ID   NEP2_NEPDI              Reviewed;         178 AA.
AC   P69477;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=Aspartic proteinase nepenthesin-2;
DE            EC=3.4.23.12;
DE   AltName: Full=Nepenthesin-II;
DE   Flags: Fragments;
OS   Nepenthes distillatoria (Pitcher plant).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Nepenthaceae; Nepenthes.
OX   NCBI_TaxID=122309;
RN   [1]
RP   PARTIAL PROTEIN SEQUENCE, CHARACTERIZATION, SUBCELLULAR LOCATION, AND
RP   VARIANT ASP-42.
RC   TISSUE=Pitcher;
RX   PubMed=15035659; DOI=10.1042/bj20031575;
RA   Athauda S.B.P., Matsumoto K., Rajapakshe S., Kuribayashi M., Kojima M.,
RA   Kubomura-Yoshida N., Iwamatsu A., Shibata C., Inoue H., Takahashi K.;
RT   "Enzymic and structural characterization of nepenthesin, a unique member of
RT   a novel subfamily of aspartic proteinases.";
RL   Biochem. J. 381:295-306(2004).
CC   -!- FUNCTION: Extracellular proteinase found in the pitcher fluid of
CC       carnivorous plants. Digest prey for nitrogen uptake.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Similar to pepsin, but also cleaves on either side of Asp and
CC         at Lys-|-Arg.; EC=3.4.23.12;
CC   -!- ACTIVITY REGULATION: Inhibited by pepstatin and by diazoacetyl-D,L-
CC       norleucine methyl ester (DAN) in the presence of Cu(2+) ions.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 3.0. Retains 80% and 60% of the original activity after
CC         incubation for 30 days at pH 3.0 and pH 4.0 respectively. Unstable at
CC         pH higher than 5.0.;
CC       Temperature dependence:
CC         Optimum temperature is 45 degrees Celsius. Thermostable up to 50
CC         degrees Celsius. Retains 44% of the original activity after
CC         incubation for 30 days at 50 degrees Celsius.;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15035659}.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.70.10; -; 1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   InterPro; IPR032861; TAXi_N.
DR   Pfam; PF14543; TAXi_N; 1.
DR   SUPFAM; SSF50630; SSF50630; 2.
PE   1: Evidence at protein level;
KW   Aspartyl protease; Direct protein sequencing; Hydrolase; Protease;
KW   Secreted; Zymogen.
FT   CHAIN           1..178
FT                   /note="Aspartic proteinase nepenthesin-2"
FT                   /id="PRO_0000199514"
FT   ACT_SITE        98
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT   VARIANT         42
FT                   /note="T -> D"
FT                   /evidence="ECO:0000269|PubMed:15035659"
FT   NON_CONS        18..19
FT                   /evidence="ECO:0000305"
FT   NON_CONS        35..36
FT                   /evidence="ECO:0000305"
FT   NON_CONS        58..59
FT                   /evidence="ECO:0000305"
FT   NON_CONS        79..80
FT                   /evidence="ECO:0000305"
FT   NON_CONS        92..93
FT                   /evidence="ECO:0000305"
FT   NON_CONS        97..98
FT                   /evidence="ECO:0000305"
FT   NON_CONS        161..162
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   178 AA;  19106 MW;  620B27F0EC3412E8 CRC64;
     QTVQVEPPYY AGDGEYLMVD LIWTQCEPCT QCFSQDSSSF STLPCESQYC QDLPSETCDC
     QYTYGYGDGS STQGYMAXED GSSVPNIAFG CGDNLQIDSG TTLTYLPQDA YNAVAQAFTD
     QINLPTVDES SSGLSTCFQE PSDGSTVQVP EISMQDGGVL NDLQNLAVSF FPTQCGAS