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Database: UniProt
Entry: E5AXU3_HORVU
LinkDB: E5AXU3_HORVU
Original site: E5AXU3_HORVU 
ID   E5AXU3_HORVU            Unreviewed;       493 AA.
AC   E5AXU3;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Vacuolar processing enzyme 1 {ECO:0000313|EMBL:CBX26636.1};
GN   Name=vpe1 {ECO:0000313|EMBL:CBX26636.1};
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513 {ECO:0000313|EMBL:CBX26636.1};
RN   [1] {ECO:0000313|EMBL:CBX26636.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=21059741; DOI=10.1093/jxb/erq348;
RA   Radchuk V., Weier D., Radchuk R., Weschke W., Weber H.;
RT   "Development of maternal seed tissue in barley is mediated by regulated
RT   cell expansion and cell disintegration and coordinated with endosperm
RT   growth.";
RL   J. Exp. Bot. 62:1217-1227(2011).
CC   -!- SIMILARITY: Belongs to the peptidase C13 family.
CC       {ECO:0000256|ARBA:ARBA00009941}.
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DR   EMBL; FR696360; CBX26636.1; -; mRNA.
DR   AlphaFoldDB; E5AXU3; -.
DR   MEROPS; C13.001; -.
DR   EnsemblPlants; HORVU.MOREX.r2.6HG0496570.1.mrna1; HORVU.MOREX.r2.6HG0496570.1.mrna1; HORVU.MOREX.r2.6HG0496570.1.
DR   Gramene; HORVU.MOREX.r2.6HG0496570.1.mrna1; HORVU.MOREX.r2.6HG0496570.1.mrna1; HORVU.MOREX.r2.6HG0496570.1.
DR   ExpressionAtlas; E5AXU3; baseline and differential.
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   CDD; cd21115; legumain_C; 1.
DR   Gene3D; 1.10.132.130; -; 1.
DR   Gene3D; 3.40.50.1460; -; 1.
DR   InterPro; IPR043577; AE.
DR   InterPro; IPR048501; Legum_prodom.
DR   InterPro; IPR046427; Legumain_prodom_sf.
DR   InterPro; IPR001096; Peptidase_C13.
DR   PANTHER; PTHR12000; HEMOGLOBINASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR12000:SF54; VACUOLAR-PROCESSING ENZYME BETA-ISOZYME; 1.
DR   Pfam; PF20985; Legum_prodom; 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 {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..493
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003195330"
FT   DOMAIN          380..475
FT                   /note="Legumain prodomain"
FT                   /evidence="ECO:0000259|Pfam:PF20985"
FT   ACT_SITE        176
FT                   /evidence="ECO:0000256|PIRSR:PIRSR019663-1"
FT   ACT_SITE        218
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR019663-1"
SQ   SEQUENCE   493 AA;  54712 MW;  0B5DDE16163E9F5F CRC64;
     MAPWWCFGLL LLLCALAGAD ASKGRWDPVI RMPGEEEPAT ARGDGGSQEE EEDGVGTRWA
     VLVAGSSGYG NYRHQADICH AYQILRKGGV KEENIVVFMY DDIAKNALNP RPGVIINHPE
     GEDVYAGVPK DYTGEAVTAK NFYAVLLGNK TAVTGGSKKV IDSKSNDHIF IYYSDHGGPG
     VLGMPNLPYL YAADFIKVLQ EKHASNTYAK MVIYVEACES GSIFEGLMPA DLNIYVTTAS
     NAEESSWGTY CPGMEPSPPS EYITCLGDLY SISWMEDSET NNLKEETIKK QYEVVKKRTS
     DMNSYSAGSH VMEYGDKTFK DEKLYLYQGF NPANTNITNK LFWQARKAAI NQRDADLLFL
     WRRYELLHEK SKEKVNVLRE ISETVTHRKH LDSSIDFIGK LLFGFENGPS MLETVRPSGI
     PLVDDWDCLK RMVRIFESHC GSLTQYGMKH MRAFANICNN GISGTSMKEA SISTCGGGHN
     SARLSTLIQG YSA
//
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