CP1A1_PLEPL
ID CP1A1_PLEPL Reviewed; 521 AA.
AC Q92100;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Cytochrome P450 1A1;
DE EC=1.14.14.1;
DE AltName: Full=CYPIA1;
GN Name=cyp1a1;
OS Pleuronectes platessa (European plaice).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Pleuronectidae;
OC Pleuronectes.
OX NCBI_TaxID=8262;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=8193668;
RA Leaver M.J., Pirrit L., George S.G.;
RT "Cytochrome P450 1A1 cDNA from plaice (Pleuronectes platessa) and induction
RT of P450 1A1 mRNA in various tissues by 3-methylcholanthrene and
RT isosafrole.";
RL Mol. Mar. Biol. Biotechnol. 2:338-345(1993).
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 -!- INDUCTION: By 3-methylcholanthrene (3MC) and isosafrole (ISF).
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X73631; CAA52010.1; -; mRNA.
DR PIR; S34184; S34184.
DR AlphaFoldDB; Q92100; -.
DR SMR; Q92100; -.
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_0000051646"
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; 59061 MW; AA7A97CB4578F9E6 CRC64;
MMLMMLPFIG SVSVSESLVA MTTMCLVYLI LKFFQTEIPE GLRRLPGPKP LPIIGNVLGL
GSKPYLSLTA MSKRYGHVFQ IQIGMRPVVV LSGTGTVRQA LIKQGDEFAG RPDLYSFRFI
NAGKSLAFST DQAGVWRARR KLAYSALRSF STLEGTTPEY SCVLEEHICK EGEYLIKQLN
TVMKADGSFD PFRHIVVSVA NVICGMCFGR RYDHDDQELV SLVTLSDEFG RVVGSGNPAD
FIPILQYLPS AEMKNFLRIN EHFTEFVQKI VTEHYTTFNK DNIRDITDSL IDHCEDRKLD
ENSNVQMSDE KIVGIVNDLF GAGFDTVSTA LSWSVMYLVA HPEIQERLYQ EIEDKVGLDR
MPLLSDKPNL PFLEAFILEI LRHSSFLPFT IPHCTTKDTS LNGYFIPKDT CVFINQWQIN
HDPELWKDPS SFNPDRFLSA DGSEVNKLDG EKVMAFGMGK RRCIGEVIAR NEVYLFLAII
IQKLHFLPIP GEKLDMTPEY GLTMKHKRCH LKATMRARNE H