ERECT_ARATH
ID ERECT_ARATH Reviewed; 976 AA.
AC Q42371; A5YYA0; A5YYB1; Q56WZ3;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=LRR receptor-like serine/threonine-protein kinase ERECTA {ECO:0000303|PubMed:8624444};
DE EC=2.7.11.1;
DE AltName: Full=Protein QUANTITATIVE RESISTANCE TO PLECTOSPHAERELLA 1;
DE AltName: Full=Protein QUANTITATIVE RESISTANCE TO RALSTONIA SOLANACEARUM 1;
DE AltName: Full=Protein TRANSPIRATION EFFICIENCY 1;
DE Flags: Precursor;
GN Name=ERECTA {ECO:0000303|PubMed:8624444}; Synonyms=ER, QRP1, QRS1, TE1;
GN OrderedLocusNames=At2g26330 {ECO:0000312|Araport:AT2G26330};
GN ORFNames=T1D16.3 {ECO:0000303|PubMed:10617197};
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 [GENOMIC DNA / MRNA], VARIANT ER-1 LYS-750, FUNCTION,
RP DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, MUTAGENESIS OF MET-282, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=8624444; DOI=10.2307/3870348;
RA Torii K.U., Mitsukawa N., Oosumi T., Matsuura Y., Yokoyama R.,
RA Whittier R.F., Komeda Y.;
RT "The Arabidopsis ERECTA gene encodes a putative receptor protein kinase
RT with extracellular leucine-rich repeats.";
RL Plant Cell 8:735-746(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 536-976.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 791-935, AND VARIANT MET-886.
RC STRAIN=cv. Ag-0, cv. An-1, cv. Br-0, cv. C24, cv. Ct-1, cv. Cvi-1,
RC cv. Edi-0, cv. Ga-0, cv. Kas-2, cv. Kin-0, cv. Landsberg erecta, cv. Ll-0,
RC cv. Lz-0, cv. Mt-0, cv. Nd-1, cv. Nok-3, cv. Oy-0, cv. Se-0, cv. Sorbo,
RC cv. Tsu-1, cv. Van-0, cv. Wa-1, and cv. Wassilewskija;
RX PubMed=17435248; DOI=10.1534/genetics.107.071928;
RA Ehrenreich I.M., Stafford P.A., Purugganan M.D.;
RT "The genetic architecture of shoot branching in Arabidopsis thaliana: a
RT comparative assessment of candidate gene associations vs. quantitative
RT trait locus mapping.";
RL Genetics 176:1223-1236(2007).
RN [8]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=9750343; DOI=10.1046/j.1365-313x.1998.00203.x;
RA Yokoyama R., Takahashi T., Kato A., Torii K.U., Komeda Y.;
RT "The Arabidopsis ERECTA gene is expressed in the shoot apical meristem and
RT organ primordia.";
RL Plant J. 15:301-310(1998).
RN [9]
RP FUNCTION, CHARACTERIZATION OF VARIANT ER-1 LYS-750, AND MUTAGENESIS OF
RP GLY-489 AND ASP-831.
RX DOI=10.1046/j.1469-8137.2001.00150.x;
RA Lease K.A., Lau N.Y., Schuster R.A., Torii K.U., Walker J.C.;
RT "Receptor serine/threonine protein kinases in signalling: analysis of the
RT erecta receptor-like kinase of Arabidopsis thaliana.";
RL New Phytol. 151:133-144(2001).
RN [10]
RP FUNCTION.
RX PubMed=11910003; DOI=10.1105/tpc.010391;
RA Douglas S.J., Chuck G., Dengler R.E., Pelecanda L., Riggs C.D.;
RT "KNAT1 and ERECTA regulate inflorescence architecture in Arabidopsis.";
RL Plant Cell 14:547-558(2002).
RN [11]
RP FUNCTION.
RX PubMed=12874130; DOI=10.1242/dev.00622;
RA Xu L., Xu Y., Dong A., Sun Y., Pi L., Xu Y., Huang H.;
RT "Novel as1 and as2 defects in leaf adaxial-abaxial polarity reveal the
RT requirement for ASYMMETRIC LEAVES1 and 2 and ERECTA functions in specifying
RT leaf adaxial identity.";
RL Development 130:4097-4107(2003).
RN [12]
RP FUNCTION, AND VARIANT ER-1 LYS-750.
RX PubMed=14617092; DOI=10.1046/j.1365-313x.2003.01877.x;
RA Godiard L., Sauviac L., Torii K.U., Grenon O., Mangin B., Grimsley N.H.,
RA Marco Y.;
RT "ERECTA, an LRR receptor-like kinase protein controlling development
RT pleiotropically affects resistance to bacterial wilt.";
RL Plant J. 36:353-365(2003).
RN [13]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=14985254; DOI=10.1242/dev.01028;
RA Shpak E.D., Berthiaume C.T., Hill E.J., Torii K.U.;
RT "Synergistic interaction of three ERECTA-family receptor-like kinases
RT controls Arabidopsis organ growth and flower development by promoting cell
RT proliferation.";
RL Development 131:1491-1501(2004).
RN [14]
RP FUNCTION.
RX PubMed=15034716; DOI=10.1007/s00425-004-1248-z;
RA Qi Y., Sun Y., Xu L., Xu Y., Huang H.;
RT "ERECTA is required for protection against heat-stress in the AS1/ AS2
RT pathway to regulate adaxial-abaxial leaf polarity in Arabidopsis.";
RL Planta 219:270-276(2004).
RN [15]
RP FUNCTION.
RX PubMed=16038894; DOI=10.1016/j.ydbio.2005.06.011;
RA Douglas S.J., Riggs C.D.;
RT "Pedicel development in Arabidopsis thaliana: contribution of vascular
RT positioning and the role of the BREVIPEDICELLUS and ERECTA genes.";
RL Dev. Biol. 284:451-463(2005).
RN [16]
RP FUNCTION.
RX PubMed=16007076; DOI=10.1038/nature03835;
RA Masle J., Gilmore S.R., Farquhar G.D.;
RT "The ERECTA gene regulates plant transpiration efficiency in Arabidopsis.";
RL Nature 436:866-870(2005).
RN [17]
RP FUNCTION, MUTAGENESIS OF GLY-489 AND ASP-831, AND VARIANT ER-1 LYS-750.
RX PubMed=15998304; DOI=10.1111/j.1365-313x.2005.02440.x;
RA Llorente F., Alonso-Blanco C., Sanchez-Rodriguez C., Jorda L., Molina A.;
RT "ERECTA receptor-like kinase and heterotrimeric G protein from Arabidopsis
RT are required for resistance to the necrotrophic fungus Plectosphaerella
RT cucumerina.";
RL Plant J. 43:165-180(2005).
RN [18]
RP FUNCTION, AND MUTAGENESIS OF MET-282.
RX PubMed=16126863; DOI=10.1104/pp.105.063495;
RA Woodward C., Bemis S.M., Hill E.J., Sawa S., Koshiba T., Torii K.U.;
RT "Interaction of auxin and ERECTA in elaborating Arabidopsis inflorescence
RT architecture revealed by the activation tagging of a new member of the
RT YUCCA family putative flavin monooxygenases.";
RL Plant Physiol. 139:192-203(2005).
RN [19]
RP FUNCTION.
RX PubMed=16002616; DOI=10.1126/science.1109710;
RA Shpak E.D., McAbee J.M., Pillitteri L.J., Torii K.U.;
RT "Stomatal patterning and differentiation by synergistic interactions of
RT receptor kinases.";
RL Science 309:290-293(2005).
RN [20]
RP FUNCTION.
RX PubMed=17652352; DOI=10.1242/dev.004788;
RA Pillitteri L.J., Bemis S.M., Shpak E.D., Torii K.U.;
RT "Haploinsufficiency after successive loss of signaling reveals a role for
RT ERECTA-family genes in Arabidopsis ovule development.";
RL Development 134:3099-3109(2007).
RN [21]
RP FUNCTION, AND VARIANT ER-1 LYS-750.
RX PubMed=17513501; DOI=10.1105/tpc.106.048041;
RA Adie B.A.T., Perez-Perez J., Perez-Perez M.M., Godoy M.,
RA Sanchez-Serrano J.-J., Schmelz E.A., Solano R.;
RT "ABA is an essential signal for plant resistance to pathogens affecting JA
RT biosynthesis and the activation of defenses in Arabidopsis.";
RL Plant Cell 19:1665-1681(2007).
RN [22]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17698961; DOI=10.1073/pnas.0701936104;
RA Hall M.C., Dworkin I., Ungerer M.C., Purugganan M.;
RT "Genetics of microenvironmental canalization in Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:13717-13722(2007).
RN [23]
RP FUNCTION.
RX PubMed=19416942; DOI=10.1534/genetics.108.097030;
RA Stinchcombe J.R., Weinig C., Heath K.D., Brock M.T., Schmitt J.;
RT "Polymorphic genes of major effect: consequences for variation, selection
RT and evolution in Arabidopsis thaliana.";
RL Genetics 182:911-922(2009).
RN [24]
RP FUNCTION.
RX PubMed=19346258; DOI=10.1093/jxb/erp084;
RA Ghandilyan A., Ilk N., Hanhart C., Mbengue M., Barboza L., Schat H.,
RA Koornneef M., El-Lithy M., Vreugdenhil D., Reymond M., Aarts M.G.M.;
RT "A strong effect of growth medium and organ type on the identification of
RT QTLs for phytate and mineral concentrations in three Arabidopsis thaliana
RT RIL populations.";
RL J. Exp. Bot. 60:1409-1425(2009).
RN [25]
RP FUNCTION, AND VARIANT ER-1 LYS-750.
RX PubMed=19589071; DOI=10.1094/mpmi-22-8-0953;
RA Sanchez-Rodriguez C., Estevez J.M., Llorente F., Hernandez-Blanco C.,
RA Jorda L., Pagan I., Berrocal M., Marco Y., Somerville S., Molina A.;
RT "The ERECTA receptor-like kinase regulates cell wall-mediated resistance to
RT pathogens in Arabidopsis thaliana.";
RL Mol. Plant Microbe Interact. 22:953-963(2009).
RN [26]
RP REVIEW.
RX PubMed=19303350; DOI=10.1016/j.tplants.2009.01.010;
RA van Zanten M., Snoek L.B., Proveniers M.C.G., Peeters A.J.M.;
RT "The many functions of ERECTA.";
RL Trends Plant Sci. 14:214-218(2009).
RN [27]
RP INTERACTION WITH EPFL5.
RX PubMed=21862708; DOI=10.1105/tpc.111.086637;
RA Abrash E.B., Davies K.A., Bergmann D.C.;
RT "Generation of signaling specificity in Arabidopsis by spatially restricted
RT buffering of ligand-receptor interactions.";
RL Plant Cell 23:2864-2879(2011).
RN [28]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, INTERACTION WITH ERL1; TMM; EPF1
RP AND EPF2, AND SUBUNIT.
RX PubMed=22241782; DOI=10.1101/gad.179895.111;
RA Lee J.S., Kuroha T., Hnilova M., Khatayevich D., Kanaoka M.M., McAbee J.M.,
RA Sarikaya M., Tamerler C., Torii K.U.;
RT "Direct interaction of ligand-receptor pairs specifying stomatal
RT patterning.";
RL Genes Dev. 26:126-136(2012).
RN [29]
RP FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH EPFL4 AND EPFL6.
RX PubMed=22474391; DOI=10.1073/pnas.1117537109;
RA Uchida N., Lee J.S., Horst R.J., Lai H.H., Kajita R., Kakimoto T.,
RA Tasaka M., Torii K.U.;
RT "Regulation of inflorescence architecture by intertissue layer ligand-
RT receptor communication between endodermis and phloem.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:6337-6342(2012).
RN [30]
RP FUNCTION.
RX PubMed=23881395; DOI=10.1093/jxb/ert196;
RA Uchida N., Tasaka M.;
RT "Regulation of plant vascular stem cells by endodermis-derived EPFL-family
RT peptide hormones and phloem-expressed ERECTA-family receptor kinases.";
RL J. Exp. Bot. 64:5335-5343(2013).
RN [31]
RP INTERACTION WITH SERK1; SERK2; SERK3/BAK1 AND SERK4.
RX PubMed=26320950; DOI=10.1016/j.cub.2015.07.068;
RA Meng X., Chen X., Mang H., Liu C., Yu X., Gao X., Torii K.U., He P.,
RA Shan L.;
RT "Differential function of Arabidopsis SERK family receptor-like kinases in
RT stomatal patterning.";
RL Curr. Biol. 25:2361-2372(2015).
RN [32]
RP INTERACTION WITH EPFL9.
RX PubMed=26083750; DOI=10.1038/nature14561;
RA Lee J.S., Hnilova M., Maes M., Lin Y.C., Putarjunan A., Han S.K., Avila J.,
RA Torii K.U.;
RT "Competitive binding of antagonistic peptides fine-tunes stomatal
RT patterning.";
RL Nature 522:439-443(2015).
RN [33]
RP SUBCELLULAR LOCATION.
RX PubMed=26203655; DOI=10.1371/journal.pgen.1005374;
RA Horst R.J., Fujita H., Lee J.S., Rychel A.L., Garrick J.M., Kawaguchi M.,
RA Peterson K.M., Torii K.U.;
RT "Molecular framework of a regulatory circuit initiating two-dimensional
RT spatial patterning of stomatal lineage.";
RL PLoS Genet. 11:E1005374-E1005374(2015).
RN [34]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH TMM.
RX PubMed=28536146; DOI=10.1101/gad.297580.117;
RA Lin G., Zhang L., Han Z., Yang X., Liu W., Li E., Chang J., Qi Y.,
RA Shpak E.D., Chai J.;
RT "A receptor-like protein acts as a specificity switch for the regulation of
RT stomatal development.";
RL Genes Dev. 31:927-938(2017).
CC -!- FUNCTION: Receptor kinase that, together with ERL1 and ERL2, regulates
CC aerial architecture, including inflorescence (e.g. shoot apical
CC meristem-originating organ shape, elongation of the internode and
CC pedicels, and adaxial-abaxial polarity), and stomatal patterning (e.g.
CC density and clustering), probably by tuning cell division and
CC expansion. Redundantly involved with ERL1 in procambial development
CC regulation. Forms a functional ligand-receptor pair with EPF2 (AC
CC Q8LC53) (PubMed:22241782). Modulates plant transpiration efficiency by
CC controlling stomatal density, leaf photosynthetic capacity, epidermal
CC cell expansion, mesophyll cell proliferation and cell-cell contact. A
CC phloem-specific expression of ER is sufficient for proper inflorescence
CC architecture (PubMed:22474391). Probable major trait regulating
CC canalization (maintenance of phenotype despite varying environment) in
CC many aspect of the plant physiology (e.g. plant morphology, light-
CC dependent leaves number, branch number, flowering time, phytate and
CC mineral concentrations) by transducing microenvironmental variation
CC into phenotypic differentiation (ecological amplifier). May maintain
CC development integrity in heat stress conditions. Regulates cell wall
CC composition and structure. Confers resistance to the pathogenic
CC bacteria Ralstonia solanacearum and to the necrotrophic fungi
CC Plectosphaerella cucumerina and Pythium irregulare, and required for
CC callose deposition upon infection. Resistance to P.cucumerina seems
CC cell wall-mediated. Forms a constitutive complex with TMM involved in
CC the recognition of the stomatal regulatory peptides EPF1, EPF2 and
CC EPFL9/STOMAGEN (PubMed:28536146). {ECO:0000269|PubMed:11910003,
CC ECO:0000269|PubMed:12874130, ECO:0000269|PubMed:14617092,
CC ECO:0000269|PubMed:14985254, ECO:0000269|PubMed:15034716,
CC ECO:0000269|PubMed:15998304, ECO:0000269|PubMed:16002616,
CC ECO:0000269|PubMed:16007076, ECO:0000269|PubMed:16038894,
CC ECO:0000269|PubMed:16126863, ECO:0000269|PubMed:17513501,
CC ECO:0000269|PubMed:17652352, ECO:0000269|PubMed:17698961,
CC ECO:0000269|PubMed:19346258, ECO:0000269|PubMed:19416942,
CC ECO:0000269|PubMed:19589071, ECO:0000269|PubMed:22241782,
CC ECO:0000269|PubMed:22474391, ECO:0000269|PubMed:23881395,
CC ECO:0000269|PubMed:28536146, ECO:0000269|PubMed:8624444,
CC ECO:0000269|Ref.9}.
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 -!- SUBUNIT: Homodimer and heterodimer with ERL1 and TMM. Interacts with
CC EPF1, EPF2, EPFL4, EPFL5 and EPFL6. Interacts with SERK1, SERK2,
CC SERK3/BAK1 and SERK4 in a EPF2-induced manner (PubMed:26320950).
CC Interacts with EPFL9/STOMAGEN (PubMed:26083750).
CC {ECO:0000269|PubMed:21862708, ECO:0000269|PubMed:22241782,
CC ECO:0000269|PubMed:22474391, ECO:0000269|PubMed:26083750,
CC ECO:0000269|PubMed:26320950, ECO:0000269|PubMed:28536146}.
CC -!- INTERACTION:
CC Q42371; Q94F62: BAK1; NbExp=4; IntAct=EBI-16940407, EBI-617138;
CC Q42371; Q6XAT2: ERL2; NbExp=4; IntAct=EBI-16940407, EBI-16895926;
CC Q42371; Q9FL28: FLS2; NbExp=2; IntAct=EBI-16940407, EBI-1799448;
CC Q42371; C0LGQ5: GSO1; NbExp=3; IntAct=EBI-16940407, EBI-16905069;
CC Q42371; C0LGX3: HSL2; NbExp=2; IntAct=EBI-16940407, EBI-16904927;
CC Q42371; Q9C8I6: IOS1; NbExp=3; IntAct=EBI-16940407, EBI-16924837;
CC Q42371; Q9ZVD4: LRR-RLK; NbExp=2; IntAct=EBI-16940407, EBI-20651739;
CC Q42371; Q9LFS4: NIK1; NbExp=3; IntAct=EBI-16940407, EBI-16146189;
CC Q42371; Q9ZRF9: RPK1; NbExp=3; IntAct=EBI-16940407, EBI-1238953;
CC Q42371; Q9SKG5: SERK4; NbExp=2; IntAct=EBI-16940407, EBI-6290483;
CC Q42371; Q8LPS5: SERK5; NbExp=3; IntAct=EBI-16940407, EBI-16887868;
CC Q42371; Q6R2K3: SRF3; NbExp=2; IntAct=EBI-16940407, EBI-20651925;
CC Q42371; Q8RWZ1: SUB; NbExp=3; IntAct=EBI-16940407, EBI-17072125;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22241782,
CC ECO:0000269|PubMed:26203655, ECO:0000303|PubMed:8624444}; Single-pass
CC type I membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in shoot apical meristems (SAM),
CC organ primordia, flowers, siliques and young rosette leaves, and, to a
CC lower extent, in stems and cauline leaves. Expressed in growing
CC inflorescence stems and pedicels. Detected in epidermis, phloem and
CC xylem. {ECO:0000269|PubMed:22474391, ECO:0000269|PubMed:8624444,
CC ECO:0000269|PubMed:9750343}.
CC -!- DEVELOPMENTAL STAGE: Strongly expressed in organ primordia and immature
CC organs but weakly in mature organs. Observed in SAM at low levels
CC during the vegetative growth with an increase at the transition to the
CC reproductive growth phase. At the reproductive stage, localized in the
CC young developing flowers. Expressed in inflorescence meristem and is
CC up-regulated during flower initiation and formation of flower organs.
CC Also found in cells that differentiate into pedicels.
CC {ECO:0000269|PubMed:14985254, ECO:0000269|PubMed:9750343}.
CC -!- DOMAIN: The kinase domain is not required for ligand binding.
CC {ECO:0000269|PubMed:22241782}.
CC -!- POLYMORPHISM: The cultivar Landsberg erecta (cv. Ler) derives from cv.
CC Landsberg (cv. La-0) in which ERECTA is mutated at Ile-750 (variant
CC er).
CC -!- DISRUPTION PHENOTYPE: In er-104 and er-105, small curly leaves and
CC compact inflorescence with short thick siliques, increased canalization
CC of rosette leaf number during long days. {ECO:0000269|PubMed:17698961,
CC ECO:0000269|PubMed:8624444}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=A complicated affair - Issue
CC 116 of April 2010;
CC URL="https://web.expasy.org/spotlight/back_issues/116";
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; D83257; BAA11869.1; -; Genomic_DNA.
DR EMBL; U47029; AAC49302.1; -; mRNA.
DR EMBL; AC004484; AAC14518.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07825.1; -; Genomic_DNA.
DR EMBL; AY035110; AAK59615.1; -; mRNA.
DR EMBL; FJ708701; ACN59296.1; -; mRNA.
DR EMBL; AK221886; BAD94220.1; -; mRNA.
DR EMBL; EF598332; ABR08864.1; -; Genomic_DNA.
DR EMBL; EF598333; ABR08865.1; -; Genomic_DNA.
DR EMBL; EF598334; ABR08866.1; -; Genomic_DNA.
DR EMBL; EF598335; ABR08867.1; -; Genomic_DNA.
DR EMBL; EF598336; ABR08868.1; -; Genomic_DNA.
DR EMBL; EF598337; ABR08869.1; -; Genomic_DNA.
DR EMBL; EF598338; ABR08870.1; -; Genomic_DNA.
DR EMBL; EF598339; ABR08871.1; -; Genomic_DNA.
DR EMBL; EF598340; ABR08872.1; -; Genomic_DNA.
DR EMBL; EF598341; ABR08873.1; -; Genomic_DNA.
DR EMBL; EF598342; ABR08874.1; -; Genomic_DNA.
DR EMBL; EF598343; ABR08875.1; -; Genomic_DNA.
DR EMBL; EF598344; ABR08876.1; -; Genomic_DNA.
DR EMBL; EF598345; ABR08877.1; -; Genomic_DNA.
DR EMBL; EF598346; ABR08878.1; -; Genomic_DNA.
DR EMBL; EF598347; ABR08879.1; -; Genomic_DNA.
DR EMBL; EF598348; ABR08880.1; -; Genomic_DNA.
DR EMBL; EF598349; ABR08881.1; -; Genomic_DNA.
DR EMBL; EF598350; ABR08882.1; -; Genomic_DNA.
DR EMBL; EF598351; ABR08883.1; -; Genomic_DNA.
DR EMBL; EF598352; ABR08884.1; -; Genomic_DNA.
DR EMBL; EF598353; ABR08885.1; -; Genomic_DNA.
DR EMBL; EF598354; ABR08886.1; -; Genomic_DNA.
DR PIR; B84659; B84659.
DR RefSeq; NP_180201.1; NM_128190.3.
DR AlphaFoldDB; Q42371; -.
DR SMR; Q42371; -.
DR BioGRID; 2525; 48.
DR IntAct; Q42371; 57.
DR STRING; 3702.AT2G26330.1; -.
DR TCDB; 1.A.87.2.11; the mechanosensitive calcium channel (mca) family.
DR iPTMnet; Q42371; -.
DR PaxDb; Q42371; -.
DR PRIDE; Q42371; -.
DR ProteomicsDB; 221805; -.
DR EnsemblPlants; AT2G26330.1; AT2G26330.1; AT2G26330.
DR GeneID; 817173; -.
DR Gramene; AT2G26330.1; AT2G26330.1; AT2G26330.
DR KEGG; ath:AT2G26330; -.
DR Araport; AT2G26330; -.
DR TAIR; locus:2005507; AT2G26330.
DR eggNOG; ENOG502QTEP; Eukaryota.
DR HOGENOM; CLU_000288_22_1_1; -.
DR InParanoid; Q42371; -.
DR OMA; VYEDIMT; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; Q42371; -.
DR PRO; PR:Q42371; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q42371; baseline and differential.
DR Genevisible; Q42371; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042277; F:peptide binding; IPI:TAIR.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0033612; F:receptor serine/threonine kinase binding; IPI:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
DR GO; GO:0019199; F:transmembrane receptor protein kinase activity; ISS:TAIR.
DR GO; GO:0070370; P:cellular heat acclimation; IMP:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR GO; GO:0048281; P:inflorescence morphogenesis; IMP:UniProtKB.
DR GO; GO:0009965; P:leaf morphogenesis; IMP:TAIR.
DR GO; GO:0010087; P:phloem or xylem histogenesis; IMP:TAIR.
DR GO; GO:0009664; P:plant-type cell wall organization; IMP:UniProtKB.
DR GO; GO:0009944; P:polarity specification of adaxial/abaxial axis; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0030155; P:regulation of cell adhesion; IMP:TAIR.
DR GO; GO:0051302; P:regulation of cell division; IMP:TAIR.
DR GO; GO:0001558; P:regulation of cell growth; IMP:TAIR.
DR GO; GO:1905421; P:regulation of plant organ morphogenesis; IMP:TAIR.
DR GO; GO:0010103; P:stomatal complex morphogenesis; IMP:TAIR.
DR GO; GO:0010148; P:transpiration; IMP:UniProtKB.
DR Gene3D; 3.80.10.10; -; 3.
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; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF13516; LRR_6; 2.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 8.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51450; LRR; 17.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 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; Cell wall biogenesis/degradation;
KW Developmental protein; Glycoprotein; Kinase; Leucine-rich repeat; Membrane;
KW Nucleotide-binding; Phosphoprotein; Plant defense; Receptor;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Signal;
KW Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..976
FT /note="LRR receptor-like serine/threonine-protein kinase
FT ERECTA"
FT /id="PRO_0000389000"
FT TOPO_DOM 25..580
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 581..601
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 602..976
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 69..92
FT /note="LRR 1"
FT REPEAT 93..115
FT /note="LRR 2"
FT REPEAT 117..140
FT /note="LRR 3"
FT REPEAT 141..163
FT /note="LRR 4"
FT REPEAT 165..187
FT /note="LRR 5"
FT REPEAT 189..212
FT /note="LRR 6"
FT REPEAT 213..235
FT /note="LRR 7"
FT REPEAT 237..259
FT /note="LRR 8"
FT REPEAT 260..282
FT /note="LRR 9"
FT REPEAT 284..306
FT /note="LRR 10"
FT REPEAT 308..330
FT /note="LRR 11"
FT REPEAT 332..355
FT /note="LRR 12"
FT REPEAT 356..379
FT /note="LRR 13"
FT REPEAT 380..401
FT /note="LRR 14"
FT REPEAT 404..425
FT /note="LRR 15"
FT REPEAT 428..449
FT /note="LRR 16"
FT REPEAT 452..473
FT /note="LRR 17"
FT REPEAT 476..498
FT /note="LRR 18"
FT REPEAT 500..522
FT /note="LRR 19"
FT REPEAT 523..545
FT /note="LRR 20"
FT DOMAIN 648..918
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 773
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 654..662
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 676
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 645
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 721
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 760
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 815
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 823
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 234
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 409
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 457
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 510
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 528
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 543
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 750
FT /note="I -> K (er-1 in strain: cv. Landsberg erecta; round
FT leaves, compact inflorescence, blunt fruits, short and
FT thick siliques and petioles, susceptibility to pathogens
FT such as R.solanacearum, P.irregulare and P.cucumerina,
FT abnormal cell-wall composition and increased canalization
FT of rosette leaf number during long days. In er-101 and er-
FT 102, compact inflorescence with short siliques and
FT pedicels)"
FT /evidence="ECO:0000269|PubMed:14617092,
FT ECO:0000269|PubMed:15998304, ECO:0000269|PubMed:17513501,
FT ECO:0000269|PubMed:19589071, ECO:0000269|PubMed:8624444,
FT ECO:0000269|Ref.9"
FT VARIANT 886
FT /note="V -> M (in strain: cv. Mt-0)"
FT /evidence="ECO:0000269|PubMed:17435248"
FT MUTAGEN 282
FT /note="M->I: In er-103; compact inflorescence with short
FT siliques, but normal leaves."
FT /evidence="ECO:0000269|PubMed:16126863,
FT ECO:0000269|PubMed:8624444"
FT MUTAGEN 489
FT /note="G->D: In er-117; compact inflorescence with short
FT siliques and pedicels, and susceptibility to P.cucumerina."
FT /evidence="ECO:0000269|PubMed:15998304, ECO:0000269|Ref.9"
FT MUTAGEN 831
FT /note="D->N: In er-114; compact inflorescence with short
FT siliques and pedicels, and susceptibility to P.cucumerina."
FT /evidence="ECO:0000269|PubMed:15998304, ECO:0000269|Ref.9"
SQ SEQUENCE 976 AA; 107334 MW; 0E51D46A4AB94C8D CRC64;
MALFRDIVLL GFLFCLSLVA TVTSEEGATL LEIKKSFKDV NNVLYDWTTS PSSDYCVWRG
VSCENVTFNV VALNLSDLNL DGEISPAIGD LKSLLSIDLR GNRLSGQIPD EIGDCSSLQN
LDLSFNELSG DIPFSISKLK QLEQLILKNN QLIGPIPSTL SQIPNLKILD LAQNKLSGEI
PRLIYWNEVL QYLGLRGNNL VGNISPDLCQ LTGLWYFDVR NNSLTGSIPE TIGNCTAFQV
LDLSYNQLTG EIPFDIGFLQ VATLSLQGNQ LSGKIPSVIG LMQALAVLDL SGNLLSGSIP
PILGNLTFTE KLYLHSNKLT GSIPPELGNM SKLHYLELND NHLTGHIPPE LGKLTDLFDL
NVANNDLEGP IPDHLSSCTN LNSLNVHGNK FSGTIPRAFQ KLESMTYLNL SSNNIKGPIP
VELSRIGNLD TLDLSNNKIN GIIPSSLGDL EHLLKMNLSR NHITGVVPGD FGNLRSIMEI
DLSNNDISGP IPEELNQLQN IILLRLENNN LTGNVGSLAN CLSLTVLNVS HNNLVGDIPK
NNNFSRFSPD SFIGNPGLCG SWLNSPCHDS RRTVRVSISR AAILGIAIGG LVILLMVLIA
ACRPHNPPPF LDGSLDKPVT YSTPKLVILH MNMALHVYED IMRMTENLSE KYIIGHGASS
TVYKCVLKNC KPVAIKRLYS HNPQSMKQFE TELEMLSSIK HRNLVSLQAY SLSHLGSLLF
YDYLENGSLW DLLHGPTKKK TLDWDTRLKI AYGAAQGLAY LHHDCSPRII HRDVKSSNIL
LDKDLEARLT DFGIAKSLCV SKSHTSTYVM GTIGYIDPEY ARTSRLTEKS DVYSYGIVLL
ELLTRRKAVD DESNLHHLIM SKTGNNEVME MADPDITSTC KDLGVVKKVF QLALLCTKRQ
PNDRPTMHQV TRVLGSFMLS EQPPAATDTS ATLAGSCYVD EYANLKTPHS VNCSSMSASD
AQLFLRFGQV ISQNSE
