Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P42867 (GPT_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 111. 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:
UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase

EC=2.7.8.15
Alternative name(s):
GlcNAc-1-P transferase
Short name=G1PT
Short name=GPT
N-acetylglucosamine-1-phosphate transferase
Gene names
Name:Dpagt1
Synonyms:Dpagt2, Gnpta
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length410 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the initial step in the synthesis of dolichol-P-P-oligosaccharides.

Catalytic activity

UDP-N-acetyl-D-glucosamine + dolichyl phosphate = UMP + N-acetyl-D-glucosaminyl-diphosphodolichol.

Enzyme regulation

Enzyme activity is stimulated by phosphatidylglycerol and mannosylphosphoryldolichol and inhibited by tunicamycin.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein.

Developmental stage

Highest activity is during the mid-phase of lactation.

Disruption phenotype

Mice die 4 to 5 days post-fertilization, just after implantation, suggesting that protein function and N-glycosylation are essential in early embryogenesis. Ref.4

Sequence similarities

Belongs to the glycosyltransferase 4 family.

RNA editing

Edited at position 74.
Partially edited. Ref.2

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 410410UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase
PRO_0000108762

Regions

Topological domain1 – 66Lumenal Potential
Transmembrane7 – 3428Helical; Potential
Topological domain35 – 5925Cytoplasmic Potential
Transmembrane60 – 8122Helical; Potential
Topological domain82 – 9615Lumenal Potential
Transmembrane97 – 11620Helical; Potential
Topological domain117 – 12711Cytoplasmic Potential
Transmembrane128 – 14720Helical; Potential
Topological domain148 – 16619Lumenal Potential
Transmembrane167 – 18620Helical; Potential
Topological domain187 – 19610Cytoplasmic Potential
Transmembrane197 – 21317Helical; Potential
Topological domain214 – 22310Lumenal Potential
Transmembrane224 – 24219Helical; Potential
Topological domain243 – 25412Cytoplasmic Potential
Transmembrane255 – 27117Helical; Potential
Topological domain272 – 2765Lumenal Potential
Transmembrane277 – 29620Helical; Potential
Topological domain297 – 38084Cytoplasmic Potential
Transmembrane381 – 39919Helical; Potential
Topological domain400 – 41011Lumenal Potential
Motif69 – 8113Dolichol recognition
Motif224 – 23613Dolichol recognition

Amino acid modifications

Glycosylation1481N-linked (GlcNAc...) Potential

Natural variations

Natural variant741C → Y in RNA edited version.

Sequences

Sequence LengthMass (Da)Tools
P42867 [UniParc].

Last modified November 28, 2003. Version 2.
Checksum: F729D6983FA67E0B

FASTA41046,412
        10         20         30         40         50         60 
MWAFPELPLP LPLLVNLIGS LLGFVATVTL IPAFRSHFIA ARLCGQDLNK LSQQQIPESQ 

        70         80         90        100        110        120 
GVISGAVFLI ILFCFIPFPF LNCFVEEQCK AFPHHEFVAL IGALLAICCM IFLGFADDVL 

       130        140        150        160        170        180 
NLRWRHKLLL PTAASLPLLM VYFTNFGNTT IVVPKPFRWI LGLHLDLGIL YYVYMGLLAV 

       190        200        210        220        230        240 
FCTNAINILA GINGLEAGQS LVISASIIVF NLVELEGDYR DDHIFSLYFM IPFFFTTLGL 

       250        260        270        280        290        300 
LYHNWYPSRV FVGDTFCYFA GMTFAVVGIL GHFSKTMLLF FMPQVFNFLY SLPQLFHIIP 

       310        320        330        340        350        360 
CPRHRMPRLN AKTGKLEMSY SKFKTKNLSF LGTFILKVAE NLRLVTVHQG ESEDGAFTEC 

       370        380        390        400        410 
NNMTLINLLL KVFGPIHERN LTLLLLLLQV LSSAATFSIR YQLVRLFYDV 

« Hide

References

« Hide 'large scale' references
[1]"Mouse UDP-GlcNAc: dolichyl-phosphate N-acetylglucosaminephosphotransferase. Molecular cloning of the cDNA, generation of anti-peptide antibodies and chromosomal localization."
Rajput B., Ma J., Muniappa N., Schantz L., Naylor S.L., Lalley P.A., Vijay I.K.
Biochem. J. 285:985-992(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Mammary gland.
[2]"Structure and organization of mouse GlcNAc-1-phosphate transferase gene."
Rajput B., Ma J., Vijay I.K.
J. Biol. Chem. 269:9590-9597(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], RNA EDITING.
Strain: BALB/c and NIH Swiss.
Tissue: Liver and Mammary gland.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Mammary tumor.
[4]"A recessive deletion in the GlcNAc-1-phosphotransferase gene results in peri-implantation embryonic lethality."
Marek K.W., Vijay I.K., Marth J.D.
Glycobiology 9:1263-1271(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X65603 mRNA. Translation: CAA46553.1.
BC010474 mRNA. Translation: AAH10474.1.
PIRS24326.
RefSeqNP_031901.2. NM_007875.2.
UniGeneMm.18353.

3D structure databases

ProteinModelPortalP42867.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteP42867.

Proteomic databases

PaxDbP42867.
PRIDEP42867.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000054708; ENSMUSP00000056282; ENSMUSG00000032123.
GeneID13478.
KEGGmmu:13478.
UCSCuc009pcv.1. mouse.

Organism-specific databases

CTD1798.
MGIMGI:1196396. Dpagt1.

Phylogenomic databases

eggNOGCOG0472.
GeneTreeENSGT00390000011424.
HOGENOMHOG000163915.
HOVERGENHBG000846.
InParanoidP42867.
KOK01001.
OMAIHERNLT.
OrthoDBEOG73804W.
PhylomeDBP42867.
TreeFamTF313734.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

ArrayExpressP42867.
BgeeP42867.
GenevestigatorP42867.

Family and domain databases

InterProIPR000715. Glycosyl_transferase_4.
[Graphical view]
PfamPF00953. Glycos_transf_4. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDPAGT1. mouse.
NextBio283963.
PROP42867.
SOURCESearch...

Entry information

Entry nameGPT_MOUSE
AccessionPrimary (citable) accession number: P42867
Secondary accession number(s): Q921W5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 28, 2003
Last modified: April 16, 2014
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot