Q9M1L7 · PRK3_ARATH
- ProteinPollen receptor-like kinase 3
- GenePRK3
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids633 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Receptor-like kinase involved in the control of pollen germination and pollen tube polar growth (PubMed:23024212).
Can phosphorylate ROPGEF1 in vitro (PubMed:23024212).
Can phosphorylate ROPGEF1 in vitro (PubMed:23024212).
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
Activity regulation
The phosphorylation activity is calcium-independent.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | membrane | |
Cellular Component | plasmodesma | |
Molecular Function | ATP binding | |
Molecular Function | protein serine kinase activity | |
Molecular Function | protein serine/threonine kinase activity | |
Biological Process | regulation of pollen tube growth |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePollen receptor-like kinase 3
- EC number
- Short namesAtPRK3
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ9M1L7
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Single-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 249-269 | Helical | ||||
Sequence: AKAIFMVILFLLIFLFVVAII |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-19 | |||||
Sequence: MTAVLFLCFLLICFSFTPS | ||||||
Chain | PRO_0000431924 | 20-633 | Pollen receptor-like kinase 3 | |||
Sequence: LQNVSESEPLVRFKRSVNITKGDLNSWRTGTDPCNGKWFGIYCQKGQTVSGIHVTRLGLSGTINIEDLKDLPNLRTIRLDNNLLSGPLPPFFKLPGLKSLLLSNNSFSGEIADDFFKETPQLKRVFLDNNRLSGKIPASLMQLAGLEELHMQGNQFTGEIPPLTDGNKVLKSLDLSNNDLEGEIPITISDRKNLEMKFEGNQRLCGSPLNIECDEKPSSTGSGNEKNNTAKAIFMVILFLLIFLFVVAIITRWKKKRQPEFRMLGKDHLSDQESVEVRVPDSIKKPIDSSKKRSNAEGSSKKGSSHNGKGAGGGPGSGMGDIIMVNSEKGSFGLPDLMKAAAEVLGNGSLGSAYKAVMANGLSVVVKRIRDMNKLAREAFDTEMQRFGKLRHPNVLTPLAYHYRREEKLVVSEYMPKSSLLYVLHGDRGVYHSELTWATRLKIIQGVARGMDFLHEEFASYDLPHGNLKSSNVLLSETYEPLISDYAFLPLLQPNNASQALFAFKSPEFVQNQQVSPKSDVYCLGIIVLEVMTGKFPSQYLNTGKGGTDIVEWVQSSIAQHKEEELIDPEIASNTDSIKQMVELLRIGAACIASNPNERQNMKEIVRRIERVTL | ||||||
Glycosylation | 22 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 37 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 53↔62 | |||||
Sequence: CNGKWFGIYC | ||||||
Glycosylation | 123 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 224↔232 | |||||
Sequence: CGSPLNIEC | ||||||
Glycosylation | 246 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 438 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 458 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 535 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in pollen and/or in flowers, but not in leaves.
Gene expression databases
Structure
Family & Domains
Features
Showing features for repeat, compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 90-115 | LRR 1 | ||||
Sequence: LPNLRTIRLDNNLLSGPLPPFFKLPG | ||||||
Repeat | 117-137 | LRR 2 | ||||
Sequence: KSLLLSNNSFSGEIADDFFKE | ||||||
Repeat | 138-162 | LRR 3 | ||||
Sequence: TPQLKRVFLDNNRLSGKIPASLMQL | ||||||
Repeat | 163-186 | LRR 4 | ||||
Sequence: AGLEELHMQGNQFTGEIPPLTDGN | ||||||
Repeat | 188-210 | LRR 5 | ||||
Sequence: VLKSLDLSNNDLEGEIPITISDR | ||||||
Compositional bias | 294-318 | Basic and acidic residues | ||||
Sequence: VEVRVPDSIKKPIDSSKKRSNAEGS | ||||||
Region | 294-339 | Disordered | ||||
Sequence: VEVRVPDSIKKPIDSSKKRSNAEGSSKKGSSHNGKGAGGGPGSGMG | ||||||
Domain | 358-633 | Protein kinase | ||||
Sequence: KAAAEVLGNGSLGSAYKAVMANGLSVVVKRIRDMNKLAREAFDTEMQRFGKLRHPNVLTPLAYHYRREEKLVVSEYMPKSSLLYVLHGDRGVYHSELTWATRLKIIQGVARGMDFLHEEFASYDLPHGNLKSSNVLLSETYEPLISDYAFLPLLQPNNASQALFAFKSPEFVQNQQVSPKSDVYCLGIIVLEVMTGKFPSQYLNTGKGGTDIVEWVQSSIAQHKEEELIDPEIASNTDSIKQMVELLRIGAACIASNPNERQNMKEIVRRIERVTL |
Domain
The protein kinase domain may be catalytically impaired due to the lack of the conserved Asp active site at position 486, which is replaced by a Asn residue.
Sequence similarities
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length633
- Mass (Da)70,249
- Last updated2000-10-01 v1
- ChecksumD3A1859FF9E02169
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 294-318 | Basic and acidic residues | ||||
Sequence: VEVRVPDSIKKPIDSSKKRSNAEGS |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL138654 EMBL· GenBank· DDBJ | CAB86675.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002686 EMBL· GenBank· DDBJ | AEE77758.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
DQ446723 EMBL· GenBank· DDBJ | ABE65985.1 EMBL· GenBank· DDBJ | mRNA | ||
FJ708731 EMBL· GenBank· DDBJ | ACN59326.1 EMBL· GenBank· DDBJ | mRNA |