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O35488

- S27A2_MOUSE

UniProt

O35488 - S27A2_MOUSE

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Protein

Very long-chain acyl-CoA synthetase

Gene
Slc27a2, Acsvl1, Facvl1, Fatp2, Vlacs, Vlcs
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi222 – 23312AMP Reviewed predictionAdd
BLAST

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. fatty acid transporter activity Source: MGI
  3. long-chain fatty acid-CoA ligase activity Source: MGI
  4. phytanate-CoA ligase activity Source: Ensembl
  5. pristanate-CoA ligase activity Source: Ensembl
  6. very long-chain fatty acid-CoA ligase activity Source: MGI

GO - Biological processi

  1. bile acid biosynthetic process Source: Ensembl
  2. fatty acid alpha-oxidation Source: Ensembl
  3. fatty acid beta-oxidation Source: Ensembl
  4. fatty acid transport Source: MGI
  5. long-chain fatty acid import Source: Ensembl
  6. long-chain fatty acid metabolic process Source: MGI
  7. methyl-branched fatty acid metabolic process Source: Ensembl
  8. very long-chain fatty acid catabolic process Source: MGI
  9. very long-chain fatty acid metabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_203193. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
REACT_210229. Synthesis of bile acids and bile salts via 24-hydroxycholesterol.

Names & Taxonomyi

Protein namesi
Recommended name:
Very long-chain acyl-CoA synthetase (EC:6.2.1.-)
Short name:
VLACS
Short name:
VLCS
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 namesi
Name:Slc27a2
Synonyms:Acsvl1, Facvl1, Fatp2, Vlacs, Vlcs
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:1347099. Slc27a2.

Subcellular locationi

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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 44Lumenal By similarity
Transmembranei5 – 2723Helical; Reviewed predictionAdd
BLAST
Topological domaini28 – 10679Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei107 – 12721Helical; Reviewed predictionAdd
BLAST
Topological domaini128 – 267140Lumenal Reviewed predictionAdd
BLAST
Transmembranei268 – 28821Helical; Reviewed predictionAdd
BLAST
Topological domaini289 – 620332Cytoplasmic By similarityAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: MGI
  2. endoplasmic reticulum lumen Source: UniProtKB
  3. integral component of endoplasmic reticulum membrane Source: Ensembl
  4. integral component of peroxisomal membrane Source: UniProtKB
  5. mitochondrion Source: MGI
  6. peroxisome Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 620620Very long-chain acyl-CoA synthetasePRO_0000193205Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei291 – 2911N6-acetyllysine1 Publication
Modified residuei577 – 5771Phosphothreonine By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO35488.
PaxDbiO35488.
PRIDEiO35488.

PTM databases

PhosphoSiteiO35488.

Expressioni

Tissue specificityi

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.1 Publication

Gene expression databases

ArrayExpressiO35488.
BgeeiO35488.
GenevestigatoriO35488.

Interactioni

Protein-protein interaction databases

IntActiO35488. 4 interactions.
MINTiMINT-1862718.
STRINGi10090.ENSMUSP00000057595.

Structurei

3D structure databases

ProteinModelPortaliO35488.
SMRiO35488. Positions 60-559.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0318.
GeneTreeiENSGT00550000074420.
HOGENOMiHOG000044189.
HOVERGENiHBG005642.
InParanoidiQ91WV6.
KOiK08746.
OMAiRSSNTDG.
OrthoDBiEOG7W6WKB.
TreeFamiTF313430.

Family and domain databases

InterProiIPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O35488-1 [UniParc]FASTAAdd to Basket

« Hide

MLPVLYTGLA GLLLLPLLLT CCCPYLLQDV RYFLRLANMA RRVRSYRQRR    50
PVRTILRAFL EQARKTPHKP FLLFRDETLT YAQVDRRSNQ VARALHDQLG 100
LRQGDCVALF MGNEPAYVWI WLGLLKLGCP MACLNYNIRA KSLLHCFQCC 150
GAKVLLASPD LQEAVEEVLP TLKKDAVSVF YVSRTSNTNG VDTILDKVDG 200
VSAEPTPESW RSEVTFTTPA VYIYTSGTTG LPKAATINHH RLWYGTGLAM 250
SSGITAQDVI YTTMPLYHSA ALMIGLHGCI VVGATLALRS KFSASQFWDD 300
CRKYNVTVIQ YIGELLRYLC NTPQKPNDRD HKVKKALGNG LRGDVWREFI 350
KRFGDIHVYE FYASTEGNIG FVNYPRKIGA VGRANYLQRK VARYELIKYD 400
VEKDEPVRDA NGYCIKVPKG EVGLLVCKIT QLTPFIGYAG GKTQTEKKKL 450
RDVFKKGDIY FNSGDLLMID RENFVYFHDR VGDTFRWKGE NVATTEVADI 500
VGLVDFVEEV NVYGVPVPGH EGRIGMASLK IKENYEFNGK KLFQHIAEYL 550
PSYARPRFLR IQDTIEITGT FKHRKVTLME EGFNPTVIKD TLYFMDDAEK 600
TFVPMTENIY NAIIDKTLKL 620
Length:620
Mass (Da):70,423
Last modified:July 27, 2011 - v2
Checksum:i62994BDB1D828B37
GO

Sequence cautioni

The sequence AAC40186.1 differs from that shown. Reason: Frameshift at positions 253, 263, 267, 281, 289, 293, 299, 301 and 307.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti35 – 351R → Q in AAB87982. 1 Publication
Sequence conflicti168 – 1681V → A in CAA11687. 1 Publication
Sequence conflicti168 – 1681V → A in AAB87982. 1 Publication
Sequence conflicti234 – 2352AA → SG in AAC40186. 1 Publication
Sequence conflicti243 – 2431W → R in AAC40186. 1 Publication
Sequence conflicti247 – 2471G → S in AAC40186. 1 Publication
Sequence conflicti257 – 2571Q → K in AAC40186. 1 Publication
Sequence conflicti271 – 2711A → T in AAC40186. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS16683.1.
RefSeqiNP_036108.2. NM_011978.2.
UniGeneiMm.290044.

Genome annotation databases

EnsembliENSMUST00000061491; ENSMUSP00000057595; ENSMUSG00000027359.
GeneIDi26458.
KEGGimmu:26458.
UCSCiuc008mdq.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS16683.1.
RefSeqi NP_036108.2. NM_011978.2.
UniGenei Mm.290044.

3D structure databases

ProteinModelPortali O35488.
SMRi O35488. Positions 60-559.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi O35488. 4 interactions.
MINTi MINT-1862718.
STRINGi 10090.ENSMUSP00000057595.

PTM databases

PhosphoSitei O35488.

Proteomic databases

MaxQBi O35488.
PaxDbi O35488.
PRIDEi O35488.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000061491 ; ENSMUSP00000057595 ; ENSMUSG00000027359 .
GeneIDi 26458.
KEGGi mmu:26458.
UCSCi uc008mdq.1. mouse.

Organism-specific databases

CTDi 11001.
MGIi MGI:1347099. Slc27a2.

Phylogenomic databases

eggNOGi COG0318.
GeneTreei ENSGT00550000074420.
HOGENOMi HOG000044189.
HOVERGENi HBG005642.
InParanoidi Q91WV6.
KOi K08746.
OMAi RSSNTDG.
OrthoDBi EOG7W6WKB.
TreeFami TF313430.

Enzyme and pathway databases

Reactomei REACT_203193. Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol.
REACT_210229. Synthesis of bile acids and bile salts via 24-hydroxycholesterol.

Miscellaneous databases

ChiTaRSi SLC27A2. mouse.
NextBioi 304569.
PROi O35488.
SOURCEi Search...

Gene expression databases

ArrayExpressi O35488.
Bgeei O35488.
Genevestigatori O35488.

Family and domain databases

InterProi IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view ]
Pfami PF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view ]
PROSITEi PS00455. AMP_BINDING. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiS27A2_MOUSE
AccessioniPrimary (citable) accession number: O35488
Secondary accession number(s): O70550, O88560, Q91WV6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 27, 2011
Last modified: September 3, 2014
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi