Detail Information for IndEnz0002013237
IED ID IndEnz0002013237
Enzyme Type ID protease013237
Protein Name Vacuolar-processing enzyme delta-isozyme
Delta-VPE
EC 3.4.22.34
Asparaginyl endopeptidase delta-VPE
Gene Name dVPE At3g20210 MAL21.23
Organism Arabidopsis thaliana (Mouse-ear cress)
Taxonomic Lineage cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids malvids Brassicales Brassicaceae Camelineae Arabidopsis Arabidopsis thaliana (Mouse-ear cress)
Enzyme Sequence MSSPLGHFQILVFLHALLIFSAESRKTQLLNDNDVESSDKSAKGTRWAVLVAGSNEYYNYRHQADICHAYQILRKGGLKDENIIVFMYDDIAFSSENPRPGVIINKPDGEDVYKGVPKDYTKEAVNVQNFYNVLLGNESGVTGGNGKVVKSGPNDNIFIYYADHGAPGLIAMPTGDEVMAKDFNEVLEKMHKRKKYNKMVIYVEACESGSMFEGILKKNLNIYAVTAANSKESSWGVYCPESYPPPPSEIGTCLGDTFSISWLEDSDLHDMSKETLEQQYHVVKRRVGSDVPETSHVCRFGTEKMLKDYLSSYIGRNPENDNFTFTESFSSPISNSGLVNPRDIPLLYLQRKIQKAPMGSLESKEAQKKLLDEKNHRKQIDQSITDILRLSVKQTNVLNLLTSTRTTGQPLVDDWDCFKTLVNSFKNHCGATVHYGLKYTGALANICNMGVDVKQTVSAIEQACSM
Enzyme Length 466
Uniprot Accession Number Q9LJX8
Absorption
Active Site ACT_SITE 164; /evidence=ECO:0000255; ACT_SITE 206; /evidence=ECO:0000255
Activity Regulation ACTIVITY REGULATION: Strongly inhibited by biotin-YVAD-fmk (a caspase-1 inhibitor) and by Ac-DEVD-fmk. {ECO:0000269|PubMed:15705955}.
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins and small molecule substrates at -Asn-|-Xaa- bonds.; EC=3.4.22.34; Evidence={ECO:0000250|UniProtKB:Q84LM2};
DNA Binding
EC Number 3.4.22.34
Enzyme Function FUNCTION: Asparagine-specific endopeptidase that may be involved in processing of proteins targeted to vacuoles (By similarity). Probably involved in post-translational proteolysis of seed storage proteins in the protein storage vacuole of developing seeds (PubMed:12417707, PubMed:14688293). Exhibits a caspase-1-like activity in extracellular granules. At the early stage of seed development, required for the formation of the seed coat, by regulating cell death of specific cell layers in inner integument (PubMed:15705955). {ECO:0000250|UniProtKB:P49043, ECO:0000269|PubMed:12417707, ECO:0000269|PubMed:14688293, ECO:0000269|PubMed:15705955}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (2); Chain (1); Glycosylation (2); Sequence conflict (1); Signal peptide (1); Site (1)
Keywords Cell wall;Glycoprotein;Hydrolase;Protease;Reference proteome;Secreted;Signal;Thiol protease;Vacuole
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000269|PubMed:15705955}. Secreted, cell wall {ECO:0000269|PubMed:15705955}. Vacuole {ECO:0000250|UniProtKB:Q39119}. Note=Localized to electron-dense structures inside and outside the walls of seed coat cells that undergo cell death. {ECO:0000269|PubMed:15705955}.
Modified Residue
Post Translational Modification PTM: Auto-catalytic activation. {ECO:0000250|UniProtKB:Q84LM2}.
Signal Peptide SIGNAL 1..24; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 18849494; 20118269; 22822203; 23858430;
Motif
Gene Encoded By
Mass 52,085
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda