ID   VPE_CITSI               Reviewed;         494 AA.
AC   P49043;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Vacuolar-processing enzyme;
DE            Short=VPE;
DE            EC=3.4.22.-;
DE   Flags: Precursor;
OS   Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX   NCBI_TaxID=2711;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Washington Navel; TISSUE=Flavedo;
RX   PubMed=7480346; DOI=10.1104/pp.109.2.541;
RA   Alonso J.M., Granell A.;
RT   "A putative vacuolar processing protease is regulated by ethylene and also
RT   during fruit ripening in Citrus fruit.";
RL   Plant Physiol. 109:541-547(1995).
CC   -!- FUNCTION: Asparagine-specific endopeptidase that may be involved in
CC       processing of proteins targeted to vacuoles that accumulate during
CC       ethylene-regulated processes such as flower opening and flavedo
CC       degreening.
CC   -!- TISSUE SPECIFICITY: High levels are seen in the flowers, a lower level
CC       expression is seen in the leaves, while very low levels are seen in the
CC       stems and roots.
CC   -!- DEVELOPMENTAL STAGE: The levels are low in green fruits but accumulate
CC       with color change occurring during ripening, reaching maximum levels in
CC       fully colored fruit. The levels increase during flower development and
CC       show highest levels in flowers at anthesis.
CC   -!- SIMILARITY: Belongs to the peptidase C13 family. {ECO:0000305}.
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DR   EMBL; Z47793; CAA87720.1; -; mRNA.
DR   PIR; S51117; S51117.
DR   RefSeq; NP_001275777.1; NM_001288848.1.
DR   AlphaFoldDB; P49043; -.
DR   SMR; P49043; -.
DR   STRING; 2711.XP_006475965.1; -.
DR   MEROPS; C13.002; -.
DR   PRIDE; P49043; -.
DR   GeneID; 102612763; -.
DR   KEGG; cit:102612763; -.
DR   eggNOG; KOG1348; Eukaryota.
DR   OrthoDB; 826971at2759; -.
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   2: Evidence at transcript level;
KW   Glycoprotein; Hydrolase; Protease; Signal; Thiol protease.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..494
FT                   /note="Vacuolar-processing enzyme"
FT                   /id="PRO_0000026516"
FT   ACT_SITE        178
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        220
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        151
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        336
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   494 AA;  54291 MW;  8B2059237E03B2B8 CRC64;
     MTRLASGVLI TLLVALAGIA DGSRDIAGDI LKLPSEAYRF FHNGGGGAKV NDDDDSVGTR
     WAVLLAGSNG FWNYRHQADI CHAYQLLRKG GLKDENIIVF MYDDIAFNEE NPRPGVIINH
     PHGDDVYKGV PKDYTGEDVT VEKFFAVVLG NKTALTGGSG KVVDSGPNDH IFIFYSDHGG
     PGVLGMPTSR YIYADELIDV LKKKHASGNY KSLVFYLEAC ESGSIFEGLL LEGLNIYATT
     ASNAEESSWG TYCPGEIPGP PPEYSTCLGD LYSIAWMEDS DIHNLRTETL HQQYELVKTR
     TASYNSYGSH VMQYGDIGLS KNNLFTYLGT NPANDNYTFV DENSLRPASK AVNQRDADLL
     HFWDKYRKAP EGTPRKAEAQ KQFFEAMSHR MHVDHSIKLI GKLLFGIEKG PEILNTVRPA
     GQPLVDDWGC LKSLVRTFES HCGALSQYGM KHMRSLANIC NTGIGKEKMA EASAQACENI
     PSGPWSSLDK GFSA