Q766C2 (NEP2_NEPGR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Aspartic proteinase nepenthesin-2
EC=3.4.23.12

Alternative name(s):
Nepenthesin-II

Gene names

Name:

nep2

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	438 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 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
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 – 79	55	Activation peptide By similarity		PRO_0000025916
	Chain	80 – 438	359	Aspartic proteinase nepenthesin-2		PRO_0000025917
Sites
	Active site	114	1	By similarity
	Active site	315	1	By similarity
Amino acid modifications
	Glycosylation	54	1	N-linked (GlcNAc...) Potential
	Disulfide bond	124 ↔ 127		Probable
	Disulfide bond	130 ↔ 204		Probable
	Disulfide bond	151 ↔ 169		Probable
	Disulfide bond	156 ↔ 164		Probable
	Disulfide bond	241 ↔ 435		Probable
	Disulfide bond	354 ↔ 395		Probable

Sequences

	Sequence		Length	Mass (Da)
	Q766C2 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 91C2A79C28123A50	FASTA	438	46,174
	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

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
EMBL GenBank DDBJ	AB114915 mRNA. Translation: BAD07475.1.
3D structure databases
ProteinModelPortal	Q766C2.
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

NEP2_NEPGR

Accession

Primary (citable) accession number: Q766C2

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	July 5, 2004
Last modified:	November 16, 2011
This is version 39 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program