PMT2_YEAST
ID PMT2_YEAST Reviewed; 759 AA.
AC P31382; D6VPJ5;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Dolichyl-phosphate-mannose--protein mannosyltransferase 2 {ECO:0000305};
DE EC=2.4.1.109 {ECO:0000269|PubMed:8543034};
GN Name=PMT2 {ECO:0000303|PubMed:8543034};
GN Synonyms=FUN25 {ECO:0000303|PubMed:8458570};
GN OrderedLocusNames=YAL023C {ECO:0000312|SGD:S000000021};
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 204511 / S288c / AB972;
RX PubMed=8458570; DOI=10.1139/g93-005;
RA Ouellette B.F.F., Clark M.W., Keng T., Storms R.K., Zhong W.-W., Zeng B.,
RA Fortin N., Delaney S., Barton A.B., Kaback D.B., Bussey H.;
RT "Sequencing of chromosome I from Saccharomyces cerevisiae: analysis of a 32
RT kb region between the LTE1 and SPO7 genes.";
RL Genome 36:32-42(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7731988; DOI=10.1073/pnas.92.9.3809;
RA Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N.,
RA Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J.,
RA Storms R.K.;
RT "The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995).
RN [3]
RP SEQUENCE REVISION TO 137-139.
RA Dolinski K.J., Cherry J.M.;
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP CATALYTIC ACTIVITY, AND INTERACTION WITH PMT1.
RX PubMed=8543034; DOI=10.1016/0014-5793(95)01324-5;
RA Gentzsch M., Immervoll T., Tanner W.;
RT "Protein O-glycosylation in Saccharomyces cerevisiae: the protein O-
RT mannosyltransferases Pmt1p and Pmt2p function as heterodimer.";
RL FEBS Lett. 377:128-130(1995).
RN [6]
RP IDENTIFICATION, AND DISRUPTION PHENOTYPE.
RX PubMed=7852348; DOI=10.1074/jbc.270.6.2770;
RA Lussier M., Gentzsch M., Sdicu A.-M., Bussey H., Tanner W.;
RT "Protein O-glycosylation in yeast. The PMT2 gene specifies a second protein
RT O-mannosyltransferase that functions in addition to the PMT1-encoded
RT activity.";
RL J. Biol. Chem. 270:2770-2775(1995).
RN [7]
RP DISRUPTION PHENOTYPE.
RX PubMed=8918452; DOI=10.1002/j.1460-2075.1996.tb00961.x;
RA Gaentzsch M., Tanner W.;
RT "The PMT gene family: protein O-glycosylation in Saccharomyces cerevisiae
RT is vital.";
RL EMBO J. 15:5752-5759(1996).
RN [8]
RP INTERACTION WITH PMT1 AND PMT5.
RX PubMed=12551906; DOI=10.1074/jbc.m212582200;
RA Girrbach V., Strahl S.;
RT "Members of the evolutionarily conserved PMT family of protein O-
RT mannosyltransferases form distinct protein complexes among themselves.";
RL J. Biol. Chem. 278:12554-12562(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.
RX PubMed=15377669; DOI=10.1074/jbc.m403234200;
RA Nakatsukasa K., Okada S., Umebayashi K., Fukuda R., Nishikawa S., Endo T.;
RT "Roles of O-mannosylation of aberrant proteins in reduction of the load for
RT endoplasmic reticulum chaperones in yeast.";
RL J. Biol. Chem. 279:49762-49772(2004).
RN [11]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [13]
RP FUNCTION.
RX PubMed=18182384; DOI=10.1093/jb/mvm249;
RA Hirayama H., Fujita M., Yoko-o T., Jigami Y.;
RT "O-mannosylation is required for degradation of the endoplasmic reticulum-
RT associated degradation substrate Gas1*p via the ubiquitin/proteasome
RT pathway in Saccharomyces cerevisiae.";
RL J. Biochem. 143:555-567(2008).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-38 AND SER-39, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [16]
RP FUNCTION OF THE PMT1-PMT2 COMPLEX, AND INTERACTION WITH PMT2; EMP24; ERV25;
RP ERP1; ERP2; CDC48; HRD1; USA1; YOS9; ERO1; PDI1; UBR1; CUE4; DFM1 AND TED1.
RX PubMed=21147851; DOI=10.1242/jcs.072181;
RA Goder V., Melero A.;
RT "Protein O-mannosyltransferases participate in ER protein quality
RT control.";
RL J. Cell Sci. 124:144-153(2011).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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).
CC -!- FUNCTION: Protein O-mannosyltransferase involved in O-glycosylation
CC which is essential for cell wall rigidity. Forms a heterodimeric
CC complex with PMT2 and more rarely with PMT5 to transfer mannose from
CC Dol-P-mannose to Ser or Thr residues on proteins. The PMT1-PMT2 complex
CC participates in oxidative protein folding, ER-associated protein
CC degradation (ERAD), as well as ER export. {ECO:0000269|PubMed:15377669,
CC ECO:0000269|PubMed:18182384, ECO:0000269|PubMed:21147851,
CC ECO:0000269|PubMed:8543034}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-
CC O-(alpha-D-mannosyl)-L-seryl-[protein] + a dolichyl phosphate + H(+);
CC Xref=Rhea:RHEA:17377, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527,
CC Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:13546, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29999, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211,
CC ChEBI:CHEBI:137321; EC=2.4.1.109;
CC Evidence={ECO:0000269|PubMed:8543034};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-mannosyl phosphate + L-threonyl-[protein] =
CC 3-O-(alpha-D-mannosyl)-L-threonyl-[protein] + a dolichyl phosphate +
CC H(+); Xref=Rhea:RHEA:53396, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527,
CC Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:13547, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30013, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211,
CC ChEBI:CHEBI:137323; EC=2.4.1.109;
CC Evidence={ECO:0000269|PubMed:8543034};
CC -!- PATHWAY: Protein modification; protein glycosylation. {ECO:0000305}.
CC -!- SUBUNIT: PMT1 and PMT2 form a functional heterodimer. The complex
CC interacts with endoplasmic reticulum proteins EMP24, ERV25, ERP1, ERP2,
CC CDC48, HRD1, USA1, YOS9, ERO1, PDI1, UBR1, Cue4, DFM1 and TED1. Forms
CC also a minor complex with PMT5. {ECO:0000269|PubMed:12551906,
CC ECO:0000269|PubMed:21147851, ECO:0000269|PubMed:8543034}.
CC -!- INTERACTION:
CC P31382; P33775: PMT1; NbExp=6; IntAct=EBI-13573, EBI-13567;
CC P31382; P52867: PMT5; NbExp=2; IntAct=EBI-13573, EBI-13591;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P33775}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Leads to diminished in vitro and in vivo O-
CC mannosylation activity. {ECO:0000269|PubMed:7852348,
CC ECO:0000269|PubMed:8918452}.
CC -!- MISCELLANEOUS: Present with 6510 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 39 family.
CC {ECO:0000305}.
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DR EMBL; L05146; AAC04934.2; -; Genomic_DNA.
DR EMBL; BK006935; DAA06965.1; -; Genomic_DNA.
DR PIR; S36711; S36711.
DR RefSeq; NP_009379.2; NM_001178168.1.
DR PDB; 6P25; EM; 3.20 A; B=1-759.
DR PDB; 6P28; X-ray; 1.35 A; A=337-532.
DR PDB; 6P2R; EM; 3.20 A; B=1-759.
DR PDB; 6ZQP; X-ray; 1.60 A; A=339-533.
DR PDBsum; 6P25; -.
DR PDBsum; 6P28; -.
DR PDBsum; 6P2R; -.
DR PDBsum; 6ZQP; -.
DR AlphaFoldDB; P31382; -.
DR SMR; P31382; -.
DR BioGRID; 31743; 241.
DR ComplexPortal; CPX-3036; PMT1-PMT2 dolichyl-phosphate-mannose-protein mannosyltransferase complex.
DR ComplexPortal; CPX-3038; PMT5-PMT2 dolichyl-phosphate-mannose-protein mannosyltransferase complex.
DR DIP; DIP-6720N; -.
DR IntAct; P31382; 3.
DR MINT; P31382; -.
DR STRING; 4932.YAL023C; -.
DR CAZy; GT39; Glycosyltransferase Family 39.
DR iPTMnet; P31382; -.
DR MaxQB; P31382; -.
DR PaxDb; P31382; -.
DR PRIDE; P31382; -.
DR EnsemblFungi; YAL023C_mRNA; YAL023C; YAL023C.
DR GeneID; 851210; -.
DR KEGG; sce:YAL023C; -.
DR SGD; S000000021; PMT2.
DR VEuPathDB; FungiDB:YAL023C; -.
DR eggNOG; KOG3359; Eukaryota.
DR GeneTree; ENSGT00940000156829; -.
DR HOGENOM; CLU_008438_5_0_1; -.
DR InParanoid; P31382; -.
DR OMA; DANDVWR; -.
DR BioCyc; MetaCyc:YAL023C-MON; -.
DR BioCyc; YEAST:YAL023C-MON; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:P31382; -.
DR Proteomes; UP000002311; Chromosome I.
DR RNAct; P31382; protein.
DR GO; GO:0097582; C:dolichyl-phosphate-mannose-protein mannosyltransferase Pmt1p-Pmt2p dimer complex; IDA:SGD.
DR GO; GO:0097584; C:dolichyl-phosphate-mannose-protein mannosyltransferase Pmt5p-Pmt2p dimer complex; IDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IC:ComplexPortal.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004169; F:dolichyl-phosphate-mannose-protein mannosyltransferase activity; IDA:SGD.
DR GO; GO:0071712; P:ER-associated misfolded protein catabolic process; IMP:SGD.
DR GO; GO:0009272; P:fungal-type cell wall biogenesis; IDA:ComplexPortal.
DR GO; GO:0032527; P:protein exit from endoplasmic reticulum; IGI:SGD.
DR GO; GO:0006493; P:protein O-linked glycosylation; IMP:SGD.
DR GO; GO:0035269; P:protein O-linked mannosylation; IDA:ComplexPortal.
DR GO; GO:1900101; P:regulation of endoplasmic reticulum unfolded protein response; IMP:SGD.
DR InterPro; IPR027005; GlyclTrfase_39-like.
DR InterPro; IPR003342; Glyco_trans_39/83.
DR InterPro; IPR036300; MIR_dom_sf.
DR InterPro; IPR016093; MIR_motif.
DR InterPro; IPR032421; PMT_4TMC.
DR PANTHER; PTHR10050; PTHR10050; 1.
DR Pfam; PF02815; MIR; 1.
DR Pfam; PF02366; PMT; 1.
DR Pfam; PF16192; PMT_4TMC; 1.
DR SMART; SM00472; MIR; 3.
DR SUPFAM; SSF82109; SSF82109; 1.
DR PROSITE; PS50919; MIR; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Endoplasmic reticulum; Glycoprotein;
KW Glycosyltransferase; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW Transferase; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..759
FT /note="Dolichyl-phosphate-mannose--protein
FT mannosyltransferase 2"
FT /id="PRO_0000121492"
FT TOPO_DOM 2..64
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 86..167
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..198
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 220..251
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 273..289
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 311..609
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 610..630
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 631..647
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 648..668
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 669..676
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 677..697
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 698..710
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 711..731
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 732..759
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 339..394
FT /note="MIR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 407..463
FT /note="MIR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 471..529
FT /note="MIR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 403
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT HELIX 59..79
FT /evidence="ECO:0007829|PDB:6P25"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:6P25"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:6P25"
FT HELIX 93..104
FT /evidence="ECO:0007829|PDB:6P25"
FT HELIX 116..126
FT /evidence="ECO:0007829|PDB:6P25"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:6P25"
FT HELIX 148..172
FT /evidence="ECO:0007829|PDB:6P25"
FT HELIX 178..188
FT /evidence="ECO:0007829|PDB:6P25"
FT HELIX 191..196
FT /evidence="ECO:0007829|PDB:6P25"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:6P25"
FT HELIX 203..221
FT /evidence="ECO:0007829|PDB:6P25"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:6P25"
FT HELIX 230..249
FT /evidence="ECO:0007829|PDB:6P25"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:6P25"
FT HELIX 254..271
FT /evidence="ECO:0007829|PDB:6P25"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:6P25"
FT HELIX 279..293
FT /evidence="ECO:0007829|PDB:6P25"
FT HELIX 295..311
FT /evidence="ECO:0007829|PDB:6P25"
FT HELIX 319..321
FT /evidence="ECO:0007829|PDB:6P25"
FT HELIX 324..329
FT /evidence="ECO:0007829|PDB:6P25"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:6P25"
FT TURN 344..346
FT /evidence="ECO:0007829|PDB:6P28"
FT STRAND 348..353
FT /evidence="ECO:0007829|PDB:6P28"
FT STRAND 360..367
FT /evidence="ECO:0007829|PDB:6P28"
FT STRAND 369..373
FT /evidence="ECO:0007829|PDB:6P25"
FT STRAND 375..382
FT /evidence="ECO:0007829|PDB:6P28"
FT HELIX 385..387
FT /evidence="ECO:0007829|PDB:6P28"
FT STRAND 389..393
FT /evidence="ECO:0007829|PDB:6P28"
FT STRAND 414..420
FT /evidence="ECO:0007829|PDB:6P28"
FT TURN 421..423
FT /evidence="ECO:0007829|PDB:6P28"
FT STRAND 426..433
FT /evidence="ECO:0007829|PDB:6P28"
FT STRAND 435..437
FT /evidence="ECO:0007829|PDB:6P28"
FT STRAND 440..446
FT /evidence="ECO:0007829|PDB:6P28"
FT STRAND 449..451
FT /evidence="ECO:0007829|PDB:6P28"
FT HELIX 454..456
FT /evidence="ECO:0007829|PDB:6P28"
FT STRAND 458..467
FT /evidence="ECO:0007829|PDB:6P28"
FT STRAND 471..473
FT /evidence="ECO:0007829|PDB:6P2R"
FT TURN 476..478
FT /evidence="ECO:0007829|PDB:6P28"
FT STRAND 479..485
FT /evidence="ECO:0007829|PDB:6P28"
FT TURN 486..488
FT /evidence="ECO:0007829|PDB:6P28"
FT STRAND 491..498
FT /evidence="ECO:0007829|PDB:6P28"
FT HELIX 501..503
FT /evidence="ECO:0007829|PDB:6P28"
FT STRAND 507..514
FT /evidence="ECO:0007829|PDB:6P28"
FT HELIX 520..522
FT /evidence="ECO:0007829|PDB:6ZQP"
FT STRAND 524..530
FT /evidence="ECO:0007829|PDB:6P28"
FT HELIX 548..564
FT /evidence="ECO:0007829|PDB:6P25"
FT HELIX 580..582
FT /evidence="ECO:0007829|PDB:6P25"
FT TURN 583..586
FT /evidence="ECO:0007829|PDB:6P25"
FT STRAND 596..599
FT /evidence="ECO:0007829|PDB:6P25"
FT HELIX 610..633
FT /evidence="ECO:0007829|PDB:6P25"
FT HELIX 642..651
FT /evidence="ECO:0007829|PDB:6P25"
FT HELIX 653..668
FT /evidence="ECO:0007829|PDB:6P25"
FT HELIX 675..677
FT /evidence="ECO:0007829|PDB:6P25"
FT HELIX 678..694
FT /evidence="ECO:0007829|PDB:6P25"
FT STRAND 696..698
FT /evidence="ECO:0007829|PDB:6P25"
FT HELIX 699..702
FT /evidence="ECO:0007829|PDB:6P25"
FT HELIX 704..727
FT /evidence="ECO:0007829|PDB:6P25"
FT HELIX 730..733
FT /evidence="ECO:0007829|PDB:6P25"
FT HELIX 741..743
FT /evidence="ECO:0007829|PDB:6P2R"
SQ SEQUENCE 759 AA; 86870 MW; B1E1480C2E04BE3D CRC64;
MSSSSSTGYS KNNAAHIKQE NTLRQRESSS ISVSEELSSA DERDAEDFSK EKPAAQSSLL
RLESVVMPVI FTALALFTRM YKIGINNHVV WDEAHFGKFG SYYLRHEFYH DVHPPLGKML
VGLSGYLAGY NGSWDFPSGE IYPDYLDYVK MRLFNASFSA LCVPLAYFTA KAIGFSLPTV
WLMTVLVLFE NSYSTLGRFI LLDSMLLFFT VASFFSFVMF HNQRSKPFSR KWWKWLLITG
ISLGCTISVK MVGLFIITMV GIYTVIDLWT FLADKSMSWK TYINHWLARI FGLIIVPFCI
FLLCFKIHFD LLSHSGTGDA NMPSLFQARL VGSDVGQGPR DIALGSSVVS IKNQALGGSL
LHSHIQTYPD GSNQQQVTCY GYKDANNEWF FNRERGLPSW SENETDIEYL KPGTSYRLVH
KSTGRNLHTH PVAAPVSKTQ WEVSGYGDNV VGDNKDNWVI EIMDQRGDED PEKLHTLTTS
FRIKNLEMGC YLAQTGNSLP EWGFRQQEVV CMKNPFKRDK RTWWNIETHE NERLPPRPED
FQYPKTNFLK DFIHLNLAMM ATNNALVPDP DKFDYLASSA WQWPTLNVGL RLCGWGDDNP
KYFLLGTPAS TWASSVAVLA FMATVVILLI RWQRQYVDLR NPSNWNVFLM GGFYPLLAWG
LHYMPFVIMS RVTYVHHYLP ALYFALIILA YCFDAGLQKW SRSKCGRIMR FVLYAGFMAL
VIGCFWYFSP ISFGMEGPSS NFRYLNWFST WDIADKQEA
