Q7XV05 · SERK2_ORYSJ
- ProteinLRR receptor kinase SERK2
- GeneSERK2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids628 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
LRR receptor kinase involved in positive regulation of somatic embryogenesis and defense response against the rice blast fungus pathogen Magnaporthe oryzae (PubMed:15968510).
Involved in the positive regulation of receptor kinase-mediated immunity. Required for immunity mediated by the LRR receptor kinases XA21 and XA26/XA3 which recognize effectors from the bacterial pathogen Xanthomonas oryzae pv. oryzae (Xoo). Required for the immune response mediated by the LRR receptor kinase FLS2 which recognizes specifically the bacterial flagellin (flg22) effector. Kinase activity and direct interaction with the immune receptors is critical for their function (PubMed:24482436).
Involved in the regulation of plant growth through the brassinosteroid (BR) signaling pathway (PubMed:19754838, PubMed:24482436).
Involved in the positive regulation of receptor kinase-mediated immunity. Required for immunity mediated by the LRR receptor kinases XA21 and XA26/XA3 which recognize effectors from the bacterial pathogen Xanthomonas oryzae pv. oryzae (Xoo). Required for the immune response mediated by the LRR receptor kinase FLS2 which recognizes specifically the bacterial flagellin (flg22) effector. Kinase activity and direct interaction with the immune receptors is critical for their function (PubMed:24482436).
Involved in the regulation of plant growth through the brassinosteroid (BR) signaling pathway (PubMed:19754838, PubMed:24482436).
Miscellaneous
Plants silencing SERK2 exhibit strong reduction of percentage of shoot regeneration from callus. Plants over-expressing SERK2 show enhanced resistance to the rice blast fungus Magnaporthe oryzae (PubMed:15968510).
Plants silencing SERK2 have compromised XA21- and XA3/XA26-mediated immunity to the bacterial leaf blight pathogen Xanthomonas oryzae pv. oryzae (Xoo). Plants silencing SERK2 display altered morphology and reduced sensitivity to the hormone brassinolide (PubMed:24482436).
Plants silencing SERK2 have compromised XA21- and XA3/XA26-mediated immunity to the bacterial leaf blight pathogen Xanthomonas oryzae pv. oryzae (Xoo). Plants silencing SERK2 display altered morphology and reduced sensitivity to the hormone brassinolide (PubMed:24482436).
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Molecular Function | ATP binding | |
Molecular Function | protein serine kinase activity | |
Molecular Function | protein serine/threonine kinase activity | |
Biological Process | brassinosteroid mediated signaling pathway | |
Biological Process | cell differentiation | |
Biological Process | defense response | |
Biological Process | positive regulation of innate immune response | |
Biological Process | regulation of defense response to fungus | |
Biological Process | regulation of growth | |
Biological Process | somatic embryogenesis |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameLRR receptor kinase SERK2
- EC number
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > BOP clade > Oryzoideae > Oryzeae > Oryzinae > Oryza > Oryza sativa
Accessions
- Primary accessionQ7XV05
- Secondary accessions
Proteomes
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 243-263 | Helical | ||||
Sequence: AIAGGVAAAAALLFAVPAIGF |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 128 | Abolishes binding capacity to BRI1. | ||||
Sequence: D → N |
PTM/Processing
Features
Showing features for signal, chain, glycosylation, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Signal | 1-31 | UniProt | |||||
Sequence: MAEARLLRRRRLCLAVPFVWVVAVAVSRVGA | |||||||
Chain | PRO_5010508816 | 32-628 | UniProt | LRR receptor kinase SERK2 | |||
Sequence: NTEGDALYSLRQSLKDANNVLQSWDPTLVNPCTWFHVTCNPDNSVIRVDLGNAQLSGALVPQLGQLKNLQYLELYSNNISGTIPNELGNLTNLVSLDLYLNNFTGFIPETLGQLYKLRFLRLNNNSLSGSIPKSLTNITTLQVLDLSNNNLSGEVPSTGSFSLFTPISFANNKDLCGPGTTKPCPGAPPFSPPPPFNPPTPTVSQGDSKTGAIAGGVAAAAALLFAVPAIGFAWWRRRKPEEHFFDVPAEEDPEVHLGQLKRFSLRELQVATDNFSNKNILGRGGFGKVYKGRLADGSLVAVKRLKEERTPGGELQFQTEVEMISMAVHRNLLRLRGFCMTPTERLLVYPYMANGSVASRLRERQPNDPPLEWQTRTRIALGSARGLSYLHDHCDPKIIHRDVKAANILLDEDFEAVVGDFGLAKLMDYKDTHVTTAVRGTIGHIAPEYLSTGKSSEKTDVFGYGIMLLELITGQRAFDLARLANDDDVMLLDWVKGLLKEKKVEMLVDPDLQSGFVEHEVESLIQVALLCTQGSPMDRPKMSEVVRMLEGDGLAERWEEWQKVEVVRQEAELAPRHNDWIVDSTYNLRAMELSGPR | |||||||
Glycosylation | 109 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 120 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 133 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 155 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 168 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 181 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Modified residue | 303 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 329 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 350 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 356 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 387 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 463 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 463 | PTMeXchange | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 466 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 466 | PTMeXchange | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 472 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 615 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 616 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 625 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 625 | PTMeXchange | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Autophosphorylated on serine and threonine residues.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in flag leaves (PubMed:11332734).
Expressed in roots, shoot apex, leaf blades, leaf sheaths, panicles and flowers (PubMed:16081169).
Expressed leaves, stems, sheaths and flowers (PubMed:24482436).
Expressed in roots, shoot apex, leaf blades, leaf sheaths, panicles and flowers (PubMed:16081169).
Expressed leaves, stems, sheaths and flowers (PubMed:24482436).
Induction
Induced by infection with the rice blast fungus Magnaporthe oryzae (PubMed:11332734, PubMed:15968510).
Induced by salicylate (SA), jasmonate (JA), abscisic acid (ABA) and benzothiadiazole (BTH) (PubMed:15968510).
Induced by salicylate (SA), jasmonate (JA), abscisic acid (ABA) and benzothiadiazole (BTH) (PubMed:15968510).
Gene expression databases
Structure
Family & Domains
Features
Showing features for repeat, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 97-121 | LRR 1 | ||||
Sequence: LKNLQYLELYSNNISGTIPNELGNL | ||||||
Repeat | 123-144 | LRR 2 | ||||
Sequence: NLVSLDLYLNNFTGFIPETLGQ | ||||||
Repeat | 145-169 | LRR 3 | ||||
Sequence: LYKLRFLRLNNNSLSGSIPKSLTNI | ||||||
Repeat | 170-194 | LRR 4 | ||||
Sequence: TTLQVLDLSNNNLSGEVPSTGSFSL | ||||||
Domain | 306-593 | Protein kinase | ||||
Sequence: FSNKNILGRGGFGKVYKGRLADGSLVAVKRLKEERTPGGELQFQTEVEMISMAVHRNLLRLRGFCMTPTERLLVYPYMANGSVASRLRERQPNDPPLEWQTRTRIALGSARGLSYLHDHCDPKIIHRDVKAANILLDEDFEAVVGDFGLAKLMDYKDTHVTTAVRGTIGHIAPEYLSTGKSSEKTDVFGYGIMLLELITGQRAFDLARLANDDDVMLLDWVKGLLKEKKVEMLVDPDLQSGFVEHEVESLIQVALLCTQGSPMDRPKMSEVVRMLEGDGLAERWEEWQ |
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.
- Length628
- Mass (Da)69,588
- Last updated2003-10-01 v1
- ChecksumF4F63F3D5879904C
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0P0WBA5 | A0A0P0WBA5_ORYSJ | Os04g0457800 | 276 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 17-18 | in Ref. 1; AAU88198 and 6; EAZ30959 | ||||
Sequence: PF → AV |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY652735 EMBL· GenBank· DDBJ | AAU88198.1 EMBL· GenBank· DDBJ | mRNA | ||
AL606636 EMBL· GenBank· DDBJ | CAD40895.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP014960 EMBL· GenBank· DDBJ | BAS89517.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP008210 EMBL· GenBank· DDBJ | BAF14889.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CM000141 EMBL· GenBank· DDBJ | EAZ30959.1 EMBL· GenBank· DDBJ | Genomic DNA |