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P97524 (S27A2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

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. May be involved in translocation of long-chain fatty acids (LFCA) across membranes By similarity.

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. 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 620620Very long-chain acyl-CoA synthetase
PRO_0000193206

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 By similarity
Modified residue5771Phosphothreonine By similarity

Sequences

Sequence LengthMass (Da)Tools
P97524 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 6CF9362DC3805526

FASTA62070,694
        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 

« Hide

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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D85100 mRNA. Translation: BAA12722.1.
RefSeqNP_113924.1. NM_031736.1.
UniGeneRn.3608.

3D structure databases

ProteinModelPortalP97524.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid249304. 1 interaction.
STRING10116.ENSRNOP00000063336.

Proteomic databases

PaxDbP97524.
PRIDEP97524.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID65192.
KEGGrno:65192.
UCSCRGD:71103. rat.

Organism-specific databases

CTD11001.
RGD71103. Slc27a2.

Phylogenomic databases

eggNOGCOG0318.
HOGENOMHOG000044189.
HOVERGENHBG005642.
KOK08746.
PhylomeDBP97524.

Gene expression databases

GenevestigatorP97524.

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

NextBio614116.

Entry information

Entry nameS27A2_RAT
AccessionPrimary (citable) accession number: P97524
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 1, 1997
Last modified: June 11, 2014
This is version 94 of the entry and version 1 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