EPHX3_XENTR
ID EPHX3_XENTR Reviewed; 367 AA.
AC Q0IIS3;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Epoxide hydrolase 3;
DE Short=EH3 {ECO:0000250|UniProtKB:Q9H6B9};
DE EC=3.3.2.10 {ECO:0000250|UniProtKB:Q9H6B9};
DE AltName: Full=Abhydrolase domain-containing protein 9;
GN Name=ephx3; Synonyms=abhd9;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=N6; TISSUE=Skeletal muscle;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the hydrolysis of epoxide-containing fatty acids.
CC Active in vitro against epoxyeicosatrienoic acids (EETs) including 8,9-
CC EET, 9,10-EET, 11,12-EET and 14,15-EET and leukotoxin.
CC {ECO:0000250|UniProtKB:Q9H6B9}.
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:Q9H6B9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19038;
CC Evidence={ECO:0000250|UniProtKB:Q9H6B9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=9,10-epoxyoctadecanoate + H2O = 9,10-dihydroxyoctadecanoate;
CC Xref=Rhea:RHEA:45352, ChEBI:CHEBI:15377, ChEBI:CHEBI:85195,
CC ChEBI:CHEBI:85197; Evidence={ECO:0000250|UniProtKB:Q9H6B9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45353;
CC Evidence={ECO:0000250|UniProtKB:Q9H6B9};
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:Q9H6B9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44033;
CC Evidence={ECO:0000250|UniProtKB:Q9H6B9};
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:Q9H6B9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44049;
CC Evidence={ECO:0000250|UniProtKB:Q9H6B9};
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:Q9H6B9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44045;
CC Evidence={ECO:0000250|UniProtKB:Q9H6B9};
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:Q9H6B9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44041;
CC Evidence={ECO:0000250|UniProtKB:Q9H6B9};
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 and to a lesser extent by 8-(3-((3S, 5S, 7S)-adamantan-1-yl)ureido)
CC octanoic acid (AUOA). {ECO:0000250|UniProtKB:Q9H6B9}.
CC -!- SUBCELLULAR LOCATION: Microsome membrane
CC {ECO:0000250|UniProtKB:Q9H6B9}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Epoxide hydrolase
CC family. {ECO:0000305}.
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DR EMBL; BC121674; AAI21675.1; -; mRNA.
DR RefSeq; NP_001072430.1; NM_001078962.1.
DR AlphaFoldDB; Q0IIS3; -.
DR SMR; Q0IIS3; -.
DR STRING; 8364.ENSXETP00000005474; -.
DR ESTHER; xentr-ephx3; Epoxide_hydrolase.
DR MEROPS; S33.978; -.
DR PaxDb; Q0IIS3; -.
DR DNASU; 779884; -.
DR GeneID; 779884; -.
DR KEGG; xtr:779884; -.
DR CTD; 79852; -.
DR Xenbase; XB-GENE-5900414; ephx3.
DR eggNOG; KOG4178; Eukaryota.
DR HOGENOM; CLU_020336_7_3_1; -.
DR InParanoid; Q0IIS3; -.
DR OMA; IAMRSNK; -.
DR OrthoDB; 616687at2759; -.
DR PhylomeDB; Q0IIS3; -.
DR TreeFam; TF314403; -.
DR Proteomes; UP000008143; Chromosome 3.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000002569; Expressed in skeletal muscle tissue and 13 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004301; F:epoxide hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0016787; F:hydrolase activity; IBA:GO_Central.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR000639; Epox_hydrolase-like.
DR Pfam; PF12697; Abhydrolase_6; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR PRINTS; PR00412; EPOXHYDRLASE.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Hydrolase; Lipid metabolism; Membrane; Microsome;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..367
FT /note="Epoxide hydrolase 3"
FT /id="PRO_0000281380"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 173
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P34913"
FT ACT_SITE 285
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P34913"
FT ACT_SITE 340
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P34913"
SQ SEQUENCE 367 AA; 42217 MW; C1EB327583F123C2 CRC64;
MQLYLSRLLL IVTRTALRVT GVFFWVLVYV AALLAAVSYI PDALRLLTRG PLSAFRWGPR
KAAPACLTSS AHGQHGYIRM KDSGIRFHYV ASGDKRNPLM LLLHGFPENW YSWRYQLDEF
SNGYRTVAID LRGFGGSDAP SRLEDYKMEI LLQDLQDLIR GLGYSRCVLV GHDWGGTLAW
TFAVRHRDMV THLIVMNAPH PSAFHDYVLS HPSQLFSSRY VFLFQLPLIP EILLSLRDFE
HIKKPLTDAT HGIQNVECKL SKEEVEAFVY YPSQKGALTP PLNYYRNLFG FFPVKAQDVL
VPTLLLWGEH DAFLEAAMVP EMQQYVRAPF RAEIIPNASH WLQQDRPQEV NKIIRDFLKE
DFLVHRN
