PNG1_YEAST
ID PNG1_YEAST Reviewed; 363 AA.
AC Q02890; D6W3S1;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase;
DE Short=PNGase;
DE EC=3.5.1.52;
DE AltName: Full=Peptide:N-glycanase 1;
DE Short=yPNG1;
GN Name=PNG1; OrderedLocusNames=YPL096W;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [2]
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 [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF HIS-218.
RX PubMed=10831608; DOI=10.1083/jcb.149.5.1039;
RA Suzuki T., Park H., Hollingsworth N.M., Sternglanz R., Lennarz W.J.;
RT "PNG1, a yeast gene encoding a highly conserved peptide:N-glycanase.";
RL J. Cell Biol. 149:1039-1052(2000).
RN [4]
RP INTERACTION WITH RAD23.
RX PubMed=11259433; DOI=10.1074/jbc.m100826200;
RA Suzuki T., Park H., Kwofie M.A., Lennarz W.J.;
RT "Rad23 provides a link between the Png1 deglycosylating enzyme and the 26 S
RT proteasome in yeast.";
RL J. Biol. Chem. 276:21601-21607(2001).
RN [5]
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF TRP-123; CYS-129;
RP CYS-132; CYS-165; CYS-168; PHE-174; TYR-177; ARG-187; GLY-189; CYS-191;
RP TRP-194; PHE-198; THR-199; LYS-203; GLY-206; ARG-210; VAL-212; HIS-218;
RP TRP-220; GLU-222; PHE-224; ARG-230; VAL-234; ASP-235; ASP-242; TRP-251;
RP LYS-253; TYR-257; PHE-261; ASP-264; VAL-266; ASP-268; TYR-273; ARG-281;
RP ARG-347; TRP-354 AND ARG-358.
RX PubMed=11812789; DOI=10.1074/jbc.m111383200;
RA Katiyar S., Suzuki T., Balgobin B.J., Lennarz W.J.;
RT "Site-directed mutagenesis study of yeast peptide:N-glycanase. Insight into
RT the reaction mechanism of deglycosylation.";
RL J. Biol. Chem. 277:12953-12959(2002).
RN [6]
RP FUNCTION.
RX PubMed=12723970; DOI=10.1042/bj20030384;
RA Chantret I., Frenoy J.-P., Moore S.E.H.;
RT "Free-oligosaccharide control in the yeast Saccharomyces cerevisiae: roles
RT for peptide:N-glycanase (Png1p) and vacuolar mannosidase (Ams1p).";
RL Biochem. J. 373:901-908(2003).
RN [7]
RP FUNCTION.
RX PubMed=12606569; DOI=10.1093/emboj/cdg107;
RA Hirsch C., Blom D., Ploegh H.L.;
RT "A role for N-glycanase in the cytosolic turnover of glycoproteins.";
RL EMBO J. 22:1036-1046(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 INTERACTION WITH RAD23.
RX PubMed=15351714; DOI=10.1016/j.bbrc.2004.08.061;
RA Biswas S., Katiyar S., Li G., Zhou X., Lennarz W.J., Schindelin H.;
RT "The N-terminus of yeast peptide: N-glycanase interacts with the DNA repair
RT protein Rad23.";
RL Biochem. Biophys. Res. Commun. 323:149-155(2004).
RN [11]
RP FUNCTION.
RX PubMed=14726951; DOI=10.1038/sj.embor.7400066;
RA Hirsch C., Misaghi S., Blom D., Pacold M.E., Ploegh H.L.;
RT "Yeast N-glycanase distinguishes between native and non-native
RT glycoproteins.";
RL EMBO Rep. 5:201-206(2004).
RN [12]
RP MASS SPECTROMETRY, AND ACTIVITY REGULATION.
RX PubMed=15610852; DOI=10.1016/j.chembiol.2004.11.010;
RA Misaghi S., Pacold M.E., Blom D., Ploegh H.L., Korbel G.A.;
RT "Using a small molecule inhibitor of peptide: N-glycanase to probe its role
RT in glycoprotein turnover.";
RL Chem. Biol. 11:1677-1687(2004).
RN [13]
RP FUNCTION.
RX PubMed=15670854; DOI=10.1016/j.febslet.2004.12.060;
RA Joshi S., Katiyar S., Lennarz W.J.;
RT "Misfolding of glycoproteins is a prerequisite for peptide: N-glycanase
RT mediated deglycosylation.";
RL FEBS Lett. 579:823-826(2005).
RN [14]
RP ACTIVITY REGULATION.
RX PubMed=16740630; DOI=10.1074/jbc.m603236200;
RA Suzuki T., Hara I., Nakano M., Zhao G., Lennarz W.J., Schindelin H.,
RA Taniguchi N., Totani K., Matsuo I., Ito Y.;
RT "Site-specific labeling of cytoplasmic peptide: N-glycanase by N,N'-
RT diacetylchitobiose-related compounds.";
RL J. Biol. Chem. 281:22152-22160(2006).
RN [15]
RP FUNCTION.
RX PubMed=16401726; DOI=10.1083/jcb.200507149;
RA Kim I., Ahn J., Liu C., Tanabe K., Apodaca J., Suzuki T., Rao H.;
RT "The Png1-Rad23 complex regulates glycoprotein turnover.";
RL J. Cell Biol. 172:211-219(2006).
RN [16]
RP ACTIVITY REGULATION.
RX PubMed=16003388; DOI=10.1038/sj.cdd.4401716;
RA Misaghi S., Korbel G.A., Kessler B., Spooner E., Ploegh H.L.;
RT "z-VAD-fmk inhibits peptide:N-glycanase and may result in ER stress.";
RL Cell Death Differ. 13:163-165(2006).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 8-342 IN COMPLEX WITH RAD23 AND
RP SUCROSE, COFACTOR, AND ZINC-BINDING.
RX PubMed=15964983; DOI=10.1073/pnas.0502082102;
RA Lee J.-H., Choi J.M., Lee C., Yi K.J., Cho Y.;
RT "Structure of a peptide:N-glycanase-Rad23 complex: insight into the
RT deglycosylation for denatured glycoproteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:9144-9149(2005).
CC -!- FUNCTION: Specifically deglycosylates the denatured form of N-linked
CC glycoproteins in the cytoplasm and assists their proteasome-mediated
CC degradation. Cleaves the beta-aspartyl-glucosamine (GlcNAc) of the
CC glycan and the amide side chain of Asn, converting Asn to Asp. Prefers
CC proteins containing high-mannose over those bearing complex type
CC oligosaccharides. Can recognize misfolded proteins in the endoplasmic
CC reticulum that are exported to the cytosol to be destroyed and
CC deglycosylate them, while it has no activity toward native proteins.
CC Deglycosylation is a prerequisite for subsequent proteasome-mediated
CC degradation of some, but not all, misfolded glycoproteins. Involved in
CC the formation of free oligosaccharide in cytosol.
CC {ECO:0000269|PubMed:10831608, ECO:0000269|PubMed:12606569,
CC ECO:0000269|PubMed:12723970, ECO:0000269|PubMed:14726951,
CC ECO:0000269|PubMed:15670854, ECO:0000269|PubMed:16401726}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of an N(4)-(acetyl-beta-D-glucosaminyl)asparagine
CC residue in which the glucosamine residue may be further glycosylated,
CC to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a
CC peptide containing an aspartate residue.; EC=3.5.1.52;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:15964983};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:15964983};
CC -!- ACTIVITY REGULATION: Inhibited by Z-VAD-fmk, a well-known caspase
CC inhibitor. Also inhibited by Man9GlcNAc2-iodoacetoamide. Both molecules
CC inhibit enzyme activity through covalent binding of the carbohydrate to
CC the single Cys-191 residue. {ECO:0000269|PubMed:15610852,
CC ECO:0000269|PubMed:16003388, ECO:0000269|PubMed:16740630}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=210 uM for asialofetuin {ECO:0000269|PubMed:11812789};
CC Vmax=140 nmol/min/mg enzyme with asialofetuin as substrate
CC {ECO:0000269|PubMed:11812789};
CC -!- SUBUNIT: Interacts with RAD23 subunit of 26S proteasome.
CC {ECO:0000269|PubMed:11259433, ECO:0000269|PubMed:15351714,
CC ECO:0000269|PubMed:15964983}.
CC -!- INTERACTION:
CC Q02890; P32628: RAD23; NbExp=3; IntAct=EBI-38139, EBI-14668;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- MASS SPECTROMETRY: Mass=43208; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:15610852};
CC -!- MISCELLANEOUS: Present with 4850 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the transglutaminase-like superfamily. PNGase
CC family. {ECO:0000305}.
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DR EMBL; U43281; AAB68203.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11337.1; -; Genomic_DNA.
DR PIR; S61970; S61970.
DR RefSeq; NP_015229.1; NM_001183910.1.
DR PDB; 1X3W; X-ray; 3.00 A; A=8-342.
DR PDB; 1X3Z; X-ray; 2.80 A; A=8-342.
DR PDB; 3ESW; X-ray; 3.40 A; A=8-341.
DR PDBsum; 1X3W; -.
DR PDBsum; 1X3Z; -.
DR PDBsum; 3ESW; -.
DR AlphaFoldDB; Q02890; -.
DR SMR; Q02890; -.
DR BioGRID; 36085; 67.
DR ComplexPortal; CPX-1320; Peptide:N-glycanase-Rad23 complex.
DR DIP; DIP-4008N; -.
DR IntAct; Q02890; 3.
DR MINT; Q02890; -.
DR STRING; 4932.YPL096W; -.
DR iPTMnet; Q02890; -.
DR MaxQB; Q02890; -.
DR PaxDb; Q02890; -.
DR PRIDE; Q02890; -.
DR EnsemblFungi; YPL096W_mRNA; YPL096W; YPL096W.
DR GeneID; 856009; -.
DR KEGG; sce:YPL096W; -.
DR SGD; S000006017; PNG1.
DR VEuPathDB; FungiDB:YPL096W; -.
DR eggNOG; KOG0909; Eukaryota.
DR GeneTree; ENSGT00390000006540; -.
DR HOGENOM; CLU_031058_0_1_1; -.
DR InParanoid; Q02890; -.
DR OMA; WIHVDAC; -.
DR BioCyc; MetaCyc:YPL096W-MON; -.
DR BioCyc; YEAST:YPL096W-MON; -.
DR BRENDA; 3.5.1.52; 984.
DR SABIO-RK; Q02890; -.
DR EvolutionaryTrace; Q02890; -.
DR PRO; PR:Q02890; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q02890; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0120125; C:PNGase complex; IPI:ComplexPortal.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000224; F:peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase activity; IDA:SGD.
DR GO; GO:0006516; P:glycoprotein catabolic process; IBA:GO_Central.
DR GO; GO:0006517; P:protein deglycosylation; IDA:SGD.
DR GO; GO:0035977; P:protein deglycosylation involved in glycoprotein catabolic process; IDA:ComplexPortal.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IMP:SGD.
DR GO; GO:0097466; P:ubiquitin-dependent glycoprotein ERAD pathway; IDA:ComplexPortal.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR018325; Rad4/PNGase_transGLS-fold.
DR InterPro; IPR002931; Transglutaminase-like.
DR Pfam; PF03835; Rad4; 1.
DR SMART; SM00460; TGc; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Hydrolase; Metal-binding; Nucleus;
KW Reference proteome; Zinc.
FT CHAIN 1..363
FT /note="Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine
FT amidase"
FT /id="PRO_0000248996"
FT REGION 325..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 191
FT /note="Nucleophile"
FT ACT_SITE 218
FT ACT_SITE 235
FT BINDING 129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 165
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 238
FT /ligand="substrate"
FT MUTAGEN 123
FT /note="W->A: No effect."
FT /evidence="ECO:0000269|PubMed:11812789"
FT MUTAGEN 129
FT /note="C->A,S: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:11812789"
FT MUTAGEN 132
FT /note="C->A,S: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:11812789"
FT MUTAGEN 165
FT /note="C->A,S: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:11812789"
FT MUTAGEN 168
FT /note="C->A,S: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:11812789"
FT MUTAGEN 174
FT /note="F->A: No effect."
FT /evidence="ECO:0000269|PubMed:11812789"
FT MUTAGEN 177
FT /note="Y->A: No effect."
FT /evidence="ECO:0000269|PubMed:11812789"
FT MUTAGEN 187
FT /note="R->A: No effect."
FT /evidence="ECO:0000269|PubMed:11812789"
FT MUTAGEN 189
FT /note="G->A: No effect."
FT /evidence="ECO:0000269|PubMed:11812789"
FT MUTAGEN 191
FT /note="C->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:11812789"
FT MUTAGEN 194
FT /note="W->A: No effect."
FT /evidence="ECO:0000269|PubMed:11812789"
FT MUTAGEN 198
FT /note="F->A: No effect."
FT /evidence="ECO:0000269|PubMed:11812789"
FT MUTAGEN 199
FT /note="T->A: No effect."
FT /evidence="ECO:0000269|PubMed:11812789"
FT MUTAGEN 203
FT /note="K->A: No effect."
FT /evidence="ECO:0000269|PubMed:11812789"
FT MUTAGEN 206
FT /note="G->A: No effect."
FT /evidence="ECO:0000269|PubMed:11812789"
FT MUTAGEN 210
FT /note="R->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:11812789"
FT MUTAGEN 212
FT /note="V->A: No effect."
FT /evidence="ECO:0000269|PubMed:11812789"
FT MUTAGEN 218
FT /note="H->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:10831608,
FT ECO:0000269|PubMed:11812789"
FT MUTAGEN 218
FT /note="H->Y: In png1-1; abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:10831608,
FT ECO:0000269|PubMed:11812789"
FT MUTAGEN 220
FT /note="W->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:11812789"
FT MUTAGEN 220
FT /note="W->F: No effect."
FT /evidence="ECO:0000269|PubMed:11812789"
FT MUTAGEN 222
FT /note="E->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:11812789"
FT MUTAGEN 224
FT /note="F->A: No effect."
FT /evidence="ECO:0000269|PubMed:11812789"
FT MUTAGEN 230
FT /note="R->A: No effect."
FT /evidence="ECO:0000269|PubMed:11812789"
FT MUTAGEN 231
FT /note="W->A: Abolishes enzyme activity."
FT MUTAGEN 231
FT /note="W->F: No effect."
FT MUTAGEN 234
FT /note="V->A: No effect."
FT /evidence="ECO:0000269|PubMed:11812789"
FT MUTAGEN 235
FT /note="D->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:11812789"
FT MUTAGEN 242
FT /note="D->A: No effect."
FT /evidence="ECO:0000269|PubMed:11812789"
FT MUTAGEN 251
FT /note="W->A: No effect."
FT /evidence="ECO:0000269|PubMed:11812789"
FT MUTAGEN 253
FT /note="K->A: No effect."
FT /evidence="ECO:0000269|PubMed:11812789"
FT MUTAGEN 257
FT /note="Y->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:11812789"
FT MUTAGEN 261
FT /note="F->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:11812789"
FT MUTAGEN 264
FT /note="D->A: No effect."
FT /evidence="ECO:0000269|PubMed:11812789"
FT MUTAGEN 266
FT /note="V->A: No effect."
FT /evidence="ECO:0000269|PubMed:11812789"
FT MUTAGEN 268
FT /note="D->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:11812789"
FT MUTAGEN 273
FT /note="Y->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:11812789"
FT MUTAGEN 281
FT /note="R->A: No effect."
FT /evidence="ECO:0000269|PubMed:11812789"
FT MUTAGEN 347
FT /note="R->A: No effect."
FT /evidence="ECO:0000269|PubMed:11812789"
FT MUTAGEN 354
FT /note="W->A: No effect."
FT /evidence="ECO:0000269|PubMed:11812789"
FT MUTAGEN 358
FT /note="R->A: No effect."
FT /evidence="ECO:0000269|PubMed:11812789"
FT HELIX 13..30
FT /evidence="ECO:0007829|PDB:1X3Z"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:1X3W"
FT HELIX 36..48
FT /evidence="ECO:0007829|PDB:1X3Z"
FT HELIX 50..65
FT /evidence="ECO:0007829|PDB:1X3Z"
FT HELIX 69..78
FT /evidence="ECO:0007829|PDB:1X3Z"
FT HELIX 81..94
FT /evidence="ECO:0007829|PDB:1X3Z"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:1X3Z"
FT HELIX 103..118
FT /evidence="ECO:0007829|PDB:1X3Z"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:1X3Z"
FT STRAND 138..146
FT /evidence="ECO:0007829|PDB:1X3Z"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:1X3Z"
FT STRAND 154..165
FT /evidence="ECO:0007829|PDB:1X3Z"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:1X3Z"
FT STRAND 171..177
FT /evidence="ECO:0007829|PDB:1X3Z"
FT HELIX 180..186
FT /evidence="ECO:0007829|PDB:1X3Z"
FT HELIX 191..203
FT /evidence="ECO:0007829|PDB:1X3Z"
FT TURN 204..206
FT /evidence="ECO:0007829|PDB:1X3Z"
FT STRAND 209..214
FT /evidence="ECO:0007829|PDB:1X3Z"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:1X3Z"
FT STRAND 218..225
FT /evidence="ECO:0007829|PDB:1X3Z"
FT TURN 226..229
FT /evidence="ECO:0007829|PDB:1X3Z"
FT STRAND 230..235
FT /evidence="ECO:0007829|PDB:1X3Z"
FT TURN 236..239
FT /evidence="ECO:0007829|PDB:1X3Z"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:1X3Z"
FT HELIX 246..250
FT /evidence="ECO:0007829|PDB:1X3Z"
FT STRAND 258..262
FT /evidence="ECO:0007829|PDB:1X3Z"
FT STRAND 265..268
FT /evidence="ECO:0007829|PDB:1X3Z"
FT HELIX 270..273
FT /evidence="ECO:0007829|PDB:1X3Z"
FT STRAND 275..278
FT /evidence="ECO:0007829|PDB:1X3Z"
FT HELIX 286..301
FT /evidence="ECO:0007829|PDB:1X3Z"
FT HELIX 306..324
FT /evidence="ECO:0007829|PDB:1X3Z"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:3ESW"
SQ SEQUENCE 363 AA; 42485 MW; 004F3E3E07C3B954 CRC64;
MGEVYEKNNI DFDSIAKMLL IKYKDFILSK FKKAAPVENI RFQNLVHTNQ FAQGVLGQSQ
HLCTVYDNPS WHSIVLETLD LDLIYKNVDK EFAKDGHAEG ENIYTDYLVK ELLRYFKQDF
FKWCNKPDCN HCGQNTSENM TPLGSQGPNG EESKFNCGTV EIYKCNRCGN ITRFPRYNDP
IKLLETRKGR CGEWCNLFTL ILKSFGLDVR YVWNREDHVW CEYFSNFLNR WVHVDSCEQS
FDQPYIYSIN WNKKMSYCIA FGKDGVVDVS KRYILQNELP RDQIKEEDLK FLCQFITKRL
RYSLNDDEIY QLACRDEQEQ IELIRGKTQE TKSESVSAAS KSSNRGRESG SADWKAQRGE
DGK
