ID   CP1A1_STECH             Reviewed;         521 AA.
AC   Q92116;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Cytochrome P450 1A1;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIA1;
GN   Name=cyp1a1;
OS   Stenotomus chrysops (Scup) (Sparus chrysops).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Spariformes; Sparidae; Stenotomus.
OX   NCBI_TaxID=35579;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=7755595; DOI=10.1042/bj3080097;
RA   Morrison H.G., Oleksiak M.F., Cornell N.W., Sogin M.L., Stegeman J.J.;
RT   "Identification of cytochrome P-450 1A (CYP1A) genes from two teleost fish,
RT   toadfish (Opsanus tau) and scup (Stenotomus chrysops), and phylogenetic
RT   analysis of CYP1A genes.";
RL   Biochem. J. 308:97-104(1995).
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; U14162; AAA74969.1; -; mRNA.
DR   PIR; S55318; S55318.
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..521
FT                   /note="Cytochrome P450 1A1"
FT                   /id="PRO_0000051648"
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;  59020 MW;  8BDC4312074025D4 CRC64;
     MVLMILPVIG SVSVSEGLVA MITMCLAYLI LRLFRTEIPE GLLQLPGPKP LPIIGNVLEV
     GRNPYLSLTA MSKRYGDVFQ IQIGMRPVVV LSGSETVRQA LIKQGDXFAG RPDLYSFRFI
     NDGKSLAFST DQAGVWRARR KLAYSALRSF ATLEGTTPEY SCALEEHVSK EAEYLVKQLH
     TVMEADGSFD PFRHIVVSVA NVICGMCFGR RYDHNHQELL NLVNLSDEFG QVVASGNPAD
     FIPILQYLPS TTMKKFLNIN DRFNTFVQKI VSEHYTTFDK DNIRDITDSL IDHCEDRKLD
     ENSNVQMSDE KIVGIVNDLF GAGFDTISTA LSWSVMYLVA YPEIQERLYQ EMNETVGPDR
     TPCLSDKPKL PFLEAFILET FRHSSFLPFT IPHCTSKDTS LNGYFIPKDT CVFINQWQIN
     HDAELWKDPS SFNPDRFLNA DGTEVNKLEG EKMMVFGMGK RRCIGEVIAR SEVFLFLAIL
     VQNLRFHSMP GEPLDMTPEY GLTMKHKRCQ LRAAMRARNE E