Q94K85 · CATB3_ARATH
- ProteinCathepsin B-like protease 3
- GeneCATHB3
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids359 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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).
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.
pH Dependence
Optimum pH is 5.5.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 131 | |||||
Sequence: C | ||||||
Active site | 286 | |||||
Sequence: H | ||||||
Active site | 307 | |||||
Sequence: N |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | plant-type vacuole | |
Cellular Component | secretory vesicle | |
Molecular Function | cysteine-type endopeptidase activity | |
Biological Process | defense response | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameCathepsin B-like protease 3
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ94K85
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
Delayed germination and decreased germination rate.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 131 | Loss of protease activity. | ||||
Sequence: C → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 24 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for signal, propeptide, glycosylation, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-26 | |||||
Sequence: MAVYNTKLCLASVFLLLGLLLAFDLK | ||||||
Propeptide | PRO_0000439421 | 27-102 | Activation peptide | |||
Sequence: GIEAESLTKQKLDSKILQDEIVKKVNENPNAGWKAAINDRFSNATVAEFKRLLGVKPTPKKHFLGVPIVSHDPSLK | ||||||
Glycosylation | 69 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Chain | PRO_0000439457 | 102-342 | Cathepsin B-like protease 3 | |||
Sequence: KLPKAFDARTAWPQCTSIGNILDQGHCGSCWAFGAVESLSDRFCIQFGMNISLSVNDLLACCGFRCGDGCDGGYPIAAWQYFSYSGVVTEECDPYFDNTGCSHPGCEPAYPTPKCSRKCVSDNKLWSESKHYSVSTYTVKSNPQDIMAEVYKNGPVEVSFTVYEDFAHYKSGVYKHITGSNIGGHAVKLIGWGTSSEGEDYWLMANQWNRGWGDDGYFMIRRGTNECGIEDEPVAGLPSSK | ||||||
Disulfide bond | 116↔145 | |||||
Sequence: CTSIGNILDQGHCGSCWAFGAVESLSDRFC | ||||||
Disulfide bond | 128↔171 | |||||
Sequence: CGSCWAFGAVESLSDRFCIQFGMNISLSVNDLLACCGFRCGDGC | ||||||
Glycosylation | 151 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 162↔216 | |||||
Sequence: CCGFRCGDGCDGGYPIAAWQYFSYSGVVTEECDPYFDNTGCSHPGCEPAYPTPKC | ||||||
Disulfide bond | 163↔167 | |||||
Sequence: CGFRC | ||||||
Disulfide bond | 193↔220 | |||||
Sequence: CDPYFDNTGCSHPGCEPAYPTPKCSRKC | ||||||
Disulfide bond | 202↔207 | |||||
Sequence: CSHPGC | ||||||
Propeptide | PRO_0000439422 | 343-359 | Removed in mature form | |||
Sequence: NVFRVDTGSNDLPVASV |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in root tips, root vasculature, emerging lateral root, hydathodes, vascular tissue of leaves, vasculature of sepals and anthers, stigma, and vascular bundles at the base and the upper part of the siliques.
Induction
By dark-induced senescence. Induced by infection with an avirulent strain of the bacterial pathogen Pseudomonase syringae pv. tomato DC3000.
Developmental stage
Expressed in developing siliques 13 to 15 days after pollination (DAP). In germinating seeds, expressed from 12 to 48 hours after imbibition with a peak of expression at 24 hours.
Gene expression databases
Interaction
Protein-protein interaction databases
Structure
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative splicing.
Q94K85-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length359
- Mass (Da)39,418
- Last updated2001-12-01 v1
- ChecksumD3199ABA3FEA831E
Q94K85-2
- Name2
- Differences from canonical
- 124-125: DQ → GL
Features
Showing features for alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_058851 | 124-125 | in isoform 2 | |||
Sequence: DQ → GL |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF083797 EMBL· GenBank· DDBJ | AAN60355.1 EMBL· GenBank· DDBJ | mRNA | ||
AF104919 EMBL· GenBank· DDBJ | AAC72872.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL161492 EMBL· GenBank· DDBJ | CAB77732.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002687 EMBL· GenBank· DDBJ | AEE82052.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002687 EMBL· GenBank· DDBJ | AEE82053.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF370193 EMBL· GenBank· DDBJ | AAK44008.1 EMBL· GenBank· DDBJ | mRNA | ||
AY065167 EMBL· GenBank· DDBJ | AAL38343.1 EMBL· GenBank· DDBJ | mRNA | ||
AY114015 EMBL· GenBank· DDBJ | AAM45063.1 EMBL· GenBank· DDBJ | mRNA | ||
BT001190 EMBL· GenBank· DDBJ | AAN65077.1 EMBL· GenBank· DDBJ | mRNA | ||
AK175280 EMBL· GenBank· DDBJ | BAD43043.1 EMBL· GenBank· DDBJ | mRNA | ||
AK175481 EMBL· GenBank· DDBJ | BAD43244.1 EMBL· GenBank· DDBJ | mRNA | ||
AK175539 EMBL· GenBank· DDBJ | BAD43302.1 EMBL· GenBank· DDBJ | mRNA | ||
AK176165 EMBL· GenBank· DDBJ | BAD43928.1 EMBL· GenBank· DDBJ | mRNA | ||
AK176244 EMBL· GenBank· DDBJ | BAD44007.1 EMBL· GenBank· DDBJ | mRNA | ||
AK176281 EMBL· GenBank· DDBJ | BAD44044.1 EMBL· GenBank· DDBJ | mRNA | ||
AK176330 EMBL· GenBank· DDBJ | BAD44093.1 EMBL· GenBank· DDBJ | mRNA | ||
AK176416 EMBL· GenBank· DDBJ | BAD44179.1 EMBL· GenBank· DDBJ | mRNA | ||
AK176433 EMBL· GenBank· DDBJ | BAD44196.1 EMBL· GenBank· DDBJ | mRNA | ||
AK176487 EMBL· GenBank· DDBJ | BAD44250.1 EMBL· GenBank· DDBJ | mRNA | ||
AK221398 EMBL· GenBank· DDBJ | BAD94342.1 EMBL· GenBank· DDBJ | mRNA | ||
AK230235 EMBL· GenBank· DDBJ | BAF02040.1 EMBL· GenBank· DDBJ | mRNA | ||
AY086034 EMBL· GenBank· DDBJ | AAM63244.1 EMBL· GenBank· DDBJ | mRNA |