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P33775

- PMT1_YEAST

UniProt

P33775 - PMT1_YEAST

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Protein
Dolichyl-phosphate-mannose--protein mannosyltransferase 1
Gene
PMT1, YDL095W, D2390
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Pathwayi

GO - Molecular functioni

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

GO - Biological processi

  1. ER-associated misfolded protein catabolic process Source: SGD
  2. protein O-linked mannosylation Source: SGD
  3. protein exit from endoplasmic reticulum 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 1 (EC:2.4.1.109)
Gene namesi
Name:PMT1
Ordered Locus Names:YDL095W
ORF Names:D2390
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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 5049Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei51 – 7121Helical; Reviewed prediction
Add
BLAST
Topological domaini72 – 13362Lumenal Reviewed prediction
Add
BLAST
Transmembranei134 – 15421Helical; Reviewed prediction
Add
BLAST
Topological domaini155 – 17925Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei180 – 20021Helical; Reviewed prediction
Add
BLAST
Topological domaini201 – 23434Lumenal Reviewed prediction
Add
BLAST
Transmembranei235 – 25925Helical; Reviewed prediction
Add
BLAST
Topological domaini260 – 27314Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei274 – 29118Helical; Reviewed prediction
Add
BLAST
Topological domaini292 – 584293Lumenal Reviewed prediction
Add
BLAST
Transmembranei585 – 60521Helical; Reviewed prediction
Add
BLAST
Topological domaini606 – 68580Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei686 – 71025Helical; Reviewed prediction
Add
BLAST
Topological domaini711 – 817107Lumenal Reviewed prediction
Add
BLAST

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

PTM / Processingi

Molecule processing

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

Amino acid modifications

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

Keywords - PTMi

Acetylation, Glycoprotein

Proteomic databases

MaxQBiP33775.
PaxDbiP33775.
PeptideAtlasiP33775.

Expressioni

Gene expression databases

GenevestigatoriP33775.

Interactioni

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.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Contains 3 MIR domains.

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1928.
GeneTreeiENSGT00740000116239.
HOGENOMiHOG000157526.
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

MSEEKTYKRV EQDDPVPELD IKQGPVRPFI VTDPSAELAS LRTMVTLKEK    50
LLVACLAVFT AVIRLHGLAW PDSVVFDEVH FGGFASQYIR GTYFMDVHPP 100
LAKMLYAGVA SLGGFQGDFD FENIGDSFPS TTPYVLMRFF SASLGALTVI 150
LMYMTLRYSG VRMWVALMSA ICFAVENSYV TISRYILLDA PLMFFIAAAV 200
YSFKKYEMYP ANSLNAYKSL LATGIALGMA SSSKWVGLFT VTWVGLLCIW 250
RLWFMIGDLT KSSKSIFKVA FAKLAFLLGV PFALYLVFFY IHFQSLTLDG 300
DGASFFSPEF RSTLKNNKIP QNVVADVGIG SIISLRHLST MGGYLHSHSH 350
NYPAGSEQQQ STLYPHMDAN NDWLLELYNA PGESLTTFQN LTDGTKVRLF 400
HTVTRCRLHS HDHKPPVSES SDWQKEVSCY GYSGFDGDAN DDWVVEIDKK 450
NSAPGVAQER VIALDTKFRL RHAMTGCYLF SHEVKLPAWG FEQQEVTCAS 500
SGRHDLTLWY VENNSNPLLP EDTKRISYKP ASFISKFIES HKKMWHINKN 550
LVEPHVYESQ PTSWPFLLRG ISYWGENNRN VYLLGNAIVW WAVTAFIGIF 600
GLIVITELFS WQLGKPILKD SKVVNFHVQV IHYLLGFAVH YAPSFLMQRQ 650
MFLHHYLPAY YFGILALGHA LDIIVSYVFR SKRQMGYAVV ITFLAASVYF 700
FKSFSPIIYG TPWTQELCQK SQWLSGWDYN CNTYFSSLEE YKNQTLTKRE 750
SQPAATSTVE EITIEGDGPS YEDLMNEDGK KIFKDTEGNE LDPEVVKKML 800
EEEGANILKV EKRAVLE 817
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.
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, 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.
    , 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. "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. 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. 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: September 3, 2014
This is version 134 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.

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

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