IED ID | IndEnz0002014046 |
Enzyme Type ID | protease014046 |
Protein Name |
Cathepsin B-like protease 3 EC 3.4.22.- Cathepsin B3 AtCathB3 |
Gene Name | CATHB3 At4g01610 T15B16.17a |
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 | MAVYNTKLCLASVFLLLGLLLAFDLKGIEAESLTKQKLDSKILQDEIVKKVNENPNAGWKAAINDRFSNATVAEFKRLLGVKPTPKKHFLGVPIVSHDPSLKLPKAFDARTAWPQCTSIGNILDQGHCGSCWAFGAVESLSDRFCIQFGMNISLSVNDLLACCGFRCGDGCDGGYPIAAWQYFSYSGVVTEECDPYFDNTGCSHPGCEPAYPTPKCSRKCVSDNKLWSESKHYSVSTYTVKSNPQDIMAEVYKNGPVEVSFTVYEDFAHYKSGVYKHITGSNIGGHAVKLIGWGTSSEGEDYWLMANQWNRGWGDDGYFMIRRGTNECGIEDEPVAGLPSSKNVFRVDTGSNDLPVASV |
Enzyme Length | 359 |
Uniprot Accession Number | Q94K85 |
Absorption | |
Active Site | ACT_SITE 131; /evidence=ECO:0000255|PROSITE-ProRule:PRU10088; ACT_SITE 286; /evidence=ECO:0000255|PROSITE-ProRule:PRU10089; ACT_SITE 307; /evidence=ECO:0000250|UniProtKB:P07858 |
Activity Regulation | ACTIVITY REGULATION: Inhibited by the cathepsin B inhibitors Ac-LVK-CHO, CA-074 and Z-FA-FMK, and the caspase-3 inhibitor Z-DEVD-CHO. {ECO:0000269|PubMed:27058316}. |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.22.- |
Enzyme Function | FUNCTION: Thiol protease that possesses high activity toward the cathepsin synthetic substrate Arg-Arg-7-amino-4-methylcoumarin (RR-AMC) and the papain substrate Gly-Arg-Arg-AMC (GRR-AMC). Can cleave the papain substrate Phe-Arg-AMC (FR-AMC) and the caspase-3 substrate Asp-Glu-Val-Asp-rhodamine 110 (DEVD-R110). Has no activity towards the caspase-6 substrate VEID-AMC, caspase-8 substrate IETD-AMC and caspase-1 substrate YVAD-AMC (PubMed:27058316). Plays a central role in plant programmed cell death (PCD). In addition to its role in protein degradation, may cleave and/or degrade a number of target proteins, activating signaling towards PCD. Contributes to the increase of caspase-3-like activity after UV-C-induced PCD and is required for abiotic stress-induced PCD (PubMed:27058316). Functions redundantly with CATHB1 and CATHB2 in basal defense and distinct forms of plant programmed cell death (PCD). Participates in the establishment of basal resistance against the bacterial pathogen Pseudomonase syringae pv. tomato DC3000. Required for full levels of PCD during resistance (R) gene-mediated hypersensitive response (HR). Involved in the regulation of senescence, a developmental form of PCD in plants (PubMed:19453434). May be involved in the degradation of seed storage proteins during seed germination (PubMed:24600022). {ECO:0000269|PubMed:19453434, ECO:0000269|PubMed:24600022, ECO:0000269|PubMed:27058316}. |
Temperature Dependency | |
PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5. {ECO:0000269|PubMed:27058316}; |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Alternative sequence (1); Chain (1); Disulfide bond (6); Glycosylation (2); Mutagenesis (1); Propeptide (2); Signal peptide (1) |
Keywords | Alternative splicing;Disulfide bond;Glycoprotein;Hydrolase;Plant defense;Protease;Reference proteome;Signal;Thiol protease;Vacuole |
Interact With | |
Induction | INDUCTION: By dark-induced senescence. Induced by infection with an avirulent strain of the bacterial pathogen Pseudomonase syringae pv. tomato DC3000. {ECO:0000269|PubMed:19453434}. |
Subcellular Location | SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:15539469}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..26; /evidence=ECO:0000269|PubMed:27058316 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 12093376; 14617064; 17142483; 17337630; 17828791; 17885809; 18650403; 18796151; 22371507; 27247031; 28627464; 28675441; 29924726; 32796124; |
Motif | |
Gene Encoded By | |
Mass | 39,418 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda | 3.4.22.B6; |