PMT1_YEAST
ID PMT1_YEAST Reviewed; 817 AA.
AC P33775; D6VRQ4;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Dolichyl-phosphate-mannose--protein mannosyltransferase 1 {ECO:0000305};
DE EC=2.4.1.109 {ECO:0000269|PubMed:10764776, ECO:0000269|PubMed:8367478};
GN Name=PMT1 {ECO:0000303|PubMed:8367478};
GN OrderedLocusNames=YDL095W {ECO:0000312|SGD:S000002253};
GN ORFNames=D2390 {ECO:0000312|SGD:S000002253};
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], PARTIAL PROTEIN SEQUENCE,
RP IDENTIFICATION, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=8367478; DOI=10.1073/pnas.90.17.8164;
RA Strahl-Bolsinger S., Immervoll T., Deutzmann R., Tanner W.;
RT "PMT1, the gene for a key enzyme of protein O-glycosylation in
RT Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:8164-8168(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8923743;
RX DOI=10.1002/(sici)1097-0061(199610)12:13%3c1377::aid-yea35%3e3.0.co;2-r;
RA Boskovic J., Soler-Mira A., Garcia-Cantalejo J.M., Ballesta J.P.G.,
RA Jimenez A., Remacha M.A.;
RT "The sequence of a 16,691 bp segment of Saccharomyces cerevisiae chromosome
RT IV identifies the DUN1, PMT1, PMT5, SRP14 and DPR1 genes, and five new open
RT reading frames.";
RL Yeast 12:1377-1384(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
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 FUNCTION, AND INTERACTION WITH PMT2.
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 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 [7]
RP FUNCTION.
RX PubMed=9466258; DOI=10.1046/j.1365-2958.1998.00660.x;
RA Bourdineaud J.P., van der Vaart J.M., Donzeau M., de Sampaio G.,
RA Verrips C.T., Lauquin G.J.;
RT "Pmt1 mannosyl transferase is involved in cell wall incorporation of
RT several proteins in Saccharomyces cerevisiae.";
RL Mol. Microbiol. 27:85-98(1998).
RN [8]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=10085156; DOI=10.1074/jbc.274.13.9068;
RA Strahl-Bolsinger S., Scheinost A.;
RT "Transmembrane topology of pmt1p, a member of an evolutionarily conserved
RT family of protein O-mannosyltransferases.";
RL J. Biol. Chem. 274:9068-9075(1999).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, DOMAIN, AND MUTAGENESIS OF ARG-64; GLU-78;
RP ARG-138 AND LEU-408.
RX PubMed=10764776; DOI=10.1074/jbc.m001771200;
RA Girrbach V., Zeller T., Priesmeier M., Strahl-Bolsinger S.;
RT "Structure-function analysis of the dolichyl phosphate-mannose: protein O-
RT mannosyltransferase ScPmt1p.";
RL J. Biol. Chem. 275:19288-19296(2000).
RN [10]
RP INTERACTION WITH PMT2 AND PMT3.
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 [11]
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 [12]
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 [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 FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF 77-ASP-GLU-78; GLU-78;
RP TYR-88 AND PRO-100.
RX PubMed=21956107; DOI=10.1074/jbc.m111.281196;
RA Lommel M., Schott A., Jank T., Hofmann V., Strahl S.;
RT "A conserved acidic motif is crucial for enzymatic activity of protein O-
RT mannosyltransferases.";
RL J. Biol. Chem. 286:39768-39775(2011).
RN [15]
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 [16]
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 PMT3 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. Required for incorporation of
CC proteins in the cell wall. {ECO:0000269|PubMed:10764776,
CC ECO:0000269|PubMed:18182384, ECO:0000269|PubMed:8367478,
CC ECO:0000269|PubMed:8543034, ECO:0000269|PubMed:9466258}.
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:10764776, ECO:0000269|PubMed:8367478};
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:10764776, ECO:0000269|PubMed:8367478};
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 PMT3. {ECO:0000269|PubMed:12551906,
CC ECO:0000269|PubMed:21147851, ECO:0000269|PubMed:8543034}.
CC -!- INTERACTION:
CC P33775; P31382: PMT2; NbExp=6; IntAct=EBI-13567, EBI-13573;
CC P33775; P47190: PMT3; NbExp=3; IntAct=EBI-13567, EBI-13579;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000303|PubMed:10085156}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:10085156}.
CC -!- DOMAIN: The large luminal loop 5 is essential for mannosyltransferase
CC activity but not for PMT1-PMT2 complex formation.
CC {ECO:0000269|PubMed:10764776}.
CC -!- DISRUPTION PHENOTYPE: Affects glycosylation of chitinase and increases
CC sensitivity to calcofluor white and caffeine.
CC {ECO:0000269|PubMed:8918452}.
CC -!- MISCELLANEOUS: Present with 41500 molecules/cell in log phase SD
CC medium. {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; L19169; AAA02928.1; -; Unassigned_DNA.
DR EMBL; X95644; CAA64917.1; -; Genomic_DNA.
DR EMBL; Z74144; CAA98663.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11764.1; -; Genomic_DNA.
DR PIR; A47716; A47716.
DR RefSeq; NP_010188.1; NM_001180154.1.
DR PDB; 6P25; EM; 3.20 A; A=1-817.
DR PDB; 6P2R; EM; 3.20 A; A=1-817.
DR PDBsum; 6P25; -.
DR PDBsum; 6P2R; -.
DR AlphaFoldDB; P33775; -.
DR SMR; P33775; -.
DR BioGRID; 31966; 216.
DR ComplexPortal; CPX-3036; PMT1-PMT2 dolichyl-phosphate-mannose-protein mannosyltransferase complex.
DR ComplexPortal; CPX-3037; PMT1-PMT3 dolichyl-phosphate-mannose-protein mannosyltransferase complex.
DR DIP; DIP-7911N; -.
DR IntAct; P33775; 2.
DR MINT; P33775; -.
DR STRING; 4932.YDL095W; -.
DR CAZy; GT39; Glycosyltransferase Family 39.
DR TCDB; 9.B.142.5.6; the integral membrane glycosyltransferase family 39 (gt39) family.
DR iPTMnet; P33775; -.
DR MaxQB; P33775; -.
DR PaxDb; P33775; -.
DR PRIDE; P33775; -.
DR EnsemblFungi; YDL095W_mRNA; YDL095W; YDL095W.
DR GeneID; 851462; -.
DR KEGG; sce:YDL095W; -.
DR SGD; S000002253; PMT1.
DR VEuPathDB; FungiDB:YDL095W; -.
DR eggNOG; KOG3359; Eukaryota.
DR GeneTree; ENSGT00940000176667; -.
DR HOGENOM; CLU_008438_2_0_1; -.
DR InParanoid; P33775; -.
DR OMA; TLSVKWV; -.
DR BioCyc; MetaCyc:YDL095W-MON; -.
DR BioCyc; YEAST:YDL095W-MON; -.
DR BRENDA; 2.4.1.109; 984.
DR UniPathway; UPA00378; -.
DR PRO; PR:P33775; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P33775; protein.
DR GO; GO:0097582; C:dolichyl-phosphate-mannose-protein mannosyltransferase Pmt1p-Pmt2p dimer complex; IDA:SGD.
DR GO; GO:0097583; C:dolichyl-phosphate-mannose-protein mannosyltransferase Pmt1p-Pmt3p 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:0035269; P:protein O-linked mannosylation; IDA:SGD.
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; IPR027004; PMT1/PTM5.
DR InterPro; IPR032421; PMT_4TMC.
DR PANTHER; PTHR10050; PTHR10050; 1.
DR PANTHER; PTHR10050:SF50; PTHR10050:SF50; 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; Direct protein sequencing;
KW Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Membrane;
KW Reference proteome; Repeat; Transferase; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..817
FT /note="Dolichyl-phosphate-mannose--protein
FT mannosyltransferase 1"
FT /id="PRO_0000121491"
FT TOPO_DOM 2..50
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:10085156"
FT TRANSMEM 51..70
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:10085156"
FT TOPO_DOM 71..135
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:10085156"
FT TRANSMEM 136..154
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:10085156"
FT TOPO_DOM 155..179
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:10085156"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:10085156"
FT TOPO_DOM 201..234
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:10085156"
FT TRANSMEM 235..259
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:10085156"
FT TOPO_DOM 260..273
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:10085156"
FT TRANSMEM 274..291
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:10085156"
FT TOPO_DOM 292..584
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:10085156"
FT TRANSMEM 585..605
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:10085156"
FT TOPO_DOM 606..685
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:10085156"
FT TRANSMEM 686..710
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:10085156"
FT TOPO_DOM 711..817
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:10085156"
FT DOMAIN 324..378
FT /note="MIR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 388..448
FT /note="MIR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 459..514
FT /note="MIR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CARBOHYD 390
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 513
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 743
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 64
FT /note="R->A: Reduces mannosyltransferase activity."
FT /evidence="ECO:0000269|PubMed:10764776"
FT MUTAGEN 77..78
FT /note="DE->AA: Impairs mannosyltransferase activity."
FT /evidence="ECO:0000269|PubMed:21956107"
FT MUTAGEN 78
FT /note="E->A: Decreases substrate-binding and reduces
FT mannosyltransferase activity."
FT /evidence="ECO:0000269|PubMed:10764776,
FT ECO:0000269|PubMed:21956107"
FT MUTAGEN 88
FT /note="Y->A: Moderately decreases complex formation with
FT PMT2."
FT /evidence="ECO:0000269|PubMed:21956107"
FT MUTAGEN 100
FT /note="P->A: Moderately decreases complex formation with
FT PMT2."
FT /evidence="ECO:0000269|PubMed:21956107"
FT MUTAGEN 138
FT /note="R->A: Impairs complex formation with PMT2."
FT /evidence="ECO:0000269|PubMed:10764776"
FT MUTAGEN 408
FT /note="L->A: Reduces mannosyltransferase activity."
FT /evidence="ECO:0000269|PubMed:10764776"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:6P25"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:6P25"
FT HELIX 36..41
FT /evidence="ECO:0007829|PDB:6P25"
FT HELIX 47..63
FT /evidence="ECO:0007829|PDB:6P25"
FT TURN 64..69
FT /evidence="ECO:0007829|PDB:6P25"
FT HELIX 78..90
FT /evidence="ECO:0007829|PDB:6P25"
FT HELIX 101..112
FT /evidence="ECO:0007829|PDB:6P25"
FT HELIX 135..158
FT /evidence="ECO:0007829|PDB:6P25"
FT HELIX 163..174
FT /evidence="ECO:0007829|PDB:6P25"
FT HELIX 177..184
FT /evidence="ECO:0007829|PDB:6P25"
FT HELIX 189..207
FT /evidence="ECO:0007829|PDB:6P25"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:6P25"
FT HELIX 214..231
FT /evidence="ECO:0007829|PDB:6P25"
FT HELIX 237..257
FT /evidence="ECO:0007829|PDB:6P25"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:6P25"
FT HELIX 263..295
FT /evidence="ECO:0007829|PDB:6P25"
FT TURN 302..305
FT /evidence="ECO:0007829|PDB:6P25"
FT TURN 308..310
FT /evidence="ECO:0007829|PDB:6P25"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:6P25"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:6P25"
FT STRAND 322..326
FT /evidence="ECO:0007829|PDB:6P25"
FT STRAND 332..342
FT /evidence="ECO:0007829|PDB:6P25"
FT STRAND 345..351
FT /evidence="ECO:0007829|PDB:6P25"
FT STRAND 359..363
FT /evidence="ECO:0007829|PDB:6P25"
FT HELIX 369..371
FT /evidence="ECO:0007829|PDB:6P25"
FT STRAND 373..377
FT /evidence="ECO:0007829|PDB:6P25"
FT STRAND 395..401
FT /evidence="ECO:0007829|PDB:6P25"
FT TURN 402..405
FT /evidence="ECO:0007829|PDB:6P25"
FT TURN 433..435
FT /evidence="ECO:0007829|PDB:6P25"
FT HELIX 439..441
FT /evidence="ECO:0007829|PDB:6P25"
FT STRAND 443..447
FT /evidence="ECO:0007829|PDB:6P25"
FT TURN 449..451
FT /evidence="ECO:0007829|PDB:6P25"
FT HELIX 456..459
FT /evidence="ECO:0007829|PDB:6P25"
FT TURN 463..465
FT /evidence="ECO:0007829|PDB:6P25"
FT STRAND 468..472
FT /evidence="ECO:0007829|PDB:6P25"
FT TURN 473..475
FT /evidence="ECO:0007829|PDB:6P25"
FT STRAND 480..486
FT /evidence="ECO:0007829|PDB:6P25"
FT STRAND 488..490
FT /evidence="ECO:0007829|PDB:6P25"
FT STRAND 493..498
FT /evidence="ECO:0007829|PDB:6P25"
FT STRAND 500..502
FT /evidence="ECO:0007829|PDB:6P25"
FT HELIX 505..507
FT /evidence="ECO:0007829|PDB:6P25"
FT STRAND 509..515
FT /evidence="ECO:0007829|PDB:6P25"
FT STRAND 517..519
FT /evidence="ECO:0007829|PDB:6P25"
FT HELIX 533..549
FT /evidence="ECO:0007829|PDB:6P25"
FT HELIX 561..566
FT /evidence="ECO:0007829|PDB:6P25"
FT STRAND 571..576
FT /evidence="ECO:0007829|PDB:6P25"
FT STRAND 579..583
FT /evidence="ECO:0007829|PDB:6P25"
FT HELIX 587..613
FT /evidence="ECO:0007829|PDB:6P25"
FT HELIX 621..639
FT /evidence="ECO:0007829|PDB:6P25"
FT HELIX 642..644
FT /evidence="ECO:0007829|PDB:6P25"
FT HELIX 653..655
FT /evidence="ECO:0007829|PDB:6P25"
FT HELIX 657..676
FT /evidence="ECO:0007829|PDB:6P25"
FT TURN 677..679
FT /evidence="ECO:0007829|PDB:6P25"
FT HELIX 683..703
FT /evidence="ECO:0007829|PDB:6P25"
FT HELIX 705..707
FT /evidence="ECO:0007829|PDB:6P25"
FT HELIX 715..721
FT /evidence="ECO:0007829|PDB:6P25"
FT STRAND 724..726
FT /evidence="ECO:0007829|PDB:6P25"
FT STRAND 733..737
FT /evidence="ECO:0007829|PDB:6P25"
FT HELIX 739..742
FT /evidence="ECO:0007829|PDB:6P25"
SQ SEQUENCE 817 AA; 92675 MW; 6309BBA71BAD8D21 CRC64;
MSEEKTYKRV EQDDPVPELD IKQGPVRPFI VTDPSAELAS LRTMVTLKEK LLVACLAVFT
AVIRLHGLAW PDSVVFDEVH FGGFASQYIR GTYFMDVHPP LAKMLYAGVA SLGGFQGDFD
FENIGDSFPS TTPYVLMRFF SASLGALTVI LMYMTLRYSG VRMWVALMSA ICFAVENSYV
TISRYILLDA PLMFFIAAAV YSFKKYEMYP ANSLNAYKSL LATGIALGMA SSSKWVGLFT
VTWVGLLCIW RLWFMIGDLT KSSKSIFKVA FAKLAFLLGV PFALYLVFFY IHFQSLTLDG
DGASFFSPEF RSTLKNNKIP QNVVADVGIG SIISLRHLST MGGYLHSHSH NYPAGSEQQQ
STLYPHMDAN NDWLLELYNA PGESLTTFQN LTDGTKVRLF HTVTRCRLHS HDHKPPVSES
SDWQKEVSCY GYSGFDGDAN DDWVVEIDKK NSAPGVAQER VIALDTKFRL RHAMTGCYLF
SHEVKLPAWG FEQQEVTCAS SGRHDLTLWY VENNSNPLLP EDTKRISYKP ASFISKFIES
HKKMWHINKN LVEPHVYESQ PTSWPFLLRG ISYWGENNRN VYLLGNAIVW WAVTAFIGIF
GLIVITELFS WQLGKPILKD SKVVNFHVQV IHYLLGFAVH YAPSFLMQRQ MFLHHYLPAY
YFGILALGHA LDIIVSYVFR SKRQMGYAVV ITFLAASVYF FKSFSPIIYG TPWTQELCQK
SQWLSGWDYN CNTYFSSLEE YKNQTLTKRE SQPAATSTVE EITIEGDGPS YEDLMNEDGK
KIFKDTEGNE LDPEVVKKML EEEGANILKV EKRAVLE
