LKHA4_YEAST
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 03-AUG-2022, entry version 195.
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=2.0 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; Q10740; -.
DR PRIDE; Q10740; -.
DR EnsemblFungi; YNL045W_mRNA; YNL045W; YNL045W.
DR GeneID; 855682; -.
DR KEGG; sce:YNL045W; -.
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; YHPICRQ; -.
DR BioCyc; YEAST:YNL045W-MON; -.
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 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; 1.10.390.10; -; 1.
DR Gene3D; 1.25.40.320; -; 1.
DR Gene3D; 2.60.40.1730; -; 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 PANTHER; PTHR45726; PTHR45726; 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; 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; 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: Reduces strongly 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
