Q766C3 (NEP1_NEPGR) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 37.
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: Aspartic proteinase nepenthesin-1 EC=3.4.23.12 Alternative name(s): Nepenthesin-I | ||
| Gene names |
| ||
| Organism | Nepenthes gracilis (Slender pitcher plant) | ||
| Taxonomic identifier | 150966 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › Caryophyllales › Nepenthaceae › Nepenthes |
Protein attributes
| Sequence length | 437 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Extracellular proteinase found in the pitcher fluid of carnivorous plants. Digest prey for nitrogen uptake. |
| Catalytic activity | Similar to pepsin, but also cleaves on either side of Asp and at Lys-|-Arg. |
| Enzyme regulation | Inhibited by pepstatin and by diazoacetyl-D,L-norleucine methyl ester (DAN) in the presence of Cu2+ ions By similarity. |
| Subcellular location | Secreted By similarity. |
| Sequence similarities | Belongs to the peptidase A1 family. |
| Biophysicochemical properties | 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. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Secreted |
| Coding sequence diversity | Polymorphism |
| Domain | Signal |
| Molecular function | Aspartyl protease Hydrolase Protease |
| PTM | Disulfide bond Glycoprotein Zymogen |
| Gene Ontology (GO) | |
| Biological process | proteolysis Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | aspartic-type endopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 24 | 24 | Potential | ||||||||
| Propeptide | 25 – 78 | 54 | Activation peptide By similarity | PRO_0000025914 | |||||||
| Chain | 79 – 437 | 359 | Aspartic proteinase nepenthesin-1 | PRO_0000025915 | |||||||
Sites | |||||||||||
| Active site | 113 | 1 | By similarity | ||||||||
| Active site | 315 | 1 | By similarity | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 53 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 98 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 131 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 198 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 267 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 307 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 345 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 123 ↔ 126 | Probable | |||||||||
| Disulfide bond | 129 ↔ 203 | Probable | |||||||||
| Disulfide bond | 150 ↔ 168 | Probable | |||||||||
| Disulfide bond | 155 ↔ 163 | Probable | |||||||||
| Disulfide bond | 240 ↔ 434 | Probable | |||||||||
| Disulfide bond | 354 ↔ 395 | Probable | |||||||||
Natural variations | |||||||||||
| Natural variant | 233 | 1 | D → V in nepenthesin-1b. Ref.1 | ||||||||
| Natural variant | 251 | 1 | N → T in nepenthesin-1b. Ref.1 | ||||||||
| Natural variant | 392 | 1 | G → E in nepenthesin-1b. Ref.1 | ||||||||
Sequences
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References
| [1] | "Enzymic and structural characterization of nepenthesin, a unique member of a novel subfamily of aspartic proteinases." Athauda S.B.P., Matsumoto K., Rajapakshe S., Kuribayashi M., Kojima M., Kubomura-Yoshida N., Iwamatsu A., Shibata C., Inoue H., Takahashi K. Biochem. J. 381:295-306(2004) [PubMed: 15035659] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], 3D-STRUCTURE MODELING, CHARACTERIZATION, VARIANTS NEPENTHESIN IB VAL-233; THR-251 AND GLU-392. Tissue: Pitcher. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AB114914 mRNA. Translation: BAD07474.1. |
3D structure databases | |
| ProteinModelPortal | Q766C3. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | A01.040. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| InterPro | IPR001461. Peptidase_A1. IPR021109. Peptidase_aspartic. IPR001969. Peptidase_aspartic_AS. IPR009007. Peptidase_aspartic_catalytic. [Graphical view] |
| Gene3D | G3DSA:2.40.70.10. Pept_Aspartc_cat. 2 hits. |
| PANTHER | PTHR13683. Peptidase_A1. 1 hit. |
| Pfam | PF00026. Asp. 1 hit. [Graphical view] |
| PRINTS | PR00792. PEPSIN. |
| SUPFAM | SSF50630. Pept_Aspartic. 1 hit. |
| PROSITE | PS00141. ASP_PROTEASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | NEP1_NEPGR | ||||||||
| Accession | Primary (citable) accession number: Q766C3 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Plant Protein Annotation Program | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

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