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Q5EA65 (GPT_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

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 By similarity.

Catalytic activity

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

Pathway

Protein modification; protein glycosylation.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.

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_0000314781

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

Experimental info

Sequence conflict3121G → D in AAI02418. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q5EA65 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: 9BD875493287FB1C

FASTA40846,045
        10         20         30         40         50         60 
MWAFPELPMP LLVNLIGSLM GFVATVTLIP AFRGHFIAAR LCGQDLNKSS REQIPESQGV 

        70         80         90        100        110        120 
ISGAVFLIIL FCFIPFPFLN CFVEQQCKAF PHHEFVALIG ALLAICCMIF LGFADDVLNL 

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

       190        200        210        220        230        240 
TNAINILAGI NGLEAGQSLV ISASIIVFNL VELDGDYRDD HIFSLYFMIP FFFTTLGLLY 

       250        260        270        280        290        300 
HNWYPSRVFV GDTFCYFAGM TFAVVGILGH FSKTMLLFFM PQVFNFLYSL PQLLHIIPCP 

       310        320        330        340        350        360 
RHRMPRLNTK TGKLEMSYSK FKTKSLSFLG TFILKVAENL GLLTVRHSED EDGAFTECNN 

       370        380        390        400 
MTLINLLLKV FGPMHERNLT LLLLLLQVVG SAVTFSIRYQ LVRLFYDV 

« Hide

References

[1]"Characterization of 954 bovine full-CDS cDNA sequences."
Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.
BMC Genomics 6:166-166(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[2]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Crossbred X Angus.
Tissue: Ileum.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BT020704 mRNA. Translation: AAX08721.1.
BC102417 mRNA. Translation: AAI02418.1.
RefSeqNP_001015664.1. NM_001015664.1.
UniGeneBt.5711.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ5EA65.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000007065; ENSBTAP00000007065; ENSBTAG00000005371.
GeneID537812.
KEGGbta:537812.

Organism-specific databases

CTD1798.

Phylogenomic databases

eggNOGCOG0472.
GeneTreeENSGT00390000011424.
HOGENOMHOG000163915.
HOVERGENHBG000846.
InParanoidQ5EA65.
KOK01001.
OMAIHERNLT.
OrthoDBEOG73804W.
TreeFamTF313734.

Enzyme and pathway databases

UniPathwayUPA00378.

Family and domain databases

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

Other

NextBio20877222.

Entry information

Entry nameGPT_BOVIN
AccessionPrimary (citable) accession number: Q5EA65
Secondary accession number(s): Q3T0F3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 15, 2005
Last modified: April 16, 2014
This is version 60 of the entry and version 1 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