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P04068

- HYEP_RABIT

UniProt

P04068 - HYEP_RABIT

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Protein

Epoxide hydrolase 1

Gene

EPHX1

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 3 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

  1. cis-stilbene-oxide hydrolase activity Source: UniProtKB-EC

GO - Biological processi

  1. aromatic compound catabolic process Source: UniProtKB-KW
  2. response to toxic substance Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Aromatic hydrocarbons catabolism, Detoxification

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
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
ProteomesiUP000001811: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB-KW
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 455455Epoxide hydrolase 1PRO_0000080858Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei295 – 2951Omega-N-methylated arginineBy similarity

Keywords - PTMi

Methylation

Interactioni

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000010259.

Structurei

3D structure databases

ProteinModelPortaliP04068.
ModBaseiSearch...
MobiDBiSearch...

Transmembrane

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

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S33 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0596.
HOGENOMiHOG000132894.
HOVERGENiHBG002366.
InParanoidiP04068.

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.

P04068-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLLELLLASV LGFVIYWFVS GDKEESLPLE DGWWGPGSRP VGLEDESIRP
60 70 80 90 100
FKVETSDEEI NDLHQRIDRI RLTPPLENSR FHYGFNSNYL KKILSYWRHE
110 120 130 140 150
FDWKKQVEIL NSYPHFKTKI EGLDIHFIHV KPPQVPPGRT PKPLLMVHGW
160 170 180 190 200
PGSFFEFYKI IPLLTDPKSH GLSDEHIFEV ICPSIPGYGF SQASSKKGFN
210 220 230 240 250
SVSTARIFYK LMLRLGFQEF YIQGGDWGAL VCTNMAQLVP SHVKGLHLNM
260 270 280 290 300
ALILRNHYTL TLLLGRRIGG LLGYTERDME LLYPFKEKVF YSLMRESGYM
310 320 330 340 350
HIRATKPDTV GCALNDSPVG LAAYILEKFS TWTNSEFRDL EDGGLERKFS
360 370 380 390 400
LQDLLTNIMI YWTTGSIVSS QRYYKENLGQ GFMAHKHERL KVHVPTGFAA
410 420 430 440 450
FPCEIMHVPE KWVRTKYPQL ISYSYMPRGG HFAAFEEPEL LARDICKFVG

LVERQ
Length:455
Mass (Da):52,512
Last modified:August 1, 1990 - v2
Checksum:i8A1F556275389AD2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti68 – 703Missing AA sequence (PubMed:6693396)Curated
Sequence conflicti113 – 1131Y → L AA sequence (PubMed:6693396)Curated
Sequence conflicti201 – 2033SVS → NVV AA sequence (PubMed:6693396)Curated
Sequence conflicti212 – 2121M → RISSY AA sequence (PubMed:6693396)Curated
Sequence conflicti248 – 2492LN → DL AA sequence (PubMed:6693396)Curated
Sequence conflicti303 – 3031R → Q AA sequence (PubMed:6693396)Curated
Sequence conflicti366 – 3716SIVSSQ → WIRTHY AA sequence (PubMed:6693396)Curated
Sequence conflicti455 – 4551Missing AA sequence (PubMed:6693396)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M21496 mRNA. Translation: AAA31392.1.
PIRiS04342. YXRBH.
RefSeqiNP_001075744.1. NM_001082275.1.
UniGeneiOcu.6248.

Genome annotation databases

GeneIDi100009104.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M21496 mRNA. Translation: AAA31392.1 .
PIRi S04342. YXRBH.
RefSeqi NP_001075744.1. NM_001082275.1.
UniGenei Ocu.6248.

3D structure databases

ProteinModelPortali P04068.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9986.ENSOCUP00000010259.

Protein family/group databases

MEROPSi S33.971.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100009104.

Organism-specific databases

CTDi 2052.

Phylogenomic databases

eggNOGi COG0596.
HOGENOMi HOG000132894.
HOVERGENi HBG002366.
InParanoidi P04068.

Family and domain databases

Gene3Di 3.40.50.1820. 1 hit.
InterProi IPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR000639. Epox_hydrolase-like.
IPR010497. Epoxide_hydro_N.
IPR016292. Epoxide_hydrolase.
[Graphical view ]
Pfami PF00561. Abhydrolase_1. 1 hit.
PF06441. EHN. 1 hit.
[Graphical view ]
PIRSFi PIRSF001112. Epoxide_hydrolase. 1 hit.
PRINTSi PR00412. EPOXHYDRLASE.
SUPFAMi SSF53474. SSF53474. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Rabbit microsomal epoxide hydrolase: isolation and characterization of the xenobiotic metabolizing enzyme cDNA."
    Hassett C., Turnblom S.M., Deangeles A., Omiecinski C.J.
    Arch. Biochem. Biophys. 271:380-389(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The covalent structure of hepatic microsomal epoxide hydrolase. II. The complete amino acid sequence."
    Heinemann F.S., Ozols J.
    J. Biol. Chem. 259:797-804(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Strain: New Zealand white.
    Tissue: Liver.

Entry informationi

Entry nameiHYEP_RABIT
AccessioniPrimary (citable) accession number: P04068
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: August 1, 1990
Last modified: October 29, 2014
This is version 105 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. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3