ID   LKHA4_YEAST             Reviewed;         671 AA.
AC   Q10740; D6W1D4;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   08-NOV-2023, entry version 201.
DE   RecName: Full=Leucine aminopeptidase 2 {ECO:0000303|PubMed:6352682};
DE            EC=3.4.11.- {ECO:0000269|PubMed:6352682};
DE   AltName: Full=Epoxide hydrolase {ECO:0000305|PubMed:21146536};
DE            EC=3.3.2.10 {ECO:0000269|PubMed:21146536};
DE   AltName: Full=Leucyl aminopeptidase yscIV;
DE            Short=AP IV;
DE   AltName: Full=Leukotriene A-4 hydrolase homolog {ECO:0000303|PubMed:8740423};
DE            Short=LTA-4 hydrolase;
GN   Name=LAP2 {ECO:0000303|PubMed:6352682}; OrderedLocusNames=YNL045W;
GN   ORFNames=N2535;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=8740423;
RX   DOI=10.1002/(sici)1097-0061(199604)12:5<493::aid-yea929>3.0.co;2-w;
RA   Nasr F., Becam A.-M., Herbert C.J.;
RT   "The sequence of 12.8 kb from the left arm of chromosome XIV reveals a
RT   sigma element, a pro-tRNA and six complete open reading frames, one of
RT   which encodes a protein similar to the human leukotriene A4 hydrolase.";
RL   Yeast 12:493-499(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169873;
RA   Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA   Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA   Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA   Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA   Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA   Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA   Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA   Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA   Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA   Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA   Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA   Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA   Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA   Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA   Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA   Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA   Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT   evolutionary implications.";
RL   Nature 387:93-98(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX   PubMed=6352682; DOI=10.1128/jb.156.1.36-48.1983;
RA   Trumbly R.J., Bradley G.;
RT   "Isolation and characterization of aminopeptidase mutants of Saccharomyces
RT   cerevisiae.";
RL   J. Bacteriol. 156:36-48(1983).
RN   [5]
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RX   PubMed=10574934; DOI=10.1074/jbc.274.49.34683;
RA   Kull F., Ohlson E., Haeggstroem J.Z.;
RT   "Cloning and characterization of a bifunctional leukotriene A(4) hydrolase
RT   from Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 274:34683-34690(1999).
RN   [6]
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF HIS-340;
RP   GLU-341; HIS-344; GLU-363; PHE-424 AND TYR-429.
RX   PubMed=11601994; DOI=10.1021/bi011348p;
RA   Kull F., Ohlson E., Lind B., Haeggstroem J.Z.;
RT   "Saccharomyces cerevisiae leukotriene A4 hydrolase: formation of
RT   leukotriene B4 and identification of catalytic residues.";
RL   Biochemistry 40:12695-12703(2001).
RN   [7]
RP   CRYSTALLIZATION.
RX   PubMed=12777785; DOI=10.1107/s0907444903007728;
RA   Andersson B., Kull F., Haeggstroem J.Z., Thunnissen M.M.G.M.;
RT   "Crystallization and X-ray diffraction data analysis of leukotriene A4
RT   hydrolase from Saccharomyces cerevisiae.";
RL   Acta Crystallogr. D 59:1093-1095(2003).
RN   [8]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [9]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [10]
RP   FUNCTION, ACTIVITY REGULATION, AND MUTAGENESIS.
RX   PubMed=16024909; DOI=10.1074/jbc.m506821200;
RA   Tholander F., Kull F., Ohlson E., Shafqat J., Thunnissen M.M.G.M.,
RA   Haeggstroem J.Z.;
RT   "Leukotriene A4 hydrolase, insights into the molecular evolution by
RT   homology modeling and mutational analysis of enzyme from Saccharomyces
RT   cerevisiae.";
RL   J. Biol. Chem. 280:33477-33486(2005).
RN   [11]
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF TYR-244.
RX   PubMed=16597475; DOI=10.1016/j.peptides.2006.02.006;
RA   Thompson M.W., Archer E.D., Romer C.E., Seipelt R.L.;
RT   "A conserved tyrosine residue of Saccharomyces cerevisiae leukotriene A4
RT   hydrolase stabilizes the transition state of the peptidase activity.";
RL   Peptides 27:1701-1709(2006).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF 40-669 IN COMPLEX WITH ZINC IONS
RP   AND BESTATIN, CATALYTIC ACTIVITY, FUNCTION, AND COFACTOR.
RX   PubMed=21146536; DOI=10.1016/j.jmb.2010.11.059;
RA   Helgstrand C., Hasan M., Uysal H., Haeggstrom J.Z., Thunnissen M.M.;
RT   "A leukotriene A4 hydrolase-related aminopeptidase from yeast undergoes
RT   induced fit upon inhibitor binding.";
RL   J. Mol. Biol. 406:120-134(2011).
CC   -!- FUNCTION: Aminopeptidase that preferentially cleaves di- and
CC       tripeptides. Also has low epoxide hydrolase activity (in vitro). Can
CC       hydrolyze the epoxide leukotriene LTA(4) but it forms preferentially
CC       5,6-dihydroxy-7,9,11,14-eicosatetraenoic acid rather than the cytokine
CC       leukotriene B(4) as the product compared to the homologous mammalian
CC       enzyme (in vitro). {ECO:0000269|PubMed:10574934,
CC       ECO:0000269|PubMed:11601994, ECO:0000269|PubMed:16024909,
CC       ECO:0000269|PubMed:16597475, ECO:0000269|PubMed:21146536,
CC       ECO:0000269|PubMed:6352682}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an epoxide + H2O = an ethanediol; Xref=Rhea:RHEA:19037,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:32955, ChEBI:CHEBI:140594;
CC         EC=3.3.2.10; Evidence={ECO:0000269|PubMed:21146536};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000269|PubMed:21146536};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:21146536};
CC   -!- ACTIVITY REGULATION: Inhibited by 3-(4-benzyloxyphenyl)-2-(R)-amino-1-
CC       propanethiol (thioamine) and N-hydroxy-N-(2-(S)-amino-3-(4-
CC       benzyloxyphenyl)propyl)-5-carboxypen-tanamide (hydroxamic acid). The
CC       aminopeptidase activity is stimulated by LTA(4).
CC       {ECO:0000269|PubMed:10574934, ECO:0000269|PubMed:16024909}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.5 mM for Leu-p-nitroanilide {ECO:0000269|PubMed:10574934,
CC         ECO:0000269|PubMed:11601994, ECO:0000269|PubMed:16597475};
CC         KM=1.8 mM for Met-p-nitroanilide {ECO:0000269|PubMed:10574934,
CC         ECO:0000269|PubMed:11601994, ECO:0000269|PubMed:16597475};
CC         KM=2 mM for Ala-p-nitroanilide {ECO:0000269|PubMed:10574934,
CC         ECO:0000269|PubMed:11601994, ECO:0000269|PubMed:16597475};
CC         Vmax=520 nmol/min/mg enzyme with Leu-p-nitroanilide as substrate
CC         {ECO:0000269|PubMed:10574934, ECO:0000269|PubMed:11601994,
CC         ECO:0000269|PubMed:16597475};
CC         Vmax=360 nmol/min/mg enzyme with Met-p-nitroanilide as substrate
CC         {ECO:0000269|PubMed:10574934, ECO:0000269|PubMed:11601994,
CC         ECO:0000269|PubMed:16597475};
CC         Vmax=170 nmol/min/mg enzyme with Ala-p-nitroanilide as substrate
CC         {ECO:0000269|PubMed:10574934, ECO:0000269|PubMed:11601994,
CC         ECO:0000269|PubMed:16597475};
CC       pH dependence:
CC         Optimum pH is about 7.3. {ECO:0000269|PubMed:10574934,
CC         ECO:0000269|PubMed:11601994, ECO:0000269|PubMed:16597475};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC       {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 5590 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the peptidase M1 family. {ECO:0000305}.
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DR   EMBL; X94547; CAA64237.1; -; Genomic_DNA.
DR   EMBL; Z71321; CAA95912.1; -; Genomic_DNA.
DR   EMBL; BK006947; DAA10500.1; -; Genomic_DNA.
DR   PIR; S61099; S61099.
DR   RefSeq; NP_014353.1; NM_001182884.1.
DR   PDB; 2XPY; X-ray; 2.73 A; A=40-671.
DR   PDB; 2XPZ; X-ray; 2.30 A; A=40-671.
DR   PDB; 2XQ0; X-ray; 1.96 A; A=40-669.
DR   PDBsum; 2XPY; -.
DR   PDBsum; 2XPZ; -.
DR   PDBsum; 2XQ0; -.
DR   AlphaFoldDB; Q10740; -.
DR   SMR; Q10740; -.
DR   BioGRID; 35779; 87.
DR   DIP; DIP-4371N; -.
DR   IntAct; Q10740; 6.
DR   MINT; Q10740; -.
DR   STRING; 4932.YNL045W; -.
DR   MEROPS; M01.034; -.
DR   iPTMnet; Q10740; -.
DR   MaxQB; Q10740; -.
DR   PaxDb; 4932-YNL045W; -.
DR   PeptideAtlas; Q10740; -.
DR   EnsemblFungi; YNL045W_mRNA; YNL045W; YNL045W.
DR   GeneID; 855682; -.
DR   KEGG; sce:YNL045W; -.
DR   AGR; SGD:S000004990; -.
DR   SGD; S000004990; LAP2.
DR   VEuPathDB; FungiDB:YNL045W; -.
DR   eggNOG; KOG1047; Eukaryota.
DR   GeneTree; ENSGT00940000156375; -.
DR   HOGENOM; CLU_014505_1_1_1; -.
DR   InParanoid; Q10740; -.
DR   OMA; CTALQWM; -.
DR   OrthoDB; 443480at2759; -.
DR   BioCyc; YEAST:YNL045W-MONOMER; -.
DR   Reactome; R-SCE-2142691; Synthesis of Leukotrienes (LT) and Eoxins (EX).
DR   Reactome; R-SCE-6798695; Neutrophil degranulation.
DR   Reactome; R-SCE-9018676; Biosynthesis of D-series resolvins.
DR   Reactome; R-SCE-9018681; Biosynthesis of protectins.
DR   Reactome; R-SCE-9018896; Biosynthesis of E-series 18(S)-resolvins.
DR   Reactome; R-SCE-9020265; Biosynthesis of aspirin-triggered D-series resolvins.
DR   Reactome; R-SCE-9023661; Biosynthesis of E-series 18(R)-resolvins.
DR   SABIO-RK; Q10740; -.
DR   BioGRID-ORCS; 855682; 4 hits in 10 CRISPR screens.
DR   EvolutionaryTrace; Q10740; -.
DR   PRO; PR:Q10740; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; Q10740; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0004177; F:aminopeptidase activity; IDA:SGD.
DR   GO; GO:0004301; F:epoxide hydrolase activity; IDA:SGD.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0044255; P:cellular lipid metabolic process; IDA:SGD.
DR   GO; GO:0043171; P:peptide catabolic process; ISS:UniProtKB.
DR   GO; GO:0030163; P:protein catabolic process; IDA:SGD.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd09599; M1_LTA4H; 1.
DR   Gene3D; 3.30.2010.30; -; 1.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR   Gene3D; 1.25.40.320; Peptidase M1, leukotriene A4 hydrolase/aminopeptidase C-terminal domain; 1.
DR   Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR   InterPro; IPR045357; Aminopeptidase_N-like_N.
DR   InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
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   NCBIfam; TIGR02411; leuko_A4_hydro; 1.
DR   PANTHER; PTHR45726; LEUKOTRIENE A-4 HYDROLASE; 1.
DR   PANTHER; PTHR45726:SF3; LEUKOTRIENE A-4 HYDROLASE; 1.
DR   Pfam; PF09127; Leuk-A4-hydro_C; 1.
DR   Pfam; PF01433; Peptidase_M1; 1.
DR   Pfam; PF17900; Peptidase_M1_N; 1.
DR   PRINTS; PR00756; ALADIPTASE.
DR   SMART; SM01263; Leuk-A4-hydro_C; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Hydrolase; Metal-binding; Metalloprotease;
KW   Nucleus; Protease; Reference proteome; Zinc.
FT   CHAIN           1..671
FT                   /note="Leucine aminopeptidase 2"
FT                   /id="PRO_0000095129"
FT   ACT_SITE        341
FT                   /note="Proton acceptor"
FT   ACT_SITE        429
FT                   /note="Proton donor"
FT   BINDING         184..186
FT                   /ligand="substrate"
FT   BINDING         311..316
FT                   /ligand="substrate"
FT   BINDING         340
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT   BINDING         344
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT   BINDING         363
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT   MUTAGEN         244
FT                   /note="Y->F: Strongly reduces the substrate affinity."
FT                   /evidence="ECO:0000269|PubMed:16597475"
FT   MUTAGEN         316
FT                   /note="E->A,Q,D: Abolishes the aminopeptidase activity."
FT                   /evidence="ECO:0000269|PubMed:16024909"
FT   MUTAGEN         340
FT                   /note="H->Q: Abolishes the epoxide hydrolase and
FT                   aminopeptidase activities."
FT                   /evidence="ECO:0000269|PubMed:11601994"
FT   MUTAGEN         341
FT                   /note="E->Q: Abolishes aminopeptidase activity. No effect
FT                   on the epoxide hydrolase activity."
FT                   /evidence="ECO:0000269|PubMed:11601994"
FT   MUTAGEN         344
FT                   /note="H->Q: Abolishes the epoxide hydrolase and
FT                   aminopeptidase activities."
FT                   /evidence="ECO:0000269|PubMed:11601994"
FT   MUTAGEN         363
FT                   /note="E->Q: Abolishes the epoxide hydrolase activity."
FT                   /evidence="ECO:0000269|PubMed:11601994"
FT   MUTAGEN         424
FT                   /note="F->Y: Increases the aminopeptidase activity and
FT                   decreases the epoxide hydrolase activity."
FT                   /evidence="ECO:0000269|PubMed:11601994"
FT   MUTAGEN         429
FT                   /note="Y->F: Abolishes the aminopeptidase activity and
FT                   decreases the epoxide hydrolase activity."
FT                   /evidence="ECO:0000269|PubMed:11601994"
FT   MUTAGEN         627
FT                   /note="R->K,A: Abolishes the aminopeptidase activity."
FT                   /evidence="ECO:0000269|PubMed:16024909"
FT   HELIX           43..48
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   STRAND          51..54
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   HELIX           64..66
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   STRAND          67..79
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   TURN            80..83
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   STRAND          84..95
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   STRAND          99..101
FT                   /evidence="ECO:0007829|PDB:2XPY"
FT   STRAND          105..109
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   STRAND          111..120
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   STRAND          127..129
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   TURN            134..136
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   STRAND          140..143
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   STRAND          147..159
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   STRAND          164..169
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   TURN            171..173
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   STRAND          175..178
FT                   /evidence="ECO:0007829|PDB:2XPY"
FT   STRAND          180..183
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   TURN            186..189
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   HELIX           190..192
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   STRAND          204..211
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   STRAND          216..222
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   STRAND          232..241
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   HELIX           243..245
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   STRAND          248..252
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   STRAND          254..259
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   STRAND          262..266
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   HELIX           268..278
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   TURN            279..281
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   HELIX           282..292
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   STRAND          297..299
FT                   /evidence="ECO:0007829|PDB:2XPZ"
FT   STRAND          303..305
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   STRAND          312..315
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   STRAND          321..323
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   HELIX           325..327
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   STRAND          330..332
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   HELIX           336..344
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   TURN            348..350
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   STRAND          351..355
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   HELIX           356..359
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   HELIX           360..378
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   HELIX           380..399
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   STRAND          401..403
FT                   /evidence="ECO:0007829|PDB:2XPZ"
FT   HELIX           404..407
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   STRAND          409..411
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   STRAND          416..418
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   HELIX           420..423
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   HELIX           427..442
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   HELIX           446..459
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   TURN            460..462
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   STRAND          463..465
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   HELIX           467..477
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   HELIX           479..481
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   HELIX           482..486
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   HELIX           490..495
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   HELIX           508..523
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   TURN            524..526
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   HELIX           530..536
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   HELIX           539..542
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   HELIX           547..558
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   STRAND          562..565
FT                   /evidence="ECO:0007829|PDB:2XPZ"
FT   HELIX           572..574
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   HELIX           576..585
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   HELIX           587..591
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   HELIX           596..608
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   HELIX           612..614
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   HELIX           615..621
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   TURN            622..624
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   HELIX           628..639
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   HELIX           643..653
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   HELIX           654..656
FT                   /evidence="ECO:0007829|PDB:2XQ0"
FT   HELIX           659..668
FT                   /evidence="ECO:0007829|PDB:2XQ0"
SQ   SEQUENCE   671 AA;  77353 MW;  454E40F030BF28FA CRC64;
     MFLLPFVIRH SSSIYLPTLR FRGLLTVISR NIHISTPHKM LPLSIEQRRP SRSPEYDQST
     LSNYKDFAVL HTDLNLSVSF EKSAISGSVT FQLKKLHEGK NKSDELHLDT SYLDVQEVHI
     DGSKADFQIE QRKEPLGSRL VINNASCNDN FTLNIQFRTT DKCTALQWLN SKQTKGGKPY
     VFSQLEAIHA RSLFPCFDTP SVKSTFTASI ESPLPVVFSG IRIEDTSKDT NIYRFEQKVP
     IPAYLIGIAS GDLSSAPIGP RSTVYTEPFR LKDCQWEFEN DVEKFIQTAE KIIFEYEWGT
     YDILVNVDSY PYGGMESPNM TFATPTLIAH DRSNIDVIAH ELAHSWSGNL VTNCSWNHFW
     LNEGWTVYLE RRIIGAIHGE PTRHFSALIG WSDLQNSIDS MKDPERFSTL VQNLNDNTDP
     DDAFSTVPYE KGFNLLFHLE TILGGKAEFD PFIRHYFKKF AKKSLDTFQF LDTLYEFYPE
     KKEILDSVDW ETWLYKPGMP PRPHFITALA DNVYQLADKW VEMAQHLKTT EDFRSEFNAI
     DIKDFNSNQL VLFLETLTQN GHSNKKPKDF DWAKFPVASR ALLDIYQDNI VKSQNAEVVF
     KMFKFQIFAK LQEEYKHLAD WLGTVGRMKF VRPGYRLLNS VDRRLALATF DKFKDTYHPI
     CKALVKQDLG L
//