ID   CP1A1_CHESA             Reviewed;         521 AA.
AC   Q9W683;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   RecName: Full=Cytochrome P450 1A1;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIA1;
GN   Name=cyp1a1;
OS   Chelon saliens (Leaping mullet) (Liza saliens).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Mugilomorphae; Mugilidae; Chelon.
OX   NCBI_TaxID=48192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RA   Sen A., Buhler D.R., Wang-Buhler J.-L.;
RT   "Cloning and sequencing of mullet (Liza saliens) liver cytochrome P450
RT   1A1.";
RL   Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AF072899; AAD22398.1; -; mRNA.
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   CDD; cd20676; CYP1A; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 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   PANTHER; PTHR24289:SF18; CYTOCHROME P450 1A2; 1.
DR   PANTHER; PTHR24289; STEROID 17-ALPHA-HYDROXYLASE/17,20 LYASE; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR01683; EP450ICYP1A.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; Cytochrome P450; 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..521
FT                   /note="Cytochrome P450 1A1"
FT                   /id="PRO_0000051639"
FT   BINDING         229
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         463
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   521 AA;  58944 MW;  1C5DBF224A73C6A0 CRC64;
     MALMILPFIG ALSVSESLVA VVTVCLVYLI IKSFQDKIPE GLSRLPGPKP LPIIGNVLEV
     GSRPYLSLTE MGKRYGNVFQ IQIGMRPVVV LSGNETVRQA LIKQGDEFAG RPDLYSFRFI
     SEGKSLAFST DQAGVWRARR KLAYSALRSF STLEGTTPEY SCVLEEHISK EAKYLIQQLD
     TVMKADGSFD PFRYIVVSVA NVICGMCFGR RYDHHDQELL SLVNLSDEFG QVVGSGNPAD
     FIPILQYLPN KTMKKFVSIN DRFISFVQKI VSEHYATFNK DNIRDITDSL IDHCEDRKLD
     ENANVQMSDE KVVGIVNDLF GAGFDTISTA LSWSVMYLVA YPEIQEXLYQ ELKENVGLDR
     TPVLSDRNNL PLLESFILEI FRHSSFLPFT IPHCTTKDTS LNGYYIPKDT CVFINQWQIN
     HDPELWKEPS SFNPDRFLSA DGTEVNKVDG EKVMIFGMGK RRCIGEVIAR NEVYLFLAIL
     IQKLHFCNLP GEPLDMTPEY GLTMKHKRCQ LRATARVRSD H
//