ID   CP1A1_SPAAU             Reviewed;         521 AA.
AC   O42457; O42458;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 106.
DE   RecName: Full=Cytochrome P450 1A1;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIA1;
GN   Name=cyp1a1;
OS   Sparus aurata (Gilthead sea bream).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Spariformes; Sparidae; Sparus.
OX   NCBI_TaxID=8175;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RA   Cousinou M., Lopez-Barea J., Dorado G.;
RL   Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 175-521.
RC   TISSUE=Liver;
RA   Tom M.;
RL   Submitted (MAY-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; AF011223; AAB64297.1; -; mRNA.
DR   EMBL; AF005719; AAB62887.1; -; mRNA.
DR   AlphaFoldDB; O42457; -.
DR   SMR; O42457; -.
DR   Ensembl; ENSSAUT00010060013.1; ENSSAUP00010057154.1; ENSSAUG00010023400.1.
DR   GeneTree; ENSGT00950000183037; -.
DR   InParanoid; O42457; -.
DR   OMA; DPRAYWQ; -.
DR   OrthoDB; 2900138at2759; -.
DR   Proteomes; UP000472265; Unplaced.
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   GO; GO:0006725; P:cellular aromatic compound metabolic process; IEA:Ensembl.
DR   GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl.
DR   GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEA:Ensembl.
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; Reference proteome.
FT   CHAIN           1..521
FT                   /note="Cytochrome P450 1A1"
FT                   /id="PRO_0000051647"
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"
FT   CONFLICT        175..177
FT                   /note="LVK -> GTR (in Ref. 2; AAB62887)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        209
FT                   /note="G -> A (in Ref. 2; AAB62887)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        212
FT                   /note="Y -> S (in Ref. 2; AAB62887)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   521 AA;  59122 MW;  8FE00D86460B303B CRC64;
     MVLMILPFVG PVSVSESLVA IITMCLVYMI LKFFRTEIPE GLCQLPGPKP LPIIGNVLEV
     GRNPYLSLTA MSKRYGDVFQ IQIGMRPVVV LSGSETVRQA LIKQGDDFAG RPDLYSFRFI
     NDGKSLAFST DQAGVWRARR KLAYSALRSF STLEGTTPEY SCALEEHVSK EAEYLVKQLN
     TVMETDGSFD PFRHIVVSVA NVICGMCFGR RYDHNNQELL NLVNLSDEFG QVVASGNPAD
     FIPILQYLPS TSMKKFVSIN DRFNAFVQKI VSEHYTTFDK DNIRDITDSL IDHCEDRKLD
     ENSNVQMSDE KVVGIVNDLF GAGFDTISTA LSWSVMYLVA YPEIQERLYQ EMKESVGLDR
     TPCLSDKPKL PFLEAFILEI FRHSSFLPFT IPHCSSKDTS LNGYFIPKDT CVFINQWQIN
     HDPELWKDPS SFNPDRFLNT DGTELNKLEG EKMMVFGLGK RRCIGEVIAR NEVFLFLAIL
     VQNLRFHAKP GEPLDMTPEY GLTMKHKRCH LRAAMRSRNE E
//