ID   HYEP_HUMAN     STANDARD;      PRT;   455 AA.
AC   P07099;
DT   01-APR-1988 (Rel. 07, Created)
DT   01-NOV-1988 (Rel. 09, Last sequence update)
DT   16-OCT-2001 (Rel. 40, Last annotation update)
DE   Epoxide hydrolase 1 (EC 3.3.2.3) (Microsomal epoxide hydrolase)
DE   (Epoxide hydratase).
GN   EPHX1 OR EPHX OR EPOX.
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   SEQUENCE FROM N.A., AND SEQUENCE OF 1-19.
RX   MEDLINE=88087301; PubMed=2891713;
RA   Skoda R.C., Demierre A., McBride O.W., Gonzalez F.J., Meyer U.A.;
RT   "Human microsomal xenobiotic epoxide hydrolase. Complementary DNA
RT   sequence, complementary DNA-directed expression in COS-1 cells, and
RT   chromosomal localization.";
RL   J. Biol. Chem. 263:1549-1554(1988).
RN   [2]
RP   SEQUENCE FROM N.A.
RC   TISSUE=Liver;
RA   Wilson N.M., Omiecinski C.J.;
RL   Submitted (JUL-1988) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   SEQUENCE FROM N.A.
RC   TISSUE=Liver;
RX   MEDLINE=88015564; PubMed=3502697;
RA   Jackson M.R., Craft J.A., Burchell B.;
RT   "Nucleotide and deduced amino acid sequence of human liver microsomal
RT   epoxide hydrolase.";
RL   Nucleic Acids Res. 15:7188-7188(1987).
RN   [4]
RP   SEQUENCE FROM N.A., AND VARIANTS HIS-113; ARG-139 AND ILE-396.
RC   TISSUE=Liver;
RX   MEDLINE=94282033; PubMed=7516776;
RA   Hassett C., Aicher L., Sidhu J.S., Omiecinski C.J.;
RT   "Human microsomal epoxide hydrolase: genetic polymorphism and
RT   functional expression in vitro of amino acid variants.";
RL   Hum. Mol. Genet. 3:421-428(1994).
RN   [5]
RP   ERRATUM.
RA   Hassett C., Aicher L., Sidhu J.S., Omiecinski C.J.;
RL   Hum. Mol. Genet. 3:1214-1214(1994).
RN   [6]
RP   SEQUENCE FROM N.A.
RX   MEDLINE=95137590; PubMed=7835893;
RA   Hassett C., Robinson K.B., Beck N.B., Omiecinski C.J.;
RT   "The human microsomal epoxide hydrolase gene (EPHX1): complete
RT   nucleotide sequence and structural characterization.";
RL   Genomics 23:433-442(1994).
RN   [7]
RP   SEQUENCE OF 9-327 FROM N.A.
RC   TISSUE=Liver;
RA   Craft J.A., Jackson M.R., Burchell B.;
RT   "Partial nucleotide sequence of a cloned cDNA for human liver
RT   microsomal epoxide hydrolase.";
RL   Biochem. Soc. Trans. 15:708-709(1987).
CC   -!- FUNCTION: BIOTRANSFORMATION ENZYME THAT CATALYZES THE HYDROLYSIS
CC       OF ARENE AND ALIPHATIC EPOXIDES TO LESS REACTIVE AND MORE WATER
CC       SOLUBLE DIHYDRODIOLS BY THE TRANS ADDITION OF WATER.
CC   -!- CATALYTIC ACTIVITY: AN EPOXIDE + H(2)O = A GLYCOL.
CC   -!- SUBCELLULAR LOCATION: MEMBRANE BOUND ON MICROSOMES.
CC   -!- SIMILARITY: BELONGS TO PEPTIDASE FAMILY S33.
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DR   EMBL; J03518; AAA61305.1; -.
DR   EMBL; X07936; CAA30759.1; -.
DR   EMBL; Y00424; CAA68486.1; -.
DR   EMBL; M36374; AAA59580.1; -.
DR   EMBL; L25878; AAA52389.1; -.
DR   EMBL; L25879; AAA52390.1; -.
DR   EMBL; AF253417; AAC41694.1; -.
DR   EMBL; U06661; AAB60649.1; -.
DR   EMBL; U06656; AAB60649.1; JOINED.
DR   EMBL; U06657; AAB60649.1; JOINED.
DR   EMBL; U06658; AAB60649.1; JOINED.
DR   EMBL; U06659; AAB60649.1; JOINED.
DR   EMBL; U06660; AAB60649.1; JOINED.
DR   PIR; S03114; S03114.
DR   PIR; A26856; A26856.
DR   PIR; A29939; A29939.
DR   MEROPS; S33.971; -.
DR   MIM; 132810; -.
DR   InterPro; IPR000073; Abhydrolase.
DR   InterPro; IPR000639; Epox_hydrolase.
DR   InterPro; IPR000379; Est_lip_thioest_actsite.
DR   Pfam; PF00561; abhydrolase; 1.
DR   PRINTS; PR00412; EPOXHYDRLASE.
KW   Hydrolase; Endoplasmic reticulum; Detoxification; Transmembrane;
KW   Liver; Aromatic hydrocarbons catabolism; Microsome; Polymorphism.
FT   TRANSMEM      2     20       SIGNAL-ANCHOR (POTENTIAL).
FT   VARIANT     113    113       Y -> H (FREQUENT ALLELE).
FT                                /FTId=VAR_005295.
FT   VARIANT     139    139       H -> R (FREQUENT ALLELE).
FT                                /FTId=VAR_005296.
FT   VARIANT     396    396       T -> I (EITHER AN INFREQUENT POLYMORPHISM
FT                                OR A SEQUENCING ERROR).
FT                                /FTId=VAR_005297.
FT   MUTAGEN     113    113       Y->H: PARTIAL LOSS OF ENZYME ACTIVITY.
FT   MUTAGEN     139    139       H->R: SMALL INCREASE IN ENZYME ACTIVITY.
FT   CONFLICT    112    112       R -> K (IN REF. 3).
FT   CONFLICT    148    148       H -> N (IN REF. 3 AND 7).
FT   CONFLICT    243    243       V -> L (IN REF. 3).
FT   CONFLICT    348    348       K -> S (IN REF. 3).
FT   CONFLICT    406    406       L -> F (IN REF. 3).
FT   CONFLICT    420    420       L -> V (IN REF. 3).
SQ   SEQUENCE   455 AA;  52949 MW;  88E333838C841390 CRC64;
     MWLEILLTSV LGFAIYWFIS RDKEETLPLE DGWWGPGTRS AAREDDSIRP FKVETSDEEI
     HDLHQRIDKF RFTPPLEDSC FHYGFNSNYL KKVISYWRNE FDWKKQVEIL NRYPHFKTKI
     EGLDIHFIHV KPPQLPAGHT PKPLLMVHGW PGSFYEFYKI IPLLTDPKNH GLSDEHVFEV
     ICPSIPGYGF SEASSKKGFN SVATARIFYK LMLRLGFQEF YIQGGDWGSL ICTNMAQLVP
     SHVKGLHLNM ALVLSNFSTL TLLLGQRFGR FLGLTERDVE LLYPVKEKVF YSLMRESGYM
     HIQCTKPDTV GSALNDSPVG LAAYILEKFS TWTNTEFRYL EDGGLERKFS LDDLLTNVML
     YWTTGTIISS QRFYKENLGQ GWMTQKHERM KVYVPTGFSA FPFELLHTPE KWVRFKYPKL
     ISYSYMVRGG HFAAFEEPEL LAQDIRKFLS VLERQ
//