ID Y1699_ARATH Reviewed; 591 AA. AC C0LGI5; O04545; DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot. DT 05-MAY-2009, sequence version 1. DT 27-MAR-2024, entry version 94. DE RecName: Full=Probable LRR receptor-like serine/threonine-protein kinase At1g69990; DE EC=2.7.11.1; DE Flags: Precursor; GN OrderedLocusNames=At1g69990; ORFNames=F20P5.27; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=11130712; DOI=10.1038/35048500; RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L., RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., RA Yu G., Fraser C.M., Venter J.C., Davis R.W.; RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."; RL Nature 408:816-820(2000). RN [2] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RX PubMed=27862469; DOI=10.1111/tpj.13415; RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S., RA Town C.D.; RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference RT genome."; RL Plant J. 89:789-804(2017). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX PubMed=20064227; DOI=10.1186/1471-2164-11-19; RA Gou X., He K., Yang H., Yuan T., Lin H., Clouse S.D., Li J.; RT "Genome-wide cloning and sequence analysis of leucine-rich repeat receptor- RT like protein kinase genes in Arabidopsis thaliana."; RL BMC Genomics 11:19-19(2010). CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; CC EC=2.7.11.1; CC -!- INTERACTION: CC C0LGI5; C0LGD9: At1g07560; NbExp=2; IntAct=EBI-20651225, EBI-16902423; CC C0LGI5; C0LGI5: At1g69990; NbExp=2; IntAct=EBI-20651225, EBI-20651225; CC C0LGI5; Q9ZQR3: At2g14510; NbExp=2; IntAct=EBI-20651225, EBI-20651957; CC C0LGI5; Q8VYT3: At4g30520; NbExp=2; IntAct=EBI-20651225, EBI-16902452; CC C0LGI5; Q94F62: BAK1; NbExp=4; IntAct=EBI-20651225, EBI-617138; CC C0LGI5; Q6XAT2: ERL2; NbExp=3; IntAct=EBI-20651225, EBI-16895926; CC C0LGI5; Q9C8I6: IOS1; NbExp=4; IntAct=EBI-20651225, EBI-16924837; CC C0LGI5; Q9ZVD4: LRR-RLK; NbExp=2; IntAct=EBI-20651225, EBI-20651739; CC C0LGI5; Q9LFS4: NIK1; NbExp=2; IntAct=EBI-20651225, EBI-16146189; CC C0LGI5; C0LGR3: RGI3; NbExp=3; IntAct=EBI-20651225, EBI-20659695; CC C0LGI5; Q9ZRF9: RPK1; NbExp=3; IntAct=EBI-20651225, EBI-1238953; CC C0LGI5; Q9SKG5: SERK4; NbExp=4; IntAct=EBI-20651225, EBI-6290483; CC C0LGI5; Q8LPS5: SERK5; NbExp=2; IntAct=EBI-20651225, EBI-16887868; CC C0LGI5; Q9C8M9: SRF6; NbExp=3; IntAct=EBI-20651225, EBI-16954301; CC C0LGI5; Q8RWZ1: SUB; NbExp=3; IntAct=EBI-20651225, EBI-17072125; CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB61113.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AC002062; AAB61113.1; ALT_SEQ; Genomic_DNA. DR EMBL; CP002684; AEE35006.1; -; Genomic_DNA. DR EMBL; FJ708675; ACN59270.1; -; mRNA. DR PIR; E96722; E96722. DR RefSeq; NP_177157.1; NM_105668.1. DR AlphaFoldDB; C0LGI5; -. DR SMR; C0LGI5; -. DR BioGRID; 28557; 28. DR IntAct; C0LGI5; 42. DR STRING; 3702.C0LGI5; -. DR PaxDb; 3702-AT1G69990-1; -. DR EnsemblPlants; AT1G69990.1; AT1G69990.1; AT1G69990. DR GeneID; 843336; -. DR Gramene; AT1G69990.1; AT1G69990.1; AT1G69990. DR KEGG; ath:AT1G69990; -. DR Araport; AT1G69990; -. DR TAIR; AT1G69990; BIR4. DR eggNOG; ENOG502QRP1; Eukaryota. DR HOGENOM; CLU_000288_92_6_1; -. DR InParanoid; C0LGI5; -. DR OMA; GMFWWFF; -. DR OrthoDB; 675128at2759; -. DR PhylomeDB; C0LGI5; -. DR PRO; PR:C0LGI5; -. DR Proteomes; UP000006548; Chromosome 1. DR ExpressionAtlas; C0LGI5; baseline and differential. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR001611; Leu-rich_rpt. DR InterPro; IPR032675; LRR_dom_sf. DR InterPro; IPR013210; LRR_N_plant-typ. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom. DR PANTHER; PTHR48055; LEUCINE-RICH REPEAT RECEPTOR PROTEIN KINASE EMS1; 1. DR PANTHER; PTHR48055:SF20; LEUCINE-RICH REPEAT RECEPTOR PROTEIN KINASE MSP1; 1. DR Pfam; PF00560; LRR_1; 1. DR Pfam; PF13855; LRR_8; 1. DR Pfam; PF08263; LRRNT_2; 1. DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1. DR PRINTS; PR00019; LEURICHRPT. DR SUPFAM; SSF52058; L domain-like; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR Genevisible; C0LGI5; AT. PE 1: Evidence at protein level; KW ATP-binding; Glycoprotein; Kinase; Leucine-rich repeat; Membrane; KW Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome; Repeat; KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane; KW Transmembrane helix. FT SIGNAL 1..18 FT /evidence="ECO:0000255" FT CHAIN 19..591 FT /note="Probable LRR receptor-like serine/threonine-protein FT kinase At1g69990" FT /id="PRO_0000387541" FT TOPO_DOM 19..218 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 219..239 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 240..591 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REPEAT 66..88 FT /note="LRR 1" FT REPEAT 90..111 FT /note="LRR 2" FT REPEAT 115..137 FT /note="LRR 3" FT REPEAT 139..162 FT /note="LRR 4" FT REPEAT 163..185 FT /note="LRR 5" FT DOMAIN 295..573 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 301..309 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 323 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 292 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q9LSI9" FT MOD_RES 378 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9LSI9" FT MOD_RES 389 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q94AG2" FT MOD_RES 463 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q94AG2" FT MOD_RES 465 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q94AG2" FT MOD_RES 466 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q94AG2" FT MOD_RES 470 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q94AG2" FT CARBOHYD 46 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 211 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" SQ SEQUENCE 591 AA; 65553 MW; D3AF9B8A24DABFB0 CRC64; MKTISIFFVI ILMSSSHAED DVLCLKGFKS SLKDPSNQLN TWSFPNSSSS ICKLTGVSCW NAKENRILSL QLQSMQLSGQ IPESLKLCRS LQSLDLSFND FSGLIPSQIC SWLPYLVTLD LSGNKLSGSI PSQIVDCKFL NSLALNQNKL TGSIPSELTR LNRLQRLSLA DNDLSGSIPS ELSHYGEDGF RGNGGLCGKP LSNCGSFNGK NLTIIVTAGV IGAVGSLCVG FGMFWWFFIR DRRKMNNYGY GAGKCKDDSD WIGLLRSHKL VQVTLFQKPI VKIKLVDLIE ATNGFDSGNI VVSSRSGVSY KADLPDGSTL EVKRLSSCCE LSEKQFRSEI NKLGQIRHPN LVPLLGFCVV EDEILLVYKH MANGTLYSQL QQWDIDWPTR VRVAVGAARG LAWLHHGCQP LYMHQYISSN VILLDEDFDA RVIDYGLGKL VSSQDSKDSS FSNGKFGYVA PEYSSTMVAS LSGDVYGFGI VLLEIVTGQK PVLINNGEEG FKESLVEWVS KHLSNGRSKD AIDRRIFGKG YDDEIMQVLR IACSCVVSRP KERPLMIQVY ESLKNLGDQH GFFSEYSDEF PLIFNKQEHL K //