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 27-MAR-2024, entry version 210. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 EMDB; EMD-20236; -. DR EMDB; EMD-20240; -. DR SMR; P31382; -. DR BioGRID; 31743; 280. 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 GlyCosmos; P31382; 3 sites, No reported glycans. DR GlyGen; P31382; 3 sites. DR iPTMnet; P31382; -. DR MaxQB; P31382; -. DR PaxDb; 4932-YAL023C; -. DR PeptideAtlas; P31382; -. DR EnsemblFungi; YAL023C_mRNA; YAL023C; YAL023C. DR GeneID; 851210; -. DR KEGG; sce:YAL023C; -. DR AGR; SGD:S000000021; -. 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; MCGWDDN; -. DR OrthoDB; 5489060at2759; -. DR BioCyc; MetaCyc:YAL023C-MONOMER; -. DR BioCyc; YEAST:YAL023C-MONOMER; -. DR UniPathway; UPA00378; -. DR BioGRID-ORCS; 851210; 0 hits in 10 CRISPR screens. 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; ISS:ComplexPortal. 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 Gene3D; 2.80.10.50; -; 1. 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; DOLICHYL-PHOSPHATE-MANNOSE--PROTEIN MANNOSYLTRANSFERASE; 1. DR PANTHER; PTHR10050:SF46; PROTEIN O-MANNOSYL-TRANSFERASE 2; 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; MIR domain; 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 //