Q1PFB9 · AGC17_ARATH
- ProteinSerine/threonine-protein kinase AGC1-7
- GeneAGC1-7
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids555 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Functions redudantly with AGC1-5 as signaling component in the pollen tube. Required for polarized growth of pollen tubes.
Catalytic activity
- L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H+
Activity regulation
Activated by PDPK1/PDK1.
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | ATP binding | |
Molecular Function | histone H2AS1 kinase activity | |
Molecular Function | kinase activity | |
Molecular Function | protein serine kinase activity | |
Biological Process | pollen tube growth | |
Biological Process | protein phosphorylation | |
Biological Process | unidimensional cell growth |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSerine/threonine-protein kinase AGC1-7
- 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 accessionQ1PFB9
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
No visible phenotype under normal growth conditions, but pollen of the double mutants agc1.5 and agc1.7 is impaired in polarized growth of pollen tube.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 36 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000431357 | 1-555 | Serine/threonine-protein kinase AGC1-7 | |||
Sequence: MLTKPGKKLDSSESTHHTTSSNYPPLDIVHQTPQPRKEMQQKPLFDPKKMDNLIKPEPAGFTNHHRPNPSPKIPSSPGSNMTESQSNLNTKPNNNNSNNNSNMSSRSNSIESTSSNPSKPHTGGDIRWDAVNTLTSKGVQLGISDFRLLKRLGYGDIGSVYLVELRGTITYFAMKVMDKASLASRNKLLRAQTEREILSQLDHPFLPTLYSHFETDKFYCLVMEFCGGGNLYSLRQKQPNKCFTEDAARFFASEVLLALEYLHMLGIVYRDLKPENVLVRDDGHIMLSDFDLSLRCSVSPTLVKSSSVHAAGGGSGSSRPVGLIDEDAAVQGCIQPSTFFPRILQSSKKNRKAKSDFGLFVNGSMPELMAEPTNVKSMSFVGTHEYLAPEIIRGEGHGSAVDWWTFGIFIYELLYGATPFKGQGNRATLHNVIGQALRFPEVPHVSSAARDLIKGLLVKEPQKRIAYKRGATEIKQHPFFEGVNWALIRSATPPHVPEPVDFSCYASKDKESMAAVDGGGKKNNNGAGGGCSTGGGDNKPNGDCNDPDYIDFEYF |
Post-translational modification
Autophosphorylated and phosphorylated by PDPK1/PDK1.
Proteomic databases
Expression
Interaction
Subunit
Interacts with PDPK1/PDK1.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q1PFB9 | PDPK1 Q9XF67 | 2 | EBI-1103730, EBI-1103587 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-126 | Disordered | ||||
Sequence: MLTKPGKKLDSSESTHHTTSSNYPPLDIVHQTPQPRKEMQQKPLFDPKKMDNLIKPEPAGFTNHHRPNPSPKIPSSPGSNMTESQSNLNTKPNNNNSNNNSNMSSRSNSIESTSSNPSKPHTGGDI | ||||||
Compositional bias | 15-38 | Polar residues | ||||
Sequence: THHTTSSNYPPLDIVHQTPQPRKE | ||||||
Compositional bias | 75-121 | Polar residues | ||||
Sequence: SSPGSNMTESQSNLNTKPNNNNSNNNSNMSSRSNSIESTSSNPSKPH | ||||||
Domain | 146-480 | Protein kinase | ||||
Sequence: FRLLKRLGYGDIGSVYLVELRGTITYFAMKVMDKASLASRNKLLRAQTEREILSQLDHPFLPTLYSHFETDKFYCLVMEFCGGGNLYSLRQKQPNKCFTEDAARFFASEVLLALEYLHMLGIVYRDLKPENVLVRDDGHIMLSDFDLSLRCSVSPTLVKSSSVHAAGGGSGSSRPVGLIDEDAAVQGCIQPSTFFPRILQSSKKNRKAKSDFGLFVNGSMPELMAEPTNVKSMSFVGTHEYLAPEIIRGEGHGSAVDWWTFGIFIYELLYGATPFKGQGNRATLHNVIGQALRFPEVPHVSSAARDLIKGLLVKEPQKRIAYKRGATEIKQHPFF | ||||||
Domain | 481-555 | AGC-kinase C-terminal | ||||
Sequence: EGVNWALIRSATPPHVPEPVDFSCYASKDKESMAAVDGGGKKNNNGAGGGCSTGGGDNKPNGDCNDPDYIDFEYF | ||||||
Region | 514-547 | Disordered | ||||
Sequence: AAVDGGGKKNNNGAGGGCSTGGGDNKPNGDCNDP |
Sequence similarities
Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length555
- Mass (Da)61,069
- Last updated2006-05-16 v1
- Checksum94CF9E1B15DB3496
Sequence caution
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 15-38 | Polar residues | ||||
Sequence: THHTTSSNYPPLDIVHQTPQPRKE | ||||||
Compositional bias | 75-121 | Polar residues | ||||
Sequence: SSPGSNMTESQSNLNTKPNNNNSNNNSNMSSRSNSIESTSSNPSKPH |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC002986 EMBL· GenBank· DDBJ | AAC17041.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
CP002684 EMBL· GenBank· DDBJ | AEE36222.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002684 EMBL· GenBank· DDBJ | AEE36223.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002684 EMBL· GenBank· DDBJ | ANM59156.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002684 EMBL· GenBank· DDBJ | ANM59157.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DQ446444 EMBL· GenBank· DDBJ | ABE65785.1 EMBL· GenBank· DDBJ | mRNA |