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Protein

Dolichol-phosphate mannosyltransferase subunit 1

Gene

DPM1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 3 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 subunit of the dolichol-phosphate mannose (DPM) synthase complex.By similarity

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 subunit 1 (EC:2.4.1.83)
Alternative name(s):
Dolichol-phosphate mannose synthase subunit 1
Short name:
DPM synthase subunit 1
Dolichyl-phosphate beta-D-mannosyltransferase subunit 1
Mannose-P-dolichol synthase subunit 1
Short name:
MPD synthase subunit 1
Gene namesi
Name:DPM1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 260259Dolichol-phosphate mannosyltransferase subunit 1PRO_0000282826Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei9 – 91PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ1JQ93.
PRIDEiQ1JQ93.

PTM databases

iPTMnetiQ1JQ93.

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.By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000010153.

Structurei

3D structure databases

ProteinModelPortaliQ1JQ93.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 2 family.Curated

Phylogenomic databases

eggNOGiKOG2978. Eukaryota.
COG0463. LUCA.
HOGENOMiHOG000283250.
HOVERGENiHBG018967.
InParanoidiQ1JQ93.
KOiK00721.

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.

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

Q1JQ93-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAEEASRSS PRFRREPKGR VSRQDKYSVL LPTYNERENL PFIVWLLVKS
60 70 80 90 100
FSESGFNYEI IIIDDGSPDG TRDVAEQLEK IYGSDRILLR PREKKLGLGT
110 120 130 140 150
AYIHGMKHAT GNYIIIMDAD LSHHPKFIPE FIRKQKEGNF DIVSGTRYKG
160 170 180 190 200
NGGVYGWDLK RKIISRVANF ITQILLRPGA SDLTGSFRLY RKEVLQKLIG
210 220 230 240 250
KCISKGYVFQ MEMIVRARQL NYTIGEVPIS FVDRVYGESK LGGNEIVSFL
260
KGLLTLFATT
Length:260
Mass (Da):29,592
Last modified:June 13, 2006 - v1
Checksum:i16AF1CEE3D474801
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC116151 mRNA. Translation: AAI16152.1.
RefSeqiNP_001069481.1. NM_001076013.2.
UniGeneiBt.869.

Genome annotation databases

GeneIDi534097.
KEGGibta:534097.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC116151 mRNA. Translation: AAI16152.1.
RefSeqiNP_001069481.1. NM_001076013.2.
UniGeneiBt.869.

3D structure databases

ProteinModelPortaliQ1JQ93.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000010153.

Protein family/group databases

CAZyiGT2. Glycosyltransferase Family 2.

PTM databases

iPTMnetiQ1JQ93.

Proteomic databases

PaxDbiQ1JQ93.
PRIDEiQ1JQ93.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi534097.
KEGGibta:534097.

Organism-specific databases

CTDi8813.

Phylogenomic databases

eggNOGiKOG2978. Eukaryota.
COG0463. LUCA.
HOGENOMiHOG000283250.
HOVERGENiHBG018967.
InParanoidiQ1JQ93.
KOiK00721.

Enzyme and pathway databases

UniPathwayiUPA00378.

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...

Entry informationi

Entry nameiDPM1_BOVIN
AccessioniPrimary (citable) accession number: Q1JQ93
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: June 13, 2006
Last modified: June 8, 2016
This is version 56 of the entry and version 1 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.