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Reviewed, UniProtKB/Swiss-Prot Q766C2 (NEP2_NEPGR)

Last modified July 22, 2008. Version 25. 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-2
    EC=3.4.23.12
Alternative name(s):
    Nepenthesin-II
Gene names
Name: nep2
OrganismNepenthes gracilis (Slender pitcher plant)
Taxonomic identifier150966 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsCaryophyllalesNepenthaceaeNepenthes

Protein attributes

Sequence length438 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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 Cu(2+) ions By similarity.

Subcellular location

SecretedBy similarity.

Sequence similarities

Belongs to the peptidase A1 family.

Biophysicochemical properties

pH dependence:

Optimum pH is 3.0. Retains 80% and 60% of the original activity after incubation for 30 days at pH 3.0 and pH 4.0 respectively. Unstable at pH higher than 5.0.

Temperature dependence:

Optimum temperature is 45 degrees Celsius. Thermostable up to 50 degrees Celsius. Retains 44% of the original activity after incubation for 30 days at 50 degrees Celsius.

Ontologies

Keywords

   Cellular componentSecreted
   DomainSignal
   Molecular functionAspartyl protease
Hydrolase
Protease
   PTMGlycoprotein
Zymogen

Gene Ontology (GO)

None. [Check GOA]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Signal peptide1 – 2424 Potential
Propeptide25 – 7955Activation peptide By similarity
Chain80 – 438359Aspartic proteinase nepenthesin-2

Sites

Active site1141 By similarity
Active site3151 By similarity

Amino acid modifications

Glycosylation541N-linked (GlcNAc...) Potential
Disulfide bond124 ↔ 127 Probable
Disulfide bond130 ↔ 204 Probable
Disulfide bond151 ↔ 169 Probable
Disulfide bond156 ↔ 164 Probable
Disulfide bond241 ↔ 435 Probable
Disulfide bond354 ↔ 395 Probable

Sequences

Sequence LengthMass (Da)Tools
Q766C2-1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 91C2A79C28123A50

FASTA43846,174
        10         20         30         40         50         60 
MASPLYSVVL GLAIVSAIVA PTSSTSRGTL LHHGQKRPQP GLRVDLEQVD SGKNLTKYEL 

        70         80         90        100        110        120 
IKRAIKRGER RMRSINAMLQ SSSGIETPVY AGDGEYLMNV AIGTPDSSFS AIMDTGSDLI 

       130        140        150        160        170        180 
WTQCEPCTQC FSQPTPIFNP QDSSSFSTLP CESQYCQDLP SETCNNNECQ YTYGYGDGST 

       190        200        210        220        230        240 
TQGYMATETF TFETSSVPNI AFGCGEDNQG FGQGNGAGLI GMGWGPLSLP SQLGVGQFSY 

       250        260        270        280        290        300 
CMTSYGSSSP STLALGSAAS GVPEGSPSTT LIHSSLNPTY YYITLQGITV GGDNLGIPSS 

       310        320        330        340        350        360 
TFQLQDDGTG GMIIDSGTTL TYLPQDAYNA VAQAFTDQIN LPTVDESSSG LSTCFQQPSD 

       370        380        390        400        410        420 
GSTVQVPEIS MQFDGGVLNL GEQNILISPA EGVICLAMGS SSQLGISIFG NIQQQETQVL 

       430 
YDLQNLAVSF VPTQCGAS 

« 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: NUCLEOTIDE SEQUENCE [MRNA], 3D-STRUCTURE MODELING, CHARACTERIZATION.
Tissue: Pitcher.

Cross-references

Sequence databases

AB114915 mRNA. Translation: BAD07475.1.

3D structure databases

HSSPHSSP built from PDB template 1AVF based on UniProtKB P20142.
ModBaseSearch...

Protein family/group databases

MEROPSA01.040.

Family and domain databases

InterProIPR001969. Pept_Asp_AS.
IPR009007. Pept_Aspartc_cat.
IPR001461. Peptidase_A1.
[Graphical view]
Gene3DG3DSA:2.40.70.10. Pept_Aspartc_cat. 1 hit.
PANTHERPTHR13683. Peptidase_A1. 1 hit.
PfamPF00026. Asp. 1 hit.
[Graphical view]
PRINTSPR00792. PEPSIN.
PROSITEPS00141. ASP_PROTEASE. 1 hit.
[Graphical view]
ProDomQ766C2.
[Graphical view] [Entries sharing at least one domain]
BLOCKSSearch...

Other Resources

ProtoNetSearch...

Entry information

Entry nameNEP2_NEPGR
AccessionPrimary (citable) accession number: Q766C2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: July 5, 2004
Last modified: July 22, 2008
This is version 25 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