P42881 (GPT_SCHPO) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 96.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames 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 |
| ||||||
| Organism | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome] | ||||||
| Taxonomic identifier | 284812 [NCBI] | ||||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces › ![]() |
Protein attributes
| Sequence length | 446 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
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 | Inhibited by tunicamycin. |
| Pathway | |
| Subcellular location | Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity. |
| Sequence similarities | Belongs to the glycosyltransferase 4 family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Endoplasmic reticulum Membrane |
| Domain | Transmembrane Transmembrane helix |
| Molecular function | Glycosyltransferase Transferase |
| PTM | Glycoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | N-glycan processing Inferred from mutant phenotype Ref.1. Source: PomBase dolichyl diphosphate biosynthetic processInferred from mutant phenotype Ref.1. Source: PomBase |
| Cellular_component | integral to endoplasmic reticulum membrane Inferred by curator. Source: PomBase |
| Molecular_function | UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity Inferred from mutant phenotype PubMed 9455919. Source: PomBase phospho-N-acetylmuramoyl-pentapeptide-transferase activityInferred from electronic annotation. Source: InterPro transferase activity, transferring glycosyl groupsInferred 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 – 446 | 446 | UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase | PRO_0000108764 | |||||
Regions | |||||||||
| Transmembrane | 1 – 21 | 21 | Helical; Potential | ||||||
| Transmembrane | 25 – 45 | 21 | Helical; Potential | ||||||
| Transmembrane | 73 – 93 | 21 | Helical; Potential | ||||||
| Transmembrane | 123 – 143 | 21 | Helical; Potential | ||||||
| Transmembrane | 155 – 175 | 21 | Helical; Potential | ||||||
| Transmembrane | 191 – 211 | 21 | Helical; Potential | ||||||
| Transmembrane | 216 – 236 | 21 | Helical; Potential | ||||||
| Transmembrane | 254 – 274 | 21 | Helical; Potential | ||||||
| Transmembrane | 282 – 302 | 21 | Helical; Potential | ||||||
| Transmembrane | 311 – 331 | 21 | Helical; Potential | ||||||
| Transmembrane | 412 – 432 | 21 | Helical; Potential | ||||||
Amino acid modifications | |||||||||
| Glycosylation | 395 | 1 | N-linked (GlcNAc...) Potential | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Asparagine-linked glycosylation in Schizosaccharomyces pombe: functional conservation of the first step in oligosaccharide-lipid assembly." Zou J., Scocca J.R., Krag S.S. Arch. Biochem. Biophys. 317:487-496(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 972 / ATCC 24843. |
| [2] | "The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. Nurse P.Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 972 / ATCC 24843. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U09454 Genomic DNA. Translation: AAA92799.1. CU329671 Genomic DNA. Translation: CAA20479.1. |
| PIR | S71622. |
| RefSeq | NP_596244.1. NM_001022163.2. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 4896.SPBC15D4.04-1. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblFungi | SPBC15D4.04.1; SPBC15D4.04.1:pep; SPBC15D4.04. |
| GeneID | 2539795. |
| KEGG | spo:SPBC15D4.04. |
Organism-specific databases | |
| PomBase | SPBC15D4.04. |
Phylogenomic databases | |
| eggNOG | COG0472. |
| HOGENOM | HOG000163915. |
| KO | K01001. |
| OMA | PFLNCFV. |
| OrthoDB | EOG4BK8CS. |
Enzyme and pathway databases | |
| UniPathway | UPA00378. |
Family and domain databases | |
| InterPro | IPR000715. Glycosyl_transferase_4. [Graphical view] |
| Pfam | PF00953. Glycos_transf_4. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 20800944. |
Entry information
| Entry name | GPT_SCHPO | ||||||||
| Accession | Primary (citable) accession number: P42881 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Fungal Protein Annotation Program | ||||||||
Relevant documents
| Schizosaccharomyces pombe Schizosaccharomyces pombe: entries and gene names |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
