CRN_ARATH
ID CRN_ARATH Reviewed; 401 AA.
AC Q9LYU7; A8MRZ3; Q3E9I0;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Inactive leucine-rich repeat receptor-like protein kinase CORYNE {ECO:0000303|PubMed:18381924};
DE AltName: Full=Protein SUPPRESSOR OF OVEREXPRESSION OF LLP1 2 {ECO:0000303|PubMed:12932329};
DE Flags: Precursor;
GN Name=CRN {ECO:0000303|PubMed:18381924};
GN Synonyms=SOL2 {ECO:0000303|PubMed:12932329};
GN OrderedLocusNames=At5g13290 {ECO:0000312|Araport:AT5G13290};
GN ORFNames=T31B5.110 {ECO:0000312|EMBL:CAB86636.1};
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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] (ISOFORMS 1 AND 2).
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND MUTAGENESIS OF GLY-74.
RX PubMed=12932329; DOI=10.1016/s0960-9822(03)00533-5;
RA Casamitjana-Martinez E., Hofhuis H.F., Xu J., Liu C.-M., Heidstra R.,
RA Scheres B.;
RT "Root-specific CLE19 overexpression and the sol1/2 suppressors implicate a
RT CLV-like pathway in the control of Arabidopsis root meristem maintenance.";
RL Curr. Biol. 13:1435-1441(2003).
RN [6]
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. La-0;
RX PubMed=14506206; DOI=10.1074/mcp.t300006-mcp200;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Large-scale analysis of in vivo phosphorylated membrane proteins by
RT immobilized metal ion affinity chromatography and mass spectrometry.";
RL Mol. Cell. Proteomics 2:1234-1243(2003).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=15308754; DOI=10.1105/tpc.104.023150;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Phosphoproteomics of the Arabidopsis plasma membrane and a new
RT phosphorylation site database.";
RL Plant Cell 16:2394-2405(2004).
RN [8]
RP FUNCTION, MUTAGENESIS OF GLY-70 AND ASP-263, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=18381924; DOI=10.1105/tpc.107.057547;
RA Mueller R., Bleckmann A., Simon R.;
RT "The receptor kinase CORYNE of Arabidopsis transmits the stem cell-limiting
RT signal CLAVATA3 independently of CLAVATA1.";
RL Plant Cell 20:934-946(2008).
RN [9]
RP FUNCTION, MUTAGENESIS OF GLY-74, AND TISSUE SPECIFICITY.
RX PubMed=18854335; DOI=10.1093/pcp/pcn148;
RA Miwa H., Betsuyaku S., Iwamoto K., Kinoshita A., Fukuda H., Sawa S.;
RT "The receptor-like kinase SOL2 mediates CLE signaling in Arabidopsis.";
RL Plant Cell Physiol. 49:1752-1757(2008).
RN [10]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH CLE PEPTIDES.
RX PubMed=20697738; DOI=10.1007/s00425-010-1236-4;
RA Meng L., Feldman L.J.;
RT "CLE14/CLE20 peptides may interact with CLAVATA2/CORYNE receptor-like
RT kinases to irreversibly inhibit cell division in the root meristem of
RT Arabidopsis.";
RL Planta 232:1061-1074(2010).
RN [11]
RP SUBCELLULAR LOCATION, SUBUNIT, AND INTERACTION WITH CLV1 AND CLV2.
RX PubMed=19843317; DOI=10.1111/j.1365-313x.2009.04049.x;
RA Zhu Y., Wang Y., Li R., Song X., Wang Q., Huang S., Jin J.B., Liu C.-M.,
RA Lin J.;
RT "Analysis of interactions among the CLAVATA3 receptors reveals a direct
RT interaction between CLAVATA2 and CORYNE in Arabidopsis.";
RL Plant J. 61:223-233(2010).
RN [12]
RP INTERACTION WITH CLV2.
RX PubMed=20626648; DOI=10.1111/j.1365-313x.2010.04295.x;
RA Guo Y., Han L., Hymes M., Denver R., Clark S.E.;
RT "CLAVATA2 forms a distinct CLE-binding receptor complex regulating
RT Arabidopsis stem cell specification.";
RL Plant J. 63:889-900(2010).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=19933383; DOI=10.1104/pp.109.149930;
RA Bleckmann A., Weidtkamp-Peters S., Seidel C.A.M., Simon R.;
RT "Stem cell signaling in Arabidopsis requires CRN to localize CLV2 to the
RT plasma membrane.";
RL Plant Physiol. 152:166-176(2010).
RN [14]
RP SUBUNIT.
RX PubMed=20220313; DOI=10.4161/psb.5.3.10790;
RA Zhu Y., Wan Y., Lin J.;
RT "Multiple receptor complexes assembled for transmitting CLV3 signaling in
RT Arabidopsis.";
RL Plant Signal. Behav. 5:300-302(2010).
RN [15]
RP SUBCELLULAR LOCATION.
RX PubMed=21051944; DOI=10.4161/psb.5.11.13359;
RA Guo Y., Clark S.E.;
RT "Membrane distributions of two ligand-binding receptor complexes in the
RT CLAVATA pathway.";
RL Plant Signal. Behav. 5:1442-1445(2010).
RN [16]
RP DISRUPTION PHENOTYPE.
RX PubMed=21705761; DOI=10.1534/genetics.111.130930;
RA Durbak A.R., Tax F.E.;
RT "CLAVATA signaling pathway receptors of Arabidopsis regulate cell
RT proliferation in fruit organ formation as well as in meristems.";
RL Genetics 189:177-194(2011).
RN [17]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=21265896; DOI=10.1111/j.1365-313x.2010.04433.x;
RA Replogle A., Wang J., Bleckmann A., Hussey R.S., Baum T.J., Sawa S.,
RA Davis E.L., Wang X., Simon R., Mitchum M.G.;
RT "Nematode CLE signaling in Arabidopsis requires CLAVATA2 and CORYNE.";
RL Plant J. 65:430-440(2011).
RN [18]
RP MUTAGENESIS OF GLY-70, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE,
RP INTERACTION WITH CLV2, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=27229734; DOI=10.1093/jxb/erw207;
RA Somssich M., Bleckmann A., Simon R.;
RT "Shared and distinct functions of the pseudokinase CORYNE (CRN) in shoot
RT and root stem cell maintenance of Arabidopsis.";
RL J. Exp. Bot. 67:4901-4915(2016).
RN [19]
RP DISRUPTION PHENOTYPE.
RX PubMed=26990325; DOI=10.1111/nph.13913;
RA Hanemian M., Barlet X., Sorin C., Yadeta K.A., Keller H., Favery B.,
RA Simon R., Thomma B.P., Hartmann C., Crespi M., Marco Y., Tremousaygue D.,
RA Deslandes L.;
RT "Arabidopsis CLAVATA1 and CLAVATA2 receptors contribute to Ralstonia
RT solanacearum pathogenicity through a miR169-dependent pathway.";
RL New Phytol. 211:502-515(2016).
RN [20]
RP FUNCTION.
RX PubMed=28586647; DOI=10.1016/j.devcel.2017.05.009;
RA Gutierrez-Alanis D., Yong-Villalobos L., Jimenez-Sandoval P.,
RA Alatorre-Cobos F., Oropeza-Aburto A., Mora-Macias J., Sanchez-Rodriguez F.,
RA Cruz-Ramirez A., Herrera-Estrella L.;
RT "Phosphate starvation-dependent iron mobilization induces CLE14 expression
RT to trigger root meristem differentiation through CLV2/PEPR2 signaling.";
RL Dev. Cell 41:555-570(2017).
RN [21]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP AND SUBUNIT.
RC STRAIN=cv. Columbia;
RX PubMed=28607033; DOI=10.15252/embr.201643535;
RA Hazak O., Brandt B., Cattaneo P., Santiago J., Rodriguez-Villalon A.,
RA Hothorn M., Hardtke C.S.;
RT "Perception of root-active CLE peptides requires CORYNE function in the
RT phloem vasculature.";
RL EMBO Rep. 18:1367-1381(2017).
CC -!- FUNCTION: Involved in the perception of CLV3 and CLV3-like (CLE)
CC peptides, that acts as a extracellular signals regulating meristems
CC maintenance. Modulates root, shoot and flower apical meristems
CC maintenance and floral organ development regulation, probably via
CC CLAVATA (CLV)-like pathways involving at least CLV3 and CLE19. In
CC complex with CLV2, perceives secreted CLV3-like effector proteins from
CC plant-parasitic cyst nematodes as ligand mimics of the plant CLE
CC signaling pathway (PubMed:21265896). This recognition is required for
CC proper feeding structure (syncytium) development and ultimately
CC successful nematode infection (PubMed:21265896). CLE14 perception by
CC CLV2/CRN complex triggers root meristem differentiation
CC (PubMed:20697738, PubMed:28586647). Required for the sensing of the
CC root CLE peptides (e.g. CLE8, CLE9/CLE10, CLE11, CLE13, CLE14, CLE16,
CC CLE17, CLE18, CLE20, CLE21, CLE25, CLE26, CLE40, CLE41/CLE44 and
CC CLE45), which involves also CLV2 and leads to root growth regulation,
CC mostly in the phloem and protophloem (PubMed:28607033). Promotes the
CC accumulation of BAM3, especially at later stages of protophloem
CC development (PubMed:28607033). {ECO:0000269|PubMed:12932329,
CC ECO:0000269|PubMed:18381924, ECO:0000269|PubMed:18854335,
CC ECO:0000269|PubMed:19933383, ECO:0000269|PubMed:20697738,
CC ECO:0000269|PubMed:21265896, ECO:0000269|PubMed:28586647,
CC ECO:0000269|PubMed:28607033}.
CC -!- SUBUNIT: Self-interacts. Parts of a tetrameric complex made of two
CC CLV2/CRN heterodimers that can interact with CLV3 and CLE peptides.
CC CLV2/CRN heterodimer interacts with CLV1 homodimers. Interacts with
CC CLV1 and CLV2 (PubMed:27229734). CLV2/CRN heterodimer can interact with
CC BAM3 (PubMed:28607033). {ECO:0000269|PubMed:19843317,
CC ECO:0000269|PubMed:19933383, ECO:0000269|PubMed:20220313,
CC ECO:0000269|PubMed:20626648, ECO:0000269|PubMed:20697738,
CC ECO:0000269|PubMed:27229734, ECO:0000269|PubMed:28607033}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14506206,
CC ECO:0000269|PubMed:15308754, ECO:0000269|PubMed:19843317,
CC ECO:0000269|PubMed:19933383, ECO:0000269|PubMed:21051944,
CC ECO:0000269|PubMed:27229734, ECO:0000269|PubMed:28607033}; Single-pass
CC type I membrane protein {ECO:0000269|PubMed:14506206,
CC ECO:0000269|PubMed:15308754, ECO:0000269|PubMed:19843317,
CC ECO:0000269|PubMed:19933383, ECO:0000269|PubMed:21051944}. Endoplasmic
CC reticulum membrane {ECO:0000269|PubMed:19933383,
CC ECO:0000269|PubMed:27229734, ECO:0000269|PubMed:28607033}; Single-pass
CC type I membrane protein {ECO:0000255}. Note=Requires CLV2 for export
CC from the endoplasmic reticulum and localization to the plasma membrane.
CC {ECO:0000269|PubMed:19933383, ECO:0000269|PubMed:27229734,
CC ECO:0000269|PubMed:28607033}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9LYU7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LYU7-2; Sequence=VSP_040147;
CC Name=3;
CC IsoId=Q9LYU7-3; Sequence=VSP_040147, VSP_040148, VSP_040149;
CC -!- TISSUE SPECIFICITY: Present in roots, stems, leaves, inflorescence,
CC flowers and siliques. Mostly expressed in shoot tips and, to a lesser
CC extent, in young organs and roots. Also expressed in the inner tissues
CC of the proximal root meristem (PubMed:21265896). Expressed in the
CC vascular cylinder of root tips, mostly in phloem poles
CC (PubMed:28607033). {ECO:0000269|PubMed:18381924,
CC ECO:0000269|PubMed:18854335, ECO:0000269|PubMed:21265896,
CC ECO:0000269|PubMed:28607033}.
CC -!- DEVELOPMENTAL STAGE: First observed in 16-cells stage embryo and
CC surrounding region. From early heart to early torpedo stage, confined
CC to the developing vasculature of the hypocotyl, cotyledons, and
CC developing root. Faint expression in the emerging shoot apical meristem
CC (SAM) at the torpedo stage. After germination, present in root, shoot
CC and inflorescence meristems, as well as in young flower primordia and
CC ovules (PubMed:18381924). In roots, detected in the stele, endodermis
CC basal and cortex cells, and at the end of the root meristem, comprising
CC the quiescent center, surrounding initials, and vascular precursors
CC (PubMed:18381924, PubMed:27229734). Also present in the vasculature of
CC primary and lateral roots, in the pericycle at sites of lateral root
CC initiation, in lateral root meristems, and in the vasculature of the
CC leaves. Accumulates in stamen and carpel primordia. Expressed in young
CC provascular tissue of floral organs and stem tissue (PubMed:18381924).
CC {ECO:0000269|PubMed:18381924, ECO:0000269|PubMed:27229734}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive.
CC -!- DISRUPTION PHENOTYPE: Insensitivity to root growth regulation by root
CC CLE peptides (e.g. CLE8, CLE9/CLE10, CLE11, CLE13, CLE14, CLE16, CLE17,
CC CLE18, CLE20, CLE21, CLE25, CLE26, CLE40, CLE41/CLE44 and CLE45)
CC (PubMed:28607033). Lower carpels production (PubMed:27229734). Impaired
CC interaction with CLV2 (PubMed:27229734). Reduced levels of BAM3,
CC especially at later stages of protophloem development
CC (PubMed:28607033). Ectopic fruit organ initiation after floral meristem
CC termination (PubMed:21705761). Enhanced resistance to nematode
CC infection (PubMed:21265896). Enhanced disease resistance response to
CC the bacterial pathogen Ralstonia solanacearum (PubMed:26990325).
CC {ECO:0000269|PubMed:21265896, ECO:0000269|PubMed:21705761,
CC ECO:0000269|PubMed:26990325, ECO:0000269|PubMed:27229734,
CC ECO:0000269|PubMed:28607033}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK228624; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BX829584; Type=Miscellaneous discrepancy; Note=Sequencing errors.; 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; AL163491; CAB86636.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91875.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91876.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91877.1; -; Genomic_DNA.
DR EMBL; BX832423; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BX829584; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK228624; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; T48576; T48576.
DR RefSeq; NP_001078577.1; NM_001085108.1. [Q9LYU7-3]
DR RefSeq; NP_196833.2; NM_121332.4. [Q9LYU7-2]
DR RefSeq; NP_850812.2; NM_180481.4. [Q9LYU7-1]
DR AlphaFoldDB; Q9LYU7; -.
DR SMR; Q9LYU7; -.
DR BioGRID; 16448; 5.
DR STRING; 3702.AT5G13290.2; -.
DR iPTMnet; Q9LYU7; -.
DR PaxDb; Q9LYU7; -.
DR PRIDE; Q9LYU7; -.
DR ProteomicsDB; 220310; -. [Q9LYU7-1]
DR EnsemblPlants; AT5G13290.1; AT5G13290.1; AT5G13290. [Q9LYU7-2]
DR EnsemblPlants; AT5G13290.2; AT5G13290.2; AT5G13290. [Q9LYU7-1]
DR EnsemblPlants; AT5G13290.3; AT5G13290.3; AT5G13290. [Q9LYU7-3]
DR GeneID; 831170; -.
DR Gramene; AT5G13290.1; AT5G13290.1; AT5G13290. [Q9LYU7-2]
DR Gramene; AT5G13290.2; AT5G13290.2; AT5G13290. [Q9LYU7-1]
DR Gramene; AT5G13290.3; AT5G13290.3; AT5G13290. [Q9LYU7-3]
DR KEGG; ath:AT5G13290; -.
DR Araport; AT5G13290; -.
DR TAIR; locus:2183906; AT5G13290.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_32_0_1; -.
DR InParanoid; Q9LYU7; -.
DR OMA; HMQQSGD; -.
DR OrthoDB; 780618at2759; -.
DR PhylomeDB; Q9LYU7; -.
DR PRO; PR:Q9LYU7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LYU7; baseline and differential.
DR Genevisible; Q9LYU7; AT.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0001653; F:peptide receptor activity; IMP: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:0004675; F:transmembrane receptor protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0042742; P:defense response to bacterium; IBA:GO_Central.
DR GO; GO:0002229; P:defense response to oomycetes; IBA:GO_Central.
DR GO; GO:0010078; P:maintenance of root meristem identity; IMP:UniProtKB.
DR GO; GO:0010088; P:phloem development; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0045595; P:regulation of cell differentiation; IMP:UniProtKB.
DR GO; GO:0009909; P:regulation of flower development; IMP:TAIR.
DR GO; GO:0010075; P:regulation of meristem growth; IDA:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR Pfam; PF00069; Pkinase; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell membrane; Endoplasmic reticulum;
KW Membrane; Nucleotide-binding; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..401
FT /note="Inactive leucine-rich repeat receptor-like protein
FT kinase CORYNE"
FT /id="PRO_0000401211"
FT TOPO_DOM 34..62
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 84..401
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 118..401
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 124..132
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 146
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 120..144
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_040147"
FT VAR_SEQ 300..331
FT /note="YTDKSDIFSFGMILGVLLTGRDPTHPFCEESA -> QKRHIQLWDDIGCSFN
FT RKRPDPPVLRRVCKRR (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_040148"
FT VAR_SEQ 332..401
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_040149"
FT MUTAGEN 70
FT /note="G->E: In crn-1; stem cell proliferation leading to
FT large meristems, and increased carpel number."
FT /evidence="ECO:0000269|PubMed:18381924,
FT ECO:0000269|PubMed:27229734"
FT MUTAGEN 74
FT /note="G->R: In sol2; stem cell proliferation leading to
FT large meristems, increased carpel number, and slightly
FT shorter roots. Suppress the short root phenotype of
FT transgenic plants constitutively overexpressing the CLE19
FT gene. Enhanced resistance to CLV3 peptide that inhibits
FT root growth."
FT /evidence="ECO:0000269|PubMed:12932329,
FT ECO:0000269|PubMed:18854335"
FT MUTAGEN 263
FT /note="D->N: In crn-2; increased carpel number."
FT /evidence="ECO:0000269|PubMed:18381924"
FT CONFLICT 393
FT /note="H -> N (in Ref. 3; BX832423)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 401 AA; 44527 MW; 5838AC6CB345B5CA CRC64;
MKQRRRRNGC SSSNTISLLL LFFLVFFSRT STSTSCRRRT VKHLSTTSTS STPLESRITS
KVIVISIVSG ILTGLVSALV LAFLVRSIVK FMKQTPILKG PVVFSPKITP KSLHAALSNG
IQLLGSDLNG KYYKMVLDNG LVVAVKRLGS LEGVGSPESS SSKSVKRRLQ KELELLAGLR
HRNLMSLRAY VRESDEFSLV YDYMPNGSLE DVMNKVRTKE VELGWEIRLR VAVGIVKGLQ
YLHFSCETQI LHYNLKPTNV MLDSEFEPRL ADCGLAKIMP SSHTAVSCYS APESSQSNRY
TDKSDIFSFG MILGVLLTGR DPTHPFCEES ASGGSLGQWL KHLQQSGEAR EALDKTILGE
EVEEDEMLMA LRITIICLSD FPADRPSSDE LVHMLTQLHS F
