CLE13_MEDTR
ID CLE13_MEDTR Reviewed; 84 AA.
AC G7JV15;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 1.
DT 25-MAY-2022, entry version 41.
DE RecName: Full=CLAVATA3/ESR (CLE)-related protein 13 {ECO:0000305};
DE Short=MtCLE13 {ECO:0000303|PubMed:20348212};
DE Contains:
DE RecName: Full=CLE13p {ECO:0000303|PubMed:20348212};
DE Flags: Precursor;
GN Name=CLE13 {ECO:0000303|PubMed:20348212};
GN OrderedLocusNames=MTR_4g079610 {ECO:0000312|EMBL:AES89755.1};
GN ORFNames=MtrunA17_Chr4g0040951 {ECO:0000312|EMBL:RHN61838.1};
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 [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 [2]
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 [3]
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 [4]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=20348212; DOI=10.1104/pp.110.153718;
RA Mortier V., Den Herder G., Whitford R., Van de Velde W., Rombauts S.,
RA D'Haeseleer K., Holsters M., Goormachtig S.;
RT "CLE peptides control Medicago truncatula nodulation locally and
RT systemically.";
RL Plant Physiol. 153:222-237(2010).
RN [5]
RP FUNCTION, INTERACTION WITH SUNN, AND INDUCTION.
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 [6]
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).
CC -!- FUNCTION: [CLE13p]: Signaling peptide involved in the regulation of
CC nodulation (PubMed:20348212). Moves from root to shoot to function with
CC the receptor kinase SUNN, in a signaling pathway that plays roles
CC during cellular differentiation, both at the onset of nodulation, and
CC later during nodule meristem development and subsequent homeostasis
CC (PubMed:20348212). Interacts with SUNN signaling to control nodule
CC numbers (PubMed:22168914). SUNN is 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 (Probable). {ECO:0000269|PubMed:20348212,
CC ECO:0000269|PubMed:22168914, ECO:0000305|PubMed:22168914}.
CC -!- SUBCELLULAR LOCATION: [CLE13p]: Secreted, extracellular space
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: [CLE13p]: Expressed in young nodules throughout the
CC central tissue (PubMed:20348212). Expressed in the apical region of
CC elongated nodules, corresponding to the meristematic and early
CC infection zones (PubMed:20348212). {ECO:0000269|PubMed:20348212}.
CC -!- INDUCTION: [CLE13p]: Induced in roots during nodulation triggered by
CC low nitrogen and infection with Sinorhizobium meliloti
CC (PubMed:20348212, PubMed:22168914). Induced in roots by treatment with
CC the cytokinin 6-benzylaminopurine (BAP) (PubMed:20348212,
CC PubMed:22168914). {ECO:0000269|PubMed:20348212,
CC ECO:0000269|PubMed:22168914}.
CC -!- PTM: [CLE13p]: The O-glycosylation (arabinosylation) of the
CC hydroxyproline Pro-72 enhances binding affinity of the CLE13p peptide
CC for its receptor. {ECO:0000250|UniProtKB:O49519}.
CC -!- MISCELLANEOUS: Overexpression of CL13 in roots almost abolishes nodule
CC formation when inoculated with Sinorhizobium species (PubMed:22168914,
CC PubMed:28592666). Roots of plants silencing CLE12 and CLE13 exhibit
CC increased number of nodules after infection with Sinorhizobium meliloti
CC (PubMed:22168914). {ECO:0000269|PubMed:22168914,
CC ECO:0000269|PubMed:28592666}.
CC -!- SIMILARITY: Belongs to the CLV3/ESR signal peptide family.
CC {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; CM001220; AES89755.1; -; Genomic_DNA.
DR EMBL; PSQE01000004; RHN61838.1; -; Genomic_DNA.
DR RefSeq; XP_003607558.1; XM_003607510.2.
DR AlphaFoldDB; G7JV15; -.
DR EnsemblPlants; AES89755; AES89755; MTR_4g079610.
DR Gramene; AES89755; AES89755; MTR_4g079610.
DR KEGG; mtr:MTR_4g079610; -.
DR HOGENOM; CLU_154904_0_0_1; -.
DR OMA; DPQHNGK; -.
DR OrthoDB; 1642840at2759; -.
DR Proteomes; UP000002051; Chromosome 4.
DR Proteomes; UP000265566; Chromosome 4.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0045168; P:cell-cell signaling involved in cell fate commitment; IEA:InterPro.
DR InterPro; IPR039617; CLAVATA3-CLE.
DR PANTHER; PTHR36016; PTHR36016; 1.
PE 1: Evidence at protein level;
KW Developmental protein; Differentiation; Glycoprotein; Hydroxylation;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..84
FT /note="CLAVATA3/ESR (CLE)-related protein 13"
FT /id="PRO_0000448634"
FT PEPTIDE 65..78
FT /note="CLE13p"
FT /id="PRO_0000448635"
FT REGION 57..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 69
FT /note="Hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:O49519"
FT MOD_RES 72
FT /note="Hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:O49519"
FT CARBOHYD 72
FT /note="O-linked (Ara...) hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:O49519"
SQ SEQUENCE 84 AA; 9625 MW; EAA3BEAAC3C96B8A CRC64;
MGRYTTDQVQ VYVLVIVLCT FFSTLQARSL RDHPLIHKNI DSRSLLQKLR IHISNHKQVR
DISGDRLSPA GPDPQHNGRS PPRK
