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Protein

Dolichyl-phosphate-mannose--protein mannosyltransferase 6

Gene

PMT6

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Protein O-mannosyltransferase involved in O-glycosylation which is essential for cell wall rigidity. Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins.2 PublicationsBy similarity

Catalytic activityi

Dolichyl D-mannosyl phosphate + protein = dolichyl phosphate + O-D-mannosylprotein.2 PublicationsBy similarity

Pathway: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.Curated
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

GO - Molecular functioni

GO - Biological processi

  • protein O-linked glycosylation Source: SGD
  • protein O-linked mannosylation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BioCyciYEAST:YGR199W-MONOMER.
BRENDAi2.4.1.109. 984.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT39. Glycosyltransferase Family 39.

Names & Taxonomyi

Protein namesi
Recommended name:
Dolichyl-phosphate-mannose--protein mannosyltransferase 6Curated (EC:2.4.1.1092 PublicationsBy similarity)
Gene namesi
Name:PMT6Imported
Ordered Locus Names:YGR199WImported
ORF Names:G77221 Publication
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome VII

Organism-specific databases

CYGDiYGR199w.
EuPathDBiFungiDB:YGR199W.
SGDiS000003431. PMT6.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 5857CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei59 – 7921HelicalSequence AnalysisAdd
BLAST
Topological domaini80 – 16485LumenalSequence AnalysisAdd
BLAST
Transmembranei165 – 18521HelicalSequence AnalysisAdd
BLAST
Topological domaini186 – 1949CytoplasmicSequence Analysis
Transmembranei195 – 21521HelicalSequence AnalysisAdd
BLAST
Topological domaini216 – 25136LumenalSequence AnalysisAdd
BLAST
Transmembranei252 – 27221HelicalSequence AnalysisAdd
BLAST
Topological domaini273 – 29321CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei294 – 31421HelicalSequence AnalysisAdd
BLAST
Topological domaini315 – 618304LumenalSequence AnalysisAdd
BLAST
Transmembranei619 – 63921HelicalSequence AnalysisAdd
BLAST
Topological domaini640 – 65617CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei657 – 67721HelicalSequence AnalysisAdd
BLAST
Topological domaini678 – 6869LumenalSequence Analysis
Transmembranei687 – 70721HelicalSequence AnalysisAdd
BLAST
Topological domaini708 – 7158CytoplasmicSequence Analysis
Transmembranei716 – 73621HelicalSequence AnalysisAdd
BLAST
Topological domaini737 – 75923LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Disruption phenotypei

Affects GAS1 and GGP1 O-mannosylation.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 759758Dolichyl-phosphate-mannose--protein mannosyltransferase 6PRO_0000121496Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Glycosylationi156 – 1561N-linked (GlcNAc...)Sequence Analysis
Glycosylationi404 – 4041N-linked (GlcNAc...)Sequence Analysis
Glycosylationi481 – 4811N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Acetylation, Glycoprotein

Proteomic databases

MaxQBiP42934.
PaxDbiP42934.

Interactioni

Subunit structurei

May form an hetodimer with PMT4.1 Publication

Protein-protein interaction databases

BioGridi33452. 48 interactions.
DIPiDIP-5551N.
IntActiP42934. 1 interaction.
MINTiMINT-561799.
STRINGi4932.YGR199W.

Structurei

3D structure databases

ProteinModelPortaliP42934.
SMRiP42934. Positions 342-525.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini340 – 39455MIR 1PROSITE-ProRule annotationAdd
BLAST
Domaini409 – 46759MIR 2PROSITE-ProRule annotationAdd
BLAST
Domaini482 – 54059MIR 3PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyltransferase 39 family.Curated
Contains 3 MIR domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1928.
GeneTreeiENSGT00740000115531.
HOGENOMiHOG000157526.
InParanoidiP42934.
KOiK00728.
OMAiSEWWEWP.
OrthoDBiEOG7BP89X.

Family and domain databases

InterProiIPR027005. GlyclTrfase_39_like.
IPR003342. Glyco_trans_39.
IPR016093. MIR_motif.
[Graphical view]
PANTHERiPTHR10050. PTHR10050. 1 hit.
PfamiPF02815. MIR. 1 hit.
PF02366. PMT. 1 hit.
[Graphical view]
SMARTiSM00472. MIR. 3 hits.
[Graphical view]
SUPFAMiSSF82109. SSF82109. 1 hit.
PROSITEiPS50919. MIR. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P42934-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKAKGTGFS SIDTEDENLR ERYVNQPKAN ASDIQDEQLD CFEQLEEKHR
60 70 80 90 100
TKKNEEYTAL KILRDVIGPL LLTITSFYLR FQHIDQNNYV VWDEAHFGKF
110 120 130 140 150
GSYYIKHEYY HDVHPPLGKM LIALSEWMAG FDGQFDFSSN NAYPENVNFK
160 170 180 190 200
LMRQFNATFG ALCTPVAFFT AKWMGFNYFT VYLIATMVTL EHSYIVLSKF
210 220 230 240 250
ILLDSMLLFF SMTTFACMIK LYTLRKQQMT KKWSLWMLLT GLSIGCVCSV
260 270 280 290 300
KWVGLFITVV VGLYTCIELF LLYCDKELPR IKYYKHWLIR IINLIVIPFL
310 320 330 340 350
IYLYCFKIHF VLLYKSGTGD STTNTLFQIN LEGTQIEAGP RDVAFGSELT
360 370 380 390 400
IRSHGLSPNL LHSHIQVYPE GSGQRQITGY GFADSNNVWK FEFSRSSGLE
410 420 430 440 450
LDQNGTLNGK IIPITDGVEV RLSHKNTGSN LHSHDVPSHV SRGNYEVSGY
460 470 480 490 500
GSQSVGDEKD DWIVEIVKQM DSPNPVYSNE NSTILHPVST FFRLRHKVLG
510 520 530 540 550
CYLASTGLTY PAWGFKQAEI VCKDSWSRRD KSTWWNVEDH WNHNLETAED
560 570 580 590 600
YVPPKSNFWT DFILTNFAMA SSNNALVPDE DKYDSLSSDA WEWPTLHKGL
610 620 630 640 650
RMCSWAGYIT RYYLMGSPFN TWISTVSLII FPFIILFILY RWRRQTLYLS
660 670 680 690 700
DDQIWQITIQ GIFPFISWMT HYLPFAMMGR VTYVHHYVPA LYFAMLVFGF
710 720 730 740 750
VLDFTLTRVH WMVKYPIYLS LFGGCIYIYN LFAPICQGMH GDKAEYLPLQ

WLSTWDIAP
Length:759
Mass (Da):88,026
Last modified:November 1, 1995 - v1
Checksum:i7A23DCEDD90F01C8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49133 Genomic DNA. Translation: CAA88992.1.
Z72984 Genomic DNA. Translation: CAA97226.1.
BK006941 Genomic DNA. Translation: DAA08292.1.
PIRiS53922.
RefSeqiNP_011715.1. NM_001181328.1.

Genome annotation databases

EnsemblFungiiYGR199W; YGR199W; YGR199W.
GeneIDi853113.
KEGGisce:YGR199W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z49133 Genomic DNA. Translation: CAA88992.1.
Z72984 Genomic DNA. Translation: CAA97226.1.
BK006941 Genomic DNA. Translation: DAA08292.1.
PIRiS53922.
RefSeqiNP_011715.1. NM_001181328.1.

3D structure databases

ProteinModelPortaliP42934.
SMRiP42934. Positions 342-525.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33452. 48 interactions.
DIPiDIP-5551N.
IntActiP42934. 1 interaction.
MINTiMINT-561799.
STRINGi4932.YGR199W.

Protein family/group databases

CAZyiGT39. Glycosyltransferase Family 39.

Proteomic databases

MaxQBiP42934.
PaxDbiP42934.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGR199W; YGR199W; YGR199W.
GeneIDi853113.
KEGGisce:YGR199W.

Organism-specific databases

CYGDiYGR199w.
EuPathDBiFungiDB:YGR199W.
SGDiS000003431. PMT6.

Phylogenomic databases

eggNOGiCOG1928.
GeneTreeiENSGT00740000115531.
HOGENOMiHOG000157526.
InParanoidiP42934.
KOiK00728.
OMAiSEWWEWP.
OrthoDBiEOG7BP89X.

Enzyme and pathway databases

UniPathwayiUPA00378.
BioCyciYEAST:YGR199W-MONOMER.
BRENDAi2.4.1.109. 984.

Miscellaneous databases

NextBioi973133.
PROiP42934.

Family and domain databases

InterProiIPR027005. GlyclTrfase_39_like.
IPR003342. Glyco_trans_39.
IPR016093. MIR_motif.
[Graphical view]
PANTHERiPTHR10050. PTHR10050. 1 hit.
PfamiPF02815. MIR. 1 hit.
PF02366. PMT. 1 hit.
[Graphical view]
SMARTiSM00472. MIR. 3 hits.
[Graphical view]
SUPFAMiSSF82109. SSF82109. 1 hit.
PROSITEiPS50919. MIR. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequencing of a 17.6 kb segment on the right arm of yeast chromosome VII reveals 12 ORFs, including CCT, ADE3 and TR-I genes, homologues of the yeast PMT and EF1G genes, of the human and bacterial electron-transferring flavoproteins (beta-chain) and of the Escherichia coli phosphoserine phosphohydrolase, and five new ORFs."
    Guerreiro P., Barreiros T., Soares H., Cyrne L., Maia e Silva A., Rodrigues-Pousada C.
    Yeast 12:273-280(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Protein-O-glycosylation in yeast: protein-specific mannosyltransferases."
    Gentzsch M., Tanner W.
    Glycobiology 7:481-486(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, SUBUNIT.
  5. "A global topology map of the Saccharomyces cerevisiae membrane proteome."
    Kim H., Melen K., Oesterberg M., von Heijne G.
    Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: ATCC 208353 / W303-1A.
  6. "O-mannosylation is required for degradation of the endoplasmic reticulum-associated degradation substrate Gas1*p via the ubiquitin/proteasome pathway in Saccharomyces cerevisiae."
    Hirayama H., Fujita M., Yoko-o T., Jigami Y.
    J. Biochem. 143:555-567(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  7. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPMT6_YEAST
AccessioniPrimary (citable) accession number: P42934
Secondary accession number(s): D6VUY1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 24, 2015
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.