CP1A3_ONCMY
ID CP1A3_ONCMY Reviewed; 522 AA.
AC Q92109; P10609; P79829;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Cytochrome P450 1A3;
DE Short=CYP1A3;
DE EC=1.14.14.1;
DE AltName: Full=CYP1A1;
GN Name=cyp1a3;
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.
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].
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 cDNA. Its C-terminal part has been shown to be derived from what is now known as the CYP1A1. CYP1A3 has also been called CYP1A1.; Evidence={ECO:0000305};
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DR EMBL; S69277; AAD14035.1; -; Genomic_DNA.
DR EMBL; U62796; AAB40626.1; -; mRNA.
DR EMBL; M21310; AAA49550.1; ALT_SEQ; mRNA.
DR AlphaFoldDB; Q92109; -.
DR SMR; Q92109; -.
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:0003824; F:catalytic activity; IDA:AgBase.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:1903165; P:response to polycyclic arene; IDA:AgBase.
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 1A3"
FT /id="PRO_0000051642"
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 57
FT /note="M -> V (in Ref. 1; AAD14035/AAA49550)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="N -> S (in Ref. 1; AAD14035/AAA49550)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="S -> P (in Ref. 1; AAD14035/AAA49550)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="T -> S (in Ref. 1; AAD14035)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="L -> C (in Ref. 1; AAD14035/AAA49550)"
FT /evidence="ECO:0000305"
FT CONFLICT 265
FT /note="N -> T (in Ref. 1; AAD14035/AAA49550)"
FT /evidence="ECO:0000305"
FT CONFLICT 276
FT /note="E -> D (in Ref. 1; AAD14035)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="I -> V (in Ref. 1; AAD14035)"
FT /evidence="ECO:0000305"
FT CONFLICT 344
FT /note="T -> I (in Ref. 1; AAD14035/AAA49550)"
FT /evidence="ECO:0000305"
FT CONFLICT 396
FT /note="I -> V (in Ref. 1; AAD14035)"
FT /evidence="ECO:0000305"
FT CONFLICT 485
FT /note="R -> C (in Ref. 1; AAD14035)"
FT /evidence="ECO:0000305"
FT CONFLICT 515..522
FT /note="MRPWGQEE -> LRHGGRKSEGHGHIYDSQHHYN (in Ref. 1;
FT AAD14035)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 522 AA; 59273 MW; 0E83F2A5EEFE3202 CRC64;
MVLMILPIIG SVSASEGLVA MVTLCLVYMI MKYMHTEIPE GLKRLPGPKP LPIIGNMLEV
HNNPHLSLTA MSERYGSVFQ IQIGMRPVVV LSGNETVRQA LIKQGEDFAG RSDLYSFKFI
NDGKSLAFST DKAGVWRARR KLAMSALRSF ATLEGTTPEY SCALEEHVLK EGEYLVKQLT
SVMDVSGSFD PFRHIVVSVA NVICGMCFGR RYSHDDQELL GLVNMSDEFG QVVGSGNPAD
FIPILRYLPN RTMKRFMDIN DRFNNFVQKI VSEHYESYDK DNIRDITDSL IDHCEDRKLD
ENANIQVSDE KIVGIVNDLF GAGFDTISTA LSWAVVYLVA YPETQERLHQ ELKEKVGMIR
TPRLSDKINL PLLEAFILEI FRHSSFLPFT IPHCTIKDTS LNGYFIPKDT CVFINQWQVN
HDPELWKEPS SFNPDRFLSA DGTELNKLEG EKVLVFGMGK RRCIGEAIGR NEVYLFLAIL
LQRLRFQEKP GHPLDMTPEY GLTMKHKRCQ LKASMRPWGQ EE
