ID B4E1M2_HUMAN Unreviewed; 502 AA. AC B4E1M2; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 24-JAN-2024, entry version 68. DE SubName: Full=cDNA FLJ54951, highly similar to Epoxide hydrolase 2 {ECO:0000313|EMBL:BAG64834.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:BAG64834.1}; RN [1] {ECO:0000313|EMBL:BAG64834.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Trachea {ECO:0000313|EMBL:BAG64834.1}; RA Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A., RA Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y., RA Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T., RA Sugano S., Nomura N., Isogai T.; RT "NEDO human cDNA sequencing project focused on splicing variants."; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK303904; BAG64834.1; -; mRNA. DR AlphaFoldDB; B4E1M2; -. DR ESTHER; human-EPHX2; Epoxide_hydrolase. DR MEROPS; S33.973; -. DR MaxQB; B4E1M2; -. DR PeptideAtlas; B4E1M2; -. DR ProteomicsDB; 5769; -. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR CDD; cd02603; HAD_sEH-N_like; 1. DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 2. DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR000073; AB_hydrolase_1. DR InterPro; IPR036412; HAD-like_sf. DR InterPro; IPR006439; HAD-SF_hydro_IA. DR InterPro; IPR011945; HAD-SF_ppase_IA/epoxid_hydro_N. DR InterPro; IPR023214; HAD_sf. DR InterPro; IPR023198; PGP-like_dom2. DR NCBIfam; TIGR02247; HAD-1A3-hyp; 1. DR NCBIfam; TIGR01509; HAD-SF-IA-v3; 1. DR PANTHER; PTHR47829:SF2; AB HYDROLASE-1 DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR47829; HYDROLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G12880)-RELATED; 1. DR Pfam; PF00561; Abhydrolase_1; 2. DR Pfam; PF00702; Hydrolase; 1. DR PRINTS; PR00413; HADHALOGNASE. DR SFLD; SFLDG01130; C1.5.1:_Epoxide_Hydrolase_Phos; 1. DR SFLD; SFLDG01129; C1.5:_HAD__Beta-PGM__Phosphata; 1. DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1. DR SUPFAM; SSF56784; HAD-like; 1. PE 2: Evidence at transcript level; KW Acetylation {ECO:0000256|ARBA:ARBA00022990}; KW Hydrolase {ECO:0000313|EMBL:BAG64834.1}. FT DOMAIN 263..319 FT /note="AB hydrolase-1" FT /evidence="ECO:0000259|Pfam:PF00561" FT DOMAIN 320..478 FT /note="AB hydrolase-1" FT /evidence="ECO:0000259|Pfam:PF00561" SQ SEQUENCE 502 AA; 56629 MW; 562297B7EF6F5EB1 CRC64; MTLRAAVFDL DGVLALPAVF GVLGRTEEAL ALPRGLLNDA FQKGGPEGAT TRLMKGEITL SQWIPLMEEN CRKCSETAKV CLPKNFSIKE IFDKAISARK INRPMLQAAL MLRKKAFCSG FTTAILTNTW LDDRAERDGL AQLMCELKMH FDFLIESCQV GMVKPEPQIY KFLLDTLKAS PSEVVFLDDI GANLKPARDL GMVTILVQDT DTALKELEKV TGIQLLNTPA PLPTSCNPSD MSHGYVTVKP RVRLHFVELG SGPAVCLCHG FPESWYSWRY QIPALAQAGY RVLAMDMKGY GESSAPPEIE EYCMEVLCKE SIKANPVFDY QLYFQEPGVA EAELEQNLSR TFKSLFRASD ESVLSMHKVC EAGGLFVNSP EEPSLSRMVT EEEIQFYVQQ FKKSGFRGPL NWYRNMERNW KWACKSLGRK ILIPALMVTA EKDFVLVPQM SQHMEDWIPH LKRGHIEDCG HWTQMDKPTE VNQILIKWLD SDARNPPVVS KM //