Q9FEB5 · DSPG4_ARATH
- ProteinPhosphoglucan phosphatase DSP4, chloroplastic
- GeneDSP4
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids379 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Miscellaneous
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 90 | substrate | ||||
Sequence: Y | ||||||
Binding site | 166 | substrate | ||||
Sequence: D | ||||||
Active site | 198 | Phosphocysteine intermediate | ||||
Sequence: C | ||||||
Binding site | 199-204 | substrate | ||||
Sequence: TAGMGR | ||||||
Binding site | 307 | substrate | ||||
Sequence: K | ||||||
Binding site | 332 | substrate | ||||
Sequence: N |
GO annotations
all annotations | all molecular function | nucleotide binding | molecular_function | nucleic acid binding | dna binding | chromatin binding | dna-binding transcription factor activity | rna binding | cytoskeletal motor activity | catalytic activity | nuclease activity | signaling receptor binding | structural molecule activity | transporter activity | binding | protein binding | translation factor activity, rna binding | lipid binding | kinase activity | transferase activity | hydrolase activity | oxygen binding | enzyme regulator activity | carbohydrate binding | signaling receptor activity | translation regulator activity | transcription regulator activity | other molecular function | all biological process | carbohydrate metabolic process | generation of precursor metabolites and energy | nucleobase-containing compound metabolic process | dna metabolic process | translation | lipid metabolic process | transport | response to stress | cell cycle | cell communication | signal transduction | cell-cell signaling | multicellular organism development | circadian rhythm | biological_process | metabolic process | catabolic process | biosynthetic process | response to light stimulus | response to external stimulus | tropism | response to biotic stimulus | response to abiotic stimulus | response to endogenous stimulus | embryo development | post-embryonic development | fruit ripening | abscission | pollination | flower development | cellular process | programmed cell death | photosynthesis | cellular component organization | cell growth | protein metabolic process | cellular homeostasis | secondary metabolic process | reproductive process | cell differentiation | protein modification process | growth | epigenetic regulation of gene expression | response to chemical | anatomical structure development | regulation of molecular function | other biological process | all cellular component | cellular_component | extracellular region | cell wall | intracellular anatomical structure | nucleus | nuclear envelope | nucleoplasm | nucleolus | cytoplasm | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | cytosol | ribosome | cytoskeleton | plasma membrane | chloroplast | plastid | thylakoid | membrane | external encapsulating structure | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | chloroplast | |
Cellular Component | chloroplast stroma | |
Molecular Function | amylopectin binding | |
Molecular Function | carbohydrate phosphatase activity | |
Molecular Function | phosphoprotein phosphatase activity | |
Molecular Function | polysaccharide binding | |
Biological Process | starch catabolic process | |
Biological Process | starch metabolic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended namePhosphoglucan phosphatase DSP4, 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 accessionQ9FEB5
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 90 | Reduces starch binding and glucan phosphatase activity. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 139 | Mildly reduces starch binding and glucan phosphatase activity. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 140 | Reduces glucan phosphatase activity. | ||||
Sequence: F → A | ||||||
Mutagenesis | 140 | Changes substrate specificity and enhances glucan dephosphorylation at C3. Leads to preferential glucan dephosphorylation at C6; when associated with G-235. | ||||
Sequence: F → W | ||||||
Mutagenesis | 167 | Increases glucan phosphatase activity. | ||||
Sequence: F → M | ||||||
Mutagenesis | 167 | No effect on glucan phosphatase activity. | ||||
Sequence: F → S | ||||||
Mutagenesis | 167 | Reduces glucan phosphatase activity 3-fold. | ||||
Sequence: F → Y | ||||||
Mutagenesis | 198 | Loss of glucan phosphatase activity. | ||||
Sequence: C → S | ||||||
Mutagenesis | 200-203 | Loss of glucan phosphatase activity. | ||||
Sequence: AGMG → TGFD | ||||||
Mutagenesis | 203 | Nearly abolishes glucan phosphatase activity. | ||||
Sequence: G → D | ||||||
Mutagenesis | 235 | Slightly reduces starch binding and glucan phosphatase activity. | ||||
Sequence: F → A | ||||||
Mutagenesis | 235 | Changes substrate specificity and enhances glucan dephosphorylation at C3. Leads to preferential glucan dephosphorylation at C6; when associated with W-140. | ||||
Sequence: F → G | ||||||
Mutagenesis | 237 | Slightly reduces glucan phosphatase activity. | ||||
Sequence: K → A | ||||||
Mutagenesis | 278 | Nearly abolishes glucan phosphatase activity. Strongly reduces starch binding efficiency. | ||||
Sequence: W → A | ||||||
Mutagenesis | 278 | Reduces starch binding efficiency. | ||||
Sequence: W → G | ||||||
Mutagenesis | 307 | Strongly reduces glucan phosphatase activity. Strongly reduces starch binding efficiency. | ||||
Sequence: K → A | ||||||
Mutagenesis | 314 | Nearly abolishes glucan phosphatase activity. | ||||
Sequence: W → A | ||||||
Mutagenesis | 329 | Loss starch-binding capacity. | ||||
Sequence: G → R | ||||||
Mutagenesis | 330 | Decreases glucan phosphatase activity. | ||||
Sequence: H → A | ||||||
Mutagenesis | 332 | Nearly abolishes glucan phosphatase activity. Loss of starch binding. | ||||
Sequence: N → A | ||||||
Mutagenesis | 333 | Loss of glucan phosphatase activity and starch-binding capacity. | ||||
Sequence: N → K |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 11 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 | 1-54 | Chloroplast | ||||
Sequence: MNCLQNLPRCSVSPLLGFGCIQRDHSSSSSSLKMLISPPIKANDPKSRLVLHAV | ||||||
Chain | PRO_0000417333 | 55-379 | Phosphoglucan phosphatase DSP4, chloroplastic | |||
Sequence: SESKSSSEMSGVAKDEEKSDEYSQDMTQAMGAVLTYRHELGMNYNFIRPDLIVGSCLQTPEDVDKLRKIGVKTIFCLQQDPDLEYFGVDISSIQAYAKKYSDIQHIRCEIRDFDAFDLRMRLPAVVGTLYKAVKRNGGVTYVHCTAGMGRAPAVALTYMFWVQGYKLMEAHKLLMSKRSCFPKLDAIRNATIDILTGLKRKTVTLTLKDKGFSRVEISGLDIGWGQRIPLTLDKGTGFWILKRELPEGQFEYKYIIDGEWTHNEAEPFIGPNKDGHTNNYAKVVDDPTSVDGTTRERLSSEDPELLEEERSKLIQFLETCSEAEV |
Proteomic databases
Expression
Induction
Gene expression databases
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9FEB5 | KIN11 P92958 | 2 | EBI-307215, EBI-307202 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, domain, motif, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 54-76 | Disordered | ||||
Sequence: VSESKSSSEMSGVAKDEEKSDEY | ||||||
Domain | 97-254 | Tyrosine-protein phosphatase | ||||
Sequence: NYNFIRPDLIVGSCLQTPEDVDKLRKIGVKTIFCLQQDPDLEYFGVDISSIQAYAKKYSDIQHIRCEIRDFDAFDLRMRLPAVVGTLYKAVKRNGGVTYVHCTAGMGRAPAVALTYMFWVQGYKLMEAHKLLMSKRSCFPKLDAIRNATIDILTGLKR | ||||||
Motif | 198-204 | Glucan phosphatase signature motif CXAGXGR | ||||
Sequence: CTAGMGR | ||||||
Region | 259-335 | Polysaccharide binding | ||||
Sequence: LTLKDKGFSRVEISGLDIGWGQRIPLTLDKGTGFWILKRELPEGQFEYKYIIDGEWTHNEAEPFIGPNKDGHTNNYA | ||||||
Region | 339-358 | Disordered | ||||
Sequence: DDPTSVDGTTRERLSSEDPE | ||||||
Compositional bias | 343-358 | Basic and acidic residues | ||||
Sequence: SVDGTTRERLSSEDPE |
Domain
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 1 isoforms produced by Alternative splicing. A number of isoforms are produced. According to EST sequences.
Q9FEB5-1
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
- Length379
- Mass (Da)42,626
- Last updated2001-03-01 v1
- Checksum4AA36B6E3E62A42B
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F4J5T0 | F4J5T0_ARATH | SEX4 | 292 | ||
A0A1I9LQR5 | A0A1I9LQR5_ARATH | SEX4 | 284 | ||
A0A1I9LQR6 | A0A1I9LQR6_ARATH | SEX4 | 281 |
Sequence caution
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 64 | in Ref. 4; AAL27495/AAN28817 | ||||
Sequence: S → R | ||||||
Sequence conflict | 84 | in Ref. 5; AAM61237 | ||||
Sequence: M → K | ||||||
Sequence conflict | 287 | in Ref. 4; AAL27495/AAN28817 | ||||
Sequence: D → G | ||||||
Compositional bias | 343-358 | Basic and acidic residues | ||||
Sequence: SVDGTTRERLSSEDPE |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ302781 EMBL· GenBank· DDBJ | CAC17593.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ302779 EMBL· GenBank· DDBJ | CAC18327.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
AJ302779 EMBL· GenBank· DDBJ | CAC18328.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL049711 EMBL· GenBank· DDBJ | CAB41338.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
CP002686 EMBL· GenBank· DDBJ | AEE78909.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF439823 EMBL· GenBank· DDBJ | AAL27495.1 EMBL· GenBank· DDBJ | mRNA | ||
AY143878 EMBL· GenBank· DDBJ | AAN28817.1 EMBL· GenBank· DDBJ | mRNA | ||
AY084675 EMBL· GenBank· DDBJ | AAM61237.1 EMBL· GenBank· DDBJ | mRNA |