CP1A1_ONCMY
ID CP1A1_ONCMY Reviewed; 522 AA.
AC Q92110; O42195; P10609; P79830;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Cytochrome P450 1A1;
DE EC=1.14.14.1;
DE AltName: Full=CYP1A2;
DE AltName: Full=CYPIA1;
GN Name=cyp1a1;
OS Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Oncorhynchus.
OX NCBI_TaxID=8022;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=8161204; DOI=10.1006/abbi.1994.1156;
RA Berndtson A.K., Chen T.T.;
RT "Two unique CYP1 genes are expressed in response to 3-methylcholanthrene
RT treatment in rainbow trout.";
RL Arch. Biochem. Biophys. 310:187-195(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Bailey G., You L., Harttig U.;
RT "Cloning, sequencing and functional expression of two trout CYP1A cDNAs in
RT yeast.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Bailey G., You L., Harttig U.;
RT "Cloning, sequencing and aflatoxin B1 metabolism by multiple rainbow trout
RT CYP1A cDNAs expressed in yeast.";
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=3203599; DOI=10.1089/dna.1.1988.7.379;
RA Heilmann L.J., Sheen Y.-Y., Bigelow S.W., Nebert D.W.;
RT "Trout P450IA1: cDNA and deduced protein sequence, expression in liver, and
RT evolutionary significance.";
RL DNA 7:379-387(1988).
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 -!- TISSUE SPECIFICITY: Liver.
CC -!- INDUCTION: By 3-methylcholanthrene (3MC).
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA49550.1; Type=Miscellaneous discrepancy; Note=Chimera. Its N-terminal part has been shown to be derived from what is now known as the CYP1A3. CYP1A1 has also been called CYP1A2.; Evidence={ECO:0000305};
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DR EMBL; S69278; AAD14036.1; -; Genomic_DNA.
DR EMBL; U62797; AAB40627.1; -; mRNA.
DR EMBL; AF015660; AAB69383.1; -; mRNA.
DR EMBL; M21310; AAA49550.1; ALT_SEQ; mRNA.
DR PIR; A28789; A28789.
DR PIR; S51557; S51557.
DR AlphaFoldDB; Q92110; -.
DR SMR; Q92110; -.
DR ABCD; Q92110; 3 sequenced antibodies.
DR GO; GO:0009925; C:basal plasma membrane; IDA:AgBase.
DR GO; GO:0005737; C:cytoplasm; IDA:AgBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000792; C:heterochromatin; IDA:AgBase.
DR GO; GO:0031528; C:microvillus membrane; IDA:AgBase.
DR GO; GO:0031965; C:nuclear membrane; IDA:AgBase.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:AgBase.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IDA:AgBase.
DR GO; GO:0005790; C:smooth endoplasmic reticulum; IDA:AgBase.
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..522
FT /note="Cytochrome P450 1A1"
FT /id="PRO_0000051641"
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"
FT CONFLICT 51
FT /note="L -> P (in Ref. 3; AAB69383)"
FT /evidence="ECO:0000305"
FT CONFLICT 97
FT /note="V -> D (in Ref. 3; AAB69383)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="K -> N (in Ref. 3; AAB69383)"
FT /evidence="ECO:0000305"
FT CONFLICT 306
FT /note="Q -> H (in Ref. 3; AAB69383)"
FT /evidence="ECO:0000305"
FT CONFLICT 390
FT /note="T -> I (in Ref. 3; AAB69383)"
FT /evidence="ECO:0000305"
FT CONFLICT 459
FT /note="D -> G (in Ref. 2; AAB40627)"
FT /evidence="ECO:0000305"
FT CONFLICT 470
FT /note="R -> H (in Ref. 3; AAB69383)"
FT /evidence="ECO:0000305"
FT CONFLICT 474
FT /note="Y -> F (in Ref. 1; AAD14036/AAA49550)"
FT /evidence="ECO:0000305"
FT CONFLICT 483
FT /note="R -> K (in Ref. 2; AAB40627)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 522 AA; 59344 MW; 9D063B5891102CE9 CRC64;
MVLMILPIIG SVSVSEGLVA IVTLCLVYML MKYKHTEIPE GLKRLPGPKP LPIIGNVLEV
YNNPHLSLTA MSERYGSVFQ IQIGMRPVVV LSGNETVRQA LIKQGEDFAG RPDLYSFKFI
NDGKSLAFST DKAGVWRARR KLAMSALRSF ATLEGTTPEY SCALEEHVCK EGEYLVKQLT
SVMDVSGSFD PFRHIVVSVA NVICGMCFGR RYSHDDQELL GLVNMSDEFG QVVGSGNPAD
FIPILRYLPN RTMKRFMDIN DRFNNFVQKI VSEHYESYDK DNIRDITDSL IDHCEDRKLD
ENANIQVSDE KIVGIVNDLF GAGFDTISTA LSWAVVYLVA YPEIQERLHQ ELKEKVGMIR
TPRLSDKINL PLLEAFILEI FRHSSFLPFT IPHCTIKDTS LNGYFIPKDT CVFINQWQVN
HDPELWKEPS SFNPDRFLSA DGTELNKLEG EKVLVFGMDK RRCIGEAIGR NEVYLFLAIL
LQRLRFQEKP GHPLDMTPEY GLTMKHKRCQ LKASMRPWGQ EE
