ID   VPE_VICSA               Reviewed;         493 AA.
AC   P49044;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Vacuolar-processing enzyme;
DE            Short=VPE;
DE            EC=3.4.22.-;
DE   AltName: Full=Proteinase B;
DE   Flags: Precursor;
OS   Vicia sativa (Spring vetch) (Tare).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Vicia.
OX   NCBI_TaxID=3908;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Seed;
RX   PubMed=7705362; DOI=10.1111/j.1432-1033.1995.tb20284.x;
RA   Becker C., Shutov A.D., Nong V.H., Senyuk V.I., Jung R., Horstmann C.,
RA   Fischer J., Nielsen N.C., Muntz K.;
RT   "Purification, cDNA cloning and characterization of proteinase B, an
RT   asparagine-specific endopeptidase from germinating vetch (Vicia sativa L.)
RT   seeds.";
RL   Eur. J. Biochem. 228:456-462(1995).
RN   [2]
RP   CHARACTERIZATION.
RC   TISSUE=Seed;
RX   PubMed=7046813;
RA   Shutov A.D., Do N.L., Vaintraub I.A.;
RT   "Purification and partial characterization of protease B from germinating
RT   vetch seeds.";
RL   Biokhimiia 47:814-821(1982).
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; Z34899; CAA84383.1; -; mRNA.
DR   PIR; S68984; S49175.
DR   AlphaFoldDB; P49044; -.
DR   SMR; P49044; -.
DR   MEROPS; C13.002; -.
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; IPR001096; Peptidase_C13.
DR   PANTHER; PTHR12000; PTHR12000; 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..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..493
FT                   /note="Vacuolar-processing enzyme"
FT                   /id="PRO_0000026525"
FT   ACT_SITE        174
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        216
FT                   /evidence="ECO:0000255"
FT   VARIANT         88
FT                   /note="S -> L"
FT   VARIANT         89
FT                   /note="K -> R"
FT   VARIANT         228
FT                   /note="D -> E"
FT   VARIANT         254
FT                   /note="P -> S"
FT   VARIANT         366
FT                   /note="R -> H"
SQ   SEQUENCE   493 AA;  54384 MW;  FE1FF8ADAFBB63AE CRC64;
     MGSSQLSTLL FFTIVVTFLT VVSSGRDLPG DYLRLPSETS RFFREPKNDD DFEGTRWAIL
     LAGSNGYWNY RHQSDVCHAY QLLRKGGSKE ENIIVFMYDD IASNEENPRP GVIINKPDGD
     DVYAGVPKDY TGAEVHADNF YAALLGNKSA LTGGSGKVVD SGPNDHIFVY YTDHGGPGVL
     GMPVGPYLYA SDLNEVLKKK HASGTYKSLV FYLEACESGS IFEGLLPDDL NIYATTASNA
     EESSWGYYCP GDKPPPPPEY STCLGDLYSI AWMEDSEVHN LQTESLQQQY KLVKNRTISE
     PYGSHVMEYG DIGLSKNDLY QYLGTNPAND NNSFVDETEN SLKLRTPSAA VNQRDADLIH
     FWEKFRKAPE GSSQKNEAEK QVLEAMSHRK HIDNSVKLIG QLLFGIEKGT ELLDVVRPAG
     SPLVDNWDCL KTMVKTFETH CGSLSQYGMK HMRSFANICN AGIPNEPMAE ASAQACASIP
     ANPWSSLQGG FSA