CP1A1_CHESA
ID CP1A1_CHESA Reviewed; 521 AA.
AC Q9W683;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Cytochrome P450 1A1;
DE EC=1.14.14.1;
DE AltName: Full=CYPIA1;
GN Name=cyp1a1;
OS Chelon saliens (Leaping mullet) (Liza saliens).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Mugilomorphae; Mugilidae; Chelon.
OX NCBI_TaxID=48192;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Sen A., Buhler D.R., Wang-Buhler J.-L.;
RT "Cloning and sequencing of mullet (Liza saliens) liver cytochrome P450
RT 1A1.";
RL Submitted (JUN-1998) 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; AF072899; AAD22398.1; -; mRNA.
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_0000051639"
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; 58944 MW; 1C5DBF224A73C6A0 CRC64;
MALMILPFIG ALSVSESLVA VVTVCLVYLI IKSFQDKIPE GLSRLPGPKP LPIIGNVLEV
GSRPYLSLTE MGKRYGNVFQ IQIGMRPVVV LSGNETVRQA LIKQGDEFAG RPDLYSFRFI
SEGKSLAFST DQAGVWRARR KLAYSALRSF STLEGTTPEY SCVLEEHISK EAKYLIQQLD
TVMKADGSFD PFRYIVVSVA NVICGMCFGR RYDHHDQELL SLVNLSDEFG QVVGSGNPAD
FIPILQYLPN KTMKKFVSIN DRFISFVQKI VSEHYATFNK DNIRDITDSL IDHCEDRKLD
ENANVQMSDE KVVGIVNDLF GAGFDTISTA LSWSVMYLVA YPEIQEXLYQ ELKENVGLDR
TPVLSDRNNL PLLESFILEI FRHSSFLPFT IPHCTTKDTS LNGYYIPKDT CVFINQWQIN
HDPELWKEPS SFNPDRFLSA DGTEVNKVDG EKVMIFGMGK RRCIGEVIAR NEVYLFLAIL
IQKLHFCNLP GEPLDMTPEY GLTMKHKRCQ LRATARVRSD H