Q2M405 · CRN8_PHYIN

Function

function

Secreted effector that induces cell death when expressed in host plants (PubMed:19741609, PubMed:20847293, PubMed:22927814).
Acts as a kinase and is able to autophosphorylate, however its cell death inducing ability is not a direct result of its kinase activity, but rather a consequence of the phosphorylated state of the five identified serine residues in the CRN8 protein (PubMed:22927814).

Catalytic activity

Features

Showing features for active site.

TypeIDPosition(s)Description
Active site470Proton acceptor

GO annotations

AspectTerm
Cellular Componentextracellular region
Cellular Componenthost cell nucleus
Molecular Functionhistone H2AS1 kinase activity
Molecular Functionprotein serine kinase activity
Biological Processphosphorylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Crinkler effector protein 8
  • EC number

Gene names

    • Name
      CRN8

Organism names

Accessions

  • Primary accession
    Q2M405

Organism-specific databases

Subcellular Location

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis249Impairs host cell death induction; when associated with A-281, A-385, A-474 and A-587.
Mutagenesis281Impairs host cell death induction; when associated with A-249, A-385, A-474 and A-587.
Mutagenesis385Impairs host cell death induction; when associated with A-249, A-281, A-474 and A-587.
Mutagenesis469Destabilizes the CRN8 protein and impairs autophosphorylation and host cell death induction; when associated with A-470.
Mutagenesis470Destabilizes the CRN8 protein and impairs autophosphorylation and host cell death induction; when associated with A-469.
Mutagenesis470Impairs autophosphorylation but does not affect host cell death induction.
Mutagenesis474Impairs host cell death induction; when associated with A-249, A-291, A-385 and A-587.
Mutagenesis587Impairs host cell death induction; when associated with A-249, A-291, A-385 and A-474.

PTM/Processing

Features

Showing features for signal, chain, glycosylation, modified residue.

Type
IDPosition(s)Description
Signal1-17
ChainPRO_000044740918-599Crinkler effector protein 8
Glycosylation23N-linked (GlcNAc...) asparagine
Modified residue249Phosphoserine
Modified residue281Phosphoserine
Modified residue385Phosphoserine
Modified residue474Phosphoserine
Modified residue587Phosphoserine

Post-translational modification

Autophosphorylated at Ser-249, Ser-281, Ser-385, Ser-474 and Ser-587. Additional serines or threonines are also targeted for phosphorylation.

Keywords

PTM databases

Interaction

Subunit

Dimerizes in host plants.

Structure

Family & Domains

Features

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

Type
IDPosition(s)Description
Region18-52LQLFLAK domain
Region53-109DWL domain
Motif110-116HVLVXXP motif
Region117-590C-terminal D2 effector domain
Domain289-590Protein kinase
Compositional bias577-591Basic and acidic residues
Region577-599Disordered
Motif590-599Host nuclear localization signal

Domain

The CRN proteins have modular architectures that include a signal peptide, a conserved N-terminus, and highly diverse C-terminal domains. The conserved CRN N-terminus harbors a distinct LXLFLAK motif, which is followed by the conserved DWL domain. A highly conserved HVLVXXP motif marks the end of the CRN N-terminal domains and forms a junction where diverse C-terminal effector domains are fused. The conserved CRN N-terminus mediates the translocation into the plant host cells.
The whole D2 effector domain that contains a protein functional kinase domain, as well as the C-terminal NLS are required for cell death induction.

Sequence similarities

In the N-terminal section; belongs to the Crinkler effector family.
In the C-terminal section; belongs to the protein kinase superfamily.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    599
  • Mass (Da)
    67,268
  • Last updated
    2006-02-21 v1
  • Checksum
    5258452242BA845E
MVTLFCAVVGVAGSTFPVDINENKSVGHLKKAIKEEKMYQFPADELQLFLAKAGGNAWLSSLTEDVKKLKKGEKTALVKSLTQEEKELQGEDPISECLEGMDPPKVKQIHVLVALPPGTSSAPISDGTDLWLSRFQHSEVAKLTLLPTRGDLNEFIGQPLPVKIGLPQSVFQAWSSPLILGQLLRDKLFELNDISPCEFLKDSVFSAAFLYPQVDGDATESAFHYFWDSIIRVVLGFVFRRAYVNRDSSRKSSSGLKRPDFLFALDHICVFRGEEKEPRTSITVPREELSKKLVWSYGGVPYVFGYAASGFELELFAIYQDVTGNVKTHLIGGFNLQHAPERFRLVLALLNLCLLFPAIVQNCPASAGTEFMDIHRANGVKVRLSPIFVDKIFHTQEEYRRVKQIYDSLKAYGVPCADAVVTVDSDQLRLTLKPRGIEMKPCSLSELFVALGNVLEALVVLHRNGWMHRDIRWSNVIKHIDRVEWFLIDFADAAQSPQKYPSGDHLTHDEHASDIFMEGGSHTTAVDLWAVGYLVKTSKIEREWTAEPERALFLDRLMNPDPSARPTADEALQLLSRFEREAAEQESQGKGVRKKHRRA

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias577-591Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY961456
EMBL· GenBank· DDBJ
AAY43402.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

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