Q93VJ2 · IRE1B_ARATH

Function

function

Senses unfolded proteins in the lumen of the endoplasmic reticulum via its N-terminal domain which leads to enzyme auto-activation. The active endoribonuclease domain splices bZIP60 mRNA to generate a new C-terminus, converting it into a potent unfolded-protein response transcriptional activator which then induces transcription of UPR target genes. Involved in organ growth regulation. Plays a role in plant immunity and abiotic stress responses. Required for ER stress-induced autophagy.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Activity regulation

The kinase domain is activated by trans-autophosphorylation. Kinase activity is required for activation of the endoribonuclease domain (By similarity).

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site465-473ATP (UniProtKB | ChEBI)
Binding site487ATP (UniProtKB | ChEBI)
Active site608Proton acceptor

GO annotations

AspectTerm
Cellular Componentendoplasmic reticulum
Cellular ComponentIRE1-TRAF2-ASK1 complex
Molecular FunctionATP binding
Molecular Functionhistone H2AS1 kinase activity
Molecular Functionmetal ion binding
Molecular Functionprotein serine kinase activity
Molecular Functionprotein serine/threonine kinase activity
Molecular FunctionRNA endonuclease activity
Molecular Functionunfolded protein binding
Biological Processautophagy
Biological Processdefense response to bacterium
Biological Processimmune system process
Biological ProcessIRE1-mediated unfolded protein response
Biological ProcessmRNA processing
Biological Processpositive regulation of autophagy in response to ER overload
Biological Processprotein phosphorylation
Biological Processresponse to salicylic acid
Biological ProcessRNA splicing

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Serine/threonine-protein kinase/endoribonuclease IRE1b
  • Alternative names
    • Endoplasmic reticulum-to-nucleus signaling 1-1
    • Inositol-requiring protein 1-1 (AtIRE1-1)
    • Serine/threonine-protein kinase/endoribonuclease IRE1-1

Including 2 domains:

  • Recommended name
    Serine/threonine-protein kinase
  • EC number

Gene names

    • Name
      IRE1B
    • Synonyms
      IRE1-1
    • ORF names
      K16H17.7
    • Ordered locus names
      At5g24360

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
    Q93VJ2
  • Secondary accessions
    • Q94IG5
    • Q9FIN6

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain22-357Lumenal
Transmembrane358-378Helical
Topological domain379-881Cytoplasmic

Keywords

Phenotypes & Variants

Disruption phenotype

No visible phenotype. Ire1a and ire1b double mutant is more sensitive to the ER stress inducer tunicamycin than the wild-type and is enable to give rise to the spliced bZIP60 mRNA form (PubMed:22355548).
Ire1a and ire1b double mutant displays short roots and a ER stress-sensitive phenotype (PubMed:21914012).

Variants

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

The viewer provides 75 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
Signal1-21
ChainPRO_000042213822-881Serine/threonine-protein kinase/endoribonuclease IRE1b
Glycosylation115N-linked (GlcNAc...) asparagine

Post-translational modification

Autophosphorylated.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Ubiquitous. Detected in the apical meristem, at leaf margins where vascular bundles end, in the anthers before pollen is formed and in the ovules at a very early stage of development. There is no expression in more mature embryos. Also strongly expressed in the cotyledons immediately after germination but not later on.

Induction

By ER stress inducer tunicamycin, by salicylic acid (SA) and by bacterial pathogen infection.

Gene expression databases

Interaction

Subunit

Homodimer; disulfide-linked. Dimer formation is driven by hydrophobic interactions within the N-terminal luminal domains and stabilized by disulfide bridges (By similarity).

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain, region.

TypeIDPosition(s)Description
Domain459-744Protein kinase
Region481-502ATP selon article
Region642-661Disordered
Domain747-878KEN

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.

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

Q93VJ2-1

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
    881
  • Mass (Da)
    99,616
  • Last updated
    2001-12-01 v1
  • Checksum
    AECD3585336081F8
MRGSALLDLILFLLVSPLAHSFKGSEISKFYDKSISNQISQSDRESGYVLVSTVDGSISLVDMSSQKLDWTFHTNEPIYSSYQAPHYHYTTDEERSSVLGDDFYMDCDKDWRLYNSSVRKGKRVNEIVDASEFIGTLPYTSTDRIVLGKKDTSVFLLDWKTGKLVKRYRMDELYSNTVVENDKEKAIVLSKEAPLLFGSGFKKSEDFPELVYIERKDFKIQCISKFGDVLWSVSYAKMEAKLQNHESVQFISGLSSSVGKNQFPLSYTTSVPMVQLRNVKYETLFPRLGFLDEALYLPFQDRKPNQLAIGDGNQLTLPGNKEAEEVLSLPLPETVISQITDIIDGSTKQAGFASKFSGLIVLIFGFCVTMLSVCGLFFYRLRQSIRIKEPYVSEVPIATPKKKKSKKNGTTKAVHKKENGFISGGNKDPSHEENEKRLLTAFPGLNNSSAEGYRVGKLFVSNKEIAKGSNGTVVLEGSYEGRLVAVKRLVQSHHDVAQKEILNLMASDKHSNIVRWYGVDQDEHFIYISLELCACSLNDLIYASSALLESPMASSSIHSIQINPIFENGKGVELWKENGHPSPVLLKLMRDIVAGLVHLHDIGIVHRDLKPQNVLIVKNSSLCAKLSDMGISKRLPADTSALTRNSTGLGSGSSGWQAPEQLRNERQTRAVDLFSLGCVLFFCMTGGKHPYGDNYERDVNVLNDQKDLFLIESLPEAVHLLTGLLNPDPNLRPRAQDVMHHPLFWNSDMRLSFLRDASDRVELENREEGSQLLAALESTAAVTLNGRWDEKLDSIFLDNIGRYRRYKFDSIRDLLRVIRNKLNHYRELPKELQELLGSVPEGFERYFSSRFPKLLIQVYTVLFDYCNNEEFFFKYSKTTVF

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
F4KH40F4KH40_ARATHIRE1-1887
F4KH41F4KH41_ARATHIRE1-1867

Sequence caution

The sequence BAB11229.1 differs from that shown. Reason: Erroneous gene model prediction

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict647in Ref. 1; BAB63366

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AB049936
EMBL· GenBank· DDBJ
BAB63366.1
EMBL· GenBank· DDBJ
mRNA
AY057897
EMBL· GenBank· DDBJ
AAL17714.1
EMBL· GenBank· DDBJ
mRNA
AB016884
EMBL· GenBank· DDBJ
BAB11229.1
EMBL· GenBank· DDBJ
Genomic DNA Sequence problems.
CP002688
EMBL· GenBank· DDBJ
AED93301.1
EMBL· GenBank· DDBJ
Genomic DNA
AY057480
EMBL· GenBank· DDBJ
AAL09714.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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