Q9SIV9 · PPA10_ARATH
- ProteinPurple acid phosphatase 10
- GenePAP10
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids468 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
Function
Catalytic activity
- a phosphate monoester + H2O = an alcohol + phosphate
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 Fe cation per subunit.
Note: Binds 1 zinc ion per subunit.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 167 | Fe cation (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 196 | Fe cation (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 196 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 199 | Fe cation (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 233 | substrate | ||||
Sequence: N | ||||||
Binding site | 233 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 318 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 328 | Proton donor | ||||
Sequence: H | ||||||
Binding site | 355 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 355-357 | substrate | ||||
Sequence: HVH | ||||||
Binding site | 357 | Fe cation (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | extracellular region | |
Cellular Component | plant-type cell wall | |
Cellular Component | plasmodesma | |
Molecular Function | acid phosphatase activity | |
Molecular Function | metal ion binding | |
Biological Process | cellular response to phosphate starvation |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePurple acid phosphatase 10
- EC number
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ9SIV9
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-25 | |||||
Sequence: MGRVRKSDFGSIVLVLCCVLNSLLC | ||||||
Chain | PRO_0000372815 | 26-468 | Purple acid phosphatase 10 | |||
Sequence: NGGITSRYVRKLEATVDMPLDSDVFRVPCGYNAPQQVHITQGDVEGKAVIVSWVTQEAKGSNKVIYWKENSTKKHKAHGKTNTYKFYNYTSGFIHHCPIRNLEYDTKYYYVLGVGQTERKFWFFTPPEIGPDVPYTFGLIGDLGQSYDSNITLTHYENNPTKGQAVLFVGDISYADTYPDHDNRRWDSWGRFAERSTAYQPWIWTTGNHELDFAPEIGENRPFKPFTHRYRTPYRSSGSTEPFWYSIKRGPAYIIVLASYSAYGKYTPQYQWLEEEFPKVNRTETPWLIVLMHSPWYNSYDYHYMEGETMRVMYEAWFVKYKVDVVFAGHVHAYERSERVSNIAYNVVNGICTPVKDQSAPVYITIGDGGNIEGLATKMTEPQPKYSAFREASFGHAIFSIKNRTHAHYGWHRNHDGYAVEGDRMWFYNRFWHPVDDSPSCNS | ||||||
Glycosylation | 95 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 113 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 175 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 306 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 377 | Interchain | ||||
Sequence: C | ||||||
Glycosylation | 428 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in roots, stems, leaves, flowers and siliques.
Induction
By phosphate deprivation, mostly isoform 2.
Gene expression databases
Interaction
Structure
Family & Domains
Sequence similarities
Belongs to the metallophosphoesterase superfamily. Purple acid phosphatase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative splicing.
Q9SIV9-1
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
- Length468
- Mass (Da)54,219
- Last updated2000-05-01 v1
- ChecksumED1EB9821C5C118B
Q9SIV9-2
- Name2
- NoteMay be due to intron retention.
- Differences from canonical
- 1-128: MGRVRKSDFGSIVLVLCCVLNSLLCNGGITSRYVRKLEATVDMPLDSDVFRVPCGYNAPQQVHITQGDVEGKAVIVSWVTQEAKGSNKVIYWKENSTKKHKAHGKTNTYKFYNYTSGFIHHCPIRNLE → MLWFFLLQ
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_037192 | 1-128 | in isoform 2 | |||
Sequence: MGRVRKSDFGSIVLVLCCVLNSLLCNGGITSRYVRKLEATVDMPLDSDVFRVPCGYNAPQQVHITQGDVEGKAVIVSWVTQEAKGSNKVIYWKENSTKKHKAHGKTNTYKFYNYTSGFIHHCPIRNLE → MLWFFLLQ | ||||||
Sequence conflict | 167 | in Ref. 1; AAM16283 | ||||
Sequence: D → N | ||||||
Sequence conflict | 280 | in Ref. 1; AAM16283 | ||||
Sequence: I → V | ||||||
Sequence conflict | 441 | in Ref. 1; AAM16283 | ||||
Sequence: D → G |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF492662 EMBL· GenBank· DDBJ | AAM15911.1 EMBL· GenBank· DDBJ | mRNA | ||
AY090893 EMBL· GenBank· DDBJ | AAM16283.1 EMBL· GenBank· DDBJ | mRNA | ||
AC007047 EMBL· GenBank· DDBJ | AAD22297.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002685 EMBL· GenBank· DDBJ | AEC06495.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002685 EMBL· GenBank· DDBJ | AEC06496.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY093236 EMBL· GenBank· DDBJ | AAM13235.1 EMBL· GenBank· DDBJ | mRNA | ||
BT008761 EMBL· GenBank· DDBJ | AAP49523.1 EMBL· GenBank· DDBJ | mRNA |