ID A8JYK8_MOUSE Unreviewed; 488 AA.
AC A8JYK8;
DT 04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT 04-DEC-2007, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE SubName: Full=Epoxide hydrolase 2, cytoplasmic {ECO:0000313|Ensembl:ENSMUSP00000152894.2};
DE SubName: Full=Epoxide hydrolase 2C {ECO:0000313|EMBL:ABU95055.1};
GN Name=Ephx2 {ECO:0000313|Ensembl:ENSMUSP00000152894.2,
GN ECO:0000313|MGI:MGI:99500};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000313|EMBL:ABU95055.1};
RN [1] {ECO:0000313|EMBL:ABU95055.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=C57BL/6 {ECO:0000313|EMBL:ABU95055.1};
RC TISSUE=Ovary {ECO:0000313|EMBL:ABU95055.1};
RX PubMed=17900570; DOI=10.1016/j.febslet.2007.09.016;
RA Shkolnik K., Ben-Dor S., Galiani D., Hourvitz A., Dekel N.;
RT "A novel ovary-specific and ovulation-associated variant of epoxide
RT hydrolase 2.";
RL FEBS Lett. 581:4891-4898(2007).
RN [2] {ECO:0007829|PubMed:17242355}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [3] {ECO:0000313|Ensembl:ENSMUSP00000152894.2, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000152894.2,
RC ECO:0000313|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4] {ECO:0007829|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5] {ECO:0007829|PubMed:23806337}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [6] {ECO:0007829|PubMed:23576753}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
RN [7] {ECO:0000313|Ensembl:ENSMUSP00000152894.2}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000152894.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Epoxide hydrolase
CC family. {ECO:0000256|ARBA:ARBA00038334}.
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DR EMBL; EF597241; ABU95055.1; -; mRNA.
DR RefSeq; NP_001258350.1; NM_001271421.1.
DR ESTHER; mouse-hyes; Epoxide_hydrolase.
DR ProteomicsDB; 338517; -.
DR Antibodypedia; 4070; 486 antibodies from 34 providers.
DR DNASU; 13850; -.
DR Ensembl; ENSMUST00000225309.2; ENSMUSP00000152894.2; ENSMUSG00000022040.9.
DR GeneID; 13850; -.
DR AGR; MGI:99500; -.
DR CTD; 2053; -.
DR MGI; MGI:99500; Ephx2.
DR VEuPathDB; HostDB:ENSMUSG00000022040; -.
DR GeneTree; ENSGT00940000158614; -.
DR OMA; YAMEVLC; -.
DR OrthoDB; 2443908at2759; -.
DR BioGRID-ORCS; 13850; 1 hit in 79 CRISPR screens.
DR ChiTaRS; Ephx2; mouse.
DR Proteomes; UP000000589; Chromosome 14.
DR Bgee; ENSMUSG00000022040; Expressed in small intestine Peyer's patch and 237 other cell types or tissues.
DR GO; GO:0004301; F:epoxide hydrolase activity; IEA:UniProt.
DR CDD; cd02603; HAD_sEH-N_like; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR000639; Epox_hydrolase-like.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR023198; PGP-like_dom2.
DR NCBIfam; TIGR01509; HAD-SF-IA-v3; 1.
DR PANTHER; PTHR43329:SF4; BIFUNCTIONAL EPOXIDE HYDROLASE 2; 1.
DR PANTHER; PTHR43329; EPOXIDE HYDROLASE; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR PRINTS; PR00412; EPOXHYDRLASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 1: Evidence at protein level;
KW Hydrolase {ECO:0000313|EMBL:ABU95055.1};
KW Proteomics identification {ECO:0007829|MaxQB:A8JYK8,
KW ECO:0007829|PeptideAtlas:A8JYK8};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589}.
FT DOMAIN 191..464
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
SQ SEQUENCE 488 AA; 55281 MW; BAA330F8BCEFE5AF CRC64;
MDESYRKSSK ACGANLPENF SISQIFSQAM AARSINRPML QAAIALKKKG FTTCIVTNNW
LDDGDKRDSL AQMMCELSQH FDFLIESCQV GMIKPEPQIY NFLLDTLKAK PNEVVFLDDF
GSNLKPARDM GMVTILVHNT ASALRELEKV TGTQFPEAPL PVPCNPNDVS HGYVTVKPGI
RLHFVEMGSG PALCLCHGFP ESWFSWRYQI PALAQAGFRV LAIDMKGYGD SSSPPEIEEY
AMELLCKEMV TFLDKLGIPQ AVFIGHDWAG VMVWNMALFY PERVRAVASL NTPFMPPDPD
VSPMKVIRSI PVFNYQLYFQ EPGVAEAELE KNMSRTFKSF FRASDETGFI AVHKATEIGG
ILVNTPEDPN LSKITTEEEI EFYIQQFKKT GFRGPLNWYR NTERNWKWSC KGLGRKILVP
ALMVTAEKDI VLRPEMSKNM EKWIPFLKRG HIEDCGHWTQ IEKPTEVNQI LIKWLQTEVQ
NPSVTSKI
//