UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase

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P42867 (GPT_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 104. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	410 AA.
Sequence status	Complete.
Protein existence	Evidence 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

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	RNA editing
Domain	Transmembrane Transmembrane helix
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	UDP-N-acetylglucosamine metabolic process Inferred from electronic annotation. Source: Compara dolichol biosynthetic process Inferred from electronic annotation. Source: Compara dolichol-linked oligosaccharide biosynthetic process Traceable author statement Ref.4. Source: MGI protein N-linked glycosylation Inferred from electronic annotation. Source: Compara
Cellular_component	endoplasmic reticulum membrane Traceable author statement Ref.1. Source: MGI integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity Inferred from direct assay Ref.1. Source: MGI UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase activity Inferred from sequence or structural similarity Ref.1. Source: MGI phospho-N-acetylmuramoyl-pentapeptide-transferase activity Inferred from electronic annotation. Source: InterPro transferase activity, transferring glycosyl groups Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 410

410

UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase

PRO_0000108762

Regions

Topological domain

1 – 6

Lumenal Potential

Transmembrane

7 – 34

Helical; Potential

Topological domain

35 – 59

Cytoplasmic Potential

Transmembrane

60 – 81

Helical; Potential

Topological domain

82 – 96

Lumenal Potential

Transmembrane

97 – 116

Helical; Potential

Topological domain

117 – 127

Cytoplasmic Potential

Transmembrane

128 – 147

Helical; Potential

Topological domain

148 – 166

Lumenal Potential

Transmembrane

167 – 186

Helical; Potential

Topological domain

187 – 196

Cytoplasmic Potential

Transmembrane

197 – 213

Helical; Potential

Topological domain

214 – 223

Lumenal Potential

Transmembrane

224 – 242

Helical; Potential

Topological domain

243 – 254

Cytoplasmic Potential

Transmembrane

255 – 271

Helical; Potential

Topological domain

272 – 276

Lumenal Potential

Transmembrane

277 – 296

Helical; Potential

Topological domain

297 – 380

Cytoplasmic Potential

Transmembrane

381 – 399

Helical; Potential

Topological domain

400 – 410

Lumenal Potential

Motif

69 – 81

Dolichol recognition

Motif

224 – 236

Dolichol recognition

Amino acid modifications

Glycosylation

148

N-linked (GlcNAc...) Potential

Natural variations

Natural variant

C → Y in RNA edited version.

Sequences

Sequence

Length

Mass (Da)

Tools

P42867 [UniParc].

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

FASTA

410

46,412

        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' referencesShow '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.
IPI	IPI00120705.
PIR	S24326.
RefSeq	NP_031901.2. NM_007875.2.
UniGene	Mm.18353.
3D structure databases
ModBase	Search...
PTM databases
PhosphoSite	P42867.
Proteomic databases
PaxDb	P42867.
PRIDE	P42867.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000054708; ENSMUSP00000056282; ENSMUSG00000032123.
GeneID	13478.
KEGG	mmu:13478.
UCSC	uc009pcv.1. mouse.
Organism-specific databases
CTD	1798.
MGI	MGI:1196396. Dpagt1.
Phylogenomic databases
eggNOG	COG0472.
GeneTree	ENSGT00390000011424.
HOGENOM	HOG000163915.
HOVERGEN	HBG000846.
InParanoid	P42867.
KO	K01001.
OMA	PFLNCFV.
OrthoDB	EOG4868CQ.
Enzyme and pathway databases
UniPathway	UPA00378.
Gene expression databases
ArrayExpress	P42867.
Bgee	P42867.
Genevestigator	P42867.
GermOnline	ENSMUSG00000032123. Mus musculus.
Family and domain databases
InterPro	IPR000715. Glycosyl_transferase_4. [Graphical view]
Pfam	PF00953. Glycos_transf_4. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	DPAGT1. mouse.
NextBio	283963.
SOURCE	Search...

Entry information

Entry name

GPT_MOUSE

Accession

Primary (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 3, 2013
This is version 104 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Sequences

References

Cross-references

Sequence databases

3D structure databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents