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P33775

- PMT1_YEAST

UniProt

P33775 - PMT1_YEAST

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Protein

Dolichyl-phosphate-mannose--protein mannosyltransferase 1

Gene

PMT1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - 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. Forms a heterodimeric complex with PMT2 and more rarely with PMT3 to transfer mannose from Dol-P-mannose to Ser or Thr residues on proteins. The PMT1-PMT2 complex participates to oxidative protein folding, ER-associated protein degradation (ERAD), as well as ER export. Required for incorporation of proteins in the cell wall.5 Publications

Catalytic activityi

Dolichyl phosphate D-mannose + protein = dolichyl phosphate + O-D-mannosylprotein.2 Publications

Pathwayi

GO - Molecular functioni

  1. dolichyl-phosphate-mannose-protein mannosyltransferase activity Source: SGD

GO - Biological processi

  1. ER-associated misfolded protein catabolic process Source: SGD
  2. protein exit from endoplasmic reticulum Source: SGD
  3. protein O-linked mannosylation Source: SGD
  4. regulation of endoplasmic reticulum unfolded protein response Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BioCyciYEAST:YDL095W-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 1Curated (EC:2.4.1.1092 Publications)
Gene namesi
Name:PMT11 Publication
Ordered Locus Names:YDL095WImported
ORF Names:D2390Imported
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome IV

Organism-specific databases

CYGDiYDL095w.
SGDiS000002253. PMT1.

Subcellular locationi

Endoplasmic reticulum membrane 1 Publication; Multi-pass membrane protein 1 Publication

GO - Cellular componenti

  1. dolichyl-phosphate-mannose-protein mannosyltransferase Pmt1p-Pmt2p dimer complex Source: SGD
  2. dolichyl-phosphate-mannose-protein mannosyltransferase Pmt1p-Pmt3p dimer complex Source: SGD
  3. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Disruption phenotypei

Affects glycosylation of chitinase and increases sensitivity to calcofluor white and caffeine.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi64 – 641R → A: Reduces mannosyltransferase activity. 1 Publication
Mutagenesisi77 – 782DE → AA: Impairs mannosyltransferase activity. 1 Publication
Mutagenesisi78 – 781E → A: Decreases substrate-binding and reduces mannosyltransferase activity. 2 Publications
Mutagenesisi88 – 881Y → A: Moderately decreases complex formation with PMT2. 1 Publication
Mutagenesisi100 – 1001P → A: Moderately decreases complex formation with PMT2. 1 Publication
Mutagenesisi138 – 1381R → A: Impairs complex formation with PMT2. 1 Publication
Mutagenesisi408 – 4081L → A: Reduces mannosyltransferase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 817816Dolichyl-phosphate-mannose--protein mannosyltransferase 1PRO_0000121491Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Glycosylationi390 – 3901N-linked (GlcNAc...)Sequence Analysis
Glycosylationi513 – 5131N-linked (GlcNAc...)Sequence Analysis
Glycosylationi743 – 7431N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Acetylation, Glycoprotein

Proteomic databases

MaxQBiP33775.
PaxDbiP33775.
PeptideAtlasiP33775.

Expressioni

Gene expression databases

GenevestigatoriP33775.

Interactioni

Subunit structurei

PMT1 and PMT2 form a functional heterodimer. The complex interacts with endoplasmic reticulum proteins EMP24, ERV25, ERP1, ERP2, CDC48, HRD1, USA1, YOS9, ERO1, PDI1, UBR1, Cue4, DFM1 and TED1. Forms also a minor complex with PMT3.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PMT2P313824EBI-13567,EBI-13573
PMT3P471903EBI-13567,EBI-13579

Protein-protein interaction databases

BioGridi31966. 154 interactions.
DIPiDIP-7911N.
IntActiP33775. 2 interactions.
MINTiMINT-2787975.
STRINGi4932.YDL095W.

Structurei

3D structure databases

ProteinModelPortaliP33775.
SMRiP33775. Positions 390-515.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 5049Cytoplasmic1 PublicationAdd
BLAST
Topological domaini71 – 13565Lumenal1 PublicationAdd
BLAST
Topological domaini155 – 17925Cytoplasmic1 PublicationAdd
BLAST
Topological domaini201 – 23434Lumenal1 PublicationAdd
BLAST
Topological domaini260 – 27314Cytoplasmic1 PublicationAdd
BLAST
Topological domaini292 – 584293Lumenal1 PublicationAdd
BLAST
Topological domaini606 – 68580Cytoplasmic1 PublicationAdd
BLAST
Topological domaini711 – 817107Lumenal1 PublicationAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei51 – 7020Helical1 PublicationAdd
BLAST
Transmembranei136 – 15419Helical1 PublicationAdd
BLAST
Transmembranei180 – 20021Helical1 PublicationAdd
BLAST
Transmembranei235 – 25925Helical1 PublicationAdd
BLAST
Transmembranei274 – 29118Helical1 PublicationAdd
BLAST
Transmembranei585 – 60521Helical1 PublicationAdd
BLAST
Transmembranei686 – 71025Helical1 PublicationAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini324 – 37855MIR 1PROSITE-ProRule annotationAdd
BLAST
Domaini388 – 44861MIR 2PROSITE-ProRule annotationAdd
BLAST
Domaini459 – 51456MIR 3PROSITE-ProRule annotationAdd
BLAST

Domaini

The large luminal loop 5 is essential for mannosyltransferase activity but not for PMT1-PMT2 complex formation.1 Publication

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.
GeneTreeiENSGT00740000116239.
HOGENOMiHOG000157526.
InParanoidiP33775.
KOiK00728.
OMAiMSSEFQA.
OrthoDBiEOG7BP89X.

Family and domain databases

InterProiIPR027005. GlyclTrfase_39_like.
IPR003342. Glyco_trans_39.
IPR016093. MIR_motif.
IPR027004. PMT1/PTM5.
[Graphical view]
PANTHERiPTHR10050. PTHR10050. 1 hit.
PTHR10050:SF28. PTHR10050:SF28. 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.

P33775-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSEEKTYKRV EQDDPVPELD IKQGPVRPFI VTDPSAELAS LRTMVTLKEK
60 70 80 90 100
LLVACLAVFT AVIRLHGLAW PDSVVFDEVH FGGFASQYIR GTYFMDVHPP
110 120 130 140 150
LAKMLYAGVA SLGGFQGDFD FENIGDSFPS TTPYVLMRFF SASLGALTVI
160 170 180 190 200
LMYMTLRYSG VRMWVALMSA ICFAVENSYV TISRYILLDA PLMFFIAAAV
210 220 230 240 250
YSFKKYEMYP ANSLNAYKSL LATGIALGMA SSSKWVGLFT VTWVGLLCIW
260 270 280 290 300
RLWFMIGDLT KSSKSIFKVA FAKLAFLLGV PFALYLVFFY IHFQSLTLDG
310 320 330 340 350
DGASFFSPEF RSTLKNNKIP QNVVADVGIG SIISLRHLST MGGYLHSHSH
360 370 380 390 400
NYPAGSEQQQ STLYPHMDAN NDWLLELYNA PGESLTTFQN LTDGTKVRLF
410 420 430 440 450
HTVTRCRLHS HDHKPPVSES SDWQKEVSCY GYSGFDGDAN DDWVVEIDKK
460 470 480 490 500
NSAPGVAQER VIALDTKFRL RHAMTGCYLF SHEVKLPAWG FEQQEVTCAS
510 520 530 540 550
SGRHDLTLWY VENNSNPLLP EDTKRISYKP ASFISKFIES HKKMWHINKN
560 570 580 590 600
LVEPHVYESQ PTSWPFLLRG ISYWGENNRN VYLLGNAIVW WAVTAFIGIF
610 620 630 640 650
GLIVITELFS WQLGKPILKD SKVVNFHVQV IHYLLGFAVH YAPSFLMQRQ
660 670 680 690 700
MFLHHYLPAY YFGILALGHA LDIIVSYVFR SKRQMGYAVV ITFLAASVYF
710 720 730 740 750
FKSFSPIIYG TPWTQELCQK SQWLSGWDYN CNTYFSSLEE YKNQTLTKRE
760 770 780 790 800
SQPAATSTVE EITIEGDGPS YEDLMNEDGK KIFKDTEGNE LDPEVVKKML
810
EEEGANILKV EKRAVLE
Length:817
Mass (Da):92,675
Last modified:February 1, 1994 - v1
Checksum:i6309BBA71BAD8D21
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L19169 Unassigned DNA. Translation: AAA02928.1.
X95644 Genomic DNA. Translation: CAA64917.1.
Z74144 Genomic DNA. Translation: CAA98663.1.
BK006938 Genomic DNA. Translation: DAA11764.1.
PIRiA47716.
RefSeqiNP_010188.1. NM_001180154.1.

Genome annotation databases

EnsemblFungiiYDL095W; YDL095W; YDL095W.
GeneIDi851462.
KEGGisce:YDL095W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L19169 Unassigned DNA. Translation: AAA02928.1 .
X95644 Genomic DNA. Translation: CAA64917.1 .
Z74144 Genomic DNA. Translation: CAA98663.1 .
BK006938 Genomic DNA. Translation: DAA11764.1 .
PIRi A47716.
RefSeqi NP_010188.1. NM_001180154.1.

3D structure databases

ProteinModelPortali P33775.
SMRi P33775. Positions 390-515.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 31966. 154 interactions.
DIPi DIP-7911N.
IntActi P33775. 2 interactions.
MINTi MINT-2787975.
STRINGi 4932.YDL095W.

Protein family/group databases

CAZyi GT39. Glycosyltransferase Family 39.

Proteomic databases

MaxQBi P33775.
PaxDbi P33775.
PeptideAtlasi P33775.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YDL095W ; YDL095W ; YDL095W .
GeneIDi 851462.
KEGGi sce:YDL095W.

Organism-specific databases

CYGDi YDL095w.
SGDi S000002253. PMT1.

Phylogenomic databases

eggNOGi COG1928.
GeneTreei ENSGT00740000116239.
HOGENOMi HOG000157526.
InParanoidi P33775.
KOi K00728.
OMAi MSSEFQA.
OrthoDBi EOG7BP89X.

Enzyme and pathway databases

UniPathwayi UPA00378 .
BioCyci YEAST:YDL095W-MONOMER.
BRENDAi 2.4.1.109. 984.

Miscellaneous databases

NextBioi 968744.

Gene expression databases

Genevestigatori P33775.

Family and domain databases

InterProi IPR027005. GlyclTrfase_39_like.
IPR003342. Glyco_trans_39.
IPR016093. MIR_motif.
IPR027004. PMT1/PTM5.
[Graphical view ]
PANTHERi PTHR10050. PTHR10050. 1 hit.
PTHR10050:SF28. PTHR10050:SF28. 1 hit.
Pfami PF02815. MIR. 1 hit.
PF02366. PMT. 1 hit.
[Graphical view ]
SMARTi SM00472. MIR. 3 hits.
[Graphical view ]
SUPFAMi SSF82109. SSF82109. 1 hit.
PROSITEi PS50919. MIR. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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 [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, IDENTIFICATION, FUNCTION, CATALYTIC ACTIVITY.
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "Protein O-glycosylation in Saccharomyces cerevisiae: the protein O-mannosyltransferases Pmt1p and Pmt2p function as heterodimer."
    Gentzsch M., Immervoll T., Tanner W.
    FEBS Lett. 377:128-130(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PMT2.
  6. "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: DISRUPTION PHENOTYPE.
  7. "Pmt1 mannosyl transferase is involved in cell wall incorporation of several proteins in Saccharomyces cerevisiae."
    Bourdineaud J.P., van der Vaart J.M., Donzeau M., de Sampaio G., Verrips C.T., Lauquin G.J.
    Mol. Microbiol. 27:85-98(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Transmembrane topology of pmt1p, a member of an evolutionarily conserved family of protein O-mannosyltransferases."
    Strahl-Bolsinger S., Scheinost A.
    J. Biol. Chem. 274:9068-9075(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TOPOLOGY.
  9. "Structure-function analysis of the dolichyl phosphate-mannose: protein O-mannosyltransferase ScPmt1p."
    Girrbach V., Zeller T., Priesmeier M., Strahl-Bolsinger S.
    J. Biol. Chem. 275:19288-19296(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, DOMAIN, MUTAGENESIS OF ARG-64; GLU-78; ARG-138 AND LEU-408.
  10. "Members of the evolutionarily conserved PMT family of protein O-mannosyltransferases form distinct protein complexes among themselves."
    Girrbach V., Strahl S.
    J. Biol. Chem. 278:12554-12562(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PMT2 AND PMT3.
  11. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  12. "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.
  13. "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: FUNCTION.
  14. "A conserved acidic motif is crucial for enzymatic activity of protein O-mannosyltransferases."
    Lommel M., Schott A., Jank T., Hofmann V., Strahl S.
    J. Biol. Chem. 286:39768-39775(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF 77-ASP-GLU-78; GLU-78; TYR-88 AND PRO-100.
  15. "Protein O-mannosyltransferases participate in ER protein quality control."
    Goder V., Melero A.
    J. Cell Sci. 124:144-153(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF THE PMT1-PMT2 COMPLEX, INTERACTION WITH PMT2; EMP24; ERV25; ERP1; ERP2; CDC48; HRD1; USA1; YOS9; ERO1; PDI1; UBR1; CUE4; DFM1 AND TED1.
  16. 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 nameiPMT1_YEAST
AccessioniPrimary (citable) accession number: P33775
Secondary accession number(s): D6VRQ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: October 29, 2014
This is version 136 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 41500 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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 IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

External Data

Dasty 3