ID SUNN_MEDTR Reviewed; 974 AA. AC G7JIK2; A0A396I6W1; Q4QVZ7; DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot. DT 11-DEC-2019, sequence version 2. DT 25-MAY-2022, entry version 59. DE RecName: Full=Leucine-rich repeat receptor-like kinase protein SUNN {ECO:0000305}; DE EC=2.7.11.1 {ECO:0000305}; DE AltName: Full=Protein SUPER NUMERIC NODULES {ECO:0000303|PubMed:16240175}; DE Flags: Precursor; GN Name=SUNN {ECO:0000303|PubMed:16240175}; GN OrderedLocusNames=MTR_4g070970 {ECO:0000312|EMBL:AES89185.1}; GN ORFNames=MtrunA17_Chr4g0035451 {ECO:0000312|EMBL:RHN61330.1}; OS Medicago truncatula (Barrel medic) (Medicago tribuloides). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade; OC NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago. OX NCBI_TaxID=3880; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, DISRUPTION RP PHENOTYPE, AND MUTAGENESIS OF SER-575 AND ARG-950. RX PubMed=16240175; DOI=10.1007/s11103-005-8102-y; RA Schnabel E., Journet E.P., de Carvalho-Niebel F., Duc G., Frugoli J.; RT "The Medicago truncatula SUNN gene encodes a CLV1-like leucine-rich repeat RT receptor kinase that regulates nodule number and root length."; RL Plant Mol. Biol. 58:809-822(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Jemalong A17; RX PubMed=22089132; DOI=10.1038/nature10625; RA Young N.D., Debelle F., Oldroyd G.E.D., Geurts R., Cannon S.B., RA Udvardi M.K., Benedito V.A., Mayer K.F.X., Gouzy J., Schoof H., RA Van de Peer Y., Proost S., Cook D.R., Meyers B.C., Spannagl M., Cheung F., RA De Mita S., Krishnakumar V., Gundlach H., Zhou S., Mudge J., Bharti A.K., RA Murray J.D., Naoumkina M.A., Rosen B., Silverstein K.A.T., Tang H., RA Rombauts S., Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M., RA Bellec A., Berger A., Berges H., Bidwell S., Bisseling T., Choisne N., RA Couloux A., Denny R., Deshpande S., Dai X., Doyle J.J., Dudez A.-M., RA Farmer A.D., Fouteau S., Franken C., Gibelin C., Gish J., Goldstein S., RA Gonzalez A.J., Green P.J., Hallab A., Hartog M., Hua A., Humphray S.J., RA Jeong D.-H., Jing Y., Jocker A., Kenton S.M., Kim D.-J., Klee K., Lai H., RA Lang C., Lin S., Macmil S.L., Magdelenat G., Matthews L., McCorrison J., RA Monaghan E.L., Mun J.-H., Najar F.Z., Nicholson C., Noirot C., RA O'Bleness M., Paule C.R., Poulain J., Prion F., Qin B., Qu C., Retzel E.F., RA Riddle C., Sallet E., Samain S., Samson N., Sanders I., Saurat O., RA Scarpelli C., Schiex T., Segurens B., Severin A.J., Sherrier D.J., Shi R., RA Sims S., Singer S.R., Sinharoy S., Sterck L., Viollet A., Wang B.-B., RA Wang K., Wang M., Wang X., Warfsmann J., Weissenbach J., White D.D., RA White J.D., Wiley G.B., Wincker P., Xing Y., Yang L., Yao Z., Ying F., RA Zhai J., Zhou L., Zuber A., Denarie J., Dixon R.A., May G.D., RA Schwartz D.C., Rogers J., Quetier F., Town C.D., Roe B.A.; RT "The Medicago genome provides insight into the evolution of rhizobial RT symbioses."; RL Nature 480:520-524(2011). RN [3] RP GENOME REANNOTATION. RC STRAIN=cv. Jemalong A17; RX PubMed=24767513; DOI=10.1186/1471-2164-15-312; RA Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S., RA Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F., RA Schwartz D.C., Town C.D.; RT "An improved genome release (version Mt4.0) for the model legume Medicago RT truncatula."; RL BMC Genomics 15:312-312(2014). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Jemalong A17; RX PubMed=30397259; DOI=10.1038/s41477-018-0286-7; RA Pecrix Y., Staton S.E., Sallet E., Lelandais-Briere C., Moreau S., RA Carrere S., Blein T., Jardinaud M.F., Latrasse D., Zouine M., Zahm M., RA Kreplak J., Mayjonade B., Satge C., Perez M., Cauet S., Marande W., RA Chantry-Darmon C., Lopez-Roques C., Bouchez O., Berard A., Debelle F., RA Munos S., Bendahmane A., Berges H., Niebel A., Buitink J., Frugier F., RA Benhamed M., Crespi M., Gouzy J., Gamas P.; RT "Whole-genome landscape of Medicago truncatula symbiotic genes."; RL Nat. Plants 4:1017-1025(2018). RN [5] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=16941903; DOI=10.1094/mpmi-19-0988; RA Amiour N., Recorbet G., Robert F., Gianinazzi S., Dumas-Gaudot E.; RT "Mutations in DMI3 and SUNN modify the appressorium-responsive root RT proteome in arbuscular mycorrhiza."; RL Mol. Plant Microbe Interact. 19:988-997(2006). RN [6] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=22168914; DOI=10.1111/j.1365-313x.2011.04881.x; RA Mortier V., De Wever E., Vuylsteke M., Holsters M., Goormachtig S.; RT "Nodule numbers are governed by interaction between CLE peptides and RT cytokinin signaling."; RL Plant J. 70:367-376(2012). RN [7] RP FUNCTION. RX PubMed=22399647; DOI=10.1104/pp.112.194993; RA Jin J., Watt M., Mathesius U.; RT "The autoregulation gene SUNN mediates changes in root organ formation in RT response to nitrogen through alteration of shoot-to-root auxin transport."; RL Plant Physiol. 159:489-500(2012). RN [8] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=22301956; DOI=10.4161/psb.7.1.18491; RA Schnabel E., Karve A., Kassaw T., Mukherjee A., Zhou X., Hall T., RA Frugoli J.; RT "The M. truncatula SUNN gene is expressed in vascular tissue, similarly to RT RDN1, consistent with the role of these nodulation regulation genes in long RT distance signaling."; RL Plant Signal. Behav. 7:4-6(2012). RN [9] RP FUNCTION. RX PubMed=27135324; DOI=10.3390/plants4020209; RA Kassaw T., Bridges W. Jr., Frugoli J.; RT "Multiple Autoregulation of Nodulation (AON) signals identified through RT split root analysis of Medicago truncatula sunn and rdn1 mutants."; RL Plants (Basel) 4:209-224(2015). RN [10] RP FUNCTION. RX PubMed=28592666; DOI=10.1104/pp.17.00278; RA Kassaw T., Nowak S., Schnabel E., Frugoli J.; RT "ROOT DETERMINED NODULATION1 is required for M. truncatula CLE12, but not RT CLE13, peptide signaling through the SUNN receptor kinase."; RL Plant Physiol. 174:2445-2456(2017). RN [11] RP FUNCTION. RX PubMed=31477892; DOI=10.1038/s41477-019-0501-1; RA Mueller L.M., Flokova K., Schnabel E., Sun X., Fei Z., Frugoli J., RA Bouwmeester H.J., Harrison M.J.; RT "A CLE-SUNN module regulates strigolactone content and fungal colonization RT in arbuscular mycorrhiza."; RL Nat. Plants 5:933-939(2019). CC -!- FUNCTION: LRR receptor kinase involved in the regulation of root growth CC and root nodule organogenesis (PubMed:16240175, PubMed:16941903, CC PubMed:22399647). Involved in long distance nodulation signaling events CC (PubMed:22399647) (Probable). Involved in the autoregulation of CC nodulation (AON), a long distance systemic signaling from root to shoot CC and back again, which allows legumes to limit the number of root CC nodules formed based on available nitrogen and previous rhizobial CC colonization (PubMed:27135324) (Probable). Acts from shoot to root to CC control AON (PubMed:27135324, PubMed:28592666). Interacts with CLE12 CC and CLE13 signaling to control nodule numbers (PubMed:22168914). CC Required for the modulation of shoot-to-root auxin transport in CC response to altered nitrogen tissue concentrations and in the absence CC of rhizobia (PubMed:22399647). Shoot-to-root auxin transport influences CC lateral root density and length (PubMed:22399647). Involved in the CC regulation of root colonization by arbuscular mycorrhizal (AM) fungi CC (PubMed:16941903, PubMed:31477892). Interacts with CLE33 and CL53 CC signaling to repress strigolactone biosynthetic genes and strigolactone CC content in the roots, and consequently reduces the promotion of further CC colonization by AM fungi (PubMed:31477892). CC {ECO:0000269|PubMed:16240175, ECO:0000269|PubMed:16941903, CC ECO:0000269|PubMed:22168914, ECO:0000269|PubMed:22399647, CC ECO:0000269|PubMed:27135324, ECO:0000269|PubMed:28592666, CC ECO:0000269|PubMed:31477892, ECO:0000305|PubMed:22168914, CC ECO:0000305|PubMed:22301956}. 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 Evidence={ECO:0000305}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990; CC Evidence={ECO:0000305}; 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; Evidence={ECO:0000305}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609; CC Evidence={ECO:0000305}; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I CC membrane protein {ECO:0000305}. CC -!- TISSUE SPECIFICITY: Expressed in roots and shoots (PubMed:16240175). CC Expressed in the vasculature of leaves, petioles, stems and roots CC (PubMed:22301956). {ECO:0000269|PubMed:16240175, CC ECO:0000269|PubMed:22301956}. CC -!- DISRUPTION PHENOTYPE: Dramatic increase in root nodule number when CC inoculated with Sinorhizobium meliloti (PubMed:16240175, CC PubMed:16941903, PubMed:22168914). Inhibition of root growth in both CC the presence and absence of rhizobia (PubMed:16240175). Increase in CC arbuscular mycorrhizal (AM) fungus colonization intensity in roots CC (hypermycorrhizal phenotype) when inoculated with AM fungi CC (PubMed:16941903). {ECO:0000269|PubMed:16240175, CC ECO:0000269|PubMed:16941903, ECO:0000269|PubMed:22168914}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}. CC -!- SEQUENCE CAUTION: CC Sequence=AES89185.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=RHN61330.1; 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; AY769943; AAW71475.1; -; Genomic_DNA. DR EMBL; CM001220; AES89185.1; ALT_INIT; Genomic_DNA. DR EMBL; PSQE01000004; RHN61330.1; ALT_SEQ; Genomic_DNA. DR RefSeq; XP_003606988.1; XM_003606940.2. DR AlphaFoldDB; G7JIK2; -. DR SMR; G7JIK2; -. DR STRING; 3880.AES89185; -. DR EnsemblPlants; AES89185; AES89185; MTR_4g070970. DR GeneID; 11439632; -. DR Gramene; AES89185; AES89185; MTR_4g070970. DR KEGG; mtr:MTR_4g070970; -. DR eggNOG; ENOG502QQ4T; Eukaryota. DR HOGENOM; CLU_000288_22_1_1; -. DR OrthoDB; 826997at2759; -. DR Proteomes; UP000002051; Chromosome 4. DR Proteomes; UP000265566; Chromosome 4. DR ExpressionAtlas; G7JIK2; differential. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. 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:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:RHEA. DR GO; GO:0033612; F:receptor serine/threonine kinase binding; IBA:GO_Central. DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW. DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW. DR Gene3D; 3.80.10.10; -; 4. 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 Pfam; PF00560; LRR_1; 1. DR Pfam; PF13516; LRR_6; 1. DR Pfam; PF13855; LRR_8; 1. DR Pfam; PF08263; LRRNT_2; 1. DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1. DR SMART; SM00369; LRR_TYP; 7. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; SSF56112; 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; Differentiation; Glycoprotein; KW Growth regulation; Kinase; Leucine-rich repeat; Membrane; KW Nucleotide-binding; Receptor; Reference proteome; Repeat; KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane; KW Transmembrane helix. FT SIGNAL 1..20 FT /evidence="ECO:0000255" FT CHAIN 21..974 FT /note="Leucine-rich repeat receptor-like kinase protein FT SUNN" FT /evidence="ECO:0000255" FT /id="PRO_0000448628" FT TRANSMEM 635..655 FT /note="Helical" FT /evidence="ECO:0000255" FT REPEAT 92..116 FT /note="LRR 1" FT /evidence="ECO:0000255" FT REPEAT 117..141 FT /note="LRR 2" FT /evidence="ECO:0000255" FT REPEAT 143..165 FT /note="LRR 3" FT /evidence="ECO:0000255" FT REPEAT 166..188 FT /note="LRR 4" FT /evidence="ECO:0000255" FT REPEAT 189..213 FT /note="LRR 5" FT /evidence="ECO:0000255" FT REPEAT 238..262 FT /note="LRR 6" FT /evidence="ECO:0000255" FT REPEAT 263..286 FT /note="LRR 7" FT /evidence="ECO:0000255" FT REPEAT 288..309 FT /note="LRR 8" FT /evidence="ECO:0000255" FT REPEAT 310..334 FT /note="LRR 9" FT /evidence="ECO:0000255" FT REPEAT 335..358 FT /note="LRR 10" FT /evidence="ECO:0000255" FT REPEAT 360..382 FT /note="LRR 11" FT /evidence="ECO:0000255" FT REPEAT 383..406 FT /note="LRR 12" FT /evidence="ECO:0000255" FT REPEAT 407..430 FT /note="LRR 13" FT /evidence="ECO:0000255" FT REPEAT 431..454 FT /note="LRR 14" FT /evidence="ECO:0000255" FT REPEAT 456..477 FT /note="LRR 15" FT /evidence="ECO:0000255" FT REPEAT 478..501 FT /note="LRR 16" FT /evidence="ECO:0000255" FT REPEAT 503..525 FT /note="LRR 17" FT /evidence="ECO:0000255" FT REPEAT 527..549 FT /note="LRR 18" FT /evidence="ECO:0000255" FT REPEAT 550..573 FT /note="LRR 19" FT /evidence="ECO:0000255" FT REPEAT 574..598 FT /note="LRR 20" FT /evidence="ECO:0000255" FT DOMAIN 685..972 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT NP_BIND 691..699 FT /note="ATP" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT ACT_SITE 810 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 713 FT /note="ATP" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT CARBOHYD 75 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 104 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 123 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 136 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 250 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 274 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 312 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 346 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 508 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 513 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 556 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 585 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT MUTAGEN 575 FT /note="S->R: In sunn-2; dramatic increase in root nodule FT number when infected by Sinorhizobium meliloti, and FT inhibition of root growth in both the presence and absence FT of rhizobia." FT /evidence="ECO:0000269|PubMed:16240175" FT MUTAGEN 950 FT /note="R->K: In sunn-1; dramatic increase in root nodule FT number when infected by Sinorhizobium meliloti, and FT inhibition of root growth in both the presence and absence FT of rhizobia." FT /evidence="ECO:0000269|PubMed:16240175" SQ SEQUENCE 974 AA; 107808 MW; 315BF83DFB7AE2A7 CRC64; MKNITCYLLL LCMLFTTCYS LNNDLDALLK LKKSMKGEKA KDDALKDWKF STSASAHCSF SGVKCDEDQR VIALNVTQVP LFGHLSKEIG ELNMLESLTI TMDNLTGELP TELSKLTSLR ILNISHNLFS GNFPGNITFG MKKLEALDAY DNNFEGPLPE EIVSLMKLKY LSFAGNFFSG TIPESYSEFQ KLEILRLNYN SLTGKIPKSL SKLKMLKELQ LGYENAYSGG IPPELGSIKS LRYLEISNAN LTGEIPPSLG NLENLDSLFL QMNNLTGTIP PELSSMRSLM SLDLSINGLS GEIPETFSKL KNLTLINFFQ NKLRGSIPAF IGDLPNLETL QVWENNFSFV LPQNLGSNGK FIYFDVTKNH LTGLIPPELC KSKKLKTFIV TDNFFRGPIP NGIGPCKSLE KIRVANNYLD GPVPPGIFQL PSVQIIELGN NRFNGQLPTE ISGNSLGNLA LSNNLFTGRI PASMKNLRSL QTLLLDANQF LGEIPAEVFA LPVLTRINIS GNNLTGGIPK TVTQCSSLTA VDFSRNMLTG EVPKGMKNLK VLSIFNVSHN SISGKIPDEI RFMTSLTTLD LSYNNFTGIV PTGGQFLVFN DRSFAGNPSL CFPHQTTCSS LLYRSRKSHA KEKAVVIAIV FATAVLMVIV TLHMMRKRKR HMAKAWKLTA FQKLEFRAEE VVECLKEENI IGKGGAGIVY RGSMANGTDV AIKRLVGQGS GRNDYGFKAE IETLGRIRHR NIMRLLGYVS NKDTNLLLYE YMPNGSLGEW LHGAKGCHLS WEMRYKIAVE AAKGLCYLHH DCSPLIIHRD VKSNNILLDA DFEAHVADFG LAKFLYDPGA SQSMSSIAGS YGYIAPEYAY TLKVDEKSDV YSFGVVLLEL IIGRKPVGEF GDGVDIVGWI NKTELELYQP SDKALVSAVV DPRLNGYPLT SVIYMFNIAM MCVKEMGPAR PTMREVVHML TNPPHSTSHN LINL //