Q9FJ47 · SAG12_ARATH
- ProteinSenescence-specific cysteine protease SAG12
- GeneSAG12
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids346 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Cysteine protease that may have a developmental senescence specific cell death function during apoptosis, heavy metal detoxification, and hypersensitive response.
Biotechnology
Good molecular marker for age-induced senescence onset measurement.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 154 | |||||
Sequence: C | ||||||
Active site | 289 | |||||
Sequence: H | ||||||
Active site | 310 | |||||
Sequence: N |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | senescence-associated vacuole | |
Molecular Function | cysteine-type peptidase activity | |
Biological Process | apoptotic process | |
Biological Process | defense response to fungus | |
Biological Process | floral organ senescence | |
Biological Process | leaf senescence | |
Biological Process | plant-type hypersensitive response | |
Biological Process | programmed cell death involved in cell development | |
Biological Process | proteolysis | |
Biological Process | response to auxin | |
Biological Process | response to cytokinin | |
Biological Process | response to fructose | |
Biological Process | response to glucose | |
Biological Process | response to sucrose | |
Biological Process | response to UV-B | |
Biological Process | stress response to copper ion |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameSenescence-specific cysteine protease SAG12
- EC number
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ9FJ47
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Localized in senescence-associated vacuoles (SAVs) with intense proteolytic activity that develop in the peripheral cytoplasm of mesophyll and guard cells.
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
No visible effect on senescence.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 33 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-25 | |||||
Sequence: MALKHMQIFLFVAIFSSFCFSITLS | ||||||
Chain | PRO_0000430524 | 26-346 | Senescence-specific cysteine protease SAG12 | |||
Sequence: RPLDNELIMQKRHIEWMTKHGRVYADVKEENNRYVVFKNNVERIEHLNSIPAGRTFKLAVNQFADLTNDEFRSMYTGFKGVSALSSQSQTKMSPFRYQNVSSGALPVSVDWRKKGAVTPIKNQGSCGCCWAFSAVAAIEGATQIKKGKLISLSEQQLVDCDTNDFGCEGGLMDTAFEHIKATGGLTTESNYPYKGEDATCNSKKTNPKATSITGYEDVPVNDEQALMKAVAHQPVSVGIEGGGFDFQFYSSGVFTGECTTYLDHAVTAIGYGESTNGSKYWIIKNSWGTKWGESGYMRIQKDVKDKQGLCGLAMKASYPTI | ||||||
Glycosylation | 124 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 151↔192 | |||||
Sequence: CGCCWAFSAVAAIEGATQIKKGKLISLSEQQLVDCDTNDFGC | ||||||
Disulfide bond | 185↔225 | |||||
Sequence: CDTNDFGCEGGLMDTAFEHIKATGGLTTESNYPYKGEDATC | ||||||
Disulfide bond | 283↔335 | |||||
Sequence: CTTYLDHAVTAIGYGESTNGSKYWIIKNSWGTKWGESGYMRIQKDVKDKQGLC | ||||||
Glycosylation | 301 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Found in senescent leaves, especially in senescence-associated vacuoles- (SAVs) containing cells (e.g. mesophyll and guard cells), and in senescencing ovules of unfertilised pistils.
Induction
Expression activated by developmentally controlled senescence pathways leading to programmed cell death (PCD), probably by epigenetic regulation via histone H3 deacetylation and by WRKY53 activation (PubMed:10380810, PubMed:10579486, PubMed:18212027, PubMed:18721318, PubMed:19143996).
Strongly up-regulated upon abscisic acid treatment (PubMed:9617813).
Repressed by cytokinin, auxin (IAA), and sugars (sucrose, glucose and fructose) which can thus repress developmental senescence (PubMed:10579486).
The senescence-associated accumulation is salicylic acid- (SA) dependent (PubMed:10972893).
Induced slightly in outer leaves by UV-B exposure (PubMed:11432956).
Expressed in late stages of heavy-metal- (e.g. copper) and hypersensitive response- (HR) mediated lesions, in chlorotic tissues surrounding the necrosis (PubMed:10380810).
The induction by cadmium is nitric oxyde- (NO) dependent and occurs one day before cell death (PubMed:19261736).
Strongly up-regulated upon abscisic acid treatment (PubMed:9617813).
Repressed by cytokinin, auxin (IAA), and sugars (sucrose, glucose and fructose) which can thus repress developmental senescence (PubMed:10579486).
The senescence-associated accumulation is salicylic acid- (SA) dependent (PubMed:10972893).
Induced slightly in outer leaves by UV-B exposure (PubMed:11432956).
Expressed in late stages of heavy-metal- (e.g. copper) and hypersensitive response- (HR) mediated lesions, in chlorotic tissues surrounding the necrosis (PubMed:10380810).
The induction by cadmium is nitric oxyde- (NO) dependent and occurs one day before cell death (PubMed:19261736).
Developmental stage
Senescent tissues specific expression (PubMed:10579486, Ref.6). Detected only after significant visible yellowing (PubMed:9617813).
In unfertilised pistils, accumulates transiently shortly after anthesis, and increased again at the end of pistil development (PubMed:21575215).
In ovules, first observed at the basal zone of the ovary, and progressively extend acropetally along the ovary (PubMed:21575215).
In unfertilised pistils, accumulates transiently shortly after anthesis, and increased again at the end of pistil development (PubMed:21575215).
In ovules, first observed at the basal zone of the ovary, and progressively extend acropetally along the ovary (PubMed:21575215).
Gene expression databases
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length346
- Mass (Da)38,234
- Last updated2001-03-01 v1
- Checksum2BE574417D50F167
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 97 | in Ref. 1; AAC49135 | ||||
Sequence: R → C | ||||||
Sequence conflict | 215 | in Ref. 1; AAC49135 | ||||
Sequence: N → D |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U37336 EMBL· GenBank· DDBJ | AAC49135.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AB016870 EMBL· GenBank· DDBJ | BAB09317.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002688 EMBL· GenBank· DDBJ | AED95312.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF370131 EMBL· GenBank· DDBJ | AAK43946.1 EMBL· GenBank· DDBJ | mRNA | ||
AY040073 EMBL· GenBank· DDBJ | AAK64131.1 EMBL· GenBank· DDBJ | mRNA | ||
AF083753 EMBL· GenBank· DDBJ | AAN60311.1 EMBL· GenBank· DDBJ | mRNA |