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Protein

Dolichol phosphate-mannose biosynthesis regulatory protein

Gene

Dpm2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Regulates the biosynthesis of dolichol phosphate-mannose. Regulatory subunit of the dolichol-phosphate mannose (DPM) synthase complex; essential for the ER localization and stable expression of DPM1. When associated with the GPI-GlcNAc transferase (GPI-GnT) complex enhances but is not essential for its activity.1 Publication

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

  • dolichyl-phosphate beta-D-mannosyltransferase activity Source: MGI
  • enzyme regulator activity Source: RGD

GO - Biological processi

  • dolichol metabolic process Source: MGI
  • GPI anchor biosynthetic process Source: MGI
  • mannosylation Source: GOC
  • protein glycosylation Source: UniProtKB-UniPathway
  • regulation of catalytic activity Source: GOC
Complete GO annotation...

Enzyme and pathway databases

UniPathwayiUPA00378.

Names & Taxonomyi

Protein namesi
Recommended name:
Dolichol phosphate-mannose biosynthesis regulatory protein
Alternative name(s):
Dolichol-phosphate mannose synthase subunit 2
Short name:
DPM synthase subunit 2
Gene namesi
Name:Dpm2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2514. Dpm2.

Subcellular locationi

  • Endoplasmic reticulum membrane 1 Publication; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei11 – 3121HelicalSequence analysisAdd
BLAST
Transmembranei49 – 6921HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • dolichol-phosphate-mannose synthase complex Source: MGI
  • endoplasmic reticulum Source: MGI
  • integral component of endoplasmic reticulum membrane Source: InterPro
  • perinuclear region of cytoplasm Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi21 – 211F → L: Abolishes interaction with DPM1; when associated with S-23. 1 Publication
Mutagenesisi23 – 231Y → S: Abolishes interaction with DPM1; when associated with L-21. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 8483Dolichol phosphate-mannose biosynthesis regulatory proteinPRO_0000220875Add
BLAST

Proteomic databases

PaxDbiQ9Z325.

Interactioni

Subunit structurei

Component of the dolichol-phosphate mannose (DPM) synthase complex composed of DPM1, DPM2 and DPM3; in the complex interacts directly with DPM3. Associates with the GPI-GlcNAc transferase (GPI-GnT) complex.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
DPM3Q9P2X02EBI-9097185,EBI-9087337From a different organism.

Protein-protein interaction databases

IntActiQ9Z325. 1 interaction.
STRINGi10116.ENSRNOP00000065111.

Family & Domainsi

Sequence similaritiesi

Belongs to the DPM2 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3488. Eukaryota.
ENOG41122UH. LUCA.
HOVERGENiHBG000508.
InParanoidiQ9Z325.
KOiK09658.
PhylomeDBiQ9Z325.

Family and domain databases

InterProiIPR009914. DPM2.
[Graphical view]
PfamiPF07297. DPM2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9Z325-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATGTDQAVG FGLVAVSLII FTYYTTWVIL LPFIDSQHVI HKYFLPRAYA
60 70 80
VLLPLAAGLL LLLFVGLFIT YVLLKSQKVT KKAQ
Length:84
Mass (Da):9,344
Last modified:January 23, 2007 - v3
Checksum:i345C9AC265573300
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB013359 mRNA. Translation: BAA33972.1.
RefSeqiNP_062125.1. NM_019252.1.
UniGeneiRn.167749.

Genome annotation databases

GeneIDi29640.
KEGGirno:29640.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB013359 mRNA. Translation: BAA33972.1.
RefSeqiNP_062125.1. NM_019252.1.
UniGeneiRn.167749.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9Z325. 1 interaction.
STRINGi10116.ENSRNOP00000065111.

Proteomic databases

PaxDbiQ9Z325.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi29640.
KEGGirno:29640.

Organism-specific databases

CTDi8818.
RGDi2514. Dpm2.

Phylogenomic databases

eggNOGiKOG3488. Eukaryota.
ENOG41122UH. LUCA.
HOVERGENiHBG000508.
InParanoidiQ9Z325.
KOiK09658.
PhylomeDBiQ9Z325.

Enzyme and pathway databases

UniPathwayiUPA00378.

Miscellaneous databases

PROiQ9Z325.

Family and domain databases

InterProiIPR009914. DPM2.
[Graphical view]
PfamiPF07297. DPM2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "DPM2 regulates biosynthesis of dolichol phosphate-mannose in mammalian cells: correct subcellular localization and stabilization of DPM1, and binding of dolichol phosphate."
    Maeda Y., Tomita S., Watanabe R., Ohishi K., Kinoshita T.
    EMBO J. 17:4920-4929(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH DPM1, MUTAGENESIS OF PHE-21 AND TYR-23.

Entry informationi

Entry nameiDPM2_RAT
AccessioniPrimary (citable) accession number: Q9Z325
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 80 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.