A0A0P0VIP0 · LRSK7_ORYSJ
- ProteinL-type lectin-domain containing receptor kinase S.7
- GeneLECRKS7
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids695 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Legume-lectin receptor-like kinase required for normal pollen development and male fertility (PubMed:31833176, PubMed:32284546).
Regulates pollen exine assembly and aperture development (PubMed:31833176, PubMed:32284546).
Plays a critical role in annulus formation, and may participate in the formation of the fibrillar-granular layer underneath the operculum (PubMed:32284546).
May function by regulating the expression of genes involved in pollen exine development (PubMed:31833176).
Kinase activity is required for its function in pollen development (PubMed:31833176).
Regulates pollen exine assembly and aperture development (PubMed:31833176, PubMed:32284546).
Plays a critical role in annulus formation, and may participate in the formation of the fibrillar-granular layer underneath the operculum (PubMed:32284546).
May function by regulating the expression of genes involved in pollen exine development (PubMed:31833176).
Kinase activity is required for its function in pollen development (PubMed:31833176).
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]This reaction proceeds in the forward direction.
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | plasma membrane | |
Cellular Component | pollen aperture | |
Molecular Function | ATP binding | |
Molecular Function | carbohydrate binding | |
Molecular Function | kinase activity | |
Molecular Function | protein serine/threonine kinase activity | |
Biological Process | defense response to bacterium | |
Biological Process | defense response to oomycetes | |
Biological Process | pollen aperture formation | |
Biological Process | pollen development | |
Biological Process | protein autophosphorylation |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameL-type lectin-domain containing receptor kinase S.7
- EC number
- Short namesOsLecRK-S.7
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > BOP clade > Oryzoideae > Oryzeae > Oryzinae > Oryza > Oryza sativa
Accessions
- Primary accessionA0A0P0VIP0
- Secondary accessions
Proteomes
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass type I membrane protein
Note: During meiosis, localizes diffusely in the cytosol and plasma membrane of microspore mother cells (MMCs). During tetrad development, localizes at the corners. At late tetrad stage, accumulates to the four corners of the tetrad, assembled into ring-like structures marking future aperture sites. When microspores are released from tetrads and preliminary aperture structures has formed, remains in a distinctly ring-shaped distribution beneath the aperture in the plasma membrane between the annulus and operculum.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 24-331 | Extracellular | ||||
Sequence: AAASSIAAAPASSYRRISWASNLTLLGSASLLPGAAGVALTTPSRDGVGAGRALFSEPVRLLLPQDAAASASASRAATPASFSTRFTFRITPSPTYGDGLAFLLTSSRTFLGASNGFLGLFPSSSASDEGELRDVSTVAVEIDTHLDVALHDPDGNHVALDAGSIFSVASAQPGVDLKAGVPITAWVEYRAPRRRLNVWLSYSPSRRPEKPALSADVDLSGLLRTYMYAGFSASNGNGAALHVVERWTFRTFGFPNSSYAPPPTKYIGPMPPNNQPLPPPPSPSPSPPPPSPPPPPHPNHRRRHLFYK | ||||||
Transmembrane | 332-352 | Helical | ||||
Sequence: VLGGVLGGMVLLGLVVVGSAV | ||||||
Topological domain | 353-695 | Cytoplasmic | ||||
Sequence: LLGRSVRRKNQEHAVASEDMGEATLSMEVARAATKGFDSGNVIGVGGSGATVYEGVLPSGSRVAVKRFQAIGSCTKAFDSELKAMLNCPHHPNLVPLAGWCRSKDELVLVYEFMPNGNLDSALHTLGGATLPWEARFRAVYGVASALAYLHDECENRIIHRDVKSSNVMLDAEFNARLGDFGLARTVSHGGLPLTTQPAGTLGYLAPEYVHTGVATERSDVYSFGVLALEVATGRRPAERGISVVNWVWTLWGRRRLVDAADRRLQGRFVADEMRRVLLVGLCCVHPDCRKRPGMRRVVSMLDGTAPLILVPDKMPPVLLQPVPNASSMNSADTANTAFFSCR |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Male sterility due to aborted pollen grains with abnormal exine an intine, and defective aperture (PubMed:32284546).
Aborted pollen grains with defective apertures and intine formation, and male sterility (PubMed:32284546).
Aborted pollen grains with defective apertures and intine formation, and male sterility (PubMed:32284546).
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 418 | Loss of kinase activity. | ||||
Sequence: K → E | ||||||
Mutagenesis | 560 | In s13283; loss of kinase activity and male sterile phenotype. | ||||
Sequence: E → K |
PTM/Processing
Features
Showing features for signal, chain, glycosylation, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-23 | |||||
Sequence: MPPRCRRLPLLFILLLAVRPLSA | ||||||
Chain | PRO_5006056350 | 24-695 | L-type lectin-domain containing receptor kinase S.7 | |||
Sequence: AAASSIAAAPASSYRRISWASNLTLLGSASLLPGAAGVALTTPSRDGVGAGRALFSEPVRLLLPQDAAASASASRAATPASFSTRFTFRITPSPTYGDGLAFLLTSSRTFLGASNGFLGLFPSSSASDEGELRDVSTVAVEIDTHLDVALHDPDGNHVALDAGSIFSVASAQPGVDLKAGVPITAWVEYRAPRRRLNVWLSYSPSRRPEKPALSADVDLSGLLRTYMYAGFSASNGNGAALHVVERWTFRTFGFPNSSYAPPPTKYIGPMPPNNQPLPPPPSPSPSPPPPSPPPPPHPNHRRRHLFYKVLGGVLGGMVLLGLVVVGSAVLLGRSVRRKNQEHAVASEDMGEATLSMEVARAATKGFDSGNVIGVGGSGATVYEGVLPSGSRVAVKRFQAIGSCTKAFDSELKAMLNCPHHPNLVPLAGWCRSKDELVLVYEFMPNGNLDSALHTLGGATLPWEARFRAVYGVASALAYLHDECENRIIHRDVKSSNVMLDAEFNARLGDFGLARTVSHGGLPLTTQPAGTLGYLAPEYVHTGVATERSDVYSFGVLALEVATGRRPAERGISVVNWVWTLWGRRRLVDAADRRLQGRFVADEMRRVLLVGLCCVHPDCRKRPGMRRVVSMLDGTAPLILVPDKMPPVLLQPVPNASSMNSADTANTAFFSCR | ||||||
Glycosylation | 45 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 279 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 376 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 378 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 386 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 403 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 657 | Phosphothreonine | ||||
Sequence: T |
Post-translational modification
Autophosphorylated at Thr-376; Ser-378; Thr-386; Thr-403 and Thr-657.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in roots, leaves, lemma, palea, pistil and anthers.
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 37-276 | Legume-lectin like | ||||
Sequence: YRRISWASNLTLLGSASLLPGAAGVALTTPSRDGVGAGRALFSEPVRLLLPQDAAASASASRAATPASFSTRFTFRITPSPTYGDGLAFLLTSSRTFLGASNGFLGLFPSSSASDEGELRDVSTVAVEIDTHLDVALHDPDGNHVALDAGSIFSVASAQPGVDLKAGVPITAWVEYRAPRRRLNVWLSYSPSRRPEKPALSADVDLSGLLRTYMYAGFSASNGNGAALHVVERWTFRTFG | ||||||
Compositional bias | 286-319 | Pro residues | ||||
Sequence: PTKYIGPMPPNNQPLPPPPSPSPSPPPPSPPPPP | ||||||
Region | 286-323 | Disordered | ||||
Sequence: PTKYIGPMPPNNQPLPPPPSPSPSPPPPSPPPPPHPNH | ||||||
Domain | 389-661 | Protein kinase | ||||
Sequence: FDSGNVIGVGGSGATVYEGVLPSGSRVAVKRFQAIGSCTKAFDSELKAMLNCPHHPNLVPLAGWCRSKDELVLVYEFMPNGNLDSALHTLGGATLPWEARFRAVYGVASALAYLHDECENRIIHRDVKSSNVMLDAEFNARLGDFGLARTVSHGGLPLTTQPAGTLGYLAPEYVHTGVATERSDVYSFGVLALEVATGRRPAERGISVVNWVWTLWGRRRLVDAADRRLQGRFVADEMRRVLLVGLCCVHPDCRKRPGMRRVVSMLDGTAPLI |
Sequence similarities
In the N-terminal section; belongs to the leguminous lectin family.
In the C-terminal section; 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.
- Length695
- Mass (Da)74,135
- Last updated2016-01-20 v1
- Checksum2F534B41133DB0C5
Sequence caution
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 286-319 | Pro residues | ||||
Sequence: PTKYIGPMPPNNQPLPPPPSPSPSPPPPSPPPPP |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AP005650 EMBL· GenBank· DDBJ | BAD19984.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
AP008208 EMBL· GenBank· DDBJ | BAF08699.2 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation | |
AP014958 EMBL· GenBank· DDBJ | BAS78542.1 EMBL· GenBank· DDBJ | Genomic DNA |