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P33775

- PMT1_YEAST

UniProt

P33775 - PMT1_YEAST

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
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 1 (01 Feb 1994)
      Previous versions | rss
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    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 exit from endoplasmic reticulum Source: SGD
    3. protein O-linked mannosylation Source: SGD
    4. regulation of endoplasmic reticulum unfolded protein response Source: SGD

    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

    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

    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 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

    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 – 5049CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini72 – 13362LumenalSequence AnalysisAdd
    BLAST
    Topological domaini155 – 17925CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini201 – 23434LumenalSequence AnalysisAdd
    BLAST
    Topological domaini260 – 27314CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini292 – 584293LumenalSequence AnalysisAdd
    BLAST
    Topological domaini606 – 68580CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini711 – 817107LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei51 – 7121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei134 – 15421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei180 – 20021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei235 – 25925HelicalSequence AnalysisAdd
    BLAST
    Transmembranei274 – 29118HelicalSequence AnalysisAdd
    BLAST
    Transmembranei585 – 60521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei686 – 71025HelicalSequence AnalysisAdd
    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

    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.
    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

    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: October 1, 2014
    This is version 135 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