Ephx2
entrez
65030
canonical
uniprot
P80299
canonical
ensembl
ENSRNOG00000017286
resolver
ensembl
ENSRNOG00055006699
resolver
ensembl
ENSRNOG00060010710
resolver
ensp
ENSRNOP00000023385
resolver
ensp
ENSRNOP00055008541
resolver
ensp
ENSRNOP00055008548
resolver
ensp
ENSRNOP00060014181
resolver
ensp
ENSRNOP00060014186
resolver
enst
ENSRNOT00055010957
resolver
enst
ENSRNOT00055010964
resolver
enst
ENSRNOT00060018220
resolver
enst
ENSRNOT00060018225
resolver
genesymbol
Ephx2
resolver
uniprot_entry
HYES_RAT
resolver
activity_regulation
ACTIVITY REGULATION: 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) (PubMed:21217101). Phosphatase activity is inhibited by dodecyl-phosphate, phospholipids such as phospho-lysophosphatidic acids and fatty acids such as palmitic acid and lauric acid (By similarity). {ECO:0000250|UniProtKB:P34913, ECO:0000269|PubMed:21217101}.
uniprot
proteins
amino_acid_sequence
MALRVAAFDLDGVLALPSIAGVLRHTEEALALPRDFLLGAFQMKFPEGPTEQLMKGKITFSQWVPLMDESCRKSSKACGASLPENFSISEIFSQAMAARSINRPMLQAAAALKKKGFTTCIVTNNWLDDSDKRDILAQMMCELSQHFDFLIESCQVGMIKPEPQIYKFVLDTLKAKPNEVVFLDDFGSNLKPARDMGMVTILVRDTASALRELEKVTGTQFPEAPLPVPCSPNDVSHGYVTVKPGIRLHFVEMGSGPAICLCHGFPESWFSWRYQIPALAQAGFRVLAIDMKGYGDSSSPPEIEEYAMELLCEEMVTFLNKLGIPQAVFIGHDWAGVLVWNMALFHPERVRAVASLNTPLMPPNPEVSPMEVIRSIPVFNYQLYFQEPGVAEAELEKNMSRTFKSFFRTSDDMGLLTVNKATEMGGILVGTPEDPKVSKITTEEEIEYYIQQFKKSGFRGPLNWYRNTERNWKWSCKALGRKILVPALMVTAEKDIVLRPEMSKNMENWIPFLKRGHIEDCGHWTQIEKPAEVNQILIKWLKTEIQNPSVTSKI
uniprot
proteins
ec_number
3.1.3.76
uniprot
proteins
ec_number
3.3.2.10
uniprot
proteins
function
FUNCTION: Bifunctional enzyme (PubMed:12574508, PubMed:8626766). The C-terminal domain has epoxide hydrolase activity and acts on epoxides (alkene oxides, oxiranes) and arene oxides (PubMed:8626766). Plays a role in xenobiotic metabolism by degrading potentially toxic epoxides (PubMed:8626766). Also determines steady-state levels of physiological mediators (By similarity). 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). {ECO:0000250|UniProtKB:P34913, ECO:0000269|PubMed:12574508, ECO:0000269|PubMed:8626766}.; FUNCTION: Bifunctional enzyme (PubMed:12574508, PubMed:8626766). The C-terminal domain has epoxide hydrolase activity and acts on epoxides (alkene oxides, oxiranes) and arene oxides (PubMed:8626766). Plays a role in xenobiotic metabolism by degrading potentially toxic epoxides (By similarity). Also determines steady-state levels of physiological mediators (By similarity). {ECO:0000250|UniProtKB:P34913, ECO:0000269|PubMed:8626766}.; FUNCTION: Bifunctional enzyme (PubMed:12574508, PubMed:8626766). 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 (PubMed:12574508). Has phosphatase activity toward lyso-glycerophospholipids with also some lower activity toward lysolipids of sphingolipid and isoprenoid phosphates (By similarity). {ECO:0000250|UniProtKB:P34913, ECO:0000269|PubMed:12574508}.
uniprot
proteins
mass_dalton
62340
uniprot
proteins
mutagenesis
MUTAGEN 332; /note="H->Q: Reduces epoxide hydrolase activity by 95%."; MUTAGEN 333; /note="D->G: Loss of epoxide hydrolase activity."; /evidence="ECO:0000269|PubMed:8626766"; MUTAGEN 334; /note="W->F: Slight reduction of epoxide hydrolase activity."; /evidence="ECO:0000269|PubMed:8626766"; MUTAGEN 433; /note="E->Q,K: Slight loss of epoxide hydrolase activity."; /evidence="ECO:0000269|PubMed:8626766"; MUTAGEN 434; /note="D->Y: Slight loss of epoxide hydrolase activity."; /evidence="ECO:0000269|PubMed:8626766"; MUTAGEN 493; /note="E->Q,K: No effect."; /evidence="ECO:0000269|PubMed:8626766"; MUTAGEN 495; /note="D->H: Loss of epoxide hydrolase activity."; /evidence="ECO:0000269|PubMed:8626766"; MUTAGEN 517; /note="H->Y: Reduces epoxide hydrolase activity by 50%. Loss of activity; when associated with Y-521."; /evidence="ECO:0000269|PubMed:8626766"; MUTAGEN 521; /note="C->Y: Loss of epoxide hydrolase activity; when associated with Y-517."; /evidence="ECO:0000269|PubMed:8626766"; MUTAGEN 523; /note="H->D,N,Y: Loss of epoxide hydrolase activity."; /evidence="ECO:0000269|PubMed:8626766"; MUTAGEN 526; /note="Q->H: Reduces epoxide hydrolase activity by 80%; when associated with T-542."; /evidence="ECO:0000269|PubMed:8626766"; MUTAGEN 540; /note="W->L,S: Reduces epoxide hydrolase activity by 95%."; /evidence="ECO:0000269|PubMed:8626766"; MUTAGEN 542; /note="K->T: Reduces epoxide hydrolase activity by 80%; when associated with H-526."; /evidence="ECO:0000269|PubMed:8626766
uniprot
proteins
post_translational_modification
PTM: 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). {ECO:0000250}.
uniprot
proteins
protein_family
AB hydrolase superfamily
uniprot
proteins
protein_family
Epoxide hydrolase family
uniprot
proteins
pubmed
12574508
uniprot
proteins
pubmed
1743286
uniprot
proteins
pubmed
21217101
uniprot
proteins
pubmed
8349641
uniprot
proteins
pubmed
8626766
uniprot
proteins
sequence_length
554
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm. Peroxisome.
uniprot
proteins