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P05182 (CP2E1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytochrome P450 2E1

EC=1.14.13.-
Alternative name(s):
4-nitrophenol 2-hydroxylase
EC=1.14.13.n7
CYPIIE1
Cytochrome P450-J
Cytochrome P450RLM6
Gene names
Name:Cyp2e1
Synonyms:Cyp2e, Cyp2e-1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length493 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Metabolizes several precarcinogens, drugs, and solvents to reactive metabolites By similarity.

Catalytic activity

4-nitrophenol + NADPH + O2 = 4-nitrocatechol + NADP+ + H2O.

Cofactor

Heme group By similarity.

Subcellular location

Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein.

Induction

By ethanol.

Sequence similarities

Belongs to the cytochrome P450 family.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Membrane
Microsome
   LigandHeme
Iron
Metal-binding
NADP
   Molecular functionMonooxygenase
Oxidoreductase
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processdrug metabolic process

Inferred from electronic annotation. Source: Ensembl

heterocycle metabolic process

Inferred from electronic annotation. Source: Ensembl

monoterpenoid metabolic process

Inferred from electronic annotation. Source: Ensembl

oxidation-reduction process

Inferred from direct assay PubMed 8809087. Source: RGD

response to drug

Inferred from expression pattern PubMed 21170329. Source: RGD

response to ethanol

Inferred from expression pattern PubMed 16337197. Source: RGD

response to organonitrogen compound

Inferred from expression pattern PubMed 19406192. Source: RGD

response to ozone

Inferred from expression pattern PubMed 9571988. Source: RGD

steroid metabolic process

Inferred from electronic annotation. Source: Ensembl

triglyceride metabolic process

Inferred from mutant phenotype PubMed 20116195. Source: RGD

xenobiotic metabolic process

Inferred from mutant phenotype PubMed 21187827. Source: RGD

   Cellular_componentGolgi membrane

Inferred from direct assay PubMed 8809087. Source: RGD

intracellular membrane-bounded organelle

Inferred from direct assay PubMed 12220509. Source: RGD

intrinsic component of endoplasmic reticulum membrane

Inferred from direct assay PubMed 14661969. Source: RGD

mitochondrion

Inferred from direct assay PubMed 16337197. Source: RGD

   Molecular_functionFMN binding

Inferred by curator PubMed 8809087. Source: RGD

heme binding

Inferred from sequence or structural similarity. Source: UniProtKB

iron ion binding

Inferred from electronic annotation. Source: InterPro

monooxygenase activity

Traceable author statement PubMed 11804847. Source: RGD

oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen

Inferred from electronic annotation. Source: UniProtKB-EC

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

Inferred from direct assay PubMed 8809087. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5 Ref.6
Chain2 – 493492Cytochrome P450 2E1
PRO_0000051758

Regions

Region298 – 3036Substrate binding By similarity

Sites

Metal binding4371Iron (heme axial ligand)

Experimental info

Sequence conflict251Q → K in AAA41060. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P05182 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 7600B9D28AED5EDB

FASTA49356,627
        10         20         30         40         50         60 
MAVLGITIAL LVWVATLLVI SIWKQIYNSW NLPPGPFPLP ILGNIFQLDL KDIPKSFTKL 

        70         80         90        100        110        120 
AKRFGPVFTL HLGSRRIVVL HGYKAVKEVL LNHKNEFSGR GDIPVFQEYK NKGIIFNNGP 

       130        140        150        160        170        180 
TWKDVRRFSL SILRDWGMGK QGNEARIQRE AQFLVEELKK TKGQPFDPTF LIGCAPCNVI 

       190        200        210        220        230        240 
ADILFNKRFD YNDKKCLRLM SLFNENFYLL STPWIQLYNN FADYLRYLPG SHRKIMKNVS 

       250        260        270        280        290        300 
EIKQYTLEKA KEHLQSLDIN CARDVTDCLL IEMEKEKHSQ EPMYTMENVS VTLADLFFAG 

       310        320        330        340        350        360 
TETTSTTLRY GLLILMKYPE IEEKLHEEID RVIGPSRVPA VRDRLDMPYM DAVVHEIQRF 

       370        380        390        400        410        420 
INLVPSNLPH EATRDTVFQG YVIPKGTVVI PTLDSLLYDS HEFPDPEKFK PEHFLNENGK 

       430        440        450        460        470        480 
FKYSDYFKAF SAGKRVCVGE GLARMELFLL LSAILQHFNL KSLVDPKDID LSPVTVGFGS 

       490 
IPPQFKLCVI PRS 

« Hide

References

« Hide 'large scale' references
[1]"Complementary DNA and protein sequences of ethanol-inducible rat and human cytochrome P-450s. Transcriptional and post-transcriptional regulation of the rat enzyme."
Song B.-J., Gelboin H.V., Park S.-S., Yang C.S., Gonzalez F.J.
J. Biol. Chem. 261:16689-16697(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The rat P450IIE1 gene: complete intron and exon sequence, chromosome mapping, and correlation of developmental expression with specific 5' cytosine demethylation."
Umeno M., Song B.-J., Kozak C., Gelboin H.V., Gonzalez F.J.
J. Biol. Chem. 263:4956-4962(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Liver.
[3]"The complete coding sequence of the rat brain cytochrome P450 2E1."
Yoo M., Shin S.W.
Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: Sprague-Dawley.
Tissue: Brain.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
[5]"Responses to insulin by two forms of rat hepatic microsomal cytochrome P-450 that undergo major (RLM6) and minor (RLM5b) elevations in diabetes."
Favreau L.V., Malchoff D.M., Mole J.E., Schenkman J.B.
J. Biol. Chem. 262:14319-14326(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-35.
Tissue: Liver.
[6]"Changes in the amount of cytochrome P450s in rat hepatic microsomes with starvation."
Imaoka S., Terano Y., Funae Y.
Arch. Biochem. Biophys. 278:168-178(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-20.
Tissue: Liver.
[7]"Molecular cloning of a cDNA for rat diabetes-inducible cytochrome P450RLM6: hormonal regulation and similarity to the cytochrome P4502E1 gene."
Richardson T.H., Schenkman J.B., Turcan R., Goldfarb P.S., Gibson G.G.
Xenobiotica 22:621-631(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 100-463.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J02627 mRNA. Translation: AAA41060.1.
M20131 Genomic DNA. Translation: AAA41033.1.
AF061442 mRNA. Translation: AAC15991.1.
BC081774 mRNA. Translation: AAH81774.1.
S48325 mRNA. Translation: AAB24151.1.
PIRA25341.
RefSeqNP_113731.1. NM_031543.1.
UniGeneRn.1372.

3D structure databases

ProteinModelPortalP05182.
SMRP05182. Positions 33-493.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid247159. 2 interactions.
IntActP05182. 1 interaction.
MINTMINT-4576828.
STRING10116.ENSRNOP00000016883.

Chemistry

BindingDBP05182.
ChEMBLCHEMBL5978.

PTM databases

PhosphoSiteP05182.

Proteomic databases

PaxDbP05182.
PRIDEP05182.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000016883; ENSRNOP00000016883; ENSRNOG00000012458.
GeneID25086.
KEGGrno:25086.
UCSCRGD:2475. rat.

Organism-specific databases

CTD1571.
RGD2475. Cyp2e1.

Phylogenomic databases

eggNOGCOG2124.
GeneTreeENSGT00680000099783.
HOGENOMHOG000036992.
HOVERGENHBG015789.
InParanoidP05182.
KOK07415.
OMAPMYTMEN.
OrthoDBEOG7RBZ85.
PhylomeDBP05182.
TreeFamTF352043.

Gene expression databases

GenevestigatorP05182.

Family and domain databases

Gene3D1.10.630.10. 1 hit.
InterProIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
IPR008070. Cyt_P450_E_grp-I_CYP2E-like.
[Graphical view]
PfamPF00067. p450. 1 hit.
[Graphical view]
PRINTSPR00463. EP450I.
PR01687. EP450ICYP2E.
PR00385. P450.
SUPFAMSSF48264. SSF48264. 1 hit.
PROSITEPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio605350.
PROP05182.

Entry information

Entry nameCP2E1_RAT
AccessionPrimary (citable) accession number: P05182
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 135 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families