PMT6_YEAST
ID PMT6_YEAST Reviewed; 759 AA.
AC P42934; D6VUY1;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Dolichyl-phosphate-mannose--protein mannosyltransferase 6 {ECO:0000305};
DE EC=2.4.1.109 {ECO:0000250|UniProtKB:P33775, ECO:0000303|PubMed:18182384, ECO:0000303|PubMed:9184828};
GN Name=PMT6 {ECO:0000312|SGD:S000003431};
GN OrderedLocusNames=YGR199W {ECO:0000312|SGD:S000003431};
GN ORFNames=G7722 {ECO:0000303|PubMed:8904340};
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 204508 / S288c;
RX PubMed=8904340;
RX DOI=10.1002/(sici)1097-0061(19960315)12:3<273::aid-yea898>3.0.co;2-1;
RA Guerreiro P., Barreiros T., Soares H., Cyrne L., Maia e Silva A.,
RA Rodrigues-Pousada C.;
RT "Sequencing of a 17.6 kb segment on the right arm of yeast chromosome VII
RT reveals 12 ORFs, including CCT, ADE3 and TR-I genes, homologues of the
RT yeast PMT and EF1G genes, of the human and bacterial electron-transferring
RT flavoproteins (beta-chain) and of the Escherichia coli phosphoserine
RT phosphohydrolase, and five new ORFs.";
RL Yeast 12:273-280(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(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 DISRUPTION PHENOTYPE, AND SUBUNIT.
RX PubMed=9184828; DOI=10.1093/glycob/7.4.481;
RA Gentzsch M., Tanner W.;
RT "Protein-O-glycosylation in yeast: protein-specific mannosyltransferases.";
RL Glycobiology 7:481-486(1997).
RN [5]
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 [6]
RP DISRUPTION PHENOTYPE.
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 [7]
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. Transfers mannose from Dol-
CC P-mannose to Ser or Thr residues on proteins.
CC {ECO:0000250|UniProtKB:P33775, ECO:0000303|PubMed:18182384,
CC ECO:0000303|PubMed:9184828}.
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:0000250|UniProtKB:P33775, ECO:0000303|PubMed:18182384,
CC ECO:0000303|PubMed:9184828};
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:0000250|UniProtKB:P33775, ECO:0000303|PubMed:18182384,
CC ECO:0000303|PubMed:9184828};
CC -!- PATHWAY: Protein modification; protein glycosylation. {ECO:0000305}.
CC -!- SUBUNIT: May form a hetodimer with PMT4. {ECO:0000303|PubMed:9184828}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P33775}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Affects GAS1 and GGP1 O-mannosylation.
CC {ECO:0000269|PubMed:18182384, ECO:0000269|PubMed:9184828}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 39 family.
CC {ECO:0000305}.
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DR EMBL; Z49133; CAA88992.1; -; Genomic_DNA.
DR EMBL; Z72984; CAA97226.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08292.1; -; Genomic_DNA.
DR PIR; S53922; S53922.
DR RefSeq; NP_011715.1; NM_001181328.1.
DR AlphaFoldDB; P42934; -.
DR SMR; P42934; -.
DR BioGRID; 33452; 90.
DR DIP; DIP-5551N; -.
DR IntAct; P42934; 1.
DR MINT; P42934; -.
DR STRING; 4932.YGR199W; -.
DR CAZy; GT39; Glycosyltransferase Family 39.
DR iPTMnet; P42934; -.
DR MaxQB; P42934; -.
DR PaxDb; P42934; -.
DR PRIDE; P42934; -.
DR EnsemblFungi; YGR199W_mRNA; YGR199W; YGR199W.
DR GeneID; 853113; -.
DR KEGG; sce:YGR199W; -.
DR SGD; S000003431; PMT6.
DR VEuPathDB; FungiDB:YGR199W; -.
DR eggNOG; KOG3359; Eukaryota.
DR HOGENOM; CLU_008438_5_0_1; -.
DR InParanoid; P42934; -.
DR OMA; GSPFNTW; -.
DR BioCyc; YEAST:YGR199W-MON; -.
DR BRENDA; 2.4.1.109; 984.
DR UniPathway; UPA00378; -.
DR PRO; PR:P42934; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P42934; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004169; F:dolichyl-phosphate-mannose-protein mannosyltransferase activity; ISA:SGD.
DR GO; GO:0006493; P:protein O-linked glycosylation; IMP:SGD.
DR GO; GO:0035269; P:protein O-linked mannosylation; 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 Acetylation; Endoplasmic reticulum; Glycoprotein; Glycosyltransferase;
KW Membrane; Reference proteome; Repeat; Transferase; Transmembrane;
KW 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 6"
FT /id="PRO_0000121496"
FT TOPO_DOM 2..58
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 80..164
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 186..194
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 216..251
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 273..293
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..314
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 315..618
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 619..639
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 640..656
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 657..677
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 678..686
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 687..707
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 708..715
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 716..736
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 737..759
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 340..394
FT /note="MIR 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 409..467
FT /note="MIR 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT DOMAIN 482..540
FT /note="MIR 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00131"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 404
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 481
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 759 AA; 88026 MW; 7A23DCEDD90F01C8 CRC64;
MSKAKGTGFS SIDTEDENLR ERYVNQPKAN ASDIQDEQLD CFEQLEEKHR TKKNEEYTAL
KILRDVIGPL LLTITSFYLR FQHIDQNNYV VWDEAHFGKF GSYYIKHEYY HDVHPPLGKM
LIALSEWMAG FDGQFDFSSN NAYPENVNFK LMRQFNATFG ALCTPVAFFT AKWMGFNYFT
VYLIATMVTL EHSYIVLSKF ILLDSMLLFF SMTTFACMIK LYTLRKQQMT KKWSLWMLLT
GLSIGCVCSV KWVGLFITVV VGLYTCIELF LLYCDKELPR IKYYKHWLIR IINLIVIPFL
IYLYCFKIHF VLLYKSGTGD STTNTLFQIN LEGTQIEAGP RDVAFGSELT IRSHGLSPNL
LHSHIQVYPE GSGQRQITGY GFADSNNVWK FEFSRSSGLE LDQNGTLNGK IIPITDGVEV
RLSHKNTGSN LHSHDVPSHV SRGNYEVSGY GSQSVGDEKD DWIVEIVKQM DSPNPVYSNE
NSTILHPVST FFRLRHKVLG CYLASTGLTY PAWGFKQAEI VCKDSWSRRD KSTWWNVEDH
WNHNLETAED YVPPKSNFWT DFILTNFAMA SSNNALVPDE DKYDSLSSDA WEWPTLHKGL
RMCSWAGYIT RYYLMGSPFN TWISTVSLII FPFIILFILY RWRRQTLYLS DDQIWQITIQ
GIFPFISWMT HYLPFAMMGR VTYVHHYVPA LYFAMLVFGF VLDFTLTRVH WMVKYPIYLS
LFGGCIYIYN LFAPICQGMH GDKAEYLPLQ WLSTWDIAP
