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   04-NOV-2026, entry version 192.
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%3c273::aid-yea898%3e3.0.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; DOI=10.1038/387s081;
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 di-trans,poly-cis-dolichyl beta-D-mannosyl phosphate + L-
CC         seryl-[protein] = 3-O-(alpha-D-mannosyl)-L-seryl-[protein] + a di-
CC         trans,poly-cis-dolichyl phosphate + H(+); Xref=Rhea:RHEA:17377,
CC         Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:13546, Rhea:RHEA-COMP:19498,
CC         Rhea:RHEA-COMP:19501, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
CC         ChEBI:CHEBI:57683, ChEBI:CHEBI:58211, ChEBI:CHEBI:137321;
CC         EC=2.4.1.109; Evidence={ECO:0000250|UniProtKB:P33775,
CC         ECO:0000303|PubMed:18182384, ECO:0000303|PubMed:9184828};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a di-trans,poly-cis-dolichyl beta-D-mannosyl phosphate + L-
CC         threonyl-[protein] = 3-O-(alpha-D-mannosyl)-L-threonyl-[protein] + a
CC         di-trans,poly-cis-dolichyl phosphate + H(+); Xref=Rhea:RHEA:53396,
CC         Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:13547, Rhea:RHEA-COMP:19498,
CC         Rhea:RHEA-COMP:19501, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:57683, ChEBI:CHEBI:58211, ChEBI:CHEBI:137323;
CC         EC=2.4.1.109; Evidence={ECO:0000250|UniProtKB:P33775,
CC         ECO:0000303|PubMed:18182384, ECO:0000303|PubMed:9184828};
CC   -!- PATHWAY: Protein modification; protein glycosylation. {ECO:0000305}.
CC   -!- SUBUNIT: May form a heterodimer with PMT4.
CC       {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; 96.
DR   DIP; DIP-5551N; -.
DR   FunCoup; P42934; 1130.
DR   IntAct; P42934; 2.
DR   STRING; 4932.YGR199W; -.
DR   CAZy; GT39; Glycosyltransferase Family 39.
DR   GlyCosmos; P42934; 3 sites, No reported glycans.
DR   GlyGen; P42934; 3 sites.
DR   iPTMnet; P42934; -.
DR   PaxDb; 4932-YGR199W; -.
DR   PeptideAtlas; P42934; -.
DR   EnsemblFungi; YGR199W_mRNA; YGR199W; YGR199W.
DR   GeneID; 853113; -.
DR   KEGG; sce:YGR199W; -.
DR   AGR; SGD:S000003431; -.
DR   SGD; S000003431; PMT6.
DR   VEuPathDB; FungiDB:YGR199W; -.
DR   eggNOG; KOG3359; Eukaryota.
DR   HOGENOM; CLU_008438_5_0_1; -.
DR   InParanoid; P42934; -.
DR   OMA; AAFTRYW; -.
DR   OrthoDB; 292747at2759; -.
DR   BioCyc; YEAST:YGR199W-MONOMER; -.
DR   BRENDA; 2.4.1.109; 984.
DR   UniPathway; UPA00378; -.
DR   BioGRID-ORCS; 853113; 1 hit in 10 CRISPR screens.
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; ISS:UniProtKB.
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 glycosylation via mannose; IMP:SGD.
DR   CDD; cd23284; beta-trefoil_MIR_PMT2-like; 1.
DR   FunFam; 2.80.10.50:FF:000080; Dolichyl-phosphate-mannose-protein mannosyltransferase 6; 1.
DR   Gene3D; 2.80.10.50; -; 1.
DR   InterPro; IPR003342; ArnT-like_N.
DR   InterPro; IPR036300; MIR_dom_sf.
DR   InterPro; IPR016093; MIR_motif.
DR   InterPro; IPR027005; PMT-like.
DR   InterPro; IPR032421; PMT_4TMC.
DR   PANTHER; PTHR10050; DOLICHYL-PHOSPHATE-MANNOSE--PROTEIN MANNOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR10050:SF52; DOLICHYL-PHOSPHATE-MANNOSE--PROTEIN MANNOSYLTRANSFERASE 6; 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   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
//