ID   VPE2_PHAVU              Reviewed;         493 AA.
AC   O24326;
DT   10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Vacuolar-processing enzyme;
DE            EC=3.4.22.-;
DE   AltName: Full=Pv-VPE;
DE   Flags: Precursor;
OS   Phaseolus vulgaris (Kidney bean) (French bean).
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; Phaseolus.
OX   NCBI_TaxID=3885;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DEVELOPMENTAL STAGE.
RC   STRAIN=cv. Moldavian; TISSUE=Cotyledon;
RX   PubMed=9874222; DOI=10.1046/j.1432-1327.1998.2580546.x;
RA   Senyuk V., Rotari V., Becker C., Zakharov A., Horstmann C., Muentz K.,
RA   Vaintraub I.;
RT   "Does an asparaginyl-specific cysteine endopeptidase trigger phaseolin
RT   degradation in cotyledons of kidney bean seedlings?";
RL   Eur. J. Biochem. 258:546-558(1998).
CC   -!- FUNCTION: Asparagine-specific endopeptidase involved in the processing
CC       of vacuolar seed protein precursors into the mature forms.
CC       {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: Not expressed in dormant seeds. First detected 1
CC       day after imbibition, reaching a maximum at 3 days after imbibition,
CC       then declining gradually. {ECO:0000269|PubMed:9874222}.
CC   -!- SIMILARITY: Belongs to the peptidase C13 family. {ECO:0000305}.
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DR   EMBL; Z99957; CAB17079.1; -; Genomic_DNA.
DR   PIR; T12044; T12044.
DR   AlphaFoldDB; O24326; -.
DR   SMR; O24326; -.
DR   STRING; 3885.XP_007155624.1; -.
DR   MEROPS; C13.001; -.
DR   eggNOG; KOG1348; Eukaryota.
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   2: Evidence at transcript level;
KW   Hydrolase; Protease; Signal; Thiol protease; Zymogen.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000255"
FT   PROPEP          35..53
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000026520"
FT   CHAIN           54..?
FT                   /note="Vacuolar-processing enzyme"
FT                   /id="PRO_0000026521"
FT   PROPEP          ?..493
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000026522"
FT   ACT_SITE        176
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        218
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   493 AA;  55137 MW;  3449D32C2F6D81E4 CRC64;
     MAVHRSLLNK PTWCRVAFWW WMLVMVMRIQ GTNGKEQDSV IKLPTQEVDA ESDEVGTRWA
     VLVAGSNGYG NYRHQADVCH AYQLLIKGGV KEENIVVFMY DDIATHELNP RPGVIINNPQ
     GPDVYAGVPK DYTGESVTSH NFFAVLLGDK SKVKGGSGKV INSKPEDRIF VYYSDHGGPG
     VLGMPNMPYL YAMDFIDVLK KKHASGGYKE MVIYVEACES GSIFEGIMPK DLNIYVTTAS
     NAQENSWGTY CPGMYPPPPP EYITCLGDLY SVAWMEDSES HNLKKESVEQ QYQSVKQRTS
     NFEAYAMGSH VMQYGDANMT AEKLYLYHGF DPATVNFPPH NGRLKSKMEV VNQRDAELLF
     MWQVYQRSNH LPEKKTDILK QIEEIVKHRK HLDGSVELIG VLLYGPEKAS SVLRSVRTTG
     LPLVDDWTCL KSMVRVYETH CGSLTQYGMK HMRAFANICN SGVSETSMEK ACVAACGGYH
     AGLLHPSNTG YSA