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Protein

Cytochrome P450 1B1

Gene

Cyp1b1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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, retinoid and xenobiotics. Preferentially oxidizes 17beta-estradiol to the carcinogenic 4-hydroxy derivative, and a variety of procarcinogenic compounds to their activated forms, including polycyclic aromatic hydrocarbons. Promotes angiogenesis by removing cellular oxygenation products, thereby decreasing oxidative stress, release of antiangiogenic factor THBS2, then allowing endothelial cells migration, cell adhesion and capillary morphogenesis. These changes are concommitant with the endothelial nitric oxide synthase activity and nitric oxide synthesis. Plays an important role in the regulation of perivascular cell proliferation, migration, and survival through modulation of the intracellular oxidative state and NF-kappa-B expression and/or activity, during angiogenesis. Contributes to oxidative homeostasis and ultrastructural organization and function of trabecular meshwork tissue through modulation of POSTN expression.6 Publications

Catalytic activityi

RH + [reduced NADPH--hemoprotein reductase] + O2 = ROH + [oxidized NADPH--hemoprotein reductase] + H2O.

Cofactori

hemeBy similarity

Enzyme regulationi

Activated by 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD). Inhibited by 12-O-Tetradecanoylphorbol-13-acetate and PRKCB.1 Publication

Kineticsi

kcat is 0.04 min(-1) for retinol, 0.08 min(-1) for retinal, 1.24 min(-1) for 7,12-dimethyltetraphene, 0.13 min(-1) for arachidonic acid.

  1. KM=392.2 µM for retinol1 Publication
  2. KM=153.9 µM for retinal1 Publication
  3. KM=138.9 µM for 7,12-dimethyltetraphene1 Publication
  4. KM=500.0 µM for arachidonic acid1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Metal bindingi470Iron (heme axial ligand)By similarity1

    GO - Molecular functioni

    GO - Biological processi

    • angiogenesis Source: MGI
    • arachidonic acid metabolic process Source: UniProtKB
    • blood vessel morphogenesis Source: UniProtKB
    • cell adhesion Source: UniProtKB
    • cellular aromatic compound metabolic process Source: MGI
    • cellular response to hydrogen peroxide Source: UniProtKB
    • cellular response to organic cyclic compound Source: MGI
    • collagen fibril organization Source: UniProtKB
    • endothelial cell-cell adhesion Source: MGI
    • endothelial cell migration Source: UniProtKB
    • estrogen metabolic process Source: UniProtKB
    • intrinsic apoptotic signaling pathway in response to oxidative stress Source: UniProtKB
    • membrane lipid catabolic process Source: UniProtKB
    • negative regulation of cell adhesion mediated by integrin Source: UniProtKB
    • negative regulation of cell migration Source: UniProtKB
    • negative regulation of cell proliferation Source: UniProtKB
    • negative regulation of NF-kappaB transcription factor activity Source: UniProtKB
    • nitric oxide biosynthetic process Source: UniProtKB
    • positive regulation of angiogenesis Source: UniProtKB
    • positive regulation of apoptotic process Source: UniProtKB
    • positive regulation of JAK-STAT cascade Source: UniProtKB
    • positive regulation of vascular endothelial growth factor production Source: UniProtKB
    • regulation of reactive oxygen species metabolic process Source: UniProtKB
    • response to toxic substance Source: MGI
    • retinal blood vessel morphogenesis Source: UniProtKB
    • retinal metabolic process Source: UniProtKB
    • retina vasculature development in camera-type eye Source: MGI
    • retinol metabolic process Source: UniProtKB
    • steroid metabolic process Source: UniProtKB
    • toxin metabolic process Source: MGI
    • trabecular meshwork development Source: UniProtKB
    • xenobiotic metabolic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Monooxygenase, Oxidoreductase

    Keywords - Ligandi

    Heme, Iron, Metal-binding

    Enzyme and pathway databases

    ReactomeiR-MMU-211976. Endogenous sterols.
    R-MMU-2142670. Synthesis of epoxy (EET) and dihydroxyeicosatrienoic acids (DHET).
    R-MMU-2142816. Synthesis of (16-20)-hydroxyeicosatetraenoic acids (HETE).

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cytochrome P450 1B1 (EC:1.14.14.1)
    Alternative name(s):
    CYPIB1
    Cytochrome P450CMEF
    Short name:
    Cytochrome P450EF
    Gene namesi
    Name:Cyp1b1
    Synonyms:Cyp1-b1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    Proteomesi
    • UP000000589 Componenti: Chromosome 17

    Organism-specific databases

    MGIiMGI:88590. Cyp1b1.

    Subcellular locationi

    GO - Cellular componenti

    • endoplasmic reticulum membrane Source: UniProtKB-SubCell
    • mitochondrion Source: UniProtKB
    • organelle membrane Source: UniProtKB-SubCell
    Complete GO annotation...

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane, Microsome, Mitochondrion

    Pathology & Biotechi

    Disruption phenotypei

    Severe ocular drainage structure abnormalities, significant elevated intraocular pressure.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000516611 – 543Cytochrome P450 1B1Add BLAST543

    Proteomic databases

    MaxQBiQ64429.
    PaxDbiQ64429.
    PRIDEiQ64429.

    PTM databases

    iPTMnetiQ64429.
    PhosphoSitePlusiQ64429.

    Expressioni

    Tissue specificityi

    Constitutively expressed in retinal, heart and kidney pericytes cells.1 Publication

    Inductioni

    By polycyclic aromatic hydrocarbons (PAH) and 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD).1 Publication

    Gene expression databases

    BgeeiENSMUSG00000024087.
    GenevisibleiQ64429. MM.

    Interactioni

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000024894.

    Structurei

    3D structure databases

    ProteinModelPortaliQ64429.
    SMRiQ64429.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the cytochrome P450 family.Curated

    Phylogenomic databases

    eggNOGiKOG0156. Eukaryota.
    COG2124. LUCA.
    GeneTreeiENSGT00760000118992.
    HOGENOMiHOG000036991.
    HOVERGENiHBG106944.
    InParanoidiQ64429.
    KOiK07410.
    OMAiSHLYFAR.
    OrthoDBiEOG091G0BT8.
    TreeFamiTF105095.

    Family and domain databases

    Gene3Di1.10.630.10. 1 hit.
    InterProiIPR032971. CYP1B1.
    IPR001128. Cyt_P450.
    IPR017972. Cyt_P450_CS.
    IPR002401. Cyt_P450_E_grp-I.
    [Graphical view]
    PANTHERiPTHR24299:SF0. PTHR24299:SF0. 1 hit.
    PfamiPF00067. p450. 1 hit.
    [Graphical view]
    PRINTSiPR00463. EP450I.
    PR00385. P450.
    SUPFAMiSSF48264. SSF48264. 1 hit.
    PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q64429-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MATSLSADSP QQLSSLSTQQ TTLLLLFSVL AAVHLGQWLL RQWQRKPWSS
    60 70 80 90 100
    PPGPFPWPLI GNAAAVGQAS HLYFARLARR YGDVFQIRLG SCPVVVLNGE
    110 120 130 140 150
    SAIHQALVQQ GSIFADRPPF ASFRVVSGGR SLAFGHYSEH WKTQRRSAYS
    160 170 180 190 200
    TMRAFSTRHP RSRGLLEGHA LAEARELVAV LVRRCAGGAF LDPTQPVIVA
    210 220 230 240 250
    VANVMSAVCF GCRYNHDDAE FLELLSHNEE FGRTVGAGSL VDVLPWLQLF
    260 270 280 290 300
    PNPVRTTFRK FEQLNRNFSN FVLDKFLRHR ESLVPGAAPR DMTDAFILSA
    310 320 330 340 350
    EKKASGAPGD DSSGLDLEDV PATITDIFGA SQDTLSTALL WLLILFTRYP
    360 370 380 390 400
    DVQARVQAEL DQVVGRDRLP CMSDQPNLPY VMAFLYESMR FSSFLPVTIP
    410 420 430 440 450
    HATTANTFVL GYYIPKNTVV FVNQWSVNHD PAKWPNPEDF DPARFLDKDG
    460 470 480 490 500
    FINKALASSV MIFSVGKRRC IGEELSKMLL FLFISILAHQ CNFKANQNES
    510 520 530 540
    SNMSFSYGLT IKPKSFRIHV SLRESMELLD NAVKKLQTEE GCK
    Length:543
    Mass (Da):60,537
    Last modified:July 27, 2011 - v3
    Checksum:i7C89B4312CB5BC4A
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti195Q → P in CAA55205 (PubMed:8195121).Curated1
    Sequence conflicti307A → D in CAA55205 (PubMed:8195121).Curated1
    Sequence conflicti328F → G in CAA55205 (PubMed:8195121).Curated1
    Sequence conflicti457A → T in CAA55205 (PubMed:8195121).Curated1
    Sequence conflicti516F → V in CAA55205 (PubMed:8195121).Curated1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U03283 mRNA. Translation: AAC52141.1.
    X78445 mRNA. Translation: CAA55205.1.
    AK137461 mRNA. Translation: BAE23362.1.
    CH466537 Genomic DNA. Translation: EDL38490.1.
    U02479 mRNA. Translation: AAC52131.1.
    CCDSiCCDS28986.1.
    PIRiA53790.
    RefSeqiNP_034124.1. NM_009994.1.
    UniGeneiMm.214016.

    Genome annotation databases

    EnsembliENSMUST00000024894; ENSMUSP00000024894; ENSMUSG00000024087.
    GeneIDi13078.
    KEGGimmu:13078.
    UCSCiuc008dqc.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U03283 mRNA. Translation: AAC52141.1.
    X78445 mRNA. Translation: CAA55205.1.
    AK137461 mRNA. Translation: BAE23362.1.
    CH466537 Genomic DNA. Translation: EDL38490.1.
    U02479 mRNA. Translation: AAC52131.1.
    CCDSiCCDS28986.1.
    PIRiA53790.
    RefSeqiNP_034124.1. NM_009994.1.
    UniGeneiMm.214016.

    3D structure databases

    ProteinModelPortaliQ64429.
    SMRiQ64429.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000024894.

    PTM databases

    iPTMnetiQ64429.
    PhosphoSitePlusiQ64429.

    Proteomic databases

    MaxQBiQ64429.
    PaxDbiQ64429.
    PRIDEiQ64429.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENSMUST00000024894; ENSMUSP00000024894; ENSMUSG00000024087.
    GeneIDi13078.
    KEGGimmu:13078.
    UCSCiuc008dqc.1. mouse.

    Organism-specific databases

    CTDi1545.
    MGIiMGI:88590. Cyp1b1.

    Phylogenomic databases

    eggNOGiKOG0156. Eukaryota.
    COG2124. LUCA.
    GeneTreeiENSGT00760000118992.
    HOGENOMiHOG000036991.
    HOVERGENiHBG106944.
    InParanoidiQ64429.
    KOiK07410.
    OMAiSHLYFAR.
    OrthoDBiEOG091G0BT8.
    TreeFamiTF105095.

    Enzyme and pathway databases

    ReactomeiR-MMU-211976. Endogenous sterols.
    R-MMU-2142670. Synthesis of epoxy (EET) and dihydroxyeicosatrienoic acids (DHET).
    R-MMU-2142816. Synthesis of (16-20)-hydroxyeicosatetraenoic acids (HETE).

    Miscellaneous databases

    PROiQ64429.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSMUSG00000024087.
    GenevisibleiQ64429. MM.

    Family and domain databases

    Gene3Di1.10.630.10. 1 hit.
    InterProiIPR032971. CYP1B1.
    IPR001128. Cyt_P450.
    IPR017972. Cyt_P450_CS.
    IPR002401. Cyt_P450_E_grp-I.
    [Graphical view]
    PANTHERiPTHR24299:SF0. PTHR24299:SF0. 1 hit.
    PfamiPF00067. p450. 1 hit.
    [Graphical view]
    PRINTSiPR00463. EP450I.
    PR00385. P450.
    SUPFAMiSSF48264. SSF48264. 1 hit.
    PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiCP1B1_MOUSE
    AccessioniPrimary (citable) accession number: Q64429
    Secondary accession number(s): Q3UVA8, Q60593, Q64461
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: July 27, 2011
    Last modified: November 2, 2016
    This is version 138 of the entry and version 3 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.