CLE44_ARATH
ID CLE44_ARATH Reviewed; 112 AA.
AC Q941C5; Q8LFN1;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=CLAVATA3/ESR (CLE)-related protein 44 {ECO:0000303|PubMed:16489133};
DE AltName: Full=Tracheary element differentiation inhibitory factor-like protein {ECO:0000303|PubMed:16902140};
DE Short=TDIF-like protein {ECO:0000303|PubMed:16902140};
DE Contains:
DE RecName: Full=CLE44p {ECO:0000303|PubMed:16489133};
DE Flags: Precursor;
GN Name=CLE44 {ECO:0000303|PubMed:16489133};
GN OrderedLocusNames=At4g13195 {ECO:0000312|Araport:AT4G13195};
GN ORFNames=F17N18 {ECO:0000312|EMBL:AL049751};
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 [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, AND GENE
RP FAMILY.
RC STRAIN=cv. Columbia;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
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 [6]
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 [7]
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 [8]
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 [9]
RP FUNCTION, MUTAGENESIS OF PRO-107, INTERACTION WITH TDR, TISSUE SPECIFICITY,
RP AND SUBCELLULAR LOCATION.
RX PubMed=18812507; DOI=10.1073/pnas.0808444105;
RA Hirakawa Y., Shinohara H., Kondo Y., Inoue A., Nakanomyo I., Ogawa M.,
RA Sawa S., Ohashi-Ito K., Matsubayashi Y., Fukuda H.;
RT "Non-cell-autonomous control of vascular stem cell fate by a CLE
RT peptide/receptor system.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:15208-15213(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 X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF 101-112 IN COMPLEX WITH SERK2 AND
RP TDR.
RX PubMed=27449136; DOI=10.1016/j.molp.2016.07.004;
RA Zhang H., Lin X., Han Z., Wang J., Qu L.-J., Chai J.;
RT "SERK family receptor-like kinases function as co-receptors with PXY for
RT plant vascular development.";
RL Mol. Plant 9:1406-1414(2016).
CC -!- FUNCTION: [CLE44p]: Extracellular signal peptide that regulates cell
CC fate. May act with TDR as a ligand-receptor pair in a signal
CC transduction pathway that represses tracheary element differentiation
CC but promotes the formation of procambial cells adjacent to phloem cells
CC in the veins. Regulates the transition of protophloem cells from
CC proliferation to differentiation, thus impinging on postembryonic
CC growth capacity of the root meristem; this signaling pathway requires
CC CRN and CLV2 (PubMed:28607033). {ECO:0000269|PubMed:16489133,
CC ECO:0000269|PubMed:16902140, ECO:0000269|PubMed:18812507,
CC ECO:0000269|PubMed:28607033}.
CC -!- SUBUNIT: [CLE44p]: Interacts specifically with the leucine-rich repeat
CC receptor-like protein kinase TDR, especially in the presence of SERK2.
CC {ECO:0000269|PubMed:18812507, ECO:0000269|PubMed:27449136}.
CC -!- SUBCELLULAR LOCATION: [CLE44p]: Secreted, extracellular space
CC {ECO:0000269|PubMed:18812507}. Note=Probably secreted from the phloem
CC cells and distributed in the procambial region.
CC {ECO:0000269|PubMed:18812507}.
CC -!- TISSUE SPECIFICITY: [CLE44p]: Mostly expressed in flowers and leaves.
CC Widely expressed along the vascular strands. In roots and hypocotyls,
CC present in endodermal cells as well as cells in the phloem and the
CC adjacent pericycle. {ECO:0000269|PubMed:16489133,
CC ECO:0000269|PubMed:18812507}.
CC -!- PTM: [CLE44p]: The O-glycosylation (arabinosylation) of the
CC hydroxyproline Pro-107 enhances binding affinity of the CLE44p peptide
CC for its receptor. {ECO:0000250|UniProtKB:O49519}.
CC -!- SIMILARITY: Belongs to the CLV3/ESR signal peptide family.
CC {ECO:0000305}.
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DR EMBL; AY618657; AAT36743.1; -; Genomic_DNA.
DR EMBL; AL049751; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL161535; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002687; AEE83243.1; -; Genomic_DNA.
DR EMBL; AY052261; AAK97731.1; -; mRNA.
DR EMBL; BT002641; AAO11557.1; -; mRNA.
DR EMBL; AY084742; AAM67243.1; -; mRNA.
DR RefSeq; NP_567397.1; NM_117389.3.
DR PDB; 2MIE; NMR; -; A=101-112.
DR PDB; 5GQR; X-ray; 3.50 A; C=101-112.
DR PDBsum; 2MIE; -.
DR PDBsum; 5GQR; -.
DR AlphaFoldDB; Q941C5; -.
DR SMR; Q941C5; -.
DR BioGRID; 12231; 1.
DR IntAct; Q941C5; 1.
DR STRING; 3702.AT4G13195.1; -.
DR PaxDb; Q941C5; -.
DR PRIDE; Q941C5; -.
DR EnsemblPlants; AT4G13195.1; AT4G13195.1; AT4G13195.
DR GeneID; 826934; -.
DR Gramene; AT4G13195.1; AT4G13195.1; AT4G13195.
DR KEGG; ath:AT4G13195; -.
DR Araport; AT4G13195; -.
DR TAIR; locus:505006439; AT4G13195.
DR eggNOG; ENOG502S9E3; Eukaryota.
DR HOGENOM; CLU_161000_0_0_1; -.
DR InParanoid; Q941C5; -.
DR OMA; MATTIDQ; -.
DR OrthoDB; 1527064at2759; -.
DR PhylomeDB; Q941C5; -.
DR PRO; PR:Q941C5; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q941C5; baseline and differential.
DR Genevisible; Q941C5; AT.
DR GO; GO:0048046; C:apoplast; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0033612; F:receptor serine/threonine kinase binding; IPI:UniProtKB.
DR GO; GO:0090506; P:axillary shoot meristem initiation; IDA:TAIR.
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:0010087; P:phloem or xylem histogenesis; IDA:TAIR.
DR GO; GO:0010067; P:procambium histogenesis; IDA:UniProtKB.
DR GO; GO:0045595; P:regulation of cell differentiation; IDA:UniProtKB.
DR GO; GO:0010089; P:xylem development; IDA:UniProtKB.
DR InterPro; IPR037495; CLE41/42/44.
DR PANTHER; PTHR35301; PTHR35301; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Developmental protein; Differentiation; Glycoprotein;
KW Hydroxylation; Reference proteome; Secreted; Signal.
FT SIGNAL 1..39
FT /evidence="ECO:0000255"
FT CHAIN 40..112
FT /note="CLAVATA3/ESR (CLE)-related protein 44"
FT /id="PRO_0000401287"
FT PEPTIDE 101..112
FT /note="CLE44p"
FT /evidence="ECO:0000250|UniProtKB:O49519"
FT /id="PRO_0000401288"
FT REGION 41..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 104
FT /note="Hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:O49519"
FT MOD_RES 107
FT /note="Hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:O49519"
FT CARBOHYD 107
FT /note="O-linked (Ara...) hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:O49519"
FT MUTAGEN 107
FT /note="P->A: Impaired repression of tracheary element
FT differentiation."
FT /evidence="ECO:0000269|PubMed:18812507"
FT CONFLICT 15..21
FT /note="FHQVIRL -> LHQLIRF (in Ref. 5; AAM67243)"
FT /evidence="ECO:0000305"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:2MIE"
SQ SEQUENCE 112 AA; 12522 MW; 3305B9C1155797BA CRC64;
MATTIDQTSI KSLHFHQVIR LIITIIFLAF LFLIGPTSSM NHHLHESSSK NTMAPSKRFL
LQPSTPSSST MKMRPTAHPR RSGTSSSSAR KRRREFRAEA HEVPSGPNPI SN
