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Reviewed, UniProtKB/Swiss-Prot P69476 (NEP1_NEPDI)

Last modified June 16, 2009. Version 24. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Aspartic proteinase nepenthesin-1
    EC=3.4.23.12
Alternative name(s):
    Nepenthesin-I
OrganismNepenthes distillatoria (Pitcher plant)
Taxonomic identifier122309 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsCaryophyllalesNepenthaceaeNepenthes

Protein attributes

Sequence length164 AA.
Sequence statusFragments.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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.

Subcellular location

Secreted. Ref.1

Tissue specificity

Parenchymal cells surrounding the secretory glands. Ref.1

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 componentSecreted
   Coding sequence diversityPolymorphism
   Molecular functionAspartyl protease
Hydrolase
Protease
   PTMGlycoprotein
Zymogen
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionaspartic-type endopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›164›164Aspartic proteinase nepenthesin-1
PRO_0000199513

Sites

Active site351 By similarity

Amino acid modifications

Glycosylation931N-linked (GlcNAc...) Potential

Natural variations

Natural variant311S → Y

Experimental info

Non-adjacent residues55 – 562
Non-adjacent residues72 – 732
Non-adjacent residues100 – 1012
Non-adjacent residues113 – 1142
Non-adjacent residues118 – 1192
Non-adjacent residues126 – 1272
Non-adjacent residues148 – 1492
Non-terminal residue1641

Sequences

Sequence LengthMass (Da)Tools
P69476-1 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: 60C08491850E4F08

FASTA16417,271
        10         20         30         40         50         60 
IGPSGVETTV YAGDGEYLMX LSIGTPAQPF SAIMDTGSDL IWTQXQPXTQ XFXQSDPQGS 

        70         80         90        100        110        120 
SSFSTLPCGY GDSETQGSMG TETFTFGSVS IPNITFGXGE GPLPLPXQLD VAKYITLDLP 

       130        140        150        160 
IDPSAFDLCF QTPSDPSNLQ IPTFVMHFDT GNSVVSFVSA QCGA 

« Hide

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: PARTIAL PROTEIN SEQUENCE, CHARACTERIZATION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, VARIANT TYR-31.
Tissue: Pitcher.

Cross-references

3D structure databases

ModBaseSearch...

Enzyme and pathway databases

BRENDA3.4.23.12. 275086.

Family and domain databases

InterProIPR001461. Peptidase_A1.
IPR001969. Peptidase_aspartic_AS.
[Graphical view]
PANTHERPTHR13683. Peptidase_A1. 1 hit.
PfamPF00026. Asp. 1 hit.
[Graphical view]
PROSITEPS00141. ASP_PROTEASE. Partial match.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNEP1_NEPDI
AccessionPrimary (citable) accession number: P69476
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: June 16, 2009
This is version 24 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents