ID   CP1A1_PAGMA             Reviewed;         515 AA.
AC   P98181;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Cytochrome P450 1A1;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIA1;
GN   Name=cyp1a1;
OS   Pagrus major (Red sea bream) (Chrysophrys major).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Spariformes; Sparidae; Pagrus.
OX   NCBI_TaxID=143350;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Liver;
RA   Mizukami Y., Okauchi M., Arizono K., Ariyoshi T., Kito H.;
RT   "Isolation and sequence of cDNA encoding a 3-methylcholanthrene-inducible
RT   cytochrome p450 from wild red sea bream, Pagrus major.";
RL   Mar. Biol. 120:343-349(1994).
CC   -!- FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases.
CC       They oxidize a variety of structurally unrelated compounds, including
CC       steroids, fatty acids, and xenobiotics.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein
CC         reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:30879, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:142491; EC=1.14.14.1;
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
CC       membrane protein. Microsome membrane; Peripheral membrane protein.
CC   -!- TISSUE SPECIFICITY: Expressed in induced liver, kidney, gill and gut.
CC       Weakly expressed in control liver.
CC   -!- INDUCTION: By 3-methylcholanthrene (3MC).
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   AlphaFoldDB; P98181; -.
DR   SMR; P98181; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR008066; Cyt_P450_E_grp-I_CYP1.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR01683; EP450ICYP1A.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
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
FT                   /note="Cytochrome P450 1A1"
FT                   /id="PRO_0000051645"
FT   BINDING         457
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   515 AA;  58541 MW;  D670A8F70826DA5B CRC64;
     MVLMILPFIG SVSVSESLVA MITMCLAYLI LKFFRTEIPE GLRELPGPKP LPIIGNVLEV
     GRNPYLSLTA MTAPRTDVFQ IQIGMRPVVV LSGNETVRQA LIKQGQEFAG RPDLYSFKFI
     NDGKSLAFST DGPAVWRARR KLAYSALRSF ATKEGTTPEY SVRLFEHVSK ERYAAISMFM
     KLMADFDPVR HIVVSVANVI CGMCFGRRYD HNNRSWLNLV NPRRDVRKVV ASGNPADFIP
     ILQYLPSTTM KKFLNINARF NEFVQKIVSE HYTTFNKDNI RDITDSLIDH CEDEPMDPMP
     DADDKIVGIV NDLFGAGFDT ISTALSWSVM YLVAYPEIQE RLYQEMETVM GPDRMPCLSD
     RTQLTLPEAF ILEIFRHSSF LPFTIPHCTT KDTSLNGYFI PKAPCIYIKQ WPVIHDDDDV
     LDPSSFNPDR FLKADGTEVN KLNGEKMMVF GMGKRRCIGE VIARNEVYLF LAILLVQLQF
     HAMPGEPLDM TPEYGLTMKH KRCHLRAAMR RGTEE