Q9XF67 · PDPK1_ARATH

Function

function

May couple lipid signals to the activation-loop phosphorylation of several protein kinases of the so-called AGC kinase family. Interacts via its pleckstrin homology domain with phosphatidic acid, PtdIns3P and PtdIns(3,4)P2 and to a lesser extent with PtdIns(4,5)P2 and PtdIns4P. May play a general role in signaling processes controlling the pathogen/stress response, polar auxin transport and development. Transphosphorylates the AGC protein kinases OXI1/AGC2-1, PK1/S6K1, PK19/S6K2 and PID resulting in their activation.

Catalytic activity

Activity regulation

Activated by phosphatidic acid (PA) and in response to the fungal elicitor xylanase.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site54-56ATP (UniProtKB | ChEBI)
Binding site73ATP (UniProtKB | ChEBI)
Binding site122-124ATP (UniProtKB | ChEBI)
Binding site128ATP (UniProtKB | ChEBI)
Active site167Proton acceptor
Binding site171ATP (UniProtKB | ChEBI)
Binding site185ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentmembrane
Molecular FunctionATP binding
Molecular Functionkinase activity
Molecular Functionphosphatidic acid binding
Molecular Functionphosphatidylinositol binding
Molecular Functionprotein kinase activity
Molecular Functionprotein serine kinase activity
Molecular Functionprotein serine/threonine kinase activity
Biological Processpositive regulation of protein kinase activity
Biological Processprotein autophosphorylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    3-phosphoinositide-dependent protein kinase 1
  • EC number
  • Short names
    AtPDK1

Gene names

    • Name
      PDPK1
    • Synonyms
      PDK1
    • ORF names
      T32M21.110
    • Ordered locus names
      At5g04510

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
    Q9XF67
  • Secondary accessions
    • Q9LZ74

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

Cytoplasm
Membrane
; Peripheral membrane protein
Note: Membrane-associated after cell stimulation.

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis167Abolishes autophosphorylation.
Mutagenesis176Strongly reduces autophosphorylation.
Mutagenesis177Reduces autophosphorylation.
Mutagenesis211Strongly reduces autophosphorylation.
Mutagenesis276Abolishes autophosphorylation.
Mutagenesis382Slightly reduces autophosphorylation.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 25 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00003999021-4913-phosphoinositide-dependent protein kinase 1
Modified residue177Phosphoserine
Modified residue211Phosphothreonine; by autocatalysis
Modified residue276Phosphoserine
Modified residue337Phosphoserine
Modified residue382Phosphoserine

Post-translational modification

Phosphorylation on Thr-211 in the activation loop is required for full activity. PDK1 itself can autophosphorylate Thr-211, leading to its own activation.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Ubiquitous.

Gene expression databases

Interaction

Subunit

Interacts with AGC1-5 and AGC1-7 (PubMed:16973627).
Interacts with the C-terminal PIF domain of the protein kinases D6PK/AGC1-1, OXI1/AGC2-1 and PID (PubMed:14749726, PubMed:16601102).

Binary interactions

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain44-311Protein kinase
Region75-119PIF-pocket
Region77-112PIF-binding
Region185-222Activation loop
Region321-377Disordered
Compositional bias336-377Polar residues
Domain386-491PH

Domain

The PH domain is responsible for the interaction with the 3-phosphoinositides. The activation loop within the kinase domain is the target of phosphorylation. The PIF-binding region in the kinase domain of PDK1 acts as a docking site, enabling it to interact with and enhance the phosphorylation of substrates containing the PIF motif.
The PIF-pocket is a small lobe in the catalytic domain required by the enzyme for the binding to the hydrophobic motif of its substrates. It is an allosteric regulatory site that can accommodate small compounds acting as allosteric inhibitors.

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete

This entry describes 1 isoforms produced by Alternative splicing. A number of isoforms are produced. According to EST sequences.

Q9XF67-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    491
  • Mass (Da)
    54,711
  • Last updated
    1999-11-01 v1
  • Checksum
    2319EE69CDB5CB38
MLAMEKEFDSKLVLQGNSSNGANVSRSKSFSFKAPQENFTSHDFEFGKIYGVGSYSKVVRAKKKETGTVYALKIMDKKFITKENKTAYVKLERIVLDQLEHPGIIKLYFTFQDTSSLYMALESCEGGELFDQITRKGRLSEDEARFYTAEVVDALEYIHSMGLIHRDIKPENLLLTSDGHIKIADFGSVKPMQDSQITVLPNAASDDKACTFVGTAAYVPPEVLNSSPATFGNDLWALGCTLYQMLSGTSPFKDASEWLIFQRIIARDIKFPNHFSEAARDLIDRLLDTEPSRRPGAGSEGYVALKRHPFFNGVDWKNLRSQTPPKLAPDPASQTASPERDDTHGSPWNLTHIGDSLATQNEGHSAPPTSSESSGSITRLASIDSFDSRWQQFLEPGESVLMISAVKKLQKITSKKVQLILTNKPKLIYVDPSKLVVKGNIIWSDNSNDLNVVVTSPSHFKICTPKKVLSFEDAKQRASVWKKAIETLQNR

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
F4JWB0F4JWB0_ARATHPDK1408
A0A1P8BAG1A0A1P8BAG1_ARATHPDK1305

Sequence caution

The sequence CAB85557.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias336-377Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF132742
EMBL· GenBank· DDBJ
AAD37165.1
EMBL· GenBank· DDBJ
mRNA
AL162875
EMBL· GenBank· DDBJ
CAB85557.1
EMBL· GenBank· DDBJ
Genomic DNA Different initiation
CP002688
EMBL· GenBank· DDBJ
AED90755.1
EMBL· GenBank· DDBJ
Genomic DNA
AF360326
EMBL· GenBank· DDBJ
AAK26036.1
EMBL· GenBank· DDBJ
mRNA
AY056336
EMBL· GenBank· DDBJ
AAL07185.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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