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P42934 (PMT6_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dolichyl-phosphate-mannose--protein mannosyltransferase 6
EC=2.4.1.109
Gene names
Name:PMT6
Ordered Locus Names:YGR199W
ORF Names:G7722
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length759 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins By similarity.

Catalytic activity

Dolichyl phosphate D-mannose + protein = dolichyl phosphate + O-D-mannosylprotein.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.

Sequence similarities

Belongs to the glycosyltransferase 39 family.

Contains 3 MIR domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 759759Dolichyl-phosphate-mannose--protein mannosyltransferase 6
PRO_0000121496

Regions

Topological domain1 – 5858Cytoplasmic Potential
Transmembrane59 – 7921Helical; Potential
Topological domain80 – 16485Lumenal Potential
Transmembrane165 – 18521Helical; Potential
Topological domain186 – 1949Cytoplasmic Potential
Transmembrane195 – 21521Helical; Potential
Topological domain216 – 25136Lumenal Potential
Transmembrane252 – 27221Helical; Potential
Topological domain273 – 29321Cytoplasmic Potential
Transmembrane294 – 31421Helical; Potential
Topological domain315 – 618304Lumenal Potential
Transmembrane619 – 63921Helical; Potential
Topological domain640 – 65617Cytoplasmic Potential
Transmembrane657 – 67721Helical; Potential
Topological domain678 – 6869Lumenal Potential
Transmembrane687 – 70721Helical; Potential
Topological domain708 – 7158Cytoplasmic Potential
Transmembrane716 – 73621Helical; Potential
Topological domain737 – 75923Lumenal Potential
Domain340 – 39455MIR 1
Domain409 – 46759MIR 2
Domain482 – 54059MIR 3

Amino acid modifications

Modified residue141Phosphothreonine Ref.5
Glycosylation1561N-linked (GlcNAc...) Potential
Glycosylation4041N-linked (GlcNAc...) Potential
Glycosylation4811N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
P42934 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 7A23DCEDD90F01C8

FASTA75988,026
        10         20         30         40         50         60 
MSKAKGTGFS SIDTEDENLR ERYVNQPKAN ASDIQDEQLD CFEQLEEKHR TKKNEEYTAL 

        70         80         90        100        110        120 
KILRDVIGPL LLTITSFYLR FQHIDQNNYV VWDEAHFGKF GSYYIKHEYY HDVHPPLGKM 

       130        140        150        160        170        180 
LIALSEWMAG FDGQFDFSSN NAYPENVNFK LMRQFNATFG ALCTPVAFFT AKWMGFNYFT 

       190        200        210        220        230        240 
VYLIATMVTL EHSYIVLSKF ILLDSMLLFF SMTTFACMIK LYTLRKQQMT KKWSLWMLLT 

       250        260        270        280        290        300 
GLSIGCVCSV KWVGLFITVV VGLYTCIELF LLYCDKELPR IKYYKHWLIR IINLIVIPFL 

       310        320        330        340        350        360 
IYLYCFKIHF VLLYKSGTGD STTNTLFQIN LEGTQIEAGP RDVAFGSELT IRSHGLSPNL 

       370        380        390        400        410        420 
LHSHIQVYPE GSGQRQITGY GFADSNNVWK FEFSRSSGLE LDQNGTLNGK IIPITDGVEV 

       430        440        450        460        470        480 
RLSHKNTGSN LHSHDVPSHV SRGNYEVSGY GSQSVGDEKD DWIVEIVKQM DSPNPVYSNE 

       490        500        510        520        530        540 
NSTILHPVST FFRLRHKVLG CYLASTGLTY PAWGFKQAEI VCKDSWSRRD KSTWWNVEDH 

       550        560        570        580        590        600 
WNHNLETAED YVPPKSNFWT DFILTNFAMA SSNNALVPDE DKYDSLSSDA WEWPTLHKGL 

       610        620        630        640        650        660 
RMCSWAGYIT RYYLMGSPFN TWISTVSLII FPFIILFILY RWRRQTLYLS DDQIWQITIQ 

       670        680        690        700        710        720 
GIFPFISWMT HYLPFAMMGR VTYVHHYVPA LYFAMLVFGF VLDFTLTRVH WMVKYPIYLS 

       730        740        750 
LFGGCIYIYN LFAPICQGMH GDKAEYLPLQ WLSTWDIAP

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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 96604 / S288c / FY1679.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"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.
[5]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z49133 Genomic DNA. Translation: CAA88992.1.
Z72984 Genomic DNA. Translation: CAA97226.1.
BK006941 Genomic DNA. Translation: DAA08292.1.
PIRS53922.
RefSeqNP_011715.1. NM_001181328.1.

3D structure databases

ProteinModelPortalP42934.
SMRP42934. Positions 342-525.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-5551N.
MINTMINT-561799.
STRING4932.YGR199W.

Protein family/group databases

CAZyGT39. Glycosyltransferase Family 39.

Proteomic databases

PaxDbP42934.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYGR199W; YGR199W; YGR199W.
GeneID853113.
KEGGsce:YGR199W.

Organism-specific databases

CYGDYGR199w.
SGDS000003431. PMT6.

Phylogenomic databases

eggNOGCOG1928.
GeneTreeENSGT00700000104570.
HOGENOMHOG000157526.
KOK00728.
OMACYLATTG.
OrthoDBEOG4G7G6K.

Enzyme and pathway databases

BioCycYEAST:YGR199W-MONOMER.
BRENDA2.4.1.109. 984.

Gene expression databases

GenevestigatorP42934.
GermOnlineYGR199W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR027005. GlyclTrfase_39_like.
IPR003342. Glyco_trans_39.
IPR016093. MIR_motif.
[Graphical view]
PANTHERPTHR10050. PTHR10050. 1 hit.
PfamPF02815. MIR. 1 hit.
PF02366. PMT. 1 hit.
[Graphical view]
SMARTSM00472. MIR. 3 hits.
[Graphical view]
SUPFAMSSF82109. MIR. 1 hit.
PROSITEPS50919. MIR. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio973133.

Entry information

Entry namePMT6_YEAST
AccessionPrimary (citable) accession number: P42934
Secondary accession number(s): D6VUY1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 29, 2013
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome VII

Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents