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P23338

- GPT_CRILO

UniProt

P23338 - GPT_CRILO

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Protein

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

Gene

DPAGT1

Organism
Cricetulus longicaudatus (Long-tailed dwarf hamster) (Chinese hamster)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli

Functioni

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

Catalytic activityi

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

Enzyme regulationi

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

Pathwayi

GO - Molecular functioni

  1. phospho-N-acetylmuramoyl-pentapeptide-transferase activity Source: InterPro
  2. transferase activity, transferring glycosyl groups Source: UniProtKB-KW
  3. UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. protein glycosylation Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

UniPathwayiUPA00378.

Names & Taxonomyi

Protein namesi
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 namesi
Name:DPAGT1
Synonyms:DPAGT2, GNPTA
OrganismiCricetulus longicaudatus (Long-tailed dwarf hamster) (Chinese hamster)
Taxonomic identifieri10030 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeCricetulus

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB-KW
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 408408UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferasePRO_0000108759Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi146 – 1461N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Structurei

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66LumenalSequence Analysis
Topological domaini33 – 5725CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini80 – 9415LumenalSequence AnalysisAdd
BLAST
Topological domaini115 – 12511CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini146 – 16419LumenalSequence AnalysisAdd
BLAST
Topological domaini185 – 19410CytoplasmicSequence Analysis
Topological domaini212 – 22110LumenalSequence Analysis
Topological domaini241 – 25212CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini270 – 2745LumenalSequence Analysis
Topological domaini295 – 37884CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini398 – 40811LumenalSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei7 – 3226HelicalSequence AnalysisAdd
BLAST
Transmembranei58 – 7922HelicalSequence AnalysisAdd
BLAST
Transmembranei95 – 11420HelicalSequence AnalysisAdd
BLAST
Transmembranei126 – 14520HelicalSequence AnalysisAdd
BLAST
Transmembranei165 – 18420HelicalSequence AnalysisAdd
BLAST
Transmembranei195 – 21117HelicalSequence AnalysisAdd
BLAST
Transmembranei222 – 24019HelicalSequence AnalysisAdd
BLAST
Transmembranei253 – 26917HelicalSequence AnalysisAdd
BLAST
Transmembranei275 – 29420HelicalSequence AnalysisAdd
BLAST
Transmembranei379 – 39719HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi67 – 7913Dolichol recognitionAdd
BLAST
Motifi222 – 23413Dolichol recognitionAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyltransferase 4 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG000846.

Family and domain databases

InterProiIPR000715. Glycosyl_transferase_4.
[Graphical view]
PfamiPF00953. Glycos_transf_4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P23338-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MWAFPELPLP LLVNLFGSLL GFVATVTLIP AFRSHFIAAR LCGQDLNKLS
60 70 80 90 100
RQQIPESQGV ICGAVFLIIL FCFIPFPFLN CFVEEQCKAF PHHEFVALIG
110 120 130 140 150
ALLAICCMIF LGFADDVLNL PWRHKLLLPT AASLPLLMVY FTNFGNTTIV
160 170 180 190 200
VPKPFRWILG LHLDLGILYY VYMGLLAVFC TNAINILAGI NGLEAGQSLV
210 220 230 240 250
ISASIIVFNL VELEGDYRDD HVFSLYFMIP FFFTTLGLLY HNWYPSQVFV
260 270 280 290 300
GDTFCYFAGM TFAVVGILGH FSKTMLLFFI PQVFNFLYSL PQLLHAIPCP
310 320 330 340 350
RHRIPRLNPK TGKLEMSYSK FKTKNLSFLG TFILKVAERL QLVTVHRGES
360 370 380 390 400
EDGAFTECNN MTLINLLLKI FGPIHERNLT LLLLLLQILS SAVTFSIRYQ

LVRLFYDV
Length:408
Mass (Da):46,191
Last modified:November 1, 1991 - v1
Checksum:i108C4D7598B8F4F3
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J05590 mRNA. Translation: AAA36965.1.
PIRiA37813.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J05590 mRNA. Translation: AAA36965.1 .
PIRi A37813.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG000846.

Enzyme and pathway databases

UniPathwayi UPA00378 .

Family and domain databases

InterProi IPR000715. Glycosyl_transferase_4.
[Graphical view ]
Pfami PF00953. Glycos_transf_4. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Cloning, sequence, and expression of a cDNA encoding hamster UDP-GlcNAc:dolichol phosphate N-acetylglucosamine-1-phosphate transferase."
    Zhu X., Lehrman M.A.
    J. Biol. Chem. 265:14250-14255(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Amplification and molecular cloning of the hamster tunicamycin-sensitive N-acetylglucosamine-1-phosphate transferase gene. The hamster and yeast enzymes share a common peptide sequence."
    Lehrman M.A., Zhu X., Khounlo S.
    J. Biol. Chem. 263:19796-19803(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 248-271.

Entry informationi

Entry nameiGPT_CRILO
AccessioniPrimary (citable) accession number: P23338
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: October 29, 2014
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3