Q9SKB2 · SBIR1_ARATH
- ProteinLeucine-rich repeat receptor-like serine/threonine/tyrosine-protein kinase SOBIR1
- GeneSOBIR1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids641 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Dual specificity kinase acting on both serine/threonine- and tyrosine-containing substrates. Acting as a counterplayer of BIR1, promotes the activation of plant defense and cell death (PubMed:19616764).
Component of the RLP23-SOBIR1-BAK1 complex that mediates NLP-triggered immunity (PubMed:27251392).
Functions as an inhibitor/regulator of abscission, probably by regulating membrane trafficking during abscission (PubMed:20081191).
Component of the RLP23-SOBIR1-BAK1 complex that mediates NLP-triggered immunity (PubMed:27251392).
Functions as an inhibitor/regulator of abscission, probably by regulating membrane trafficking during abscission (PubMed:20081191).
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 | peroxisome | |
Cellular Component | plasma membrane | |
Molecular Function | ATP binding | |
Molecular Function | protein serine kinase activity | |
Molecular Function | protein serine/threonine kinase activity | |
Molecular Function | protein tyrosine kinase activity | |
Molecular Function | transmembrane receptor protein tyrosine kinase activity | |
Biological Process | defense response | |
Biological Process | negative regulation of floral organ abscission | |
Biological Process | positive regulation of defense response |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameLeucine-rich repeat receptor-like serine/threonine/tyrosine-protein kinase SOBIR1
- 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 accessionQ9SKB2
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass type I membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 32-284 | Extracellular | ||||
Sequence: VEWLDIDSSDLKALQVIETELGVNSQRSSASDVNPCGRRGVFCERRHSATTGEYVLRVTRLVYRSRSLTGTISPVIGMLSELKELTLSNNQLVNAVPVDILSCKQLEVLDLRKNRFSGQIPGNFSSLSRLRILDLSSNKLSGNLNFLKNLRNLENLSVANNLFSGKIPEQIVSFHNLRFFDFSGNRYLEGPAPVMSSIKLQTSPHQTRHILAETPTSSPTNKPNNSTTSKAPKGAPKPGKLKKKKKKSKKKKV | ||||||
Transmembrane | 285-305 | Helical | ||||
Sequence: AAWILGFVVGAIGGTISGFVF | ||||||
Topological domain | 306-641 | Cytoplasmic | ||||
Sequence: SVLFKLIIQAIRGSEKPPGPSIFSPLIKKAEDLAFLENEEALASLEIIGRGGCGEVFKAELPGSNGKIIAVKKVIQPPKDADELTDEDSKFLNKKMRQIRSEINTVGHIRHRNLLPLLAHVSRPECHYLVYEYMEKGSLQDILTDVQAGNQELMWPARHKIALGIAAGLEYLHMDHNPRIIHRDLKPANVLLDDDMEARISDFGLAKAMPDAVTHITTSHVAGTVGYIAPEFYQTHKFTDKCDIYSFGVILGILVIGKLPSDEFFQHTDEMSLIKWMRNIITSENPSLAIDPKLMDQGFDEQMLLVLKIACYCTLDDPKQRPNSKDVRTMLSQIKH |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Suppresses BIR1 (bir1-1) disruption phenotype. When associated with AGD5/NEV disruption, premature shedding of floral organs and enlarge abscission zones.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 129 | In sobir1-8; suppresses BIR1 (bir1-1) disruption phenotype. | ||||
Sequence: V → M | ||||||
Mutagenesis | 329 | In sobir1-4; suppresses BIR1 (bir1-1) disruption phenotype. | ||||
Sequence: S → N | ||||||
Mutagenesis | 356 | In sobir1-7; suppresses BIR1 (bir1-1) disruption phenotype. | ||||
Sequence: G → R | ||||||
Mutagenesis | 377 | Loss of kinase activity. | ||||
Sequence: K → E | ||||||
Mutagenesis | 407 | In evr-2; loss of kinase activity. | ||||
Sequence: E → K | ||||||
Mutagenesis | 417 | In sobir1-9; suppresses BIR1 (bir1-1) disruption phenotype. | ||||
Sequence: R → W | ||||||
Mutagenesis | 455 | In sobir1-10; suppresses BIR1 (bir1-1) disruption phenotype. | ||||
Sequence: N → D | ||||||
Mutagenesis | 557 | In sobir1-5; suppresses BIR1 (bir1-1) disruption phenotype. | ||||
Sequence: G → R | ||||||
Mutagenesis | 575 | In sobir1-2; suppresses BIR1 (bir1-1) disruption phenotype. | ||||
Sequence: E → K | ||||||
Mutagenesis | 626 | In sobir1-6; suppresses BIR1 (bir1-1) disruption phenotype. | ||||
Sequence: R → K |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 22 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for signal, chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-31 | |||||
Sequence: MAVPTGSANLFLRPLILAVLSFLLLSSFVSS | ||||||
Chain | PRO_0000403355 | 32-641 | Leucine-rich repeat receptor-like serine/threonine/tyrosine-protein kinase SOBIR1 | |||
Sequence: VEWLDIDSSDLKALQVIETELGVNSQRSSASDVNPCGRRGVFCERRHSATTGEYVLRVTRLVYRSRSLTGTISPVIGMLSELKELTLSNNQLVNAVPVDILSCKQLEVLDLRKNRFSGQIPGNFSSLSRLRILDLSSNKLSGNLNFLKNLRNLENLSVANNLFSGKIPEQIVSFHNLRFFDFSGNRYLEGPAPVMSSIKLQTSPHQTRHILAETPTSSPTNKPNNSTTSKAPKGAPKPGKLKKKKKKSKKKKVAAWILGFVVGAIGGTISGFVFSVLFKLIIQAIRGSEKPPGPSIFSPLIKKAEDLAFLENEEALASLEIIGRGGCGEVFKAELPGSNGKIIAVKKVIQPPKDADELTDEDSKFLNKKMRQIRSEINTVGHIRHRNLLPLLAHVSRPECHYLVYEYMEKGSLQDILTDVQAGNQELMWPARHKIALGIAAGLEYLHMDHNPRIIHRDLKPANVLLDDDMEARISDFGLAKAMPDAVTHITTSHVAGTVGYIAPEFYQTHKFTDKCDIYSFGVILGILVIGKLPSDEFFQHTDEMSLIKWMRNIITSENPSLAIDPKLMDQGFDEQMLLVLKIACYCTLDDPKQRPNSKDVRTMLSQIKH | ||||||
Glycosylation | 154 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 186 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 256 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
Autophosphorylated on Ser, Thr and Tyr residues.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Mostly present in leaves and flowers, with increasing expression in older flowers.
Developmental stage
Expressed in floral organ abscission zones (AZs) prior to cell separation and subsequent shedding. Also present within the style of developing fruits, at the bases of cauline leaves, and in the stems of the first rosette leaves.
Gene expression databases
Interaction
Subunit
Interacts with CST (PubMed:21628627).
Interacts with RLP23 (PubMed:24525519, PubMed:27251392).
Component of a trimeric complex composed of RLP23, SOBIR1 and BAK1. BAK1 is recruited into a pre-formed RLP23-SOBIR1 complex in a ligand-dependent manner (PubMed:27251392).
Interacts with RLP23 (PubMed:24525519, PubMed:27251392).
Component of a trimeric complex composed of RLP23, SOBIR1 and BAK1. BAK1 is recruited into a pre-formed RLP23-SOBIR1 complex in a ligand-dependent manner (PubMed:27251392).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9SKB2 | At1g64210 Q9SH71 | 2 | EBI-16905883, EBI-20651385 | |
BINARY | Q9SKB2 | At1g68400 Q9M9C5 | 3 | EBI-16905883, EBI-1238661 | |
BINARY | Q9SKB2 | At2g02780 C0LGJ9 | 2 | EBI-16905883, EBI-20651541 | |
BINARY | Q9SKB2 | At3g50230 A0A1I9LQ53 | 3 | EBI-16905883, EBI-20654045 | |
BINARY | Q9SKB2 | At4g31250 C0LGR9 | 2 | EBI-16905883, EBI-16955262 | |
BINARY | Q9SKB2 | GSO1 C0LGQ5 | 2 | EBI-16905883, EBI-16905069 | |
BINARY | Q9SKB2 | PRK4 Q9LJY0 | 2 | EBI-16905883, EBI-16914444 | |
BINARY | Q9SKB2 | RLK902 Q9LVI6 | 3 | EBI-16905883, EBI-1626936 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for repeat, compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 112-133 | LRR 1 | ||||
Sequence: ELKELTLSNNQLVNAVPVDILS | ||||||
Repeat | 136-159 | LRR 2 | ||||
Sequence: QLEVLDLRKNRFSGQIPGNFSSLS | ||||||
Repeat | 160-182 | LRR 3 | ||||
Sequence: RLRILDLSSNKLSGNLNFLKNLR | ||||||
Repeat | 183-205 | LRR 4 | ||||
Sequence: NLENLSVANNLFSGKIPEQIVSF | ||||||
Repeat | 207-228 | LRR 5 | ||||
Sequence: NLRFFDFSGNRYLEGPAPVMSS | ||||||
Compositional bias | 243-263 | Polar residues | ||||
Sequence: AETPTSSPTNKPNNSTTSKAP | ||||||
Region | 243-278 | Disordered | ||||
Sequence: AETPTSSPTNKPNNSTTSKAPKGAPKPGKLKKKKKK | ||||||
Domain | 347-641 | Protein kinase | ||||
Sequence: LASLEIIGRGGCGEVFKAELPGSNGKIIAVKKVIQPPKDADELTDEDSKFLNKKMRQIRSEINTVGHIRHRNLLPLLAHVSRPECHYLVYEYMEKGSLQDILTDVQAGNQELMWPARHKIALGIAAGLEYLHMDHNPRIIHRDLKPANVLLDDDMEARISDFGLAKAMPDAVTHITTSHVAGTVGYIAPEFYQTHKFTDKCDIYSFGVILGILVIGKLPSDEFFQHTDEMSLIKWMRNIITSENPSLAIDPKLMDQGFDEQMLLVLKIACYCTLDDPKQRPNSKDVRTMLSQIKH |
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.
- Length641
- Mass (Da)71,111
- Last updated2000-05-01 v1
- ChecksumC061139D4B52681C
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 112 | in Ref. 3; AAL25569 | ||||
Sequence: E → V | ||||||
Compositional bias | 243-263 | Polar residues | ||||
Sequence: AETPTSSPTNKPNNSTTSKAP | ||||||
Sequence conflict | 490 | in Ref. 3; AAL25569 | ||||
Sequence: L → S |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC006533 EMBL· GenBank· DDBJ | AAD32284.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002685 EMBL· GenBank· DDBJ | AEC08599.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF370596 EMBL· GenBank· DDBJ | AAK43915.1 EMBL· GenBank· DDBJ | mRNA | ||
AY058153 EMBL· GenBank· DDBJ | AAL25569.1 EMBL· GenBank· DDBJ | mRNA | ||
FJ708707 EMBL· GenBank· DDBJ | ACN59302.1 EMBL· GenBank· DDBJ | mRNA |