ID   E5RFU2_HUMAN            Unreviewed;       523 AA.
AC   E5RFU2;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   02-SEP-2026, entry version 87.
DE   RecName: Full=Bifunctional epoxide hydrolase 2 {ECO:0000256|ARBA:ARBA00072563};
DE            EC=3.1.3.76 {ECO:0000256|ARBA:ARBA00066597};
DE            EC=3.3.2.10 {ECO:0000256|ARBA:ARBA00013006};
GN   Name=EPHX2 {ECO:0000313|Ensembl:ENSP00000427956.1};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000427956.1, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0000313|Ensembl:ENSP00000427956.1, ECO:0000313|Proteomes:UP000005640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11237011; DOI=10.1038/35057062;
RG   International Human Genome Sequencing Consortium;
RA   Lander E.S., Linton L.M., Birren B., Nusbaum C., Zody M.C., Baldwin J.,
RA   Devon K., Dewar K., Doyle M., FitzHugh W., Funke R., Gage D., Harris K.,
RA   Heaford A., Howland J., Kann L., Lehoczky J., LeVine R., McEwan P.,
RA   McKernan K., Meldrim J., Mesirov J.P., Miranda C., Morris W., Naylor J.,
RA   Raymond C., Rosetti M., Santos R., Sheridan A., Sougnez C.,
RA   Stange-Thomann N., Stojanovic N., Subramanian A., Wyman D., Rogers J.,
RA   Sulston J., Ainscough R., Beck S., Bentley D., Burton J., Clee C.,
RA   Carter N., Coulson A., Deadman R., Deloukas P., Dunham A., Dunham I.,
RA   Durbin R., French L., Grafham D., Gregory S., Hubbard T., Humphray S.,
RA   Hunt A., Jones M., Lloyd C., McMurray A., Matthews L., Mercer S., Milne S.,
RA   Mullikin J.C., Mungall A., Plumb R., Ross M., Shownkeen R., Sims S.,
RA   Waterston R.H., Wilson R.K., Hillier L.W., McPherson J.D., Marra M.A.,
RA   Mardis E.R., Fulton L.A., Chinwalla A.T., Pepin K.H., Gish W.R.,
RA   Chissoe S.L., Wendl M.C., Delehaunty K.D., Miner T.L., Delehaunty A.,
RA   Kramer J.B., Cook L.L., Fulton R.S., Johnson D.L., Minx P.J., Clifton S.W.,
RA   Hawkins T., Branscomb E., Predki P., Richardson P., Wenning S., Slezak T.,
RA   Doggett N., Cheng J.F., Olsen A., Lucas S., Elkin C., Uberbacher E.,
RA   Frazier M., Gibbs R.A., Muzny D.M., Scherer S.E., Bouck J.B.,
RA   Sodergren E.J., Worley K.C., Rives C.M., Gorrell J.H., Metzker M.L.,
RA   Naylor S.L., Kucherlapati R.S., Nelson D.L., Weinstock G.M., Sakaki Y.,
RA   Fujiyama A., Hattori M., Yada T., Toyoda A., Itoh T., Kawagoe C.,
RA   Watanabe H., Totoki Y., Taylor T., Weissenbach J., Heilig R., Saurin W.,
RA   Artiguenave F., Brottier P., Bruls T., Pelletier E., Robert C., Wincker P.,
RA   Smith D.R., Doucette-Stamm L., Rubenfield M., Weinstock K., Lee H.M.,
RA   Dubois J., Rosenthal A., Platzer M., Nyakatura G., Taudien S., Rump A.,
RA   Yang H., Yu J., Wang J., Huang G., Gu J., Hood L., Rowen L., Madan A.,
RA   Qin S., Davis R.W., Federspiel N.A., Abola A.P., Proctor M.J., Myers R.M.,
RA   Schmutz J., Dickson M., Grimwood J., Cox D.R., Olson M.V., Kaul R.,
RA   Raymond C., Shimizu N., Kawasaki K., Minoshima S., Evans G.A.,
RA   Athanasiou M., Schultz R., Roe B.A., Chen F., Pan H., Ramser J.,
RA   Lehrach H., Reinhardt R., McCombie W.R., de la Bastide M., Dedhia N.,
RA   Blocker H., Hornischer K., Nordsiek G., Agarwala R., Aravind L.,
RA   Bailey J.A., Bateman A., Batzoglou S., Birney E., Bork P., Brown D.G.,
RA   Burge C.B., Cerutti L., Chen H.C., Church D., Clamp M., Copley R.R.,
RA   Doerks T., Eddy S.R., Eichler E.E., Furey T.S., Galagan J., Gilbert J.G.,
RA   Harmon C., Hayashizaki Y., Haussler D., Hermjakob H., Hokamp K., Jang W.,
RA   Johnson L.S., Jones T.A., Kasif S., Kaspryzk A., Kennedy S., Kent W.J.,
RA   Kitts P., Koonin E.V., Korf I., Kulp D., Lancet D., Lowe T.M.,
RA   McLysaght A., Mikkelsen T., Moran J.V., Mulder N., Pollara V.J.,
RA   Ponting C.P., Schuler G., Schultz J., Slater G., Smit A.F., Stupka E.,
RA   Szustakowski J., Thierry-Mieg D., Thierry-Mieg J., Wagner L., Wallis J.,
RA   Wheeler R., Williams A., Wolf Y.I., Wolfe K.H., Yang S.P., Yeh R.F.,
RA   Collins F., Guyer M.S., Peterson J., Felsenfeld A., Wetterstrand K.A.,
RA   Patrinos A., Morgan M.J., de Jong P., Catanese J.J., Osoegawa K.,
RA   Shizuya H., Choi S., Chen Y.J.;
RT   "Initial sequencing and analysis of the human genome.";
RL   Nature 409:860-921(2001).
RN   [2] {ECO:0000313|Ensembl:ENSP00000427956.1, ECO:0000313|Proteomes:UP000005640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15496913; DOI=10.1038/nature03001;
RG   International Human Genome Sequencing Consortium;
RT   "Finishing the euchromatic sequence of the human genome.";
RL   Nature 431:931-945(2004).
RN   [3] {ECO:0000313|Ensembl:ENSP00000427956.1, ECO:0000313|Proteomes:UP000005640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16421571; DOI=10.1038/nature04406;
RA   Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA   Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA   Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA   Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA   Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L.III.,
RA   Engels R., Glockner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA   Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA   Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA   Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA   O'Neill K., Parker S.C., Polley A., Raymond C.K., Reichwald K.,
RA   Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA   Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA   Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA   Platzer M., Shimizu N., Lander E.S.;
RT   "DNA sequence and analysis of human chromosome 8.";
RL   Nature 439:331-335(2006).
RN   [4] {ECO:0007829|PubMed:19608861}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [5] {ECO:0007829|PubMed:21269460}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Burckstummer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [6] {ECO:0007829|PubMed:24275569}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [7] {ECO:0000313|Ensembl:ENSP00000427956.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JAN-2026) to UniProtKB.
CC   -!- FUNCTION: Bifunctional enzyme. The C-terminal domain has epoxide
CC       hydrolase activity and acts on epoxides (alkene oxides, oxiranes) and
CC       arene oxides. Plays a role in xenobiotic metabolism by degrading
CC       potentially toxic epoxides. Also determines steady-state levels of
CC       physiological mediators. {ECO:0000256|ARBA:ARBA00056125}.
CC   -!- FUNCTION: Bifunctional enzyme. The N-terminal domain has lipid
CC       phosphatase activity, with the highest activity towards threo-9,10-
CC       phosphonooxy-hydroxy-octadecanoic acid, followed by erythro-9,10-
CC       phosphonooxy-hydroxy-octadecanoic acid, 12-phosphonooxy-octadec-9Z-
CC       enoic acid and 12-phosphonooxy-octadec-9E-enoic acid. Has phosphatase
CC       activity toward lyso-glycerophospholipids with also some lower activity
CC       toward lysolipids of sphingolipid and isoprenoid phosphates.
CC       {ECO:0000256|ARBA:ARBA00056280}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(11R,12S)-epoxy-(5Z,8Z,14Z)-eicosatrienoate + H2O = (11R,12R)-
CC         dihydroxy-(5Z,8Z,14Z)-eicosatrienoate; Xref=Rhea:RHEA:54000,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:131970, ChEBI:CHEBI:138004;
CC         Evidence={ECO:0000256|ARBA:ARBA00050196};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54001;
CC         Evidence={ECO:0000256|ARBA:ARBA00050196};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(11R,12S)-epoxy-(5Z,8Z,14Z)-eicosatrienoate + H2O = (11S,12S)-
CC         dihydroxy-(5Z,8Z,14Z)-eicosatrienoate; Xref=Rhea:RHEA:54004,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:131970, ChEBI:CHEBI:138005;
CC         Evidence={ECO:0000256|ARBA:ARBA00050975};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54005;
CC         Evidence={ECO:0000256|ARBA:ARBA00050975};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(11S,12R)-epoxy-(5Z,8Z,14Z)-eicosatrienoate + H2O = (11R,12R)-
CC         dihydroxy-(5Z,8Z,14Z)-eicosatrienoate; Xref=Rhea:RHEA:53980,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:131969, ChEBI:CHEBI:138004;
CC         Evidence={ECO:0000256|ARBA:ARBA00051095};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53981;
CC         Evidence={ECO:0000256|ARBA:ARBA00051095};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(11S,12R)-epoxy-(5Z,8Z,14Z)-eicosatrienoate + H2O = (11S,12S)-
CC         dihydroxy-(5Z,8Z,14Z)-eicosatrienoate; Xref=Rhea:RHEA:53984,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:131969, ChEBI:CHEBI:138005;
CC         Evidence={ECO:0000256|ARBA:ARBA00051491};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53985;
CC         Evidence={ECO:0000256|ARBA:ARBA00051491};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(14R,15S)-epoxy-(5Z,8Z,11Z)-eicosatrienoate + H2O = (14R,15R)-
CC         dihydroxy-(5Z,8Z,11Z)-eicosatrienoate; Xref=Rhea:RHEA:53976,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:131965, ChEBI:CHEBI:138003;
CC         Evidence={ECO:0000256|ARBA:ARBA00052977};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53977;
CC         Evidence={ECO:0000256|ARBA:ARBA00052977};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(14S,15R)-epoxy-(5Z,8Z,11Z)-eicosatrienoate + H2O = (14R,15R)-
CC         dihydroxy-(5Z,8Z,11Z)-eicosatrienoate; Xref=Rhea:RHEA:53992,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:131964, ChEBI:CHEBI:138003;
CC         Evidence={ECO:0000256|ARBA:ARBA00052898};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53993;
CC         Evidence={ECO:0000256|ARBA:ARBA00052898};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(14S,15R)-epoxy-(5Z,8Z,11Z)-eicosatrienoate + H2O = (14S,15S)-
CC         dihydroxy-(5Z,8Z,11Z)-eicosatrienoate; Xref=Rhea:RHEA:53996,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:131964, ChEBI:CHEBI:138006;
CC         Evidence={ECO:0000256|ARBA:ARBA00051997};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53997;
CC         Evidence={ECO:0000256|ARBA:ARBA00051997};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(8S,9R)-epoxy-(5Z,11Z,14Z)-eicosatrienoate + H2O = (8R,9R)-
CC         dihydroxy-(5Z,11Z,14Z)-eicosatrienoate; Xref=Rhea:RHEA:54016,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:131974, ChEBI:CHEBI:138008;
CC         Evidence={ECO:0000256|ARBA:ARBA00051985};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54017;
CC         Evidence={ECO:0000256|ARBA:ARBA00051985};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(8S,9R)-epoxy-(5Z,11Z,14Z)-eicosatrienoate + H2O = (8S,9S)-
CC         dihydroxy-(5Z,11Z,14Z)-eicosatrienoate; Xref=Rhea:RHEA:53972,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:131974, ChEBI:CHEBI:138002;
CC         Evidence={ECO:0000256|ARBA:ARBA00050509};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53973;
CC         Evidence={ECO:0000256|ARBA:ARBA00050509};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9S,10S)-10-hydroxy-9-(phosphooxy)octadecanoate + H2O =
CC         (9S,10S)-9,10-dihydroxyoctadecanoate + phosphate;
CC         Xref=Rhea:RHEA:16537, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58796, ChEBI:CHEBI:58797; EC=3.1.3.76;
CC         Evidence={ECO:0000256|ARBA:ARBA00051289};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate +
CC         H2O = 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol + phosphate;
CC         Xref=Rhea:RHEA:53600, ChEBI:CHEBI:15377, ChEBI:CHEBI:34071,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:74938;
CC         Evidence={ECO:0000256|ARBA:ARBA00052983};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53601;
CC         Evidence={ECO:0000256|ARBA:ARBA00052983};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 1-(9Z-
CC         octadecenoyl)-sn-glycerol + phosphate; Xref=Rhea:RHEA:39835,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:74544,
CC         ChEBI:CHEBI:75757; Evidence={ECO:0000256|ARBA:ARBA00000235};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39836;
CC         Evidence={ECO:0000256|ARBA:ARBA00000235};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-sn-glycero-3-phosphate + H2O = 1-hexadecanoyl-
CC         sn-glycerol + phosphate; Xref=Rhea:RHEA:53604, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57518, ChEBI:CHEBI:75542;
CC         Evidence={ECO:0000256|ARBA:ARBA00052278};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53605;
CC         Evidence={ECO:0000256|ARBA:ARBA00052278};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-octadecanoyl-sn-glycero-3-phosphate + H2O = 1-octadecanoyl-
CC         sn-glycerol + phosphate; Xref=Rhea:RHEA:53596, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:74565, ChEBI:CHEBI:75550;
CC         Evidence={ECO:0000256|ARBA:ARBA00051948};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53597;
CC         Evidence={ECO:0000256|ARBA:ARBA00051948};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-tetradecanoyl-sn-glycerol 3-phosphate + H2O = 1-
CC         tetradecanoyl-sn-glycerol + phosphate; Xref=Rhea:RHEA:53592,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:72683,
CC         ChEBI:CHEBI:75536; Evidence={ECO:0000256|ARBA:ARBA00052782};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53593;
CC         Evidence={ECO:0000256|ARBA:ARBA00052782};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=10-hydroxy-(11S,12S)-epoxy- (5Z,8Z,14Z)-eicosatrienoate + H2O
CC         = (10,11S,12R)-trihydroxy-(5Z,8Z,14Z)-eicosatrienoate;
CC         Xref=Rhea:RHEA:50900, ChEBI:CHEBI:15377, ChEBI:CHEBI:78084,
CC         ChEBI:CHEBI:78099; Evidence={ECO:0000256|ARBA:ARBA00052784};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50901;
CC         Evidence={ECO:0000256|ARBA:ARBA00052784};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=11,12-epoxy-(5Z,8Z,14Z)-eicosatrienoate + H2O = 11,12-
CC         dihydroxy-(5Z,8Z,14Z)-eicosatrienoate; Xref=Rhea:RHEA:44044,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:76625, ChEBI:CHEBI:84031;
CC         Evidence={ECO:0000256|ARBA:ARBA00000146};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44045;
CC         Evidence={ECO:0000256|ARBA:ARBA00000146};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=12-(phosphooxy)octadecanoate + H2O = 12-hydroxyoctadecanoate +
CC         phosphate; Xref=Rhea:RHEA:45280, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:84201, ChEBI:CHEBI:85134;
CC         Evidence={ECO:0000256|ARBA:ARBA00050963};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45281;
CC         Evidence={ECO:0000256|ARBA:ARBA00050963};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=12-phosphooxy-(9E)-octadecenoate + H2O = 12-hydroxy-(9E)-
CC         octadecenoate + phosphate; Xref=Rhea:RHEA:45276, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:85137, ChEBI:CHEBI:85152;
CC         Evidence={ECO:0000256|ARBA:ARBA00052939};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45277;
CC         Evidence={ECO:0000256|ARBA:ARBA00052939};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=12-phosphooxy-(9Z)-octadecenoate + H2O = 12-hydroxy-(9Z)-
CC         octadecenoate + phosphate; Xref=Rhea:RHEA:45272, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:85141, ChEBI:CHEBI:85150;
CC         Evidence={ECO:0000256|ARBA:ARBA00052672};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45273;
CC         Evidence={ECO:0000256|ARBA:ARBA00052672};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=14,15-epoxy-(5Z,8Z,11Z)-eicosatrienoate + H2O = 14,15-
CC         dihydroxy-(5Z,8Z,11Z)-eicosatrienoate; Xref=Rhea:RHEA:44040,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:84024, ChEBI:CHEBI:84029;
CC         Evidence={ECO:0000256|ARBA:ARBA00051246};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44041;
CC         Evidence={ECO:0000256|ARBA:ARBA00051246};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=8,9-epoxy-(5Z,11Z,14Z)-eicosatrienoate + H2O = 8,9-dihydroxy-
CC         (5Z,11Z,14Z)-eicosatrienoate; Xref=Rhea:RHEA:44048,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:84025, ChEBI:CHEBI:84032;
CC         Evidence={ECO:0000256|ARBA:ARBA00001899};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44049;
CC         Evidence={ECO:0000256|ARBA:ARBA00001899};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=8-hydroxy-(11S,12S)-epoxy-(5Z,9E,14Z)-eicosatrienoate + H2O =
CC         (8,11R,12S)-trihydroxy-(5Z,9E,14Z)-eicosatrienoate;
CC         Xref=Rhea:RHEA:50896, ChEBI:CHEBI:15377, ChEBI:CHEBI:78100,
CC         ChEBI:CHEBI:132127; Evidence={ECO:0000256|ARBA:ARBA00052193};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50897;
CC         Evidence={ECO:0000256|ARBA:ARBA00052193};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=9,10-epoxy-(12Z)-octadecenoate + H2O = 9,10-dihydroxy-(12Z)-
CC         octadecenoate; Xref=Rhea:RHEA:44032, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:84023, ChEBI:CHEBI:84027;
CC         Evidence={ECO:0000256|ARBA:ARBA00051902};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44033;
CC         Evidence={ECO:0000256|ARBA:ARBA00051902};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an epoxide + H2O = an ethanediol; Xref=Rhea:RHEA:19037,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:32955, ChEBI:CHEBI:140594;
CC         EC=3.3.2.10; Evidence={ECO:0000256|ARBA:ARBA00001268};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Epoxide hydrolase
CC       family. {ECO:0000256|ARBA:ARBA00038334}.
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DR   EMBL; AF311103; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001400948.1; NM_001414019.1.
DR   AlphaFoldDB; E5RFU2; -.
DR   SMR; E5RFU2; -.
DR   MassIVE; E5RFU2; -.
DR   ProteomicsDB; 15458; -.
DR   Antibodypedia; 4070; 442 antibodies from 37 providers.
DR   Ensembl; ENST00000518379.5; ENSP00000427956.1; ENSG00000120915.16.
DR   GeneID; 2053; -.
DR   UCSC; uc064lll.1; human.
DR   CTD; 2053; -.
DR   HGNC; HGNC:3402; EPHX2.
DR   VEuPathDB; HostDB:ENSG00000120915; -.
DR   GeneTree; ENSGT00940000158614; -.
DR   OrthoDB; 408373at2759; -.
DR   ChiTaRS; EPHX2; human.
DR   Proteomes; UP000005640; Chromosome 8.
DR   Bgee; ENSG00000120915; Expressed in right lobe of liver and 129 other cell types or tissues.
DR   ExpressionAtlas; E5RFU2; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0033885; F:10-hydroxy-9-(phosphonooxy)octadecanoate phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004301; F:epoxide hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0097176; P:epoxide metabolic process; IEA:UniProtKB-ARBA.
DR   CDD; cd02603; HAD_sEH-N_like; 1.
DR   FunFam; 1.10.150.240:FF:000011; Bifunctional epoxide hydrolase 2; 1.
DR   FunFam; 3.40.50.1820:FF:000067; Bifunctional epoxide hydrolase 2; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   Gene3D; 1.10.150.240; Putative phosphatase, domain 2; 1.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR029058; AB_hydrolase_fold.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006439; HAD-SF_hydro_IA.
DR   InterPro; IPR011945; HAD-SF_ppase_IA/epoxid_hydro_N.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR023198; PGP-like_dom2.
DR   NCBIfam; TIGR02247; HAD-1A3-hyp; 1.
DR   NCBIfam; TIGR01509; HAD-SF-IA-v3; 1.
DR   PANTHER; PTHR43329; EPOXIDE HYDROLASE; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00111; ABHYDROLASE.
DR   PRINTS; PR00413; HADHALOGNASE.
DR   SFLD; SFLDG01130; C1.5.1:_Epoxide_Hydrolase_Phos; 1.
DR   SFLD; SFLDG01129; C1.5:_HAD__Beta-PGM__Phosphata; 1.
DR   SFLD; SFLDF00040; epoxide_hydrolase_n-terminal_p; 1.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
PE   1: Evidence at protein level;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Aromatic hydrocarbons catabolism {ECO:0000256|ARBA:ARBA00022797};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Detoxification {ECO:0000256|ARBA:ARBA00022575};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:E5RFU2,
KW   ECO:0007829|ProteomicsDB:E5RFU2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640}.
FT   DOMAIN          246..499
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF00561"
SQ   SEQUENCE   523 AA;  58855 MW;  DD9880A21053CCB3 CRC64;
     MTLRAAVFDL DGVLALPAVF GVLGRTEEAL ALPRGLLNDA FQKGGPEGAT TRLMKGEITL
     SQWIPLMEEN CRKCSETAKV CLPKNFSIKE IFDKAISARK INRPMLQAAL MLRKKGFTTA
     ILTNTWLDDR AERDGLAQLM CELKMHFDFL IESCQVGMVK PEPQIYKFLL DTLKASPSEV
     VFLDDIGANL KPARDLGMVT ILVQDTDTAL KELEKVTGIQ LLNTPAPLPT SCNPSDMSHG
     YVTVKIPALA QAGYRVLAMD MKGYGESSAP PEIEEYCMEV LCKEMVTFLD KLGLSQAVFI
     GHDWGGMLVW YMALFYPERV RAVASLNTPF IPANPNMSPL ESIKANPVFD YQLYFQEPGV
     AEAELEQNLS RTFKSLFRAS DESVLSMHKV CEAGGLFVNS PEEPSLSRMV TEEEIQFYVQ
     QFKKSGFRGP LNWYRNMERN WKWACKSLGR KILIPALMVT AEKDFVLVPQ MSQHMEDWIP
     HLKRGHIEDC GHWTQMDKPT EVNQILIKWL DSDARNPPVV SKM
//