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Protein

Bifunctional epoxide hydrolase 2

Gene

EPHX2

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Bifunctional enzyme. The C-terminal domain has epoxide hydrolase activity and acts on epoxides (alkene oxides, oxiranes) and arene oxides. Plays a role in xenobiotic metabolism by degrading potentially toxic epoxides. Also determines steady-state levels of physiological mediators. The N-terminal domain has lipid phosphatase activity, with the highest activity towards threo-9,10-phosphonooxy-hydroxy-octadecanoic acid, followed by erythro-9,10-phosphonooxy-hydroxy-octadecanoic acid, 12-phosphonooxy-octadec-9Z-enoic acid, 12-phosphonooxy-octadec-9E-enoic acid, and p-nitrophenyl phospate (By similarity).By similarity1 Publication

Catalytic activityi

An epoxide + H2O = a glycol.
(9S,10S)-10-hydroxy-9-(phosphonooxy)octadecanoate + H2O = (9S,10S)-9,10-dihydroxyoctadecanoate + phosphate.

Cofactori

Mg2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi9 – 91MagnesiumBy similarity
Metal bindingi11 – 111MagnesiumBy similarity
Metal bindingi185 – 1851MagnesiumBy similarity
Active sitei335 – 3351NucleophileBy similarity
Binding sitei383 – 3831SubstrateBy similarity
Active sitei466 – 4661Proton donorBy similarity
Active sitei524 – 5241Proton acceptorBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Aromatic hydrocarbons catabolism, Detoxification, Lipid metabolism

Keywords - Ligandi

Magnesium, Metal-binding

Protein family/group databases

ESTHERisussc-q6q2c2. Epoxide_hydrolase.
MEROPSiS33.973.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional epoxide hydrolase 2
Including the following 2 domains:
Cytosolic epoxide hydrolase 2 (EC:3.3.2.10)
Short name:
CEH
Alternative name(s):
Epoxide hydratase
Soluble epoxide hydrolase
Short name:
SEH
Lipid-phosphate phosphatase (EC:3.1.3.76)
Gene namesi
Name:EPHX2
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 555555Bifunctional epoxide hydrolase 2PRO_0000084113Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei43 – 431N6-acetyllysineBy similarity
Modified residuei191 – 1911N6-acetyllysineBy similarity
Modified residuei215 – 2151N6-acetyllysineBy similarity
Modified residuei370 – 3701PhosphoserineBy similarity
Modified residuei455 – 4551N6-succinyllysineBy similarity
Modified residuei505 – 5051N6-succinyllysineBy similarity
Lipidationi522 – 5221S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteineBy similarity
Modified residuei554 – 5541N6-succinyllysineBy similarity

Post-translational modificationi

The covalent modification of cysteine by 15-deoxy-Delta12,14-prostaglandin-J2 is autocatalytic and reversible. It may occur as an alternative to other cysteine modifications, such as S-nitrosylation and S-palmitoylation (By similarity).By similarity

Keywords - PTMi

Acetylation, Lipoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ6Q2C2.
PeptideAtlasiQ6Q2C2.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000010323.

Structurei

3D structure databases

ProteinModelPortaliQ6Q2C2.
SMRiQ6Q2C2. Positions 3-548.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 224224PhosphataseAdd
BLAST
Regioni123 – 1242Phosphate bindingBy similarity
Regioni235 – 555321Epoxide hydrolaseAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi553 – 5553Microbody targeting signalSequence analysis

Domaini

The N-terminal domain has phosphatase activity. The C-terminal domain has epoxide hydrolase activity.

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3085. Eukaryota.
KOG4178. Eukaryota.
COG1011. LUCA.
HOGENOMiHOG000028073.
HOVERGENiHBG006095.
InParanoidiQ6Q2C2.
KOiK08726.

Family and domain databases

Gene3Di1.10.150.240. 1 hit.
3.40.50.1000. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR000639. Epox_hydrolase-like.
IPR023214. HAD-like_dom.
IPR006439. HAD-SF_hydro_IA.
IPR011945. HAD-SF_ppase_IA/epoxid_hydro_N.
IPR023198. PGP_dom2.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
PRINTSiPR00111. ABHYDROLASE.
PR00412. EPOXHYDRLASE.
SUPFAMiSSF53474. SSF53474. 1 hit.
SSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR02247. HAD-1A3-hyp. 1 hit.
TIGR01509. HAD-SF-IA-v3. 1 hit.

Sequencei

Sequence statusi: Complete.

Q6Q2C2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALRAAVFDL DGVLALPSIT TSWARAEEKL ALPRGFLNEA FKKGGQDGSV
60 70 80 90 100
ARVMTGEITF SQWVPFMEED CRKCAEDSGI RLPENFSVKH IFDKALSEKK
110 120 130 140 150
INYPMLQAAL TLKKKGFSTC ILTNNWLDDS AQRGSRAQLM CELRPHFDFL
160 170 180 190 200
IESCRVGMAK PDPQIYKLML DTLKAEPNEV VFLDDVGTHL KPVRDLGMAT
210 220 230 240 250
ILVRDTDTAL RELEKVTGVQ LLQTPALPPT SCDPSALSHG YVLIKPGVRL
260 270 280 290 300
HFVEMGSGPA VCLCHGFPES WFSWRYQIPA LAQAGFRVLA VDMKGYGESS
310 320 330 340 350
APPEIEEYSL EVLCKDMVTF LNKLGLSQAV FIGHDWGGVL VWNMALFYPE
360 370 380 390 400
RVRAVASLNT PFMPSNPNVS PMEIIKANPV FDYQLYFQEP GVAEAELEQN
410 420 430 440 450
LDRTFKNFFR AHDETFLTTN RVRELGGLFV GTPEEPSLSR LVTEEDIQFY
460 470 480 490 500
VQQFKKSGFR GPLNWYRNME RNWQWGCKGS GRKILIPALM VTAENDLVLH
510 520 530 540 550
PKMSKHMENW IPHLKRGHIK DCGHWTQIDK PAELNRILIE WLETDARNPL

VDSKL
Length:555
Mass (Da):62,767
Last modified:July 5, 2004 - v1
Checksum:i996EF83CBF82FBEF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY566232 mRNA. Translation: AAS68016.1.
RefSeqiNP_001001641.1. NM_001001641.1.
UniGeneiSsc.8278.

Genome annotation databases

GeneIDi414425.
KEGGissc:414425.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY566232 mRNA. Translation: AAS68016.1.
RefSeqiNP_001001641.1. NM_001001641.1.
UniGeneiSsc.8278.

3D structure databases

ProteinModelPortaliQ6Q2C2.
SMRiQ6Q2C2. Positions 3-548.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000010323.

Protein family/group databases

ESTHERisussc-q6q2c2. Epoxide_hydrolase.
MEROPSiS33.973.

Proteomic databases

PaxDbiQ6Q2C2.
PeptideAtlasiQ6Q2C2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi414425.
KEGGissc:414425.

Organism-specific databases

CTDi2053.

Phylogenomic databases

eggNOGiKOG3085. Eukaryota.
KOG4178. Eukaryota.
COG1011. LUCA.
HOGENOMiHOG000028073.
HOVERGENiHBG006095.
InParanoidiQ6Q2C2.
KOiK08726.

Family and domain databases

Gene3Di1.10.150.240. 1 hit.
3.40.50.1000. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR000639. Epox_hydrolase-like.
IPR023214. HAD-like_dom.
IPR006439. HAD-SF_hydro_IA.
IPR011945. HAD-SF_ppase_IA/epoxid_hydro_N.
IPR023198. PGP_dom2.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
PRINTSiPR00111. ABHYDROLASE.
PR00412. EPOXHYDRLASE.
SUPFAMiSSF53474. SSF53474. 1 hit.
SSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR02247. HAD-1A3-hyp. 1 hit.
TIGR01509. HAD-SF-IA-v3. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Cytochrome p450-dependent lipid metabolism in preovulatory follicles."
    Newman J.W., Stok J.E., Vidal J.D., Corbin C.J., Huang Q., Hammock B.D., Conley A.J.
    Endocrinology 145:5097-5105(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
    Tissue: Ovary.

Entry informationi

Entry nameiHYES_PIG
AccessioniPrimary (citable) accession number: Q6Q2C2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: July 5, 2004
Last modified: July 6, 2016
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.