ID   CP1A2_MOUSE             Reviewed;         513 AA.
AC   P00186; Q9QWJ4;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   05-MAY-2009, entry version 95.
DE   RecName: Full=Cytochrome P450 1A2;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIA2;
DE   AltName: Full=P450-P2/P450-P3;
GN   Name=Cyp1a2; Synonyms=Cyp1a-2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (P3).
RC   STRAIN=C57BL/6N;
RX   MEDLINE=84289486; PubMed=6547952;
RA   Kimura S., Gonzalez F.J., Nebert D.W.;
RT   "The murine Ah locus. Comparison of the complete cytochrome P1-450 and
RT   P3-450 cDNA nucleotide and amino acid sequences.";
RL   J. Biol. Chem. 259:10705-10713(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (P3).
RC   STRAIN=C57BL/6N;
RX   MEDLINE=84169582; PubMed=6324134; DOI=10.1093/nar/12.6.2917;
RA   Kimura S., Gonzalez F.J., Nebert D.W.;
RT   "Mouse cytochrome P3-450: complete cDNA and amino acid sequence.";
RL   Nucleic Acids Res. 12:2917-2928(1984).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (P3).
RX   MEDLINE=85182627; PubMed=3988744;
RA   Gonzalez F.J., Kimura S., Nebert D.W.;
RT   "Comparison of the flanking regions and introns of the mouse 2,3,7,8-
RT   tetrachlorodibenzo-p-dioxin-inducible cytochrome P1-450 and P3-450
RT   genes.";
RL   J. Biol. Chem. 260:5040-5049(1985).
RN   [4]
RP   ERRATUM.
RA   Gonzalez F.J., Kimura S., Nebert D.W.;
RL   J. Biol. Chem. 260:11884-11889(1985).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (P3).
RX   MEDLINE=85028449; PubMed=6548461; DOI=10.1016/0378-1119(84)90057-X;
RA   Gonzalez F.J., McKenzie P.I., Kimura S., Nebert D.W.;
RT   "Isolation and characterization of full-length mouse cDNA and genomic
RT   clones of 3-methylcholanthrene-inducible cytochrome P1-450 and P3-
RT   450.";
RL   Gene 29:281-292(1984).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] (P2).
RC   STRAIN=DBA/2N; TISSUE=Liver;
RX   MEDLINE=86312932; PubMed=3755821; DOI=10.1093/nar/14.16.6765;
RA   Kimura S., Nebert D.W.;
RT   "cDNA and complete amino acid sequence of mouse P2(450): allelic
RT   variant of mouse P3(450) gene.";
RL   Nucleic Acids Res. 14:6765-6766(1986).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (P3).
RC   TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   PROTEIN SEQUENCE OF 2-26.
RC   STRAIN=DBA/2;
RX   MEDLINE=86243357; PubMed=3718958; DOI=10.1021/bi00357a015;
RA   Cheng K.C., Park S.S., Krutzsch H.C., Grantham P.H., Gelboin H.V.,
RA   Friedman F.K.;
RT   "Amino-terminal sequence and structure of monoclonal antibody
RT   immunopurified cytochromes P-450.";
RL   Biochemistry 25:2397-2402(1986).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 277-315.
RX   MEDLINE=86269072; PubMed=2425809; DOI=10.1016/0006-2952(86)90577-0;
RA   Peterson T.C., Gonzalez F.J., Nebert D.W.;
RT   "Methylation differences in the murine P-1-450 and P-3-450 genes in
RT   wild-type and mutant hepatoma cell culture.";
RL   Biochem. Pharmacol. 35:2107-2114(1986).
RN   [10]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-288, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026;
RA   Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,
RA   Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
RT   "Substrate and functional diversity of lysine acetylation revealed by
RT   a proteomics survey.";
RL   Mol. Cell 23:607-618(2006).
CC   -!- FUNCTION: Cytochromes P450 are a group of heme-thiolate
CC       monooxygenases. In liver microsomes, this enzyme is involved in an
CC       NADPH-dependent electron transport pathway. It oxidizes a variety
CC       of structurally unrelated compounds, including steroids, fatty
CC       acids, and xenobiotics. Most active in catalyzing 2-hydroxylation
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: RH + reduced flavoprotein + O(2) = ROH +
CC       oxidized flavoprotein + H(2)O.
CC   -!- COFACTOR: Heme group (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
CC       membrane protein. Microsome membrane; Peripheral membrane protein.
CC   -!- INDUCTION: By 3-methylcholanthrene (3MC).
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
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DR   EMBL; X01682; CAA25837.1; -; Genomic_DNA.
DR   EMBL; X00479; CAA25156.1; -; mRNA.
DR   EMBL; X04283; CAA27832.1; -; mRNA.
DR   EMBL; K02589; AAA37509.1; ALT_SEQ; mRNA.
DR   EMBL; M10022; AAA37508.1; -; Genomic_DNA.
DR   EMBL; BC018298; AAH18298.1; -; mRNA.
DR   EMBL; BC054827; AAH54827.1; -; mRNA.
DR   IPI; IPI00128287; -.
DR   PIR; B92495; O4MSM3.
DR   RefSeq; NP_034123.1; -.
DR   UniGene; Mm.15537; -.
DR   HSSP; P00179; 1DT6.
DR   SMR; P00186; 33-512.
DR   PhosphoSite; P00186; -.
DR   PRIDE; P00186; -.
DR   Ensembl; ENSMUSG00000032310; Mus musculus.
DR   GeneID; 13077; -.
DR   KEGG; mmu:13077; -.
DR   MGI; MGI:88589; Cyp1a2.
DR   HOGENOM; P00186; -.
DR   HOVERGEN; P00186; -.
DR   OMA; P00186; KQWKDPF.
DR   BRENDA; 1.14.14.1; 244.
DR   NextBio; 283024; -.
DR   ArrayExpress; P00186; -.
DR   Bgee; P00186; -.
DR   GermOnline; ENSMUSG00000032310; Mus musculus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005792; C:microsome; IDA:MGI.
DR   GO; GO:0070330; F:aromatase activity; IEA:EC.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0045333; P:cellular respiration; IMP:MGI.
DR   GO; GO:0018894; P:dibenzo-p-dioxin metabolic process; IMP:MGI.
DR   GO; GO:0017144; P:drug metabolic process; IMP:MGI.
DR   GO; GO:0050665; P:hydrogen peroxide biosynthetic process; IMP:MGI.
DR   GO; GO:0030324; P:lung development; IMP:MGI.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006778; P:porphyrin metabolic process; IMP:MGI.
DR   GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR   GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR   GO; GO:0009404; P:toxin metabolic process; IMP:MGI.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017973; Cyt_P450_C.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR008066; Cyt_P450_E_grp-I_CYP1.
DR   Gene3D; G3DSA:1.10.630.10; Cyt_P450; 1.
DR   PANTHER; PTHR19383; Cyt_P450; 1.
DR   PANTHER; PTHR19383:SF63; Cyt_P450_E_grp-I_CYP1; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR01683; EP450ICYP1A.
DR   PRINTS; PR00385; P450.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Endoplasmic reticulum; Heme;
KW   Iron; Membrane; Metal-binding; Microsome; Monooxygenase;
KW   Oxidoreductase; Polymorphism.
FT   CHAIN         1    513       Cytochrome P450 1A2.
FT                                /FTId=PRO_0000051654.
FT   METAL       456    456       Iron (heme axial ligand).
FT   MOD_RES     288    288       N6-acetyllysine.
FT   VARIANT     384    384       I -> M (in P2).
SQ   SEQUENCE   513 AA;  58184 MW;  DC2D7D976B126E3B CRC64;
     MAFSQYISLA PELLLATAIF CLVFWMVRAS RTQVPKGLKN PPGPWGLPFI GHMLTVGKNP
     HLSLTRLSQQ YGDVLQIRIG STPVVVLSGL NTIKQALVRQ GDDFKGRPDL YSFTLITNGK
     SMTFNPDSGP VWAARRRLAQ DALKSFSIAS DPTSASSCYL EEHVSKEANH LVSKLQKAMA
     EVGHFEPVSQ VVESVANVIG AMCFGKNFPR KSEEMLNIVN NSKDFVENVT SGNAVDFFPV
     LRYLPNPALK RFKTFNDNFV LFLQKTVQEH YQDFNKNSIQ DITSALFKHS ENYKDNGGLI
     PEEKIVNIVN DIFGAGFDTV TTAITWSILL LVTWPNVQRK IHEELDTVVG RDRQPRLSDR
     PQLPYLEAFI LEIYRYTSFV PFTIPHSTTR DTSLNGFHIP KERCIYINQW QVNHDEKQWK
     DPFVFRPERF LTNNNSAIDK TQSEKVMLFG LGKRRCIGEI PAKWEVFLFL AILLQHLEFS
     VPPGVKVDLT PNYGLTMKPG TCEHVQAWPR FSK
//