CP1A1_DICLA
ID CP1A1_DICLA Reviewed; 520 AA.
AC P79716;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, 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 Dicentrarchus labrax (European seabass) (Morone labrax).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Moronidae; Dicentrarchus.
OX NCBI_TaxID=13489;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=9972466; DOI=10.1016/s0742-8413(98)10045-2;
RA Stien X., Amichot M., Berge J.-B., Lafaurie M.;
RT "Molecular cloning of a CYP1A cDNA from the teleost fish Dicentrarchus
RT labrax.";
RL Comp. Biochem. Physiol. 121C:241-248(1998).
CC -!- FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases.
CC In liver microsomes, this enzyme is involved in an NADPH-dependent
CC electron transport pathway. It oxidizes a variety of structurally
CC unrelated compounds, including 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; U78316; AAB36951.1; -; mRNA.
DR AlphaFoldDB; P79716; -.
DR SMR; P79716; -.
DR Proteomes; UP000694389; 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 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; Reference proteome.
FT CHAIN 1..520
FT /note="Cytochrome P450 1A1"
FT /id="PRO_0000051635"
FT BINDING 230
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 464
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 520 AA; 58744 MW; 86761584B28E57FB CRC64;
MVLMILPFIG SVSVSESLVA LTTVCLVYLI LKFFRTEIPE GLHRLPGPKP LPLIGNVLEV
GNKPYLSLTA MSKRYGDVFR FRLGMRPSGC LSGSETVRKA LIKQGDEFAG RPDLYSFRFI
NDGKSLAFST DKAGVWRALR KLAYSALRSF SSLEESTPRD SCVLEEHSAK EGEYLYSNML
NAVMKVTGSF DPFRHIVVSV ANVICGMCFG RRYGHNDQEL LSLVNLSDPF GQVVGSGNPA
DFIPVLQFLP STTMKNFMDI NARFNKFVQK IVSEHYTTYD KDNIRDITDS LIDHCEDRKL
DENANVQMSD EKIVGIVNDL FGAGFDTIST ALSWSVMYLV AYPEIEERLY QELKENVGLD
RTPLLCDRPN LPFLEAFILE IFRHSSFLPF TIPHCTSKDT SLNGYFIPKD TCVFINQWQI
NHDPELWKDP SSFNPDRFLS ADGTELNKLE GEKVMVFGLG KRRCIGEVIA RNGVFLFLAI
IVQKLHFKTL PGEPLDMTPE YGLTMKHKRC HLRATMRASE