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P47190

- PMT3_YEAST

UniProt

P47190 - PMT3_YEAST

Protein

Dolichyl-phosphate-mannose--protein mannosyltransferase 3

Gene

PMT3

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 124 (01 Oct 2014)
      Sequence version 2 (05 Oct 2010)
      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
    2. protein binding Source: IntAct

    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:YOR321W-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 3 (EC:2.4.1.109)
    Gene namesi
    Name:PMT3
    Ordered Locus Names:YOR321W
    ORF Names:O6148
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XV

    Organism-specific databases

    SGDiS000005848. PMT3.

    Subcellular locationi

    GO - Cellular componenti

    1. dolichyl-phosphate-mannose-protein mannosyltransferase Pmt1p-Pmt3p dimer complex Source: SGD
    2. dolichyl-phosphate-mannose-protein mannosyltransferase Pmt5p-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
    Chaini1 – 753753Dolichyl-phosphate-mannose--protein mannosyltransferase 3PRO_0000121493Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi124 – 1241N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi324 – 3241N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi398 – 3981N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQBiP47190.
    PaxDbiP47190.

    Expressioni

    Gene expression databases

    GenevestigatoriP47190.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PMT1P337753EBI-13579,EBI-13567

    Protein-protein interaction databases

    BioGridi34707. 24 interactions.
    DIPiDIP-5158N.
    IntActiP47190. 4 interactions.
    MINTiMINT-574047.
    STRINGi4932.YOR321W.

    Structurei

    3D structure databases

    ProteinModelPortaliP47190.
    SMRiP47190. Positions 351-504.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 5050CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini72 – 14877LumenalSequence AnalysisAdd
    BLAST
    Topological domaini170 – 1745CytoplasmicSequence Analysis
    Topological domaini196 – 23540LumenalSequence AnalysisAdd
    BLAST
    Topological domaini257 – 28226CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini304 – 602299LumenalSequence AnalysisAdd
    BLAST
    Topological domaini624 – 63916CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini661 – 6655LumenalSequence Analysis
    Topological domaini687 – 70317CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini725 – 75329LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei51 – 7121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei149 – 16921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei175 – 19521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei236 – 25621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei283 – 30321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei603 – 62321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei640 – 66021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei666 – 68621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei704 – 72421HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini332 – 38756MIR 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini401 – 45757MIR 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini465 – 52359MIR 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.
    OMAiFAAHFHI.
    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.

    P47190-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPYRVATGYS EKSTDDDLIW RTPIVKEELE DADNFLKDDA ELYDKVKNES    50
    AVSHLDTIVM PIIFTVLGMF TRMYKIGRNN HVVWDEAHFG KFGSYYLRHE 100
    FYHDVHPPLG KMLVGLSGYL AGYNGSWDFP SGEVYPDYID YVKMRLFQAM 150
    FSSLCVPLAY FTGRAIGFSR LSVWLFTILV IFENSYATLG KFILLDSMLL 200
    FFTVSSYFCL AKFHTMRKSP FSARWWLWLC LTGLNLGCAI SVKMVGLFII 250
    SVVGIYTISE LWNLLSDRSV SWKVYVNHWL ARIFGLIIIP VCVFLLCFKI 300
    HFDLLSNSGP GDSTMPSLFQ ASLNGTKVGK GPRDVALGSS IISIKNQALG 350
    GALLHSHVQP FPEGSEQQQV TVYGYSDANN EWFFQRIRGV EPWTDAENKT 400
    IEFVKGGEMY RLMHRLTGKN LHTHEVPAPI SKSEYEVSAY GDVDLGDYKD 450
    NWIIEIVEQV GEEDPTLLHP LSTSFRIKNS ILGCYLAQSG KHLPEWGFRQ 500
    GEVVCLKHAS KRDKRTWWNI ETHENERLPQ GEDFVYPKTS FFRNFMQLNS 550
    AMMATNNALV PNPEKFDGIA SSAWQWPTLN VGVRLCEWSE KSIKYFLLGS 600
    PASVWPSSIA VCALIIHVIF LTLKWQRQCV ILSDPVERDV FVMAAFYPLL 650
    AWLLHYMPFV VMSRVVYAHH YLPTLYFALM ILSYYFDMIT KRWATRNTGK 700
    FLRLGAYIVY GSIVIAGFFY FSPFSFGMDG PVDDYAYLAW LPTWQIVEDI 750
    RNT 753
    Length:753
    Mass (Da):86,323
    Last modified:October 5, 2010 - v2
    Checksum:iF076473B41EB6CBA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti397 – 3971E → H in CAA58728. (PubMed:8585318)Curated
    Sequence conflicti567 – 5671D → N in CAA58728. (PubMed:8585318)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X83797 Genomic DNA. Translation: CAA58728.1.
    X90565 Genomic DNA. Translation: CAA62176.1.
    Z75229 Genomic DNA. Translation: CAA99641.1.
    BK006948 Genomic DNA. Translation: DAA11085.1.
    PIRiS58331.
    RefSeqiNP_014966.1. NM_001183741.1.

    Genome annotation databases

    EnsemblFungiiYOR321W; YOR321W; YOR321W.
    GeneIDi854499.
    KEGGisce:YOR321W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X83797 Genomic DNA. Translation: CAA58728.1 .
    X90565 Genomic DNA. Translation: CAA62176.1 .
    Z75229 Genomic DNA. Translation: CAA99641.1 .
    BK006948 Genomic DNA. Translation: DAA11085.1 .
    PIRi S58331.
    RefSeqi NP_014966.1. NM_001183741.1.

    3D structure databases

    ProteinModelPortali P47190.
    SMRi P47190. Positions 351-504.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 34707. 24 interactions.
    DIPi DIP-5158N.
    IntActi P47190. 4 interactions.
    MINTi MINT-574047.
    STRINGi 4932.YOR321W.

    Protein family/group databases

    CAZyi GT39. Glycosyltransferase Family 39.

    Proteomic databases

    MaxQBi P47190.
    PaxDbi P47190.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YOR321W ; YOR321W ; YOR321W .
    GeneIDi 854499.
    KEGGi sce:YOR321W.

    Organism-specific databases

    SGDi S000005848. PMT3.

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyci YEAST:YOR321W-MONOMER.
    BRENDAi 2.4.1.109. 984.

    Miscellaneous databases

    NextBioi 976837.

    Gene expression databases

    Genevestigatori P47190.

    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. "PMT3 and PMT4, two new members of the protein-O-mannosyltransferase gene family of Saccharomyces cerevisiae."
      Immervoll T., Gentzsch M., Tanner W.
      Yeast 11:1345-1351(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Sequencing of a 35.71 kb DNA segment on the right arm of yeast chromosome XV reveals regions of similarity to chromosomes I and XIII."
      Pearson B.M., Hernando Y., Payne J., Wolf S.S., Kalogeropoulos A., Schweizer M.
      Yeast 12:1021-1031(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 96604 / S288c / FY1679.
    3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
      Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
      , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
      Nature 387:98-102(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. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    6. "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.

    Entry informationi

    Entry nameiPMT3_YEAST
    AccessioniPrimary (citable) accession number: P47190
    Secondary accession number(s): D6W319
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: October 5, 2010
    Last modified: October 1, 2014
    This is version 124 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 2720 molecules/cell in log phase SD medium.1 Publication

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

    External Data

    Dasty 3