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 02-SEP-2026, entry version 65. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR MEROPS; A01.A47; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR Gene3D; 2.40.70.10; Acid Proteases; 1. DR InterPro; IPR033121; PEPTIDASE_A1. DR InterPro; IPR021109; Peptidase_aspartic_dom_sf. DR InterPro; IPR051708; Plant_Aspart_Prot_A1. DR InterPro; IPR032861; TAXi_N. DR PANTHER; PTHR47967:SF23; OS04G0448300 PROTEIN; 1. DR PANTHER; PTHR47967; OS07G0603500 PROTEIN-RELATED; 1. DR Pfam; PF14543; TAXi_N; 1. DR SUPFAM; SSF50630; Acid proteases; 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 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 //