P25353 · NPP1_YEAST
- ProteinEctonucleotide pyrophosphatase/phosphodiesterase 1
- GeneNPP1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids742 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Mediates extracellular nucleotide derived phosphate hydrolysis along with NPP2 and PHO5.
Miscellaneous
Present with 3420 molecules/cell in log phase SD medium.
Catalytic activity
- a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-phosphate + diphosphate + H+
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 219 | Nucleophile | ||||
Sequence: T |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | membrane | |
Molecular Function | nucleoside triphosphate diphosphatase activity | |
Molecular Function | phosphodiesterase I activity | |
Molecular Function | ribonucleoside triphosphate phosphatase activity | |
Biological Process | cellular response to phosphate starvation | |
Biological Process | nucleoside triphosphate metabolic process |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameEctonucleotide pyrophosphatase/phosphodiesterase 1
- Short namesE-NPP 1
Including 2 domains:
- Recommended nameAlkaline phosphodiesterase 1
- EC number
- Recommended nameNucleotide pyrophosphatase
- EC number
- Short namesNPPase
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP25353
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Single-pass type II membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-113 | Cytoplasmic | ||||
Sequence: MELQNDLESLDNELNDFSEDPFRDDFITDEDAVRSGWRSAWTRMKYWFYKNRLKWTNNPIVIGDAKDSRDGSNFRRGIPLYELDANGQPIDTELVDENELSFGTGFHSKVPFK | ||||||
Transmembrane | 114-134 | Helical | ||||
Sequence: IIFRTLFGSLVFAIFLILMIN | ||||||
Topological domain | 135-742 | Extracellular | ||||
Sequence: IAKPHHSTRVLSHFGSPEFDPYVKYFNGTHEFFPLTIVISLDGFHPSLISKRNTPFLHDLYELKYDGGMNITSTPFMVPSFPTETFPNHWTLVTGQYPIHHGIVSNVFWDPDLNEEFHPGVLDPRIWNNNDTEPIWQTVQSAFDGDIPFKAATHMWPGSDVNYTKYNEEKLQPEHKNPIARERTPFYFDEFNAKEPLSQKLSKIIEYVDMSTLNERPQLILGYVPNVDAFGHKHGYPSESEYYYEDFTETLGEVDTFLKQLVESLQERNLTSFTNLVIVSDHGMSDIVVPSNVIIWEDLLDEKLRKDYVSHAYLEGPMMAISLKDSGNINEVYHNLKTSIDEDKYTVYVNGNFPKEWNFNDGKNHHMASIWIVPEPGYAVMKKEQLKKVAKGDHKDKNEDNVFTIGSHGYDNNAIDMRSVFIGMGPYFPQGYIEPFQNTEIYNLLCDICGVAEKDRNSNDGTGMLMNQLREPQSSEEVEIEDDFDYLVSKFGEFSTYNIIWGGYPEETEQDNVDNDNDDNDDGNTDEIAAMPSSSLTIKLEMTTSIPSATETLLGETSPSSRSSSSSSIQASATASTVGDWLQDIINDAKDLIDDIIDSIDDLVDSDT |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000202566 | 1-742 | Ectonucleotide pyrophosphatase/phosphodiesterase 1 | |||
Sequence: MELQNDLESLDNELNDFSEDPFRDDFITDEDAVRSGWRSAWTRMKYWFYKNRLKWTNNPIVIGDAKDSRDGSNFRRGIPLYELDANGQPIDTELVDENELSFGTGFHSKVPFKIIFRTLFGSLVFAIFLILMINIAKPHHSTRVLSHFGSPEFDPYVKYFNGTHEFFPLTIVISLDGFHPSLISKRNTPFLHDLYELKYDGGMNITSTPFMVPSFPTETFPNHWTLVTGQYPIHHGIVSNVFWDPDLNEEFHPGVLDPRIWNNNDTEPIWQTVQSAFDGDIPFKAATHMWPGSDVNYTKYNEEKLQPEHKNPIARERTPFYFDEFNAKEPLSQKLSKIIEYVDMSTLNERPQLILGYVPNVDAFGHKHGYPSESEYYYEDFTETLGEVDTFLKQLVESLQERNLTSFTNLVIVSDHGMSDIVVPSNVIIWEDLLDEKLRKDYVSHAYLEGPMMAISLKDSGNINEVYHNLKTSIDEDKYTVYVNGNFPKEWNFNDGKNHHMASIWIVPEPGYAVMKKEQLKKVAKGDHKDKNEDNVFTIGSHGYDNNAIDMRSVFIGMGPYFPQGYIEPFQNTEIYNLLCDICGVAEKDRNSNDGTGMLMNQLREPQSSEEVEIEDDFDYLVSKFGEFSTYNIIWGGYPEETEQDNVDNDNDDNDDGNTDEIAAMPSSSLTIKLEMTTSIPSATETLLGETSPSSRSSSSSSIQASATASTVGDWLQDIINDAKDLIDDIIDSIDDLVDSDT | ||||||
Glycosylation | 161 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 204 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 264 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 296 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 403 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
Autophosphorylated as part of the catalytic cycle of phosphodiesterase/pyrophosphatase activity.
N-glycosylated.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Induction
Up-regulated during phosphate starvation.
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 168-545 | Phosphodiesterase | ||||
Sequence: PLTIVISLDGFHPSLISKRNTPFLHDLYELKYDGGMNITSTPFMVPSFPTETFPNHWTLVTGQYPIHHGIVSNVFWDPDLNEEFHPGVLDPRIWNNNDTEPIWQTVQSAFDGDIPFKAATHMWPGSDVNYTKYNEEKLQPEHKNPIARERTPFYFDEFNAKEPLSQKLSKIIEYVDMSTLNERPQLILGYVPNVDAFGHKHGYPSESEYYYEDFTETLGEVDTFLKQLVESLQERNLTSFTNLVIVSDHGMSDIVVPSNVIIWEDLLDEKLRKDYVSHAYLEGPMMAISLKDSGNINEVYHNLKTSIDEDKYTVYVNGNFPKEWNFNDGKNHHMASIWIVPEPGYAVMKKEQLKKVAKGDHKDKNEDNVFTIGSHGYD | ||||||
Region | 640-670 | Disordered | ||||
Sequence: EETEQDNVDNDNDDNDDGNTDEIAAMPSSSL | ||||||
Compositional bias | 643-659 | Acidic residues | ||||
Sequence: EQDNVDNDNDDNDDGNT | ||||||
Region | 686-711 | Disordered | ||||
Sequence: TLLGETSPSSRSSSSSSIQASATAST |
Sequence similarities
Belongs to the nucleotide pyrophosphatase/phosphodiesterase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length742
- Mass (Da)84,734
- Last updated2003-06-27 v2
- Checksum83BD5F00D69B09C5
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 643-659 | Acidic residues | ||||
Sequence: EQDNVDNDNDDNDDGNT |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X59720 EMBL· GenBank· DDBJ | CAC42978.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006937 EMBL· GenBank· DDBJ | DAA07505.1 EMBL· GenBank· DDBJ | Genomic DNA |