Q9SRK5 · LSF2_ARATH
- ProteinPhosphoglucan phosphatase LSF2, chloroplastic
- GeneLSF2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids282 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Starch-associated phosphoglucan phosphatase that selectively dephosphorylates the glucan C3 position. Probably participates in the regulation of starch degradation.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 83 | substrate | ||||
Sequence: Y | ||||||
Binding site | 153-156 | substrate | ||||
Sequence: RHMR | ||||||
Binding site | 161 | substrate | ||||
Sequence: D | ||||||
Binding site | 177-180 | substrate | ||||
Sequence: SLEW | ||||||
Active site | 193 | Phosphocysteine intermediate | ||||
Sequence: C | ||||||
Binding site | 194-199 | substrate | ||||
Sequence: SAGLGR | ||||||
Binding site | 230 | substrate | ||||
Sequence: G | ||||||
Binding site | 245 | substrate | ||||
Sequence: K | ||||||
Binding site | 251 | substrate | ||||
Sequence: E | ||||||
Binding site | 259-263 | substrate | ||||
Sequence: NAFED | ||||||
Binding site | 268 | substrate | ||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast | |
Molecular Function | carbohydrate phosphatase activity | |
Molecular Function | phosphoprotein phosphatase activity | |
Molecular Function | starch binding | |
Molecular Function | sugar-phosphatase activity | |
Biological Process | starch catabolic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhosphoglucan phosphatase LSF2, chloroplastic
- 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 accessionQ9SRK5
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
No visible phenotype under normal growth conditions, but starch of mutant plants contains high levels of C3-bound phosphate.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 83 | Decreases starch C3 dephosphorylation. No effect on phosphatase activity with p-nitrophenyl phosphate. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 85 | Nearly abolishes starch C3 dephosphorylation. No effect on phosphatase activity with p-nitrophenyl phosphate. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 135 | Decreases starch C3 dephosphorylation. No effect on phosphatase activity with p-nitrophenyl phosphate. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 136 | Abolishes starch C3 dephosphorylation. No effect on phosphatase activity with p-nitrophenyl phosphate. | ||||
Sequence: W → A | ||||||
Mutagenesis | 153 | Decreases starch C3 dephosphorylation. No effect on phosphatase activity with p-nitrophenyl phosphate. | ||||
Sequence: R → A | ||||||
Mutagenesis | 155 | Decreases starch C3 dephosphorylation. No effect on phosphatase activity with p-nitrophenyl phosphate. | ||||
Sequence: M → A | ||||||
Mutagenesis | 157 | Decreases starch binding and starch C3 dephosphorylation. Moderate decrease of phosphatase activity with soluble substrates; when associated with A-261. Nearly abolishes activity with water-insoluble starch; when associated with A-261. | ||||
Sequence: R → A | ||||||
Mutagenesis | 162 | Decreases starch C3 dephosphorylation. No effect on phosphatase activity with p-nitrophenyl phosphate. | ||||
Sequence: F → A | ||||||
Mutagenesis | 180 | Decreases starch C3 dephosphorylation. No effect on phosphatase activity with p-nitrophenyl phosphate. | ||||
Sequence: W → A | ||||||
Mutagenesis | 193 | Abolishes phosphatase activity. | ||||
Sequence: C → S | ||||||
Mutagenesis | 194-198 | Abolishes glucan phosphatase activity. | ||||
Sequence: SAGLG → TTGFD | ||||||
Mutagenesis | 245 | Decreases starch C3 dephosphorylation. No effect on phosphatase activity with p-nitrophenyl phosphate. | ||||
Sequence: K → A | ||||||
Mutagenesis | 261 | Strongly decreases starch binding and starch C3 dephosphorylation. Moderate decrease of phosphatase activity with soluble substrates; when associated with A-157. Nearly abolishes activity with water-insoluble starch; when associated with A-157. | ||||
Sequence: F → A | ||||||
Mutagenesis | 268 | Decreases starch C3 dephosphorylation. No effect on phosphatase activity with p-nitrophenyl phosphate. | ||||
Sequence: E → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 27 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for transit peptide, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-61 | Chloroplast | ||||
Sequence: MSVIGSKSCIFSVARYTRENEKSSCFTSINKKSSLDLRFPRNLAGVSCKFSGENPGTNGVS | ||||||
Chain | PRO_0000417335 | 62-282 | Phosphoglucan phosphatase LSF2, chloroplastic | |||
Sequence: LSSKNKMEDYNTAMKRLMRSPYEYHHDLGMNYTLIRDELIVGSQPQKPEDIDHLKQEQNVAYILNLQQDKDIEYWGIDLDSIVRRCKELGIRHMRRPAKDFDPLSLRSQLPKAVSSLEWAVSEGKGRVYVHCSAGLGRAPGVSIAYMYWFCDMNLNTAYDTLVSKRPCGPNKGAIRGATYDLAKNDPWKEPFESLPENAFEDIADWERKLIQERVRALRGT |
Proteomic databases
Expression
Tissue specificity
Widely expressed.
Induction
Expressed with a circadian rhythm showing a peak at the end of the day and then decreasing to reach the lowest levels at the end of the night.
Gene expression databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 92-249 | Tyrosine-protein phosphatase | ||||
Sequence: NYTLIRDELIVGSQPQKPEDIDHLKQEQNVAYILNLQQDKDIEYWGIDLDSIVRRCKELGIRHMRRPAKDFDPLSLRSQLPKAVSSLEWAVSEGKGRVYVHCSAGLGRAPGVSIAYMYWFCDMNLNTAYDTLVSKRPCGPNKGAIRGATYDLAKNDPW | ||||||
Motif | 193-199 | Glucan phosphatase signature motif CXAGXGR | ||||
Sequence: CSAGLGR |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length282
- Mass (Da)32,087
- Last updated2000-05-01 v1
- ChecksumBDB1A93855C98849
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 38-39 | in Ref. 5; AAM64580 | ||||
Sequence: RF → SL |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC009991 EMBL· GenBank· DDBJ | AAF01527.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002686 EMBL· GenBank· DDBJ | AEE74980.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BT024510 EMBL· GenBank· DDBJ | ABD19691.1 EMBL· GenBank· DDBJ | mRNA | ||
AK226225 EMBL· GenBank· DDBJ | BAE98389.1 EMBL· GenBank· DDBJ | mRNA | ||
AY087019 EMBL· GenBank· DDBJ | AAM64580.1 EMBL· GenBank· DDBJ | mRNA |