Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Aspartic proteinase nepenthesin-2

Gene

nep2

Organism
Nepenthes gracilis (Slender pitcher plant)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Extracellular proteinase found in the pitcher fluid of carnivorous plants. Digest prey for nitrogen uptake.

Catalytic activityi

Similar to pepsin, but also cleaves on either side of Asp and at Lys-|-Arg.

Enzyme regulationi

Inhibited by pepstatin and by diazoacetyl-D,L-norleucine methyl ester (DAN) in the presence of Cu2+ ions.By similarity

pH dependencei

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 dependencei

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei114 – 1141PROSITE-ProRule annotation
Active sitei315 – 3151PROSITE-ProRule annotation

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Aspartyl protease, Hydrolase, Protease

Protein family/group databases

MEROPSiA01.040.

Names & Taxonomyi

Protein namesi
Recommended name:
Aspartic proteinase nepenthesin-2 (EC:3.4.23.12)
Alternative name(s):
Nepenthesin-II
Gene namesi
Name:nep2
OrganismiNepenthes gracilis (Slender pitcher plant)
Taxonomic identifieri150966 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesNepenthaceaeNepenthes

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence analysisAdd
BLAST
Propeptidei25 – 7955Activation peptideBy similarityPRO_0000025916Add
BLAST
Chaini80 – 438359Aspartic proteinase nepenthesin-2PRO_0000025917Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi54 – 541N-linked (GlcNAc...)Sequence analysis
Disulfide bondi124 ↔ 127Curated
Disulfide bondi130 ↔ 204Curated
Disulfide bondi151 ↔ 169Curated
Disulfide bondi156 ↔ 164Curated
Disulfide bondi241 ↔ 435Curated
Disulfide bondi354 ↔ 395Curated

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Structurei

3D structure databases

ProteinModelPortaliQ766C2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini96 – 431336Peptidase A1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase A1 family.Curated
Contains 1 peptidase A1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.40.70.10. 2 hits.
InterProiIPR001461. Aspartic_peptidase_A1.
IPR001969. Aspartic_peptidase_AS.
IPR033121. PEPTIDASE_A1.
IPR021109. Peptidase_aspartic_dom.
IPR032799. TAXi_C.
IPR032861. TAXi_N.
[Graphical view]
PANTHERiPTHR13683. PTHR13683. 1 hit.
PfamiPF14541. TAXi_C. 1 hit.
PF14543. TAXi_N. 1 hit.
[Graphical view]
PRINTSiPR00792. PEPSIN.
SUPFAMiSSF50630. SSF50630. 1 hit.
PROSITEiPS00141. ASP_PROTEASE. 1 hit.
PS51767. PEPTIDASE_A1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q766C2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASPLYSVVL GLAIVSAIVA PTSSTSRGTL LHHGQKRPQP GLRVDLEQVD
60 70 80 90 100
SGKNLTKYEL IKRAIKRGER RMRSINAMLQ SSSGIETPVY AGDGEYLMNV
110 120 130 140 150
AIGTPDSSFS AIMDTGSDLI WTQCEPCTQC FSQPTPIFNP QDSSSFSTLP
160 170 180 190 200
CESQYCQDLP SETCNNNECQ YTYGYGDGST TQGYMATETF TFETSSVPNI
210 220 230 240 250
AFGCGEDNQG FGQGNGAGLI GMGWGPLSLP SQLGVGQFSY CMTSYGSSSP
260 270 280 290 300
STLALGSAAS GVPEGSPSTT LIHSSLNPTY YYITLQGITV GGDNLGIPSS
310 320 330 340 350
TFQLQDDGTG GMIIDSGTTL TYLPQDAYNA VAQAFTDQIN LPTVDESSSG
360 370 380 390 400
LSTCFQQPSD GSTVQVPEIS MQFDGGVLNL GEQNILISPA EGVICLAMGS
410 420 430
SSQLGISIFG NIQQQETQVL YDLQNLAVSF VPTQCGAS
Length:438
Mass (Da):46,174
Last modified:July 5, 2004 - v1
Checksum:i91C2A79C28123A50
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB114915 mRNA. Translation: BAD07475.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB114915 mRNA. Translation: BAD07475.1.

3D structure databases

ProteinModelPortaliQ766C2.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiA01.040.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di2.40.70.10. 2 hits.
InterProiIPR001461. Aspartic_peptidase_A1.
IPR001969. Aspartic_peptidase_AS.
IPR033121. PEPTIDASE_A1.
IPR021109. Peptidase_aspartic_dom.
IPR032799. TAXi_C.
IPR032861. TAXi_N.
[Graphical view]
PANTHERiPTHR13683. PTHR13683. 1 hit.
PfamiPF14541. TAXi_C. 1 hit.
PF14543. TAXi_N. 1 hit.
[Graphical view]
PRINTSiPR00792. PEPSIN.
SUPFAMiSSF50630. SSF50630. 1 hit.
PROSITEiPS00141. ASP_PROTEASE. 1 hit.
PS51767. PEPTIDASE_A1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], 3D-STRUCTURE MODELING, CHARACTERIZATION.
    Tissue: Pitcher.

Entry informationi

Entry nameiNEP2_NEPGR
AccessioniPrimary (citable) accession number: Q766C2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: July 5, 2004
Last modified: April 13, 2016
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.