Q9SKB2 · SBIR1_ARATH

  • Protein
    Leucine-rich repeat receptor-like serine/threonine/tyrosine-protein kinase SOBIR1
  • Gene
    SOBIR1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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).

Catalytic activity

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site353-361ATP (UniProtKB | ChEBI)
Binding site377ATP (UniProtKB | ChEBI)
Active site489Proton acceptor

GO annotations

AspectTerm
Cellular Componentperoxisome
Cellular Componentplasma membrane
Molecular FunctionATP binding
Molecular Functionprotein serine kinase activity
Molecular Functionprotein serine/threonine kinase activity
Molecular Functionprotein tyrosine kinase activity
Molecular Functiontransmembrane receptor protein tyrosine kinase activity
Biological Processdefense response
Biological Processnegative regulation of floral organ abscission
Biological Processpositive regulation of defense response

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Leucine-rich repeat receptor-like serine/threonine/tyrosine-protein kinase SOBIR1
  • EC number
  • Alternative names
    • Protein EVERSHED
    • Protein SUPPRESSOR OF BIR1-1

Gene names

    • Name
      SOBIR1
    • Synonyms
      EVR
    • ORF names
      F20M17.8
    • Ordered locus names
      At2g31880

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Columbia
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis

Accessions

  • Primary accession
    Q9SKB2
  • Secondary accessions
    • Q93Z40

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

Cell membrane
; Single-pass type I membrane protein

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain32-284Extracellular
Transmembrane285-305Helical
Topological domain306-641Cytoplasmic

Keywords

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.

TypeIDPosition(s)Description
Mutagenesis129In sobir1-8; suppresses BIR1 (bir1-1) disruption phenotype.
Mutagenesis329In sobir1-4; suppresses BIR1 (bir1-1) disruption phenotype.
Mutagenesis356In sobir1-7; suppresses BIR1 (bir1-1) disruption phenotype.
Mutagenesis377Loss of kinase activity.
Mutagenesis407In evr-2; loss of kinase activity.
Mutagenesis417In sobir1-9; suppresses BIR1 (bir1-1) disruption phenotype.
Mutagenesis455In sobir1-10; suppresses BIR1 (bir1-1) disruption phenotype.
Mutagenesis557In sobir1-5; suppresses BIR1 (bir1-1) disruption phenotype.
Mutagenesis575In sobir1-2; suppresses BIR1 (bir1-1) disruption phenotype.
Mutagenesis626In sobir1-6; suppresses BIR1 (bir1-1) disruption phenotype.

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.

Go to variant viewer

PTM/Processing

Features

Showing features for signal, chain, glycosylation.

TypeIDPosition(s)Description
Signal1-31
ChainPRO_000040335532-641Leucine-rich repeat receptor-like serine/threonine/tyrosine-protein kinase SOBIR1
Glycosylation154N-linked (GlcNAc...) asparagine
Glycosylation186N-linked (GlcNAc...) asparagine
Glycosylation256N-linked (GlcNAc...) asparagine

Post-translational modification

Autophosphorylated on Ser, Thr and Tyr residues.

Keywords

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).

Binary interactions

Protein-protein interaction databases

Family & Domains

Features

Showing features for repeat, compositional bias, region, domain.

TypeIDPosition(s)Description
Repeat112-133LRR 1
Repeat136-159LRR 2
Repeat160-182LRR 3
Repeat183-205LRR 4
Repeat207-228LRR 5
Compositional bias243-263Polar residues
Region243-278Disordered
Domain347-641Protein kinase

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    641
  • Mass (Da)
    71,111
  • Last updated
    2000-05-01 v1
  • Checksum
    C061139D4B52681C
MAVPTGSANLFLRPLILAVLSFLLLSSFVSSVEWLDIDSSDLKALQVIETELGVNSQRSSASDVNPCGRRGVFCERRHSATTGEYVLRVTRLVYRSRSLTGTISPVIGMLSELKELTLSNNQLVNAVPVDILSCKQLEVLDLRKNRFSGQIPGNFSSLSRLRILDLSSNKLSGNLNFLKNLRNLENLSVANNLFSGKIPEQIVSFHNLRFFDFSGNRYLEGPAPVMSSIKLQTSPHQTRHILAETPTSSPTNKPNNSTTSKAPKGAPKPGKLKKKKKKSKKKKVAAWILGFVVGAIGGTISGFVFSVLFKLIIQAIRGSEKPPGPSIFSPLIKKAEDLAFLENEEALASLEIIGRGGCGEVFKAELPGSNGKIIAVKKVIQPPKDADELTDEDSKFLNKKMRQIRSEINTVGHIRHRNLLPLLAHVSRPECHYLVYEYMEKGSLQDILTDVQAGNQELMWPARHKIALGIAAGLEYLHMDHNPRIIHRDLKPANVLLDDDMEARISDFGLAKAMPDAVTHITTSHVAGTVGYIAPEFYQTHKFTDKCDIYSFGVILGILVIGKLPSDEFFQHTDEMSLIKWMRNIITSENPSLAIDPKLMDQGFDEQMLLVLKIACYCTLDDPKQRPNSKDVRTMLSQIKH

Features

Showing features for sequence conflict, compositional bias.

TypeIDPosition(s)Description
Sequence conflict112in Ref. 3; AAL25569
Compositional bias243-263Polar residues
Sequence conflict490in Ref. 3; AAL25569

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

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