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Q9C100 (PMT2_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 87. 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

Names and origin

Protein namesRecommended name:
Dolichyl-phosphate-mannose--protein mannosyltransferase 2

EC=2.4.1.109
Gene names
Name:ogm2
Synonyms:oma2
ORF Names:SPAPB1E7.09
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length739 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins. Ref.2

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 – 739739Dolichyl-phosphate-mannose--protein mannosyltransferase 2
PRO_0000237686

Regions

Transmembrane54 – 7421Helical; Potential
Transmembrane146 – 16621Helical; Potential
Transmembrane168 – 18821Helical; Potential
Transmembrane189 – 20921Helical; Potential
Transmembrane229 – 24921Helical; Potential
Transmembrane285 – 30521Helical; Potential
Transmembrane602 – 62221Helical; Potential
Transmembrane639 – 65921Helical; Potential
Transmembrane692 – 71221Helical; Potential
Domain332 – 38655MIR 1
Domain399 – 45557MIR 2
Domain463 – 52159MIR 3

Amino acid modifications

Glycosylation1671N-linked (GlcNAc...) Potential
Glycosylation4041N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q9C100 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: F0F0BBD35D889252

FASTA73985,037
        10         20         30         40         50         60 
MSYEQLHAQS GQLRQRFPSK HSEIEDEVAN EKEELKDATK SALGEVKTNK KYYILGYFLV 

        70         80         90        100        110        120 
PLLLTVIAGF VRVWKIADSN VVIWDEAHFG KFASYYLKHE FYFDVHPPLG KMLNAVAGKL 

       130        140        150        160        170        180 
VGYDGSFDFS SGATYPEDLN YKFMRLWNAA FGTLCIPLVY FTALNFNYSF LAATLCTLMV 

       190        200        210        220        230        240 
ALDNHLATIS RFILLDSMLL FFIISTFFCL SRYHVYHKAP FTFYWFKWLF LTGVCIGCVC 

       250        260        270        280        290        300 
SVKLVGLFIT AVVGLYTVDE LWCLLNDKRV TWKAYAGHWI ARVCLLIFLP ILIYAFTFWI 

       310        320        330        340        350        360 
QFAVLYRSGP GDAQMPSLFQ ARLEGSPLTK NPIDLMYGSK FTLKSRNPTG ALLHSHVQTY 

       370        380        390        400        410        420 
PEGSEQQQVT GYHHKDGNNE WMFVPTHGVA YNYEENDPMN PILNGSVVRL IHPFTNRNLH 

       430        440        450        460        470        480 
THKIPAPLNK RMYEVSGYGL GDVGDEKDYW IVNILYDTAH RDAYNVRSLS TVFQLYNPVV 

       490        500        510        520        530        540 
GCYLSSSSSS LPSWGFGQIE MYCDPDPDPS NTDTQWNVEE HINPRLPEGS INDYPSSFWS 

       550        560        570        580        590        600 
DFLHLNRAML RANNGLIPDE DKLDALRSEA YQWPFLLATL RMCGWGDNQI KYLLVGNPVA 

       610        620        630        640        650        660 
YWFATSSLIV FALFVVGAVL AWRRRVLRWS QEACDTFHYA GIYPFLGWFF NYLPYYIMGR 

       670        680        690        700        710        720 
VLYVHHYEPS YALSTFTAAF VVDWFTKKMP KIVRVVVFIS LYAIIAGVFI YFKDVTFGMH 

       730 
GPASDFHRLR WLNSWNVHD 

« 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329670 Genomic DNA. Translation: CAC36926.1.
RefSeqNP_594135.1. NM_001019559.2.

3D structure databases

ProteinModelPortalQ9C100.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid280071. 2 interactions.
MINTMINT-4702145.
STRING4896.SPAPB1E7.09-1.

Protein family/group databases

CAZyGT39. Glycosyltransferase Family 39.

Proteomic databases

MaxQBQ9C100.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAPB1E7.09.1; SPAPB1E7.09.1:pep; SPAPB1E7.09.
GeneID2543657.
KEGGspo:SPAPB1E7.09.

Organism-specific databases

PomBaseSPAPB1E7.09.

Phylogenomic databases

eggNOGCOG1928.
HOGENOMHOG000157526.
KOK00728.
OMAWLCISRF.
OrthoDBEOG7BP89X.
PhylomeDBQ9C100.

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.
[Graphical view]
PANTHERPTHR10050. PTHR10050. 1 hit.
PfamPF02815. MIR. 1 hit.
PF02366. PMT. 1 hit.
[Graphical view]
SMARTSM00472. MIR. 3 hits.
[Graphical view]
SUPFAMSSF82109. SSF82109. 1 hit.
PROSITEPS50919. MIR. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio20804663.
PROQ9C100.

Entry information

Entry namePMT2_SCHPO
AccessionPrimary (citable) accession number: Q9C100
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: June 1, 2001
Last modified: June 11, 2014
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways