GenomeNet

Database: UniProt
Entry: P09960
LinkDB: P09960
Original site: P09960 
ID   LKHA4_HUMAN             Reviewed;         611 AA.
AC   P09960; B4DNQ9; F8VV40; Q6IAT6; Q9UCT7;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   17-JUN-2020, entry version 234.
DE   RecName: Full=Leukotriene A-4 hydrolase;
DE            Short=LTA-4 hydrolase;
DE            EC=3.3.2.6;
DE   AltName: Full=Leukotriene A(4) hydrolase;
GN   Name=LTA4H; Synonyms=LTA4;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=3654641;
RA   Minami M., Ohno S., Kawasaki H., Raedmark O., Samuelsson B., Joernvall H.,
RA   Shimizu T., Seyama Y., Suzuki K.;
RT   "Molecular cloning of a cDNA coding for human leukotriene A4 hydrolase.
RT   Complete primary structure of an enzyme involved in eicosanoid synthesis.";
RL   J. Biol. Chem. 262:13873-13876(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=2821541; DOI=10.1073/pnas.84.19.6677;
RA   Funk C.D., Raadmark O., Fu J.Y., Matsumoto T., Joernvall H., Shimizu T.,
RA   Samuelsson B.;
RT   "Molecular cloning and amino acid sequence of leukotriene A4 hydrolase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 84:6677-6681(1987).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7628486; DOI=10.1111/j.1432-1033.1995.tb20671.x;
RA   Mancini J.A., Evans J.F.;
RT   "Cloning and characterization of the human leukotriene A4 hydrolase gene.";
RL   Eur. J. Biochem. 231:65-71(1995).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Lung;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   TISSUE=Esophageal carcinoma;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16541075; DOI=10.1038/nature04569;
RA   Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA   Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA   Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA   Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA   Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA   Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA   Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA   Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA   Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA   Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA   Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA   Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA   Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA   Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA   Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA   Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA   Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA   David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA   D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA   Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA   Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA   Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA   LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA   Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA   Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA   Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA   Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA   Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA   Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA   Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA   Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA   Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA   Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA   Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA   Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA   Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA   Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA   Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA   Gibbs R.A.;
RT   "The finished DNA sequence of human chromosome 12.";
RL   Nature 440:346-351(2006).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Eye;
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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [10]
RP   PROTEIN SEQUENCE OF 2-22, FUNCTION, AND CATALYTIC ACTIVITY.
RC   TISSUE=B-cell;
RX   PubMed=1897988; DOI=10.1016/0003-9861(91)90402-5;
RA   Odlander B., Claesson H.E., Bergman T., Radmark O., Joernvall H.,
RA   Haeggstrom J.Z.;
RT   "Leukotriene A4 hydrolase in the human B-lymphocytic cell line Raji:
RT   indications of catalytically divergent forms of the enzyme.";
RL   Arch. Biochem. Biophys. 287:167-174(1991).
RN   [11]
RP   PROTEIN SEQUENCE OF 2-16.
RX   PubMed=6490615;
RA   Radmark O., Shimizu T., Joernvall H., Samuelsson B.;
RT   "Leukotriene A4 hydrolase in human leukocytes. Purification and
RT   properties.";
RL   J. Biol. Chem. 259:12339-12345(1984).
RN   [12]
RP   PROTEIN SEQUENCE OF 366-386, ACTIVITY REGULATION, COVALENT MODIFICATION AT
RP   TYR-379, AND CATALYTIC ACTIVITY.
RX   PubMed=7667299; DOI=10.1073/pnas.92.18.8383;
RA   Mueller M.J., Wetterholm A., Blomster M., Jornvall H., Samuelsson B.,
RA   Haeggstrom J.Z.;
RT   "Leukotriene A4 hydrolase: mapping of a henicosapeptide involved in
RT   mechanism-based inactivation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:8383-8387(1995).
RN   [13]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 511-611, AND ALTERNATIVE SPLICING
RP   (ISOFORMS 1 AND 2).
RX   PubMed=8615763; DOI=10.1042/bj3140733;
RA   Jendraschak E., Kaminski W.E., Kiefl R., von Schacky C.;
RT   "The human leukotriene A4 hydrolase gene is expressed in two alternatively
RT   spliced mRNA forms.";
RL   Biochem. J. 314:733-737(1996).
RN   [14]
RP   ZINC-BINDING, FUNCTION AS A PEPTIDASE, AND SIMILARITY TO ZINC PROTEASES.
RX   PubMed=1975494; DOI=10.1016/0006-291x(90)91379-7;
RA   Toh H., Minami M., Shimizu T.;
RT   "Molecular evolution and zinc ion binding motif of leukotriene A4
RT   hydrolase.";
RL   Biochem. Biophys. Res. Commun. 171:216-221(1990).
RN   [15]
RP   ZINC-BINDING, AND FUNCTION AS A PEPTIDASE.
RX   PubMed=2244921; DOI=10.1016/0006-291x(90)91540-9;
RA   Haeggstroem J.Z., Wetterholm A., Shapiro R., Vallee B.L., Samuelsson B.;
RT   "Leukotriene A4 hydrolase: a zinc metalloenzyme.";
RL   Biochem. Biophys. Res. Commun. 172:965-970(1990).
RN   [16]
RP   MUTAGENESIS OF ZINC LIGANDS.
RX   PubMed=1881903; DOI=10.1073/pnas.88.17.7620;
RA   Medina J.F., Wetterholm A., Raadmark O., Shapiro R., Haeggstroem J.Z.,
RA   Vallee B.L., Samuelsson B.;
RT   "Leukotriene A4 hydrolase: determination of the three zinc-binding ligands
RT   by site-directed mutagenesis and zinc analysis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:7620-7624(1991).
RN   [17]
RP   MUTAGENESIS OF GLU-297.
RX   PubMed=1516710; DOI=10.1016/0014-5793(92)80806-r;
RA   Minami M., Bito H., Ohishi N., Tsuge H., Miyano M., Mori M., Wada H.,
RA   Mutoh H., Shimada S., Izumi T., Abe K., Shimuzu T.;
RT   "Leukotriene A4 hydrolase, a bifunctional enzyme. Distinction of
RT   leukotriene A4 hydrolase and aminopeptidase activities by site-directed
RT   mutagenesis at Glu-297.";
RL   FEBS Lett. 309:353-357(1992).
RN   [18]
RP   MUTAGENESIS OF GLU-297.
RX   PubMed=1357660; DOI=10.1073/pnas.89.19.9141;
RA   Wetterholm A., Medina J.F., Raadmark O., Shapiro R., Haeggstroem J.Z.,
RA   Vallee B.L., Samuelsson B.;
RT   "Leukotriene A4 hydrolase: abrogation of the peptidase activity by mutation
RT   of glutamic acid-296.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:9141-9145(1992).
RN   [19]
RP   PHOSPHORYLATION AT SER-416.
RX   PubMed=9395533; DOI=10.1074/jbc.272.50.31865;
RA   Rybina I.V., Liu H., Gor Y., Feinmark S.J.;
RT   "Regulation of leukotriene A4 hydrolase activity in endothelial cells by
RT   phosphorylation.";
RL   J. Biol. Chem. 272:31865-31871(1997).
RN   [20]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-73; LYS-337; LYS-414 AND LYS-573,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
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   [21]
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., Buerckstuemmer T.,
RA   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   [22]
RP   CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [23]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [24]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [25]
RP   X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH ZINC AND BESTATIN.
RX   PubMed=11175901; DOI=10.1038/84117;
RA   Thunnissen M.M.G.M., Nordlund P., Haeggstroem J.Z.;
RT   "Crystal structure of human leukotriene A(4) hydrolase, a bifunctional
RT   enzyme in inflammation.";
RL   Nat. Struct. Biol. 8:131-135(2001).
RN   [26]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH CAPTOPRIL AND ZINC
RP   IONS, FUNCTION, COFACTOR, CATALYTIC ACTIVITY, AND ACTIVE SITE.
RX   PubMed=12207002; DOI=10.1096/fj.01-1017fje;
RA   Thunnissen M.M., Andersson B., Samuelsson B., Wong C.H., Haeggstrom J.Z.;
RT   "Crystal structures of leukotriene A4 hydrolase in complex with captopril
RT   and two competitive tight-binding inhibitors.";
RL   FASEB J. 16:1648-1650(2002).
RN   [27]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2-611 IN COMPLEX WITH ZINC, ACTIVE
RP   SITE, AND MUTAGENESIS OF GLN-137; GLY-270; MET-271; GLU-272 AND ASN-273.
RX   PubMed=11675384; DOI=10.1074/jbc.m106577200;
RA   Rudberg P.C., Tholander F., Thunnissen M.M.G.M., Haeggstroem J.Z.;
RT   "Leukotriene A4 hydrolase/aminopeptidase. Glutamate 271 is a catalytic
RT   residue with specific roles in two distinct enzyme mechanisms.";
RL   J. Biol. Chem. 277:1398-1404(2002).
RN   [28]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANT ASN-376 IN COMPLEX WITH
RP   BESTATIN AND ZINC IONS, FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF
RP   GLN-135; HIS-140; ASP-372; ASP-374; ASP-376 AND GLU-385.
RX   PubMed=11917124; DOI=10.1073/pnas.072090099;
RA   Rudberg P.C., Tholander F., Thunnissen M.M., Samuelsson B.,
RA   Haeggstrom J.Z.;
RT   "Leukotriene A4 hydrolase: selective abrogation of leukotriene B4 formation
RT   by mutation of aspartic acid 375.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:4215-4220(2002).
RN   [29]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF MUTANT ALA-564 IN COMPLEX WITH
RP   ZINC IONS, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, AND MUTAGENESIS OF
RP   ARG-564 AND LYS-566.
RX   PubMed=15078870; DOI=10.1074/jbc.m401031200;
RA   Rudberg P.C., Tholander F., Andberg M., Thunnissen M.M., Haeggstrom J.Z.;
RT   "Leukotriene A4 hydrolase: identification of a common carboxylate
RT   recognition site for the epoxide hydrolase and aminopeptidase substrates.";
RL   J. Biol. Chem. 279:27376-27382(2004).
RN   [30]
RP   X-RAY CRYSTALLOGRAPHY (1.47 ANGSTROMS) OF MUTANT GLN-297 IN COMPLEXES WITH
RP   SUBSTRATE TRIPEPTIDES AND ZINC IONS, CATALYTIC ACTIVITY, FUNCTION,
RP   COFACTOR, AND MUTAGENESIS OF GLU-297 AND ASP-376.
RX   PubMed=18804029; DOI=10.1016/j.chembiol.2008.07.018;
RA   Tholander F., Muroya A., Roques B.P., Fournie-Zaluski M.C.,
RA   Thunnissen M.M., Haeggstrom J.Z.;
RT   "Structure-based dissection of the active site chemistry of leukotriene A4
RT   hydrolase: implications for M1 aminopeptidases and inhibitor design.";
RL   Chem. Biol. 15:920-929(2008).
RN   [31]
RP   X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) IN COMPLEXES WITH INHIBITORS AND
RP   ZINC IONS.
RX   PubMed=19618939; DOI=10.1021/jm900259h;
RA   Davies D.R., Mamat B., Magnusson O.T., Christensen J., Haraldsson M.H.,
RA   Mishra R., Pease B., Hansen E., Singh J., Zembower D., Kim H.,
RA   Kiselyov A.S., Burgin A.B., Gurney M.E., Stewart L.J.;
RT   "Discovery of leukotriene A4 hydrolase inhibitors using metabolomics biased
RT   fragment crystallography.";
RL   J. Med. Chem. 52:4694-4715(2009).
CC   -!- FUNCTION: Epoxide hydrolase that catalyzes the final step in the
CC       biosynthesis of the proinflammatory mediator leukotriene B4. Has also
CC       aminopeptidase activity. {ECO:0000269|PubMed:11917124,
CC       ECO:0000269|PubMed:12207002, ECO:0000269|PubMed:15078870,
CC       ECO:0000269|PubMed:18804029, ECO:0000269|PubMed:1897988,
CC       ECO:0000269|PubMed:1975494, ECO:0000269|PubMed:2244921}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + leukotriene A4 = leukotriene B4; Xref=Rhea:RHEA:22324,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:57461, ChEBI:CHEBI:57463; EC=3.3.2.6;
CC         Evidence={ECO:0000269|PubMed:11917124, ECO:0000269|PubMed:12207002,
CC         ECO:0000269|PubMed:15078870, ECO:0000269|PubMed:18804029,
CC         ECO:0000269|PubMed:1897988, ECO:0000269|PubMed:7667299};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000269|PubMed:12207002, ECO:0000269|PubMed:15078870,
CC         ECO:0000269|PubMed:18804029};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:12207002,
CC       ECO:0000269|PubMed:15078870, ECO:0000269|PubMed:18804029};
CC   -!- ACTIVITY REGULATION: Inhibited by bestatin. Subject to suicide
CC       inhibition by leukotriene A4, due to the formation of a covalent adduct
CC       at Tyr-379. {ECO:0000269|PubMed:7667299}.
CC   -!- PATHWAY: Lipid metabolism; leukotriene B4 biosynthesis.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11917124,
CC       ECO:0000269|PubMed:12207002, ECO:0000269|PubMed:15078870}.
CC   -!- INTERACTION:
CC       P09960; Q9BSI4: TINF2; NbExp=2; IntAct=EBI-721089, EBI-717399;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1; Synonyms=L-LTA4;
CC         IsoId=P09960-1; Sequence=Displayed;
CC       Name=2; Synonyms=S-LTA4;
CC         IsoId=P09960-2; Sequence=VSP_041108, VSP_041109;
CC       Name=3;
CC         IsoId=P09960-3; Sequence=VSP_041107, VSP_041108, VSP_041109;
CC       Name=4;
CC         IsoId=P09960-4; Sequence=VSP_041107;
CC   -!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed in monocytes,
CC       lymphocytes, neutrophils, reticulocytes, platelets and fibroblasts.
CC   -!- PTM: Phosphorylation at Ser-416 inhibits enzymatic activity.
CC       {ECO:0000269|PubMed:9395533}.
CC   -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
DR   EMBL; J03459; AAA36176.1; -; mRNA.
DR   EMBL; J02959; AAA36177.1; -; mRNA.
DR   EMBL; U27293; AAA89077.1; -; Genomic_DNA.
DR   EMBL; U27275; AAA89077.1; JOINED; Genomic_DNA.
DR   EMBL; U27276; AAA89077.1; JOINED; Genomic_DNA.
DR   EMBL; U27277; AAA89077.1; JOINED; Genomic_DNA.
DR   EMBL; U27278; AAA89077.1; JOINED; Genomic_DNA.
DR   EMBL; U27279; AAA89077.1; JOINED; Genomic_DNA.
DR   EMBL; U27280; AAA89077.1; JOINED; Genomic_DNA.
DR   EMBL; U27281; AAA89077.1; JOINED; Genomic_DNA.
DR   EMBL; U27282; AAA89077.1; JOINED; Genomic_DNA.
DR   EMBL; U27283; AAA89077.1; JOINED; Genomic_DNA.
DR   EMBL; U27284; AAA89077.1; JOINED; Genomic_DNA.
DR   EMBL; U27285; AAA89077.1; JOINED; Genomic_DNA.
DR   EMBL; U27286; AAA89077.1; JOINED; Genomic_DNA.
DR   EMBL; U27287; AAA89077.1; JOINED; Genomic_DNA.
DR   EMBL; U27288; AAA89077.1; JOINED; Genomic_DNA.
DR   EMBL; U27289; AAA89077.1; JOINED; Genomic_DNA.
DR   EMBL; U27290; AAA89077.1; JOINED; Genomic_DNA.
DR   EMBL; U27291; AAA89077.1; JOINED; Genomic_DNA.
DR   EMBL; U27292; AAA89077.1; JOINED; Genomic_DNA.
DR   EMBL; AK298017; BAG60321.1; -; mRNA.
DR   EMBL; CR457068; CAG33349.1; -; mRNA.
DR   EMBL; BX647158; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AC007298; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471054; EAW97559.1; -; Genomic_DNA.
DR   EMBL; BC032528; AAH32528.1; -; mRNA.
DR   EMBL; U43410; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; U43411; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS58266.1; -. [P09960-3]
DR   CCDS; CCDS58267.1; -. [P09960-4]
DR   CCDS; CCDS9059.1; -. [P09960-1]
DR   PIR; S65947; S65947.
DR   RefSeq; NP_000886.1; NM_000895.2. [P09960-1]
DR   RefSeq; NP_001243572.1; NM_001256643.1. [P09960-4]
DR   RefSeq; NP_001243573.1; NM_001256644.1. [P09960-3]
DR   RefSeq; XP_005268928.1; XM_005268871.1. [P09960-2]
DR   PDB; 1GW6; X-ray; 2.20 A; A=2-611.
DR   PDB; 1H19; X-ray; 2.10 A; A=2-611.
DR   PDB; 1HS6; X-ray; 1.95 A; A=1-611.
DR   PDB; 1SQM; X-ray; 2.30 A; A=2-611.
DR   PDB; 2R59; X-ray; 1.89 A; A=2-611.
DR   PDB; 2VJ8; X-ray; 1.80 A; A=1-611.
DR   PDB; 3B7R; X-ray; 1.81 A; L=2-611.
DR   PDB; 3B7S; X-ray; 1.47 A; A=2-611.
DR   PDB; 3B7T; X-ray; 2.30 A; A=2-611.
DR   PDB; 3B7U; X-ray; 1.90 A; X=2-611.
DR   PDB; 3CHO; X-ray; 1.80 A; A=2-611.
DR   PDB; 3CHP; X-ray; 2.10 A; A=2-611.
DR   PDB; 3CHQ; X-ray; 2.09 A; A=2-611.
DR   PDB; 3CHR; X-ray; 2.20 A; A=2-611.
DR   PDB; 3CHS; X-ray; 2.55 A; A=2-611.
DR   PDB; 3FH5; X-ray; 1.63 A; A=1-611.
DR   PDB; 3FH7; X-ray; 2.05 A; A=1-611.
DR   PDB; 3FH8; X-ray; 1.67 A; A=1-611.
DR   PDB; 3FHE; X-ray; 2.16 A; A=1-611.
DR   PDB; 3FTS; X-ray; 2.33 A; A=1-611.
DR   PDB; 3FTU; X-ray; 1.90 A; A=1-611.
DR   PDB; 3FTV; X-ray; 1.70 A; A=1-611.
DR   PDB; 3FTW; X-ray; 1.85 A; A=1-611.
DR   PDB; 3FTX; X-ray; 1.96 A; A=1-611.
DR   PDB; 3FTY; X-ray; 2.15 A; A=1-611.
DR   PDB; 3FTZ; X-ray; 2.00 A; A=1-611.
DR   PDB; 3FU0; X-ray; 1.80 A; A=1-611.
DR   PDB; 3FU3; X-ray; 2.00 A; A=1-611.
DR   PDB; 3FU5; X-ray; 2.30 A; A=1-611.
DR   PDB; 3FU6; X-ray; 2.05 A; A=1-611.
DR   PDB; 3FUD; X-ray; 2.20 A; A=1-611.
DR   PDB; 3FUE; X-ray; 2.38 A; A=1-611.
DR   PDB; 3FUF; X-ray; 2.60 A; A=1-611.
DR   PDB; 3FUH; X-ray; 1.80 A; A=1-611.
DR   PDB; 3FUI; X-ray; 2.20 A; A=1-611.
DR   PDB; 3FUJ; X-ray; 1.90 A; A=1-611.
DR   PDB; 3FUK; X-ray; 1.95 A; A=1-611.
DR   PDB; 3FUL; X-ray; 2.39 A; A=1-611.
DR   PDB; 3FUM; X-ray; 2.15 A; A=1-611.
DR   PDB; 3FUN; X-ray; 1.58 A; A=1-611.
DR   PDB; 3U9W; X-ray; 1.25 A; A=4-611.
DR   PDB; 4DPR; X-ray; 2.02 A; A=1-611.
DR   PDB; 4L2L; X-ray; 1.65 A; A=1-611.
DR   PDB; 4MKT; X-ray; 1.62 A; A=1-611.
DR   PDB; 4MS6; X-ray; 1.72 A; A=1-611.
DR   PDB; 4R7L; X-ray; 1.66 A; A=1-611.
DR   PDB; 4RSY; X-ray; 1.93 A; A=1-611.
DR   PDB; 4RVB; X-ray; 1.93 A; A=1-611.
DR   PDB; 5AEN; X-ray; 1.86 A; A=4-611.
DR   PDB; 5BPP; X-ray; 2.03 A; A=1-611.
DR   PDB; 5FWQ; X-ray; 2.05 A; A=1-611.
DR   PDB; 5N3W; X-ray; 2.30 A; A=1-611.
DR   PDB; 5NI2; X-ray; 1.50 A; A=2-611.
DR   PDB; 5NI4; X-ray; 1.90 A; A/B/C=2-611.
DR   PDB; 5NI6; X-ray; 1.54 A; A=2-611.
DR   PDB; 5NIA; X-ray; 1.76 A; A=2-611.
DR   PDB; 5NID; X-ray; 1.57 A; A=2-611.
DR   PDB; 5NIE; X-ray; 2.60 A; A/B/C=2-611.
DR   PDB; 6ENB; X-ray; 1.84 A; A=2-611.
DR   PDB; 6ENC; X-ray; 1.95 A; A=2-611.
DR   PDB; 6END; X-ray; 2.24 A; A=2-611.
DR   PDB; 6O5H; X-ray; 2.84 A; A/B/C=4-611.
DR   PDBsum; 1GW6; -.
DR   PDBsum; 1H19; -.
DR   PDBsum; 1HS6; -.
DR   PDBsum; 1SQM; -.
DR   PDBsum; 2R59; -.
DR   PDBsum; 2VJ8; -.
DR   PDBsum; 3B7R; -.
DR   PDBsum; 3B7S; -.
DR   PDBsum; 3B7T; -.
DR   PDBsum; 3B7U; -.
DR   PDBsum; 3CHO; -.
DR   PDBsum; 3CHP; -.
DR   PDBsum; 3CHQ; -.
DR   PDBsum; 3CHR; -.
DR   PDBsum; 3CHS; -.
DR   PDBsum; 3FH5; -.
DR   PDBsum; 3FH7; -.
DR   PDBsum; 3FH8; -.
DR   PDBsum; 3FHE; -.
DR   PDBsum; 3FTS; -.
DR   PDBsum; 3FTU; -.
DR   PDBsum; 3FTV; -.
DR   PDBsum; 3FTW; -.
DR   PDBsum; 3FTX; -.
DR   PDBsum; 3FTY; -.
DR   PDBsum; 3FTZ; -.
DR   PDBsum; 3FU0; -.
DR   PDBsum; 3FU3; -.
DR   PDBsum; 3FU5; -.
DR   PDBsum; 3FU6; -.
DR   PDBsum; 3FUD; -.
DR   PDBsum; 3FUE; -.
DR   PDBsum; 3FUF; -.
DR   PDBsum; 3FUH; -.
DR   PDBsum; 3FUI; -.
DR   PDBsum; 3FUJ; -.
DR   PDBsum; 3FUK; -.
DR   PDBsum; 3FUL; -.
DR   PDBsum; 3FUM; -.
DR   PDBsum; 3FUN; -.
DR   PDBsum; 3U9W; -.
DR   PDBsum; 4DPR; -.
DR   PDBsum; 4L2L; -.
DR   PDBsum; 4MKT; -.
DR   PDBsum; 4MS6; -.
DR   PDBsum; 4R7L; -.
DR   PDBsum; 4RSY; -.
DR   PDBsum; 4RVB; -.
DR   PDBsum; 5AEN; -.
DR   PDBsum; 5BPP; -.
DR   PDBsum; 5FWQ; -.
DR   PDBsum; 5N3W; -.
DR   PDBsum; 5NI2; -.
DR   PDBsum; 5NI4; -.
DR   PDBsum; 5NI6; -.
DR   PDBsum; 5NIA; -.
DR   PDBsum; 5NID; -.
DR   PDBsum; 5NIE; -.
DR   PDBsum; 6ENB; -.
DR   PDBsum; 6ENC; -.
DR   PDBsum; 6END; -.
DR   PDBsum; 6O5H; -.
DR   SMR; P09960; -.
DR   BioGRID; 110226; 26.
DR   IntAct; P09960; 8.
DR   STRING; 9606.ENSP00000228740; -.
DR   BindingDB; P09960; -.
DR   ChEMBL; CHEMBL4618; -.
DR   DrugBank; DB07102; (2S)-2-amino-5-oxo-5-[(4-phenylmethoxyphenyl)amino]pentanoic acid.
DR   DrugBank; DB06917; (4-fluorophenyl)(pyridin-4-yl)methanone.
DR   DrugBank; DB07258; (R)-pyridin-4-yl[4-(2-pyrrolidin-1-ylethoxy)phenyl]methanol.
DR   DrugBank; DB07094; 1-(2,2'-bithiophen-5-yl)methanamine.
DR   DrugBank; DB07259; 1-(4-thiophen-2-ylphenyl)methanamine.
DR   DrugBank; DB02352; 3-(Benzyloxy)Pyridin-2-Amine.
DR   DrugBank; DB07292; 4-(2-amino-1,3-thiazol-4-yl)phenol.
DR   DrugBank; DB07104; 4-amino-N-[4-(benzyloxy)phenyl]butanamide.
DR   DrugBank; DB06828; 5-[2-(1H-pyrrol-1-yl)ethoxy]-1H-indole.
DR   DrugBank; DB08466; 5-[2-(4-hydroxyphenyl)ethyl]benzene-1,3-diol.
DR   DrugBank; DB01197; Captopril.
DR   DrugBank; DB05177; DG051.
DR   DrugBank; DB03366; Imidazole.
DR   DrugBank; DB06851; N-(pyridin-3-ylmethyl)aniline.
DR   DrugBank; DB08040; N-[(2R)-2-benzyl-4-(hydroxyamino)-4-oxobutanoyl]-L-alanine.
DR   DrugBank; DB02062; N-[3-[(1-Aminoethyl)(Hydroxy)Phosphoryl]-2-(1,1'-Biphenyl-4-Ylmethyl)Propanoyl]Alanine.
DR   DrugBank; DB07099; N-[4-(benzyloxy)phenyl]glycinamide.
DR   DrugBank; DB07260; N-benzyl-4-[(2R)-pyrrolidin-2-ylmethoxy]aniline.
DR   DrugBank; DB07196; N-methyl-1-(2-thiophen-2-ylphenyl)methanamine.
DR   DrugBank; DB11781; Tosedostat.
DR   DrugBank; DB03424; Ubenimex.
DR   DrugBank; DB07237; {4-[(2R)-pyrrolidin-2-ylmethoxy]phenyl}(4-thiophen-3-ylphenyl)methanone.
DR   DrugCentral; P09960; -.
DR   GuidetoPHARMACOLOGY; 1395; -.
DR   SwissLipids; SLP:000001118; -.
DR   MEROPS; M01.004; -.
DR   MoonProt; P09960; -.
DR   iPTMnet; P09960; -.
DR   MetOSite; P09960; -.
DR   PhosphoSitePlus; P09960; -.
DR   SwissPalm; P09960; -.
DR   BioMuta; LTA4H; -.
DR   DMDM; 126353; -.
DR   REPRODUCTION-2DPAGE; IPI00219077; -.
DR   CPTAC; CPTAC-92; -.
DR   CPTAC; CPTAC-93; -.
DR   EPD; P09960; -.
DR   jPOST; P09960; -.
DR   MassIVE; P09960; -.
DR   MaxQB; P09960; -.
DR   PaxDb; P09960; -.
DR   PeptideAtlas; P09960; -.
DR   PRIDE; P09960; -.
DR   ProteomicsDB; 28779; -.
DR   ProteomicsDB; 52284; -. [P09960-1]
DR   ProteomicsDB; 52285; -. [P09960-2]
DR   ProteomicsDB; 52286; -. [P09960-3]
DR   Antibodypedia; 4453; 484 antibodies.
DR   DNASU; 4048; -.
DR   Ensembl; ENST00000228740; ENSP00000228740; ENSG00000111144. [P09960-1]
DR   Ensembl; ENST00000413268; ENSP00000395051; ENSG00000111144. [P09960-3]
DR   Ensembl; ENST00000552789; ENSP00000449958; ENSG00000111144. [P09960-4]
DR   GeneID; 4048; -.
DR   KEGG; hsa:4048; -.
DR   UCSC; uc001ten.3; human. [P09960-1]
DR   CTD; 4048; -.
DR   DisGeNET; 4048; -.
DR   EuPathDB; HostDB:ENSG00000111144.9; -.
DR   GeneCards; LTA4H; -.
DR   HGNC; HGNC:6710; LTA4H.
DR   HPA; ENSG00000111144; Low tissue specificity.
DR   MIM; 151570; gene.
DR   neXtProt; NX_P09960; -.
DR   OpenTargets; ENSG00000111144; -.
DR   PharmGKB; PA24345; -.
DR   eggNOG; KOG1047; Eukaryota.
DR   eggNOG; COG0308; LUCA.
DR   GeneTree; ENSGT00940000156375; -.
DR   HOGENOM; CLU_014505_0_0_1; -.
DR   InParanoid; P09960; -.
DR   KO; K01254; -.
DR   OMA; NSNFRMK; -.
DR   PhylomeDB; P09960; -.
DR   TreeFam; TF300758; -.
DR   BioCyc; MetaCyc:HS03372-MONOMER; -.
DR   BRENDA; 3.3.2.6; 2681.
DR   Reactome; R-HSA-2142691; Synthesis of Leukotrienes (LT) and Eoxins (EX).
DR   Reactome; R-HSA-6798695; Neutrophil degranulation.
DR   Reactome; R-HSA-9018676; Biosynthesis of D-series resolvins.
DR   Reactome; R-HSA-9018681; Biosynthesis of protectins.
DR   Reactome; R-HSA-9018896; Biosynthesis of E-series 18(S)-resolvins.
DR   Reactome; R-HSA-9020265; Biosynthesis of aspirin-triggered D-series resolvins.
DR   Reactome; R-HSA-9023661; Biosynthesis of E-series 18(R)-resolvins.
DR   SABIO-RK; P09960; -.
DR   UniPathway; UPA00878; -.
DR   BioGRID-ORCS; 4048; 1 hit in 790 CRISPR screens.
DR   ChiTaRS; LTA4H; human.
DR   EvolutionaryTrace; P09960; -.
DR   GenomeRNAi; 4048; -.
DR   Pharos; P09960; Tchem.
DR   PRO; PR:P09960; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; P09960; protein.
DR   Bgee; ENSG00000111144; Expressed in visceral pleura and 232 other tissues.
DR   ExpressionAtlas; P09960; baseline and differential.
DR   Genevisible; P09960; HS.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:1904724; C:tertiary granule lumen; TAS:Reactome.
DR   GO; GO:0004177; F:aminopeptidase activity; IDA:UniProtKB.
DR   GO; GO:0004301; F:epoxide hydrolase activity; IDA:UniProtKB.
DR   GO; GO:0004463; F:leukotriene-A4 hydrolase activity; IDA:UniProtKB.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IMP:CAFA.
DR   GO; GO:0008233; F:peptidase activity; TAS:ProtInc.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR   GO; GO:0044255; P:cellular lipid metabolic process; IBA:GO_Central.
DR   GO; GO:0044267; P:cellular protein metabolic process; IMP:CAFA.
DR   GO; GO:0019370; P:leukotriene biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0006691; P:leukotriene metabolic process; TAS:Reactome.
DR   GO; GO:0042759; P:long-chain fatty acid biosynthetic process; TAS:Reactome.
DR   GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
DR   GO; GO:0043171; P:peptide catabolic process; IDA:UniProtKB.
DR   CDD; cd09599; M1_LTA4H; 1.
DR   Gene3D; 1.10.390.10; -; 1.
DR   Gene3D; 1.25.40.320; -; 1.
DR   Gene3D; 2.60.40.1730; -; 1.
DR   InterPro; IPR042097; Aminopeptidase_N-like_N.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR012777; LTA4H.
DR   InterPro; IPR038502; M1_LTA-4_hydro/amino_C_sf.
DR   InterPro; IPR034015; M1_LTA4H.
DR   InterPro; IPR001930; Peptidase_M1.
DR   InterPro; IPR015211; Peptidase_M1_C.
DR   InterPro; IPR014782; Peptidase_M1_dom.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   Pfam; PF09127; Leuk-A4-hydro_C; 1.
DR   Pfam; PF01433; Peptidase_M1; 1.
DR   PRINTS; PR00756; ALADIPTASE.
DR   SMART; SM01263; Leuk-A4-hydro_C; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   SUPFAM; SSF63737; SSF63737; 1.
DR   TIGRFAMs; TIGR02411; leuko_A4_hydro; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW   Direct protein sequencing; Hydrolase; Leukotriene biosynthesis;
KW   Metal-binding; Metalloprotease; Phosphoprotein; Polymorphism; Protease;
KW   Reference proteome; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000244|PubMed:22223895,
FT                   ECO:0000269|PubMed:1897988, ECO:0000269|PubMed:6490615"
FT   CHAIN           2..611
FT                   /note="Leukotriene A-4 hydrolase"
FT                   /id="PRO_0000095124"
FT   REGION          135..137
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000269|PubMed:18804029"
FT   REGION          267..272
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000269|PubMed:18804029"
FT   REGION          564..566
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000269|PubMed:18804029"
FT   ACT_SITE        297
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000244|PDB:1H19,
FT                   ECO:0000269|PubMed:11675384, ECO:0000305|PubMed:12207002"
FT   ACT_SITE        384
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000244|PDB:1H19,
FT                   ECO:0000269|PubMed:11675384, ECO:0000305|PubMed:12207002"
FT   METAL           296
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000244|PDB:1GW6, ECO:0000244|PDB:1H19,
FT                   ECO:0000244|PDB:1HS6, ECO:0000244|PDB:1SQM,
FT                   ECO:0000244|PDB:2R59, ECO:0000244|PDB:2VJ8,
FT                   ECO:0000244|PDB:3B7R, ECO:0000244|PDB:3B7S,
FT                   ECO:0000244|PDB:3B7T, ECO:0000244|PDB:3B7U,
FT                   ECO:0000244|PDB:3CHO, ECO:0000244|PDB:3CHP,
FT                   ECO:0000244|PDB:3CHQ, ECO:0000244|PDB:3CHR,
FT                   ECO:0000244|PDB:3CHS, ECO:0000244|PDB:3FH5,
FT                   ECO:0000244|PDB:3FH7, ECO:0000244|PDB:3FH8,
FT                   ECO:0000244|PDB:3FHE, ECO:0000244|PDB:3FTS,
FT                   ECO:0000244|PDB:3FTU, ECO:0000244|PDB:3FTV,
FT                   ECO:0000244|PDB:3FTW, ECO:0000244|PDB:3FTX,
FT                   ECO:0000244|PDB:3FTY, ECO:0000244|PDB:3FTZ,
FT                   ECO:0000244|PDB:3FU0, ECO:0000244|PDB:3FU3,
FT                   ECO:0000244|PDB:3FU5, ECO:0000244|PDB:3FU6,
FT                   ECO:0000244|PDB:3FUD, ECO:0000244|PDB:3FUE,
FT                   ECO:0000244|PDB:3FUF, ECO:0000244|PDB:3FUH,
FT                   ECO:0000244|PDB:3FUI, ECO:0000244|PDB:3FUJ,
FT                   ECO:0000244|PDB:3FUK, ECO:0000244|PDB:3FUL,
FT                   ECO:0000244|PDB:3FUM, ECO:0000244|PDB:3FUN,
FT                   ECO:0000244|PDB:3U9W, ECO:0000244|PDB:4DPR,
FT                   ECO:0000244|PDB:4L2L, ECO:0000244|PDB:4MKT,
FT                   ECO:0000244|PDB:4MS6, ECO:0000244|PDB:5AEN,
FT                   ECO:0000269|PubMed:11175901, ECO:0000269|PubMed:11675384,
FT                   ECO:0000269|PubMed:11917124, ECO:0000269|PubMed:12207002,
FT                   ECO:0000269|PubMed:15078870, ECO:0000269|PubMed:18804029,
FT                   ECO:0000269|PubMed:19618939"
FT   METAL           300
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000244|PDB:1GW6, ECO:0000244|PDB:1H19,
FT                   ECO:0000244|PDB:1HS6, ECO:0000244|PDB:1SQM,
FT                   ECO:0000244|PDB:2R59, ECO:0000244|PDB:2VJ8,
FT                   ECO:0000244|PDB:3B7R, ECO:0000244|PDB:3B7S,
FT                   ECO:0000244|PDB:3B7T, ECO:0000244|PDB:3B7U,
FT                   ECO:0000244|PDB:3CHO, ECO:0000244|PDB:3CHP,
FT                   ECO:0000244|PDB:3CHQ, ECO:0000244|PDB:3CHR,
FT                   ECO:0000244|PDB:3CHS, ECO:0000244|PDB:3FH5,
FT                   ECO:0000244|PDB:3FH7, ECO:0000244|PDB:3FH8,
FT                   ECO:0000244|PDB:3FHE, ECO:0000244|PDB:3FTS,
FT                   ECO:0000244|PDB:3FTU, ECO:0000244|PDB:3FTV,
FT                   ECO:0000244|PDB:3FTW, ECO:0000244|PDB:3FTX,
FT                   ECO:0000244|PDB:3FTY, ECO:0000244|PDB:3FTZ,
FT                   ECO:0000244|PDB:3FU0, ECO:0000244|PDB:3FU3,
FT                   ECO:0000244|PDB:3FU5, ECO:0000244|PDB:3FU6,
FT                   ECO:0000244|PDB:3FUD, ECO:0000244|PDB:3FUE,
FT                   ECO:0000244|PDB:3FUF, ECO:0000244|PDB:3FUH,
FT                   ECO:0000244|PDB:3FUI, ECO:0000244|PDB:3FUJ,
FT                   ECO:0000244|PDB:3FUK, ECO:0000244|PDB:3FUL,
FT                   ECO:0000244|PDB:3FUM, ECO:0000244|PDB:3FUN,
FT                   ECO:0000244|PDB:3U9W, ECO:0000244|PDB:4DPR,
FT                   ECO:0000244|PDB:4L2L, ECO:0000244|PDB:4MKT,
FT                   ECO:0000244|PDB:4MS6, ECO:0000244|PDB:5AEN,
FT                   ECO:0000269|PubMed:11175901, ECO:0000269|PubMed:11675384,
FT                   ECO:0000269|PubMed:11917124, ECO:0000269|PubMed:12207002,
FT                   ECO:0000269|PubMed:15078870, ECO:0000269|PubMed:18804029,
FT                   ECO:0000269|PubMed:19618939"
FT   METAL           319
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000244|PDB:1GW6, ECO:0000244|PDB:1H19,
FT                   ECO:0000244|PDB:1HS6, ECO:0000244|PDB:1SQM,
FT                   ECO:0000244|PDB:2R59, ECO:0000244|PDB:2VJ8,
FT                   ECO:0000244|PDB:3B7R, ECO:0000244|PDB:3B7S,
FT                   ECO:0000244|PDB:3B7T, ECO:0000244|PDB:3B7U,
FT                   ECO:0000244|PDB:3CHO, ECO:0000244|PDB:3CHP,
FT                   ECO:0000244|PDB:3CHQ, ECO:0000244|PDB:3CHR,
FT                   ECO:0000244|PDB:3CHS, ECO:0000244|PDB:3FH5,
FT                   ECO:0000244|PDB:3FH7, ECO:0000244|PDB:3FH8,
FT                   ECO:0000244|PDB:3FHE, ECO:0000244|PDB:3FTS,
FT                   ECO:0000244|PDB:3FTU, ECO:0000244|PDB:3FTV,
FT                   ECO:0000244|PDB:3FTW, ECO:0000244|PDB:3FTX,
FT                   ECO:0000244|PDB:3FTY, ECO:0000244|PDB:3FTZ,
FT                   ECO:0000244|PDB:3FU0, ECO:0000244|PDB:3FU3,
FT                   ECO:0000244|PDB:3FU5, ECO:0000244|PDB:3FU6,
FT                   ECO:0000244|PDB:3FUD, ECO:0000244|PDB:3FUE,
FT                   ECO:0000244|PDB:3FUF, ECO:0000244|PDB:3FUH,
FT                   ECO:0000244|PDB:3FUI, ECO:0000244|PDB:3FUJ,
FT                   ECO:0000244|PDB:3FUK, ECO:0000244|PDB:3FUL,
FT                   ECO:0000244|PDB:3FUM, ECO:0000244|PDB:3FUN,
FT                   ECO:0000244|PDB:3U9W, ECO:0000244|PDB:4DPR,
FT                   ECO:0000244|PDB:4L2L, ECO:0000244|PDB:4MKT,
FT                   ECO:0000244|PDB:4MS6, ECO:0000244|PDB:5AEN,
FT                   ECO:0000269|PubMed:11175901, ECO:0000269|PubMed:11675384,
FT                   ECO:0000269|PubMed:11917124, ECO:0000269|PubMed:12207002,
FT                   ECO:0000269|PubMed:15078870, ECO:0000269|PubMed:18804029,
FT                   ECO:0000269|PubMed:19618939"
FT   SITE            376
FT                   /note="Essential for epoxide hydrolase activity, but not
FT                   for aminopeptidase activity"
FT   SITE            379
FT                   /note="Covalently modified during suicide inhibition by
FT                   leukotrienes"
FT   MOD_RES         73
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000244|PubMed:19608861"
FT   MOD_RES         337
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000244|PubMed:19608861"
FT   MOD_RES         414
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000244|PubMed:19608861"
FT   MOD_RES         416
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:9395533"
FT   MOD_RES         573
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000244|PubMed:19608861"
FT   VAR_SEQ         1..53
FT                   /note="MPEIVDTCSLASPASVCRTKHLHLRCSVDFTRRTLTGTAALTVQSQEDNLRS
FT                   L -> MLPQRNLSKRQVPTMHIPVKTRRLLAALK (in isoform 3 and
FT                   isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:17974005"
FT                   /id="VSP_041107"
FT   VAR_SEQ         511..532
FT                   /note="APLPLGHIKRMQEVYNFNAINN -> MAAALHSIQVGGRNSFGAKDGN (in
FT                   isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_041108"
FT   VAR_SEQ         533..611
FT                   /note="Missing (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_041109"
FT   VARIANT         131
FT                   /note="Y -> H (in dbSNP:rs45630737)"
FT                   /id="VAR_051570"
FT   MUTAGEN         135
FT                   /note="Q->A,L: Srongly increased epoxide hydrolase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:11917124"
FT   MUTAGEN         135
FT                   /note="Q->A: Strongly reduced aminopeptidase activity.
FT                   Strongly decreased affinity for leukotriene. Abolishes
FT                   epoxide hydrolase activity."
FT                   /evidence="ECO:0000269|PubMed:11917124"
FT   MUTAGEN         137
FT                   /note="Q->A: No loss of activity."
FT                   /evidence="ECO:0000269|PubMed:11675384"
FT   MUTAGEN         137
FT                   /note="Q->L: Aminopeptidase activity strongly impaired, but
FT                   keeps LTA4 activity."
FT                   /evidence="ECO:0000269|PubMed:11675384"
FT   MUTAGEN         137
FT                   /note="Q->N: Aminopeptidase activity almost absent, but
FT                   keeps LTA4 activity."
FT                   /evidence="ECO:0000269|PubMed:11675384"
FT   MUTAGEN         140
FT                   /note="H->Q: Aminopeptidase activity almost absent, but
FT                   keeps LTA4 activity."
FT                   /evidence="ECO:0000269|PubMed:11917124"
FT   MUTAGEN         269
FT                   /note="G->A: No loss of activity."
FT                   /evidence="ECO:0000269|PubMed:1881903"
FT   MUTAGEN         270
FT                   /note="G->A: No loss of activity."
FT                   /evidence="ECO:0000269|PubMed:11675384"
FT   MUTAGEN         271
FT                   /note="M->L: No loss of activity."
FT                   /evidence="ECO:0000269|PubMed:11675384"
FT   MUTAGEN         272
FT                   /note="E->A,D: Complete loss of activity."
FT                   /evidence="ECO:0000269|PubMed:11675384"
FT   MUTAGEN         272
FT                   /note="E->Q: Loss of LTA4 activity, and aminopeptidase
FT                   activity strongly impaired."
FT                   /evidence="ECO:0000269|PubMed:11675384"
FT   MUTAGEN         273
FT                   /note="N->A: No loss of activity."
FT                   /evidence="ECO:0000269|PubMed:11675384"
FT   MUTAGEN         296
FT                   /note="H->Y: Complete loss of activity."
FT                   /evidence="ECO:0000269|PubMed:1881903"
FT   MUTAGEN         297
FT                   /note="E->A: Loss of both activities."
FT                   /evidence="ECO:0000269|PubMed:1357660,
FT                   ECO:0000269|PubMed:1516710, ECO:0000269|PubMed:18804029"
FT   MUTAGEN         297
FT                   /note="E->K: Loss of both activities."
FT                   /evidence="ECO:0000269|PubMed:1357660,
FT                   ECO:0000269|PubMed:1516710, ECO:0000269|PubMed:18804029"
FT   MUTAGEN         297
FT                   /note="E->Q: Loss of aminopeptidase activity, but keeps
FT                   LTA4 activity."
FT                   /evidence="ECO:0000269|PubMed:1357660,
FT                   ECO:0000269|PubMed:1516710, ECO:0000269|PubMed:18804029"
FT   MUTAGEN         300
FT                   /note="H->L: Complete loss of activity."
FT                   /evidence="ECO:0000269|PubMed:1881903"
FT   MUTAGEN         319
FT                   /note="E->A: Complete loss of activity."
FT                   /evidence="ECO:0000269|PubMed:1881903"
FT   MUTAGEN         372
FT                   /note="D->N: No loss of activity."
FT                   /evidence="ECO:0000269|PubMed:11917124"
FT   MUTAGEN         374
FT                   /note="D->N: No loss of activity."
FT                   /evidence="ECO:0000269|PubMed:11917124"
FT   MUTAGEN         376
FT                   /note="D->A: Strongly reduced hydrolysis of peptides
FT                   starting with Arg. Small effect on hydrolysis of peptides
FT                   starting with Ala. Strongly reduced epoxide hydrolase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:11917124,
FT                   ECO:0000269|PubMed:18804029"
FT   MUTAGEN         376
FT                   /note="D->E: Strongly reduced aminopeptidase activity.
FT                   Abolishes epoxide hydrolase activity."
FT                   /evidence="ECO:0000269|PubMed:11917124,
FT                   ECO:0000269|PubMed:18804029"
FT   MUTAGEN         376
FT                   /note="D->N: Abolishes aminopeptidase and epoxide hydrolase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:11917124,
FT                   ECO:0000269|PubMed:18804029"
FT   MUTAGEN         385
FT                   /note="E->Q: Reduced aminopeptidase activity. Minor effect
FT                   on epoxide hydrolase activity."
FT                   /evidence="ECO:0000269|PubMed:11917124"
FT   MUTAGEN         564
FT                   /note="R->A,K,M: Abolishes epoxide hydrolase activity.
FT                   Reduced aminopeptidase activity."
FT                   /evidence="ECO:0000269|PubMed:15078870"
FT   MUTAGEN         566
FT                   /note="K->A,M: Strongly reduced affinity for peptide
FT                   substrates. Reduced epoxide hydrolase and aminopeptidase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:15078870"
FT   MUTAGEN         566
FT                   /note="K->R: No effect on epoxide hydrolase and
FT                   aminopeptidase activity."
FT                   /evidence="ECO:0000269|PubMed:15078870"
FT   CONFLICT        115
FT                   /note="A -> T (in Ref. 6; BX647158)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        123
FT                   /note="Q -> R (in Ref. 6; BX647158)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        297
FT                   /note="E -> G (in Ref. 4; BAG60321)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        309
FT                   /note="N -> S (in Ref. 6; BX647158)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        378
FT                   /note="A -> V (in Ref. 6; BX647158)"
FT                   /evidence="ECO:0000305"
FT   TURN            14..16
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   STRAND          17..29
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   TURN            30..33
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   STRAND          34..45
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   STRAND          50..59
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   STRAND          61..67
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   STRAND          74..76
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   HELIX           81..83
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   STRAND          85..95
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   STRAND          100..108
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   STRAND          116..119
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   HELIX           121..123
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   STRAND          124..129
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   STRAND          131..134
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   TURN            137..140
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   HELIX           141..143
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   STRAND          155..164
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   STRAND          167..180
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   STRAND          182..184
FT                   /evidence="ECO:0000244|PDB:2VJ8"
FT   STRAND          187..198
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   HELIX           200..202
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   STRAND          205..209
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   STRAND          211..216
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   STRAND          219..223
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   HELIX           225..227
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   HELIX           228..234
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   TURN            235..237
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   HELIX           238..249
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   STRAND          253..255
FT                   /evidence="ECO:0000244|PDB:5NIE"
FT   STRAND          258..261
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   STRAND          267..271
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   STRAND          276..279
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   HELIX           281..283
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   STRAND          286..288
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   TURN            289..291
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   HELIX           292..299
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   TURN            300..302
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   TURN            304..306
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   STRAND          307..311
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   HELIX           312..314
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   HELIX           315..334
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   HELIX           336..357
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   HELIX           362..364
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   STRAND          365..367
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   HELIX           375..378
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   HELIX           382..398
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   HELIX           401..415
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   STRAND          418..420
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   HELIX           422..432
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   HELIX           434..436
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   HELIX           437..441
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   HELIX           445..450
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   TURN            464..466
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   HELIX           467..478
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   HELIX           481..486
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   HELIX           489..492
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   HELIX           497..508
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   HELIX           515..525
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   HELIX           527..529
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   HELIX           533..545
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   HELIX           551..561
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   HELIX           565..577
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   HELIX           579..592
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   HELIX           593..595
FT                   /evidence="ECO:0000244|PDB:3U9W"
FT   HELIX           598..608
FT                   /evidence="ECO:0000244|PDB:3U9W"
SQ   SEQUENCE   611 AA;  69285 MW;  329BF6D04D4A06E1 CRC64;
     MPEIVDTCSL ASPASVCRTK HLHLRCSVDF TRRTLTGTAA LTVQSQEDNL RSLVLDTKDL
     TIEKVVINGQ EVKYALGERQ SYKGSPMEIS LPIALSKNQE IVIEISFETS PKSSALQWLT
     PEQTSGKEHP YLFSQCQAIH CRAILPCQDT PSVKLTYTAE VSVPKELVAL MSAIRDGETP
     DPEDPSRKIY KFIQKVPIPC YLIALVVGAL ESRQIGPRTL VWSEKEQVEK SAYEFSETES
     MLKIAEDLGG PYVWGQYDLL VLPPSFPYGG MENPCLTFVT PTLLAGDKSL SNVIAHEISH
     SWTGNLVTNK TWDHFWLNEG HTVYLERHIC GRLFGEKFRH FNALGGWGEL QNSVKTFGET
     HPFTKLVVDL TDIDPDVAYS SVPYEKGFAL LFYLEQLLGG PEIFLGFLKA YVEKFSYKSI
     TTDDWKDFLY SYFKDKVDVL NQVDWNAWLY SPGLPPIKPN YDMTLTNACI ALSQRWITAK
     EDDLNSFNAT DLKDLSSHQL NEFLAQTLQR APLPLGHIKR MQEVYNFNAI NNSEIRFRWL
     RLCIQSKWED AIPLALKMAT EQGRMKFTRP LFKDLAAFDK SHDQAVRTYQ EHKASMHPVT
     AMLVGKDLKV D
//
DBGET integrated database retrieval system