CLE12_ARATH
ID CLE12_ARATH Reviewed; 118 AA.
AC Q29PU4; Q8LBM7;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=CLAVATA3/ESR (CLE)-related protein 12 {ECO:0000303|PubMed:18034320};
DE Contains:
DE RecName: Full=CLE12p {ECO:0000303|PubMed:18034320};
DE Flags: Precursor;
GN Name=CLE12 {ECO:0000303|PubMed:18034320};
GN OrderedLocusNames=At1g68795 {ECO:0000312|Araport:AT1G68795};
GN ORFNames=F14K14 {ECO:0000312|EMBL:AC011914};
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 Kim C.J., Chen H., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
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 [6]
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 [7]
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 [8]
RP 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 [9]
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 [10]
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 [11]
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 [12]
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).
CC -!- FUNCTION: [CLE12p]: Extracellular signal peptide that regulates cell
CC fate. Represses root apical meristem maintenance.
CC {ECO:0000269|PubMed:16407446, ECO:0000269|PubMed:16902140}.
CC -!- SUBCELLULAR LOCATION: [CLE12p]: Secreted, extracellular space
CC {ECO:0000250|UniProtKB:O49519}.
CC -!- TISSUE SPECIFICITY: [CLE12p]: Mostly expressed in seedlings, roots,
CC flowers, stems and apex, and, to a lower extent, in leaves and
CC siliques. {ECO:0000269|PubMed:12602871}.
CC -!- PTM: [CLE12p]: The O-glycosylation (arabinosylation) of the
CC hydroxyproline Pro-113 enhances binding affinity of the CLE12p 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=AAM64673.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC011914; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002684; AEE34840.1; -; Genomic_DNA.
DR EMBL; BT024812; ABD60695.1; -; mRNA.
DR EMBL; AY087115; AAM64673.1; ALT_INIT; mRNA.
DR RefSeq; NP_564943.1; NM_105553.3.
DR AlphaFoldDB; Q29PU4; -.
DR STRING; 3702.AT1G68795.1; -.
DR iPTMnet; Q29PU4; -.
DR PaxDb; Q29PU4; -.
DR PRIDE; Q29PU4; -.
DR ProteomicsDB; 246537; -.
DR EnsemblPlants; AT1G68795.1; AT1G68795.1; AT1G68795.
DR GeneID; 843211; -.
DR Gramene; AT1G68795.1; AT1G68795.1; AT1G68795.
DR KEGG; ath:AT1G68795; -.
DR Araport; AT1G68795; -.
DR TAIR; locus:505006210; AT1G68795.
DR eggNOG; ENOG502S8TY; Eukaryota.
DR HOGENOM; CLU_145048_0_0_1; -.
DR InParanoid; Q29PU4; -.
DR OMA; FDFTPFH; -.
DR OrthoDB; 1527625at2759; -.
DR PhylomeDB; Q29PU4; -.
DR PRO; PR:Q29PU4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q29PU4; baseline and differential.
DR Genevisible; Q29PU4; 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 InterPro; IPR039618; CLE9/10/11/12/13.
DR PANTHER; PTHR34359; PTHR34359; 1.
PE 2: Evidence at transcript level;
KW Developmental protein; Differentiation; Glycoprotein; Hydroxylation;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..118
FT /note="CLAVATA3/ESR (CLE)-related protein 12"
FT /id="PRO_0000401255"
FT PEPTIDE 107..118
FT /note="CLE12p"
FT /evidence="ECO:0000250|UniProtKB:O49519"
FT /id="PRO_0000401256"
FT REGION 75..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 110
FT /note="Hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:O49519"
FT MOD_RES 113
FT /note="Hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:O49519"
FT CARBOHYD 113
FT /note="O-linked (Ara...) hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:O49519"
SQ SEQUENCE 118 AA; 14044 MW; 0AB03EBB6A9F8999 CRC64;
MLRISSSSSM ALKFSQILFI VLWLSLFFLL LHHLYSLNFR RLYSLNAVEP SLLKQHYRSY
RLVSRKVLSD RFDFTPFHSR DNSRHNHRSG EQYDGDEIDP RYGVEKRRVP SGPNPLHH
