C0LGS2 (Y4361_ARATH) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 38.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Probable LRR receptor-like serine/threonine-protein kinase At4g36180 EC=2.7.11.1 | ||||
| Gene names |
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| Organism | Arabidopsis thaliana (Mouse-ear cress) [Reference proteome] | ||||
| Taxonomic identifier | 3702 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis![]() |
Protein attributes
| Sequence length | 1136 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Catalytic activity | ATP + a protein = ADP + a phosphoprotein. |
| Subcellular location | |
| Sequence similarities | Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Contains 26 LRR (leucine-rich) repeats. Contains 1 protein kinase domain. |
| Sequence caution | The sequence CAA18124.1 differs from that shown. Reason: Erroneous initiation. The sequence CAB81527.1 differs from that shown. Reason: Erroneous initiation. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cell membrane Membrane |
| Domain | Leucine-rich repeat Repeat Signal Transmembrane Transmembrane helix |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Kinase Receptor Serine/threonine-protein kinase Transferase |
| PTM | Glycoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Cellular_component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membraneInferred from direct assay Ref.5Ref.6. Source: TAIR |
| Molecular_function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activityInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 22 | 22 | Potential | ||||||
| Chain | 23 – 1136 | 1114 | Probable LRR receptor-like serine/threonine-protein kinase At4g36180 | PRO_0000387557 | |||||
Regions | |||||||||
| Topological domain | 23 – 751 | 729 | Extracellular Potential | ||||||
| Transmembrane | 752 – 772 | 21 | Helical; Potential | ||||||
| Topological domain | 773 – 1136 | 364 | Cytoplasmic Potential | ||||||
| Repeat | 93 – 115 | 23 | LRR 1 | ||||||
| Repeat | 117 – 139 | 23 | LRR 2 | ||||||
| Repeat | 141 – 162 | 22 | LRR 3 | ||||||
| Repeat | 163 – 186 | 24 | LRR 4 | ||||||
| Repeat | 187 – 210 | 24 | LRR 5 | ||||||
| Repeat | 211 – 233 | 23 | LRR 6 | ||||||
| Repeat | 235 – 256 | 22 | LRR 7 | ||||||
| Repeat | 259 – 280 | 22 | LRR 8 | ||||||
| Repeat | 283 – 304 | 22 | LRR 9 | ||||||
| Repeat | 309 – 330 | 22 | LRR 10 | ||||||
| Repeat | 333 – 355 | 23 | LRR 11 | ||||||
| Repeat | 357 – 379 | 23 | LRR 12 | ||||||
| Repeat | 381 – 403 | 23 | LRR 13 | ||||||
| Repeat | 405 – 426 | 22 | LRR 14 | ||||||
| Repeat | 429 – 452 | 24 | LRR 15 | ||||||
| Repeat | 453 – 479 | 27 | LRR 16 | ||||||
| Repeat | 480 – 500 | 21 | LRR 17 | ||||||
| Repeat | 501 – 524 | 24 | LRR 18 | ||||||
| Repeat | 525 – 546 | 22 | LRR 19 | ||||||
| Repeat | 549 – 571 | 23 | LRR 30 | ||||||
| Repeat | 573 – 595 | 23 | LRR 21 | ||||||
| Repeat | 597 – 620 | 24 | LRR 22 | ||||||
| Repeat | 621 – 643 | 23 | LRR 23 | ||||||
| Repeat | 645 – 666 | 22 | LRR 24 | ||||||
| Repeat | 669 – 691 | 23 | LRR 25 | ||||||
| Repeat | 694 – 716 | 23 | LRR 26 | ||||||
| Domain | 841 – 1123 | 283 | Protein kinase | ||||||
Amino acid modifications | |||||||||
| Glycosylation | 105 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 138 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 184 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 192 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 232 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 269 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 281 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 365 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 441 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 474 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 477 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 482 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 511 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 535 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 554 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 594 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 631 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 669 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 679 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 699 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 719 | 1 | N-linked (GlcNAc...) Potential | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. McCombie W.R.Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia. |
| [2] | The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia. |
| [3] | "Genome-wide cloning and sequence analysis of leucine-rich repeat receptor-like protein kinase genes in Arabidopsis thaliana." Gou X., He K., Yang H., Yuan T., Lin H., Clouse S.D., Li J. BMC Genomics 11:19-19(2010) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia. |
| [4] | "Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. Ecker J.R.Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 730-1136. Strain: cv. Columbia. |
| [5] | "Quantitative phosphoproteomics of early elicitor signaling in Arabidopsis." Benschop J.J., Mohammed S., O'Flaherty M., Heck A.J.R., Slijper M., Menke F.L.H. Mol. Cell. Proteomics 6:1198-1214(2007) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], SUBCELLULAR LOCATION. Strain: cv. Columbia. |
| [6] | "A high content in lipid-modified peripheral proteins and integral receptor kinases features in the arabidopsis plasma membrane proteome." Marmagne A., Ferro M., Meinnel T., Bruley C., Kuhn L., Garin J., Barbier-Brygoo H., Ephritikhine G. Mol. Cell. Proteomics 6:1980-1996(2007) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], SUBCELLULAR LOCATION. |
Web resources
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AL022141 Genomic DNA. Translation: CAA18124.1. Different initiation. AL161588 Genomic DNA. Translation: CAB81527.1. Different initiation. CP002687 Genomic DNA. Translation: AEE86628.1. FJ708764 mRNA. Translation: ACN59357.1. AY080606 mRNA. Translation: AAL86290.1. |
| IPI | IPI00531277. |
| PIR | T04587. |
| RefSeq | NP_195341.2. NM_119785.3. |
| UniGene | At.2123. |
3D structure databases | |
| ProteinModelPortal | C0LGS2. |
| SMR | C0LGS2. Positions 28-734, 827-1116. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 3702.AT4G36180.1-P. |
Proteomic databases | |
| PaxDb | C0LGS2. |
| PRIDE | C0LGS2. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblPlants | AT4G36180.1; AT4G36180.1; AT4G36180. |
| GeneID | 829775. |
| KEGG | ath:AT4G36180. |
Organism-specific databases | |
| GeneFarm | 2360. 51. |
| TAIR | At4g36180. |
Phylogenomic databases | |
| eggNOG | COG4886. |
| HOGENOM | HOG000116551. |
| InParanoid | O65510. |
| OMA | NCSSLVH. |
| PhylomeDB | C0LGS2. |
| ProtClustDB | CLSN2682550. |
Family and domain databases | |
| Gene3D | 2.60.120.200. 1 hit. |
| InterPro | IPR013320. ConA-like_subgrp. IPR011009. Kinase-like_dom. IPR001611. Leu-rich_rpt. IPR025875. Leu-rich_rpt_4. IPR013210. LRR-contain_N2. IPR000719. Prot_kinase_cat_dom. IPR001245. Ser-Thr/Tyr_kinase_cat_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view] |
| Pfam | PF00560. LRR_1. 3 hits. PF12799. LRR_4. 2 hits. PF08263. LRRNT_2. 1 hit. PF07714. Pkinase_Tyr. 1 hit. [Graphical view] |
| SUPFAM | SSF56112. Kinase_like. 1 hit. |
| PROSITE | PS00107. PROTEIN_KINASE_ATP. False negative. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | Y4361_ARATH | ||||||||
| Accession | Primary (citable) accession number: C0LGS2 Secondary accession number(s): O65510, Q8RXY8 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Plant Protein Annotation Program | ||||||||
Relevant documents
| Arabidopsis thaliana Arabidopsis thaliana: entries and gene names |
| SIMILARITY comments Index of protein domains and families |

Clusters with
