ID   CP1A2_MACFA             Reviewed;         516 AA.
AC   O77809;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-JUN-2009, entry version 54.
DE   RecName: Full=Cytochrome P450 1A2;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIA2;
GN   Name=CYP1A2;
OS   Macaca fascicularis (Crab eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, AND CHARACTERIZATION.
RC   TISSUE=Liver;
RX   MEDLINE=98361563; PubMed=9698097; DOI=10.1016/S0006-2952(98)00100-2;
RA   Sakuma T., Hieda M., Igarashi T., Ohgiya S., Nagata R., Nemoto N.,
RA   Kamataki T.;
RT   "Molecular cloning and functional analysis of cynomolgus monkey
RT   CYP1A2.";
RL   Biochem. Pharmacol. 56:131-139(1998).
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.
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   -!- TISSUE SPECIFICITY: Liver.
CC   -!- INDUCTION: By 3-methylcholanthrene (3MC).
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
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DR   EMBL; D86474; BAA33789.1; -; mRNA.
DR   HSSP; P00179; 1DT6.
DR   SMR; O77809; 34-514.
DR   HOVERGEN; O77809; -.
DR   BRENDA; 1.14.14.1; 3438.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005792; C:microsome; IEA:UniProtKB-SubCell.
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:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
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; Endoplasmic reticulum; Heme; Iron; Membrane;
KW   Metal-binding; Microsome; Monooxygenase; Oxidoreductase.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    516       Cytochrome P450 1A2.
FT                                /FTId=PRO_0000051652.
FT   METAL       458    458       Iron (heme axial ligand) (By similarity).
FT   MOD_RES     289    289       N6-acetyllysine (By similarity).
SQ   SEQUENCE   516 AA;  58197 MW;  3F71E3999EC4CDF7 CRC64;
     MALSQSVPFL ATELLLASAI FCLVFWVLRG SRPRVPKGLK SPPEPWGWPL LGHVLTLGKN
     PHLALSRMSQ LYGDVLQIRI GSTPVLVLSG LDTIRQALVR QGDDFKGRPD LYSFTFITDG
     QSMSFSPDSG PVWAARRRLA QNALNTFSIA SDPASSSSCY LEEHVSKEAE ALISRLQELM
     AGPGHFDPYN QVVVSVANVI GAMCFGQHFP ESSDEMLSLV KNSHEFVESA SSGNPVDFFP
     ILRYLPNPAL QRFKAFNQRF RRFLQKTVQE HYQDFDKNSV QDITGALFKH SKKGPRASGN
     LIPQEKIVNL VNDIFGAGFD TIATAISWSL MYLVTKPEIQ RKIQKELDAV IGRGRRPRLS
     DRPQLPYLEA FILETFRHSS FVPFTIPHST TRDTTLNGFY IPRECCVFIN QWQVNHDPQL
     WGDPSEFRPE RFLTAEGTTI NKPLSEKIML FGLGKRRCIG EVLGKWEVFL FLAILLQQLE
     FSVPPGVKVD LTPIYGLTMK HARCEHFQAR LRFSIK
//