NEP1_NEPGR
ID NEP1_NEPGR Reviewed; 437 AA.
AC Q766C3;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Aspartic proteinase nepenthesin-1;
DE EC=3.4.23.12;
DE AltName: Full=Nepenthesin-I;
DE Flags: Precursor;
GN Name=nep1;
OS Nepenthes gracilis (Slender pitcher plant).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Nepenthaceae; Nepenthes.
OX NCBI_TaxID=150966;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], 3D-STRUCTURE MODELING, CHARACTERIZATION, AND
RP VARIANTS NEPENTHESIN IB VAL-233; THR-251 AND GLU-392.
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 {ECO:0000250}.
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:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR EMBL; AB114914; BAD07474.1; -; mRNA.
DR AlphaFoldDB; Q766C3; -.
DR SMR; Q766C3; -.
DR MEROPS; A01.040; -.
DR BRENDA; 3.4.23.12; 8734.
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 CDD; cd05476; pepsin_A_like_plant; 1.
DR Gene3D; 2.40.70.10; -; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR034161; Pepsin-like_plant.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR032799; TAXi_C.
DR InterPro; IPR032861; TAXi_N.
DR Pfam; PF14541; TAXi_C; 1.
DR Pfam; PF14543; TAXi_N; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; SSF50630; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 1: Evidence at protein level;
KW Aspartyl protease; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW Secreted; Signal; Zymogen.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..78
FT /note="Activation peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000025914"
FT CHAIN 79..437
FT /note="Aspartic proteinase nepenthesin-1"
FT /id="PRO_0000025915"
FT DOMAIN 95..430
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 113
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT ACT_SITE 315
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 123..126
FT /evidence="ECO:0000305"
FT DISULFID 129..203
FT /evidence="ECO:0000305"
FT DISULFID 150..168
FT /evidence="ECO:0000305"
FT DISULFID 155..163
FT /evidence="ECO:0000305"
FT DISULFID 240..434
FT /evidence="ECO:0000305"
FT DISULFID 354..395
FT /evidence="ECO:0000305"
FT VARIANT 233
FT /note="D -> V (in nepenthesin-1b)"
FT /evidence="ECO:0000269|PubMed:15035659"
FT VARIANT 251
FT /note="N -> T (in nepenthesin-1b)"
FT /evidence="ECO:0000269|PubMed:15035659"
FT VARIANT 392
FT /note="G -> E (in nepenthesin-1b)"
FT /evidence="ECO:0000269|PubMed:15035659"
SQ SEQUENCE 437 AA; 46357 MW; A430C3A84ED3FF3E CRC64;
MASSLYSFLL ALSIVYIFVA PTHSTSRTAL NHRHEAKVTG FQIMLEHVDS GKNLTKFQLL
ERAIERGSRR LQRLEAMLNG PSGVETSVYA GDGEYLMNLS IGTPAQPFSA IMDTGSDLIW
TQCQPCTQCF NQSTPIFNPQ GSSSFSTLPC SSQLCQALSS PTCSNNFCQY TYGYGDGSET
QGSMGTETLT FGSVSIPNIT FGCGENNQGF GQGNGAGLVG MGRGPLSLPS QLDVTKFSYC
MTPIGSSTPS NLLLGSLANS VTAGSPNTTL IQSSQIPTFY YITLNGLSVG STRLPIDPSA
FALNSNNGTG GIIIDSGTTL TYFVNNAYQS VRQEFISQIN LPVVNGSSSG FDLCFQTPSD
PSNLQIPTFV MHFDGGDLEL PSENYFISPS NGLICLAMGS SSQGMSIFGN IQQQNMLVVY
DTGNSVVSFA SAQCGAS
