| IED ID | IndEnz0002013839 |
| Enzyme Type ID | protease013839 |
| Protein Name |
Cysteine proteinase RD21A EC 3.4.22.- Protein RESPONSIVE TO DEHYDRATION 21 RD21 |
| Gene Name | RD21A At1g47128 F2G19.31 |
| 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 | MGFLKPTMAILFLAMVAVSSAVDMSIISYDEKHGVSTTGGRSEAEVMSIYEAWLVKHGKAQSQNSLVEKDRRFEIFKDNLRFVDEHNEKNLSYRLGLTRFADLTNDEYRSKYLGAKMEKKGERRTSLRYEARVGDELPESIDWRKKGAVAEVKDQGGCGSCWAFSTIGAVEGINQIVTGDLITLSEQELVDCDTSYNEGCNGGLMDYAFEFIIKNGGIDTDKDYPYKGVDGTCDQIRKNAKVVTIDSYEDVPTYSEESLKKAVAHQPISIAIEAGGRAFQLYDSGIFDGSCGTQLDHGVVAVGYGTENGKDYWIVRNSWGKSWGESGYLRMARNIASSSGKCGIAIEPSYPIKNGENPPNPGPSPPSPIKPPTQCDSYYTCPESNTCCCLFEYGKYCFAWGCCPLEAATCCDDNYSCCPHEYPVCDLDQGTCLLSKNSPFSVKALKRKPATPFWSQGRKNIA |
| Enzyme Length | 462 |
| Uniprot Accession Number | P43297 |
| Absorption | |
| Active Site | ACT_SITE 161; /evidence="ECO:0000255|PROSITE-ProRule:PRU10088, ECO:0000269|PubMed:22396764"; ACT_SITE 297; /evidence="ECO:0000255|PROSITE-ProRule:PRU10089, ECO:0000269|PubMed:22396764"; ACT_SITE 317; /evidence="ECO:0000255|PROSITE-ProRule:PRU10090, ECO:0000269|PubMed:22396764" |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by the cysteine protease inhibitor E-64. {ECO:0000269|PubMed:26160583}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.22.- |
| Enzyme Function | FUNCTION: Cysteine protease that plays a role in immunity, senescence, and biotic and abiotic stresses (Probable). Involved in immunity against the necrotrophic fungal pathogen Botrytis cinerea (PubMed:22238602). Involved in elicitor-stimulated programmed cell death (PCD). During infection by the necrotrophic fungal pathogen Botrytis cinerea, functions as PCD-promoting protease that is released from the ER body or vacuole to the cytoplasm (PubMed:23398119). Accumulates in endoplasmic reticulum-derived bodies in epidermal cells and may participate in cell death in stressed or injured cells (PubMed:11577182). Involved in water stress-induced cell death through its protease activity that is released to the cytoplasm after vacuolar collapse (PubMed:26884487). Possesses protease activity in vitro and is involved in cell death in the transmitting tract and septum epidermis during flower development (PubMed:26160583). Possesses peptide ligase activity. Can ligate peptides to unmodified N-termini of acceptor proteins. Probably ligates through a thioester intermediate (PubMed:18660805). {ECO:0000269|PubMed:11577182, ECO:0000269|PubMed:18660805, ECO:0000269|PubMed:22238602, ECO:0000269|PubMed:23398119, ECO:0000269|PubMed:26160583, ECO:0000269|PubMed:26884487, ECO:0000305|PubMed:22396764}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Disulfide bond (5); Glycosylation (2); Mutagenesis (3); Propeptide (2); Signal peptide (1) |
| Keywords | Cytoplasm;Disulfide bond;Glycoprotein;Golgi apparatus;Hydrolase;Protease;Reference proteome;Signal;Thiol protease;Vacuole |
| Interact With | Q9XI01 |
| Induction | INDUCTION: By high salt conditions and drought stress. {ECO:0000269|PubMed:8325504}. |
| Subcellular Location | SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:11577182, ECO:0000269|PubMed:11743107, ECO:0000269|PubMed:23398119}. Golgi apparatus {ECO:0000269|PubMed:22396764}. Cytoplasm, Stress granule {ECO:0000269|PubMed:26978070}. Cytoplasm, P-body {ECO:0000269|PubMed:26978070}. Note=Specifically accumulates in body structures that directly bud from the endoplasmic reticulum and fuse with the vacuole (PubMed:11577182). Passes through the Golgi on its route to the vacuole (PubMed:22396764). {ECO:0000269|PubMed:11577182, ECO:0000269|PubMed:22396764}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 14500793; 14749481; 15028209; 15215502; 15539469; 16442528; 18538804; 18650403; 18676877; 18838434; 21166475; 21700722; 22085334; 22115780; 22371507; 23696092; 28003327; 28061816; 28179567; 28627464; 29497469; 30801789; 30823989; 32453812; |
| Motif | |
| Gene Encoded By | |
| Mass | 50,966 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |