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Protein

Bifunctional epoxide hydrolase 2

Gene

EPHX2

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: -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 (By similarity). Also determines steady-state levels of physiological mediators (PubMed:15308618). 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 and 12-phosphonooxy-octadec-9E-enoic acid (By similarity).By similarity1 Publication

Catalytic activityi

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

Cofactori

Mg2+By similarity

Enzyme regulationi

Inhibited by 1-(1-acetylpiperidin-4-yl)-3-(4-(trifl uoromethoxy)phenyl)urea (TPAU), 1-cyclohexyl-3-dodecylurea (CDU), 12-(3-adamantan-1-yl-ureido)-dodecanoic acid (AUDA), 1-((3S, 5S, 7S)-adamantan-1-yl)-3-(5-(2-(2-ethoxyethoxy) ethoxy)pentyl)urea (AEPU), N-adamantyl-N[']-cyclohexyl urea (ACU), 4-(((1S, 4S)-4-(3-((3S, 5S, 7S)-adamantan-1-yl) ureido)cyclohexyl)oxy)benzoic acid (c-AUCB), 4-(((1R, 4R)-4-(3-((3S, 5S, 7S)-adamantan-1-yl)ureido)cyclohexyl)oxy)benzoic acid (t-AUCB), 4-(((1R, 4R)-4-(3-(4(trifluoromethoxy)phenyl)ureido)cyclohexyl)oxy)benzoic acid (t-TAUCB) and to a lesser extent by 8-(3-((3S, 5S, 7S)-adamantan-1-yl)ureido) octanoic acid (AUOA).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi9MagnesiumBy similarity1
Metal bindingi11MagnesiumBy similarity1
Metal bindingi185MagnesiumBy similarity1
Active sitei335NucleophileBy similarity1
Binding sitei383SubstrateBy similarity1
Active sitei466Proton donorBy similarity1
Active sitei524Proton acceptorBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Multifunctional enzyme
Biological processAromatic hydrocarbons catabolism, Detoxification, Lipid metabolism
LigandMagnesium, 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:3.3.2.10By similarity)
Short name:
CEH
Alternative name(s):
Epoxide hydratase
Soluble epoxide hydrolase
Short name:
SEH
Lipid-phosphate phosphatase (EC:3.1.3.76By similarity)
Gene namesi
Name:EPHX2
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000841131 – 555Bifunctional epoxide hydrolase 2Add BLAST555

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei43N6-acetyllysineBy similarity1
Modified residuei191N6-acetyllysineBy similarity1
Modified residuei215N6-acetyllysineBy similarity1
Modified residuei370PhosphoserineBy similarity1
Modified residuei455N6-succinyllysineBy similarity1
Modified residuei505N6-succinyllysineBy similarity1
Lipidationi522S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteineBy similarity1
Modified residuei554N6-succinyllysineBy similarity1

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
PRIDEiQ6Q2C2

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000010323

Structurei

3D structure databases

ProteinModelPortaliQ6Q2C2
SMRiQ6Q2C2
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini259 – 531AB hydrolase-1Sequence analysisAdd BLAST273

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 224PhosphataseAdd BLAST224
Regioni123 – 124Phosphate bindingBy similarity2
Regioni235 – 555Epoxide hydrolaseAdd BLAST321

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi553 – 555Microbody targeting signalSequence analysis3

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, 2 hits
3.40.50.1820, 1 hit
InterProiView protein in InterPro
IPR029058 AB_hydrolase
IPR000073 AB_hydrolase_1
IPR000639 Epox_hydrolase-like
IPR036412 HAD-like_sf
IPR006439 HAD-SF_hydro_IA
IPR011945 HAD-SF_ppase_IA/epoxid_hydro_N
IPR023214 HAD_sf
IPR023198 PGP-like_dom2
PfamiView protein in Pfam
PF00561 Abhydrolase_1, 1 hit
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

Similar proteinsi

Entry informationi

Entry nameiHYES_PIG
AccessioniPrimary (citable) accession number: Q6Q2C2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: July 5, 2004
Last modified: March 28, 2018
This is version 86 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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