Q42371 · ERECT_ARATH
- ProteinLRR receptor-like serine/threonine-protein kinase ERECTA
- GeneERECTA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids976 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
Features
Showing features for binding site, active site.
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameLRR receptor-like serine/threonine-protein kinase ERECTA
- EC number
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ42371
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass type I membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 25-580 | Extracellular | ||||
Sequence: EEGATLLEIKKSFKDVNNVLYDWTTSPSSDYCVWRGVSCENVTFNVVALNLSDLNLDGEISPAIGDLKSLLSIDLRGNRLSGQIPDEIGDCSSLQNLDLSFNELSGDIPFSISKLKQLEQLILKNNQLIGPIPSTLSQIPNLKILDLAQNKLSGEIPRLIYWNEVLQYLGLRGNNLVGNISPDLCQLTGLWYFDVRNNSLTGSIPETIGNCTAFQVLDLSYNQLTGEIPFDIGFLQVATLSLQGNQLSGKIPSVIGLMQALAVLDLSGNLLSGSIPPILGNLTFTEKLYLHSNKLTGSIPPELGNMSKLHYLELNDNHLTGHIPPELGKLTDLFDLNVANNDLEGPIPDHLSSCTNLNSLNVHGNKFSGTIPRAFQKLESMTYLNLSSNNIKGPIPVELSRIGNLDTLDLSNNKINGIIPSSLGDLEHLLKMNLSRNHITGVVPGDFGNLRSIMEIDLSNNDISGPIPEELNQLQNIILLRLENNNLTGNVGSLANCLSLTVLNVSHNNLVGDIPKNNNFSRFSPDSFIGNPGLCGSWLNSPCHDSRRTVRVSISR | ||||||
Transmembrane | 581-601 | Helical | ||||
Sequence: AAILGIAIGGLVILLMVLIAA | ||||||
Topological domain | 602-976 | Cytoplasmic | ||||
Sequence: CRPHNPPPFLDGSLDKPVTYSTPKLVILHMNMALHVYEDIMRMTENLSEKYIIGHGASSTVYKCVLKNCKPVAIKRLYSHNPQSMKQFETELEMLSSIKHRNLVSLQAYSLSHLGSLLFYDYLENGSLWDLLHGPTKKKTLDWDTRLKIAYGAAQGLAYLHHDCSPRIIHRDVKSSNILLDKDLEARLTDFGIAKSLCVSKSHTSTYVMGTIGYIDPEYARTSRLTEKSDVYSYGIVLLELLTRRKAVDDESNLHHLIMSKTGNNEVMEMADPDITSTCKDLGVVKKVFQLALLCTKRQPNDRPTMHQVTRVLGSFMLSEQPPAATDTSATLAGSCYVDEYANLKTPHSVNCSSMSASDAQLFLRFGQVISQNSE |
Keywords
- Cellular component
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 282 | In er-103; compact inflorescence with short siliques, but normal leaves. | ||||
Sequence: M → I | ||||||
Mutagenesis | 489 | In er-117; compact inflorescence with short siliques and pedicels, and susceptibility to P.cucumerina. | ||||
Sequence: G → D | ||||||
Natural variant | 750 | er-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 | ||||
Sequence: I → K | ||||||
Mutagenesis | 831 | In er-114; compact inflorescence with short siliques and pedicels, and susceptibility to P.cucumerina. | ||||
Sequence: D → N | ||||||
Natural variant | 886 | in strain: cv. Mt-0 | ||||
Sequence: V → M |
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.
PTM/Processing
Features
Showing features for signal, chain, glycosylation, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-24 | |||||
Sequence: MALFRDIVLLGFLFCLSLVATVTS | ||||||
Chain | PRO_0000389000 | 25-976 | LRR receptor-like serine/threonine-protein kinase ERECTA | |||
Sequence: EEGATLLEIKKSFKDVNNVLYDWTTSPSSDYCVWRGVSCENVTFNVVALNLSDLNLDGEISPAIGDLKSLLSIDLRGNRLSGQIPDEIGDCSSLQNLDLSFNELSGDIPFSISKLKQLEQLILKNNQLIGPIPSTLSQIPNLKILDLAQNKLSGEIPRLIYWNEVLQYLGLRGNNLVGNISPDLCQLTGLWYFDVRNNSLTGSIPETIGNCTAFQVLDLSYNQLTGEIPFDIGFLQVATLSLQGNQLSGKIPSVIGLMQALAVLDLSGNLLSGSIPPILGNLTFTEKLYLHSNKLTGSIPPELGNMSKLHYLELNDNHLTGHIPPELGKLTDLFDLNVANNDLEGPIPDHLSSCTNLNSLNVHGNKFSGTIPRAFQKLESMTYLNLSSNNIKGPIPVELSRIGNLDTLDLSNNKINGIIPSSLGDLEHLLKMNLSRNHITGVVPGDFGNLRSIMEIDLSNNDISGPIPEELNQLQNIILLRLENNNLTGNVGSLANCLSLTVLNVSHNNLVGDIPKNNNFSRFSPDSFIGNPGLCGSWLNSPCHDSRRTVRVSISRAAILGIAIGGLVILLMVLIAACRPHNPPPFLDGSLDKPVTYSTPKLVILHMNMALHVYEDIMRMTENLSEKYIIGHGASSTVYKCVLKNCKPVAIKRLYSHNPQSMKQFETELEMLSSIKHRNLVSLQAYSLSHLGSLLFYDYLENGSLWDLLHGPTKKKTLDWDTRLKIAYGAAQGLAYLHHDCSPRIIHRDVKSSNILLDKDLEARLTDFGIAKSLCVSKSHTSTYVMGTIGYIDPEYARTSRLTEKSDVYSYGIVLLELLTRRKAVDDESNLHHLIMSKTGNNEVMEMADPDITSTCKDLGVVKKVFQLALLCTKRQPNDRPTMHQVTRVLGSFMLSEQPPAATDTSATLAGSCYVDEYANLKTPHSVNCSSMSASDAQLFLRFGQVISQNSE | ||||||
Glycosylation | 65 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 74 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 221 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 234 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 305 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 329 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 409 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 457 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 510 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 528 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 543 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 645 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 721 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 760 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 815 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 823 | Phosphothreonine | ||||
Sequence: T |
Keywords
- PTM
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).
Interacts with EPFL9/STOMAGEN (PubMed:26083750).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q42371 | BAK1 Q94F62 | 4 | EBI-16940407, EBI-617138 | |
BINARY | Q42371 | ERL2 Q6XAT2 | 4 | EBI-16940407, EBI-16895926 | |
BINARY | Q42371 | FLS2 Q9FL28 | 2 | EBI-16940407, EBI-1799448 | |
BINARY | Q42371 | GSO1 C0LGQ5 | 3 | EBI-16940407, EBI-16905069 | |
BINARY | Q42371 | HSL2 C0LGX3 | 2 | EBI-16940407, EBI-16904927 | |
BINARY | Q42371 | IOS1 Q9C8I6 | 3 | EBI-16940407, EBI-16924837 | |
BINARY | Q42371 | LRR-RLK Q9ZVD4 | 2 | EBI-16940407, EBI-20651739 | |
BINARY | Q42371 | NIK1 Q9LFS4 | 3 | EBI-16940407, EBI-16146189 | |
BINARY | Q42371 | RPK1 Q9ZRF9 | 3 | EBI-16940407, EBI-1238953 | |
BINARY | Q42371 | SERK4 Q9SKG5 | 2 | EBI-16940407, EBI-6290483 | |
BINARY | Q42371 | SERK5 Q8LPS5 | 3 | EBI-16940407, EBI-16887868 | |
BINARY | Q42371 | SRF3 Q6R2K3 | 2 | EBI-16940407, EBI-20651925 | |
BINARY | Q42371 | SUB Q8RWZ1 | 3 | EBI-16940407, EBI-17072125 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for repeat, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 69-92 | LRR 1 | ||||
Sequence: NVVALNLSDLNLDGEISPAIGDLK | ||||||
Repeat | 93-115 | LRR 2 | ||||
Sequence: SLLSIDLRGNRLSGQIPDEIGDC | ||||||
Repeat | 117-140 | LRR 3 | ||||
Sequence: SLQNLDLSFNELSGDIPFSISKLK | ||||||
Repeat | 141-163 | LRR 4 | ||||
Sequence: QLEQLILKNNQLIGPIPSTLSQI | ||||||
Repeat | 165-187 | LRR 5 | ||||
Sequence: NLKILDLAQNKLSGEIPRLIYWN | ||||||
Repeat | 189-212 | LRR 6 | ||||
Sequence: VLQYLGLRGNNLVGNISPDLCQLT | ||||||
Repeat | 213-235 | LRR 7 | ||||
Sequence: GLWYFDVRNNSLTGSIPETIGNC | ||||||
Repeat | 237-259 | LRR 8 | ||||
Sequence: AFQVLDLSYNQLTGEIPFDIGFL | ||||||
Repeat | 260-282 | LRR 9 | ||||
Sequence: QVATLSLQGNQLSGKIPSVIGLM | ||||||
Repeat | 284-306 | LRR 10 | ||||
Sequence: ALAVLDLSGNLLSGSIPPILGNL | ||||||
Repeat | 308-330 | LRR 11 | ||||
Sequence: FTEKLYLHSNKLTGSIPPELGNM | ||||||
Repeat | 332-355 | LRR 12 | ||||
Sequence: KLHYLELNDNHLTGHIPPELGKLT | ||||||
Repeat | 356-379 | LRR 13 | ||||
Sequence: DLFDLNVANNDLEGPIPDHLSSCT | ||||||
Repeat | 380-401 | LRR 14 | ||||
Sequence: NLNSLNVHGNKFSGTIPRAFQK | ||||||
Repeat | 404-425 | LRR 15 | ||||
Sequence: SMTYLNLSSNNIKGPIPVELSR | ||||||
Repeat | 428-449 | LRR 16 | ||||
Sequence: NLDTLDLSNNKINGIIPSSLGD | ||||||
Repeat | 452-473 | LRR 17 | ||||
Sequence: HLLKMNLSRNHITGVVPGDFGN | ||||||
Repeat | 476-498 | LRR 18 | ||||
Sequence: SIMEIDLSNNDISGPIPEELNQL | ||||||
Repeat | 500-522 | LRR 19 | ||||
Sequence: NIILLRLENNNLTGNVGSLANCL | ||||||
Repeat | 523-545 | LRR 20 | ||||
Sequence: SLTVLNVSHNNLVGDIPKNNNFS | ||||||
Domain | 648-918 | Protein kinase | ||||
Sequence: LSEKYIIGHGASSTVYKCVLKNCKPVAIKRLYSHNPQSMKQFETELEMLSSIKHRNLVSLQAYSLSHLGSLLFYDYLENGSLWDLLHGPTKKKTLDWDTRLKIAYGAAQGLAYLHHDCSPRIIHRDVKSSNILLDKDLEARLTDFGIAKSLCVSKSHTSTYVMGTIGYIDPEYARTSRLTEKSDVYSYGIVLLELLTRRKAVDDESNLHHLIMSKTGNNEVMEMADPDITSTCKDLGVVKKVFQLALLCTKRQPNDRPTMHQVTRVLGSFM |
Domain
The kinase domain is not required for ligand binding.
Sequence similarities
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length976
- Mass (Da)107,334
- Last updated1996-11-01 v1
- Checksum0E51D46A4AB94C8D
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
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |