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P24140 (GPT_CRIGR) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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, GTR2
OrganismCricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Taxonomic identifier10029 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Cricetidae › Cricetinae › Cricetulus

Protein attributes

Sequence length408 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.

Sequence similarities

Belongs to the glycosyltransferase 4 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 408408UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase
PRO_0000108760

Regions

Topological domain1 – 66Lumenal Potential
Transmembrane7 – 3226Helical; Potential
Topological domain33 – 5725Cytoplasmic Potential
Transmembrane58 – 7922Helical; Potential
Topological domain80 – 9415Lumenal Potential
Transmembrane95 – 11420Helical; Potential
Topological domain115 – 12511Cytoplasmic Potential
Transmembrane126 – 14520Helical; Potential
Topological domain146 – 16419Lumenal Potential
Transmembrane165 – 18420Helical; Potential
Topological domain185 – 19410Cytoplasmic Potential
Transmembrane195 – 21117Helical; Potential
Topological domain212 – 22110Lumenal Potential
Transmembrane222 – 24019Helical; Potential
Topological domain241 – 25212Cytoplasmic Potential
Transmembrane253 – 26917Helical; Potential
Topological domain270 – 2745Lumenal Potential
Transmembrane275 – 29420Helical; Potential
Topological domain295 – 37884Cytoplasmic Potential
Transmembrane379 – 39719Helical; Potential
Topological domain398 – 40811Lumenal Potential
Motif67 – 7913Dolichol recognition
Motif222 – 23413Dolichol recognition

Amino acid modifications

Glycosylation1461N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
P24140 [UniParc].

Last modified March 1, 1992. Version 1.
Checksum: CB0FF5946C07BEF3

FASTA40846,250
        10         20         30         40         50         60 
MWAFPELPLP LLVNLFGSLL GFVATVTLIP AFRSHFIAAR LCGQDLNKLS RQQIPESQGV 

        70         80         90        100        110        120 
ICGAVFLIIL FCFIPFPFLN CFVEEQCKAF PHHEFVALIG ALLAICCMIF LGFADDVLNL 

       130        140        150        160        170        180 
RWRHKLLLPT AASLPLLMVY FTNFGNTTIV VPKPFRWILG LHLDLGILYY VYMGLLAVFC 

       190        200        210        220        230        240 
TNAINILAGI NGLEAGQSLV ISASIIVFNL VELEGDYRDD HVFSLYFMIP FFFTTLGLLY 

       250        260        270        280        290        300 
HNWYPSQVFV GDTFCYFAGM TFAVVGILGH FSKTMLLFFI PQVFNFLYSL PQLLHAIPCP 

       310        320        330        340        350        360 
RHRIPRLNPK TGKLEMSYSK FKTKNLSFLG TFILKVAERL QLVTVHRGES EDGAFTECNN 

       370        380        390        400 
MTLINLLLKI FGPIHERNLT LLLLLLQILS SAVTFSIRYQ LVRLFYDV

« Hide

References

[1]"Sequence of a cDNA that specifies the uridine diphosphate N-acetyl-D-glucosamine:dolichol phosphate N-acetylglucosamine-1-phosphate transferase from Chinese hamster ovary cells."
Scocca J.R., Krag S.S.
J. Biol. Chem. 265:20621-20626(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Ovary.
[2]"Genomic organization and expression of hamster UDP-N-acetylglucosamine:dolichyl phosphate N-acetylglucosaminyl phosphoryl transferase."
Scocca J.R., Zou J., Krag S.S.
Glycobiology 5:129-136(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M36899 mRNA. Translation: AAA37027.1.
U15161 Genomic DNA. Translation: AAA51872.1.
U09453 Genomic DNA. Translation: AAA85220.1.
RefSeqNP_001230970.1. NM_001244041.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100689054.

Organism-specific databases

CTD1798.

Phylogenomic databases

HOVERGENHBG000846.

Enzyme and pathway databases

UniPathwayUPA00378.

Family and domain databases

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

Entry information

Entry nameGPT_CRIGR
AccessionPrimary (citable) accession number: P24140
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: April 3, 2013
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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