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P20852

- CP2A5_MOUSE

UniProt

P20852 - CP2A5_MOUSE

Protein

Cytochrome P450 2A5

Gene

Cyp2a5

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 1 (01 Feb 1991)
      Previous versions | rss
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    Functioni

    Exhibits a high coumarin 7-hydroxylase activity.

    Catalytic activityi

    RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O.

    Cofactori

    Heme group.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi439 – 4391Iron (heme axial ligand)

    GO - Molecular functioni

    1. aromatase activity Source: UniProtKB-EC
    2. heme binding Source: InterPro
    3. iron ion binding Source: InterPro

    GO - Biological processi

    1. response to stilbenoid Source: UniProtKB

    Keywords - Molecular functioni

    Monooxygenase, Oxidoreductase

    Keywords - Ligandi

    Heme, Iron, Metal-binding

    Enzyme and pathway databases

    SABIO-RKP20852.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cytochrome P450 2A5 (EC:1.14.14.1)
    Alternative name(s):
    CYPIIA5
    Coumarin 7-hydroxylase
    Cytochrome P450-15-COH
    Cytochrome P450-IIA3.2
    Gene namesi
    Name:Cyp2a5
    Synonyms:Cyp2a-5
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:88597. Cyp2a5.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane, Microsome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 494494Cytochrome P450 2A5PRO_0000051667Add
    BLAST

    Proteomic databases

    MaxQBiP20852.
    PaxDbiP20852.
    PRIDEiP20852.

    PTM databases

    PhosphoSiteiP20852.

    Expressioni

    Tissue specificityi

    Liver, with a strong circadian rhythmicity. Circadian expression is regulated by DBP.1 Publication

    Developmental stagei

    In liver; activity 6 fold higher in females than in males.

    Gene expression databases

    GenevestigatoriP20852.

    Interactioni

    Protein-protein interaction databases

    MINTiMINT-1862789.

    Structurei

    3D structure databases

    ProteinModelPortaliP20852.
    SMRiP20852. Positions 31-494.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the cytochrome P450 family.Curated

    Phylogenomic databases

    eggNOGiCOG2124.
    HOGENOMiHOG000036992.
    HOVERGENiHBG015789.
    InParanoidiP20852.
    PhylomeDBiP20852.

    Family and domain databases

    Gene3Di1.10.630.10. 1 hit.
    InterProiIPR001128. Cyt_P450.
    IPR017972. Cyt_P450_CS.
    IPR002401. Cyt_P450_E_grp-I.
    IPR008067. Cyt_P450_E_grp-I_CYP2A-like.
    [Graphical view]
    PfamiPF00067. p450. 1 hit.
    [Graphical view]
    PRINTSiPR00463. EP450I.
    PR01684. EP450ICYP2A.
    PR00385. P450.
    SUPFAMiSSF48264. SSF48264. 1 hit.
    PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P20852-1 [UniParc]FASTAAdd to Basket

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    MLTSGLLLVA AVAFLSVLVL MSVWKQRKLS GKLPPGPTPL PFIGNFLQLN    50
    TEQMYNSLMK ISQRYGPVFT IYLGPRRIVV LCGQEAVKEA LVDQAEEFSG 100
    RGEQATFDWL FKGYGVVFSS GERAKQLRRF SIATLRDFGV GKRGIEERIQ 150
    EEAGFLIDSF RKTNGAFIDP TFYLSRTVSN VISSIVFGDR FDYEDKEFLS 200
    LLRMMLGSFQ FTATSMGQLY EMFSSVMKHL PGPQQQAFKE LQGLEDFITK 250
    KVEHNQRTLD PNSPRDFIDS FLIRMLEEKK NPNTEFYMKN LVLTTLNLFF 300
    AGTETVSTTL RYGFLLLMKH PDIEAKVHEE IDRVIGRNRQ PKYEDRMKMP 350
    YTEAVIHEIQ RFADMIPMGL ARRVTKDTKF RDFLLPKGTE VFPMLGSVLK 400
    DPKFFSNPKD FNPKHFLDDK GQFKKNDAFV PFSIGKRYCF GEGLARMELF 450
    LFLTNIMQNF HFKSTQAPQD IDVSPRLVGF ATIPPTYTMS FLSR 494
    Length:494
    Mass (Da):56,741
    Last modified:February 1, 1991 - v1
    Checksum:i1C2516D5FA2551D0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M25211
    , M26204, M25205, M25206, M25207, M25208, M25209, M25210 Genomic DNA. Translation: AAA37798.1.
    X89864 mRNA. Translation: CAA61963.1.
    CCDSiCCDS21008.1.
    PIRiB33531.
    UniGeneiMm.389848.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M25211
    , M26204 , M25205 , M25206 , M25207 , M25208 , M25209 , M25210 Genomic DNA. Translation: AAA37798.1 .
    X89864 mRNA. Translation: CAA61963.1 .
    CCDSi CCDS21008.1.
    PIRi B33531.
    UniGenei Mm.389848.

    3D structure databases

    ProteinModelPortali P20852.
    SMRi P20852. Positions 31-494.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-1862789.

    Chemistry

    BindingDBi P20852.
    ChEMBLi CHEMBL4085.

    PTM databases

    PhosphoSitei P20852.

    Proteomic databases

    MaxQBi P20852.
    PaxDbi P20852.
    PRIDEi P20852.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    MGIi MGI:88597. Cyp2a5.

    Phylogenomic databases

    eggNOGi COG2124.
    HOGENOMi HOG000036992.
    HOVERGENi HBG015789.
    InParanoidi P20852.
    PhylomeDBi P20852.

    Enzyme and pathway databases

    SABIO-RK P20852.

    Miscellaneous databases

    PROi P20852.
    SOURCEi Search...

    Gene expression databases

    Genevestigatori P20852.

    Family and domain databases

    Gene3Di 1.10.630.10. 1 hit.
    InterProi IPR001128. Cyt_P450.
    IPR017972. Cyt_P450_CS.
    IPR002401. Cyt_P450_E_grp-I.
    IPR008067. Cyt_P450_E_grp-I_CYP2A-like.
    [Graphical view ]
    Pfami PF00067. p450. 1 hit.
    [Graphical view ]
    PRINTSi PR00463. EP450I.
    PR01684. EP450ICYP2A.
    PR00385. P450.
    SUPFAMi SSF48264. SSF48264. 1 hit.
    PROSITEi PS00086. CYTOCHROME_P450. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The structure and characterization of type I P-450(15) alpha gene as major steroid 15 alpha-hydroxylase and its comparison with type II P-450(15) alpha gene."
      Lindberg R., Burkhart B., Ichikawa T., Negishi M.
      J. Biol. Chem. 264:6465-6471(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Kidney.
    2. "cDNA and amino acid sequence of a new cyp2a isoform overexpressed in chemically induced mouse hepatoma."
      Jounaidi Y.
      Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: 17NC/Z.
    3. "Alteration of mouse cytochrome P450coh substrate specificity by mutation of a single amino-acid residue."
      Lindberg R., Negishi M.
      Nature 339:632-634(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS.
    4. "Circadian expression of the steroid 15 alpha-hydroxylase (Cyp2a4) and coumarin 7-hydroxylase (Cyp2a5) genes in mouse liver is regulated by the PAR leucine zipper transcription factor DBP."
      Lavery D.J., Lopez-Molina L., Margueron R., Fleury-Olela F., Conquet F., Schibler U., Bonfils C.
      Mol. Cell. Biol. 19:6488-6499(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiCP2A5_MOUSE
    AccessioniPrimary (citable) accession number: P20852
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: February 1, 1991
    Last modified: October 1, 2014
    This is version 112 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    There are only 11 differences between the sequence of testosterone 15-alpha-hydroxylase and that of coumarin 7-hydroxylase. By site-directed mutagenesis it has been shown that modification of position 209 is sufficient to convert the specificity of the two forms of the enzyme.

    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