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P33775 (PMT1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dolichyl-phosphate-mannose--protein mannosyltransferase 1

EC=2.4.1.109
Gene names
Name:PMT1
Ordered Locus Names:YDL095W
ORF Names:D2390
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length817 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins. Seems to be active on chitinase.

Catalytic activity

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

Pathway

Protein modification; protein glycosylation.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein.

Miscellaneous

Present with 41500 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the glycosyltransferase 39 family.

Contains 3 MIR domains.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PMT2P313824EBI-13567,EBI-13573
PMT3P471903EBI-13567,EBI-13579

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 817816Dolichyl-phosphate-mannose--protein mannosyltransferase 1
PRO_0000121491

Regions

Topological domain2 – 5049Cytoplasmic Potential
Transmembrane51 – 7121Helical; Potential
Topological domain72 – 13362Lumenal Potential
Transmembrane134 – 15421Helical; Potential
Topological domain155 – 17925Cytoplasmic Potential
Transmembrane180 – 20021Helical; Potential
Topological domain201 – 23434Lumenal Potential
Transmembrane235 – 25925Helical; Potential
Topological domain260 – 27314Cytoplasmic Potential
Transmembrane274 – 29118Helical; Potential
Topological domain292 – 584293Lumenal Potential
Transmembrane585 – 60521Helical; Potential
Topological domain606 – 68580Cytoplasmic Potential
Transmembrane686 – 71025Helical; Potential
Topological domain711 – 817107Lumenal Potential
Domain324 – 37855MIR 1
Domain388 – 44861MIR 2
Domain459 – 51456MIR 3

Amino acid modifications

Modified residue21N-acetylserine Ref.8
Glycosylation3901N-linked (GlcNAc...) Potential
Glycosylation5131N-linked (GlcNAc...) Potential
Glycosylation7431N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
P33775 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: 6309BBA71BAD8D21

FASTA81792,675
        10         20         30         40         50         60 
MSEEKTYKRV EQDDPVPELD IKQGPVRPFI VTDPSAELAS LRTMVTLKEK LLVACLAVFT 

        70         80         90        100        110        120 
AVIRLHGLAW PDSVVFDEVH FGGFASQYIR GTYFMDVHPP LAKMLYAGVA SLGGFQGDFD 

       130        140        150        160        170        180 
FENIGDSFPS TTPYVLMRFF SASLGALTVI LMYMTLRYSG VRMWVALMSA ICFAVENSYV 

       190        200        210        220        230        240 
TISRYILLDA PLMFFIAAAV YSFKKYEMYP ANSLNAYKSL LATGIALGMA SSSKWVGLFT 

       250        260        270        280        290        300 
VTWVGLLCIW RLWFMIGDLT KSSKSIFKVA FAKLAFLLGV PFALYLVFFY IHFQSLTLDG 

       310        320        330        340        350        360 
DGASFFSPEF RSTLKNNKIP QNVVADVGIG SIISLRHLST MGGYLHSHSH NYPAGSEQQQ 

       370        380        390        400        410        420 
STLYPHMDAN NDWLLELYNA PGESLTTFQN LTDGTKVRLF HTVTRCRLHS HDHKPPVSES 

       430        440        450        460        470        480 
SDWQKEVSCY GYSGFDGDAN DDWVVEIDKK NSAPGVAQER VIALDTKFRL RHAMTGCYLF 

       490        500        510        520        530        540 
SHEVKLPAWG FEQQEVTCAS SGRHDLTLWY VENNSNPLLP EDTKRISYKP ASFISKFIES 

       550        560        570        580        590        600 
HKKMWHINKN LVEPHVYESQ PTSWPFLLRG ISYWGENNRN VYLLGNAIVW WAVTAFIGIF 

       610        620        630        640        650        660 
GLIVITELFS WQLGKPILKD SKVVNFHVQV IHYLLGFAVH YAPSFLMQRQ MFLHHYLPAY 

       670        680        690        700        710        720 
YFGILALGHA LDIIVSYVFR SKRQMGYAVV ITFLAASVYF FKSFSPIIYG TPWTQELCQK 

       730        740        750        760        770        780 
SQWLSGWDYN CNTYFSSLEE YKNQTLTKRE SQPAATSTVE EITIEGDGPS YEDLMNEDGK 

       790        800        810 
KIFKDTEGNE LDPEVVKKML EEEGANILKV EKRAVLE 

« Hide

References

« Hide 'large scale' references
[1]"PMT1, the gene for a key enzyme of protein O-glycosylation in Saccharomyces cerevisiae."
Strahl-Bolsinger S., Immervoll T., Deutzmann R., Tanner W.
Proc. Natl. Acad. Sci. U.S.A. 90:8164-8168(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE, PARTIAL PROTEIN SEQUENCE.
[2]"The sequence of a 16,691 bp segment of Saccharomyces cerevisiae chromosome IV identifies the DUN1, PMT1, PMT5, SRP14 and DPR1 genes, and five new open reading frames."
Boskovic J., Soler-Mira A., Garcia-Cantalejo J.M., Ballesta J.P.G., Jimenez A., Remacha M.A.
Yeast 12:1377-1384(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. expand/collapse author list , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"The PMT gene family: protein O-glycosylation in Saccharomyces cerevisiae is vital."
Gaentzsch M., Tanner W.
EMBO J. 15:5752-5759(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[6]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]"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.
[8]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L19169 Unassigned DNA. Translation: AAA02928.1.
X95644 Genomic DNA. Translation: CAA64917.1.
Z74144 Genomic DNA. Translation: CAA98663.1.
BK006938 Genomic DNA. Translation: DAA11764.1.
PIRA47716.
RefSeqNP_010188.1. NM_001180154.1.

3D structure databases

ProteinModelPortalP33775.
SMRP33775. Positions 390-515.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31966. 153 interactions.
DIPDIP-7911N.
IntActP33775. 2 interactions.
MINTMINT-2787975.
STRING4932.YDL095W.

Protein family/group databases

CAZyGT39. Glycosyltransferase Family 39.

Proteomic databases

MaxQBP33775.
PaxDbP33775.
PeptideAtlasP33775.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDL095W; YDL095W; YDL095W.
GeneID851462.
KEGGsce:YDL095W.

Organism-specific databases

CYGDYDL095w.
SGDS000002253. PMT1.

Phylogenomic databases

eggNOGCOG1928.
GeneTreeENSGT00740000116239.
HOGENOMHOG000157526.
KOK00728.
OMAMSSEFQA.
OrthoDBEOG7BP89X.

Enzyme and pathway databases

BioCycYEAST:YDL095W-MONOMER.
BRENDA2.4.1.109. 984.
UniPathwayUPA00378.

Gene expression databases

GenevestigatorP33775.

Family and domain databases

InterProIPR027005. GlyclTrfase_39_like.
IPR003342. Glyco_trans_39.
IPR016093. MIR_motif.
IPR027004. PMT1/PTM5.
[Graphical view]
PANTHERPTHR10050. PTHR10050. 1 hit.
PTHR10050:SF28. PTHR10050:SF28. 1 hit.
PfamPF02815. MIR. 1 hit.
PF02366. PMT. 1 hit.
[Graphical view]
SMARTSM00472. MIR. 3 hits.
[Graphical view]
SUPFAMSSF82109. SSF82109. 1 hit.
PROSITEPS50919. MIR. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio968744.

Entry information

Entry namePMT1_YEAST
AccessionPrimary (citable) accession number: P33775
Secondary accession number(s): D6VRQ4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: June 11, 2014
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IV

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

Yeast

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

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways