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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_RAT                Reviewed;         554 AA.
P80299;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 1.
22-NOV-2017, entry version 133.
RecName: Full=Bifunctional epoxide hydrolase 2;
Includes:
RecName: Full=Cytosolic epoxide hydrolase 2;
Short=CEH;
EC=3.3.2.10 {ECO:0000269|PubMed:8626766};
AltName: Full=Epoxide hydratase;
AltName: Full=Soluble epoxide hydrolase;
Short=SEH;
Includes:
RecName: Full=Lipid-phosphate phosphatase;
EC=3.1.3.76 {ECO:0000305|PubMed:12574508};
Name=Ephx2;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Liver;
PubMed=8349641;
Knehr M., Thomas H., Arand M., Gebel T., Zeller H.-D., Oesch F.;
"Isolation and characterization of a cDNA encoding rat liver cytosolic
epoxide hydrolase and its functional expression in Escherichia coli.";
J. Biol. Chem. 268:17623-17627(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 450-554, AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Liver;
PubMed=1743286; DOI=10.1016/0014-5793(91)81333-4;
Arand M., Knehr M., Thomas H., Zeller H.-D., Oesch F.;
"An impaired peroxisomal targeting sequence leading to an unusual
bicompartmental distribution of cytosolic epoxide hydrolase.";
FEBS Lett. 294:19-22(1991).
[3]
FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-333; TRP-334;
GLU-433; ASP-434; GLU-493; ASP-495; HIS-517; CYS-521; HIS-523;
GLN-526; TRP-540 AND LYS-542, AND ACTIVE SITE.
PubMed=8626766; DOI=10.1074/jbc.271.8.4223;
Arand M., Wagner H., Oesch F.;
"Asp333, Asp495, and His523 form the catalytic triad of rat soluble
epoxide hydrolase.";
J. Biol. Chem. 271:4223-4229(1996).
[4]
FUNCTION, PHOSPHATASE ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
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).
-!- FUNCTION: Bifunctional enzyme (PubMed:8626766, PubMed:12574508).
The C-terminal domain has epoxide hydrolase activity and acts on
epoxides (alkene oxides, oxiranes) and arene oxides
(PubMed:8626766). Plays a role in xenobiotic metabolism by
degrading potentially toxic epoxides (PubMed:8626766). Also
determines steady-state levels of physiological mediators (By
similarity). The N-terminal domain has lipid phosphatase activity,
with the highest activity towards threo-9,10-phosphonooxy-hydroxy-
octadecanoic acid, followed by erythro-9,10-phosphonooxy-hydroxy-
octadecanoic acid, 12-phosphonooxy-octadec-9Z-enoic acid and 12-
phosphonooxy-octadec-9E-enoic acid (By similarity).
{ECO:0000250|UniProtKB:P34913, ECO:0000269|PubMed:12574508,
ECO:0000269|PubMed:8626766}.
-!- CATALYTIC ACTIVITY: An epoxide + H(2)O = a glycol.
{ECO:0000269|PubMed:8626766}.
-!- CATALYTIC ACTIVITY: (9S,10S)-10-hydroxy-9-
(phosphonooxy)octadecanoate + H(2)O = (9S,10S)-9,10-
dihydroxyoctadecanoate + phosphate. {ECO:0000305|PubMed:12574508}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:P34913};
-!- 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:0000250|UniProtKB:P34913}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.235 mM for p-nitrophenyl phosphate
{ECO:0000269|PubMed:12574508};
Vmax=1450 nmol/min/mg enzyme {ECO:0000269|PubMed:12574508};
-!- SUBUNIT: Homodimer.
-!- SUBCELLULAR LOCATION: Cytoplasm. Peroxisome.
-!- 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 covalent modification of cysteine by 15-deoxy-Delta12,14-
prostaglandin-J2 is autocatalytic and reversible. It may occur as
an alternative to other cysteine modifications, such as S-
nitrosylation and S-palmitoylation (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the AB hydrolase superfamily. Epoxide
hydrolase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X65083; CAA46211.1; -; mRNA.
EMBL; X60328; CAA42898.1; -; mRNA.
PIR; A47503; A47503.
RefSeq; NP_075225.1; NM_022936.1.
UniGene; Rn.54495; -.
ProteinModelPortal; P80299; -.
SMR; P80299; -.
STRING; 10116.ENSRNOP00000023385; -.
BindingDB; P80299; -.
ChEMBL; CHEMBL5669; -.
SwissLipids; SLP:000001643; -.
ESTHER; ratno-hyes; Epoxide_hydrolase.
MEROPS; S33.973; -.
iPTMnet; P80299; -.
PhosphoSitePlus; P80299; -.
PaxDb; P80299; -.
PRIDE; P80299; -.
GeneID; 65030; -.
KEGG; rno:65030; -.
UCSC; RGD:620732; rat.
CTD; 2053; -.
RGD; 620732; Ephx2.
eggNOG; KOG3085; Eukaryota.
eggNOG; KOG4178; Eukaryota.
eggNOG; COG1011; LUCA.
HOGENOM; HOG000028073; -.
HOVERGEN; HBG006095; -.
InParanoid; P80299; -.
KO; K08726; -.
PhylomeDB; P80299; -.
BRENDA; 3.3.2.10; 5301.
SABIO-RK; P80299; -.
PRO; PR:P80299; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0005777; C:peroxisome; IDA:RGD.
GO; GO:0033885; F:10-hydroxy-9-(phosphonooxy)octadecanoate phosphatase activity; IEA:UniProtKB-EC.
GO; GO:0004301; F:epoxide hydrolase activity; IDA:RGD.
GO; GO:0042577; F:lipid phosphatase activity; ISS:UniProtKB.
GO; GO:0000287; F:magnesium ion binding; IMP:RGD.
GO; GO:0016791; F:phosphatase activity; IDA:RGD.
GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
GO; GO:0005102; F:receptor binding; ISO:RGD.
GO; GO:0015643; F:toxic substance binding; ISO:RGD.
GO; GO:0042632; P:cholesterol homeostasis; ISO:RGD.
GO; GO:0016311; P:dephosphorylation; ISO:RGD.
GO; GO:0097176; P:epoxide metabolic process; ISO:RGD.
GO; GO:0006954; P:inflammatory response; IMP:RGD.
GO; GO:0043651; P:linoleic acid metabolic process; IMP:RGD.
GO; GO:0046839; P:phospholipid dephosphorylation; ISS:UniProtKB.
GO; GO:0045777; P:positive regulation of blood pressure; IMP:RGD.
GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
GO; GO:0002539; P:prostaglandin production involved in inflammatory response; IMP:RGD.
GO; GO:0090181; P:regulation of cholesterol metabolic process; ISO:RGD.
GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
GO; GO:0019233; P:sensory perception of pain; IMP:RGD.
GO; GO:0046272; P:stilbene catabolic process; ISO:RGD.
Gene3D; 1.10.150.240; -; 1.
Gene3D; 3.40.50.1000; -; 1.
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_dom2.
Pfam; PF00561; Abhydrolase_1; 1.
PRINTS; PR00111; ABHYDROLASE.
PRINTS; PR00412; EPOXHYDRLASE.
SUPFAM; SSF53474; SSF53474; 2.
SUPFAM; SSF56784; SSF56784; 1.
TIGRFAMs; TIGR02247; HAD-1A3-hyp; 1.
TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1.
1: Evidence at protein level;
Acetylation; Aromatic hydrocarbons catabolism; Complete proteome;
Cytoplasm; Detoxification; Direct protein sequencing; Hydrolase;
Lipid metabolism; Lipoprotein; Magnesium; Metal-binding;
Multifunctional enzyme; Peroxisome; Phosphoprotein;
Reference proteome.
CHAIN 1 554 Bifunctional epoxide hydrolase 2.
/FTId=PRO_0000084114.
DOMAIN 257 530 AB hydrolase-1. {ECO:0000255}.
REGION 1 224 Phosphatase.
REGION 123 124 Phosphate binding.
{ECO:0000250|UniProtKB:P34913}.
REGION 233 554 Epoxide hydrolase.
MOTIF 552 554 Microbody targeting signal.
{ECO:0000255}.
ACT_SITE 333 333 Nucleophile.
{ECO:0000269|PubMed:8626766}.
ACT_SITE 465 465 Proton donor.
{ECO:0000250|UniProtKB:P34913}.
ACT_SITE 523 523 Proton acceptor.
{ECO:0000269|PubMed:8626766}.
METAL 9 9 Magnesium.
{ECO:0000250|UniProtKB:P34913}.
METAL 11 11 Magnesium.
{ECO:0000250|UniProtKB:P34913}.
METAL 185 185 Magnesium.
{ECO:0000250|UniProtKB:P34913}.
BINDING 381 381 Substrate.
{ECO:0000250|UniProtKB:P34913}.
MOD_RES 55 55 N6-succinyllysine.
{ECO:0000250|UniProtKB:P34914}.
MOD_RES 176 176 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P34914}.
MOD_RES 176 176 N6-succinyllysine; alternate.
{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 368 368 Phosphoserine.
{ECO:0000250|UniProtKB:P34914}.
MOD_RES 420 420 N6-succinyllysine.
{ECO:0000250|UniProtKB:P34914}.
MOD_RES 454 454 N6-succinyllysine.
{ECO:0000250|UniProtKB:P34914}.
MOD_RES 504 504 N6-succinyllysine.
{ECO:0000250|UniProtKB:P34914}.
MOD_RES 553 553 N6-succinyllysine.
{ECO:0000250|UniProtKB:P34914}.
LIPID 521 521 S-(15-deoxy-Delta12,14-prostaglandin J2-
9-yl)cysteine. {ECO:0000250}.
MUTAGEN 332 332 H->Q: Reduces epoxide hydrolase activity
by 95%.
MUTAGEN 333 333 D->G: Loss of epoxide hydrolase activity.
{ECO:0000269|PubMed:8626766}.
MUTAGEN 334 334 W->F: Slight reduction of epoxide
hydrolase activity.
{ECO:0000269|PubMed:8626766}.
MUTAGEN 433 433 E->Q,K: Slight loss of epoxide hydrolase
activity. {ECO:0000269|PubMed:8626766}.
MUTAGEN 434 434 D->Y: Slight loss of epoxide hydrolase
activity. {ECO:0000269|PubMed:8626766}.
MUTAGEN 493 493 E->Q,K: No effect.
{ECO:0000269|PubMed:8626766}.
MUTAGEN 495 495 D->H: Loss of epoxide hydrolase activity.
{ECO:0000269|PubMed:8626766}.
MUTAGEN 517 517 H->Y: Reduces epoxide hydrolase activity
by 50%. Loss of activity; when associated
with Y-521. {ECO:0000269|PubMed:8626766}.
MUTAGEN 521 521 C->Y: Loss of epoxide hydrolase activity;
when associated with Y-517.
{ECO:0000269|PubMed:8626766}.
MUTAGEN 523 523 H->D,N,Y: Loss of epoxide hydrolase
activity. {ECO:0000269|PubMed:8626766}.
MUTAGEN 526 526 Q->H: Reduces epoxide hydrolase activity
by 80%; when associated with T-542.
{ECO:0000269|PubMed:8626766}.
MUTAGEN 540 540 W->L,S: Reduces epoxide hydrolase
activity by 95%.
{ECO:0000269|PubMed:8626766}.
MUTAGEN 542 542 K->T: Reduces epoxide hydrolase activity
by 80%; when associated with H-526.
{ECO:0000269|PubMed:8626766}.
SEQUENCE 554 AA; 62340 MW; 145FDCA53F582138 CRC64;
MALRVAAFDL DGVLALPSIA GVLRHTEEAL ALPRDFLLGA FQMKFPEGPT EQLMKGKITF
SQWVPLMDES CRKSSKACGA SLPENFSISE IFSQAMAARS INRPMLQAAA ALKKKGFTTC
IVTNNWLDDS DKRDILAQMM CELSQHFDFL IESCQVGMIK PEPQIYKFVL DTLKAKPNEV
VFLDDFGSNL KPARDMGMVT ILVRDTASAL RELEKVTGTQ FPEAPLPVPC SPNDVSHGYV
TVKPGIRLHF VEMGSGPAIC LCHGFPESWF SWRYQIPALA QAGFRVLAID MKGYGDSSSP
PEIEEYAMEL LCEEMVTFLN KLGIPQAVFI GHDWAGVLVW NMALFHPERV RAVASLNTPL
MPPNPEVSPM EVIRSIPVFN YQLYFQEPGV AEAELEKNMS RTFKSFFRTS DDMGLLTVNK
ATEMGGILVG TPEDPKVSKI TTEEEIEYYI QQFKKSGFRG PLNWYRNTER NWKWSCKALG
RKILVPALMV TAEKDIVLRP EMSKNMENWI PFLKRGHIED CGHWTQIEKP AEVNQILIKW
LKTEIQNPSV TSKI


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