Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O35488

- S27A2_MOUSE

UniProt

O35488 - S27A2_MOUSE

Protein

Very long-chain acyl-CoA synthetase

Gene

Slc27a2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.By similarity1 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 – 23312AMPSequence AnalysisAdd
    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

    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 By similarity; Multi-pass membrane protein By similarity. Peroxisome membrane By similarity; Multi-pass membrane protein By similarity
    Note: Peripheral membrane associated with the lumenal side of peroxisomes.By similarity

    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

    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 – 5771PhosphothreonineBy 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 44LumenalBy similarity
    Topological domaini28 – 10679CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini128 – 267140LumenalSequence AnalysisAdd
    BLAST
    Topological domaini289 – 620332CytoplasmicBy similarityAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei5 – 2723HelicalSequence AnalysisAdd
    BLAST
    Transmembranei107 – 12721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei268 – 28821HelicalSequence AnalysisAdd
    BLAST

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti35 – 351R → Q in AAB87982. (PubMed:11980911)Curated
    Sequence conflicti168 – 1681V → A in CAA11687. (PubMed:9559670)Curated
    Sequence conflicti168 – 1681V → A in AAB87982. (PubMed:11980911)Curated
    Sequence conflicti234 – 2352AA → SG in AAC40186. (PubMed:9671728)Curated
    Sequence conflicti243 – 2431W → R in AAC40186. (PubMed:9671728)Curated
    Sequence conflicti247 – 2471G → S in AAC40186. (PubMed:9671728)Curated
    Sequence conflicti257 – 2571Q → K in AAC40186. (PubMed:9671728)Curated
    Sequence conflicti271 – 2711A → T in AAC40186. (PubMed:9671728)Curated

    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

    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: October 1, 2014
    This is version 111 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