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P42934

- PMT6_YEAST

UniProt

P42934 - PMT6_YEAST

Protein

Dolichyl-phosphate-mannose--protein mannosyltransferase 6

Gene

PMT6

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
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    Functioni

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

    Catalytic activityi

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

    GO - Molecular functioni

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

    GO - Biological processi

    1. protein O-linked glycosylation Source: SGD
    2. protein O-linked mannosylation Source: SGD

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Enzyme and pathway databases

    BioCyciYEAST:YGR199W-MONOMER.
    BRENDAi2.4.1.109. 984.

    Protein family/group databases

    CAZyiGT39. Glycosyltransferase Family 39.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dolichyl-phosphate-mannose--protein mannosyltransferase 6 (EC:2.4.1.109)
    Gene namesi
    Name:PMT6
    Ordered Locus Names:YGR199W
    ORF Names:G7722
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome VII

    Organism-specific databases

    CYGDiYGR199w.
    SGDiS000003431. PMT6.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    2. 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 – 759758Dolichyl-phosphate-mannose--protein mannosyltransferase 6PRO_0000121496Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Glycosylationi156 – 1561N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi404 – 4041N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi481 – 4811N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Acetylation, Glycoprotein

    Proteomic databases

    MaxQBiP42934.
    PaxDbiP42934.

    Expressioni

    Gene expression databases

    GenevestigatoriP42934.

    Interactioni

    Protein-protein interaction databases

    BioGridi33452. 48 interactions.
    DIPiDIP-5551N.
    IntActiP42934. 1 interaction.
    MINTiMINT-561799.
    STRINGi4932.YGR199W.

    Structurei

    3D structure databases

    ProteinModelPortaliP42934.
    SMRiP42934. Positions 342-525.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini2 – 5857CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini80 – 16485LumenalSequence AnalysisAdd
    BLAST
    Topological domaini186 – 1949CytoplasmicSequence Analysis
    Topological domaini216 – 25136LumenalSequence AnalysisAdd
    BLAST
    Topological domaini273 – 29321CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini315 – 618304LumenalSequence AnalysisAdd
    BLAST
    Topological domaini640 – 65617CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini678 – 6869LumenalSequence Analysis
    Topological domaini708 – 7158CytoplasmicSequence Analysis
    Topological domaini737 – 75923LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei59 – 7921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei165 – 18521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei195 – 21521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei252 – 27221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei294 – 31421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei619 – 63921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei657 – 67721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei687 – 70721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei716 – 73621HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini340 – 39455MIR 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini409 – 46759MIR 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini482 – 54059MIR 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.
    GeneTreeiENSGT00740000115531.
    HOGENOMiHOG000157526.
    KOiK00728.
    OMAiSEWWEWP.
    OrthoDBiEOG7BP89X.

    Family and domain databases

    InterProiIPR027005. GlyclTrfase_39_like.
    IPR003342. Glyco_trans_39.
    IPR016093. MIR_motif.
    [Graphical view]
    PANTHERiPTHR10050. PTHR10050. 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.

    P42934-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSKAKGTGFS SIDTEDENLR ERYVNQPKAN ASDIQDEQLD CFEQLEEKHR    50
    TKKNEEYTAL KILRDVIGPL LLTITSFYLR FQHIDQNNYV VWDEAHFGKF 100
    GSYYIKHEYY HDVHPPLGKM LIALSEWMAG FDGQFDFSSN NAYPENVNFK 150
    LMRQFNATFG ALCTPVAFFT AKWMGFNYFT VYLIATMVTL EHSYIVLSKF 200
    ILLDSMLLFF SMTTFACMIK LYTLRKQQMT KKWSLWMLLT GLSIGCVCSV 250
    KWVGLFITVV VGLYTCIELF LLYCDKELPR IKYYKHWLIR IINLIVIPFL 300
    IYLYCFKIHF VLLYKSGTGD STTNTLFQIN LEGTQIEAGP RDVAFGSELT 350
    IRSHGLSPNL LHSHIQVYPE GSGQRQITGY GFADSNNVWK FEFSRSSGLE 400
    LDQNGTLNGK IIPITDGVEV RLSHKNTGSN LHSHDVPSHV SRGNYEVSGY 450
    GSQSVGDEKD DWIVEIVKQM DSPNPVYSNE NSTILHPVST FFRLRHKVLG 500
    CYLASTGLTY PAWGFKQAEI VCKDSWSRRD KSTWWNVEDH WNHNLETAED 550
    YVPPKSNFWT DFILTNFAMA SSNNALVPDE DKYDSLSSDA WEWPTLHKGL 600
    RMCSWAGYIT RYYLMGSPFN TWISTVSLII FPFIILFILY RWRRQTLYLS 650
    DDQIWQITIQ GIFPFISWMT HYLPFAMMGR VTYVHHYVPA LYFAMLVFGF 700
    VLDFTLTRVH WMVKYPIYLS LFGGCIYIYN LFAPICQGMH GDKAEYLPLQ 750
    WLSTWDIAP 759
    Length:759
    Mass (Da):88,026
    Last modified:November 1, 1995 - v1
    Checksum:i7A23DCEDD90F01C8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z49133 Genomic DNA. Translation: CAA88992.1.
    Z72984 Genomic DNA. Translation: CAA97226.1.
    BK006941 Genomic DNA. Translation: DAA08292.1.
    PIRiS53922.
    RefSeqiNP_011715.1. NM_001181328.1.

    Genome annotation databases

    EnsemblFungiiYGR199W; YGR199W; YGR199W.
    GeneIDi853113.
    KEGGisce:YGR199W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z49133 Genomic DNA. Translation: CAA88992.1 .
    Z72984 Genomic DNA. Translation: CAA97226.1 .
    BK006941 Genomic DNA. Translation: DAA08292.1 .
    PIRi S53922.
    RefSeqi NP_011715.1. NM_001181328.1.

    3D structure databases

    ProteinModelPortali P42934.
    SMRi P42934. Positions 342-525.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 33452. 48 interactions.
    DIPi DIP-5551N.
    IntActi P42934. 1 interaction.
    MINTi MINT-561799.
    STRINGi 4932.YGR199W.

    Protein family/group databases

    CAZyi GT39. Glycosyltransferase Family 39.

    Proteomic databases

    MaxQBi P42934.
    PaxDbi P42934.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YGR199W ; YGR199W ; YGR199W .
    GeneIDi 853113.
    KEGGi sce:YGR199W.

    Organism-specific databases

    CYGDi YGR199w.
    SGDi S000003431. PMT6.

    Phylogenomic databases

    eggNOGi COG1928.
    GeneTreei ENSGT00740000115531.
    HOGENOMi HOG000157526.
    KOi K00728.
    OMAi SEWWEWP.
    OrthoDBi EOG7BP89X.

    Enzyme and pathway databases

    BioCyci YEAST:YGR199W-MONOMER.
    BRENDAi 2.4.1.109. 984.

    Miscellaneous databases

    NextBioi 973133.

    Gene expression databases

    Genevestigatori P42934.

    Family and domain databases

    InterProi IPR027005. GlyclTrfase_39_like.
    IPR003342. Glyco_trans_39.
    IPR016093. MIR_motif.
    [Graphical view ]
    PANTHERi PTHR10050. PTHR10050. 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. "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.
      , 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 204508 / S288c.
    3. 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. 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 nameiPMT6_YEAST
    AccessioniPrimary (citable) accession number: P42934
    Secondary accession number(s): D6VUY1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 122 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome VII
      Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

    External Data

    Dasty 3