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P97524

- S27A2_RAT

UniProt

P97524 - S27A2_RAT

Protein

Very long-chain acyl-CoA synthetase

Gene

Slc27a2

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 1 (01 May 1997)
      Previous versions | rss
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    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. May be involved in translocation of long-chain fatty acids (LFCA) across membranes By similarity.By similarity

    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. long-chain fatty acid-CoA ligase activity Source: UniProtKB
    3. protein binding Source: RGD
    4. very long-chain fatty acid-CoA ligase activity Source: UniProtKB

    GO - Biological processi

    1. long-chain fatty acid metabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    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
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi71103. Slc27a2.

    Subcellular locationi

    Endoplasmic reticulum membrane 1 Publication; Multi-pass membrane protein 1 Publication. Peroxisome membrane 1 Publication; Multi-pass membrane protein 1 Publication
    Note: Peripheral membrane associated with the lumenal side of peroxisomes.

    GO - Cellular componenti

    1. endoplasmic reticulum lumen Source: UniProtKB
    2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    3. integral component of peroxisomal membrane Source: UniProtKB
    4. intracellular membrane-bounded organelle Source: RGD
    5. peroxisomal membrane Source: HGNC
    6. peroxisome Source: RGD

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane, Peroxisome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 620620Very long-chain acyl-CoA synthetasePRO_0000193206Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei291 – 2911N6-acetyllysineBy similarity
    Modified residuei577 – 5771PhosphothreonineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiP97524.
    PRIDEiP97524.

    Expressioni

    Gene expression databases

    GenevestigatoriP97524.

    Interactioni

    Protein-protein interaction databases

    BioGridi249304. 1 interaction.
    STRINGi10116.ENSRNOP00000063336.

    Structurei

    3D structure databases

    ProteinModelPortaliP97524.
    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.
    HOGENOMiHOG000044189.
    HOVERGENiHBG005642.
    KOiK08746.
    PhylomeDBiP97524.

    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.

    P97524-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLPVLYTGLA GLLLLPLLLT CCCPYLLQDV RFFLQLANMA RQVRSYRQRR    50
    PVRTILHVFL EQARKTPHKP FLLFRDETLT YAQVDRRSNQ VARALHDHLG 100
    LRQGDCVALF MGNEPAYVWL WLGLLKLGCP MACLNYNIRA KSLLHCFQCC 150
    GAKVLLASPE LHEAVEEVLP TLKKEGVSVF YVSRTSNTNG VDTVLDKVDG 200
    VSADPIPESW RSEVTFTTPA VYIYTSGTTG LPKAATINHH RLWYGTSLAL 250
    RSGIKAHDVI YTTMPLYHSA ALMIGLHGCI VVGATFALRS KFSASQFWDD 300
    CRKYNATVIQ YIGELLRYLC NTPQKPNDRD HKVKIALGNG LRGDVWREFI 350
    KRFGDIHIYE FYASTEGNIG FMNYPRKIGA VGRENYLQKK VVRHELIKYD 400
    VEKDEPVRDA NGYCIKVPKG EVGLLICKIT ELTPFFGYAG GKTQTEKKKL 450
    RDVFKKGDVY FNSGDLLMID RENFIYFHDR VGDTFRWKGE NVATTEVADI 500
    VGLVDFVEEV NVYGVPVPGH EGRIGMASIK MKENYEFNGK KLFQHISEYL 550
    PSYSRPRFLR IQDTIEITGT FKHRKVTLME EGFNPSVIKD TLYFMDDTEK 600
    TYVPMTEDIY NAIIDKTLKL 620
    Length:620
    Mass (Da):70,694
    Last modified:May 1, 1997 - v1
    Checksum:i6CF9362DC3805526
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D85100 mRNA. Translation: BAA12722.1.
    RefSeqiNP_113924.1. NM_031736.1.
    UniGeneiRn.3608.

    Genome annotation databases

    GeneIDi65192.
    KEGGirno:65192.
    UCSCiRGD:71103. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D85100 mRNA. Translation: BAA12722.1 .
    RefSeqi NP_113924.1. NM_031736.1.
    UniGenei Rn.3608.

    3D structure databases

    ProteinModelPortali P97524.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 249304. 1 interaction.
    STRINGi 10116.ENSRNOP00000063336.

    Proteomic databases

    PaxDbi P97524.
    PRIDEi P97524.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 65192.
    KEGGi rno:65192.
    UCSCi RGD:71103. rat.

    Organism-specific databases

    CTDi 11001.
    RGDi 71103. Slc27a2.

    Phylogenomic databases

    eggNOGi COG0318.
    HOGENOMi HOG000044189.
    HOVERGENi HBG005642.
    KOi K08746.
    PhylomeDBi P97524.

    Miscellaneous databases

    NextBioi 614116.

    Gene expression databases

    Genevestigatori P97524.

    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. "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.

    Entry informationi

    Entry nameiS27A2_RAT
    AccessioniPrimary (citable) accession number: P97524
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: May 1, 1997
    Last modified: October 1, 2014
    This is version 95 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3