NEP1_NEPDI
ID NEP1_NEPDI Reviewed; 164 AA.
AC P69476;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Aspartic proteinase nepenthesin-1;
DE EC=3.4.23.12;
DE AltName: Full=Nepenthesin-I;
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, TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, AND VARIANT TYR-31.
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 2.6. Retains 95% and 79% of the original activity after
CC incubation for 30 days at pH 3.0 and pH 10.0 respectively.;
CC Temperature dependence:
CC Optimum temperature is 55 degrees Celsius. Thermostable up to 50
CC degrees Celsius. Retains 60% of the original activity after
CC incubation for 30 days at 50 degrees Celsius.;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15035659}.
CC -!- TISSUE SPECIFICITY: Parenchymal cells surrounding the secretory glands.
CC {ECO:0000269|PubMed:15035659}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR MEROPS; A01.A47; -.
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; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR032861; TAXi_N.
DR Pfam; PF14543; TAXi_N; 1.
DR SUPFAM; SSF50630; SSF50630; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 1: Evidence at protein level;
KW Aspartyl protease; Direct protein sequencing; Glycoprotein; Hydrolase;
KW Protease; Secreted; Zymogen.
FT CHAIN 1..>164
FT /note="Aspartic proteinase nepenthesin-1"
FT /id="PRO_0000199513"
FT DOMAIN 17..>164
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT REGION 50..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 35
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 31
FT /note="S -> Y"
FT /evidence="ECO:0000269|PubMed:15035659"
FT NON_CONS 55..56
FT /evidence="ECO:0000305"
FT NON_CONS 72..73
FT /evidence="ECO:0000305"
FT NON_CONS 100..101
FT /evidence="ECO:0000305"
FT NON_CONS 113..114
FT /evidence="ECO:0000305"
FT NON_CONS 118..119
FT /evidence="ECO:0000305"
FT NON_CONS 126..127
FT /evidence="ECO:0000305"
FT NON_CONS 148..149
FT /evidence="ECO:0000305"
FT NON_TER 164
SQ SEQUENCE 164 AA; 17271 MW; 60C08491850E4F08 CRC64;
IGPSGVETTV YAGDGEYLMX LSIGTPAQPF SAIMDTGSDL IWTQXQPXTQ XFXQSDPQGS
SSFSTLPCGY GDSETQGSMG TETFTFGSVS IPNITFGXGE GPLPLPXQLD VAKYITLDLP
IDPSAFDLCF QTPSDPSNLQ IPTFVMHFDT GNSVVSFVSA QCGA