Q42371 · ERECT_ARATH

Function

function

Receptor kinase that, together with ERL1 and ERL2, regulates aerial architecture, including inflorescence (e.g. shoot apical meristem-originating organ shape, elongation of the internode and pedicels, and adaxial-abaxial polarity), and stomatal patterning (e.g. density and clustering), probably by tuning cell division and expansion. Redundantly involved with ERL1 in procambial development regulation. Forms a functional ligand-receptor pair with EPF2 (AC Q8LC53) (PubMed:22241782).
Modulates plant transpiration efficiency by controlling stomatal density, leaf photosynthetic capacity, epidermal cell expansion, mesophyll cell proliferation and cell-cell contact. A phloem-specific expression of ER is sufficient for proper inflorescence architecture (PubMed:22474391).
Probable major trait regulating canalization (maintenance of phenotype despite varying environment) in many aspect of the plant physiology (e.g. plant morphology, light-dependent leaves number, branch number, flowering time, phytate and mineral concentrations) by transducing microenvironmental variation into phenotypic differentiation (ecological amplifier). May maintain development integrity in heat stress conditions. Regulates cell wall composition and structure. Confers resistance to the pathogenic bacteria Ralstonia solanacearum and to the necrotrophic fungi Plectosphaerella cucumerina and Pythium irregulare, and required for callose deposition upon infection. Resistance to P.cucumerina seems cell wall-mediated. Forms a constitutive complex with TMM involved in the recognition of the stomatal regulatory peptides EPF1, EPF2 and EPFL9/STOMAGEN (PubMed:28536146).

Catalytic activity

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site654-662ATP (UniProtKB | ChEBI)
Binding site676ATP (UniProtKB | ChEBI)
Active site773Proton acceptor

GO annotations

AspectTerm
Cellular Componentmitochondrion
Cellular Componentplasma membrane
Molecular FunctionATP binding
Molecular Functionpeptide binding
Molecular Functionprotein serine kinase activity
Molecular Functionprotein serine/threonine kinase activity
Molecular Functionreceptor serine/threonine kinase binding
Molecular Functionsignaling receptor binding
Molecular Functiontransmembrane receptor protein kinase activity
Biological Processcellular heat acclimation
Biological Processdefense response to bacterium
Biological Processdefense response to fungus
Biological Processinflorescence morphogenesis
Biological Processleaf morphogenesis
Biological Processphloem or xylem histogenesis
Biological Processplant-type cell wall organization
Biological Processpolarity specification of adaxial/abaxial axis
Biological Processregulation of cell adhesion
Biological Processregulation of cell division
Biological Processregulation of cell growth
Biological Processregulation of plant organ morphogenesis
Biological Processstomatal complex morphogenesis
Biological Processtranspiration

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    LRR receptor-like serine/threonine-protein kinase ERECTA
  • EC number
  • Alternative names
    • Protein QUANTITATIVE RESISTANCE TO PLECTOSPHAERELLA 1
    • Protein QUANTITATIVE RESISTANCE TO RALSTONIA SOLANACEARUM 1
    • Protein TRANSPIRATION EFFICIENCY 1

Gene names

    • Name
      ERECTA
    • Synonyms
      ER, QRP1, QRS1, TE1
    • ORF names
      T1D16.3
    • Ordered locus names
      At2g26330

Organism names

  • Taxonomic identifier
  • Strains
    • cv. Columbia
    • cv. Landsberg erecta
    • cv. Ag-0
    • cv. An-1
    • cv. Br-0
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis

Accessions

  • Primary accession
    Q42371
  • Secondary accessions
    • A5YYA0
    • A5YYB1
    • Q56WZ3

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 domain25-580Extracellular
Transmembrane581-601Helical
Topological domain602-976Cytoplasmic

Keywords

Phenotypes & Variants

Disruption phenotype

In er-104 and er-105, small curly leaves and compact inflorescence with short thick siliques, increased canalization of rosette leaf number during long days.

Features

Showing features for mutagenesis, natural variant.

TypeIDPosition(s)Description
Mutagenesis282In er-103; compact inflorescence with short siliques, but normal leaves.
Mutagenesis489In er-117; compact inflorescence with short siliques and pedicels, and susceptibility to P.cucumerina.
Natural variant750er-1 in strain: cv. Landsberg erecta; round leaves, compact inflorescence, blunt fruits, short and thick siliques and petioles, susceptibility to pathogens such as R.solanacearum, P.irregulare and P.cucumerina, abnormal cell-wall composition and increased canalization of rosette leaf number during long days. In er-101 and er-102, compact inflorescence with short siliques and pedicels
Mutagenesis831In er-114; compact inflorescence with short siliques and pedicels, and susceptibility to P.cucumerina.
Natural variant886in strain: cv. Mt-0

Variants

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

The viewer provides 51 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, modified residue.

TypeIDPosition(s)Description
Signal1-24
ChainPRO_000038900025-976LRR receptor-like serine/threonine-protein kinase ERECTA
Glycosylation65N-linked (GlcNAc...) asparagine
Glycosylation74N-linked (GlcNAc...) asparagine
Glycosylation221N-linked (GlcNAc...) asparagine
Glycosylation234N-linked (GlcNAc...) asparagine
Glycosylation305N-linked (GlcNAc...) asparagine
Glycosylation329N-linked (GlcNAc...) asparagine
Glycosylation409N-linked (GlcNAc...) asparagine
Glycosylation457N-linked (GlcNAc...) asparagine
Glycosylation510N-linked (GlcNAc...) asparagine
Glycosylation528N-linked (GlcNAc...) asparagine
Glycosylation543N-linked (GlcNAc...) asparagine
Modified residue645Phosphothreonine
Modified residue721Phosphotyrosine
Modified residue760Phosphotyrosine
Modified residue815Phosphotyrosine
Modified residue823Phosphothreonine

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Mostly expressed in shoot apical meristems (SAM), organ primordia, flowers, siliques and young rosette leaves, and, to a lower extent, in stems and cauline leaves. Expressed in growing inflorescence stems and pedicels. Detected in epidermis, phloem and xylem.

Developmental stage

Strongly expressed in organ primordia and immature organs but weakly in mature organs. Observed in SAM at low levels during the vegetative growth with an increase at the transition to the reproductive growth phase. At the reproductive stage, localized in the young developing flowers. Expressed in inflorescence meristem and is up-regulated during flower initiation and formation of flower organs. Also found in cells that differentiate into pedicels.

Gene expression databases

Interaction

Subunit

Homodimer and heterodimer with ERL1 and TMM. Interacts with EPF1, EPF2, EPFL4, EPFL5 and EPFL6. Interacts with SERK1, SERK2, SERK3/BAK1 and SERK4 in a EPF2-induced manner (PubMed:26320950).
Interacts with EPFL9/STOMAGEN (PubMed:26083750).

Binary interactions

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for repeat, domain.

TypeIDPosition(s)Description
Repeat69-92LRR 1
Repeat93-115LRR 2
Repeat117-140LRR 3
Repeat141-163LRR 4
Repeat165-187LRR 5
Repeat189-212LRR 6
Repeat213-235LRR 7
Repeat237-259LRR 8
Repeat260-282LRR 9
Repeat284-306LRR 10
Repeat308-330LRR 11
Repeat332-355LRR 12
Repeat356-379LRR 13
Repeat380-401LRR 14
Repeat404-425LRR 15
Repeat428-449LRR 16
Repeat452-473LRR 17
Repeat476-498LRR 18
Repeat500-522LRR 19
Repeat523-545LRR 20
Domain648-918Protein kinase

Domain

The kinase domain is not required for ligand binding.

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
    976
  • Mass (Da)
    107,334
  • Last updated
    1996-11-01 v1
  • Checksum
    0E51D46A4AB94C8D
MALFRDIVLLGFLFCLSLVATVTSEEGATLLEIKKSFKDVNNVLYDWTTSPSSDYCVWRGVSCENVTFNVVALNLSDLNLDGEISPAIGDLKSLLSIDLRGNRLSGQIPDEIGDCSSLQNLDLSFNELSGDIPFSISKLKQLEQLILKNNQLIGPIPSTLSQIPNLKILDLAQNKLSGEIPRLIYWNEVLQYLGLRGNNLVGNISPDLCQLTGLWYFDVRNNSLTGSIPETIGNCTAFQVLDLSYNQLTGEIPFDIGFLQVATLSLQGNQLSGKIPSVIGLMQALAVLDLSGNLLSGSIPPILGNLTFTEKLYLHSNKLTGSIPPELGNMSKLHYLELNDNHLTGHIPPELGKLTDLFDLNVANNDLEGPIPDHLSSCTNLNSLNVHGNKFSGTIPRAFQKLESMTYLNLSSNNIKGPIPVELSRIGNLDTLDLSNNKINGIIPSSLGDLEHLLKMNLSRNHITGVVPGDFGNLRSIMEIDLSNNDISGPIPEELNQLQNIILLRLENNNLTGNVGSLANCLSLTVLNVSHNNLVGDIPKNNNFSRFSPDSFIGNPGLCGSWLNSPCHDSRRTVRVSISRAAILGIAIGGLVILLMVLIAACRPHNPPPFLDGSLDKPVTYSTPKLVILHMNMALHVYEDIMRMTENLSEKYIIGHGASSTVYKCVLKNCKPVAIKRLYSHNPQSMKQFETELEMLSSIKHRNLVSLQAYSLSHLGSLLFYDYLENGSLWDLLHGPTKKKTLDWDTRLKIAYGAAQGLAYLHHDCSPRIIHRDVKSSNILLDKDLEARLTDFGIAKSLCVSKSHTSTYVMGTIGYIDPEYARTSRLTEKSDVYSYGIVLLELLTRRKAVDDESNLHHLIMSKTGNNEVMEMADPDITSTCKDLGVVKKVFQLALLCTKRQPNDRPTMHQVTRVLGSFMLSEQPPAATDTSATLAGSCYVDEYANLKTPHSVNCSSMSASDAQLFLRFGQVISQNSE

Polymorphism

The cultivar Landsberg erecta (cv. Ler) derives from cv. Landsberg (cv. La-0) in which ERECTA is mutated at Ile-750 (variant er).

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
D83257
EMBL· GenBank· DDBJ
BAA11869.1
EMBL· GenBank· DDBJ
Genomic DNA
U47029
EMBL· GenBank· DDBJ
AAC49302.1
EMBL· GenBank· DDBJ
mRNA
AC004484
EMBL· GenBank· DDBJ
AAC14518.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002685
EMBL· GenBank· DDBJ
AEC07825.1
EMBL· GenBank· DDBJ
Genomic DNA
AY035110
EMBL· GenBank· DDBJ
AAK59615.1
EMBL· GenBank· DDBJ
mRNA
FJ708701
EMBL· GenBank· DDBJ
ACN59296.1
EMBL· GenBank· DDBJ
mRNA
AK221886
EMBL· GenBank· DDBJ
BAD94220.1
EMBL· GenBank· DDBJ
mRNA
EF598332
EMBL· GenBank· DDBJ
ABR08864.1
EMBL· GenBank· DDBJ
Genomic DNA
EF598333
EMBL· GenBank· DDBJ
ABR08865.1
EMBL· GenBank· DDBJ
Genomic DNA
EF598334
EMBL· GenBank· DDBJ
ABR08866.1
EMBL· GenBank· DDBJ
Genomic DNA
EF598335
EMBL· GenBank· DDBJ
ABR08867.1
EMBL· GenBank· DDBJ
Genomic DNA
EF598336
EMBL· GenBank· DDBJ
ABR08868.1
EMBL· GenBank· DDBJ
Genomic DNA
EF598337
EMBL· GenBank· DDBJ
ABR08869.1
EMBL· GenBank· DDBJ
Genomic DNA
EF598338
EMBL· GenBank· DDBJ
ABR08870.1
EMBL· GenBank· DDBJ
Genomic DNA
EF598339
EMBL· GenBank· DDBJ
ABR08871.1
EMBL· GenBank· DDBJ
Genomic DNA
EF598340
EMBL· GenBank· DDBJ
ABR08872.1
EMBL· GenBank· DDBJ
Genomic DNA
EF598341
EMBL· GenBank· DDBJ
ABR08873.1
EMBL· GenBank· DDBJ
Genomic DNA
EF598342
EMBL· GenBank· DDBJ
ABR08874.1
EMBL· GenBank· DDBJ
Genomic DNA
EF598343
EMBL· GenBank· DDBJ
ABR08875.1
EMBL· GenBank· DDBJ
Genomic DNA
EF598344
EMBL· GenBank· DDBJ
ABR08876.1
EMBL· GenBank· DDBJ
Genomic DNA
EF598345
EMBL· GenBank· DDBJ
ABR08877.1
EMBL· GenBank· DDBJ
Genomic DNA
EF598346
EMBL· GenBank· DDBJ
ABR08878.1
EMBL· GenBank· DDBJ
Genomic DNA
EF598347
EMBL· GenBank· DDBJ
ABR08879.1
EMBL· GenBank· DDBJ
Genomic DNA
EF598348
EMBL· GenBank· DDBJ
ABR08880.1
EMBL· GenBank· DDBJ
Genomic DNA
EF598349
EMBL· GenBank· DDBJ
ABR08881.1
EMBL· GenBank· DDBJ
Genomic DNA
EF598350
EMBL· GenBank· DDBJ
ABR08882.1
EMBL· GenBank· DDBJ
Genomic DNA
EF598351
EMBL· GenBank· DDBJ
ABR08883.1
EMBL· GenBank· DDBJ
Genomic DNA
EF598352
EMBL· GenBank· DDBJ
ABR08884.1
EMBL· GenBank· DDBJ
Genomic DNA
EF598353
EMBL· GenBank· DDBJ
ABR08885.1
EMBL· GenBank· DDBJ
Genomic DNA
EF598354
EMBL· GenBank· DDBJ
ABR08886.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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