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O13898

- PMT1_SCHPO

UniProt

O13898 - PMT1_SCHPO

Protein

Dolichyl-phosphate-mannose--protein mannosyltransferase 1

Gene

ogm1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    Functioni

    Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins. Required for normal cell growth adn septum formation. Shown to actively O-mannosylate wsc1.2 Publications

    Catalytic activityi

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

    Pathwayi

    GO - Molecular functioni

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

    GO - Biological processi

    1. cell wall mannoprotein biosynthetic process Source: PomBase
    2. chain elongation of O-linked mannose residue Source: PomBase
    3. protein O-linked mannosylation Source: PomBase

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Enzyme and pathway databases

    BRENDAi2.4.1.109. 5615.
    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:ogm1
    Synonyms:oma1
    ORF Names:SPAC22A12.07c
    OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
    Taxonomic identifieri284812 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
    ProteomesiUP000002485: Chromosome I

    Organism-specific databases

    PomBaseiSPAC22A12.07c.

    Subcellular locationi

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

    GO - Cellular componenti

    1. dolichyl-phosphate-mannose-protein mannosyltransferase complex Source: PomBase
    2. endomembrane system Source: PomBase
    3. endoplasmic reticulum membrane Source: PomBase
    4. integral component of membrane Source: UniProtKB-KW
    5. nuclear membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 893893Dolichyl-phosphate-mannose--protein mannosyltransferase 1PRO_0000121499Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi370 – 3701N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi443 – 4431N-linked (GlcNAc...)Sequence Analysis
    Modified residuei451 – 4511Phosphothreonine1 Publication
    Glycosylationi665 – 6651N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi720 – 7201N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiO13898.

    Interactioni

    Protein-protein interaction databases

    BioGridi277924. 4 interactions.
    STRINGi4896.SPAC22A12.07c-1.

    Structurei

    3D structure databases

    ProteinModelPortaliO13898.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei29 – 4921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei77 – 9721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei124 – 14421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei147 – 16721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei170 – 19021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei224 – 24421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei258 – 27821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei573 – 59321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei610 – 63021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei643 – 66321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei671 – 69121HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini310 – 36455MIR 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini374 – 43360MIR 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini443 – 49957MIR 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.
    KOiK00728.
    OMAiFANCELM.
    OrthoDBiEOG7BP89X.
    PhylomeDBiO13898.

    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.

    O13898-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDKQSTFQDP KEKHRIQRDV KLSRPRKRFS FLDYVVVIFL TVVAFCVRAQ    50
    RLMNPAKVVF EELRYYNYAV DYVNNKLLMD VYPPLGKLLF SLVAALTGNK 100
    YELNTLDEPG QQYPFTDVAY SMRLFTCLLG SLLVPLMYGT VYFPTKSKTA 150
    ASLAALFVIF DNGLITMSRY IMIEIPALYF MSLTAFYWSV YEAQQKRPFS 200
    LRWHTSLLST GVALGLALST KLSAMFTFGW LLILAAFHLW NLLGDLSVPM 250
    YRIVKHLFSY IFYLIGVPIT VYLAVFAVHS HIAYKASVAD AFLPPEHRHA 300
    LAGNRFDDQF ADVAYGSLVT IRNAIPEHGY LHSSELLYPE GTEQQIISLV 350
    DEPNQNALWI IEHEHSQDNN RSNIELLKDG SVVRLRHVMT GRALHSHEHK 400
    PIVSNNDWQL EASAYGGFGF EGDANDLFRI QILEKKSKHA TSNGTVETLN 450
    TKFRLIHVFA NCELMSSHRR FPDWGDYQRE VTCCRNCVER STTWFIESNY 500
    HDGLPSDSRK ITYRKPGFLE SFVEHNKLMW LKDRKMGDGH VYESSALTWP 550
    LLLGPLRFFY EQHLQVFFMG NPFVWYSVIS LVAFFVIVQI FCLARWNLGY 600
    NDFGPSAFHY NYNIGKFVVA WLLHWAPYIL ETDRVFLYHY LPALYFGIAA 650
    LGVSWSFLGN AVFGNRTAYK ALSVIIMALM FLVYRLYSPF TYMTTLTKSS 700
    CRALELKGSW NFHCNTYLDN LSDYKFSSDA GETYFEKAAP HPFVYSEDTA 750
    KKSEGDTPLN KNLNDYYPSW DQRVEAGYKL AAQQKAEQEA REAAEKAASE 800
    AAERSSSEAA ASSSSESVAA ASVEAERLAM EADEFNGASE TVDGASVEAE 850
    RSAMEAAALN NAAESTEVVG SSPESVASEQ EENVAESAQA RVE 893
    Length:893
    Mass (Da):101,335
    Last modified:January 1, 1998 - v1
    Checksum:i67047E4D896A3568
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU329670 Genomic DNA. Translation: CAB16577.1.
    PIRiT38147.
    RefSeqiNP_593237.1. NM_001018634.2.

    Genome annotation databases

    EnsemblFungiiSPAC22A12.07c.1; SPAC22A12.07c.1:pep; SPAC22A12.07c.
    GeneIDi2541418.
    KEGGispo:SPAC22A12.07c.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU329670 Genomic DNA. Translation: CAB16577.1 .
    PIRi T38147.
    RefSeqi NP_593237.1. NM_001018634.2.

    3D structure databases

    ProteinModelPortali O13898.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 277924. 4 interactions.
    STRINGi 4896.SPAC22A12.07c-1.

    Protein family/group databases

    CAZyi GT39. Glycosyltransferase Family 39.

    Proteomic databases

    MaxQBi O13898.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii SPAC22A12.07c.1 ; SPAC22A12.07c.1:pep ; SPAC22A12.07c .
    GeneIDi 2541418.
    KEGGi spo:SPAC22A12.07c.

    Organism-specific databases

    PomBasei SPAC22A12.07c.

    Phylogenomic databases

    eggNOGi COG1928.
    KOi K00728.
    OMAi FANCELM.
    OrthoDBi EOG7BP89X.
    PhylomeDBi O13898.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .
    BRENDAi 2.4.1.109. 5615.

    Miscellaneous databases

    NextBioi 20802522.

    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. "The genome sequence of Schizosaccharomyces pombe."
      Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
      , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
      Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 972 / ATCC 24843.
    2. "Characterization of O-mannosyltransferase family in Schizosaccharomyces pombe."
      Tanaka N., Fujita Y., Suzuki S., Morishita M., Giga-Hama Y., Shimoda C., Takegawa K.
      Biochem. Biophys. Res. Commun. 330:813-820(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    3. "Protein O-mannosylation is crucial for cell wall integrity, septation and viability in fission yeast."
      Willer T., Brandl M., Sipiczki M., Strahl S.
      Mol. Microbiol. 57:156-170(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-451, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiPMT1_SCHPO
    AccessioniPrimary (citable) accession number: O13898
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 111 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. Schizosaccharomyces pombe
      Schizosaccharomyces pombe: entries and gene names
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3