O65351 · SBT17_ARATH
- ProteinSubtilisin-like protease SBT1.7
- GeneSBT1.7
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids757 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Serine protease. Has a substrate preference for the hydrophobic residues Phe and Ala and the basic residue Asp in the P1 position, and for Asp, Leu or Ala in the P1' position (PubMed:12413398).
Essential for mucilage release from seed coats. Triggers the accumulation and/or activation of cell wall modifying enzymes necessary either for the loosening of the outer primary cell wall, or to facilitate swelling of the mucilage (PubMed:18266922).
Essential for mucilage release from seed coats. Triggers the accumulation and/or activation of cell wall modifying enzymes necessary either for the loosening of the outer primary cell wall, or to facilitate swelling of the mucilage (PubMed:18266922).
Activity regulation
Activated by calcium. Inhibited by the serine protease inhibitors 4-(2-aminoethyl)benzenesulphonyl fluoride (AEBSF), PMSF, di-isopropyl phosphofluoridate (DFP) and soybean trypsin inhibitor (SBTI). Not inhibited by benzamidine or iodoacetamide. Leupeptin and pepstatin A have a minor inhibitory action.
pH Dependence
Optimum pH is 5.0.
Temperature Dependence
Optimum temperature is 80 degrees Celsius. Thermostable.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 139 | Charge relay system | ||||
Sequence: D | ||||||
Active site | 212 | Charge relay system | ||||
Sequence: H | ||||||
Active site | 542 | Charge relay system | ||||
Sequence: S |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | apoplast | |
Cellular Component | extracellular region | |
Cellular Component | secretory vesicle | |
Molecular Function | serine-type endopeptidase activity | |
Biological Process | mucilage extrusion from seed coat | |
Biological Process | mucilage metabolic process involved in seed coat development | |
Biological Process | proteolysis | |
Biological Process | seed coat development |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameSubtilisin-like protease SBT1.7
- 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 accessionO65351
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Intracellular spaces and cell wall.
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
No visible phenotype under normal growth conditions, but mutant seeds are defective in mucilage extrusion.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 47 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for signal, propeptide, chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-24 | |||||
Sequence: MSSSFLSSTAFFLLLCLGFCHVSS | ||||||
Propeptide | PRO_0000042846 | 25-106 | ||||
Sequence: SSSDQGTYIVHMAKSQMPSSFDLHSNWYDSSLRSISDSAELLYTYENAIHGFSTRLTQEEADSLMTQPGVISVLPEHRYELH | ||||||
Chain | PRO_0000042847 | 107-757 | Subtilisin-like protease SBT1.7 | |||
Sequence: TTRTPLFLGLDEHTADLFPEAGSYSDVVVGVLDTGVWPESKSYSDEGFGPIPSSWKGGCEAGTNFTASLCNRKLIGARFFARGYESTMGPIDESKESRSPRDDDGHGTHTSSTAAGSVVEGASLLGYASGTARGMAPRARVAVYKVCWLGGCFSSDILAAIDKAIADNVNVLSMSLGGGMSDYYRDGVAIGAFAAMERGILVSCSAGNAGPSSSSLSNVAPWITTVGAGTLDRDFPALAILGNGKNFTGVSLFKGEALPDKLLPFIYAGNASNATNGNLCMTGTLIPEKVKGKIVMCDRGINARVQKGDVVKAAGGVGMILANTAANGEELVADAHLLPATTVGEKAGDIIRHYVTTDPNPTASISILGTVVGVKPSPVVAAFSSRGPNSITPNILKPDLIAPGVNILAAWTGAAGPTGLASDSRRVEFNIISGTSMSCPHVSGLAALLKSVHPEWSPAAIRSALMTTAYKTYKDGKPLLDIATGKPSTPFDHGAGHVSPTTATNPGLIYDLTTEDYLGFLCALNYTSPQIRSVSRRNYTCDPSKSYSVADLNYPSFAVNVDGVGAYKYTRTVTSVGGAGTYSVKVTSETTGVKISVEPAVLNFKEANEKKSYTVTFTVDSSKPSGSNSFGSIEWSDGKHVVGSPVAISWT | ||||||
Glycosylation | 170 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 352 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 376 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 379 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 631 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 644 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in immature siliques and at lower levels in stems and flowers (PubMed:11055401, PubMed:12413398, PubMed:7647567).
Widely expressed at low levels (PubMed:18266922).
Widely expressed at low levels (PubMed:18266922).
Induction
By methyl jasmonate.
Developmental stage
Highest levels of expression detected during silique development (PubMed:7647567).
Hihghly expressed in the seed coat during seed development (PubMed:18266922).
Hihghly expressed in the seed coat during seed development (PubMed:18266922).
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain, compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 31-106 | Inhibitor I9 | ||||
Sequence: TYIVHMAKSQMPSSFDLHSNWYDSSLRSISDSAELLYTYENAIHGFSTRLTQEEADSLMTQPGVISVLPEHRYELH | ||||||
Domain | 102-610 | Peptidase S8 | ||||
Sequence: RYELHTTRTPLFLGLDEHTADLFPEAGSYSDVVVGVLDTGVWPESKSYSDEGFGPIPSSWKGGCEAGTNFTASLCNRKLIGARFFARGYESTMGPIDESKESRSPRDDDGHGTHTSSTAAGSVVEGASLLGYASGTARGMAPRARVAVYKVCWLGGCFSSDILAAIDKAIADNVNVLSMSLGGGMSDYYRDGVAIGAFAAMERGILVSCSAGNAGPSSSSLSNVAPWITTVGAGTLDRDFPALAILGNGKNFTGVSLFKGEALPDKLLPFIYAGNASNATNGNLCMTGTLIPEKVKGKIVMCDRGINARVQKGDVVKAAGGVGMILANTAANGEELVADAHLLPATTVGEKAGDIIRHYVTTDPNPTASISILGTVVGVKPSPVVAAFSSRGPNSITPNILKPDLIAPGVNILAAWTGAAGPTGLASDSRRVEFNIISGTSMSCPHVSGLAALLKSVHPEWSPAAIRSALMTTAYKTYKDGKPLLDIATGKPSTPFDHGAGHVSPTTAT | ||||||
Compositional bias | 196-214 | Basic and acidic residues | ||||
Sequence: PIDESKESRSPRDDDGHGT | ||||||
Region | 196-219 | Disordered | ||||
Sequence: PIDESKESRSPRDDDGHGTHTSST |
Sequence similarities
Belongs to the peptidase S8 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length757
- Mass (Da)79,415
- Last updated1998-08-01 v1
- ChecksumE7F68FCAD16700AB
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 41 | in Ref. 5; CAA59963 | ||||
Sequence: M → T | ||||||
Compositional bias | 196-214 | Basic and acidic residues | ||||
Sequence: PIDESKESRSPRDDDGHGT | ||||||
Sequence conflict | 242-247 | in Ref. 5; CAA59963 | ||||
Sequence: APRARV → LHAL | ||||||
Sequence conflict | 562 | in Ref. 4; AAM10321/AAN46863 | ||||
Sequence: W → C | ||||||
Sequence conflict | 670 | in Ref. 5; CAA59963 | ||||
Sequence: V → A |
Mass Spectrometry
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF065639 EMBL· GenBank· DDBJ | AAC18851.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AB007645 EMBL· GenBank· DDBJ | BAB09021.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002688 EMBL· GenBank· DDBJ | AED98332.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF360285 EMBL· GenBank· DDBJ | AAK25995.1 EMBL· GenBank· DDBJ | mRNA | ||
AY091773 EMBL· GenBank· DDBJ | AAM10321.1 EMBL· GenBank· DDBJ | mRNA | ||
AY142612 EMBL· GenBank· DDBJ | AAN13181.1 EMBL· GenBank· DDBJ | mRNA | ||
BT001082 EMBL· GenBank· DDBJ | AAN46863.1 EMBL· GenBank· DDBJ | mRNA | ||
X85974 EMBL· GenBank· DDBJ | CAA59963.1 EMBL· GenBank· DDBJ | mRNA |