ID Y4361_ARATH Reviewed; 1136 AA. AC C0LGS2; O65510; Q8RXY8; DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot. DT 05-MAY-2009, sequence version 1. DT 02-SEP-2026, entry version 116. DE RecName: Full=Probable LRR receptor-like serine/threonine-protein kinase At4g36180; DE EC=2.7.11.1; DE Flags: Precursor; GN OrderedLocusNames=At4g36180; ORFNames=F23E13.70; 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=10617198; DOI=10.1038/47134; RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M., RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., RA Martienssen R., McCombie W.R.; RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."; RL Nature 402:769-777(1999). 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 GENOME REANNOTATION. RC STRAIN=cv. Columbia; RG The Arabidopsis Information Resource (TAIR); RT "Community-consensus reference genome of Arabidopsis thaliana Col-0."; RL Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases. RN [4] 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). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 730-1136. RC STRAIN=cv. Columbia; RX PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., RA Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION. RX PubMed=17644812; DOI=10.1074/mcp.m700099-mcp200; RA Marmagne A., Ferro M., Meinnel T., Bruley C., Kuhn L., Garin J., RA Barbier-Brygoo H., Ephritikhine G.; RT "A high content in lipid-modified peripheral proteins and integral receptor RT kinases features in the arabidopsis plasma membrane proteome."; RL Mol. Cell. Proteomics 6:1980-1996(2007). CC -!- CATALYTIC ACTIVITY: CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + CC H(+); 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=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + CC ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA- CC COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; CC -!- INTERACTION: CC C0LGS2; F4I065: At1g49100; NbExp=2; IntAct=EBI-16955302, EBI-20654598; CC C0LGS2; C0LGJ9: At2g02780; NbExp=2; IntAct=EBI-16955302, EBI-20651541; CC C0LGS2; C0LGL4: At2g28960; NbExp=2; IntAct=EBI-16955302, EBI-16946048; CC C0LGS2; O81069: At2g28990; NbExp=2; IntAct=EBI-16955302, EBI-16887698; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:17644812}; CC Single-pass type I membrane protein {ECO:0000305|PubMed:17644812}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}. CC -!- SEQUENCE CAUTION: CC Sequence=CAA18124.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=CAB81527.1; Type=Erroneous initiation; 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; AL022141; CAA18124.1; ALT_INIT; Genomic_DNA. DR EMBL; AL161588; CAB81527.1; ALT_INIT; Genomic_DNA. DR EMBL; CP002687; AEE86628.1; -; Genomic_DNA. DR EMBL; OZ408686; CAO7050107.1; -; Genomic_DNA. DR EMBL; FJ708764; ACN59357.1; -; mRNA. DR EMBL; AY080606; AAL86290.1; -; mRNA. DR PIR; T04587; T04587. DR RefSeq; NP_195341.2; NM_119785.4. DR AlphaFoldDB; C0LGS2; -. DR SMR; C0LGS2; -. DR BioGRID; 15057; 37. DR FunCoup; C0LGS2; 1133. DR IntAct; C0LGS2; 40. DR STRING; 3702.C0LGS2; -. DR GlyGen; C0LGS2; 22 sites. DR iPTMnet; C0LGS2; -. DR PaxDb; 3702-C0LGS2; -. DR ProteomicsDB; 242369; -. DR GeneID; 829775; -. DR KEGG; ath:AT4G36180; -. DR Araport; AT4G36180; -. DR TAIR; AT4G36180; -. DR eggNOG; ENOG502QTHE; Eukaryota. DR HOGENOM; CLU_000288_22_1_1; -. DR InParanoid; C0LGS2; -. DR OMA; TNNRVTE; -. DR PhylomeDB; C0LGS2; -. DR PRO; PR:C0LGS2; -. DR Proteomes; UP000006548; Chromosome 4. DR GO; GO:0005886; C:plasma membrane; HDA:TAIR. DR GO; GO:0090406; C:pollen tube; IDA:TAIR. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0016301; F:kinase activity; IDA:TAIR. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC. DR FunFam; 3.80.10.10:FF:000041; LRR receptor-like serine/threonine-protein kinase ERECTA; 1. DR FunFam; 3.80.10.10:FF:000101; LRR receptor-like serine/threonine-protein kinase ERECTA; 1. DR FunFam; 3.80.10.10:FF:000095; LRR receptor-like serine/threonine-protein kinase GSO1; 1. DR FunFam; 1.10.510.10:FF:000192; LRR receptor-like serine/threonine-protein kinase RPK2; 1. DR FunFam; 3.80.10.10:FF:000299; Piriformospora indica-insensitive protein 2; 1. DR FunFam; 3.30.200.20:FF:000404; Putative LRR receptor-like serine/threonine-protein kinase; 1. DR Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1. DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 5. 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; IPR003591; Leu-rich_rpt_typical-subtyp. 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 InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR48052:SF63; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR48052; UNNAMED PRODUCT; 1. DR Pfam; PF00560; LRR_1; 8. DR Pfam; PF13855; LRR_8; 4. DR Pfam; PF08263; LRRNT_2; 1. DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1. DR SMART; SM00369; LRR_TYP; 13. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF52058; L domain-like; 3. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 1: Evidence at protein level; KW ATP-binding; Cell membrane; Glycoprotein; Kinase; Leucine-rich repeat; KW Membrane; Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome; KW Repeat; Serine/threonine-protein kinase; Signal; Transferase; KW Transmembrane; Transmembrane helix. FT SIGNAL 1..22 FT /evidence="ECO:0000255" FT CHAIN 23..1136 FT /note="Probable LRR receptor-like serine/threonine-protein FT kinase At4g36180" FT /id="PRO_0000387557" FT TOPO_DOM 23..751 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 752..772 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 773..1136 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REPEAT 93..115 FT /note="LRR 1" FT REPEAT 117..139 FT /note="LRR 2" FT REPEAT 141..162 FT /note="LRR 3" FT REPEAT 163..186 FT /note="LRR 4" FT REPEAT 187..210 FT /note="LRR 5" FT REPEAT 211..233 FT /note="LRR 6" FT REPEAT 235..256 FT /note="LRR 7" FT REPEAT 259..280 FT /note="LRR 8" FT REPEAT 283..304 FT /note="LRR 9" FT REPEAT 309..330 FT /note="LRR 10" FT REPEAT 333..355 FT /note="LRR 11" FT REPEAT 357..379 FT /note="LRR 12" FT REPEAT 381..403 FT /note="LRR 13" FT REPEAT 405..426 FT /note="LRR 14" FT REPEAT 429..452 FT /note="LRR 15" FT REPEAT 453..479 FT /note="LRR 16" FT REPEAT 480..500 FT /note="LRR 17" FT REPEAT 501..524 FT /note="LRR 18" FT REPEAT 525..546 FT /note="LRR 19" FT REPEAT 549..571 FT /note="LRR 30" FT REPEAT 573..595 FT /note="LRR 21" FT REPEAT 597..620 FT /note="LRR 22" FT REPEAT 621..643 FT /note="LRR 23" FT REPEAT 645..666 FT /note="LRR 24" FT REPEAT 669..691 FT /note="LRR 25" FT REPEAT 694..716 FT /note="LRR 26" FT DOMAIN 841..1123 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 786..819 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 799..815 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 830 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:O22476" FT MOD_RES 838 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:O22476" FT MOD_RES 915 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:O22476" FT MOD_RES 1010 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:C0LGT6" FT CARBOHYD 105 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 138 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 184 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 192 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 232 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 269 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 281 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 365 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 441 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 474 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 477 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 482 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 511 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 535 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 554 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 594 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 631 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 669 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 679 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 699 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 719 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" SQ SEQUENCE 1136 AA; 123664 MW; 7AA32A277F6F2820 CRC64; MAMDISLFFI FLVIYAPLVS YADESQAEID ALTAFKLNLH DPLGALTSWD PSTPAAPCDW RGVGCTNHRV TEIRLPRLQL SGRISDRISG LRMLRKLSLR SNSFNGTIPT SLAYCTRLLS VFLQYNSLSG KLPPAMRNLT SLEVFNVAGN RLSGEIPVGL PSSLQFLDIS SNTFSGQIPS GLANLTQLQL LNLSYNQLTG EIPASLGNLQ SLQYLWLDFN LLQGTLPSAI SNCSSLVHLS ASENEIGGVI PAAYGALPKL EVLSLSNNNF SGTVPFSLFC NTSLTIVQLG FNAFSDIVRP ETTANCRTGL QVLDLQENRI SGRFPLWLTN ILSLKNLDVS GNLFSGEIPP DIGNLKRLEE LKLANNSLTG EIPVEIKQCG SLDVLDFEGN SLKGQIPEFL GYMKALKVLS LGRNSFSGYV PSSMVNLQQL ERLNLGENNL NGSFPVELMA LTSLSELDLS GNRFSGAVPV SISNLSNLSF LNLSGNGFSG EIPASVGNLF KLTALDLSKQ NMSGEVPVEL SGLPNVQVIA LQGNNFSGVV PEGFSSLVSL RYVNLSSNSF SGEIPQTFGF LRLLVSLSLS DNHISGSIPP EIGNCSALEV LELRSNRLMG HIPADLSRLP RLKVLDLGQN NLSGEIPPEI SQSSSLNSLS LDHNHLSGVI PGSFSGLSNL TKMDLSVNNL TGEIPASLAL ISSNLVYFNV SSNNLKGEIP ASLGSRINNT SEFSGNTELC GKPLNRRCES STAEGKKKKR KMILMIVMAA IGAFLLSLFC CFYVYTLLKW RKKLKQQSTT GEKKRSPGRT SAGSRVRSST SRSSTENGEP KLVMFNNKIT LAETIEATRQ FDEENVLSRT RYGLLFKANY NDGMVLSIRR LPNGSLLNEN LFKKEAEVLG KVKHRNITVL RGYYAGPPDL RLLVYDYMPN GNLSTLLQEA SHQDGHVLNW PMRHLIALGI ARGLGFLHQS NMVHGDIKPQ NVLFDADFEA HISDFGLDRL TIRSPSRSAV TANTIGTLGY VSPEATLSGE ITRESDIYSF GIVLLEILTG KRPVMFTQDE DIVKWVKKQL QRGQVTELLE PGLLELDPES SEWEEFLLGI KVGLLCTATD PLDRPTMSDV VFMLEGCRVG PDVPSSADPT SQPSPA //