ID   CP1A2_CALJA             Reviewed;         516 AA.
AC   O77810;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-JUN-2009, entry version 56.
DE   RecName: Full=Cytochrome P450 1A2;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIA2;
GN   Name=CYP1A2;
OS   Callithrix jacchus (Common marmoset).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Platyrrhini; Cebidae; Callitrichinae; Callithrix.
OX   NCBI_TaxID=9483;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   MEDLINE=98028640; PubMed=9364010; DOI=10.1093/carcin/18.10.1985;
RA   Sakuma T., Igarashi T., Hieda M., Ohgiya S., Isogai M., Ninomiya S.,
RA   Nagata R., Nemoto N., Kamataki T.;
RT   "Marmoset CYP1A2: primary structure and constitutive expression in
RT   livers.";
RL   Carcinogenesis 18:1985-1991(1997).
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 (By similarity). Microsome membrane; Peripheral
CC       membrane protein (By similarity).
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
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DR   EMBL; D86475; BAA33790.1; -; mRNA.
DR   HSSP; P00179; 1DT6.
DR   SMR; O77810; 34-514.
DR   HOVERGEN; O77810; -.
DR   BRENDA; 1.14.14.1; 265156.
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   2: Evidence at transcript 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_0000232907.
FT   METAL       458    458       Iron (heme axial ligand) (By similarity).
FT   MOD_RES     289    289       N6-acetyllysine (By similarity).
SQ   SEQUENCE   516 AA;  58407 MW;  E2186060C285D938 CRC64;
     MALSQFVPFS ATELLLTSTV FCLVFWVFKG LRPRVPKGLK SPPEPWRWPL LGHVLTLGKN
     PHLALTKMSQ RYGDVLQIHI GSTPVVVLSG LDTIRQALVR QGDDFKGRPD LYSFTLITDG
     QSMSFSPDSG PVWAARRRLA QNALNTFSIA SDPASSSSCY LEEHVSKEAE ALIGRLQELM
     AGPGRFDPYN QIVESVVKVI GAMCFGQHFP ESSDEMLSLM KNSHVFVENA TSGNPVDFFP
     ILRYLPNPAL QRFKAFNQRF LRFLRETVQE HYQDSDKNSV QDITGALFKH CEKRSGASGD
     LIPQEKIVNL VNDIFGAGFD TITTAISWSL MYLVTKPEIQ RKIQKELDTV IGRGRRPRLS
     DRPQLPYLEA FILETFRHSS FVPFTIPHST TRDTTLKGFY IPKECCVFIN QWQVNHDPQL
     WGDPSEFRPE RFLTAKGTAL NKPLSEKILL FGLGKRRCIG EVLGKWEVFL FLAILLQQLE
     FSVPPGVQID LTPTYGLTMK HARCEHVQAR LRFSFQ
//