ID   VPE_SOYBN               Reviewed;         495 AA.
AC   P49045;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Vacuolar-processing enzyme;
DE            Short=VPE;
DE            EC=3.4.22.-;
DE   Flags: Precursor;
OS   Glycine max (Soybean) (Glycine hispida).
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; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Seed cotyledon;
RX   PubMed=8075902; DOI=10.1093/oxfordjournals.pcp.a078648;
RA   Shimada T., Hiraiwa N., Nishimura M., Hara-Nishimura I.;
RT   "Vacuolar processing enzyme of soybean that converts proproteins to the
RT   corresponding mature forms.";
RL   Plant Cell Physiol. 35:713-718(1994).
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; D28876; BAA06030.1; -; mRNA.
DR   PIR; T07132; T07132.
DR   RefSeq; NP_001236678.1; NM_001249749.1.
DR   AlphaFoldDB; P49045; -.
DR   SMR; P49045; -.
DR   STRING; 3847.GLYMA17G14680.1; -.
DR   MEROPS; C13.001; -.
DR   PRIDE; P49045; -.
DR   GeneID; 547964; -.
DR   KEGG; gmx:547964; -.
DR   eggNOG; KOG1348; Eukaryota.
DR   OrthoDB; 826971at2759; -.
DR   Proteomes; UP000008827; Unplaced.
DR   GO; GO:0005773; C:vacuole; IEA:GOC.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR   GO; GO:0006624; P:vacuolar protein processing; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Hydrolase; Protease; Reference proteome; Signal; Thiol protease.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000255"
FT   CHAIN           33..495
FT                   /note="Vacuolar-processing enzyme"
FT                   /id="PRO_0000026524"
FT   ACT_SITE        178
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        220
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   495 AA;  55164 MW;  27FADB0D2B791F61 CRC64;
     MALDRSIISK TTWYSVVLWM MVVLVRVHGA AARPNRKEWD SVIKLPTEPV DADSDEVGTR
     WAVLVAGSNG YGNYRHQADV CHAYQLLIKG GLKEENIVVF MYDDIATNEL NPRHGVIINH
     PEGEDLYAGV PKDYTGDNVT TENLFAVILG DKSKLKGGSG KVINSKPEDR IFIYYSDHGG
     PGILGMPNMP YLYAMDFIDV LKKKHASGSY KEMVIYVEAC ESGSVFEGIM PKDLNIYVTT
     ASNAQENSWG TYCPGMDPSP PPEYITCLGD LYSVAWMEDS EAHNLKRESV KQQYKSVKQR
     TSNFNNYAMG SHVMQYGDTN ITAEKLYLYQ GFDPATVNFP PQNGRLETKM EVVNQRDAEL
     FLLWQMYQRS NHQSENKTDI LKQIAETVKH RKHIDGSVEL IGVLLYGPGK GSSVLQSVRA
     PGSSLVDDWT CLKSMVRVFE THCGTLTQYG MKHMRAFANI CNSGVSEASM EEACLAACEG
     YNAGLFHPSN RGYSA