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Protein

Dolichol-phosphate mannosyltransferase

Gene

dpm1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Transfers mannose from GDP-mannose to dolichol monophosphate to form dolichol phosphate mannose (Dol-P-Man) which is the mannosyl donor in pathways leading to N-glycosylation, glycosyl phosphatidylinositol membrane anchoring, and O-mannosylation of proteins.

Catalytic activityi

GDP-mannose + dolichyl phosphate = GDP + dolichyl D-mannosyl phosphate.

Pathwayi: 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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT2. Glycosyltransferase Family 2.

Names & Taxonomyi

Protein namesi
Recommended name:
Dolichol-phosphate mannosyltransferase (EC:2.4.1.83)
Alternative name(s):
Dolichol-phosphate mannose synthase
Short name:
DPM synthase
Dolichyl-phosphate beta-D-mannosyltransferase
Mannose-P-dolichol synthase
Short name:
MPD synthase
Gene namesi
Name:dpm1
ORF Names:SPAC31G5.16c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC31G5.16c.
PomBaseiSPAC31G5.16c. dpm1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: PomBase
  • endoplasmic reticulum Source: PomBase
  • endoplasmic reticulum membrane Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 236236Dolichol-phosphate mannosyltransferasePRO_0000059173Add
BLAST

Proteomic databases

MaxQBiO14466.

Interactioni

Protein-protein interaction databases

MINTiMINT-4672880.

Structurei

3D structure databases

ProteinModelPortaliO14466.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 2 family.Curated

Phylogenomic databases

HOGENOMiHOG000283250.
InParanoidiO14466.
KOiK00721.
OMAiTAYIHGF.
OrthoDBiEOG7W9S51.
PhylomeDBiO14466.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF00535. Glycos_transf_2. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.

Sequencei

Sequence statusi: Complete.

O14466-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKYSVLLPT YNERKNLPII TYLIAKTFDQ EKLDWEIVII DDASPDGTQE
60 70 80 90 100
VAKELQKIYG EDKILLKPRS GKLGLGTAYI HGLKFATGDF VIIMDADFSH
110 120 130 140 150
HPKYLPEFIK LQKEHNYDIV LGTRYAKDGG VYGWNLKRKF ISRGANLLAS
160 170 180 190 200
TVLGTGVSDV TGSFRLYKKP VLETLMSEVT SKGYVFQMEI IARAREHNYT
210 220 230
IGEVPIAFVD RLYGESKLGM DDILGYLKGV FSLLFI
Length:236
Mass (Da):26,672
Last modified:January 1, 1998 - v1
Checksum:iECDB1DE892C1795E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF007873 mRNA. Translation: AAC98795.1.
CU329670 Genomic DNA. Translation: CAB11700.1.
PIRiT38633.
RefSeqiNP_594017.1. NM_001019443.2.

Genome annotation databases

EnsemblFungiiSPAC31G5.16c.1; SPAC31G5.16c.1:pep; SPAC31G5.16c.
GeneIDi2543121.
KEGGispo:SPAC31G5.16c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF007873 mRNA. Translation: AAC98795.1.
CU329670 Genomic DNA. Translation: CAB11700.1.
PIRiT38633.
RefSeqiNP_594017.1. NM_001019443.2.

3D structure databases

ProteinModelPortaliO14466.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4672880.

Protein family/group databases

CAZyiGT2. Glycosyltransferase Family 2.

Proteomic databases

MaxQBiO14466.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC31G5.16c.1; SPAC31G5.16c.1:pep; SPAC31G5.16c.
GeneIDi2543121.
KEGGispo:SPAC31G5.16c.

Organism-specific databases

EuPathDBiFungiDB:SPAC31G5.16c.
PomBaseiSPAC31G5.16c. dpm1.

Phylogenomic databases

HOGENOMiHOG000283250.
InParanoidiO14466.
KOiK00721.
OMAiTAYIHGF.
OrthoDBiEOG7W9S51.
PhylomeDBiO14466.

Enzyme and pathway databases

UniPathwayiUPA00378.

Miscellaneous databases

NextBioi20804148.
PROiO14466.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF00535. Glycos_transf_2. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Human and Saccharomyces cerevisiae dolichol phosphate mannose synthases represent two classes of the enzyme, but both function in Schizosaccharomyces pombe."
    Colussi P.A., Taron C.H., Mack J.C., Orlean P.
    Proc. Natl. Acad. Sci. U.S.A. 94:7873-7878(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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.

Entry informationi

Entry nameiDPM1_SCHPO
AccessioniPrimary (citable) accession number: O14466
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: January 1, 1998
Last modified: May 11, 2016
This is version 101 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

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 one 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.