CLE9_ARATH
ID CLE9_ARATH Reviewed; 120 AA.
AC Q9FZE4; Q8LCX2;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=CLAVATA3/ESR (CLE)-related protein 9 {ECO:0000303|PubMed:16489133};
DE Contains:
DE RecName: Full=CLE9p {ECO:0000303|PubMed:16489133};
DE Flags: Precursor;
GN Name=CLE9 {ECO:0000303|PubMed:16489133};
GN OrderedLocusNames=At1g26600 {ECO:0000312|Araport:AT1G26600};
GN ORFNames=T1K7.3 {ECO:0000312|EMBL:AAF98585.1};
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;
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
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 SUBCELLULAR LOCATION, AND 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.
RX PubMed=16407446; DOI=10.1104/pp.105.072678;
RA Ni J., Clark S.E.;
RT "Evidence for functional conservation, sufficiency, and proteolytic
RT processing of the CLAVATA3 CLE domain.";
RL Plant Physiol. 140:726-733(2006).
RN [7]
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 [8]
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 [9]
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 [10]
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 [11]
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 [12]
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).
CC -!- FUNCTION: [CLE9p]: 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:16407446, ECO:0000269|PubMed:16489133,
CC ECO:0000269|PubMed:16902140, ECO:0000269|PubMed:28607033}.
CC -!- SUBCELLULAR LOCATION: [CLE9p]: Secreted, extracellular space
CC {ECO:0000269|PubMed:12602871}.
CC -!- TISSUE SPECIFICITY: [CLE9p]: Mostly expressed in leaves, flowers, stems
CC and apex, and, to a lower extent, in seedlings, roots, siliques and
CC pollen. {ECO:0000269|PubMed:12602871}.
CC -!- PTM: [CLE9p]: The O-glycosylation (arabinosylation) of the
CC hydroxyproline Pro-115 enhances binding affinity of the CLE9p 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=AAF98585.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC013427; AAF98585.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002684; AEE30708.1; -; Genomic_DNA.
DR EMBL; AY086355; AAM64423.1; -; mRNA.
DR PIR; B86393; B86393.
DR RefSeq; NP_564251.1; NM_102422.3.
DR PDB; 7OGU; X-ray; 2.87 A; CCC/FFF/III/LLL=109-120.
DR PDBsum; 7OGU; -.
DR AlphaFoldDB; Q9FZE4; -.
DR SMR; Q9FZE4; -.
DR STRING; 3702.AT1G26600.1; -.
DR PaxDb; Q9FZE4; -.
DR PRIDE; Q9FZE4; -.
DR EnsemblPlants; AT1G26600.1; AT1G26600.1; AT1G26600.
DR GeneID; 839200; -.
DR Gramene; AT1G26600.1; AT1G26600.1; AT1G26600.
DR KEGG; ath:AT1G26600; -.
DR Araport; AT1G26600; -.
DR TAIR; locus:2197905; AT1G26600.
DR eggNOG; ENOG502S9T8; Eukaryota.
DR HOGENOM; CLU_169217_0_0_1; -.
DR InParanoid; Q9FZE4; -.
DR OMA; CFFCVAF; -.
DR PhylomeDB; Q9FZE4; -.
DR PRO; PR:Q9FZE4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FZE4; baseline and differential.
DR Genevisible; Q9FZE4; AT.
DR GO; GO:0048046; C:apoplast; ISM:TAIR.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
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; PTHR34359; PTHR34359; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Developmental protein; Differentiation; Glycoprotein;
KW Hydroxylation; Reference proteome; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..120
FT /note="CLAVATA3/ESR (CLE)-related protein 9"
FT /id="PRO_0000401249"
FT PEPTIDE 109..120
FT /note="CLE9p"
FT /evidence="ECO:0000250|UniProtKB:O49519"
FT /id="PRO_0000401250"
FT REGION 85..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 112
FT /note="Hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:O49519"
FT MOD_RES 115
FT /note="Hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:O49519"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 115
FT /note="O-linked (Ara...) hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:O49519"
FT CONFLICT 94
FT /note="S -> F (in Ref. 3; AAM64423)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 120 AA; 13966 MW; F6486B55566E9452 CRC64;
MTMTHLNRLI LISLLFVSLL LKSSTASSTV VDEGNRTSRN FRYRTHRFVP RFNHHPYHVT
PHRSCDSFIR PYARSMCIEL QRIHRSSRKQ PLLSPPPPEI DPRYGVDKRL VPSGPNPLHN
