P69476 · NEP1_NEPDI
- ProteinAspartic proteinase nepenthesin-1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids164 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Extracellular proteinase found in the pitcher fluid of carnivorous plants. Digest prey for nitrogen uptake.
Catalytic activity
Activity regulation
Inhibited by pepstatin and by diazoacetyl-D,L-norleucine methyl ester (DAN) in the presence of Cu2+ ions.
pH Dependence
Optimum pH is 2.6. Retains 95% and 79% of the original activity after incubation for 30 days at pH 3.0 and pH 10.0 respectively.
Temperature Dependence
Optimum temperature is 55 degrees Celsius. Thermostable up to 50 degrees Celsius. Retains 60% of the original activity after incubation for 30 days at 50 degrees Celsius.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 35 | |||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | aspartic-type endopeptidase activity | |
Biological Process | proteolysis |
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameAspartic proteinase nepenthesin-1
- EC number
- Alternative names
Organism names
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > Caryophyllales > Nepenthaceae > Nepenthes
Accessions
- Primary accessionP69476
Subcellular Location
Phenotypes & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | 31 | |||||
Sequence: S → Y |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1 variant from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000199513 | 1-164 | Aspartic proteinase nepenthesin-1 | |||
Sequence: IGPSGVETTVYAGDGEYLMXLSIGTPAQPFSAIMDTGSDLIWTQXQPXTQXFXQSDPQGSSSFSTLPCGYGDSETQGSMGTETFTFGSVSIPNITFGXGEGPLPLPXQLDVAKYITLDLPIDPSAFDLCFQTPSDPSNLQIPTFVMHFDTGNSVVSFVSAQCGA | ||||||
Glycosylation | 93 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Expression
Tissue specificity
Parenchymal cells surrounding the secretory glands.
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 17-164 | Peptidase A1 | ||||
Sequence: YLMXLSIGTPAQPFSAIMDTGSDLIWTQXQPXTQXFXQSDPQGSSSFSTLPCGYGDSETQGSMGTETFTFGSVSIPNITFGXGEGPLPLPXQLDVAKYITLDLPIDPSAFDLCFQTPSDPSNLQIPTFVMHFDTGNSVVSFVSAQCGA | ||||||
Region | 50-82 | Disordered | ||||
Sequence: QXFXQSDPQGSSSFSTLPCGYGDSETQGSMGTE |
Sequence similarities
Belongs to the peptidase A1 family.
Family and domain databases
Sequence
- Sequence statusFragments
- Length164
- Mass (Da)17,271
- Last updated2005-03-15 v1
- Checksum60C08491850E4F08
Features
Showing features for non-adjacent residues, non-terminal residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-adjacent residues | 55-56 | |||||
Sequence: SD | ||||||
Non-adjacent residues | 72-73 | |||||
Sequence: DS | ||||||
Non-adjacent residues | 100-101 | |||||
Sequence: EG | ||||||
Non-adjacent residues | 113-114 | |||||
Sequence: KY | ||||||
Non-adjacent residues | 118-119 | |||||
Sequence: DL | ||||||
Non-adjacent residues | 126-127 | |||||
Sequence: FD | ||||||
Non-adjacent residues | 148-149 | |||||
Sequence: FD | ||||||
Non-terminal residue | 164 | |||||
Sequence: A |
Keywords
- Technical term