ID   CP1A1_MESAU             Reviewed;         524 AA.
AC   Q00557; Q64665;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   16-JUN-2009, entry version 59.
DE   RecName: Full=Cytochrome P450 1A1;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIA1;
DE   AltName: Full=P-450MC;
GN   Name=CYP1A1;
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Lung;
RX   MEDLINE=92138673; PubMed=1778988;
RA   Sagami I., Ohmachi T., Fujii H., Kikuchi H., Watanabe M.;
RT   "Hamster cytochrome P-450 IA gene family, P-450IA1 and P-450IA2 in
RT   lung and liver: cDNA cloning and sequence analysis.";
RL   J. Biochem. 110:641-647(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Ohgiya S., Goda T., Ishizaki K., Morimoto M., Sakamoto T.,
RA   Kamataki T., Shinriki N.;
RT   "Molecular cloning and expression of hamster cytochrome P450 1A1 and
RT   cytochrome P450 reductase.";
RL   Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases.
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   -!- INDUCTION: By 3-methylcholanthrene (3MC).
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
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DR   EMBL; D10251; BAA01096.1; -; mRNA.
DR   EMBL; D12977; BAA02354.1; -; mRNA.
DR   EMBL; D10913; BAA01717.1; -; Genomic_DNA.
DR   PIR; JX0189; JX0189.
DR   HSSP; P00179; 1DT6.
DR   HOVERGEN; Q00557; -.
DR   BRENDA; 1.14.14.1; 824.
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   Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW   Monooxygenase; Oxidoreductase.
FT   CHAIN         1    524       Cytochrome P450 1A1.
FT                                /FTId=PRO_0000051630.
FT   METAL       461    461       Iron (heme axial ligand) (By similarity).
FT   CONFLICT     18     18       L -> V (in Ref. 1; BAA01096).
FT   CONFLICT    521    521       H -> Y (in Ref. 1; BAA01096).
SQ   SEQUENCE   524 AA;  59136 MW;  2A4C6AF9AE5FD8E0 CRC64;
     MSSIYGLLNF MSATELLLAI TVFCLGFWVV RALRTQVPKG LKTPPGPWGL PILGHVLTLG
     KNPHLSLTKL SKQYGDVLQI RIGSTPVVVL SGLDTIRQAL VRQGDDFKGR PDFYSFTLIT
     NGKSMTFNPD CGPVWAARRR LAQDALKSFS IALDPASASS CYLEEYVIKE ADYLISKFQK
     LMAEVGHFDP DRYLVVSVTN VICAMCFGQR YDHDDQELLS IVNLSNEFGK VTGSGYPPDF
     IPILRYLPNS SLDAFKDLNK KFYSFMQKSV KEHYRTFEKG HIRDITDSLI EHCQDKSLDE
     NANVQLSDDR VINIIVDLFG AGFDTVTTAI SWSLMYLVTN PGVQRKIQEE LDTVIGRSRR
     PRLCDRSQLP YLEAFILETF RHSSFLPFTI PHSTTRDTSL CGFYIPKGHC VFVNQWQINH
     NQELWGDPNK FRPERFLTSS GTLDKVLSGK VTLFGLGKRK CIGETIGRLE VFLFLAILLQ
     QIEFTVSPGE KVDMTPIYGL TLKHARCEYF QAQTRSSGPQ HPQA
//