ID   VPE1_ORYSI              Reviewed;         497 AA.
AC   B8ASK4;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Vacuolar-processing enzyme beta-isozyme 1 {ECO:0000305};
DE            Short=Beta-VPE 1 {ECO:0000305};
DE            Short=OsVPE1 {ECO:0000305};
DE            EC=3.4.22.34 {ECO:0000250|UniProtKB:Q84LM2};
DE   AltName: Full=Asparaginyl endopeptidase VPE1 {ECO:0000305};
DE   Flags: Precursor;
GN   ORFNames=OsI_16797 {ECO:0000312|EMBL:EEC77714.1};
OS   Oryza sativa subsp. indica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39946 {ECO:0000312|EMBL:EEC77714.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. 93-11;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
CC   -!- FUNCTION: Asparagine-specific endopeptidase that may be involved in
CC       processing of proteins targeted to vacuoles (By similarity). Cysteine
CC       protease required for post-translational proteolysis of seed storage
CC       proteins in the protein storage vacuole (PSV) of developing seeds, by
CC       processing of proglutelin precursor to mature glutelin subunits, thus
CC       contributing to the formation of protein crystalline structures in PSV
CC       (By similarity). {ECO:0000250|UniProtKB:P49043,
CC       ECO:0000250|UniProtKB:Q84LM2}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of proteins and small molecule substrates at
CC         -Asn-|-Xaa- bonds.; EC=3.4.22.34;
CC         Evidence={ECO:0000250|UniProtKB:Q84LM2};
CC   -!- SUBCELLULAR LOCATION: Protein storage vacuole
CC       {ECO:0000250|UniProtKB:Q84LM2}.
CC   -!- PTM: Auto-catalytic activation. {ECO:0000250|UniProtKB:Q84LM2}.
CC   -!- SIMILARITY: Belongs to the peptidase C13 family. {ECO:0000305}.
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DR   EMBL; CM000129; EEC77714.1; -; Genomic_DNA.
DR   AlphaFoldDB; B8ASK4; -.
DR   SMR; B8ASK4; -.
DR   STRING; 39946.B8ASK4; -.
DR   MEROPS; C13.001; -.
DR   EnsemblPlants; BGIOSGA014644-TA; BGIOSGA014644-PA; BGIOSGA014644.
DR   Gramene; BGIOSGA014644-TA; BGIOSGA014644-PA; BGIOSGA014644.
DR   HOGENOM; CLU_024160_0_0_1; -.
DR   OMA; MKLPCLG; -.
DR   Proteomes; UP000007015; Chromosome 4.
DR   GO; GO:0000326; C:protein storage vacuole; ISS:UniProtKB.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; ISS:UniProtKB.
DR   GO; GO:1990019; P:protein storage vacuole organization; ISS:UniProtKB.
DR   GO; GO:0051603; P:proteolysis involved in protein catabolic process; IEA:InterPro.
DR   GO; GO:0006624; P:vacuolar protein processing; ISS:UniProtKB.
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   3: Inferred from homology;
KW   Glycoprotein; Hydrolase; Protease; Reference proteome; Signal;
KW   Thiol protease; Vacuole.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..497
FT                   /note="Vacuolar-processing enzyme beta-isozyme 1"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000431975"
FT   SITE            269
FT                   /note="Required for post-translational maturation and
FT                   enzyme activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q84LM2"
FT   CARBOHYD        153
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        340
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   497 AA;  54826 MW;  3DA6AAC46A8E5AFA CRC64;
     MAARCWVWGF VVALLAVAAA ADGEEEEGKW EPLIRMPTEE GDDAEAAAPA PAPAAADYGG
     TRWAVLVAGS SGYGNYRHQA DVCHACQILQ KGGVKEENIV VFMYDDIAHN ILNPRPGTII
     NHPKGGDVYA GVPKDYTGHQ VTTENFFAVL LGNKTAVTGG SGKVIDSKPE DHIFIYYSDH
     GGPGVLGMPN LPYLYAGDFI KVLQKKHASN SYSKMVIYVE ACESGSIFEG LMPENLNIYV
     TTASNAVENS WGTYCPGEEP SPPPEYITCL GDMYSVAWME DSETHNLKKE TIEDQYELVK
     KRTSNANKLN EGSHVMEYGD KTFKDEKLFL YQGFNPANGN ITNELIWPVP KATVNQRDAD
     LLFMWKRYEQ LNGVSEDKLR ALREIEDTIA HRKHLDSSID FIGKLVFGFE NGPLALEAAR
     SSGQPLVDNW DCLKKMVRIF ESQCGSLTQY GMKYMRAFAN ICNNGVSEAK MMEASINACG
     RYNSARWSPM TEGGHSA