CP1A1_OPSTA
ID CP1A1_OPSTA Reviewed; 521 AA.
AC Q92095;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, 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;
OS Opsanus tau (Oyster toadfish) (Gadus tau).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Batrachoidaria; Batrachoididae; Opsanus.
OX NCBI_TaxID=8068;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=7755595; DOI=10.1042/bj3080097;
RA Morrison H.G., Oleksiak M.F., Cornell N.W., Sogin M.L., Stegeman J.J.;
RT "Identification of cytochrome P-450 1A (CYP1A) genes from two teleost fish,
RT toadfish (Opsanus tau) and scup (Stenotomus chrysops), and phylogenetic
RT analysis of CYP1A genes.";
RL Biochem. J. 308:97-104(1995).
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; U14161; AAA74968.1; -; mRNA.
DR PIR; S55317; S55317.
DR AlphaFoldDB; Q92095; -.
DR SMR; Q92095; -.
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_0000051643"
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; 59247 MW; 4F73866C793FD3F3 CRC64;
MALIILPFIG SLSVSESLVA LITICVVYLI LTYSHTKIPA GLQRLPGPKP LPIIGNVLEI
GRKPYQTLTA LSKRYGPVFQ IQIGMRPVVV LSGSETVRQA LIKQGEDFSG RPDLYTFQFI
SDGKSLAFST DKVGVWRARR KLAYSALRSF SSLESTNQEY SCMLEEHICK EGEYLVKQLN
TSMKANGSFD PFRNIVVSVA NVICGMCFGR RYDHYDQELV SLVNLSEEFG QVVGTGNLAD
FIPVLRFLPS TAMKKFLSIN DRFDKFVKKI VSEHYATYNK DNIRDITDSL IDHCEDRKLD
ENCNVQVSDE KIVGIVNDLF GAGFDTVSTG LSWSVMYLVA YPEIQERLYQ EIKDSVGTER
MPLLSDRPSL PFLDAFILEI FRHSSFLPFT IPHCTTKNTS LNGYFIPKDT CVFINQWQIN
HDPELWKDPF SFNPERFLSA DGTELNRLEG EKVMLFGLGK RRCIGEVIAR NEVFLFLAII
IQRLQFHMLP GEPLDMTPEY GLTMKHKRCQ LRATMREKNE Q