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O35488 (S27A2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Very long-chain acyl-CoA synthetase

Short name=VLACS
Short name=VLCS
EC=6.2.1.-
Alternative name(s):
Fatty acid transport protein 2
Short name=FATP-2
Fatty-acid-coenzyme A ligase, very long-chain 1
Long-chain-fatty-acid--CoA ligase
EC=6.2.1.3
Solute carrier family 27 member 2
THCA-CoA ligase
Very long-chain-fatty-acid-CoA ligase
Gene names
Name:Slc27a2
Synonyms:Acsvl1, Facvl1, Fatp2, Vlacs, Vlcs
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length620 AA.
Sequence statusComplete.
Protein existenceEvidence 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 By similarity. May be involved in translocation of long-chain fatty acids (LFCA) across membranes. Ref.6

Catalytic activity

ATP + a long-chain fatty 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.

Ontologies

Keywords
   Biological processFatty acid metabolism
Lipid metabolism
   Cellular componentEndoplasmic reticulum
Membrane
Peroxisome
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbile acid biosynthetic process

Inferred from electronic annotation. Source: Ensembl

fatty acid alpha-oxidation

Inferred from electronic annotation. Source: Ensembl

fatty acid beta-oxidation

Inferred from electronic annotation. Source: Ensembl

fatty acid transport

Inferred from direct assay PubMed 9271215. Source: MGI

long-chain fatty acid import

Inferred from electronic annotation. Source: Ensembl

long-chain fatty acid metabolic process

Inferred from direct assay PubMed 12048192. Source: MGI

methyl-branched fatty acid metabolic process

Inferred from electronic annotation. Source: Ensembl

very long-chain fatty acid catabolic process

Inferred from mutant phenotype PubMed 12719378. Source: MGI

very long-chain fatty acid metabolic process

Inferred from direct assay PubMed 12048192. Source: MGI

   Cellular_componentendoplasmic reticulum

Inferred from direct assay PubMed 12048192. Source: MGI

endoplasmic reticulum lumen

Inferred from sequence or structural similarity PubMed 10198260. Source: UniProtKB

integral component of endoplasmic reticulum membrane

Inferred from electronic annotation. Source: Ensembl

integral component of peroxisomal membrane

Inferred from sequence or structural similarity PubMed 10198260. Source: UniProtKB

mitochondrion

Inferred from direct assay PubMed 14651853. Source: MGI

peroxisome

Inferred from direct assay PubMed 12048192. Source: MGI

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

fatty acid transporter activity

Inferred from direct assay Ref.2. Source: MGI

long-chain fatty acid-CoA ligase activity

Inferred from direct assay PubMed 12048192. Source: MGI

phytanate-CoA ligase activity

Inferred from electronic annotation. Source: Ensembl

pristanate-CoA ligase activity

Inferred from electronic annotation. Source: Ensembl

very long-chain fatty acid-CoA ligase activity

Inferred from direct assay PubMed 12048192. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 620620Very long-chain acyl-CoA synthetase
PRO_0000193205

Regions

Topological domain1 – 44Lumenal By similarity
Transmembrane5 – 2723Helical; Potential
Topological domain28 – 10679Cytoplasmic Potential
Transmembrane107 – 12721Helical; Potential
Topological domain128 – 267140Lumenal Potential
Transmembrane268 – 28821Helical; Potential
Topological domain289 – 620332Cytoplasmic By similarity
Nucleotide binding222 – 23312AMP Potential

Amino acid modifications

Modified residue2911N6-acetyllysine Ref.7
Modified residue5771Phosphothreonine By similarity

Experimental info

Sequence conflict351R → Q in AAB87982. Ref.3
Sequence conflict1681V → A in CAA11687. Ref.1
Sequence conflict1681V → A in AAB87982. Ref.3
Sequence conflict234 – 2352AA → SG in AAC40186. Ref.2
Sequence conflict2431W → R in AAC40186. Ref.2
Sequence conflict2471G → S in AAC40186. Ref.2
Sequence conflict2571Q → K in AAC40186. Ref.2
Sequence conflict2711A → T in AAC40186. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O35488 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 62994BDB1D828B37

FASTA62070,423
        10         20         30         40         50         60 
MLPVLYTGLA GLLLLPLLLT CCCPYLLQDV RYFLRLANMA RRVRSYRQRR PVRTILRAFL 

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

       130        140        150        160        170        180 
WLGLLKLGCP MACLNYNIRA KSLLHCFQCC GAKVLLASPD LQEAVEEVLP 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 

« Hide

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Strain: C57BL/6.
Tissue: Liver.
[4]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Kidney and Liver.
[6]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION IN FATTY ACID TRANSPORT.
[7]"Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-291, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ223958 mRNA. Translation: CAA11687.1.
AF072757 mRNA. Translation: AAC40186.1. Sequence problems.
AF033031 mRNA. Translation: AAB87982.1.
AL831764, AL844555 Genomic DNA. Translation: CAM17405.1.
AL844555, AL831764 Genomic DNA. Translation: CAM18704.1.
BC013442 mRNA. Translation: AAH13442.1.
BC022170 mRNA. Translation: AAH22170.1.
BC024735 mRNA. Translation: AAH24735.1.
RefSeqNP_036108.2. NM_011978.2.
UniGeneMm.290044.

3D structure databases

ProteinModelPortalO35488.
SMRO35488. Positions 60-559.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActO35488. 4 interactions.
MINTMINT-1862718.
STRING10090.ENSMUSP00000057595.

PTM databases

PhosphoSiteO35488.

Proteomic databases

PaxDbO35488.
PRIDEO35488.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000061491; ENSMUSP00000057595; ENSMUSG00000027359.
GeneID26458.
KEGGmmu:26458.
UCSCuc008mdq.1. mouse.

Organism-specific databases

CTD11001.
MGIMGI:1347099. Slc27a2.

Phylogenomic databases

eggNOGCOG0318.
GeneTreeENSGT00550000074420.
HOGENOMHOG000044189.
HOVERGENHBG005642.
InParanoidQ91WV6.
KOK08746.
OMARSSNTDG.
OrthoDBEOG7W6WKB.
TreeFamTF313430.

Gene expression databases

ArrayExpressO35488.
BgeeO35488.
GenevestigatorO35488.

Family and domain databases

InterProIPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
PROSITEPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSLC27A2. mouse.
NextBio304569.
PROO35488.
SOURCESearch...

Entry information

Entry nameS27A2_MOUSE
AccessionPrimary (citable) accession number: O35488
Secondary accession number(s): O70550, O88560, Q91WV6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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