G3V450 · G3V450_HUMAN
- Proteinnucleoside diphosphate phosphatase
- GeneENTPD5
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids211 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Hydrolyzes nucleoside diphosphates with a preference for GDP, IDP and UDP compared to ADP and CDP. In the lumen of the endoplasmic reticulum, hydrolyzes UDP that acts as an end-product feedback inhibitor of the UDP-Glc:glycoprotein glucosyltransferases. UMP can be transported back by an UDP-sugar antiporter to the cytosol where it is consumed to regenerate UDP-glucose. Therefore, it positively regulates protein reglucosylation by clearing UDP from the ER lumen and by promoting the regeneration of UDP-glucose. Protein reglucosylation is essential to proper glycoprotein folding and quality control in the ER.
Catalytic activity
- ADP + H2O = AMP + phosphate + H+This reaction proceeds in the forward direction.
Cofactor
Protein has several cofactor binding sites:
Pathway
Protein modification; protein glycosylation.
Features
Showing features for active site, binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | ATP binding | |
Molecular Function | hydrolase activity |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namenucleoside diphosphate phosphatase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionG3V450
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-20 | |||||
Sequence: MATSWGTVFFMLVVSCVCSA | ||||||
Chain | PRO_5003457299 | 21-211 | nucleoside diphosphate phosphatase | |||
Sequence: VSHRNQQTWFEGIFLSSMCPINVSASTLYGIMFDAGSTGTRIHVYTFVQKMPGQLPILEGEVFDSVKPGLSAFVDQPKQGAETVQGLLEVAKDSIPRSHWKKTPVVLKATAGLRLLPEHKAKALLFEVKEIFRKSPFLVPKGSVSIMDGSDEGILAWVTVNFLTGQLHGHRQETVGTLDLGGASTQITFLP |
Keywords
- PTM
Proteomic databases
Expression
Gene expression databases
Interaction
Subunit
Monomer; active form. Homodimer; disulfide-linked. Homodimers are enzymatically inactive.
Structure
Sequence
- Sequence statusFragment
- Length211
- Mass (Da)22,969
- Last updated2011-11-16 v1
- Checksum3FA17DF3A4BE2C48
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Features
Showing features for non-terminal residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-terminal residue | 211 | |||||
Sequence: P |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC005480 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC005484 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |