CLE10_ARATH
ID CLE10_ARATH Reviewed; 107 AA.
AC Q4PSX1; Q9C984;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=CLAVATA3/ESR (CLE)-related protein 10 {ECO:0000303|PubMed:16489133};
DE Contains:
DE RecName: Full=CLE10p {ECO:0000303|PubMed:16489133};
DE Flags: Precursor;
GN Name=CLE10 {ECO:0000303|PubMed:16489133};
GN OrderedLocusNames=At1g69320 {ECO:0000312|Araport:AT1G69320};
GN ORFNames=F23O10.10 {ECO:0000312|EMBL:AAG52495.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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].
RC STRAIN=cv. Columbia;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [4]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11457943; DOI=10.1104/pp.126.3.939;
RA Cock J.M., McCormick S.;
RT "A large family of genes that share homology with CLAVATA3.";
RL Plant Physiol. 126:939-942(2001).
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=12602871; DOI=10.1023/a:1022038932376;
RA Sharma V.K., Ramirez J., Fletcher J.C.;
RT "The Arabidopsis CLV3-like (CLE) genes are expressed in diverse tissues and
RT encode secreted proteins.";
RL Plant Mol. Biol. 51:415-425(2003).
RN [6]
RP FUNCTION, AND GENE FAMILY.
RX PubMed=16489133; DOI=10.1104/pp.105.075515;
RA Strabala T.J., O'donnell P.J., Smit A.-M., Ampomah-Dwamena C., Martin E.J.,
RA Netzler N., Nieuwenhuizen N.J., Quinn B.D., Foote H.C.C., Hudson K.R.;
RT "Gain-of-function phenotypes of many CLAVATA3/ESR genes, including four new
RT family members, correlate with tandem variations in the conserved
RT CLAVATA3/ESR domain.";
RL Plant Physiol. 140:1331-1344(2006).
RN [7]
RP FUNCTION.
RX PubMed=16902140; DOI=10.1126/science.1128436;
RA Ito Y., Nakanomyo I., Motose H., Iwamoto K., Sawa S., Dohmae N., Fukuda H.;
RT "Dodeca-CLE peptides as suppressors of plant stem cell differentiation.";
RL Science 313:842-845(2006).
RN [8]
RP REVIEW.
RX PubMed=18034320; DOI=10.1007/s00018-007-7411-5;
RA Jun J.H., Fiume E., Fletcher J.C.;
RT "The CLE family of plant polypeptide signaling molecules.";
RL Cell. Mol. Life Sci. 65:743-755(2008).
RN [9]
RP REVIEW.
RX PubMed=18078779; DOI=10.1016/j.pbi.2007.10.010;
RA Mitchum M.G., Wang X., Davis E.L.;
RT "Diverse and conserved roles of CLE peptides.";
RL Curr. Opin. Plant Biol. 11:75-81(2008).
RN [10]
RP REVIEW.
RX PubMed=20016993; DOI=10.1007/s00709-009-0095-y;
RA Wang G., Fiers M.;
RT "CLE peptide signaling during plant development.";
RL Protoplasma 240:33-43(2010).
RN [11]
RP FUNCTION.
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).
RN [12]
RP STRUCTURE BY NMR OF 96-107.
RA DiGennaro P.M., Bobay B.G., Bird D.M.;
RT "Inferring function of CLE peptides from high resolution tertiary
RT structures.";
RL Submitted (DEC-2013) to the PDB data bank.
CC -!- FUNCTION: [CLE10p]: Extracellular signal peptide that regulates cell
CC fate. Represses root apical meristem maintenance. Regulates the
CC transition of protophloem cells from proliferation to differentiation,
CC thus impinging on postembryonic growth capacity of the root meristem;
CC this signaling pathway requires CRN and CLV2 (PubMed:28607033).
CC {ECO:0000269|PubMed:16489133, ECO:0000269|PubMed:16902140,
CC ECO:0000269|PubMed:28607033}.
CC -!- SUBCELLULAR LOCATION: [CLE10p]: Secreted, extracellular space
CC {ECO:0000250|UniProtKB:O49519}.
CC -!- TISSUE SPECIFICITY: [CLE10p]: Expressed in stems, apex, leaves,
CC flowers, siliques and pollen. {ECO:0000269|PubMed:12602871}.
CC -!- PTM: [CLE10p]: The O-glycosylation (arabinosylation) of the
CC hydroxyproline Pro-102 enhances binding affinity of the CLE10p peptide
CC for its receptor. {ECO:0000250|UniProtKB:O49519}.
CC -!- SIMILARITY: Belongs to the CLV3/ESR signal peptide family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG52495.1; 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; AC018364; AAG52495.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE34910.1; -; Genomic_DNA.
DR EMBL; DQ056515; AAY78671.1; -; mRNA.
DR RefSeq; NP_564958.2; NM_105599.3.
DR PDB; 2MID; NMR; -; A=96-107.
DR PDBsum; 2MID; -.
DR AlphaFoldDB; Q4PSX1; -.
DR SMR; Q4PSX1; -.
DR STRING; 3702.AT1G69320.1; -.
DR PaxDb; Q4PSX1; -.
DR PRIDE; Q4PSX1; -.
DR EnsemblPlants; AT1G69320.1; AT1G69320.1; AT1G69320.
DR GeneID; 843263; -.
DR Gramene; AT1G69320.1; AT1G69320.1; AT1G69320.
DR KEGG; ath:AT1G69320; -.
DR Araport; AT1G69320; -.
DR TAIR; locus:2007091; AT1G69320.
DR eggNOG; ENOG502S9T8; Eukaryota.
DR HOGENOM; CLU_169217_0_0_1; -.
DR InParanoid; Q4PSX1; -.
DR OMA; PKVQHAY; -.
DR OrthoDB; 1611145at2759; -.
DR PhylomeDB; Q4PSX1; -.
DR PRO; PR:Q4PSX1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q4PSX1; baseline and differential.
DR Genevisible; Q4PSX1; AT.
DR GO; GO:0048046; C:apoplast; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0033612; F:receptor serine/threonine kinase binding; ISS:UniProtKB.
DR GO; GO:0045168; P:cell-cell signaling involved in cell fate commitment; ISS:UniProtKB.
DR GO; GO:0010078; P:maintenance of root meristem identity; IDA:UniProtKB.
DR GO; GO:0010088; P:phloem development; IDA:UniProtKB.
DR GO; GO:0045595; P:regulation of cell differentiation; IDA:UniProtKB.
DR InterPro; IPR039618; CLE9/10/11/12/13.
DR PANTHER; PTHR31471:SF64; PTHR31471:SF64; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Developmental protein; Differentiation; Glycoprotein;
KW Hydroxylation; Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..107
FT /note="CLAVATA3/ESR (CLE)-related protein 10"
FT /id="PRO_0000401251"
FT PEPTIDE 96..107
FT /note="CLE10p"
FT /evidence="ECO:0000250|UniProtKB:O49519"
FT /id="PRO_0000401252"
FT REGION 73..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 99
FT /note="Hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:O49519"
FT MOD_RES 102
FT /note="Hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:O49519"
FT CARBOHYD 27
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 102
FT /note="O-linked (Ara...) hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:O49519"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:2MID"
SQ SEQUENCE 107 AA; 12553 MW; 05D3594FDA22F96E CRC64;
MKTNRNRPIN ILIVFFLLTT ARAATRNWTN RTHRTVPKVQ HAYYAYPHRS CESFSRPYAR
SMCIELERIH RSSRQPLFSP PPPPTEIDQR YGVEKRLVPS GPNPLHN
