P69476 · NEP1_NEPDI

Function

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.
    EC:3.4.23.12 (UniProtKB | ENZYME | Rhea)

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.

116420406080100120140160
TypeIDPosition(s)Description
Active site35

GO annotations

AspectTerm
Cellular Componentextracellular region
Molecular Functionaspartic-type endopeptidase activity
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Aspartic proteinase nepenthesin-1
  • EC number
  • Alternative names
    • Nepenthesin-I

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > Caryophyllales > Nepenthaceae > Nepenthes

Accessions

  • Primary accession
    P69476

Subcellular Location

Keywords

Phenotypes & Variants

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variant31

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.

Go to variant viewer

PTM/Processing

Features

Showing features for chain, glycosylation.

TypeIDPosition(s)Description
ChainPRO_00001995131-164Aspartic proteinase nepenthesin-1
Glycosylation93N-linked (GlcNAc...) asparagine

Keywords

Expression

Tissue specificity

Parenchymal cells surrounding the secretory glands.

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain17-164Peptidase A1
Region50-82Disordered

Sequence similarities

Belongs to the peptidase A1 family.

Family and domain databases

Sequence

  • Sequence status
    Fragments
  • Length
    164
  • Mass (Da)
    17,271
  • Last updated
    2005-03-15 v1
  • Checksum
    60C08491850E4F08
IGPSGVETTVYAGDGEYLMXLSIGTPAQPFSAIMDTGSDLIWTQXQPXTQXFXQSDPQGSSSFSTLPCGYGDSETQGSMGTETFTFGSVSIPNITFGXGEGPLPLPXQLDVAKYITLDLPIDPSAFDLCFQTPSDPSNLQIPTFVMHFDTGNSVVSFVSAQCGA

Features

Showing features for non-adjacent residues, non-terminal residue.

TypeIDPosition(s)Description
Non-adjacent residues55-56
Non-adjacent residues72-73
Non-adjacent residues100-101
Non-adjacent residues113-114
Non-adjacent residues118-119
Non-adjacent residues126-127
Non-adjacent residues148-149
Non-terminal residue164

Keywords

Similar Proteins

Disclaimer

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