ID   VPE_RICCO               Reviewed;         497 AA.
AC   P49042;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Vacuolar-processing enzyme;
DE            Short=VPE;
DE            EC=3.4.22.-;
DE   Flags: Precursor;
OS   Ricinus communis (Castor bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC   Ricinus.
OX   NCBI_TaxID=3988;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8312744; DOI=10.2307/3869746;
RA   Hara-Nishimura I., Takeuchi Y., Nishimura M.;
RT   "Molecular characterization of a vacuolar processing enzyme related to a
RT   putative cysteine proteinase of Schistosoma mansoni.";
RL   Plant Cell 5:1651-1659(1993).
RN   [2]
RP   CHARACTERIZATION.
RX   PubMed=1743299; DOI=10.1016/0014-5793(91)81349-d;
RA   Hara-Nishimura I., Inoue K., Nishimura M.;
RT   "A unique vacuolar processing enzyme responsible for conversion of several
RT   proprotein precursors into the mature forms.";
RL   FEBS Lett. 294:89-93(1991).
CC   -!- FUNCTION: Asparagine-specific endopeptidase involved in the processing
CC       of vacuolar seed protein precursors into the mature forms.
CC   -!- SIMILARITY: Belongs to the peptidase C13 family. {ECO:0000305}.
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DR   EMBL; D17401; BAA04225.1; -; mRNA.
DR   PIR; JQ2387; JQ2387.
DR   RefSeq; NP_001310660.1; NM_001323731.1.
DR   AlphaFoldDB; P49042; -.
DR   SMR; P49042; -.
DR   STRING; 3988.XP_002509577.1; -.
DR   MEROPS; C13.001; -.
DR   PRIDE; P49042; -.
DR   GeneID; 8272115; -.
DR   KEGG; rcu:8272115; -.
DR   eggNOG; KOG1348; Eukaryota.
DR   OrthoDB; 826971at2759; -.
DR   GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0051603; P:proteolysis involved in protein catabolic process; IEA:InterPro.
DR   InterPro; IPR043577; AE.
DR   InterPro; IPR033165; Legumain_beta.
DR   InterPro; IPR001096; Peptidase_C13.
DR   PANTHER; PTHR12000; PTHR12000; 1.
DR   PANTHER; PTHR12000:SF25; PTHR12000:SF25; 1.
DR   Pfam; PF01650; Peptidase_C13; 1.
DR   PIRSF; PIRSF500139; AE; 1.
DR   PIRSF; PIRSF019663; Legumain; 1.
DR   PRINTS; PR00776; HEMOGLOBNASE.
PE   1: Evidence at protein level;
KW   Hydrolase; Protease; Signal; Thiol protease.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..497
FT                   /note="Vacuolar-processing enzyme"
FT                   /id="PRO_0000026523"
FT   ACT_SITE        180
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        222
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   497 AA;  55106 MW;  BF067B2CCEECF5EB CRC64;
     METHKSLLFF TNYVLFLVFT LSFLPIPGLL ASRLNPFEPG ILMPTEEAEP VQVDDDDQLG
     TRWAVLVAGS MGFGNYRHQA DVCHAYQLLR KGGLKEENII VFMYDDIAKN ELNPRPGVII
     NHPQGEDVYA GVPKDYTGEH VTAKNLYAVL LGDKSAVQGG SGKVVDSKPN DRIFLYYSDH
     GGPGVLGMPN LPYLYAMDFI EVLKKKHAAG GYKKMVIYVE ACESGSIFEG IMPKDVDIYV
     TTASNAQESS WGTYCPGMEP SPPPEFTTCL GDLYSVAWME DSESHNLKKE TVKQQYSSVK
     ARTSNYNTYA AGSHVMQYGN QSIKADKLYL FQGFDPASVN FPPNNAHLNA PMEVVNQRDA
     ELHFMWQLYK RSENGSEKKK EILQQIKDAI KHRSHLDSSM QLIGDLLFGP KKASAILKSV
     REPGSPLVDD WGCLKSMVRV FETCCGSLTQ YGMKHMRTFA NICNAGVSHT SMEEACNAAC
     SGHDAGQWHP TNQGYSA