ID   CP1A1_MICTO             Reviewed;         515 AA.
AC   Q92148;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 64.
DE   RecName: Full=Cytochrome P450 1A1;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIA1;
GN   Name=cyp1a1;
OS   Microgadus tomcod (Atlantic tomcod).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Paracanthopterygii; Gadiformes; Gadidae; Microgadus.
OX   NCBI_TaxID=34823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=Hudson river; TISSUE=Liver;
RX   MEDLINE=96004797; PubMed=7574676; DOI=10.1006/abbi.1995.1453;
RA   Roy N.K., Kreamer G.L., Konkle B., Grunwald C., Wirgin I.;
RT   "Characterization and prevalence of a polymorphism in the 3'
RT   untranslated region of cytochrome P4501A1 in cancer-prone Atlantic
RT   tomcod.";
RL   Arch. Biochem. Biophys. 322:204-213(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8807670;
RA   Roy N.K., Konkle B., Wirgin I.;
RT   "Characterization of CYP1A1 gene regulatory elements in cancer-prone
RT   Atlantic tomcod.";
RL   Pharmacogenetics 6:273-277(1996).
CC   -!- FUNCTION: Cytochromes P450 are a group of heme-thiolate
CC       monooxygenases. They oxidize a variety of structurally unrelated
CC       compounds, including steroids, fatty 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 benzo[a]pyrene (B[A]P) and beta-naphthoflavone
CC       (beta-NF).
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
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DR   EMBL; L41917; AAB00085.1; -; Genomic_DNA.
DR   EMBL; L41886; AAB00082.1; -; mRNA.
DR   PIR; S66464; S66464.
DR   HSSP; P00179; 1DT6.
DR   HOVERGEN; Q92148; -.
DR   BRENDA; 1.14.14.1; 292506.
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; 2.
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    515       Cytochrome P450 1A1.
FT                                /FTId=PRO_0000051640.
FT   METAL       459    459       Iron (heme axial ligand) (By similarity).
SQ   SEQUENCE   515 AA;  57826 MW;  CB73707629A01C25 CRC64;
     MALMILPLIG SVSVSETLVA MITVCMIYML MKFLHPDVPE APPAPGPQAL PIIGNVWSWE
     NGLPEPHGHG QRYGDILQIQ IGMRSVVVLS GHETVRQALI KQGHDLRPPD LYSFQFINDG
     KSLAFSTDQA GVWSPPKAGH ECPALLFHAR GHHAAVLLHV GGACLQGGRL PRQAAVQRHG
     TDASFDPFRH IVVSVANVIC GMCFGRRYGH EDQELLSLVN LTDEFGKVVG SGNLADFIPL
     LRFLPNATMK RFMAINERFM TFVQKIVTEH YNTYDKDNIR DITDSLIDHC EDRKLDENSN
     IQMSDEKIVG IVNDLFGAGF DTVSTALSWS VMYLVAHPEI QERLHQEIKD KVGLSRSPVL
     TDRHNLPILE AFIFEIFRHS SFLPFTIPHC ATKDTSLDGY FIPKDTCVFI NQWQINHDPE
     LWKEPSTFNP DRFLSADASE LNKLAGEKVM LFGMGKRRCI GEMVARNEVF LFLAILVQRL
     TFHAVPGEPL DMTPEYGLTM KHKRCHLRAT VRTTE
//