ID   CP1A1_CHEAU             Reviewed;         521 AA.
AC   O42231;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 96.
DE   RecName: Full=Cytochrome P450 1A1;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIA1;
GN   Name=cyp1a1;
OS   Chelon auratus (Golden grey mullet) (Liza aurata).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Mugilomorphae; Mugilidae; Chelon.
OX   NCBI_TaxID=48191;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RA   Cousinou M., Lopez-Barea J., Dorado G.;
RL   Submitted (SEP-1997) 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; AF022433; AAB70307.1; -; mRNA.
DR   AlphaFoldDB; O42231; -.
DR   SMR; O42231; -.
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_0000051638"
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;  59064 MW;  CD23195E40228DBE CRC64;
     MALMILPFIG ALSVSESLVA LVTVCLVYLI IKSFQANIPE GLSRLPGPKP LPIIGNVLEV
     GSRPYLSLTE MSKRYGNVFQ IQIGMRPVVV LSGNETVRQA LIKQGDEFAG RPDLYSFRFI
     SEGKSLAFST DQAGVWRARR KLAYSALRSF STLEGTTPEY SCVLEEHISK EAEYLIKQLD
     TVMKADGSFD PFRYIVVSVA NVICGMCFGR RYDHHDRELL SLVNLSDEFG QVVGSGNPAD
     FIPILQYLPN KTMKKFVNIN DRFISFVQKI VSEHYATFNK DNIRDITDSL IDHCEDRKLD
     ENANVQMSDE KVVGIVNDLF GAGLDTISTA LSWSVMYLVA YPEIQERLYQ ELKENVGLDR
     TPVLSDRNNL PLLEAFILEI FRHSSFLPFT IPHCTTKDTS LNGYYIPKDT CVFINQWQIN
     HDPELWKEPS SFNPDRFLSA DGTEVNKVDG EKVMVFGLGK RRCIGEVIAR NEVYMFLAIL
     IQKLHFYNLP GEPLDMTPEY GLTMKHKRCH LRATVRVRSD H
//