UniProt:Q84LM2 Os04g0537900

chain
  • signal peptide:1-23
  • chain:24-497
checksum 763ADC8F30380A6D
comment
  • FUNCTION Asparagine-specific endopeptidase that may be involved in processing of proteins targeted to vacuoles. Cysteine protease required for post-translational proteolysis of seed storage proteins in the protein storage vacuole (PSV) of developing seeds, by processing of proglutelin precursor to mature glutelin subunits, thus contributing to the formation of protein crystalline structures in PSV (PubMed:19154227, PubMed:19933265, Ref.1).CATALYTIC ACTIVITY Hydrolysis of proteins and small molecule substrates at -Asn-|-Xaa- bonds.SUBCELLULAR LOCATION Expressed in developing seeds.PTM Auto-catalytic activation.DISRUPTION PHENOTYPE In PAK22, higher quantities of 57 kDa polypeptides and lower levels of 40 kDa acidic and 20 kDa basic glutelin subunits in seeds due to reduced vacuolar processing enzyme (VPE) activity and leading to non-crystalline lattice structure of protein storage vacuoles (PSVs). Seedlings growth retardation.SIMILARITY Belongs to the peptidase C13 family.
created [InstanceEdit:9626508] Gupta, Parul, 2018-10-27
databaseName UniProt
dbId 9626412
description
  • recommendedName: fullName evidence="8"Vacuolar-processing enzyme beta-isozyme 1 shortName evidence="8"Beta-VPE 1 shortName evidence="8"OsVPE1 ecNumber evidence="5"3.4.22.34 alternativeName: fullName evidence="10"Asparaginyl endopeptidase VPE1
displayName UniProt:Q84LM2 Os04g0537900
geneName
  • Os04g0537900
  • VPE1
  • Glup3
  • OsJ_15605
identifier Q84LM2
isSequenceChanged false
keyword
  • Disulfide bond
  • Glycoprotein
  • Hydrolase
  • Protease
  • Reference proteome
  • Seed storage protein
  • Signal
  • Storage protein
  • Thiol protease
  • Vacuole
modified [InstanceEdit:9917590] Weiser, Joel, 2024-08-09
name
  • VPE1
referenceDatabase [ReferenceDatabase:2] UniProt
schemaClass ReferenceGeneProduct
secondaryIdentifier
  • VPE1_ORYSJ
  • A0A0P0WCV4
sequenceLength 497
species [Species:1250427] Oryza sativa subsp. japonica
url http://purl.uniprot.org/uniprot/Q84LM2