ID   VPE1_PHAVU              Reviewed;         484 AA.
AC   O24325;
DT   10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Vacuolar-processing enzyme;
DE            Short=VPE;
DE            EC=3.4.22.-;
DE   AltName: Full=Legumain-like proteinase;
DE            Short=LLP;
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], PROTEIN SEQUENCE OF 45-56, FUNCTION, AND
RP   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. Probably involved in the
CC       degradation of phaseolin during and after germination.
CC       {ECO:0000269|PubMed:9874222}.
CC   -!- DEVELOPMENTAL STAGE: Not expressed in dormant seeds. First detected 2
CC       days after imbibition, reaching a maximum at 5-6 days after imbibition,
CC       then declining. {ECO:0000269|PubMed:9874222}.
CC   -!- SIMILARITY: Belongs to the peptidase C13 family. {ECO:0000305}.
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DR   EMBL; Z99956; CAB17078.1; -; Genomic_DNA.
DR   PIR; T12043; T12043.
DR   AlphaFoldDB; O24325; -.
DR   SMR; O24325; -.
DR   STRING; 3885.XP_007160985.1; -.
DR   MEROPS; C13.002; -.
DR   ProMEX; O24325; -.
DR   eggNOG; KOG1348; Eukaryota.
DR   BRENDA; 3.4.22.34; 4746.
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   Direct protein sequencing; Hydrolase; Protease; Signal; Thiol protease;
KW   Zymogen.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   PROPEP          25..44
FT                   /evidence="ECO:0000269|PubMed:9874222"
FT                   /id="PRO_0000026517"
FT   CHAIN           45..?
FT                   /note="Vacuolar-processing enzyme"
FT                   /id="PRO_0000026518"
FT   PROPEP          ?..484
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000026519"
FT   ACT_SITE        167
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        209
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   484 AA;  53389 MW;  548DABEB99F7201D CRC64;
     MATTTATTSL LALLLLFLVA LVSAGRDLVG DFLRLPSDSG NGDNVHGTRW AILFAGSSGY
     WNYRHQADIC HAYQLLRKGG LKDENIIVFM YDDIAFNSEN PRRGVIINSP NGDEVYKGVP
     KDYTGEDVTA HNFYAALLGD KSKLTGGSGK VVNSGPNDHI FIFYSDHGGP GVLGSPAGPY
     IYASDLNEVL KKKHASGTYK NLVFYLEACE SGSIFEGLLP EDINVYATTA SNADESSWGT
     YCPGEDPSPP PEYSTCLGDL YSVAWMEDSD RHNLRTETLH QQYKLVKERT ISGGLYYGSH
     VMQYGDVGLS KDILFHYLGT DPANENLTFV DENSLWSSSK AVNQRDADLV HFWDKFRKAP
     EGSPKKNEAR KQVLEVMSHR MHIDDSVELV GKLLFGIEKA PELLNAVRPA GSALVDDWDC
     LKTMVRTFET HCGSLSQYGM KHMRSFANMC NVGIKKEQMR EASAQACVTI PANPWSSLQR
     GFSA