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Cytochrome P450 2E1 (EC 1.14.13.-) (4-nitrophenol 2-hydroxylase) (EC 1.14.13.n7) (CYPIIE1) (Cytochrome P450-ALC) (Cytochrome P450-J)

 CP2E1_MOUSE             Reviewed;         493 AA.
Q05421; Q9Z198;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 1.
23-MAY-2018, entry version 164.
RecName: Full=Cytochrome P450 2E1;
EC=1.14.13.-;
AltName: Full=4-nitrophenol 2-hydroxylase;
EC=1.14.13.n7;
AltName: Full=CYPIIE1;
AltName: Full=Cytochrome P450-ALC;
AltName: Full=Cytochrome P450-J;
Name=Cyp2e1; Synonyms=Cyp2e, Cyp2e-1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6S; TISSUE=Liver;
PubMed=8344939;
Davis J.F., Felder M.R.;
"Mouse ethanol-inducible cytochrome P-450 (P450IIE1). Characterization
of cDNA clones and testosterone induction in kidney tissue.";
J. Biol. Chem. 268:16584-16589(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ; TISSUE=Liver;
PubMed=1536649; DOI=10.1042/bj2810689;
Freeman J.E., Stirling D., Russel A.L., Wolf C.R.;
"cDNA sequence, deduced amino acid sequence, predicted gene structure
and chemical regulation of mouse Cyp2e1.";
Biochem. J. 281:689-695(1992).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 455-493.
TISSUE=Liver;
PubMed=6851839;
Ivanov P.L., Ryskov A.P., Kramerov D.A., Georgiev G.P.;
"Primary structure of the repeating element B2 and of the adjoining
sequences in cloned mRNA actively transcribing in mouse liver cells.";
Dokl. Akad. Nauk SSSR 269:227-230(1983).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 455-493.
PubMed=6194512; DOI=10.1093/nar/11.18.6541;
Ryskov A.P., Ivanov P.L., Kramerov D.A., Georgiev G.P.;
"Mouse ubiquitous B2 repeat in polysomal and cytoplasmic poly(A)+RNAs:
unidirectional orientation and 3'-end localization.";
Nucleic Acids Res. 11:6541-6558(1983).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 455-493.
Ryskov A.P., Ivanov P.L., Kramerov D.A., Georgiev G.P.;
"Universal orientation and 3' terminal localization of repetitive
sequences of the B2 family in mRNA.";
Mol. Biol. (Mosk.) 18:74-83(1984).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney, and Liver;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Metabolizes several precarcinogens, drugs, and solvents
to reactive metabolites. {ECO:0000250}.
-!- CATALYTIC ACTIVITY: 4-nitrophenol + NADPH + O(2) = 4-nitrocatechol
+ NADP(+) + H(2)O.
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
membrane protein. Microsome membrane; Peripheral membrane protein.
-!- TISSUE SPECIFICITY: Highest level in the liver and to a lesser
extent in the kidney, with a higher level in the male kidney than
in the female.
-!- DEVELOPMENTAL STAGE: Detectable in the female liver on day 1 and
reaches steady state levels on days 16-20.
-!- INDUCTION: By ethanol and acetone in the liver and by testosterone
in the kidney and adrenal tissues.
-!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; L11650; AAA39879.1; -; mRNA.
EMBL; X62595; CAA44481.1; -; mRNA.
EMBL; BC013451; AAH13451.1; -; mRNA.
EMBL; M54877; AAA37275.1; -; mRNA.
EMBL; X01026; CAA25510.1; ALT_SEQ; mRNA.
CCDS; CCDS21985.1; -.
PIR; A47350; A47350.
PIR; S19657; A21231.
RefSeq; NP_067257.1; NM_021282.2.
UniGene; Mm.21758; -.
ProteinModelPortal; Q05421; -.
SMR; Q05421; -.
IntAct; Q05421; 2.
MINT; Q05421; -.
STRING; 10090.ENSMUSP00000026552; -.
iPTMnet; Q05421; -.
PhosphoSitePlus; Q05421; -.
SwissPalm; Q05421; -.
MaxQB; Q05421; -.
PaxDb; Q05421; -.
PeptideAtlas; Q05421; -.
PRIDE; Q05421; -.
Ensembl; ENSMUST00000026552; ENSMUSP00000026552; ENSMUSG00000025479.
GeneID; 13106; -.
KEGG; mmu:13106; -.
UCSC; uc009kic.1; mouse.
CTD; 1571; -.
MGI; MGI:88607; Cyp2e1.
eggNOG; KOG0156; Eukaryota.
eggNOG; COG2124; LUCA.
GeneTree; ENSGT00880000137861; -.
HOGENOM; HOG000036992; -.
HOVERGEN; HBG015789; -.
InParanoid; Q05421; -.
KO; K07415; -.
OMA; HEATQDT; -.
OrthoDB; EOG091G0BT8; -.
PhylomeDB; Q05421; -.
TreeFam; TF352043; -.
BioCyc; MetaCyc:MONOMER-12920; -.
Reactome; R-MMU-211981; Xenobiotics.
Reactome; R-MMU-211999; CYP2E1 reactions.
Reactome; R-MMU-9027307; Biosynthesis of maresin-like SPMs.
ChiTaRS; Cyp2e1; mouse.
PRO; PR:Q05421; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000025479; -.
ExpressionAtlas; Q05421; baseline and differential.
Genevisible; Q05421; MM.
GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
GO; GO:0000139; C:Golgi membrane; IEA:Ensembl.
GO; GO:0031227; C:intrinsic component of endoplasmic reticulum membrane; IEA:Ensembl.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0008392; F:arachidonic acid epoxygenase activity; IBA:GO_Central.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0020037; F:heme binding; ISS:UniProtKB.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0004497; F:monooxygenase activity; IDA:MGI.
GO; GO:0016491; F:oxidoreductase activity; ISO:MGI.
GO; GO:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen; IEA:Ensembl.
GO; GO:0008395; F:steroid hydroxylase activity; IBA:GO_Central.
GO; GO:0017144; P:drug metabolic process; ISO:MGI.
GO; GO:0019373; P:epoxygenase P450 pathway; IBA:GO_Central.
GO; GO:0046483; P:heterocycle metabolic process; ISO:MGI.
GO; GO:0016098; P:monoterpenoid metabolic process; ISO:MGI.
GO; GO:0055114; P:oxidation-reduction process; ISO:MGI.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
GO; GO:0010243; P:response to organonitrogen compound; IEA:Ensembl.
GO; GO:0010193; P:response to ozone; IEA:Ensembl.
GO; GO:0008202; P:steroid metabolic process; ISO:MGI.
GO; GO:0006641; P:triglyceride metabolic process; IEA:Ensembl.
GO; GO:0006805; P:xenobiotic metabolic process; IEA:Ensembl.
Gene3D; 1.10.630.10; -; 1.
InterPro; IPR001128; Cyt_P450.
InterPro; IPR017972; Cyt_P450_CS.
InterPro; IPR002401; Cyt_P450_E_grp-I.
InterPro; IPR008070; Cyt_P450_E_grp-I_CYP2E-like.
InterPro; IPR036396; Cyt_P450_sf.
Pfam; PF00067; p450; 1.
PRINTS; PR00463; EP450I.
PRINTS; PR01687; EP450ICYP2E.
PRINTS; PR00385; P450.
SUPFAM; SSF48264; SSF48264; 1.
PROSITE; PS00086; CYTOCHROME_P450; 1.
1: Evidence at protein level;
Complete proteome; Endoplasmic reticulum; Heme; Iron; Membrane;
Metal-binding; Microsome; Monooxygenase; NADP; Oxidoreductase;
Reference proteome.
CHAIN 1 493 Cytochrome P450 2E1.
/FTId=PRO_0000051755.
REGION 298 303 Substrate binding. {ECO:0000250}.
METAL 437 437 Iron (heme axial ligand). {ECO:0000250}.
SEQUENCE 493 AA; 56805 MW; 4031AB016DA56A9C CRC64;
MAVLGITVAL LVWIATLLLV SIWKQIYRSW NLPPGPFPIP FFGNIFQLDL KDIPKSLTKL
AKRFGPVFTL HLGQRRIVVL HGYKAVKEVL LNHKNEFSGR GDIPVFQEYK NKGIIFNNGP
TWKDVRRFSL SILRDWGMGK QGNEARIQRE AHFLVEELKK TKGQPFDPTF LIGCAPCNVI
ADILFNKRFD YDDKKCLELM SLFNENFYLL STPWIQAYNY FSDYLQYLPG SHRKVMKNVS
EIRQYTLGKA KEHLKSLDIN CPRDVTDCLL IEMEKEKHSQ EPMYTMENIS VTLADLFFAG
TETTSTTLRY GLLILMKYPE IEEKLHEEID RVIGPSRAPA VRDRMNMPYM DAVVHEIQRF
INLVPSNLPH EATRDTVFRG YVIPKGTVVI PTLDSLLFDN YEFPDPETFK PEHFLNENGK
FKYSDYFKAF SAGKRVCVGE GLARMELFLL LSAILQHFNL KSLVDPKDID LSPVTIGFGS
IPREFKLCVI PRS


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