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Bifunctional epoxide hydrolase 2 [Includes: Cytosolic epoxide hydrolase 2 (CEH) (EC 3.3.2.10) (Epoxide hydratase) (Soluble epoxide hydrolase) (SEH); Lipid-phosphate phosphatase (EC 3.1.3.76)]

 HYES_HUMAN              Reviewed;         555 AA.
P34913; B2Z3B1; B3KTU8; B3KUA0; G3V134; J3KPH7; Q16764; Q9HBJ1;
Q9HBJ2;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
07-JUN-2005, sequence version 2.
20-JUN-2018, entry version 183.
RecName: Full=Bifunctional epoxide hydrolase 2;
Includes:
RecName: Full=Cytosolic epoxide hydrolase 2;
Short=CEH;
EC=3.3.2.10 {ECO:0000269|PubMed:12574510, ECO:0000269|PubMed:12869654, ECO:0000269|PubMed:15196990, ECO:0000269|PubMed:22798687};
AltName: Full=Epoxide hydratase;
AltName: Full=Soluble epoxide hydrolase;
Short=SEH;
Includes:
RecName: Full=Lipid-phosphate phosphatase;
EC=3.1.3.76 {ECO:0000269|PubMed:12574508, ECO:0000269|PubMed:12574510};
Name=EPHX2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), PARTIAL PROTEIN
SEQUENCE, AND VARIANT GLN-287.
TISSUE=Liver;
PubMed=8342951; DOI=10.1006/abbi.1993.1411;
Beetham J.K., Tian T., Hammock B.D.;
"cDNA cloning and expression of a soluble epoxide hydrolase from human
liver.";
Arch. Biochem. Biophys. 305:197-201(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Placenta;
PubMed=8619856; DOI=10.1006/bbrc.1996.0596;
Sandberg M., Meijer J.;
"Structural characterization of the human soluble epoxide hydrolase
gene (EPHX2).";
Biochem. Biophys. Res. Commun. 221:333-339(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS GLN-287 AND
ARG-403 INS.
TISSUE=Liver;
PubMed=10862610; DOI=10.1074/jbc.M001153200;
Sandberg M., Hassett C., Adman E.T., Meijer J., Omiecinski C.J.;
"Identification and functional characterization of human soluble
epoxide hydrolase genetic polymorphisms.";
J. Biol. Chem. 275:28873-28881(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANT
ARG-403 INS.
TISSUE=Kidney, and Prostate;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ALA-21; GLN-52;
ARG-55; CYS-103; TYR-154; LEU-225; GLN-287; VAL-369 AND GLY-470.
NIEHS SNPs program;
Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16421571; DOI=10.1038/nature04406;
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
Lander E.S.;
"DNA sequence and analysis of human chromosome 8.";
Nature 439:331-335(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=B-cell, and Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
FUNCTION, CATALYTIC ACTIVITY, AND CHARACTERIZATION OF VARIANTS ARG-55;
CYS-103; TYR-154; GLN-287 AND GLY-470.
PubMed=12869654; DOI=10.1124/mol.64.2.482;
Przybyla-Zawislak B.D., Srivastava P.K., Vazquez-Matias J.,
Mohrenweiser H.W., Maxwell J.E., Hammock B.D., Bradbury J.A.,
Enayetallah A.E., Zeldin D.C., Grant D.F.;
"Polymorphisms in human soluble epoxide hydrolase.";
Mol. Pharmacol. 64:482-490(2003).
[11]
CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION AS
PHOSPHATASE, AND MUTAGENESIS OF ASP-9.
PubMed=12574508; DOI=10.1073/pnas.0437829100;
Cronin A., Mowbray S., Durk H., Homburg S., Fleming I.,
Fisslthaler B., Oesch F., Arand M.;
"The N-terminal domain of mammalian soluble epoxide hydrolase is a
phosphatase.";
Proc. Natl. Acad. Sci. U.S.A. 100:1552-1557(2003).
[12]
FUNCTION, CATALYTIC ACTIVITY, FUNCTION AS LIPID PHOSPHATASE, COFACTOR,
AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=12574510; DOI=10.1073/pnas.0437724100;
Newman J.W., Morisseau C., Harris T.R., Hammock B.D.;
"The soluble epoxide hydrolase encoded by EPXH2 is a bifunctional
enzyme with novel lipid phosphate phosphatase activity.";
Proc. Natl. Acad. Sci. U.S.A. 100:1558-1563(2003).
[13]
CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
CHARACTERIZATION OF VARIANTS ARG-55; CYS-103; TYR-154; GLN-287 AND
GLY-470.
PubMed=15196990; DOI=10.1016/j.abb.2004.05.003;
Srivastava P.K., Sharma V.K., Kalonia D.S., Grant D.F.;
"Polymorphisms in human soluble epoxide hydrolase: effects on enzyme
activity, enzyme stability, and quaternary structure.";
Arch. Biochem. Biophys. 427:164-169(2004).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-43, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[16]
LIPIDATION AT CYS-522, AND MUTAGENESIS OF CYS-522.
PubMed=21164107; DOI=10.1161/CIRCRESAHA.110.235879;
Charles R.L., Burgoyne J.R., Mayr M., Weldon S.M., Hubner N., Dong H.,
Morisseau C., Hammock B.D., Landar A., Eaton P.;
"Redox regulation of soluble epoxide hydrolase by 15-deoxy-delta-
prostaglandin J2 controls coronary hypoxic vasodilation.";
Circ. Res. 108:324-334(2011).
[17]
FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, AND
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=22798687; DOI=10.1194/jlr.M024448;
Decker M., Adamska M., Cronin A., Di Giallonardo F., Burgener J.,
Marowsky A., Falck J.R., Morisseau C., Hammock B.D., Gruzdev A.,
Zeldin D.C., Arand M.;
"EH3 (ABHD9): the first member of a new epoxide hydrolase family with
high activity for fatty acid epoxides.";
J. Lipid Res. 53:2038-2045(2012).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[19]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH PHOSPHATE;
MAGNESIUM AND EPOXIDE HYDROLASE INHIBITOR, AND ACTIVE SITE.
PubMed=15096040; DOI=10.1021/bi036189j;
Gomez G.A., Morisseau C., Hammock B.D., Christianson D.W.;
"Structure of human epoxide hydrolase reveals mechanistic inferences
on bifunctional catalysis in epoxide and phosphate ester hydrolysis.";
Biochemistry 43:4716-4723(2004).
[20]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEXES WITH DIALKYLUREA
INHIBITORS AND MAGNESIUM, AND ACTIVE SITE.
PubMed=16322563; DOI=10.1110/ps.051720206;
Gomez G.A., Morisseau C., Hammock B.D., Christianson D.W.;
"Human soluble epoxide hydrolase: structural basis of inhibition by 4-
(3-cyclohexylureido)-carboxylic acids.";
Protein Sci. 15:58-64(2006).
[21]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEXES WITH ARYLAMIDE
INHIBITORS, AND ACTIVE SITE.
PubMed=19746975; DOI=10.1021/jm9005302;
Eldrup A.B., Soleymanzadeh F., Taylor S.J., Muegge I., Farrow N.A.,
Joseph D., McKellop K., Man C.C., Kukulka A., De Lombaert S.;
"Structure-based optimization of arylamides as inhibitors of soluble
epoxide hydrolase.";
J. Med. Chem. 52:5880-5895(2009).
[22]
X-RAY CRYSTALLOGRAPHY (2.79 ANGSTROMS) IN COMPLEX WITH SYNTHETIC
INHIBITOR, AND ACTIVE SITE.
PubMed=19969453; DOI=10.1016/j.bmcl.2009.11.091;
Eldrup A.B., Soleymanzadeh F., Farrow N.A., Kukulka A.,
De Lombaert S.;
"Optimization of piperidyl-ureas as inhibitors of soluble epoxide
hydrolase.";
Bioorg. Med. Chem. Lett. 20:571-575(2010).
[23]
X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) IN COMPLEX WITH SYNTHETIC
INHIBITOR, AND ACTIVE SITE.
PubMed=20934334; DOI=10.1016/j.bmcl.2010.09.095;
Lo H.Y., Man C.C., Fleck R.W., Farrow N.A., Ingraham R.H., Kukulka A.,
Proudfoot J.R., Betageri R., Kirrane T., Patel U., Sharma R.,
Hoermann M.A., Kabcenell A., Lombaert S.D.;
"Substituted pyrazoles as novel sEH antagonist: investigation of key
binding interactions within the catalytic domain.";
Bioorg. Med. Chem. Lett. 20:6379-6383(2010).
-!- 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).
{ECO:0000250|UniProtKB:P80299, ECO:0000269|PubMed:12574508,
ECO:0000269|PubMed:12574510, ECO:0000269|PubMed:12869654,
ECO:0000269|PubMed:22798687}.
-!- CATALYTIC ACTIVITY: An epoxide + H(2)O = a glycol.
{ECO:0000269|PubMed:12574510, ECO:0000269|PubMed:12869654,
ECO:0000269|PubMed:22798687}.
-!- CATALYTIC ACTIVITY: (9S,10S)-10-hydroxy-9-
(phosphonooxy)octadecanoate + H(2)O = (9S,10S)-9,10-
dihydroxyoctadecanoate + phosphate. {ECO:0000269|PubMed:12574508,
ECO:0000269|PubMed:12574510, ECO:0000269|PubMed:15196990}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:12574510,
ECO:0000269|PubMed:15096040, ECO:0000269|PubMed:16322563};
-!- ENZYME 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). {ECO:0000269|PubMed:22798687}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=21 uM for threo-9,10-phosphonooxy-hydroxy-octadecanoic acid
{ECO:0000269|PubMed:12574508, ECO:0000269|PubMed:12574510,
ECO:0000269|PubMed:15196990};
KM=1.7 uM for 8,9-EET {ECO:0000269|PubMed:22798687};
KM=3.4 uM for 11,12-EET {ECO:0000269|PubMed:22798687};
KM=15 uM for 14,15-EET {ECO:0000269|PubMed:22798687};
KM=1.5 uM for leukotoxin {ECO:0000269|PubMed:22798687};
KM=1.1 mM for p-nitrophenyl phosphate
{ECO:0000269|PubMed:12574508, ECO:0000269|PubMed:12574510,
ECO:0000269|PubMed:15196990};
Vmax=338 nmol/min/mg enzyme with threo-9,10-phosphonooxy-
hydroxy-octadecanoic acid {ECO:0000269|PubMed:12574508,
ECO:0000269|PubMed:12574510, ECO:0000269|PubMed:15196990};
Vmax=0.9 umol/min/mg enzyme with 8,9-EET as substrate
{ECO:0000269|PubMed:22798687};
Vmax=4.5 umol/min/mg enzyme with 11,12-EET as substrate
{ECO:0000269|PubMed:22798687};
Vmax=7 umol/min/mg enzyme with 14,15-EET as substrate
{ECO:0000269|PubMed:22798687};
Vmax=0.55 umol/min/mg enzyme with leukotoxin as substrate
{ECO:0000269|PubMed:22798687};
Vmax=5.8 nmol/min/mg enzyme with p-nitrophenyl phosphate
{ECO:0000269|PubMed:12574508, ECO:0000269|PubMed:12574510,
ECO:0000269|PubMed:15196990};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15096040,
ECO:0000269|PubMed:19969453, ECO:0000269|PubMed:20934334}.
-!- SUBCELLULAR LOCATION: Cytoplasm. Peroxisome.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P34913-1; Sequence=Displayed;
Name=2;
IsoId=P34913-2; Sequence=VSP_045598;
Note=No experimental confirmation available.;
Name=3;
IsoId=P34913-3; Sequence=VSP_045597;
Note=No experimental confirmation available.;
-!- INDUCTION: By compounds that cause peroxisome proliferation such
as clofibrate, tiadenol and fenofibrate.
-!- DOMAIN: The N-terminal domain has phosphatase activity. The C-
terminal domain has epoxide hydrolase activity.
-!- PTM: The N-terminus is blocked.
-!- 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 (Probable). {ECO:0000305}.
-!- SIMILARITY: Belongs to the AB hydrolase superfamily. Epoxide
hydrolase family. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/ephx2/";
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EMBL; L05779; AAA02756.1; -; mRNA.
EMBL; X97024; CAA65751.1; -; Genomic_DNA.
EMBL; X97025; CAA65751.1; JOINED; Genomic_DNA.
EMBL; X97026; CAA65751.1; JOINED; Genomic_DNA.
EMBL; X97027; CAA65751.1; JOINED; Genomic_DNA.
EMBL; X97028; CAA65751.1; JOINED; Genomic_DNA.
EMBL; X97029; CAA65751.1; JOINED; Genomic_DNA.
EMBL; X97030; CAA65751.1; JOINED; Genomic_DNA.
EMBL; X97031; CAA65751.1; JOINED; Genomic_DNA.
EMBL; X97032; CAA65751.1; JOINED; Genomic_DNA.
EMBL; X97033; CAA65751.1; JOINED; Genomic_DNA.
EMBL; X97034; CAA65751.1; JOINED; Genomic_DNA.
EMBL; X97035; CAA65751.1; JOINED; Genomic_DNA.
EMBL; X97036; CAA65751.1; JOINED; Genomic_DNA.
EMBL; X97037; CAA65751.1; JOINED; Genomic_DNA.
EMBL; X97038; CAA65751.1; JOINED; Genomic_DNA.
EMBL; AF233334; AAG14966.1; -; mRNA.
EMBL; AF233335; AAG14967.1; -; mRNA.
EMBL; AF233336; AAG14968.1; -; mRNA.
EMBL; BT006885; AAP35531.1; -; mRNA.
EMBL; AK096089; BAG53210.1; -; mRNA.
EMBL; AK096770; BAG53362.1; -; mRNA.
EMBL; EU584434; ACD11487.1; -; Genomic_DNA.
EMBL; AF311103; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471080; EAW63548.1; -; Genomic_DNA.
EMBL; CH471080; EAW63549.1; -; Genomic_DNA.
EMBL; CH471080; EAW63551.1; -; Genomic_DNA.
EMBL; BC007708; AAH07708.1; -; mRNA.
EMBL; BC011628; AAH11628.1; -; mRNA.
EMBL; BC013874; AAH13874.1; -; mRNA.
CCDS; CCDS59097.1; -. [P34913-2]
CCDS; CCDS59098.1; -. [P34913-3]
CCDS; CCDS6060.1; -. [P34913-1]
PIR; JC4711; JC4711.
RefSeq; NP_001243411.1; NM_001256482.1. [P34913-2]
RefSeq; NP_001243412.1; NM_001256483.1. [P34913-3]
RefSeq; NP_001243413.1; NM_001256484.1. [P34913-2]
RefSeq; NP_001970.2; NM_001979.5. [P34913-1]
UniGene; Hs.212088; -.
PDB; 1S8O; X-ray; 2.60 A; A=1-555.
PDB; 1VJ5; X-ray; 2.35 A; A=1-555.
PDB; 1ZD2; X-ray; 3.00 A; P=1-555.
PDB; 1ZD3; X-ray; 2.30 A; A=1-555.
PDB; 1ZD4; X-ray; 2.70 A; A=1-555.
PDB; 1ZD5; X-ray; 2.60 A; A=1-555.
PDB; 3ANS; X-ray; 1.98 A; A/B=230-555.
PDB; 3ANT; X-ray; 2.40 A; A/B=230-555.
PDB; 3I1Y; X-ray; 2.47 A; A=1-555.
PDB; 3I28; X-ray; 1.95 A; A=1-555.
PDB; 3KOO; X-ray; 2.79 A; A=1-555.
PDB; 3OTQ; X-ray; 3.00 A; A=1-555.
PDB; 3PDC; X-ray; 2.60 A; A/B=226-548.
PDB; 3WK4; X-ray; 2.11 A; A=1-555.
PDB; 3WK5; X-ray; 2.77 A; A=1-555.
PDB; 3WK6; X-ray; 2.10 A; A=1-555.
PDB; 3WK7; X-ray; 2.20 A; A=1-555.
PDB; 3WK8; X-ray; 2.20 A; A=1-555.
PDB; 3WK9; X-ray; 2.20 A; A=1-555.
PDB; 3WKA; X-ray; 2.01 A; A=1-555.
PDB; 3WKB; X-ray; 2.20 A; A=1-555.
PDB; 3WKC; X-ray; 2.20 A; A=1-555.
PDB; 3WKD; X-ray; 2.48 A; A=1-555.
PDB; 3WKE; X-ray; 2.75 A; A=1-555.
PDB; 4C4X; X-ray; 2.17 A; A/B=230-555.
PDB; 4C4Y; X-ray; 2.41 A; A=230-555.
PDB; 4C4Z; X-ray; 2.06 A; A/B=230-555.
PDB; 4HAI; X-ray; 2.55 A; A=1-555.
PDB; 4J03; X-ray; 2.92 A; A=1-555.
PDB; 4JNC; X-ray; 1.96 A; A=238-549.
PDB; 4OCZ; X-ray; 2.94 A; A=1-555.
PDB; 4OD0; X-ray; 2.92 A; A=1-555.
PDB; 4X6X; X-ray; 1.80 A; A/B=230-555.
PDB; 4X6Y; X-ray; 2.10 A; A/B=230-555.
PDB; 4Y2J; X-ray; 2.15 A; A=1-555.
PDB; 4Y2P; X-ray; 2.05 A; A=1-555.
PDB; 4Y2Q; X-ray; 2.40 A; A=1-555.
PDB; 4Y2R; X-ray; 2.45 A; A=1-555.
PDB; 4Y2S; X-ray; 2.30 A; A=1-555.
PDB; 4Y2T; X-ray; 2.40 A; A=1-555.
PDB; 4Y2U; X-ray; 2.75 A; A=1-555.
PDB; 4Y2V; X-ray; 2.40 A; A=1-555.
PDB; 4Y2X; X-ray; 2.50 A; A=1-555.
PDB; 4Y2Y; X-ray; 2.30 A; A=1-555.
PDB; 5AHX; X-ray; 2.00 A; A=1-548.
PDB; 5AI0; X-ray; 1.75 A; A=1-548.
PDB; 5AI4; X-ray; 1.93 A; A=1-548.
PDB; 5AI5; X-ray; 2.28 A; A=1-548.
PDB; 5AI6; X-ray; 2.30 A; A=1-548.
PDB; 5AI8; X-ray; 1.85 A; A=1-548.
PDB; 5AI9; X-ray; 1.80 A; A=1-548.
PDB; 5AIA; X-ray; 2.26 A; A=1-548.
PDB; 5AIB; X-ray; 1.95 A; A=1-548.
PDB; 5AIC; X-ray; 1.89 A; A=1-548.
PDB; 5AK3; X-ray; 2.28 A; A=1-548.
PDB; 5AK4; X-ray; 1.79 A; A=1-548.
PDB; 5AK5; X-ray; 2.22 A; A=1-548.
PDB; 5AK6; X-ray; 2.15 A; A=1-548.
PDB; 5AKE; X-ray; 2.26 A; A=1-548.
PDB; 5AKG; X-ray; 2.51 A; A=1-548.
PDB; 5AKH; X-ray; 2.10 A; A=1-548.
PDB; 5AKI; X-ray; 1.81 A; A=1-548.
PDB; 5AKJ; X-ray; 2.03 A; A=1-548.
PDB; 5AKK; X-ray; 1.90 A; A=1-548.
PDB; 5AKL; X-ray; 2.00 A; A=1-548.
PDB; 5AKX; X-ray; 2.09 A; A=1-548.
PDB; 5AKY; X-ray; 2.18 A; A=1-548.
PDB; 5AKZ; X-ray; 2.18 A; A=1-548.
PDB; 5ALD; X-ray; 2.26 A; A=1-548.
PDB; 5ALE; X-ray; 1.95 A; A=1-548.
PDB; 5ALF; X-ray; 2.32 A; A=1-548.
PDB; 5ALG; X-ray; 2.40 A; A=1-548.
PDB; 5ALH; X-ray; 1.90 A; A=1-548.
PDB; 5ALI; X-ray; 1.85 A; A=1-548.
PDB; 5ALJ; X-ray; 2.10 A; A=1-548.
PDB; 5ALK; X-ray; 2.33 A; A=1-548.
PDB; 5ALL; X-ray; 2.20 A; A=1-548.
PDB; 5ALM; X-ray; 2.00 A; A=1-548.
PDB; 5ALN; X-ray; 2.00 A; A=1-548.
PDB; 5ALO; X-ray; 2.00 A; A=1-548.
PDB; 5ALP; X-ray; 2.06 A; A=1-548.
PDB; 5ALQ; X-ray; 2.78 A; A=1-548.
PDB; 5ALR; X-ray; 2.60 A; A=1-548.
PDB; 5ALS; X-ray; 2.57 A; A=1-548.
PDB; 5ALT; X-ray; 2.15 A; A=1-548.
PDB; 5ALU; X-ray; 1.87 A; A=1-548.
PDB; 5ALV; X-ray; 1.80 A; A=1-548.
PDB; 5ALW; X-ray; 2.20 A; A=1-548.
PDB; 5ALX; X-ray; 2.23 A; A=1-548.
PDB; 5ALY; X-ray; 1.90 A; A=1-548.
PDB; 5ALZ; X-ray; 2.30 A; A=1-548.
PDB; 5AM0; X-ray; 1.88 A; A=1-548.
PDB; 5AM1; X-ray; 2.15 A; A=1-548.
PDB; 5AM2; X-ray; 1.70 A; A=1-548.
PDB; 5AM3; X-ray; 2.20 A; A=1-548.
PDB; 5AM4; X-ray; 1.87 A; A=1-548.
PDB; 5AM5; X-ray; 2.26 A; A=1-548.
PDB; 5FP0; X-ray; 2.35 A; A=1-548.
PDB; 5MWA; X-ray; 1.55 A; A=2-224.
PDB; 6AUM; X-ray; 2.95 A; A=1-555.
PDBsum; 1S8O; -.
PDBsum; 1VJ5; -.
PDBsum; 1ZD2; -.
PDBsum; 1ZD3; -.
PDBsum; 1ZD4; -.
PDBsum; 1ZD5; -.
PDBsum; 3ANS; -.
PDBsum; 3ANT; -.
PDBsum; 3I1Y; -.
PDBsum; 3I28; -.
PDBsum; 3KOO; -.
PDBsum; 3OTQ; -.
PDBsum; 3PDC; -.
PDBsum; 3WK4; -.
PDBsum; 3WK5; -.
PDBsum; 3WK6; -.
PDBsum; 3WK7; -.
PDBsum; 3WK8; -.
PDBsum; 3WK9; -.
PDBsum; 3WKA; -.
PDBsum; 3WKB; -.
PDBsum; 3WKC; -.
PDBsum; 3WKD; -.
PDBsum; 3WKE; -.
PDBsum; 4C4X; -.
PDBsum; 4C4Y; -.
PDBsum; 4C4Z; -.
PDBsum; 4HAI; -.
PDBsum; 4J03; -.
PDBsum; 4JNC; -.
PDBsum; 4OCZ; -.
PDBsum; 4OD0; -.
PDBsum; 4X6X; -.
PDBsum; 4X6Y; -.
PDBsum; 4Y2J; -.
PDBsum; 4Y2P; -.
PDBsum; 4Y2Q; -.
PDBsum; 4Y2R; -.
PDBsum; 4Y2S; -.
PDBsum; 4Y2T; -.
PDBsum; 4Y2U; -.
PDBsum; 4Y2V; -.
PDBsum; 4Y2X; -.
PDBsum; 4Y2Y; -.
PDBsum; 5AHX; -.
PDBsum; 5AI0; -.
PDBsum; 5AI4; -.
PDBsum; 5AI5; -.
PDBsum; 5AI6; -.
PDBsum; 5AI8; -.
PDBsum; 5AI9; -.
PDBsum; 5AIA; -.
PDBsum; 5AIB; -.
PDBsum; 5AIC; -.
PDBsum; 5AK3; -.
PDBsum; 5AK4; -.
PDBsum; 5AK5; -.
PDBsum; 5AK6; -.
PDBsum; 5AKE; -.
PDBsum; 5AKG; -.
PDBsum; 5AKH; -.
PDBsum; 5AKI; -.
PDBsum; 5AKJ; -.
PDBsum; 5AKK; -.
PDBsum; 5AKL; -.
PDBsum; 5AKX; -.
PDBsum; 5AKY; -.
PDBsum; 5AKZ; -.
PDBsum; 5ALD; -.
PDBsum; 5ALE; -.
PDBsum; 5ALF; -.
PDBsum; 5ALG; -.
PDBsum; 5ALH; -.
PDBsum; 5ALI; -.
PDBsum; 5ALJ; -.
PDBsum; 5ALK; -.
PDBsum; 5ALL; -.
PDBsum; 5ALM; -.
PDBsum; 5ALN; -.
PDBsum; 5ALO; -.
PDBsum; 5ALP; -.
PDBsum; 5ALQ; -.
PDBsum; 5ALR; -.
PDBsum; 5ALS; -.
PDBsum; 5ALT; -.
PDBsum; 5ALU; -.
PDBsum; 5ALV; -.
PDBsum; 5ALW; -.
PDBsum; 5ALX; -.
PDBsum; 5ALY; -.
PDBsum; 5ALZ; -.
PDBsum; 5AM0; -.
PDBsum; 5AM1; -.
PDBsum; 5AM2; -.
PDBsum; 5AM3; -.
PDBsum; 5AM4; -.
PDBsum; 5AM5; -.
PDBsum; 5FP0; -.
PDBsum; 5MWA; -.
PDBsum; 6AUM; -.
ProteinModelPortal; P34913; -.
SMR; P34913; -.
BioGrid; 108367; 5.
IntAct; P34913; 5.
STRING; 9606.ENSP00000430269; -.
BindingDB; P34913; -.
ChEMBL; CHEMBL2409; -.
DrugBank; DB08257; 4-{[(CYCLOHEXYLAMINO)CARBONYL]AMINO}BUTANOIC ACID.
DrugBank; DB08258; 6-{[(CYCLOHEXYLAMINO)CARBONYL]AMINO}HEXANOIC ACID.
DrugBank; DB08259; 7-{[(CYCLOHEXYLAMINO)CARBONYL]AMINO}HEPTANOIC ACID.
DrugBank; DB08256; N-[(CYCLOHEXYLAMINO)CARBONYL]GLYCINE.
DrugBank; DB02029; N-Cyclohexyl-N'-(4-Iodophenyl)Urea.
DrugBank; DB04213; N-Cyclohexyl-N'-(Propyl)Phenyl Urea.
DrugBank; DB03677; N-Cyclohexyl-N'-Decylurea.
GuidetoPHARMACOLOGY; 2970; -.
SwissLipids; SLP:000001105; -.
ESTHER; human-EPHX2; Epoxide_hydrolase.
MEROPS; S33.973; -.
DEPOD; P34913; -.
iPTMnet; P34913; -.
PhosphoSitePlus; P34913; -.
BioMuta; EPHX2; -.
DMDM; 67476665; -.
EPD; P34913; -.
MaxQB; P34913; -.
PaxDb; P34913; -.
PeptideAtlas; P34913; -.
PRIDE; P34913; -.
ProteomicsDB; 54953; -.
DNASU; 2053; -.
Ensembl; ENST00000380476; ENSP00000369843; ENSG00000120915. [P34913-2]
Ensembl; ENST00000521400; ENSP00000430269; ENSG00000120915. [P34913-1]
Ensembl; ENST00000521780; ENSP00000430302; ENSG00000120915. [P34913-3]
GeneID; 2053; -.
KEGG; hsa:2053; -.
UCSC; uc003xfu.5; human. [P34913-1]
CTD; 2053; -.
DisGeNET; 2053; -.
EuPathDB; HostDB:ENSG00000120915.13; -.
GeneCards; EPHX2; -.
HGNC; HGNC:3402; EPHX2.
HPA; HPA023094; -.
HPA; HPA023660; -.
MalaCards; EPHX2; -.
MIM; 132811; gene.
neXtProt; NX_P34913; -.
OpenTargets; ENSG00000120915; -.
PharmGKB; PA27830; -.
eggNOG; KOG3085; Eukaryota.
eggNOG; KOG4178; Eukaryota.
eggNOG; COG1011; LUCA.
GeneTree; ENSGT00530000063213; -.
HOGENOM; HOG000028073; -.
HOVERGEN; HBG006095; -.
InParanoid; P34913; -.
KO; K08726; -.
OMA; GHWTQMD; -.
OrthoDB; EOG091G078G; -.
PhylomeDB; P34913; -.
TreeFam; TF315395; -.
BRENDA; 3.3.2.10; 2681.
Reactome; R-HSA-2142670; Synthesis of epoxy (EET) and dihydroxyeicosatrienoic acids (DHET).
Reactome; R-HSA-9018682; Biosynthesis of maresins.
Reactome; R-HSA-9033241; Peroxisomal protein import.
SABIO-RK; P34913; -.
ChiTaRS; EPHX2; human.
EvolutionaryTrace; P34913; -.
GeneWiki; Epoxide_hydrolase_2; -.
GenomeRNAi; 2053; -.
PRO; PR:P34913; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000120915; -.
CleanEx; HS_EPHX2; -.
ExpressionAtlas; P34913; baseline and differential.
Genevisible; P34913; HS.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005782; C:peroxisomal matrix; TAS:Reactome.
GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
GO; GO:0033885; F:10-hydroxy-9-(phosphonooxy)octadecanoate phosphatase activity; IEA:UniProtKB-EC.
GO; GO:0004301; F:epoxide hydrolase activity; IDA:UniProtKB.
GO; GO:0042577; F:lipid phosphatase activity; IDA:UniProtKB.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0016791; F:phosphatase activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
GO; GO:0015643; F:toxic substance binding; IDA:UniProtKB.
GO; GO:0006874; P:cellular calcium ion homeostasis; NAS:UniProtKB.
GO; GO:0042632; P:cholesterol homeostasis; IDA:UniProtKB.
GO; GO:0016311; P:dephosphorylation; IDA:UniProtKB.
GO; GO:0017144; P:drug metabolic process; NAS:UniProtKB.
GO; GO:0097176; P:epoxide metabolic process; IDA:UniProtKB.
GO; GO:0019373; P:epoxygenase P450 pathway; TAS:Reactome.
GO; GO:0006954; P:inflammatory response; NAS:UniProtKB.
GO; GO:0042759; P:long-chain fatty acid biosynthetic process; TAS:Reactome.
GO; GO:0046839; P:phospholipid dephosphorylation; IDA:UniProtKB.
GO; GO:0097755; P:positive regulation of blood vessel diameter; NAS:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
GO; GO:0006625; P:protein targeting to peroxisome; TAS:Reactome.
GO; GO:0072593; P:reactive oxygen species metabolic process; NAS:UniProtKB.
GO; GO:0008217; P:regulation of blood pressure; NAS:UniProtKB.
GO; GO:0090181; P:regulation of cholesterol metabolic process; IMP:UniProtKB.
GO; GO:0009636; P:response to toxic substance; NAS:UniProtKB.
GO; GO:0046272; P:stilbene catabolic process; IDA:UniProtKB.
GO; GO:0006805; P:xenobiotic metabolic process; NAS:UniProtKB.
Gene3D; 1.10.150.240; -; 1.
Gene3D; 3.40.50.1000; -; 2.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR000073; AB_hydrolase_1.
InterPro; IPR000639; Epox_hydrolase-like.
InterPro; IPR036412; HAD-like_sf.
InterPro; IPR006439; HAD-SF_hydro_IA.
InterPro; IPR011945; HAD-SF_ppase_IA/epoxid_hydro_N.
InterPro; IPR023214; HAD_sf.
InterPro; IPR023198; PGP-like_dom2.
Pfam; PF00561; Abhydrolase_1; 1.
PRINTS; PR00111; ABHYDROLASE.
PRINTS; PR00412; EPOXHYDRLASE.
SUPFAM; SSF53474; SSF53474; 1.
SUPFAM; SSF56784; SSF56784; 1.
TIGRFAMs; TIGR02247; HAD-1A3-hyp; 1.
TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing;
Aromatic hydrocarbons catabolism; Complete proteome; Cytoplasm;
Detoxification; Direct protein sequencing; Hydrolase;
Lipid metabolism; Lipoprotein; Magnesium; Metal-binding;
Multifunctional enzyme; Peroxisome; Phosphoprotein; Polymorphism;
Reference proteome.
CHAIN 1 555 Bifunctional epoxide hydrolase 2.
/FTId=PRO_0000084111.
DOMAIN 259 531 AB hydrolase-1. {ECO:0000255}.
REGION 1 224 Phosphatase.
REGION 123 124 Phosphate binding.
{ECO:0000269|PubMed:15096040}.
REGION 235 555 Epoxide hydrolase.
MOTIF 553 555 Microbody targeting signal.
{ECO:0000255}.
ACT_SITE 335 335 Nucleophile.
{ECO:0000269|PubMed:15096040,
ECO:0000269|PubMed:16322563,
ECO:0000269|PubMed:19746975,
ECO:0000269|PubMed:19969453,
ECO:0000269|PubMed:20934334}.
ACT_SITE 466 466 Proton donor.
{ECO:0000269|PubMed:15096040,
ECO:0000269|PubMed:16322563,
ECO:0000269|PubMed:19746975,
ECO:0000269|PubMed:19969453,
ECO:0000269|PubMed:20934334}.
ACT_SITE 524 524 Proton acceptor.
{ECO:0000269|PubMed:15096040,
ECO:0000269|PubMed:16322563,
ECO:0000269|PubMed:19746975,
ECO:0000269|PubMed:19969453,
ECO:0000269|PubMed:20934334}.
METAL 9 9 Magnesium. {ECO:0000269|PubMed:15096040}.
METAL 11 11 Magnesium. {ECO:0000269|PubMed:15096040}.
METAL 185 185 Magnesium. {ECO:0000269|PubMed:15096040}.
BINDING 383 383 Substrate. {ECO:0000269|PubMed:15096040,
ECO:0000269|PubMed:16322563,
ECO:0000269|PubMed:19746975,
ECO:0000269|PubMed:19969453,
ECO:0000269|PubMed:20934334}.
MOD_RES 43 43 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 55 55 N6-succinyllysine.
{ECO:0000250|UniProtKB:P34914}.
MOD_RES 191 191 N6-acetyllysine.
{ECO:0000250|UniProtKB:P34914}.
MOD_RES 215 215 N6-acetyllysine.
{ECO:0000250|UniProtKB:P34914}.
MOD_RES 370 370 Phosphoserine.
{ECO:0000250|UniProtKB:P34914}.
MOD_RES 421 421 N6-succinyllysine.
{ECO:0000250|UniProtKB:P34914}.
MOD_RES 455 455 N6-succinyllysine.
{ECO:0000250|UniProtKB:P34914}.
MOD_RES 554 554 N6-succinyllysine.
{ECO:0000250|UniProtKB:P34914}.
LIPID 522 522 S-(15-deoxy-Delta12,14-prostaglandin J2-
9-yl)cysteine.
{ECO:0000305|PubMed:21164107}.
VAR_SEQ 1 66 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045597.
VAR_SEQ 1 53 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045598.
VARIANT 21 21 G -> A (in dbSNP:rs72473930).
{ECO:0000269|Ref.6}.
/FTId=VAR_055392.
VARIANT 52 52 R -> Q (in dbSNP:rs72475803).
{ECO:0000269|Ref.6}.
/FTId=VAR_055393.
VARIANT 55 55 K -> R (decreased phosphatase activity;
no effect on epoxyde hydrolase activity;
dbSNP:rs41507953).
{ECO:0000269|PubMed:12869654,
ECO:0000269|PubMed:15196990,
ECO:0000269|Ref.6}.
/FTId=VAR_051059.
VARIANT 103 103 R -> C (decreased phosphatase activity;
no effect on epoxyde hydrolase activity;
dbSNP:rs17057255).
{ECO:0000269|PubMed:12869654,
ECO:0000269|PubMed:15196990,
ECO:0000269|Ref.6}.
/FTId=VAR_033991.
VARIANT 154 154 C -> Y (decreased phosphatase activity;
no effect on epoxyde hydrolase activity;
dbSNP:rs57699806).
{ECO:0000269|PubMed:12869654,
ECO:0000269|PubMed:15196990,
ECO:0000269|Ref.6}.
/FTId=VAR_055394.
VARIANT 225 225 P -> L (in dbSNP:rs72475821).
{ECO:0000269|Ref.6}.
/FTId=VAR_055395.
VARIANT 287 287 R -> Q (no effect on phosphatase
activity; decreased epoxyde hydrolase
activity; dbSNP:rs751141).
{ECO:0000269|PubMed:10862610,
ECO:0000269|PubMed:12869654,
ECO:0000269|PubMed:15196990,
ECO:0000269|PubMed:8342951,
ECO:0000269|Ref.6}.
/FTId=VAR_014852.
VARIANT 369 369 M -> V (in dbSNP:rs72475894).
{ECO:0000269|Ref.6}.
/FTId=VAR_055396.
VARIANT 403 403 R -> RR. {ECO:0000269|PubMed:10862610,
ECO:0000269|PubMed:14702039}.
/FTId=VAR_022613.
VARIANT 470 470 E -> G (no effect on phosphatase activity
and epoxyde hydrolase activity;
dbSNP:rs68053459).
{ECO:0000269|PubMed:12869654,
ECO:0000269|PubMed:15196990,
ECO:0000269|Ref.6}.
/FTId=VAR_055397.
MUTAGEN 9 9 D->A: Loss of phosphatase activity.
{ECO:0000269|PubMed:12574508}.
MUTAGEN 522 522 C->S: Loss of S-(15-deoxy-Delta12,14-
prostaglandin J2-9-yl)cysteine-induced
inhibition of epoxide hydrolase activity.
{ECO:0000269|PubMed:21164107}.
CONFLICT 5 5 A -> G (in Ref. 1; AAA02756).
{ECO:0000305}.
CONFLICT 257 258 SG -> W (in Ref. 1; AAA02756).
{ECO:0000305}.
CONFLICT 409 409 F -> L (in Ref. 5; BAG53362).
{ECO:0000305}.
CONFLICT 473 473 W -> R (in Ref. 5; BAG53362).
{ECO:0000305}.
CONFLICT 494 494 E -> G (in Ref. 5; BAG53362).
{ECO:0000305}.
STRAND 5 8 {ECO:0000244|PDB:5MWA}.
TURN 12 14 {ECO:0000244|PDB:5MWA}.
STRAND 15 17 {ECO:0000244|PDB:5AM2}.
HELIX 19 29 {ECO:0000244|PDB:5MWA}.
HELIX 36 42 {ECO:0000244|PDB:5MWA}.
HELIX 45 47 {ECO:0000244|PDB:5MWA}.
HELIX 49 54 {ECO:0000244|PDB:5MWA}.
STRAND 57 59 {ECO:0000244|PDB:5ALI}.
HELIX 60 72 {ECO:0000244|PDB:5MWA}.
TURN 77 79 {ECO:0000244|PDB:5ALG}.
HELIX 88 97 {ECO:0000244|PDB:5MWA}.
HELIX 103 114 {ECO:0000244|PDB:5MWA}.
STRAND 118 123 {ECO:0000244|PDB:5MWA}.
TURN 131 133 {ECO:0000244|PDB:5AM2}.
HELIX 140 145 {ECO:0000244|PDB:5MWA}.
STRAND 147 152 {ECO:0000244|PDB:5MWA}.
HELIX 153 156 {ECO:0000244|PDB:5MWA}.
STRAND 160 162 {ECO:0000244|PDB:5ALQ}.
HELIX 163 173 {ECO:0000244|PDB:5MWA}.
HELIX 177 179 {ECO:0000244|PDB:5MWA}.
STRAND 180 185 {ECO:0000244|PDB:5MWA}.
HELIX 187 195 {ECO:0000244|PDB:5MWA}.
STRAND 199 202 {ECO:0000244|PDB:5MWA}.
HELIX 206 217 {ECO:0000244|PDB:5MWA}.
HELIX 234 236 {ECO:0000244|PDB:5AM2}.
STRAND 237 245 {ECO:0000244|PDB:5AM2}.
STRAND 248 255 {ECO:0000244|PDB:5AM2}.
STRAND 257 264 {ECO:0000244|PDB:5AM2}.
HELIX 271 274 {ECO:0000244|PDB:5AM2}.
TURN 275 277 {ECO:0000244|PDB:5AM2}.
HELIX 278 283 {ECO:0000244|PDB:5AM2}.
STRAND 287 291 {ECO:0000244|PDB:5AM2}.
HELIX 305 308 {ECO:0000244|PDB:5AM2}.
HELIX 310 324 {ECO:0000244|PDB:5AM2}.
STRAND 329 334 {ECO:0000244|PDB:5AM2}.
HELIX 336 347 {ECO:0000244|PDB:5AM2}.
HELIX 349 351 {ECO:0000244|PDB:5AM2}.
STRAND 352 359 {ECO:0000244|PDB:5AM2}.
STRAND 367 369 {ECO:0000244|PDB:4X6X}.
HELIX 371 376 {ECO:0000244|PDB:5AM2}.
HELIX 379 382 {ECO:0000244|PDB:5AM2}.
HELIX 383 386 {ECO:0000244|PDB:5AM2}.
HELIX 392 398 {ECO:0000244|PDB:5AM2}.
HELIX 401 408 {ECO:0000244|PDB:5AM2}.
HELIX 412 414 {ECO:0000244|PDB:4X6X}.
HELIX 419 421 {ECO:0000244|PDB:4JNC}.
TURN 424 426 {ECO:0000244|PDB:5AM2}.
TURN 428 431 {ECO:0000244|PDB:5AM2}.
STRAND 440 442 {ECO:0000244|PDB:5AIA}.
HELIX 444 455 {ECO:0000244|PDB:5AM2}.
TURN 456 459 {ECO:0000244|PDB:5AM2}.
HELIX 460 464 {ECO:0000244|PDB:5AM2}.
TURN 465 468 {ECO:0000244|PDB:5ALV}.
HELIX 469 477 {ECO:0000244|PDB:5AM2}.
TURN 478 481 {ECO:0000244|PDB:5AM2}.
STRAND 488 493 {ECO:0000244|PDB:5AM2}.
STRAND 497 499 {ECO:0000244|PDB:5AM2}.
HELIX 501 504 {ECO:0000244|PDB:5AM2}.
HELIX 507 509 {ECO:0000244|PDB:5AM2}.
STRAND 515 519 {ECO:0000244|PDB:5AM2}.
HELIX 526 529 {ECO:0000244|PDB:5AM2}.
HELIX 531 545 {ECO:0000244|PDB:5AM2}.
SEQUENCE 555 AA; 62616 MW; 1B5ACE7F80F9A26C 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
YVTVKPRVRL HFVELGSGPA VCLCHGFPES WYSWRYQIPA LAQAGYRVLA MDMKGYGESS
APPEIEEYCM EVLCKEMVTF LDKLGLSQAV FIGHDWGGML VWYMALFYPE RVRAVASLNT
PFIPANPNMS PLESIKANPV FDYQLYFQEP GVAEAELEQN LSRTFKSLFR ASDESVLSMH
KVCEAGGLFV NSPEEPSLSR MVTEEEIQFY VQQFKKSGFR GPLNWYRNME RNWKWACKSL
GRKILIPALM VTAEKDFVLV PQMSQHMEDW IPHLKRGHIE DCGHWTQMDK PTEVNQILIK
WLDSDARNPP VVSKM


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