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Protein

Epoxide hydrolase 1

Gene

Ephx1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Biotransformation enzyme that catalyzes the hydrolysis of arene and aliphatic epoxides to less reactive and more water soluble dihydrodiols by the trans addition of water.

Catalytic activityi

Cis-stilbene oxide + H2O = (+)-(1R,2R)-1,2-diphenylethane-1,2-diol.

GO - Molecular functioni

GO - Biological processi

  • aromatic compound catabolic process Source: UniProtKB-KW
  • cellular aromatic compound metabolic process Source: MGI
  • response to organic cyclic compound Source: MGI
  • response to toxic substance Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Aromatic hydrocarbons catabolism, Detoxification

Enzyme and pathway databases

SABIO-RKQ9D379.

Protein family/group databases

MEROPSiS33.971.

Names & Taxonomyi

Protein namesi
Recommended name:
Epoxide hydrolase 1 (EC:3.3.2.9)
Alternative name(s):
Epoxide hydratase
Microsomal epoxide hydrolase
Gene namesi
Name:Ephx1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:95405. Ephx1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei2 – 2019Helical; Signal-anchorSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 455455Epoxide hydrolase 1PRO_0000080856Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei295 – 2951Dimethylated arginine; alternateBy similarity
Modified residuei295 – 2951Omega-N-methylated arginine; alternateBy similarity
Modified residuei439 – 4391N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Methylation

Proteomic databases

MaxQBiQ9D379.
PaxDbiQ9D379.
PRIDEiQ9D379.

PTM databases

PhosphoSiteiQ9D379.

Expressioni

Gene expression databases

BgeeiQ9D379.
CleanExiMM_EPHX1.
ExpressionAtlasiQ9D379. baseline and differential.
GenevestigatoriQ9D379.

Interactioni

Protein-protein interaction databases

IntActiQ9D379. 6 interactions.
MINTiMINT-1862106.
STRINGi10090.ENSMUSP00000047551.

Structurei

3D structure databases

ProteinModelPortaliQ9D379.
SMRiQ9D379. Positions 27-449.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S33 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0596.
GeneTreeiENSGT00390000002210.
HOGENOMiHOG000132894.
HOVERGENiHBG002366.
InParanoidiQ9D379.
KOiK01253.
OMAiWGITRIA.
TreeFamiTF313813.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR000639. Epox_hydrolase-like.
IPR010497. Epoxide_hydro_N.
IPR016292. Epoxide_hydrolase.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
PF06441. EHN. 1 hit.
[Graphical view]
PIRSFiPIRSF001112. Epoxide_hydrolase. 1 hit.
PRINTSiPR00412. EPOXHYDRLASE.
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9D379-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWLELILASV LGFVIYWFVS RDKEETLPLE DGWWGPGSKP SAKEDESIRP
60 70 80 90 100
FKVETSDEEI KDLHQRIDRF RASPPLEGSR FHYGFNSSYL KKVVSFWRNE
110 120 130 140 150
FDWRKQVEIL NQYPHFKTKI EGLDIHFIHV KPPQLPSGRT PKPLLMVHGW
160 170 180 190 200
PGSFYEFYKI IPLLTDPKTH GLSDEHVFEV ICPSIPGYGF SEASSKKGLN
210 220 230 240 250
SVATARIFYK LMSRLGFQKF YIQGGDWGSL ICTNIAQMVP NHVKGLHLNM
260 270 280 290 300
SFISRNIYSL TPLLGQRFGR FLGYTEKDLE LLYPFKEKVF YNIMRESGYL
310 320 330 340 350
HIQATKPDTV GCALNDSPVG LAAYILEKFS TWTKSEYREL EDGGLERKFS
360 370 380 390 400
LEDLLTNIMI YWTTGTIVSS QRFYKENLGQ GVMVHRHEGM KVFVPTGYSA
410 420 430 440 450
FPSEILHAPE KWVKVKYPKL ISYSYMERGG HFAAFEEPKL LAQDIRKFVS

LAELQ
Length:455
Mass (Da):52,577
Last modified:July 27, 2011 - v2
Checksum:i1567F619D9114C58
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti410 – 4101E → K in BAB31132 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U89491 mRNA. Translation: AAB49762.1.
AK018249 mRNA. Translation: BAB31132.1.
CH466555 Genomic DNA. Translation: EDL13136.1.
BC045194 mRNA. Translation: AAH45194.1.
BC061493 mRNA. Translation: AAH61493.1.
CCDSiCCDS15579.1.
RefSeqiNP_034275.1. NM_010145.2.
UniGeneiMm.9075.

Genome annotation databases

EnsembliENSMUST00000036928; ENSMUSP00000047551; ENSMUSG00000038776.
GeneIDi13849.
KEGGimmu:13849.
UCSCiuc007dwz.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U89491 mRNA. Translation: AAB49762.1.
AK018249 mRNA. Translation: BAB31132.1.
CH466555 Genomic DNA. Translation: EDL13136.1.
BC045194 mRNA. Translation: AAH45194.1.
BC061493 mRNA. Translation: AAH61493.1.
CCDSiCCDS15579.1.
RefSeqiNP_034275.1. NM_010145.2.
UniGeneiMm.9075.

3D structure databases

ProteinModelPortaliQ9D379.
SMRiQ9D379. Positions 27-449.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9D379. 6 interactions.
MINTiMINT-1862106.
STRINGi10090.ENSMUSP00000047551.

Chemistry

ChEMBLiCHEMBL1075293.

Protein family/group databases

MEROPSiS33.971.

PTM databases

PhosphoSiteiQ9D379.

Proteomic databases

MaxQBiQ9D379.
PaxDbiQ9D379.
PRIDEiQ9D379.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000036928; ENSMUSP00000047551; ENSMUSG00000038776.
GeneIDi13849.
KEGGimmu:13849.
UCSCiuc007dwz.1. mouse.

Organism-specific databases

CTDi2052.
MGIiMGI:95405. Ephx1.

Phylogenomic databases

eggNOGiCOG0596.
GeneTreeiENSGT00390000002210.
HOGENOMiHOG000132894.
HOVERGENiHBG002366.
InParanoidiQ9D379.
KOiK01253.
OMAiWGITRIA.
TreeFamiTF313813.

Enzyme and pathway databases

SABIO-RKQ9D379.

Miscellaneous databases

ChiTaRSiEphx1. mouse.
NextBioi284700.
PROiQ9D379.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D379.
CleanExiMM_EPHX1.
ExpressionAtlasiQ9D379. baseline and differential.
GenevestigatoriQ9D379.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR000639. Epox_hydrolase-like.
IPR010497. Epoxide_hydro_N.
IPR016292. Epoxide_hydrolase.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
PF06441. EHN. 1 hit.
[Graphical view]
PIRSFiPIRSF001112. Epoxide_hydrolase. 1 hit.
PRINTSiPR00412. EPOXHYDRLASE.
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The Ephx1(d) allele encoding an Arg338Cys substitution is associated with heat lability."
    Hartsfield J.K. Jr., Everett E.T.
    Mamm. Genome 11:915-918(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6J.
    Tissue: Liver.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Medulla oblongata.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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].
    Strain: FVB/N.
    Tissue: Colon and Mammary tumor.
  5. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 339-347, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain.
  6. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-439, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiHYEP_MOUSE
AccessioniPrimary (citable) accession number: Q9D379
Secondary accession number(s): P97869
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2002
Last sequence update: July 27, 2011
Last modified: March 4, 2015
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.