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P00185

- CP1A1_RAT

UniProt

P00185 - CP1A1_RAT

Protein

Cytochrome P450 1A1

Gene

Cyp1a1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (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
    Binding sitei228 – 2281SubstrateBy similarity
    Metal bindingi461 – 4611Iron (heme axial ligand)

    GO - Molecular functioni

    1. aromatase activity Source: UniProtKB-EC
    2. catalytic activity Source: RGD
    3. demethylase activity Source: RGD
    4. enzyme binding Source: RGD
    5. flavonoid 3'-monooxygenase activity Source: RGD
    6. heme binding Source: InterPro
    7. iron ion binding Source: InterPro
    8. monooxygenase activity Source: RGD
    9. oxidoreductase activity Source: RGD
    10. oxidoreductase activity, acting on diphenols and related substances as donors Source: RGD
    11. protein binding Source: RGD
    12. steroid hydroxylase activity Source: RGD
    13. vitamin D 24-hydroxylase activity Source: Ensembl

    GO - Biological processi

    1. 9-cis-retinoic acid biosynthetic process Source: RGD
    2. aging Source: RGD
    3. amine metabolic process Source: Ensembl
    4. camera-type eye development Source: RGD
    5. cell proliferation Source: RGD
    6. coumarin metabolic process Source: RGD
    7. demethylation Source: GOC
    8. developmental process Source: RGD
    9. dibenzo-p-dioxin catabolic process Source: RGD
    10. dibenzo-p-dioxin metabolic process Source: RGD
    11. digestive tract development Source: RGD
    12. drug metabolic process Source: Ensembl
    13. embryo development ending in birth or egg hatching Source: RGD
    14. flavonoid metabolic process Source: RGD
    15. hepatocyte differentiation Source: RGD
    16. hydrogen peroxide biosynthetic process Source: Ensembl
    17. insecticide metabolic process Source: RGD
    18. liver development Source: RGD
    19. maternal process involved in parturition Source: RGD
    20. porphyrin-containing compound metabolic process Source: RGD
    21. positive regulation of G1/S transition of mitotic cell cycle Source: RGD
    22. response to antibiotic Source: RGD
    23. response to arsenic-containing substance Source: RGD
    24. response to drug Source: RGD
    25. response to food Source: RGD
    26. response to herbicide Source: RGD
    27. response to hyperoxia Source: RGD
    28. response to hypoxia Source: RGD
    29. response to immobilization stress Source: RGD
    30. response to iron(III) ion Source: RGD
    31. response to lipopolysaccharide Source: RGD
    32. response to nematode Source: RGD
    33. response to organic cyclic compound Source: RGD
    34. response to organic substance Source: RGD
    35. response to virus Source: RGD
    36. response to vitamin A Source: RGD
    37. response to wounding Source: RGD

    Keywords - Molecular functioni

    Monooxygenase, Oxidoreductase

    Keywords - Ligandi

    Heme, Iron, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_196408. PPARA activates gene expression.
    REACT_198836. Synthesis of (16-20)-hydroxyeicosatetraenoic acids (HETE).
    REACT_198844. Synthesis of epoxy (EET) and dihydroxyeicosatrienoic acids (DHET).
    SABIO-RKP00185.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cytochrome P450 1A1 (EC:1.14.14.1)
    Short name:
    CYP1A1
    Alternative name(s):
    CYPIA1
    Cytochrome P450-C
    Cytochrome P450MT2
    Cleaved into the following 2 chains:
    Gene namesi
    Name:Cyp1a1
    Synonyms:Cyp1a-1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 8

    Organism-specific databases

    RGDi2458. Cyp1a1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: RGD
    2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    3. intracellular membrane-bounded organelle Source: RGD
    4. mitochondrial membrane Source: UniProtKB-SubCell
    5. mitochondrion Source: RGD

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum, Membrane, Microsome, Mitochondrion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi32 – 332VT → AI: No proteolytic cleavage. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini2 – 524523Cytochrome P450 1A1PRO_0000003564Add
    BLAST
    Chaini5 – 524520Cytochrome P450MT2APRO_0000003565Add
    BLAST
    Chaini33 – 524492Cytochrome P450MT2BPRO_0000003566Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi71 – 711O-linked (GlcNAc)1 Publication

    Post-translational modificationi

    Two forms; MT2A (long form) and MT2B (short form); are produced by NH2-terminal proteolytic cleavage. This cleavage activates a cryptic mitochondrial targeting signal.

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiP00185.
    PRIDEiP00185.

    Expressioni

    Tissue specificityi

    Liver.

    Inductioni

    By 3-methylcholanthrene (3MC) and beta-naphthoflavone (BNF).

    Gene expression databases

    GenevestigatoriP00185.

    Interactioni

    Protein-protein interaction databases

    BioGridi246477. 2 interactions.
    STRINGi10116.ENSRNOP00000026473.

    Structurei

    3D structure databases

    ProteinModelPortaliP00185.
    SMRiP00185. Positions 37-513.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni33 – 4412Mitochondrial targeting signalAdd
    BLAST

    Domaini

    Contains a chimeric signal that facilitates targeting of the protein to both the endoplasmic reticulum and mitochondria. A 12 amino acid sequence between 33 and 44 functions as a putative mitochondrial-targeting signal. The removal of the first 4- or 32-amino acid residues from the intact protein positions the mitochondrial targeting signal for efficient binding to the mitochondrial import receptors. The membrane-free P4501A1 seems to be more sensitive to proteolysis.

    Sequence similaritiesi

    Belongs to the cytochrome P450 family.Curated

    Phylogenomic databases

    eggNOGiCOG2124.
    GeneTreeiENSGT00750000117317.
    HOVERGENiHBG106944.
    InParanoidiP00185.
    KOiK07408.
    OMAiKVITIVF.
    OrthoDBiEOG7RBZ85.
    PhylomeDBiP00185.
    TreeFamiTF105095.

    Family and domain databases

    Gene3Di1.10.630.10. 1 hit.
    InterProiIPR001128. Cyt_P450.
    IPR017972. Cyt_P450_CS.
    IPR002401. Cyt_P450_E_grp-I.
    IPR008066. Cyt_P450_E_grp-I_CYP1.
    [Graphical view]
    PfamiPF00067. p450. 1 hit.
    [Graphical view]
    PRINTSiPR00463. EP450I.
    PR01683. EP450ICYP1A.
    PR00385. P450.
    SUPFAMiSSF48264. SSF48264. 1 hit.
    PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P00185-1 [UniParc]FASTAAdd to Basket

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    MPSVYGFPAF TSATELLLAV TTFCLGFWVV RVTRTWVPKG LKSPPGPWGL    50
    PFIGHVLTLG KNPHLSLTKL SQQYGDVLQI RIGSTPVVVL SGLNTIKQAL 100
    VKQGDDFKGR PDLYSFTLIA NGQSMTFNPD SGPLWAARRR LAQNALKSFS 150
    IASDPTLASS CYLEEHVSKE AEYLISKFQK LMAEVGHFDP FKYLVVSVAN 200
    VICAICFGRR YDHDDQELLS IVNLSNEFGE VTGSGYPADF IPILRYLPNS 250
    SLDAFKDLNK KFYSFMKKLI KEHYRTFEKG HIRDITDSLI EHCQDRRLDE 300
    NANVQLSDDK VITIVFDLFG AGFDTITTAI SWSLMYLVTN PRIQRKIQEE 350
    LDTVIGRDRQ PRLSDRPQLP YLEAFILETF RHSSFVPFTI PHSTIRDTSL 400
    NGFYIPKGHC VFVNQWQVNH DQELWGDPNE FRPERFLTSS GTLDKHLSEK 450
    VILFGLGKRK CIGETIGRLE VFLFLAILLQ QMEFNVSPGE KVDMTPAYGL 500
    TLKHARCEHF QVQMRSSGPQ HLQA 524
    Length:524
    Mass (Da):59,393
    Last modified:July 21, 1986 - v1
    Checksum:iC766DF8044D598C5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti21 – 222TT → VV AA sequence (PubMed:3041969)Curated
    Sequence conflicti53 – 531I → M in CAA25153. (PubMed:6324135)Curated
    Sequence conflicti494 – 4941M → S in AAA41025. (PubMed:3838427)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K02246 Genomic DNA. Translation: AAA41027.1.
    X00469 mRNA. Translation: CAA25153.1.
    M26129 Genomic DNA. Translation: AAA41025.1.
    PIRiA00185. O4RTMC.
    RefSeqiNP_036672.2. NM_012540.2.
    XP_006243212.1. XM_006243150.1.
    UniGeneiRn.10352.

    Genome annotation databases

    EnsembliENSRNOT00000026473; ENSRNOP00000026473; ENSRNOG00000019500.
    GeneIDi24296.
    KEGGirno:24296.
    UCSCiRGD:2458. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    K02246 Genomic DNA. Translation: AAA41027.1 .
    X00469 mRNA. Translation: CAA25153.1 .
    M26129 Genomic DNA. Translation: AAA41025.1 .
    PIRi A00185. O4RTMC.
    RefSeqi NP_036672.2. NM_012540.2.
    XP_006243212.1. XM_006243150.1.
    UniGenei Rn.10352.

    3D structure databases

    ProteinModelPortali P00185.
    SMRi P00185. Positions 37-513.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 246477. 2 interactions.
    STRINGi 10116.ENSRNOP00000026473.

    Chemistry

    ChEMBLi CHEMBL2922.

    Proteomic databases

    PaxDbi P00185.
    PRIDEi P00185.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000026473 ; ENSRNOP00000026473 ; ENSRNOG00000019500 .
    GeneIDi 24296.
    KEGGi rno:24296.
    UCSCi RGD:2458. rat.

    Organism-specific databases

    CTDi 1543.
    RGDi 2458. Cyp1a1.

    Phylogenomic databases

    eggNOGi COG2124.
    GeneTreei ENSGT00750000117317.
    HOVERGENi HBG106944.
    InParanoidi P00185.
    KOi K07408.
    OMAi KVITIVF.
    OrthoDBi EOG7RBZ85.
    PhylomeDBi P00185.
    TreeFami TF105095.

    Enzyme and pathway databases

    Reactomei REACT_196408. PPARA activates gene expression.
    REACT_198836. Synthesis of (16-20)-hydroxyeicosatetraenoic acids (HETE).
    REACT_198844. Synthesis of epoxy (EET) and dihydroxyeicosatrienoic acids (DHET).
    SABIO-RK P00185.

    Miscellaneous databases

    NextBioi 602902.
    PROi P00185.

    Gene expression databases

    Genevestigatori P00185.

    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.
    IPR008066. Cyt_P450_E_grp-I_CYP1.
    [Graphical view ]
    Pfami PF00067. p450. 1 hit.
    [Graphical view ]
    PRINTSi PR00463. EP450I.
    PR01683. EP450ICYP1A.
    PR00385. P450.
    SUPFAMi SSF48264. SSF48264. 1 hit.
    PROSITEi PS00086. CYTOCHROME_P450. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Distinct organization of methylcholanthrene- and phenobarbital-inducible cytochrome P-450 genes in the rat."
      Sogawa K., Gotoh O., Kawajiri K., Fujii-Kuriyama Y.
      Proc. Natl. Acad. Sci. U.S.A. 81:5066-5070(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Nucleotide sequence of a full-length cDNA coding for 3-methylcholanthrene-induced rat liver cytochrome P-450MC."
      Yabusaki Y., Shimizu M., Murakami H., Nakamura K., Oeda K., Ohkawa H.
      Nucleic Acids Res. 12:2929-2938(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "Amino-terminal sequence and structure of monoclonal antibody immunopurified cytochromes P-450."
      Cheng K.C., Park S.S., Krutzsch H.C., Grantham P.H., Gelboin H.V., Friedman F.K.
      Biochemistry 25:2397-2402(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-26.
    5. "Effect of nutritional imbalances on cytochrome P-450 isozymes in rat liver."
      Amelizad Z., Narbonne J.F., Wolf C.R., Robertson L.W., Oesch F.
      Biochem. Pharmacol. 37:3245-3249(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-22.
    6. "Identification and characterization of cytochrome P4501A1 amino acid residues interacting with a radiolabeled photoaffinity diazido-benzphetamine analogue."
      Cvrk T., Hodek P., Strobel H.W.
      Arch. Biochem. Biophys. 330:142-152(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE.
    7. "Targeting of NH2-terminal-processed microsomal protein to mitochondria: a novel pathway for the biogenesis of hepatic mitochondrial P450MT2."
      Addya S., Anandatheerthavarada H.K., Biswas G., Bhagwat S.V., Mullick J., Avadhani N.G.
      J. Cell Biol. 139:589-599(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF 32-VAL-THR-33.
      Strain: Sprague-Dawley.
      Tissue: Liver.
    8. "Discovery and confirmation of O-GlcNAcylated proteins in rat liver mitochondria by combination of mass spectrometry and immunological methods."
      Cao W., Cao J., Huang J., Yao J., Yan G., Xu H., Yang P.
      PLoS ONE 8:E76399-E76399(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT SER-71.

    Entry informationi

    Entry nameiCP1A1_RAT
    AccessioniPrimary (citable) accession number: P00185
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 139 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