ID   CP1A1_CHACA             Reviewed;         521 AA.
AC   Q92039;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Cytochrome P450 1A1;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIA1;
GN   Name=cyp1a1; Synonyms=cyp1a;
OS   Chaetodon capistratus (Four-eye butterflyfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Chaetodontiformes; Chaetodontidae; Chaetodon.
OX   NCBI_TaxID=37949;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RA   Vrolijk N.H., Lin C., Chen T.T.;
RT   "Characterization and expression of a CYP1A gene from the tropical teleost,
RT   Chaetodon capistratus.";
RL   Submitted (APR-1995) 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; U19855; AAA62123.1; -; mRNA.
DR   AlphaFoldDB; Q92039; -.
DR   SMR; Q92039; -.
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_0000051634"
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;  58653 MW;  45FFA98CC37BE919 CRC64;
     MALMILPFIG SVSVSESLVA LTAVCLVYLI LKFFRTEIPA GLRQLPGPKP LPIIGNVLEV
     GSKPHLSLTA MSKRYGDVFQ IQIGMRPVVV LSGSETVRQA LIKQGDEFSG RPDLYSFTFI
     NDGKSLAFST DQAGVCGACR KLAYSALRSF STLDGTTPEY SCMLEEHICK EGECLINQLN
     TVMKADGSFD PFRHIVVSVA NVICGMCFGR RYDHNDQDLL RLVNLSDEFG QVAGSGNPAD
     FINILRFLPS TTMKKFMTIN ADFNTFVKKI VGEHYATFDK NNIRDITDSL IDHCEDRKLD
     ENCNVQMSDE KIVGIVNDLF GAGFDTVSTA LSWSVMYLVA YPDIQERLFQ EIKDNVGLDR
     TPLLSDRSKV PYLEAFILEL FRHSSFLPFT IPHCSAKDTS LNGYFIPKDT CVFINQWQIN
     RDPELWKDPS SFNPDRFLSC NGTEVNKQEG EKVMVFGMGK RRCIGEVIAR NEVYRGLAIL
     IQRLQFHEMP GELLDMTPEY GLTMKHKRCH LRATMRARNE Q