HYEP_PIG
ID HYEP_PIG Reviewed; 454 AA.
AC P79381;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Epoxide hydrolase 1;
DE EC=3.3.2.9 {ECO:0000250|UniProtKB:P07687};
DE AltName: Full=Epoxide hydratase;
DE AltName: Full=Microsomal epoxide hydrolase;
DE Short=mEH {ECO:0000305};
GN Name=EPHX1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kawakami K., Kimura M., Suzuki H., Hamasima N.;
RT "Cloning of the pig epoxide hydrolase gene.";
RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Biotransformation enzyme that catalyzes the hydrolysis of
CC arene and aliphatic epoxides to less reactive and more water soluble
CC dihydrodiols by the trans addition of water. May play a role in the
CC metabolism of endogenous lipids such as epoxide-containing fatty acids.
CC Metabolizes the abundant endocannabinoid 2-arachidonoylglycerol (2-AG)
CC to free arachidonic acid (AA) and glycerol (By similarity).
CC {ECO:0000250|UniProtKB:P07099, ECO:0000250|UniProtKB:P07687}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cis-stilbene oxide + H2O = (1R,2R)-hydrobenzoin;
CC Xref=Rhea:RHEA:23900, ChEBI:CHEBI:15377, ChEBI:CHEBI:50004,
CC ChEBI:CHEBI:50014; EC=3.3.2.9;
CC Evidence={ECO:0000250|UniProtKB:P07099,
CC ECO:0000250|UniProtKB:P07687};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23901;
CC Evidence={ECO:0000250|UniProtKB:P07099};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(4-methoxyphenyl)-N-methyl-N-[(3-methyloxetan-3-
CC yl)methyl]methanamine + H2O = 2-{[(4-
CC methoxybenzyl)(methyl)amino]methyl}-2-methylpropane-1,3-diol;
CC Xref=Rhea:RHEA:55764, ChEBI:CHEBI:15377, ChEBI:CHEBI:139161,
CC ChEBI:CHEBI:139164; EC=3.3.2.9;
CC Evidence={ECO:0000250|UniProtKB:P07687};
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:P07099};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44049;
CC Evidence={ECO:0000250|UniProtKB:P07099};
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:P07099};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44045;
CC Evidence={ECO:0000250|UniProtKB:P07099};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-glycerol + H2O =
CC (5Z,8Z,11Z,14Z)-eicosatetraenoate + glycerol + H(+);
CC Xref=Rhea:RHEA:26132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17754, ChEBI:CHEBI:32395, ChEBI:CHEBI:52392;
CC Evidence={ECO:0000250|UniProtKB:P07099};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26133;
CC Evidence={ECO:0000250|UniProtKB:P07099};
CC -!- ACTIVITY REGULATION: Inhibited by 10-hydroxystearamide and methoxy-
CC arachidonyl fluorophosphate. {ECO:0000250|UniProtKB:P07099}.
CC -!- SUBCELLULAR LOCATION: Microsome membrane
CC {ECO:0000250|UniProtKB:P07687}; Single-pass type III membrane protein
CC {ECO:0000250|UniProtKB:P07687}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P07687}; Single-pass type III membrane protein
CC {ECO:0000250|UniProtKB:P07687}.
CC -!- SIMILARITY: Belongs to the peptidase S33 family. {ECO:0000305}.
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DR EMBL; AB000883; BAA19200.1; -; mRNA.
DR RefSeq; NP_999520.1; NM_214355.1.
DR RefSeq; XP_005653835.1; XM_005653778.1.
DR RefSeq; XP_005653836.1; XM_005653779.1.
DR RefSeq; XP_005653837.1; XM_005653780.1.
DR RefSeq; XP_005653838.1; XM_005653781.2.
DR RefSeq; XP_005653839.1; XM_005653782.1.
DR RefSeq; XP_005653840.1; XM_005653783.1.
DR RefSeq; XP_013833722.1; XM_013978268.1.
DR AlphaFoldDB; P79381; -.
DR SMR; P79381; -.
DR STRING; 9823.ENSSSCP00000011571; -.
DR ESTHER; pig-hyep; Epoxide_hydrolase.
DR MEROPS; S33.971; -.
DR PaxDb; P79381; -.
DR PeptideAtlas; P79381; -.
DR PRIDE; P79381; -.
DR Ensembl; ENSSSCT00015043861; ENSSSCP00015017323; ENSSSCG00015033152.
DR Ensembl; ENSSSCT00045065906; ENSSSCP00045046673; ENSSSCG00045038103.
DR Ensembl; ENSSSCT00045065922; ENSSSCP00045046688; ENSSSCG00045038103.
DR Ensembl; ENSSSCT00045065941; ENSSSCP00045046706; ENSSSCG00045038103.
DR Ensembl; ENSSSCT00045065962; ENSSSCP00045046726; ENSSSCG00045038103.
DR Ensembl; ENSSSCT00045065992; ENSSSCP00045046752; ENSSSCG00045038103.
DR Ensembl; ENSSSCT00045066013; ENSSSCP00045046770; ENSSSCG00045038103.
DR Ensembl; ENSSSCT00045066037; ENSSSCP00045046791; ENSSSCG00045038103.
DR Ensembl; ENSSSCT00045066069; ENSSSCP00045046818; ENSSSCG00045038103.
DR Ensembl; ENSSSCT00045066109; ENSSSCP00045046847; ENSSSCG00045038103.
DR Ensembl; ENSSSCT00055028045; ENSSSCP00055022343; ENSSSCG00055014206.
DR Ensembl; ENSSSCT00070013483; ENSSSCP00070011117; ENSSSCG00070006950.
DR Ensembl; ENSSSCT00070013491; ENSSSCP00070011123; ENSSSCG00070006950.
DR Ensembl; ENSSSCT00070013511; ENSSSCP00070011138; ENSSSCG00070006950.
DR GeneID; 397639; -.
DR KEGG; ssc:397639; -.
DR CTD; 2052; -.
DR eggNOG; KOG2565; Eukaryota.
DR HOGENOM; CLU_019414_3_0_1; -.
DR InParanoid; P79381; -.
DR OrthoDB; 898504at2759; -.
DR TreeFam; TF313813; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unassembled WGS sequence.
DR Genevisible; P79381; SS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0033961; F:cis-stilbene-oxide hydrolase activity; ISS:UniProtKB.
DR GO; GO:0004301; F:epoxide hydrolase activity; ISS:UniProtKB.
DR GO; GO:0019369; P:arachidonic acid metabolic process; ISS:UniProtKB.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0097176; P:epoxide metabolic process; IBA:GO_Central.
DR GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000639; Epox_hydrolase-like.
DR InterPro; IPR010497; Epoxide_hydro_N.
DR InterPro; IPR016292; Epoxide_hydrolase.
DR Pfam; PF06441; EHN; 1.
DR PIRSF; PIRSF001112; Epoxide_hydrolase; 1.
DR PRINTS; PR00412; EPOXHYDRLASE.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 2: Evidence at transcript level;
KW Aromatic hydrocarbons catabolism; Detoxification; Endoplasmic reticulum;
KW Hydrolase; Lipid metabolism; Membrane; Methylation; Microsome;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..454
FT /note="Epoxide hydrolase 1"
FT /id="PRO_0000080857"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P07687"
FT TOPO_DOM 22..454
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P07687"
FT ACT_SITE 226
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P07687"
FT ACT_SITE 373
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P34913"
FT ACT_SITE 430
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P07687"
FT MOD_RES 294
FT /note="Dimethylated arginine"
FT /evidence="ECO:0000250|UniProtKB:P07687"
SQ SEQUENCE 454 AA; 52394 MW; BF3D34884565E092 CRC64;
MWLEILLASV LGFVIYWFVS KDKEETLLLG DGWWGPGSRP AAAEDESIRP FKVETSDEEI
NDLHQRIEKF RLTPPLEDSR FHYGFNSNYL KKIISYWRNT FDWRKQVEVL NKYPHFKTKI
EGLDIHFIHV KPPQLPSGRT AKPLLMVHGW PGCFYEFYKI IPLLTDPKNH GLSDEHVFEV
ICPSIPGYGF SEASSKKGFN SVAAARIFYK LMLRLGFQEF YLQGGDWGSL ICTNMAQLVP
SHVKGLHLNV ALVLRNVYTL TFFLGRRLGR LFGYTERDLE LLYPFKKTFY TLMRESGYMH
IQSTKPDTVG CALNDSPVGL AAYILEKFST WTNEEFRDLE DGGLERKFSL DELLTVIMLY
WTTGTITSSQ RFYKENLGQG VMANKHEAIK VHVPTGFAAF PSEVLHCPEK WVKNKYPKLI
SYSYMARGGH FAAFEEPELL AQDIRKFMGL LEQQ
