About Products Protein Database Contact

EPHX2

Gene
EPHX2
Protein
Bifunctional epoxide hydrolase 2
Organism
Homo sapiens
Length
555 amino acids
Function
Bifunctional enzyme (PubMed:12574510). The C-terminal domain has epoxide hydrolase activity and acts on epoxides (alkene oxides, oxiranes) and arene oxides (PubMed:12869654, PubMed:12574510, PubMed:22798687). Plays a role in xenobiotic metabolism by degrading potentially toxic epoxides (By similarity). Also determines steady-state levels of physiological mediators (PubMed:12869654, PubMed:12574510, PubMed:22798687). 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:12574510).
Similarity
Belongs to the AB hydrolase superfamily. Epoxide hydrolase family.
Mass
62.616 kDa
Sequence
MTLRAAVFDLDGVLALPAVFGVLGRTEEALALPRGLLNDAFQKGGPEGATTRLMKGEITLSQWIPLMEENCRKCSETAKVCLPKNFSIKEIFDKAISARKINRPMLQAALMLRKKGFTTAILTNTWLDDRAERDGLAQLMCELKMHFDFLIESCQVGMVKPEPQIYKFLLDTLKASPSEVVFLDDIGANLKPARDLGMVTILVQDTDTALKELEKVTGIQLLNTPAPLPTSCNPSDMSHGYVTVKPRVRLHFVELGSGPAVCLCHGFPESWYSWRYQIPALAQAGYRVLAMDMKGYGESSAPPEIEEYCMEVLCKEMVTFLDKLGLSQAVFIGHDWGGMLVWYMALFYPERVRAVASLNTPFIPANPNMSPLESIKANPVFDYQLYFQEPGVAEAELEQNLSRTFKSLFRASDESVLSMHKVCEAGGLFVNSPEEPSLSRMVTEEEIQFYVQQFKKSGFRGPLNWYRNMERNWKWACKSLGRKILIPALMVTAEKDFVLVPQMSQHMEDWIPHLKRGHIEDCGHWTQMDKPTEVNQILIKWLDSDARNPPVVSKM

Gene
EPHX2
Protein
Bifunctional epoxide hydrolase 2
Organism
Sus scrofa
Length
555 amino acids
Function
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).
Similarity
Belongs to the AB hydrolase superfamily. Epoxide hydrolase family.
Mass
62.767 kDa
Sequence
MALRAAVFDLDGVLALPSITTSWARAEEKLALPRGFLNEAFKKGGQDGSVARVMTGEITFSQWVPFMEEDCRKCAEDSGIRLPENFSVKHIFDKALSEKKINYPMLQAALTLKKKGFSTCILTNNWLDDSAQRGSRAQLMCELRPHFDFLIESCRVGMAKPDPQIYKLMLDTLKAEPNEVVFLDDVGTHLKPVRDLGMATILVRDTDTALRELEKVTGVQLLQTPALPPTSCDPSALSHGYVLIKPGVRLHFVEMGSGPAVCLCHGFPESWFSWRYQIPALAQAGFRVLAVDMKGYGESSAPPEIEEYSLEVLCKDMVTFLNKLGLSQAVFIGHDWGGVLVWNMALFYPERVRAVASLNTPFMPSNPNVSPMEIIKANPVFDYQLYFQEPGVAEAELEQNLDRTFKNFFRAHDETFLTTNRVRELGGLFVGTPEEPSLSRLVTEEDIQFYVQQFKKSGFRGPLNWYRNMERNWQWGCKGSGRKILIPALMVTAENDLVLHPKMSKHMENWIPHLKRGHIKDCGHWTQIDKPAELNRILIEWLETDARNPLVDSKL

Gene
EPHX2
Protein
Bifunctional epoxide hydrolase 2
Organism
Homo sapiens
Length
555 amino acids
Function
Bifunctional enzyme (PubMed:12574510). The C-terminal domain has epoxide hydrolase activity and acts on epoxides (alkene oxides, oxiranes) and arene oxides (PubMed:12869654, PubMed:12574510, PubMed:22798687). Plays a role in xenobiotic metabolism by degrading potentially toxic epoxides (By similarity). Also determines steady-state levels of physiological mediators (PubMed:12869654, PubMed:12574510, PubMed:22798687). 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:12574510).
Similarity
Belongs to the AB hydrolase superfamily. Epoxide hydrolase family.
Mass
62.616 kDa
Sequence
MTLRAAVFDLDGVLALPAVFGVLGRTEEALALPRGLLNDAFQKGGPEGATTRLMKGEITLSQWIPLMEENCRKCSETAKVCLPKNFSIKEIFDKAISARKINRPMLQAALMLRKKGFTTAILTNTWLDDRAERDGLAQLMCELKMHFDFLIESCQVGMVKPEPQIYKFLLDTLKASPSEVVFLDDIGANLKPARDLGMVTILVQDTDTALKELEKVTGIQLLNTPAPLPTSCNPSDMSHGYVTVKPRVRLHFVELGSGPAVCLCHGFPESWYSWRYQIPALAQAGYRVLAMDMKGYGESSAPPEIEEYCMEVLCKEMVTFLDKLGLSQAVFIGHDWGGMLVWYMALFYPERVRAVASLNTPFIPANPNMSPLESIKANPVFDYQLYFQEPGVAEAELEQNLSRTFKSLFRASDESVLSMHKVCEAGGLFVNSPEEPSLSRMVTEEEIQFYVQQFKKSGFRGPLNWYRNMERNWKWACKSLGRKILIPALMVTAEKDFVLVPQMSQHMEDWIPHLKRGHIEDCGHWTQMDKPTEVNQILIKWLDSDARNPPVVSKM

Gene
EPHX2
Protein
Bifunctional epoxide hydrolase 2
Organism
Sus scrofa
Length
555 amino acids
Function
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).
Similarity
Belongs to the AB hydrolase superfamily. Epoxide hydrolase family.
Mass
62.767 kDa
Sequence
MALRAAVFDLDGVLALPSITTSWARAEEKLALPRGFLNEAFKKGGQDGSVARVMTGEITFSQWVPFMEEDCRKCAEDSGIRLPENFSVKHIFDKALSEKKINYPMLQAALTLKKKGFSTCILTNNWLDDSAQRGSRAQLMCELRPHFDFLIESCRVGMAKPDPQIYKLMLDTLKAEPNEVVFLDDVGTHLKPVRDLGMATILVRDTDTALRELEKVTGVQLLQTPALPPTSCDPSALSHGYVLIKPGVRLHFVEMGSGPAVCLCHGFPESWFSWRYQIPALAQAGFRVLAVDMKGYGESSAPPEIEEYSLEVLCKDMVTFLNKLGLSQAVFIGHDWGGVLVWNMALFYPERVRAVASLNTPFMPSNPNVSPMEIIKANPVFDYQLYFQEPGVAEAELEQNLDRTFKNFFRAHDETFLTTNRVRELGGLFVGTPEEPSLSRLVTEEDIQFYVQQFKKSGFRGPLNWYRNMERNWQWGCKGSGRKILIPALMVTAENDLVLHPKMSKHMENWIPHLKRGHIKDCGHWTQIDKPAELNRILIEWLETDARNPLVDSKL

Gene
Ephx2
Protein
Bifunctional epoxide hydrolase 2
Organism
Mus musculus
Length
554 amino acids
Function
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 and 12-phosphonooxy-octadec-9E-enoic acid.
Similarity
Belongs to the AB hydrolase superfamily. Epoxide hydrolase family.
Mass
62.515 kDa
Sequence
MALRVAAFDLDGVLALPSIAGAFRRSEEALALPRDFLLGAYQTEFPEGPTEQLMKGKITFSQWVPLMDESYRKSSKACGANLPENFSISQIFSQAMAARSINRPMLQAAIALKKKGFTTCIVTNNWLDDGDKRDSLAQMMCELSQHFDFLIESCQVGMIKPEPQIYNFLLDTLKAKPNEVVFLDDFGSNLKPARDMGMVTILVHNTASALRELEKVTGTQFPEAPLPVPCNPNDVSHGYVTVKPGIRLHFVEMGSGPALCLCHGFPESWFSWRYQIPALAQAGFRVLAIDMKGYGDSSSPPEIEEYAMELLCKEMVTFLDKLGIPQAVFIGHDWAGVMVWNMALFYPERVRAVASLNTPFMPPDPDVSPMKVIRSIPVFNYQLYFQEPGVAEAELEKNMSRTFKSFFRASDETGFIAVHKATEIGGILVNTPEDPNLSKITTEEEIEFYIQQFKKTGFRGPLNWYRNTERNWKWSCKGLGRKILVPALMVTAEKDIVLRPEMSKNMEKWIPFLKRGHIEDCGHWTQIEKPTEVNQILIKWLQTEVQNPSVTSKI

Gene
Ephx2
Protein
Bifunctional epoxide hydrolase 2
Organism
Rattus norvegicus
Length
554 amino acids
Function
Bifunctional enzyme (PubMed:8626766, PubMed:12574508). 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).
Similarity
Belongs to the AB hydrolase superfamily. Epoxide hydrolase family.
Mass
62.34 kDa
Sequence
MALRVAAFDLDGVLALPSIAGVLRHTEEALALPRDFLLGAFQMKFPEGPTEQLMKGKITFSQWVPLMDESCRKSSKACGASLPENFSISEIFSQAMAARSINRPMLQAAAALKKKGFTTCIVTNNWLDDSDKRDILAQMMCELSQHFDFLIESCQVGMIKPEPQIYKFVLDTLKAKPNEVVFLDDFGSNLKPARDMGMVTILVRDTASALRELEKVTGTQFPEAPLPVPCSPNDVSHGYVTVKPGIRLHFVEMGSGPAICLCHGFPESWFSWRYQIPALAQAGFRVLAIDMKGYGDSSSPPEIEEYAMELLCEEMVTFLNKLGIPQAVFIGHDWAGVLVWNMALFHPERVRAVASLNTPLMPPNPEVSPMEVIRSIPVFNYQLYFQEPGVAEAELEKNMSRTFKSFFRTSDDMGLLTVNKATEMGGILVGTPEDPKVSKITTEEEIEYYIQQFKKSGFRGPLNWYRNTERNWKWSCKALGRKILVPALMVTAEKDIVLRPEMSKNMENWIPFLKRGHIEDCGHWTQIEKPAEVNQILIKWLKTEIQNPSVTSKI

Gene
Ephx2
Protein
Bifunctional epoxide hydrolase 2
Organism
Mus musculus
Length
554 amino acids
Function
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 and 12-phosphonooxy-octadec-9E-enoic acid.
Similarity
Belongs to the AB hydrolase superfamily. Epoxide hydrolase family.
Mass
62.515 kDa
Sequence
MALRVAAFDLDGVLALPSIAGAFRRSEEALALPRDFLLGAYQTEFPEGPTEQLMKGKITFSQWVPLMDESYRKSSKACGANLPENFSISQIFSQAMAARSINRPMLQAAIALKKKGFTTCIVTNNWLDDGDKRDSLAQMMCELSQHFDFLIESCQVGMIKPEPQIYNFLLDTLKAKPNEVVFLDDFGSNLKPARDMGMVTILVHNTASALRELEKVTGTQFPEAPLPVPCNPNDVSHGYVTVKPGIRLHFVEMGSGPALCLCHGFPESWFSWRYQIPALAQAGFRVLAIDMKGYGDSSSPPEIEEYAMELLCKEMVTFLDKLGIPQAVFIGHDWAGVMVWNMALFYPERVRAVASLNTPFMPPDPDVSPMKVIRSIPVFNYQLYFQEPGVAEAELEKNMSRTFKSFFRASDETGFIAVHKATEIGGILVNTPEDPNLSKITTEEEIEFYIQQFKKTGFRGPLNWYRNTERNWKWSCKGLGRKILVPALMVTAEKDIVLRPEMSKNMEKWIPFLKRGHIEDCGHWTQIEKPTEVNQILIKWLQTEVQNPSVTSKI

Gene
Ephx2
Protein
Bifunctional epoxide hydrolase 2
Organism
Rattus norvegicus
Length
554 amino acids
Function
Bifunctional enzyme (PubMed:8626766, PubMed:12574508). 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).
Similarity
Belongs to the AB hydrolase superfamily. Epoxide hydrolase family.
Mass
62.34 kDa
Sequence
MALRVAAFDLDGVLALPSIAGVLRHTEEALALPRDFLLGAFQMKFPEGPTEQLMKGKITFSQWVPLMDESCRKSSKACGASLPENFSISEIFSQAMAARSINRPMLQAAAALKKKGFTTCIVTNNWLDDSDKRDILAQMMCELSQHFDFLIESCQVGMIKPEPQIYKFVLDTLKAKPNEVVFLDDFGSNLKPARDMGMVTILVRDTASALRELEKVTGTQFPEAPLPVPCSPNDVSHGYVTVKPGIRLHFVEMGSGPAICLCHGFPESWFSWRYQIPALAQAGFRVLAIDMKGYGDSSSPPEIEEYAMELLCEEMVTFLNKLGIPQAVFIGHDWAGVLVWNMALFHPERVRAVASLNTPLMPPNPEVSPMEVIRSIPVFNYQLYFQEPGVAEAELEKNMSRTFKSFFRTSDDMGLLTVNKATEMGGILVGTPEDPKVSKITTEEEIEYYIQQFKKSGFRGPLNWYRNTERNWKWSCKALGRKILVPALMVTAEKDIVLRPEMSKNMENWIPFLKRGHIEDCGHWTQIEKPAEVNQILIKWLKTEIQNPSVTSKI