ID   HYES_MOUSE              Reviewed;         554 AA.
AC   P34914; Q8CGV0;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   24-JAN-2024, entry version 198.
DE   RecName: Full=Bifunctional epoxide hydrolase 2 {ECO:0000305};
DE   Includes:
DE     RecName: Full=Cytosolic epoxide hydrolase 2;
DE              Short=CEH;
DE              EC=3.3.2.10 {ECO:0000269|PubMed:21217101};
DE     AltName: Full=Epoxide hydratase;
DE     AltName: Full=Soluble epoxide hydrolase {ECO:0000303|PubMed:21217101};
DE              Short=SEH {ECO:0000303|PubMed:21217101};
DE   Includes:
DE     RecName: Full=Lipid-phosphate phosphatase;
DE              EC=3.1.3.76 {ECO:0000250|UniProtKB:P34913};
GN   Name=Ephx2 {ECO:0000312|MGI:MGI:99500}; Synonyms=Eph2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, AND
RP   INDUCTION.
RC   TISSUE=Liver;
RX   PubMed=8349642; DOI=10.1016/s0021-9258(19)85378-4;
RA   Grant D.F., Storms D.H., Hammock B.D.;
RT   "Molecular cloning and expression of murine liver soluble epoxide
RT   hydrolase.";
RL   J. Biol. Chem. 268:17628-17633(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND INDUCTION.
RC   STRAIN=NMRI;
RX   PubMed=8750907; DOI=10.1007/s002040050250;
RA   Johansson C., Stark A., Sandberg M., Ek B., Rask L., Meijer J.;
RT   "Tissue specific basal expression of soluble murine epoxide hydrolase and
RT   effects of clofibrate on the mRNA levels in extrahepatic tissues and
RT   liver.";
RL   Arch. Toxicol. 70:61-63(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND INDUCTION.
RC   STRAIN=C57BL/6J;
RX   PubMed=15601917; DOI=10.1095/biolreprod.104.035899;
RA   Hennebold J.D., Mah K., Perez W., Vance J.E., Stouffer R.L., Morisseau C.,
RA   Hammock B.D., Adashi E.Y.;
RT   "Identification and characterization of an ovary-selective isoform of
RT   epoxide hydrolase.";
RL   Biol. Reprod. 72:968-975(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=7840649; DOI=10.1006/abbi.1995.1059;
RA   Zeldin D.C., Wei S., Falck J.R., Hammock B.D., Snapper J.R.,
RA   Capdevila J.H.;
RT   "Metabolism of epoxyeicosatrienoic acids by cytosolic epoxide hydrolase:
RT   substrate structural determinants of asymmetric catalysis.";
RL   Arch. Biochem. Biophys. 316:443-451(1995).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-368, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-368, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [8]
RP   FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP   TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=21217101; DOI=10.1194/jlr.m009639;
RA   Cronin A., Decker M., Arand M.;
RT   "Mammalian soluble epoxide hydrolase is identical to liver hepoxilin
RT   hydrolase.";
RL   J. Lipid Res. 52:712-719(2011).
RN   [9]
RP   SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-55; LYS-176; LYS-371; LYS-420;
RP   LYS-454; LYS-504; LYS-508 AND LYS-553, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
RN   [10]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-176; LYS-191; LYS-215 AND
RP   LYS-508, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA   Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA   Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT   "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT   identifies substrates of SIRT3 in metabolic pathways.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), AND ACTIVE SITE.
RC   TISSUE=Liver;
RX   PubMed=10485878; DOI=10.1073/pnas.96.19.10637;
RA   Argiriadi M.A., Morisseau C., Hammock B.D., Christianson D.W.;
RT   "Detoxification of environmental mutagens and carcinogens: structure,
RT   mechanism, and evolution of liver epoxide hydrolase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:10637-10642(1999).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH EPOXIDE HYDROLASE
RP   INHIBITOR, AND ACTIVE SITE.
RX   PubMed=10747889; DOI=10.1074/jbc.m000278200;
RA   Argiriadi M.A., Morisseau C., Goodrow M.H., Dowdy D.L., Hammock B.D.,
RA   Christianson D.W.;
RT   "Binding of alkylurea inhibitors to epoxide hydrolase implicates active
RT   site tyrosines in substrate activation.";
RL   J. Biol. Chem. 275:15265-15270(2000).
CC   -!- FUNCTION: Bifunctional enzyme. The C-terminal domain has epoxide
CC       hydrolase activity and acts on epoxides (alkene oxides, oxiranes) and
CC       arene oxides (PubMed:7840649, PubMed:21217101). Plays a role in
CC       xenobiotic metabolism by degrading potentially toxic epoxides (By
CC       similarity). Also determines steady-state levels of physiological
CC       mediators (By similarity). {ECO:0000250|UniProtKB:P34913,
CC       ECO:0000250|UniProtKB:P80299, ECO:0000269|PubMed:21217101,
CC       ECO:0000269|PubMed:7840649}.
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 (By similarity).
CC       Has phosphatase activity toward lyso-glycerophospholipids with also
CC       some lower activity toward lysolipids of sphingolipid and isoprenoid
CC       phosphates (By similarity). {ECO:0000250|UniProtKB:P34913}.
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:0000250|UniProtKB:P34913};
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:0000250|UniProtKB:P34913};
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:0000269|PubMed:21217101};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50897;
CC         Evidence={ECO:0000269|PubMed:21217101};
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:0000269|PubMed:21217101};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50901;
CC         Evidence={ECO:0000269|PubMed:21217101};
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:0000269|PubMed:7840649};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53973;
CC         Evidence={ECO:0000305|PubMed:7840649};
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:0000269|PubMed:7840649};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53981;
CC         Evidence={ECO:0000305|PubMed:7840649};
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:0000269|PubMed:7840649};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53985;
CC         Evidence={ECO:0000305|PubMed:7840649};
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:0000269|PubMed:7840649};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53993;
CC         Evidence={ECO:0000305|PubMed:7840649};
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:0000269|PubMed:7840649};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53997;
CC         Evidence={ECO:0000305|PubMed:7840649};
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:0000269|PubMed:7840649};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54005;
CC         Evidence={ECO:0000305|PubMed:7840649};
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:0000269|PubMed:7840649};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54001;
CC         Evidence={ECO:0000305|PubMed:7840649};
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:0000269|PubMed:7840649};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54017;
CC         Evidence={ECO:0000305|PubMed:7840649};
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:0000250|UniProtKB:P34913};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45273;
CC         Evidence={ECO:0000250|UniProtKB:P34913};
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:0000250|UniProtKB:P34913};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45277;
CC         Evidence={ECO:0000250|UniProtKB:P34913};
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:0000250|UniProtKB:P34913};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45281;
CC         Evidence={ECO:0000250|UniProtKB:P34913};
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:0000250|UniProtKB:P34913};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44049;
CC         Evidence={ECO:0000250|UniProtKB:P34913};
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:0000250|UniProtKB:P34913};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44045;
CC         Evidence={ECO:0000250|UniProtKB:P34913};
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:0000250|UniProtKB:P34913};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44041;
CC         Evidence={ECO:0000250|UniProtKB:P34913};
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:0000250|UniProtKB:P34913};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44033;
CC         Evidence={ECO:0000250|UniProtKB:P34913};
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:0000250|UniProtKB:P34913};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53593;
CC         Evidence={ECO:0000250|UniProtKB:P34913};
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:0000250|UniProtKB:P34913};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53597;
CC         Evidence={ECO:0000250|UniProtKB:P34913};
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:0000250|UniProtKB:P34913};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53601;
CC         Evidence={ECO:0000250|UniProtKB:P34913};
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:0000250|UniProtKB:P34913};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53605;
CC         Evidence={ECO:0000250|UniProtKB:P34913};
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:0000250|UniProtKB:P34913};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39836;
CC         Evidence={ECO:0000250|UniProtKB:P34913};
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:0000269|PubMed:7840649};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53977;
CC         Evidence={ECO:0000305|PubMed:7840649};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P34913};
CC   -!- ACTIVITY REGULATION: Inhibited by 1-(1-acetylpiperidin-4-yl)-3-(4-
CC       (trifl uoromethoxy)phenyl)urea (TPAU), 1-cyclohexyl-3-dodecylurea
CC       (CDU), 12-(3-adamantan-1-yl-ureido)-dodecanoic acid (AUDA), 1-((3S, 5S,
CC       7S)-adamantan-1-yl)-3-(5-(2-(2-ethoxyethoxy) ethoxy)pentyl)urea (AEPU),
CC       N-adamantyl-N[']-cyclohexyl urea (ACU), 4-(((1S, 4S)-4-(3-((3S, 5S,
CC       7S)-adamantan-1-yl) ureido)cyclohexyl)oxy)benzoic acid (c-AUCB), 4-
CC       (((1R, 4R)-4-(3-((3S, 5S, 7S)-adamantan-1-
CC       yl)ureido)cyclohexyl)oxy)benzoic acid (t-AUCB), 4-(((1R, 4R)-4-(3-
CC       (4(trifluoromethoxy)phenyl)ureido)cyclohexyl)oxy)benzoic acid (t-TAUCB)
CC       and to a lesser extent by 8-(3-((3S, 5S, 7S)-adamantan-1-yl)ureido)
CC       octanoic acid (AUOA) (By similarity). Phosphatase activity is inhibited
CC       by dodecyl-phosphate, phospholipids such as phospho-lysophosphatidic
CC       acids and fatty acids such as palmitic acid and lauric acid
CC       (PubMed:21217101). {ECO:0000250|UniProtKB:P34913,
CC       ECO:0000269|PubMed:21217101}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=4 uM for 14(R),15(S)-EET {ECO:0000269|PubMed:7840649};
CC         KM=5 uM for 14(S),15(R)-EET {ECO:0000269|PubMed:7840649};
CC         KM=3 uM for 11(R),12(R)-EET {ECO:0000269|PubMed:7840649};
CC         KM=4 uM for 11(S),12(R)-EET {ECO:0000269|PubMed:7840649};
CC         KM=41 uM for 8(R),9(S)-EET {ECO:0000269|PubMed:7840649};
CC         KM=5 uM for 8(S),9(R)-EET {ECO:0000269|PubMed:7840649};
CC         Vmax=9.03 umol/min/mg enzyme with 14(R),15(S)-EET as substrate
CC         {ECO:0000269|PubMed:7840649};
CC         Vmax=1.36 umol/min/mg enzyme with 14(S),15(R)-EET as substrate
CC         {ECO:0000269|PubMed:7840649};
CC         Vmax=0.82 umol/min/mg enzyme with 11(R),12(R)-EET as substrate
CC         {ECO:0000269|PubMed:7840649};
CC         Vmax=3.02 umol/min/mg enzyme with 11(S),12(R)-EET as substrate
CC         {ECO:0000269|PubMed:7840649};
CC         Vmax=0.83 umol/min/mg enzyme with 8(R),9(S)-EET as substrate
CC         {ECO:0000269|PubMed:7840649};
CC         Vmax=3.1 umol/min/mg enzyme with 8(S),9(R)-EET as substrate
CC         {ECO:0000269|PubMed:7840649};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10747889,
CC       ECO:0000269|PubMed:21217101}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21217101,
CC       ECO:0000269|PubMed:7840649}. Peroxisome.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=Ephx2A;
CC         IsoId=P34914-1; Sequence=Displayed;
CC       Name=2; Synonyms=Ephx2B;
CC         IsoId=P34914-2; Sequence=VSP_013904;
CC   -!- TISSUE SPECIFICITY: Detected in liver, intestine, ovary and kidney.
CC       Detected at low levels in heart and muscle.
CC       {ECO:0000269|PubMed:15601917, ECO:0000269|PubMed:21217101,
CC       ECO:0000269|PubMed:7840649, ECO:0000269|PubMed:8750907}.
CC   -!- INDUCTION: Up-regulated during the luteal phase of the stimulated
CC       estrus cycle and by compounds that cause peroxisome proliferation, such
CC       as clofibrate, tiadenol and fenofibrate. {ECO:0000269|PubMed:15601917,
CC       ECO:0000269|PubMed:8349642, ECO:0000269|PubMed:8750907}.
CC   -!- DOMAIN: The N-terminal domain has phosphatase activity. The C-terminal
CC       domain has epoxide hydrolase activity.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- PTM: The covalent modification of cysteine by 15-deoxy-Delta12,14-
CC       prostaglandin-J2 is autocatalytic and reversible. It may occur as an
CC       alternative to other cysteine modifications, such as S-nitrosylation
CC       and S-palmitoylation (By similarity). {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: In knockout mice, hepoxilin turnover to
CC       trioxilins is greatly abolished (PubMed:21217101). In livers, the
CC       activity toward HxA3 (8-hydroxy-(11S,12S)-epoxy-(5Z,9E,14Z)-
CC       eicosatrienoate) and HxB3 (10-hydroxy-(11S,12S)-epoxy- (5Z,8Z,14Z)-
CC       eicosatrienoate) is greatly reduced compared with the WT mice
CC       (PubMed:21217101). {ECO:0000269|PubMed:21217101}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Epoxide hydrolase
CC       family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
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DR   EMBL; L05781; AAA37555.1; -; mRNA.
DR   EMBL; Z37107; CAA85471.1; -; mRNA.
DR   EMBL; AY098585; AAM28238.1; -; mRNA.
DR   EMBL; BC015087; AAH15087.1; -; mRNA.
DR   CCDS; CCDS27218.1; -. [P34914-1]
DR   CCDS; CCDS88694.1; -. [P34914-2]
DR   PIR; A47504; A47504.
DR   RefSeq; NP_001258332.1; NM_001271403.1. [P34914-2]
DR   RefSeq; NP_031966.2; NM_007940.4. [P34914-1]
DR   PDB; 1CQZ; X-ray; 2.80 A; A/B=1-554.
DR   PDB; 1CR6; X-ray; 2.80 A; A/B=1-554.
DR   PDB; 1EK1; X-ray; 3.10 A; A/B=1-554.
DR   PDB; 1EK2; X-ray; 3.00 A; A/B=1-554.
DR   PDBsum; 1CQZ; -.
DR   PDBsum; 1CR6; -.
DR   PDBsum; 1EK1; -.
DR   PDBsum; 1EK2; -.
DR   AlphaFoldDB; P34914; -.
DR   SMR; P34914; -.
DR   BioGRID; 199481; 3.
DR   IntAct; P34914; 3.
DR   MINT; P34914; -.
DR   STRING; 10090.ENSMUSP00000069209; -.
DR   BindingDB; P34914; -.
DR   ChEMBL; CHEMBL4140; -.
DR   GuidetoPHARMACOLOGY; 2970; -.
DR   SwissLipids; SLP:000001106; -.
DR   ESTHER; mouse-hyes; Epoxide_hydrolase.
DR   MEROPS; S33.973; -.
DR   GlyGen; P34914; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P34914; -.
DR   MetOSite; P34914; -.
DR   PhosphoSitePlus; P34914; -.
DR   SwissPalm; P34914; -.
DR   jPOST; P34914; -.
DR   MaxQB; P34914; -.
DR   PaxDb; 10090-ENSMUSP00000069209; -.
DR   PeptideAtlas; P34914; -.
DR   ProteomicsDB; 267029; -. [P34914-1]
DR   ProteomicsDB; 267030; -. [P34914-2]
DR   Pumba; P34914; -.
DR   Antibodypedia; 4070; 486 antibodies from 34 providers.
DR   DNASU; 13850; -.
DR   Ensembl; ENSMUST00000070515.2; ENSMUSP00000069209.2; ENSMUSG00000022040.9. [P34914-1]
DR   Ensembl; ENSMUST00000224698.2; ENSMUSP00000153161.2; ENSMUSG00000022040.9. [P34914-2]
DR   GeneID; 13850; -.
DR   KEGG; mmu:13850; -.
DR   UCSC; uc007ujv.2; mouse. [P34914-1]
DR   UCSC; uc033grp.1; mouse. [P34914-2]
DR   AGR; MGI:99500; -.
DR   CTD; 2053; -.
DR   MGI; MGI:99500; Ephx2.
DR   VEuPathDB; HostDB:ENSMUSG00000022040; -.
DR   eggNOG; KOG3085; Eukaryota.
DR   eggNOG; KOG4178; Eukaryota.
DR   GeneTree; ENSGT00940000158614; -.
DR   HOGENOM; CLU_036085_1_1_1; -.
DR   InParanoid; P34914; -.
DR   OMA; YAMEVLC; -.
DR   OrthoDB; 2443908at2759; -.
DR   PhylomeDB; P34914; -.
DR   TreeFam; TF315395; -.
DR   BRENDA; 3.3.2.10; 3474.
DR   Reactome; R-MMU-2142670; Synthesis of epoxy (EET) and dihydroxyeicosatrienoic acids (DHET).
DR   Reactome; R-MMU-9018682; Biosynthesis of maresins.
DR   Reactome; R-MMU-9033241; Peroxisomal protein import.
DR   BioGRID-ORCS; 13850; 1 hit in 79 CRISPR screens.
DR   ChiTaRS; Ephx2; mouse.
DR   EvolutionaryTrace; P34914; -.
DR   PRO; PR:P34914; -.
DR   Proteomes; UP000000589; Chromosome 14.
DR   RNAct; P34914; Protein.
DR   Bgee; ENSMUSG00000022040; Expressed in small intestine Peyer's patch and 237 other cell types or tissues.
DR   ExpressionAtlas; P34914; baseline and differential.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005777; C:peroxisome; ISO:MGI.
DR   GO; GO:0033885; F:10-hydroxy-9-(phosphonooxy)octadecanoate phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004301; F:epoxide hydrolase activity; IMP:UniProtKB.
DR   GO; GO:0042577; F:lipid phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0052642; F:lysophosphatidic acid phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR   GO; GO:0016791; F:phosphatase activity; ISO:MGI.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR   GO; GO:0015643; F:toxic substance binding; ISO:MGI.
DR   GO; GO:0042632; P:cholesterol homeostasis; IDA:UniProtKB.
DR   GO; GO:0016311; P:dephosphorylation; ISS:UniProtKB.
DR   GO; GO:0097176; P:epoxide metabolic process; IMP:UniProtKB.
DR   GO; GO:0043651; P:linoleic acid metabolic process; ISO:MGI.
DR   GO; GO:0046839; P:phospholipid dephosphorylation; ISS:UniProtKB.
DR   GO; GO:0045777; P:positive regulation of blood pressure; ISO:MGI.
DR   GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
DR   GO; GO:0002539; P:prostaglandin production involved in inflammatory response; ISO:MGI.
DR   GO; GO:0090181; P:regulation of cholesterol metabolic process; IMP:UniProtKB.
DR   GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR   GO; GO:0046272; P:stilbene catabolic process; ISO:MGI.
DR   CDD; cd02603; HAD_sEH-N_like; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR000639; Epox_hydrolase-like.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006439; HAD-SF_hydro_IA.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR023198; PGP-like_dom2.
DR   NCBIfam; TIGR01509; HAD-SF-IA-v3; 1.
DR   PANTHER; PTHR43329:SF4; BIFUNCTIONAL EPOXIDE HYDROLASE 2; 1.
DR   PANTHER; PTHR43329; EPOXIDE HYDROLASE; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00111; ABHYDROLASE.
DR   PRINTS; PR00412; EPOXHYDRLASE.
DR   SFLD; SFLDG01129; C1.5:_HAD__Beta-PGM__Phosphata; 1.
DR   SFLD; SFLDF00040; epoxide_hydrolase_n-terminal_p; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   SWISS-2DPAGE; P34914; -.
DR   Genevisible; P34914; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing;
KW   Aromatic hydrocarbons catabolism; Cytoplasm; Detoxification;
KW   Direct protein sequencing; Hydrolase; Lipid metabolism; Lipoprotein;
KW   Magnesium; Metal-binding; Multifunctional enzyme; Peroxisome;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..554
FT                   /note="Bifunctional epoxide hydrolase 2"
FT                   /id="PRO_0000084112"
FT   DOMAIN          257..530
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   REGION          1..224
FT                   /note="Phosphatase"
FT   REGION          233..554
FT                   /note="Epoxide hydrolase"
FT   MOTIF           552..554
FT                   /note="Microbody targeting signal"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        333
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000269|PubMed:10485878,
FT                   ECO:0000269|PubMed:10747889"
FT   ACT_SITE        465
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000269|PubMed:10485878,
FT                   ECO:0000269|PubMed:10747889"
FT   ACT_SITE        523
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000269|PubMed:10485878,
FT                   ECO:0000269|PubMed:10747889"
FT   BINDING         9
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P34913"
FT   BINDING         11
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P34913"
FT   BINDING         123..124
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000250|UniProtKB:P34913"
FT   BINDING         185
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P34913"
FT   BINDING         381
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P34913"
FT   MOD_RES         55
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         176
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         176
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         191
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         215
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         368
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         371
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         420
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         454
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         504
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         508
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         508
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         553
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   LIPID           521
FT                   /note="S-(15-deoxy-Delta12,14-prostaglandin J2-9-
FT                   yl)cysteine"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..62
FT                   /note="MALRVAAFDLDGVLALPSIAGAFRRSEEALALPRDFLLGAYQTEFPEGPTEQ
FT                   LMKGKITFSQ -> MRFAAMAAFSVFFVSKGLLMNSNIWCVGQEGPSQEDTDTIHTSE
FT                   (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15601917"
FT                   /id="VSP_013904"
FT   CONFLICT        77
FT                   /note="A -> T (in Ref. 2; CAA85471)"
FT                   /evidence="ECO:0000305"
FT   STRAND          5..8
FT                   /evidence="ECO:0007829|PDB:1CQZ"
FT   HELIX           10..12
FT                   /evidence="ECO:0007829|PDB:1CR6"
FT   STRAND          13..17
FT                   /evidence="ECO:0007829|PDB:1CQZ"
FT   HELIX           20..28
FT                   /evidence="ECO:0007829|PDB:1CQZ"
FT   TURN            29..31
FT                   /evidence="ECO:0007829|PDB:1CQZ"
FT   TURN            34..37
FT                   /evidence="ECO:0007829|PDB:1CQZ"
FT   HELIX           38..41
FT                   /evidence="ECO:0007829|PDB:1CQZ"
FT   TURN            51..56
FT                   /evidence="ECO:0007829|PDB:1CQZ"
FT   STRAND          57..62
FT                   /evidence="ECO:0007829|PDB:1EK1"
FT   HELIX           64..74
FT                   /evidence="ECO:0007829|PDB:1CQZ"
FT   TURN            75..78
FT                   /evidence="ECO:0007829|PDB:1CQZ"
FT   HELIX           94..97
FT                   /evidence="ECO:0007829|PDB:1CQZ"
FT   HELIX           103..114
FT                   /evidence="ECO:0007829|PDB:1CQZ"
FT   STRAND          118..123
FT                   /evidence="ECO:0007829|PDB:1CQZ"
FT   STRAND          130..132
FT                   /evidence="ECO:0007829|PDB:1CR6"
FT   HELIX           134..143
FT                   /evidence="ECO:0007829|PDB:1CQZ"
FT   HELIX           144..146
FT                   /evidence="ECO:0007829|PDB:1CQZ"
FT   STRAND          148..152
FT                   /evidence="ECO:0007829|PDB:1CQZ"
FT   HELIX           153..156
FT                   /evidence="ECO:0007829|PDB:1CQZ"
FT   HELIX           163..173
FT                   /evidence="ECO:0007829|PDB:1CQZ"
FT   STRAND          177..187
FT                   /evidence="ECO:0007829|PDB:1CQZ"
FT   TURN            188..190
FT                   /evidence="ECO:0007829|PDB:1CQZ"
FT   HELIX           191..195
FT                   /evidence="ECO:0007829|PDB:1CQZ"
FT   STRAND          199..202
FT                   /evidence="ECO:0007829|PDB:1CQZ"
FT   STRAND          205..207
FT                   /evidence="ECO:0007829|PDB:1CQZ"
FT   HELIX           208..215
FT                   /evidence="ECO:0007829|PDB:1CQZ"
FT   STRAND          216..218
FT                   /evidence="ECO:0007829|PDB:1EK2"
FT   STRAND          232..241
FT                   /evidence="ECO:0007829|PDB:1CQZ"
FT   STRAND          243..245
FT                   /evidence="ECO:0007829|PDB:1CQZ"
FT   STRAND          247..254
FT                   /evidence="ECO:0007829|PDB:1CQZ"
FT   STRAND          256..262
FT                   /evidence="ECO:0007829|PDB:1CQZ"
FT   HELIX           269..274
FT                   /evidence="ECO:0007829|PDB:1CQZ"
FT   HELIX           275..281
FT                   /evidence="ECO:0007829|PDB:1CQZ"
FT   STRAND          285..290
FT                   /evidence="ECO:0007829|PDB:1CQZ"
FT   HELIX           304..306
FT                   /evidence="ECO:0007829|PDB:1CQZ"
FT   HELIX           308..322
FT                   /evidence="ECO:0007829|PDB:1CQZ"
FT   STRAND          327..332
FT                   /evidence="ECO:0007829|PDB:1CQZ"
FT   HELIX           334..345
FT                   /evidence="ECO:0007829|PDB:1CQZ"
FT   TURN            347..349
FT                   /evidence="ECO:0007829|PDB:1EK2"
FT   STRAND          350..357
FT                   /evidence="ECO:0007829|PDB:1CQZ"
FT   HELIX           369..375
FT                   /evidence="ECO:0007829|PDB:1CQZ"
FT   HELIX           377..379
FT                   /evidence="ECO:0007829|PDB:1CQZ"
FT   HELIX           380..385
FT                   /evidence="ECO:0007829|PDB:1CQZ"
FT   HELIX           390..397
FT                   /evidence="ECO:0007829|PDB:1CQZ"
FT   HELIX           399..406
FT                   /evidence="ECO:0007829|PDB:1CQZ"
FT   TURN            418..420
FT                   /evidence="ECO:0007829|PDB:1CQZ"
FT   HELIX           421..424
FT                   /evidence="ECO:0007829|PDB:1CQZ"
FT   TURN            427..430
FT                   /evidence="ECO:0007829|PDB:1CQZ"
FT   STRAND          439..441
FT                   /evidence="ECO:0007829|PDB:1CQZ"
FT   HELIX           443..456
FT                   /evidence="ECO:0007829|PDB:1CQZ"
FT   HELIX           459..462
FT                   /evidence="ECO:0007829|PDB:1CQZ"
FT   HELIX           463..467
FT                   /evidence="ECO:0007829|PDB:1CQZ"
FT   HELIX           468..475
FT                   /evidence="ECO:0007829|PDB:1CQZ"
FT   HELIX           476..478
FT                   /evidence="ECO:0007829|PDB:1CQZ"
FT   STRAND          487..492
FT                   /evidence="ECO:0007829|PDB:1CQZ"
FT   STRAND          496..498
FT                   /evidence="ECO:0007829|PDB:1CQZ"
FT   HELIX           500..503
FT                   /evidence="ECO:0007829|PDB:1CQZ"
FT   HELIX           506..508
FT                   /evidence="ECO:0007829|PDB:1CQZ"
FT   STRAND          514..518
FT                   /evidence="ECO:0007829|PDB:1CQZ"
FT   HELIX           525..528
FT                   /evidence="ECO:0007829|PDB:1CQZ"
FT   HELIX           530..543
FT                   /evidence="ECO:0007829|PDB:1CQZ"
SQ   SEQUENCE   554 AA;  62515 MW;  2F3A3F7DACE47C93 CRC64;
     MALRVAAFDL DGVLALPSIA GAFRRSEEAL ALPRDFLLGA YQTEFPEGPT EQLMKGKITF
     SQWVPLMDES YRKSSKACGA NLPENFSISQ IFSQAMAARS INRPMLQAAI ALKKKGFTTC
     IVTNNWLDDG DKRDSLAQMM CELSQHFDFL IESCQVGMIK PEPQIYNFLL DTLKAKPNEV
     VFLDDFGSNL KPARDMGMVT ILVHNTASAL RELEKVTGTQ FPEAPLPVPC NPNDVSHGYV
     TVKPGIRLHF VEMGSGPALC LCHGFPESWF SWRYQIPALA QAGFRVLAID MKGYGDSSSP
     PEIEEYAMEL LCKEMVTFLD KLGIPQAVFI GHDWAGVMVW NMALFYPERV RAVASLNTPF
     MPPDPDVSPM KVIRSIPVFN YQLYFQEPGV AEAELEKNMS RTFKSFFRAS DETGFIAVHK
     ATEIGGILVN TPEDPNLSKI TTEEEIEFYI QQFKKTGFRG PLNWYRNTER NWKWSCKGLG
     RKILVPALMV TAEKDIVLRP EMSKNMEKWI PFLKRGHIED CGHWTQIEKP TEVNQILIKW
     LQTEVQNPSV TSKI
//