Reviewed, UniProtKB/Swiss-Prot P69477 (NEP2_NEPDI)

Names and origin

Protein names	Recommended name:     Aspartic proteinase nepenthesin-2     EC=3.4.23.12 Alternative name(s):     Nepenthesin-II
Organism	Nepenthes distillatoria (Pitcher plant)
Taxonomic identifier	122309 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › Caryophyllales › Nepenthaceae › Nepenthes

Protein attributes

Sequence length	178 AA.
Sequence status	Fragments.
Sequence processing	The displayed sequence is not processed.
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 Cu(2+) ions.
Subcellular location	Secreted.
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 component	Secreted
Coding sequence diversity	Polymorphism
Molecular function	Aspartyl protease Hydrolase Protease
PTM	Zymogen
Technical term	Direct protein sequencing
Gene Ontology (GO)
None. [Check GOA]

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Chain	1 – 178	178	Aspartic proteinase nepenthesin-2
Sites
	Active site	98	1	By similarity
Natural variations
	Natural variant	42	1	T → D
Experimental info
	Non-adjacent residues	18 – 19	2
	Non-adjacent residues	35 – 36	2
	Non-adjacent residues	58 – 59	2
	Non-adjacent residues	79 – 80	2
	Non-adjacent residues	92 – 93	2
	Non-adjacent residues	97 – 98	2
	Non-adjacent residues	161 – 162	2

Sequences

	Sequence		Length	Mass (Da)
	P69477-1 [UniParc]. Last modified March 15, 2005. Version 1. Checksum: 620B27F0EC3412E8	FASTA	178	19,106
	10 20 30 40 50 60 QTVQVEPPYY AGDGEYLMVD LIWTQCEPCT QCFSQDSSSF STLPCESQYC QDLPSETCDC 70 80 90 100 110 120 QYTYGYGDGS STQGYMAXED GSSVPNIAFG CGDNLQIDSG TTLTYLPQDA YNAVAQAFTD 130 140 150 160 170 QINLPTVDES SSGLSTCFQE PSDGSTVQVP EISMQDGGVL NDLQNLAVSF FPTQCGAS

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, SUBCELLULAR LOCATION, VARIANT ASP-42. Tissue: Pitcher.

Cross-references

3D structure databases
ModBase	Search...
Family and domain databases
InterPro	IPR001969. Pept_Asp_AS. IPR009007. Pept_Aspartc_cat. IPR001461. Peptidase_A1. [Graphical view]
Gene3D	G3DSA:2.40.70.10. Pept_Aspartc_cat. 1 hit.
PANTHER	PTHR13683. Peptidase_A1. 1 hit.
PROSITE	PS00141. ASP_PROTEASE. Partial match. [Graphical view]
BLOCKS	Search...
Other Resources
ProtoNet	Search...

Entry information

Entry name

NEP2_NEPDI

Accession

Primary (citable) accession number: P69477

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	March 15, 2005
Last modified:	July 22, 2008
This is version 17 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)