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Protein

Dolichyl-phosphate-mannose--protein mannosyltransferase 1

Gene

ogm1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: 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. Required for normal cell growth and septum formation. Shown to actively O-mannosylate wsc1.2 Publications

Catalytic activityi

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

Pathway: protein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

GO - Molecular functioni

  • dolichyl-phosphate-mannose-protein mannosyltransferase activity Source: PomBase

GO - Biological processi

  • cell wall mannoprotein biosynthetic process Source: PomBase
  • chain elongation of O-linked mannose residue Source: PomBase
  • protein O-linked mannosylation Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BRENDAi2.4.1.109. 5613.
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 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC22A12.07c.
PomBaseiSPAC22A12.07c. ogm1.

Subcellular locationi

Topology

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

GO - Cellular componenti

  • endomembrane system Source: PomBase
  • endoplasmic reticulum membrane Source: PomBase
  • integral component of membrane Source: UniProtKB-KW
  • nuclear membrane Source: UniProtKB-SubCell
Complete GO annotation...

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. 3 interactions.
STRINGi4896.SPAC22A12.07c.1.

Structurei

3D structure databases

ProteinModelPortaliO13898.
ModBaseiSearch...
MobiDBiSearch...

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.
InParanoidiO13898.
KOiK00728.
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

        10         20         30         40         50
MDKQSTFQDP KEKHRIQRDV KLSRPRKRFS FLDYVVVIFL TVVAFCVRAQ
60 70 80 90 100
RLMNPAKVVF EELRYYNYAV DYVNNKLLMD VYPPLGKLLF SLVAALTGNK
110 120 130 140 150
YELNTLDEPG QQYPFTDVAY SMRLFTCLLG SLLVPLMYGT VYFPTKSKTA
160 170 180 190 200
ASLAALFVIF DNGLITMSRY IMIEIPALYF MSLTAFYWSV YEAQQKRPFS
210 220 230 240 250
LRWHTSLLST GVALGLALST KLSAMFTFGW LLILAAFHLW NLLGDLSVPM
260 270 280 290 300
YRIVKHLFSY IFYLIGVPIT VYLAVFAVHS HIAYKASVAD AFLPPEHRHA
310 320 330 340 350
LAGNRFDDQF ADVAYGSLVT IRNAIPEHGY LHSSELLYPE GTEQQIISLV
360 370 380 390 400
DEPNQNALWI IEHEHSQDNN RSNIELLKDG SVVRLRHVMT GRALHSHEHK
410 420 430 440 450
PIVSNNDWQL EASAYGGFGF EGDANDLFRI QILEKKSKHA TSNGTVETLN
460 470 480 490 500
TKFRLIHVFA NCELMSSHRR FPDWGDYQRE VTCCRNCVER STTWFIESNY
510 520 530 540 550
HDGLPSDSRK ITYRKPGFLE SFVEHNKLMW LKDRKMGDGH VYESSALTWP
560 570 580 590 600
LLLGPLRFFY EQHLQVFFMG NPFVWYSVIS LVAFFVIVQI FCLARWNLGY
610 620 630 640 650
NDFGPSAFHY NYNIGKFVVA WLLHWAPYIL ETDRVFLYHY LPALYFGIAA
660 670 680 690 700
LGVSWSFLGN AVFGNRTAYK ALSVIIMALM FLVYRLYSPF TYMTTLTKSS
710 720 730 740 750
CRALELKGSW NFHCNTYLDN LSDYKFSSDA GETYFEKAAP HPFVYSEDTA
760 770 780 790 800
KKSEGDTPLN KNLNDYYPSW DQRVEAGYKL AAQQKAEQEA REAAEKAASE
810 820 830 840 850
AAERSSSEAA ASSSSESVAA ASVEAERLAM EADEFNGASE TVDGASVEAE
860 870 880 890
RSAMEAAALN NAAESTEVVG SSPESVASEQ EENVAESAQA RVE
Length:893
Mass (Da):101,335
Last modified:January 1, 1998 - v1
Checksum:i67047E4D896A3568
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB16577.1.
PIRiT38147.
RefSeqiNP_593237.1. NM_001018634.2.

3D structure databases

ProteinModelPortaliO13898.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277924. 3 interactions.
STRINGi4896.SPAC22A12.07c.1.

Protein family/group databases

CAZyiGT39. Glycosyltransferase Family 39.

Proteomic databases

MaxQBiO13898.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:SPAC22A12.07c.
PomBaseiSPAC22A12.07c. ogm1.

Phylogenomic databases

eggNOGiCOG1928.
InParanoidiO13898.
KOiK00728.
OrthoDBiEOG7BP89X.
PhylomeDBiO13898.

Enzyme and pathway databases

UniPathwayiUPA00378.
BRENDAi2.4.1.109. 5613.

Miscellaneous databases

NextBioi20802522.
PROiO13898.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: June 24, 2015
This is version 118 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.