Q9LHP4 · RGI1_ARATH
- ProteinLRR receptor-like serine/threonine-protein kinase RGI1
- GeneRGI1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1141 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Together with RGI2, RGI3, RGI4 and RGI5, acts as a receptor of RGF peptides (e.g. RGF1, GLV5/CLEL1/RGF2, GLV7/CLEL3/RGF3, GLV3/RGF4, GLV10/CLEL7/RGF5 and RGF10/CLELN), peptide hormones which maintain the postembryonic root stem cell niche by regulating the expression levels and patterns of the transcription factor PLETHORA (PLT, e.g. PLT1 and PLT2) (PubMed:27001831, PubMed:27229311, PubMed:27229312).
Links RGF peptides signal with their downstream components (PubMed:27001831, PubMed:27229311).
Links RGF peptides signal with their downstream components (PubMed:27001831, PubMed:27229311).
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
Features
Showing features for binding site, site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Molecular Function | ATP binding | |
Molecular Function | peptide binding | |
Molecular Function | peptide receptor activity | |
Molecular Function | protein serine kinase activity | |
Molecular Function | protein serine/threonine kinase activity | |
Biological Process | maintenance of meristem identity | |
Biological Process | maintenance of root meristem identity | |
Biological Process | regulation of root development | |
Biological Process | regulation of root meristem growth | |
Biological Process | root meristem growth |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameLRR receptor-like serine/threonine-protein kinase RGI1
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ9LHP4
- 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 | 34-726 | Extracellular | ||||
Sequence: EQNPEASILYSWLHSSSPTPSSLSLFNWNSIDNTPCNNWTFITCSSQGFITDIDIESVPLQLSLPKNLPAFRSLQKLTISGANLTGTLPESLGDCLGLKVLDLSSNGLVGDIPWSLSKLRNLETLILNSNQLTGKIPPDISKCSKLKSLILFDNLLTGSIPTELGKLSGLEVIRIGGNKEISGQIPSEIGDCSNLTVLGLAETSVSGNLPSSLGKLKKLETLSIYTTMISGEIPSDLGNCSELVDLFLYENSLSGSIPREIGQLTKLEQLFLWQNSLVGGIPEEIGNCSNLKMIDLSLNLLSGSIPSSIGRLSFLEEFMISDNKFSGSIPTTISNCSSLVQLQLDKNQISGLIPSELGTLTKLTLFFAWSNQLEGSIPPGLADCTDLQALDLSRNSLTGTIPSGLFMLRNLTKLLLISNSLSGFIPQEIGNCSSLVRLRLGFNRITGEIPSGIGSLKKINFLDFSSNRLHGKVPDEIGSCSELQMIDLSNNSLEGSLPNPVSSLSGLQVLDVSANQFSGKIPASLGRLVSLNKLILSKNLFSGSIPTSLGMCSGLQLLDLGSNELSGEIPSELGDIENLEIALNLSSNRLTGKIPSKIASLNKLSILDLSHNMLEGDLAPLANIENLVSLNISYNSFSGYLPDNKLFRQLSPQDLEGNKKLCSSTQDSCFLTYRKGNGLGDDGDASRTRKLRL | ||||||
Transmembrane | 727-747 | Helical | ||||
Sequence: TLALLITLTVVLMILGAVAVI | ||||||
Topological domain | 748-1141 | Cytoplasmic | ||||
Sequence: RARRNIDNERDSELGETYKWQFTPFQKLNFSVDQIIRCLVEPNVIGKGCSGVVYRADVDNGEVIAVKKLWPAMVNGGHDEKTKNVRDSFSAEVKTLGTIRHKNIVRFLGCCWNRNTRLLMYDYMPNGSLGSLLHERRGSSLDWDLRYRILLGAAQGLAYLHHDCLPPIVHRDIKANNILIGLDFEPYIADFGLAKLVDEGDIGRCSNTVAGSYGYIAPEYGYSMKITEKSDVYSYGVVVLEVLTGKQPIDPTVPEGIHLVDWVRQNRGSLEVLDSTLRSRTEAEADEMMQVLGTALLCVNSSPDERPTMKDVAAMLKEIKQEREEYAKVDLLLKKSPPPTTTMQEECRKNEMMMIPAAAASSSKEMRREERLLKSNNTSFSASSLLYSSSSSIE |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Smaller root meristem size and fewer root meristematic cortex cells, associated with shorter roots and a slighty reduced sensitivity to RGF1 (PubMed:27229311).
Quintuple mutants rgi1 rgi2 rgi3 rgi4 rgi5 display a consistent short primary root phenotype with a small size of meristem associated with a total insensitivity to RGF1 and undetectable levels of PLT1 and PLT2 (PubMed:27229312).
The triple mutant missing RGI1, RGI2 and RGI3 is insensitive to externally applied RGF peptides (e.g. RGF1 and RGF2) and has short roots characterized by a strong decrease in meristematic cell number and declined levels of PLT1 and PLT2 at the root tip (PubMed:27001831).
Quintuple mutants rgi1 rgi2 rgi3 rgi4 rgi5 display a consistent short primary root phenotype with a small size of meristem associated with a total insensitivity to RGF1 and undetectable levels of PLT1 and PLT2 (PubMed:27229312).
The triple mutant missing RGI1, RGI2 and RGI3 is insensitive to externally applied RGF peptides (e.g. RGF1 and RGF2) and has short roots characterized by a strong decrease in meristematic cell number and declined levels of PLT1 and PLT2 at the root tip (PubMed:27001831).
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 814 | Lost autophosphorylation. | ||||
Sequence: K → E | ||||||
Mutagenesis | 815 | Normal autophosphorylation. | ||||
Sequence: K → E |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 70 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-33 | |||||
Sequence: MSLHSLIFFSSSSSSLLFSFFFIFIFCFSLSDA | ||||||
Chain | PRO_0000287221 | 34-1141 | LRR receptor-like serine/threonine-protein kinase RGI1 | |||
Sequence: EQNPEASILYSWLHSSSPTPSSLSLFNWNSIDNTPCNNWTFITCSSQGFITDIDIESVPLQLSLPKNLPAFRSLQKLTISGANLTGTLPESLGDCLGLKVLDLSSNGLVGDIPWSLSKLRNLETLILNSNQLTGKIPPDISKCSKLKSLILFDNLLTGSIPTELGKLSGLEVIRIGGNKEISGQIPSEIGDCSNLTVLGLAETSVSGNLPSSLGKLKKLETLSIYTTMISGEIPSDLGNCSELVDLFLYENSLSGSIPREIGQLTKLEQLFLWQNSLVGGIPEEIGNCSNLKMIDLSLNLLSGSIPSSIGRLSFLEEFMISDNKFSGSIPTTISNCSSLVQLQLDKNQISGLIPSELGTLTKLTLFFAWSNQLEGSIPPGLADCTDLQALDLSRNSLTGTIPSGLFMLRNLTKLLLISNSLSGFIPQEIGNCSSLVRLRLGFNRITGEIPSGIGSLKKINFLDFSSNRLHGKVPDEIGSCSELQMIDLSNNSLEGSLPNPVSSLSGLQVLDVSANQFSGKIPASLGRLVSLNKLILSKNLFSGSIPTSLGMCSGLQLLDLGSNELSGEIPSELGDIENLEIALNLSSNRLTGKIPSKIASLNKLSILDLSHNMLEGDLAPLANIENLVSLNISYNSFSGYLPDNKLFRQLSPQDLEGNKKLCSSTQDSCFLTYRKGNGLGDDGDASRTRKLRLTLALLITLTVVLMILGAVAVIRARRNIDNERDSELGETYKWQFTPFQKLNFSVDQIIRCLVEPNVIGKGCSGVVYRADVDNGEVIAVKKLWPAMVNGGHDEKTKNVRDSFSAEVKTLGTIRHKNIVRFLGCCWNRNTRLLMYDYMPNGSLGSLLHERRGSSLDWDLRYRILLGAAQGLAYLHHDCLPPIVHRDIKANNILIGLDFEPYIADFGLAKLVDEGDIGRCSNTVAGSYGYIAPEYGYSMKITEKSDVYSYGVVVLEVLTGKQPIDPTVPEGIHLVDWVRQNRGSLEVLDSTLRSRTEAEADEMMQVLGTALLCVNSSPDERPTMKDVAAMLKEIKQEREEYAKVDLLLKKSPPPTTTMQEECRKNEMMMIPAAAASSSKEMRREERLLKSNNTSFSASSLLYSSSSSIE | ||||||
Disulfide bond | 69↔77 | |||||
Sequence: CNNWTFITC | ||||||
Glycosylation | 71 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 116 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 227 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 272 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 320 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 368 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 443 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 464 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 523 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 617 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 664 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 868 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 906 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 962 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 969 | Phosphotyrosine | ||||
Sequence: Y |
Post-translational modification
Phosphorylated and ubiquitinated upon interaction with RGF1, thus leading to activation a subsequent degradation (PubMed:27229312).
Stabilized by UBP12 and UBP13-mediated deubiquitination (PubMed:29339500).
Stabilized by UBP12 and UBP13-mediated deubiquitination (PubMed:29339500).
Autophosphorylated.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in roots.
Developmental stage
Present in the whole roots with a predominant expression in the proximal meristem, including the elongation zone, and a gradual decreases toward the differentiation zone.
Gene expression databases
Interaction
Subunit
Interacts with beet curly top virus AL4/C4 (PubMed:17280695).
Binds to RGF peptides such as RGF1, GLV5/CLEL1/RGF2, GLV7/CLEL3/RGF3, GLV3/RGF4, GLV10/CLEL7/RGF5 and RGF10/CLELN; these interactions trigger the formation of heterodimers with SERK1, SERK2 or BAK1/SERK3 via LRR regions (PubMed:27001831, PubMed:27229311, PubMed:27229312).
Interacts with UBP13 (PubMed:29339500).
Binds to RGF peptides such as RGF1, GLV5/CLEL1/RGF2, GLV7/CLEL3/RGF3, GLV3/RGF4, GLV10/CLEL7/RGF5 and RGF10/CLELN; these interactions trigger the formation of heterodimers with SERK1, SERK2 or BAK1/SERK3 via LRR regions (PubMed:27001831, PubMed:27229311, PubMed:27229312).
Interacts with UBP13 (PubMed:29339500).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9LHP4 | At5g49770 Q9LT96 | 2 | EBI-20660903, EBI-17123993 | |
BINARY | Q9LHP4 | BRL2 Q9ZPS9 | 4 | EBI-20660903, EBI-2292728 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for repeat, motif, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 80-104 | LRR 1 | ||||
Sequence: QGFITDIDIESVPLQLSLPKNLPAF | ||||||
Repeat | 105-128 | LRR 2 | ||||
Sequence: RSLQKLTISGANLTGTLPESLGDC | ||||||
Repeat | 130-152 | LRR 3 | ||||
Sequence: GLKVLDLSSNGLVGDIPWSLSKL | ||||||
Repeat | 153-176 | LRR 4 | ||||
Sequence: RNLETLILNSNQLTGKIPPDISKC | ||||||
Repeat | 178-200 | LRR 5 | ||||
Sequence: KLKSLILFDNLLTGSIPTELGKL | ||||||
Motif | 185-186 | Small peptide recognition | ||||
Sequence: FD | ||||||
Repeat | 202-225 | LRR 6 | ||||
Sequence: GLEVIRIGGNKEISGQIPSEIGDC | ||||||
Motif | 207-210 | Small peptide recognition | ||||
Sequence: RIGG | ||||||
Repeat | 226-249 | LRR 7 | ||||
Sequence: SNLTVLGLAETSVSGNLPSSLGKL | ||||||
Motif | 230-235 | Small peptide recognition | ||||
Sequence: VLGLAE | ||||||
Repeat | 250-273 | LRR 8 | ||||
Sequence: KKLETLSIYTTMISGEIPSDLGNC | ||||||
Motif | 258 | Small peptide recognition | ||||
Sequence: Y | ||||||
Repeat | 275-297 | LRR 9 | ||||
Sequence: ELVDLFLYENSLSGSIPREIGQL | ||||||
Motif | 280-282 | Small peptide recognition | ||||
Sequence: FLY | ||||||
Repeat | 298-321 | LRR 10 | ||||
Sequence: TKLEQLFLWQNSLVGGIPEEIGNC | ||||||
Repeat | 322-345 | LRR 11 | ||||
Sequence: SNLKMIDLSLNLLSGSIPSSIGRL | ||||||
Motif | 328-331 | Small peptide recognition | ||||
Sequence: DLSL | ||||||
Repeat | 347-369 | LRR 12 | ||||
Sequence: FLEEFMISDNKFSGSIPTTISNC | ||||||
Motif | 350-352 | Small peptide recognition | ||||
Sequence: EFM | ||||||
Repeat | 370-392 | LRR 13 | ||||
Sequence: SSLVQLQLDKNQISGLIPSELGT | ||||||
Repeat | 394-417 | LRR 14 | ||||
Sequence: TKLTLFFAWSNQLEGSIPPGLADC | ||||||
Motif | 398-402 | Small peptide recognition | ||||
Sequence: LFFAW | ||||||
Repeat | 418-441 | LRR 15 | ||||
Sequence: TDLQALDLSRNSLTGTIPSGLFML | ||||||
Motif | 424-427 | Small peptide recognition | ||||
Sequence: DLSR | ||||||
Repeat | 443-464 | LRR 16 | ||||
Sequence: NLTKLLLISNSLSGFIPQEIGN | ||||||
Motif | 446-450 | Small peptide recognition | ||||
Sequence: KLLLI | ||||||
Repeat | 465-489 | LRR 17 | ||||
Sequence: CSSLVRLRLGFNRITGEIPSGIGSL | ||||||
Motif | 470-472 | Small peptide recognition | ||||
Sequence: RLR | ||||||
Repeat | 490-513 | LRR 18 | ||||
Sequence: KKINFLDFSSNRLHGKVPDEIGSC | ||||||
Repeat | 514-537 | LRR 19 | ||||
Sequence: SELQMIDLSNNSLEGSLPNPVSSL | ||||||
Repeat | 538-561 | LRR 20 | ||||
Sequence: SGLQVLDVSANQFSGKIPASLGRL | ||||||
Repeat | 563-585 | LRR 21 | ||||
Sequence: SLNKLILSKNLFSGSIPTSLGMC | ||||||
Repeat | 586-609 | LRR 22 | ||||
Sequence: SGLQLLDLGSNELSGEIPSELGDI | ||||||
Repeat | 610-634 | LRR 23 | ||||
Sequence: ENLEIALNLSSNRLTGKIPSKIASL | ||||||
Repeat | 636-657 | LRR 24 | ||||
Sequence: KLSILDLSHNMLEGDLAPLANI | ||||||
Repeat | 658-682 | LRR 25 | ||||
Sequence: ENLVSLNISYNSFSGYLPDNKLFRQ | ||||||
Domain | 786-1074 | Protein kinase | ||||
Sequence: LVEPNVIGKGCSGVVYRADVDNGEVIAVKKLWPAMVNGGHDEKTKNVRDSFSAEVKTLGTIRHKNIVRFLGCCWNRNTRLLMYDYMPNGSLGSLLHERRGSSLDWDLRYRILLGAAQGLAYLHHDCLPPIVHRDIKANNILIGLDFEPYIADFGLAKLVDEGDIGRCSNTVAGSYGYIAPEYGYSMKITEKSDVYSYGVVVLEVLTGKQPIDPTVPEGIHLVDWVRQNRGSLEVLDSTLRSRTEAEADEMMQVLGTALLCVNSSPDERPTMKDVAAMLKEIKQEREEYA |
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.
- Length1,141
- Mass (Da)124,504
- Last updated2000-10-01 v1
- Checksum1C9CE94DADC78B01
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 220 | in Ref. 1; CAD79350 | ||||
Sequence: S → L |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ550163 EMBL· GenBank· DDBJ | CAD79350.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
AP002037 EMBL· GenBank· DDBJ | BAB03091.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AB028621 EMBL· GenBank· DDBJ | BAB03091.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002686 EMBL· GenBank· DDBJ | AEE76878.1 EMBL· GenBank· DDBJ | Genomic DNA |