ID   CP1A1_LIMLI             Reviewed;         521 AA.
AC   O42430;
DT   30-MAY-2000, 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   Limanda limanda (Common dab) (Pleuronectes limanda).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Pleuronectiformes; Pleuronectoidei; Pleuronectidae; Limanda.
OX   NCBI_TaxID=27771;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=11423384; DOI=10.1016/s1532-0456(01)00188-0;
RA   Craft J.A., Robertson F.E., McPhail M.E., Brown E., Stagg R.M.;
RT   "Measurement of cytochrome P4501A induction in dab (Limanda limanda) and
RT   other teleosts with species-specific cDNA probes: isolation and
RT   characterisation of dab cDNA and its use in expression studies with beta-
RT   naphthoflavone-treated fish.";
RL   Comp. Biochem. Physiol. 129C:115-127(2001).
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; AJ001724; CAA04953.1; -; mRNA.
DR   AlphaFoldDB; O42430; -.
DR   SMR; O42430; -.
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_0000051637"
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;  59063 MW;  11DE326C8A7FBDF9 CRC64;
     MMLMMLPFIG SVSVSESLVA MTTVCLVYLI LKFFQTEIPE GLRRLPGPKP LPIIGNVLEM
     GSRPYLSLTA MSKRYGNVFQ IQIGMRPVVV LSGSETVRQA LIKQGDDFAG RPDLYSFRFI
     NEGKSLAFST DKAGIWRARR KLAYSALRSF ATLEGTTPEY SCVLEEHVCK EGEYLIKQLN
     TAMTADGSFD PFRHIVVSVA NVICGMCFGR RYDHDDQELV GLVTLSDEFG RVVGSGNPAD
     FIPILQYLPS ATMKNFLRIN GRFTEFVQKI VTEHYTTFDK DNIRDITDSL IDHCEDRKLD
     ENSNVQMSDE KIVGIVNDLF GAGFDTVSTA LSWSVMYLVA HPEIQERLYQ EIEDKVGLDR
     MPLLSDKPNL PFLEAFILEI LRHSSFLPFT IPHCTTKDTS LNGYFIPKDT CVFINQWQIN
     HDPEMWKDPS SFNPDRFLSA DGSEVNKLDG EKVMAFGMGK RRCIGEVIAR NEVYLFLAIL
     IQKLHFLPIP GEKLDMTPEY GLTMKHKRCH LKATMRARNE H
//