CP1A1_PLAFE
ID CP1A1_PLAFE Reviewed; 521 AA.
AC Q9YH64;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Cytochrome P450 1A1;
DE EC=1.14.14.1;
DE AltName: Full=CYPIA1;
GN Name=cyp1a1; Synonyms=cyp1a;
OS Platichthys flesus (European flounder) (Pleuronectes flesus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Pleuronectidae;
OC Platichthys.
OX NCBI_TaxID=8260;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=North Sea population; TISSUE=Liver;
RX PubMed=11460673; DOI=10.1016/s0141-1136(00)00053-2;
RA Williams T.D., Lee J.S., Sheader D.L., Chipman J.K.;
RT "The cytochrome P450 1A gene (CYP1A) from European flounder (Platichthys
RT flesus), analysis of regulatory regions and development of a dual
RT luciferase reporter gene system.";
RL Mar. Environ. Res. 50:1-6(2000).
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; AJ132353; CAA10645.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9YH64; -.
DR SMR; Q9YH64; -.
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 3: Inferred from homology;
KW Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW Monooxygenase; Oxidoreductase.
FT CHAIN 1..521
FT /note="Cytochrome P450 1A1"
FT /id="PRO_0000051636"
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; 59009 MW; 58BA7DC3913C9091 CRC64;
MMLMMLPFIG SVSVSESLVA MTTMCLVYLI LKFFQTEIPE GLLRLPGPKP LPIIGNVLGL
GSKPYLSLTD MSKRYGHVFQ IQIGMRPVVV LSGSETVRQA LIKQGDDFAG RPDLYSFRFI
NAGKSLAFST DQAGVWRARR KLAYSALRSF SNLEGTTPEY SCVLEEHICK EGEYLIKQLN
TVMKADGSFD PFRHIVVSVA NVICGMCFGR RYDHDDQELV GLVTLSDEFG RVVGSGNPAD
FIPILQYLPS AAMKNFLRIN SRFTEFVQKI VTEHYTTFDK 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