Very long-chain acyl-CoA synthetase

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Reviewed, UniProtKB/Swiss-Prot O35488 (S27A2_MOUSE)

Last modified November 3, 2009. Version 71. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

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

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Protein attributes

Sequence length	620 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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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 By similarity. May be involved in translocation of long-chain fatty acids (LFCA) across membranes.
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 By similarity. Peroxisome membrane; Multi-pass membrane protein By similarity. Note: Peripheral membrane associated with the lumenal side of peroxisomes By similarity.
Tissue specificity	Strong expression in liver and kidney, low expression in brain and testis, no expression in skeletal muscle and spleen. Shows uniform distribution in liver acinus. Ref.3
Sequence similarities	Belongs to the ATP-dependent AMP-binding enzyme family.
Sequence caution	The sequence AAC40186.1 differs from that shown. Reason: Frameshift at positions 253, 263, 267, 281, 289, 293, 299, 301 and 307.

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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
Gene Ontology (GO)
Biological process	fatty acid transport Inferred from direct assay. Source: MGI long-chain fatty acid metabolic process Inferred from direct assay. Source: MGI very-long-chain fatty acid catabolic process Inferred from mutant phenotype. Source: MGI
Cellular component	endoplasmic reticulum Inferred from direct assay. Source: MGI integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell microsome Inferred from mutant phenotype. Source: MGI mitochondrion Inferred from direct assay. Source: MGI peroxisome Inferred from direct assay. Source: MGI
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW fatty acid transporter activity Ref.2 Inferred from direct assay. Source: MGI long-chain-fatty-acid-CoA ligase activity Inferred from direct assay. Source: MGI very-long-chain-fatty-acid-CoA ligase activity Inferred from direct assay. Source: MGI
Complete GO annotation...

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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_0000193205

Regions

Topological domain

1 – 4

Lumenal By similarity

Transmembrane

5 – 27

Potential

Topological domain

28 – 106

Cytoplasmic Potential

Transmembrane

107 – 127

Potential

Topological domain

128 – 267

140

Lumenal Potential

Transmembrane

268 – 288

Potential

Topological domain

289 – 620

332

Cytoplasmic By similarity

Nucleotide binding

222 – 233

AMP Potential

Amino acid modifications

Modified residue

291

N6-acetyllysine Ref.5

Modified residue

325

N6-acetyllysine Ref.5

Modified residue

577

Phosphothreonine By similarity

Experimental info

Sequence conflict

Q → R Ref.1

Sequence conflict

Q → R Ref.2

Sequence conflict

168

A → V in AAC40186. Ref.2

Sequence conflict

234 – 235

AA → SG in AAC40186. Ref.2

Sequence conflict

243

W → R in AAC40186. Ref.2

Sequence conflict

247

G → S in AAC40186. Ref.2

Sequence conflict

257

Q → K in AAC40186. Ref.2

Sequence conflict

271

A → T in AAC40186. Ref.2

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Sequences

Sequence

Length

Mass (Da)

Tools

O35488-1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 77C98BD0DE3B9FFB
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FASTA

620

70,366

        10         20         30         40         50         60 
MLPVLYTGLA GLLLLPLLLT CCCPYLLQDV RYFLQLANMA RRVRSYRQRR PVRTILRAFL 

        70         80         90        100        110        120 
EQARKTPHKP FLLFRDETLT YAQVDRRSNQ VARALHDQLG LRQGDCVALF MGNEPAYVWI 

       130        140        150        160        170        180 
WLGLLKLGCP MACLNYNIRA KSLLHCFQCC GAKVLLASPD LQEAVEEALP TLKKDAVSVF 

       190        200        210        220        230        240 
YVSRTSNTNG VDTILDKVDG VSAEPTPESW RSEVTFTTPA VYIYTSGTTG LPKAATINHH 

       250        260        270        280        290        300 
RLWYGTGLAM SSGITAQDVI YTTMPLYHSA ALMIGLHGCI VVGATLALRS KFSASQFWDD 

       310        320        330        340        350        360 
CRKYNVTVIQ YIGELLRYLC NTPQKPNDRD HKVKKALGNG LRGDVWREFI KRFGDIHVYE 

       370        380        390        400        410        420 
FYASTEGNIG FVNYPRKIGA VGRANYLQRK VARYELIKYD VEKDEPVRDA NGYCIKVPKG 

       430        440        450        460        470        480 
EVGLLVCKIT QLTPFIGYAG GKTQTEKKKL RDVFKKGDIY FNSGDLLMID RENFVYFHDR 

       490        500        510        520        530        540 
VGDTFRWKGE NVATTEVADI VGLVDFVEEV NVYGVPVPGH EGRIGMASLK IKENYEFNGK 

       550        560        570        580        590        600 
KLFQHIAEYL PSYARPRFLR IQDTIEITGT FKHRKVTLME EGFNPTVIKD TLYFMDDAEK 

       610        620 
TFVPMTENIY NAIIDKTLKL

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA cloning and mRNA distribution of a mouse very long-chain acyl-CoA synthetase." Berger J., Truppe C., Neumann H., Forss-Petter S. FEBS Lett. 425:305-309(1998) [PubMed: 9559670] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c. Tissue: Liver.
[2]	"A family of fatty acid transporters conserved from mycobacterium to man." Hirsch D., Stahl A., Lodish H.F. Proc. Natl. Acad. Sci. U.S.A. 95:8625-8629(1998) [PubMed: 9671728] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"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: 11980911] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Strain: C57BL/6. Tissue: Liver.
[4]	"Comparative biochemical studies of the murine fatty acid transport proteins (FATP) expressed in yeast." DiRusso C.C., Li H., Darwis D., Watkins P.A., Berger J., Black P.N. J. Biol. Chem. 280:16829-16837(2005) [PubMed: 15699031] [Abstract] Cited for: FUNCTION IN FATTY ACID TRANSPORT.
[5]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-291 AND LYS-325, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	AJ223958 mRNA. Translation: CAA11687.1. AF072757 mRNA. Translation: AAC40186.1. Sequence problems. AF033031 mRNA. Translation: AAB87982.1.
IPI	IPI00130924.
RefSeq	NP_036108.2.
UniGene	Mm.290044
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	O35488.
PTM databases
PhosphoSite	O35488.
Proteomic databases
PRIDE	O35488.
Genome annotation databases
Ensembl	ENSMUST00000061491; ENSMUSP00000057595; ENSMUSG00000027359; Mus musculus. [Genome view]
GeneID	26458.
KEGG	mmu:26458.
Organism-specific databases
MGI	MGI:1347099. Slc27a2.
Phylogenomic databases
HOGENOM	O35488.
HOVERGEN	O35488.
Enzyme and pathway databases
BRENDA	6.2.1.3. 244.
Gene expression databases
ArrayExpress	O35488.
Bgee	O35488.
Genevestigator	O35488.
GermOnline	ENSMUSG00000027359. Mus musculus.
Family and domain databases
InterPro	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
SOURCE	Search...

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Entry information

Entry name

S27A2_MOUSE

Accession

Primary (citable) accession number: O35488
Secondary accession number(s): O70550, O88560

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 1, 1998
Last modified:	November 3, 2009
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents