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P00176

- CP2B1_RAT

UniProt

P00176 - CP2B1_RAT

Protein

Cytochrome P450 2B1

Gene

Cyp2b1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    Functioni

    Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.

    Catalytic activityi

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

    Cofactori

    Heme group.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi436 – 4361Iron (heme axial ligand)

    GO - Molecular functioni

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

    GO - Biological processi

    1. drug metabolic process Source: RGD
    2. response to calcium ion Source: RGD
    3. response to drug Source: RGD
    4. response to insulin Source: RGD
    5. response to metal ion Source: RGD
    6. response to organic cyclic compound Source: RGD
    7. response to sulfur dioxide Source: RGD

    Keywords - Molecular functioni

    Monooxygenase, Oxidoreductase

    Keywords - Ligandi

    Heme, Iron, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cytochrome P450 2B1 (EC:1.14.14.1)
    Alternative name(s):
    CYPIIB1
    Cytochrome P450-B
    Short name:
    Cytochrome P450b
    Cytochrome P450-LM2
    Cytochrome P450-PB1
    Cytochrome P450-PB2
    Gene namesi
    Name:Cyp2b1
    Synonyms:Cyp2b-1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi2466. Cyp2b1.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    2. intracellular membrane-bounded organelle Source: RGD

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane, Microsome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 491491Cytochrome P450 2B1PRO_0000051678Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei128 – 1281Phosphoserine; by PKA1 Publication

    Post-translational modificationi

    Phosphorylation is accompanied by a decrease in enzyme activity.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP00176.
    PRIDEiP00176.

    PTM databases

    PhosphoSiteiP00176.

    Expressioni

    Inductioni

    By phenobarbital.

    Gene expression databases

    GenevestigatoriP00176.

    Interactioni

    Structurei

    3D structure databases

    ProteinModelPortaliP00176.
    SMRiP00176. Positions 28-491.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the cytochrome P450 family.Curated

    Phylogenomic databases

    eggNOGiCOG2124.
    HOGENOMiHOG000036992.
    HOVERGENiHBG015789.
    PhylomeDBiP00176.

    Family and domain databases

    Gene3Di1.10.630.10. 1 hit.
    InterProiIPR001128. Cyt_P450.
    IPR017972. Cyt_P450_CS.
    IPR002401. Cyt_P450_E_grp-I.
    IPR008068. Cyt_P450_E_grp-I_CYP2B-like.
    [Graphical view]
    PfamiPF00067. p450. 1 hit.
    [Graphical view]
    PRINTSiPR00463. EP450I.
    PR01685. EP450ICYP2B.
    PR00385. P450.
    SUPFAMiSSF48264. SSF48264. 1 hit.
    PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P00176-1 [UniParc]FASTAAdd to Basket

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    MEPTILLLLA LLVGFLLLLV RGHPKSRGNF PPGPRPLPLL GNLLQLDRGG    50
    LLNSFMQLRE KYGDVFTVHL GPRPVVMLCG TDTIKEALVG QAEDFSGRGT 100
    IAVIEPIFKE YGVIFANGER WKALRRFSLA TMRDFGMGKR SVEERIQEEA 150
    QCLVEELRKS QGAPLDPTFL FQCITANIIC SIVFGERFDY TDRQFLRLLE 200
    LFYRTFSLLS SFSSQVFEFF SGFLKYFPGA HRQISKNLQE ILDYIGHIVE 250
    KHRATLDPSA PRDFIDTYLL RMEKEKSNHH TEFHHENLMI SLLSLFFAGT 300
    ETSSTTLRYG FLLMLKYPHV AEKVQKEIDQ VIGSHRLPTL DDRSKMPYTD 350
    AVIHEIQRFS DLVPIGVPHR VTKDTMFRGY LLPKNTEVYP ILSSALHDPQ 400
    YFDHPDSFNP EHFLDANGAL KKSEAFMPFS TGKRICLGEG IARNELFLFF 450
    TTILQNFSVS SHLAPKDIDL TPKESGIGKI PPTYQICFSA R 491
    Length:491
    Mass (Da):55,934
    Last modified:July 21, 1986 - v1
    Checksum:i74615501AD5497DD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti4 – 41T → S(PubMed:2989270)Curated
    Sequence conflicti4 – 41T → S AA sequence (PubMed:2539047)Curated
    Sequence conflicti92 – 921A → P in AAA41046. (PubMed:2989270)Curated
    Sequence conflicti161 – 1611Q → E AA sequence (PubMed:2539047)Curated
    Sequence conflicti205 – 2051T → R in AAA41046. (PubMed:2989270)Curated
    Sequence conflicti328 – 3281I → V in AAA41046. (PubMed:2989270)Curated
    Sequence conflicti357 – 3571Q → H in AAA41046. (PubMed:2989270)Curated
    Sequence conflicti392 – 3921L → R in AAA41046. (PubMed:2989270)Curated
    Sequence conflicti416 – 4161A → V in AAA41046. (PubMed:2989270)Curated
    Sequence conflicti434 – 4341R → H in AAA41046. (PubMed:2989270)Curated
    Sequence conflicti473 – 4731K → M no nucleotide entry (PubMed:6306654)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti303 – 3031S → G in isozyme PB2.
    Natural varianti321 – 3222AE → TV in isozyme PB2.
    Natural varianti337 – 3371L → P in isozyme PB2.
    Natural varianti339 – 3391T → S in isozyme PB2.
    Natural varianti344 – 3441S → T in isozyme PB2.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L00320
    , L00313, L00314, L00315, L00316, L00317, L00318, L00319, M11251 Genomic DNA. Translation: AAA41046.1.
    J00719 mRNA. Translation: AAA41024.1.
    M37134 mRNA. Translation: AAC42028.1.
    PIRiA00176. O4RTPB.
    A21162. O4RTP2.
    UniGeneiRn.228579.

    Genome annotation databases

    UCSCiRGD:2466. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L00320
    , L00313 , L00314 , L00315 , L00316 , L00317 , L00318 , L00319 , M11251 Genomic DNA. Translation: AAA41046.1 .
    J00719 mRNA. Translation: AAA41024.1 .
    M37134 mRNA. Translation: AAC42028.1 .
    PIRi A00176. O4RTPB.
    A21162. O4RTP2.
    UniGenei Rn.228579.

    3D structure databases

    ProteinModelPortali P00176.
    SMRi P00176. Positions 28-491.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi P00176.
    ChEMBLi CHEMBL3335.

    PTM databases

    PhosphoSitei P00176.

    Proteomic databases

    PaxDbi P00176.
    PRIDEi P00176.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    UCSCi RGD:2466. rat.

    Organism-specific databases

    RGDi 2466. Cyp2b1.

    Phylogenomic databases

    eggNOGi COG2124.
    HOGENOMi HOG000036992.
    HOVERGENi HBG015789.
    PhylomeDBi P00176.

    Gene expression databases

    Genevestigatori P00176.

    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.
    IPR008068. Cyt_P450_E_grp-I_CYP2B-like.
    [Graphical view ]
    Pfami PF00067. p450. 1 hit.
    [Graphical view ]
    PRINTSi PR00463. EP450I.
    PR01685. EP450ICYP2B.
    PR00385. P450.
    SUPFAMi SSF48264. SSF48264. 1 hit.
    PROSITEi PS00086. CYTOCHROME_P450. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Gene structure of a phenobarbital-inducible cytochrome P-450 in rat liver."
      Mizukami Y., Sogawa K., Suwa Y., Muramatsu M., Fujii-Kuriyama Y.
      Proc. Natl. Acad. Sci. U.S.A. 80:3958-3962(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Gene structure of a major form of phenobarbital-inducible cytochrome P-450 in rat liver."
      Suwa Y., Mizukami Y., Sogawa K., Fujii-Kuriyama Y.
      J. Biol. Chem. 260:7980-7984(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Primary structure of a cytochrome P-450: coding nucleotide sequence of phenobarbital-inducible cytochrome P-450 cDNA from rat liver."
      Fujii-Kuriyama Y., Mizukami Y., Kawajiri K., Sogawa K., Muramatsu M.
      Proc. Natl. Acad. Sci. U.S.A. 79:2793-2797(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-491 (ISOZYMES PB1 AND PB2).
    4. Fujii-Kuriyama Y., Mizukami Y., Kawajiri K., Sogawa K., Muramatsu M.
      Proc. Natl. Acad. Sci. U.S.A. 79:5443-5443(1982)
      Cited for: SEQUENCE REVISION TO 166; 292 AND 378 (ISOZYMES PB1 AND PB2).
    5. "Antibodies targeted against hypervariable and constant regions of cytochromes P450IIB1 and P450IIB2."
      Oesch F., Waxman D.J., Morrissey J.J., Honscha W., Kissel W., Friedberg T.
      Arch. Biochem. Biophys. 270:23-32(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-18; 146-165; 329-379 AND 401-423.
    6. "Amino acid compositions and partial amino acid sequences of three highly purified forms of liver microsomal cytochrome P-450 from rats treated with polychlorinated biphenyls, phenobarbital, or 3-methylcholanthrene."
      Botelho L.H., Ryan D.E., Levin W.
      J. Biol. Chem. 254:5635-5640(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-22.
    7. "Identification of active-site peptides from 3H-labeled 2-ethynylnaphthalene-inactivated P450 2B1 and 2B4 using amino acid sequencing and mass spectrometry."
      Roberts E.S., Hopkins N.E., Zaluzec E.J., Gage D.A., Alworth W.L., Hollenberg P.F.
      Biochemistry 33:3766-3771(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 273-283 AND 290-301.
    8. "Phosphorylation of hepatic phenobarbital-inducible cytochrome P-450."
      Pyerin W., Taniguchi H.
      EMBO J. 8:3003-3010(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-128.

    Entry informationi

    Entry nameiCP2B1_RAT
    AccessioniPrimary (citable) accession number: P00176
    Secondary accession number(s): Q64584
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 127 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