Skip Header

Contribute Send feedback
Read comments (?) or add your own

O13898 (PMT1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dolichyl-phosphate-mannose--protein mannosyltransferase 1
EC=2.4.1.109
Gene names
Name:ogm1
Synonyms:oma1
ORF Names:SPAC22A12.07c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces ›

Protein attributes

Sequence length893 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2 Ref.3

Catalytic activity

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

Pathway

Protein modification; protein glycosylation.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein. Nucleus membrane; Multi-pass membrane protein Ref.2.

Sequence similarities

Belongs to the glycosyltransferase 39 family.

Contains 3 MIR domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 893893Dolichyl-phosphate-mannose--protein mannosyltransferase 1
PRO_0000121499

Regions

Transmembrane29 – 4921Helical; Potential
Transmembrane77 – 9721Helical; Potential
Transmembrane124 – 14421Helical; Potential
Transmembrane147 – 16721Helical; Potential
Transmembrane170 – 19021Helical; Potential
Transmembrane224 – 24421Helical; Potential
Transmembrane258 – 27821Helical; Potential
Transmembrane573 – 59321Helical; Potential
Transmembrane610 – 63021Helical; Potential
Transmembrane643 – 66321Helical; Potential
Transmembrane671 – 69121Helical; Potential
Domain310 – 36455MIR 1
Domain374 – 43360MIR 2
Domain443 – 49957MIR 3

Amino acid modifications

Modified residue4511Phosphothreonine Ref.4
Glycosylation3701N-linked (GlcNAc...) Potential
Glycosylation4431N-linked (GlcNAc...) Potential
Glycosylation6651N-linked (GlcNAc...) Potential
Glycosylation7201N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
O13898 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 67047E4D896A3568

FASTA893101,335
        10         20         30         40         50         60 
MDKQSTFQDP KEKHRIQRDV KLSRPRKRFS FLDYVVVIFL TVVAFCVRAQ RLMNPAKVVF 

        70         80         90        100        110        120 
EELRYYNYAV DYVNNKLLMD VYPPLGKLLF SLVAALTGNK YELNTLDEPG QQYPFTDVAY 

       130        140        150        160        170        180 
SMRLFTCLLG SLLVPLMYGT VYFPTKSKTA ASLAALFVIF DNGLITMSRY IMIEIPALYF 

       190        200        210        220        230        240 
MSLTAFYWSV YEAQQKRPFS LRWHTSLLST GVALGLALST KLSAMFTFGW LLILAAFHLW 

       250        260        270        280        290        300 
NLLGDLSVPM YRIVKHLFSY IFYLIGVPIT VYLAVFAVHS HIAYKASVAD AFLPPEHRHA 

       310        320        330        340        350        360 
LAGNRFDDQF ADVAYGSLVT IRNAIPEHGY LHSSELLYPE GTEQQIISLV DEPNQNALWI 

       370        380        390        400        410        420 
IEHEHSQDNN RSNIELLKDG SVVRLRHVMT GRALHSHEHK PIVSNNDWQL EASAYGGFGF 

       430        440        450        460        470        480 
EGDANDLFRI QILEKKSKHA TSNGTVETLN TKFRLIHVFA NCELMSSHRR FPDWGDYQRE 

       490        500        510        520        530        540 
VTCCRNCVER STTWFIESNY HDGLPSDSRK ITYRKPGFLE SFVEHNKLMW LKDRKMGDGH 

       550        560        570        580        590        600 
VYESSALTWP LLLGPLRFFY EQHLQVFFMG NPFVWYSVIS LVAFFVIVQI FCLARWNLGY 

       610        620        630        640        650        660 
NDFGPSAFHY NYNIGKFVVA WLLHWAPYIL ETDRVFLYHY LPALYFGIAA LGVSWSFLGN 

       670        680        690        700        710        720 
AVFGNRTAYK ALSVIIMALM FLVYRLYSPF TYMTTLTKSS CRALELKGSW NFHCNTYLDN 

       730        740        750        760        770        780 
LSDYKFSSDA GETYFEKAAP HPFVYSEDTA KKSEGDTPLN KNLNDYYPSW DQRVEAGYKL 

       790        800        810        820        830        840 
AAQQKAEQEA REAAEKAASE AAERSSSEAA ASSSSESVAA ASVEAERLAM EADEFNGASE 

       850        860        870        880        890 
TVDGASVEAE RSAMEAAALN NAAESTEVVG SSPESVASEQ EENVAESAQA RVE

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Phosphoproteome analysis of fission yeast."
Wilson-Grady J.T., Villen J., Gygi S.P.
J. Proteome Res. 7:1088-1097(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-451, MASS SPECTROMETRY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CU329670 Genomic DNA. Translation: CAB16577.1.
PIRT38147.
RefSeqNP_593237.1. NM_001018634.2.

3D structure databases

ProteinModelPortalO13898.
ModBaseSearch...

Protein-protein interaction databases

STRING4896.SPAC22A12.07c-1.

Protein family/group databases

CAZyGT39. Glycosyltransferase Family 39.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC22A12.07c.1; SPAC22A12.07c.1:pep; SPAC22A12.07c.
GeneID2541418.
KEGGspo:SPAC22A12.07c.

Organism-specific databases

PomBaseSPAC22A12.07c.

Phylogenomic databases

eggNOGCOG1928.
KOK00728.
OrthoDBEOG4C2MJK.

Enzyme and pathway databases

BRENDA2.4.1.109. 5615.
UniPathwayUPA00378.

Family and domain databases

InterProIPR027005. GlyclTrfase_39_like.
IPR003342. Glyco_trans_39.
IPR016093. MIR_motif.
IPR027004. PMT1.
[Graphical view]
PANTHERPTHR10050. PTHR10050. 1 hit.
PTHR10050:SF12. PTHR10050:SF12. 1 hit.
PfamPF02815. MIR. 1 hit.
PF02366. PMT. 1 hit.
[Graphical view]
SMARTSM00472. MIR. 3 hits.
[Graphical view]
SUPFAMSSF82109. MIR. 1 hit.
PROSITEPS50919. MIR. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio20802522.

Entry information

Entry namePMT1_SCHPO
AccessionPrimary (citable) accession number: O13898
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 1, 1998
Last modified: May 1, 2013
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents