVFL 70 80 90 100 110 120 EQARKTPHKP FLLFRDETLT YAQVDRRSNQ VARALHDHLG LRQGDCVALF MGNEPAYVWL 130 140 150 160 170 180 WLGLLKLGCP MACLNYNIRA KSLLHCFQCC GAKVLLASPE LHEAVEEVLP TLKKEGVSVF 190 200 210 220 230 240 YVSRTSNTNG VDTVLDKVDG VSADPIPESW RSEVTFTTPA VYIYTSGTTG LPKAATINHH 250 260 270 280 290 300 RLWYGTSLAL RSGIKAHDVI YTTMPLYHSA ALMIGLHGCI VVGATFALRS KFSASQFWDD 310 320 330 340 350 360 CRKYNATVIQ YIGELLRYLC NTPQKPNDRD HKVKIALGNG LRGDVWREFI KRFGDIHIYE 370 380 390 400 410 420 FYASTEGNIG FMNYPRKIGA VGRENYLQKK VVRHELIKYD VEKDEPVRDA NGYCIKVPKG 430 440 450 460 470 480 EVGLLICKIT ELTPFFGYAG GKTQTEKKKL RDVFKKGDVY FNSGDLLMID RENFIYFHDR 490 500 510 520 530 540 VGDTFRWKGE NVATTEVADI VGLVDFVEEV NVYGVPVPGH EGRIGMASIK MKENYEFNGK 550 560 570 580 590 600 KLFQHISEYL PSYSRPRFLR IQDTIEITGT FKHRKVTLME EGFNPSVIKD TLYFMDDTEK 610 620 TYVPMTEDIY NAIIDKTLKL

References

[1]	"Molecular cloning of cDNA encoding rat very long-chain acyl-CoA synthetase." Uchiyama A., Aoyama T., Kamijo K., Uchida Y., Kondo N., Orii T., Hashimoto T. J. Biol. Chem. 271:30360-30365(1996) [PubMed: 8939997] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Strain: Wistar. Tissue: Liver.
[2]	"Intraperoxisomal localization of very-long-chain fatty acyl-CoA synthetase: implication in X-adrenoleukodystrophy." Smith B.T., Sengupta T.K., Singh I. Exp. Cell Res. 254:309-320(2000) [PubMed: 10640429] [Abstract] Cited for: SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D85100 mRNA. Translation: BAA12722.1.
IPI	IPI00205417.
RefSeq	NP_113924.1.
UniGene	Rn.3608
3D structure databases
SMR	P97524. Positions 57-583.
ModBase	Search...
Proteomic databases
PRIDE	P97524.
Genome annotation databases
Ensembl	ENSRNOT00000067523; ENSRNOP00000063336; ENSRNOG00000010128; Rattus norvegicus. [Genome view]
GeneID	65192.
KEGG	rno:65192.
Organism-specific databases
CTD	65192.
RGD	71103. Slc27a2.
Phylogenomic databases
HOVERGEN	P97524.
PhylomeDB	P97524.
Enzyme and pathway databases
BRENDA	6.2.1.3. 248.
Gene expression databases
Genevestigator	P97524.
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 Resources
NextBio	614116.

Entry information

Entry name

S27A2_RAT

Accession

Primary (citable) accession number: P97524

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	May 1, 1997
Last modified:	January 19, 2010
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)