ID HYES_HUMAN Reviewed; 555 AA. AC P34913; B2Z3B1; Q16764; Q9HBJ1; Q9HBJ2; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 07-JUN-2005, sequence version 2. DT 31-OCT-2012, entry version 129. DE RecName: Full=Bifunctional epoxide hydrolase 2; DE Includes: DE RecName: Full=Cytosolic epoxide hydrolase 2; DE Short=CEH; DE EC=3.3.2.10; DE AltName: Full=Epoxide hydratase; DE AltName: Full=Soluble epoxide hydrolase; DE Short=SEH; DE Includes: DE RecName: Full=Lipid-phosphate phosphatase; DE EC=3.1.3.76; GN Name=EPHX2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PARTIAL PROTEIN SEQUENCE, RP AND VARIANT GLN-287. RC TISSUE=Liver; RX MEDLINE=93343630; PubMed=8342951; DOI=10.1006/abbi.1993.1411; RA Beetham J.K., Tian T., Hammock B.D.; RT "cDNA cloning and expression of a soluble epoxide hydrolase from human RT liver."; RL Arch. Biochem. Biophys. 305:197-201(1993). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Placenta; RX MEDLINE=96192049; PubMed=8619856; DOI=10.1006/bbrc.1996.0596; RA Sandberg M., Meijer J.; RT "Structural characterization of the human soluble epoxide hydrolase RT gene (EPHX2)."; RL Biochem. Biophys. Res. Commun. 221:333-339(1996). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS GLN-287 AND ARG-403 INS. RC TISSUE=Liver; RX MEDLINE=20435850; PubMed=10862610; DOI=10.1074/jbc.M001153200; RA Sandberg M., Hassett C., Adman E.T., Meijer J., Omiecinski C.J.; RT "Identification and functional characterization of human soluble RT epoxide hydrolase genetic polymorphisms."; RL J. Biol. Chem. 275:28873-28881(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor RT vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ALA-21; GLN-52; RP ARG-55; CYS-103; TYR-154; LEU-225; GLN-287; VAL-369 AND GLY-470. RG NIEHS SNPs program; RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=B-cell, and Lung; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP CATALYTIC ACTIVITY, AND CHARACTERIZATION OF VARIANTS ARG-55; CYS-103; RP TYR-154; GLN-287 AND GLY-470. RX PubMed=12869654; DOI=10.1124/mol.64.2.482; RA Przybyla-Zawislak B.D., Srivastava P.K., Vazquez-Matias J., RA Mohrenweiser H.W., Maxwell J.E., Hammock B.D., Bradbury J.A., RA Enayetallah A.E., Zeldin D.C., Grant D.F.; RT "Polymorphisms in human soluble epoxide hydrolase."; RL Mol. Pharmacol. 64:482-490(2003). RN [9] RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION AS RP PHOSPHATASE, AND MUTAGENESIS OF ASP-9. RX PubMed=12574508; DOI=10.1073/pnas.0437829100; RA Cronin A., Mowbray S., Durk H., Homburg S., Fleming I., RA Fisslthaler B., Oesch F., Arand M.; RT "The N-terminal domain of mammalian soluble epoxide hydrolase is a RT phosphatase."; RL Proc. Natl. Acad. Sci. U.S.A. 100:1552-1557(2003). RN [10] RP CATALYTIC ACTIVITY, FUNCTION AS LIPID PHOSPHATASE, COFACTOR, AND RP BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=12574510; DOI=10.1073/pnas.0437724100; RA Newman J.W., Morisseau C., Harris T.R., Hammock B.D.; RT "The soluble epoxide hydrolase encoded by EPXH2 is a bifunctional RT enzyme with novel lipid phosphate phosphatase activity."; RL Proc. Natl. Acad. Sci. U.S.A. 100:1558-1563(2003). RN [11] RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND RP CHARACTERIZATION OF VARIANTS ARG-55; CYS-103; TYR-154; GLN-287 AND RP GLY-470. RX PubMed=15196990; DOI=10.1016/j.abb.2004.05.003; RA Srivastava P.K., Sharma V.K., Kalonia D.S., Grant D.F.; RT "Polymorphisms in human soluble epoxide hydrolase: effects on enzyme RT activity, enzyme stability, and quaternary structure."; RL Arch. Biochem. Biophys. 427:164-169(2004). RN [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-43, AND MASS SPECTROMETRY. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [14] RP PROBABLE LIPID MODIFICATION AT CYS-522, AND MUTAGENESIS OF CYS-522. RX PubMed=21164107; DOI=10.1161/CIRCRESAHA.110.235879; RA Charles R.L., Burgoyne J.R., Mayr M., Weldon S.M., Hubner N., Dong H., RA Morisseau C., Hammock B.D., Landar A., Eaton P.; RT "Redox regulation of soluble epoxide hydrolase by 15-deoxy-delta- RT prostaglandin J2 controls coronary hypoxic vasodilation."; RL Circ. Res. 108:324-334(2011). RN [15] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH PHOSPHATE; RP MAGNESIUM AND EPOXIDE HYDROLASE INHIBITOR. RX PubMed=15096040; DOI=10.1021/bi036189j; RA Gomez G.A., Morisseau C., Hammock B.D., Christianson D.W.; RT "Structure of human epoxide hydrolase reveals mechanistic inferences RT on bifunctional catalysis in epoxide and phosphate ester hydrolysis."; RL Biochemistry 43:4716-4723(2004). RN [16] RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEXES WITH DIALKYLUREA RP INHIBITORS AND MAGNESIUM. RX PubMed=16322563; DOI=10.1110/ps.051720206; RA Gomez G.A., Morisseau C., Hammock B.D., Christianson D.W.; RT "Human soluble epoxide hydrolase: structural basis of inhibition by 4- RT (3-cyclohexylureido)-carboxylic acids."; RL Protein Sci. 15:58-64(2006). RN [17] RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEXES WITH ARYLAMIDE RP INHIBITORS. RX PubMed=19746975; DOI=10.1021/jm9005302; RA Eldrup A.B., Soleymanzadeh F., Taylor S.J., Muegge I., Farrow N.A., RA Joseph D., McKellop K., Man C.C., Kukulka A., De Lombaert S.; RT "Structure-based optimization of arylamides as inhibitors of soluble RT epoxide hydrolase."; RL J. Med. Chem. 52:5880-5895(2009). RN [18] RP X-RAY CRYSTALLOGRAPHY (2.79 ANGSTROMS) IN COMPLEX WITH SYNTHETIC RP INHIBITOR. RX PubMed=19969453; DOI=10.1016/j.bmcl.2009.11.091; RA Eldrup A.B., Soleymanzadeh F., Farrow N.A., Kukulka A., RA De Lombaert S.; RT "Optimization of piperidyl-ureas as inhibitors of soluble epoxide RT hydrolase."; RL Bioorg. Med. Chem. Lett. 20:571-575(2010). RN [19] RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) IN COMPLEX WITH SYNTHETIC RP INHIBITOR. RX PubMed=20934334; DOI=10.1016/j.bmcl.2010.09.095; RA Lo H.Y., Man C.C., Fleck R.W., Farrow N.A., Ingraham R.H., Kukulka A., RA Proudfoot J.R., Betageri R., Kirrane T., Patel U., Sharma R., RA Hoermann M.A., Kabcenell A., Lombaert S.D.; RT "Substituted pyrazoles as novel sEH antagonist: investigation of key RT binding interactions within the catalytic domain."; RL Bioorg. Med. Chem. Lett. 20:6379-6383(2010). CC -!- FUNCTION: Bifunctional enzyme. The C-terminal domain has epoxide CC hydrolase activity and acts on epoxides (alkene oxides, oxiranes) CC and arene oxides. Plays a role in xenobiotic metabolism by CC degrading potentially toxic epoxides. Also determines steady-state CC levels of physiological mediators. The N-terminal domain has lipid CC phosphatase activity, with the highest activity towards threo- CC 9,10-phosphonooxy-hydroxy-octadecanoic acid, followed by erythro- CC 9,10-phosphonooxy-hydroxy-octadecanoic acid, 12-phosphonooxy- CC octadec-9Z-enoic acid, 12-phosphonooxy-octadec-9E-enoic acid, and CC p-nitrophenyl phospate. CC -!- CATALYTIC ACTIVITY: An epoxide + H(2)O = a glycol. CC -!- CATALYTIC ACTIVITY: (9S,10S)-10-hydroxy-9- CC (phosphonooxy)octadecanoate + H(2)O = (9S,10S)-9,10- CC dihydroxyoctadecanoate + phosphate. CC -!- COFACTOR: Magnesium. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=21 uM for threo-9,10-phosphonooxy-hydroxy-octadecanoic acid; CC KM=1.1 mM for p-nitrophenyl phosphate; CC Vmax=338 nmol/min/mg enzyme with threo-9,10-phosphonooxy- CC hydroxy-octadecanoic acid; CC Vmax=5.8 nmol/min/mg enzyme with p-nitrophenyl phosphate; CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. Peroxisome. CC -!- INDUCTION: By compounds that cause peroxisome proliferation such CC as clofibrate, tiadenol and fenofibrate. CC -!- DOMAIN: The N-terminal domain has phosphatase activity. The C- CC terminal domain has epoxide hydrolase activity. CC -!- PTM: The N-terminus is blocked. CC -!- PTM: The covalent modification of cysteine by 15-deoxy-Delta12,14- CC prostaglandin-J2 is autocatalytic and reversible. It may occur as CC an alternative to other cysteine modifications, such as S- CC nitrosylation and S-palmitoylation (Probable). CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Epoxide CC hydrolase family. CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/ephx2/"; 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; L05779; AAA02756.1; -; mRNA. DR EMBL; X97024; CAA65751.1; -; Genomic_DNA. DR EMBL; X97025; CAA65751.1; JOINED; Genomic_DNA. DR EMBL; X97026; CAA65751.1; JOINED; Genomic_DNA. DR EMBL; X97027; CAA65751.1; JOINED; Genomic_DNA. DR EMBL; X97028; CAA65751.1; JOINED; Genomic_DNA. DR EMBL; X97029; CAA65751.1; JOINED; Genomic_DNA. DR EMBL; X97030; CAA65751.1; JOINED; Genomic_DNA. DR EMBL; X97031; CAA65751.1; JOINED; Genomic_DNA. DR EMBL; X97032; CAA65751.1; JOINED; Genomic_DNA. DR EMBL; X97033; CAA65751.1; JOINED; Genomic_DNA. DR EMBL; X97034; CAA65751.1; JOINED; Genomic_DNA. DR EMBL; X97035; CAA65751.1; JOINED; Genomic_DNA. DR EMBL; X97036; CAA65751.1; JOINED; Genomic_DNA. DR EMBL; X97037; CAA65751.1; JOINED; Genomic_DNA. DR EMBL; X97038; CAA65751.1; JOINED; Genomic_DNA. DR EMBL; AF233334; AAG14966.1; -; mRNA. DR EMBL; AF233335; AAG14967.1; -; mRNA. DR EMBL; AF233336; AAG14968.1; -; mRNA. DR EMBL; BT006885; AAP35531.1; -; mRNA. DR EMBL; EU584434; ACD11487.1; -; Genomic_DNA. DR EMBL; CH471080; EAW63548.1; -; Genomic_DNA. DR EMBL; BC007708; AAH07708.1; -; mRNA. DR EMBL; BC011628; AAH11628.1; -; mRNA. DR EMBL; BC013874; AAH13874.1; -; mRNA. DR IPI; IPI00104341; -. DR PIR; JC4711; JC4711. DR RefSeq; NP_001970.2; NM_001979.5. DR UniGene; Hs.212088; -. DR PDB; 1S8O; X-ray; 2.60 A; A=1-555. DR PDB; 1VJ5; X-ray; 2.35 A; A=1-555. DR PDB; 1ZD2; X-ray; 3.00 A; P=1-555. DR PDB; 1ZD3; X-ray; 2.30 A; A=1-555. DR PDB; 1ZD4; X-ray; 2.70 A; A=1-555. DR PDB; 1ZD5; X-ray; 2.60 A; A=1-555. DR PDB; 3ANS; X-ray; 1.98 A; A/B=230-555. DR PDB; 3ANT; X-ray; 2.40 A; A/B=230-555. DR PDB; 3I1Y; X-ray; 2.47 A; A=1-555. DR PDB; 3I28; X-ray; 1.95 A; A=1-555. DR PDB; 3KOO; X-ray; 2.79 A; A=1-555. DR PDB; 3OTQ; X-ray; 3.00 A; A=1-555. DR PDB; 3PDC; X-ray; 2.60 A; A/B=226-548. DR PDBsum; 1S8O; -. DR PDBsum; 1VJ5; -. DR PDBsum; 1ZD2; -. DR PDBsum; 1ZD3; -. DR PDBsum; 1ZD4; -. DR PDBsum; 1ZD5; -. DR PDBsum; 3ANS; -. DR PDBsum; 3ANT; -. DR PDBsum; 3I1Y; -. DR PDBsum; 3I28; -. DR PDBsum; 3KOO; -. DR PDBsum; 3OTQ; -. DR PDBsum; 3PDC; -. DR ProteinModelPortal; P34913; -. DR SMR; P34913; 2-548. DR IntAct; P34913; 3. DR MINT; MINT-1385532; -. DR STRING; P34913; -. DR MEROPS; S33.973; -. DR PhosphoSite; P34913; -. DR DMDM; 67476665; -. DR PeptideAtlas; P34913; -. DR PRIDE; P34913; -. DR DNASU; 2053; -. DR Ensembl; ENST00000521400; ENSP00000430269; ENSG00000120915. DR GeneID; 2053; -. DR KEGG; hsa:2053; -. DR UCSC; uc003xfu.3; human. DR CTD; 2053; -. DR GeneCards; GC08P027348; -. DR HGNC; HGNC:3402; EPHX2. DR HPA; CAB009808; -. DR HPA; HPA023094; -. DR HPA; HPA023660; -. DR HPA; HPA023779; -. DR MIM; 132811; gene. DR neXtProt; NX_P34913; -. DR PharmGKB; PA27830; -. DR eggNOG; COG0596; -. DR HOGENOM; HOG000028073; -. DR HOVERGEN; HBG006095; -. DR InParanoid; P34913; -. DR KO; K08726; -. DR OMA; HIEDCGH; -. DR OrthoDB; EOG45QHCT; -. DR PhylomeDB; P34913; -. DR DrugBank; DB00675; Tamoxifen. DR EvolutionaryTrace; P34913; -. DR GenomeRNAi; 2053; -. DR NextBio; 8347; -. DR ArrayExpress; P34913; -. DR Bgee; P34913; -. DR CleanEx; HS_EPHX2; -. DR Genevestigator; P34913; -. DR GermOnline; ENSG00000120915; Homo sapiens. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0005925; C:focal adhesion; IDA:HPA. DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB. DR GO; GO:0033885; F:10-hydroxy-9-(phosphonooxy)octadecanoate phosphatase activity; IEA:EC. DR GO; GO:0003869; F:4-nitrophenylphosphatase activity; IDA:UniProtKB. DR GO; GO:0004301; F:epoxide hydrolase activity; IDA:UniProtKB. DR GO; GO:0042577; F:lipid phosphatase activity; IDA:UniProtKB. DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB. DR GO; GO:0015643; F:toxin binding; IDA:UniProtKB. DR GO; GO:0006874; P:cellular calcium ion homeostasis; NAS:UniProtKB. DR GO; GO:0042632; P:cholesterol homeostasis; IDA:UniProtKB. DR GO; GO:0017144; P:drug metabolic process; NAS:UniProtKB. DR GO; GO:0006954; P:inflammatory response; NAS:UniProtKB. DR GO; GO:0046839; P:phospholipid dephosphorylation; IDA:UniProtKB. DR GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB. DR GO; GO:0045909; P:positive regulation of vasodilation; NAS:UniProtKB. DR GO; GO:0072593; P:reactive oxygen species metabolic process; NAS:UniProtKB. DR GO; GO:0008217; P:regulation of blood pressure; NAS:UniProtKB. DR GO; GO:0090181; P:regulation of cholesterol metabolic process; IMP:UniProtKB. DR GO; GO:0009636; P:response to toxin; NAS:UniProtKB. DR GO; GO:0046272; P:stilbene catabolic process; IDA:UniProtKB. DR GO; GO:0006805; P:xenobiotic metabolic process; NAS:UniProtKB. DR Gene3D; G3DSA:3.40.50.1000; HAD-like_dom; 1. DR InterPro; IPR000073; AB_hydrolase_1. DR InterPro; IPR000639; Epox_hydrolase-like. DR InterPro; IPR023214; HAD-like_dom. DR InterPro; IPR006402; HAD-SF_hydro_IA_v3. DR InterPro; IPR011945; HAD-SF_ppase_IA/epoxid_hydro_N. DR Pfam; PF00561; Abhydrolase_1; 1. DR PRINTS; PR00111; ABHYDROLASE. DR PRINTS; PR00412; EPOXHYDRLASE. DR SUPFAM; SSF56784; HAD-like_dom; 1. DR TIGRFAMs; TIGR02247; HAD-1A3-hyp; 1. DR TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Aromatic hydrocarbons catabolism; KW Complete proteome; Cytoplasm; Detoxification; KW Direct protein sequencing; Hydrolase; Lipid metabolism; Lipoprotein; KW Magnesium; Metal-binding; Multifunctional enzyme; Peroxisome; KW Polymorphism; Reference proteome. FT CHAIN 1 555 Bifunctional epoxide hydrolase 2. FT /FTId=PRO_0000084111. FT REGION 1 224 Phosphatase. FT REGION 123 124 Phosphate binding. FT REGION 235 555 Epoxide hydrolase. FT MOTIF 553 555 Microbody targeting signal (Potential). FT ACT_SITE 335 335 Nucleophile. FT ACT_SITE 466 466 Proton donor. FT ACT_SITE 524 524 Proton acceptor. FT METAL 9 9 Magnesium. FT METAL 11 11 Magnesium. FT METAL 185 185 Magnesium. FT BINDING 383 383 Substrate. FT MOD_RES 43 43 N6-acetyllysine. FT LIPID 522 522 S-(15-deoxy-Delta12,14-prostaglandin J2- FT 9-yl)cysteine (Probable). FT VARIANT 21 21 G -> A. FT /FTId=VAR_055392. FT VARIANT 52 52 R -> Q. FT /FTId=VAR_055393. FT VARIANT 55 55 K -> R (decreased phosphatase activity; FT no effect on epoxyde hydrolase activity; FT dbSNP:rs41507953). FT /FTId=VAR_051059. FT VARIANT 103 103 R -> C (decreased phosphatase activity; FT no effect on epoxyde hydrolase activity; FT dbSNP:rs17057255). FT /FTId=VAR_033991. FT VARIANT 154 154 C -> Y (decreased phosphatase activity; FT no effect on epoxyde hydrolase activity; FT dbSNP:rs57699806). FT /FTId=VAR_055394. FT VARIANT 225 225 P -> L. FT /FTId=VAR_055395. FT VARIANT 287 287 R -> Q (no effect on phosphatase FT activity; decreased epoxyde hydrolase FT activity; dbSNP:rs751141). FT /FTId=VAR_014852. FT VARIANT 369 369 M -> V. FT /FTId=VAR_055396. FT VARIANT 403 403 R -> RR. FT /FTId=VAR_022613. FT VARIANT 470 470 E -> G (no effect on phosphatase activity FT and epoxyde hydrolase activity). FT /FTId=VAR_055397. FT MUTAGEN 9 9 D->A: Loss of phosphatase activity. FT MUTAGEN 522 522 C->S: Loss of S-(15-deoxy-Delta12,14- FT prostaglandin J2-9-yl)cysteine-induced FT inhibition of epoxide hydrolase activity. FT CONFLICT 5 5 A -> G (in Ref. 1; AAA02756). FT CONFLICT 257 258 SG -> W (in Ref. 1; AAA02756). FT STRAND 5 8 FT TURN 12 14 FT STRAND 15 17 FT HELIX 20 29 FT HELIX 36 42 FT HELIX 45 47 FT HELIX 49 54 FT STRAND 57 59 FT HELIX 60 77 FT HELIX 88 98 FT HELIX 103 114 FT STRAND 118 123 FT TURN 131 133 FT HELIX 134 144 FT STRAND 147 152 FT HELIX 153 156 FT HELIX 163 173 FT HELIX 177 179 FT STRAND 180 185 FT HELIX 187 196 FT STRAND 199 202 FT HELIX 206 217 FT HELIX 234 236 FT STRAND 237 245 FT STRAND 248 255 FT STRAND 257 264 FT HELIX 271 274 FT HELIX 277 283 FT STRAND 287 291 FT HELIX 305 308 FT HELIX 310 324 FT STRAND 329 334 FT HELIX 336 347 FT HELIX 349 351 FT STRAND 352 359 FT STRAND 367 369 FT HELIX 371 376 FT HELIX 379 381 FT HELIX 382 388 FT HELIX 392 399 FT HELIX 401 408 FT HELIX 412 414 FT STRAND 419 421 FT HELIX 422 425 FT STRAND 427 429 FT STRAND 440 442 FT HELIX 444 454 FT TURN 455 459 FT HELIX 460 464 FT HELIX 465 467 FT HELIX 469 477 FT TURN 478 481 FT STRAND 488 493 FT STRAND 497 499 FT HELIX 501 504 FT HELIX 507 509 FT STRAND 515 519 FT HELIX 526 529 FT HELIX 531 545 SQ SEQUENCE 555 AA; 62616 MW; 1B5ACE7F80F9A26C CRC64; MTLRAAVFDL DGVLALPAVF GVLGRTEEAL ALPRGLLNDA FQKGGPEGAT TRLMKGEITL SQWIPLMEEN CRKCSETAKV CLPKNFSIKE IFDKAISARK INRPMLQAAL MLRKKGFTTA ILTNTWLDDR AERDGLAQLM CELKMHFDFL IESCQVGMVK PEPQIYKFLL DTLKASPSEV VFLDDIGANL KPARDLGMVT ILVQDTDTAL KELEKVTGIQ LLNTPAPLPT SCNPSDMSHG YVTVKPRVRL HFVELGSGPA VCLCHGFPES WYSWRYQIPA LAQAGYRVLA MDMKGYGESS APPEIEEYCM EVLCKEMVTF LDKLGLSQAV FIGHDWGGML VWYMALFYPE RVRAVASLNT PFIPANPNMS PLESIKANPV FDYQLYFQEP GVAEAELEQN LSRTFKSLFR ASDESVLSMH KVCEAGGLFV NSPEEPSLSR MVTEEEIQFY VQQFKKSGFR GPLNWYRNME RNWKWACKSL GRKILIPALM VTAEKDFVLV PQMSQHMEDW IPHLKRGHIE DCGHWTQMDK PTEVNQILIK WLDSDARNPP VVSKM //