BAME3_ARATH
ID BAME3_ARATH Reviewed; 992 AA.
AC O65440; C0LGQ6;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 3.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Leucine-rich repeat receptor-like serine/threonine-protein kinase BAM3 {ECO:0000303|PubMed:16367950};
DE EC=2.7.11.1 {ECO:0000255|PROSITE-ProRule:PRU00159};
DE AltName: Full=Protein BARELY ANY MERISTEM 3 {ECO:0000303|PubMed:16367950};
DE Flags: Precursor;
GN Name=BAM3 {ECO:0000303|PubMed:16367950};
GN OrderedLocusNames=At4g20270 {ECO:0000312|Araport:AT4G20270};
GN ORFNames=F1C12.190 {ECO:0000312|EMBL:CAA18252.1};
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=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 [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] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=20064227; DOI=10.1186/1471-2164-11-19;
RA Gou X., He K., Yang H., Yuan T., Lin H., Clouse S.D., Li J.;
RT "Genome-wide cloning and sequence analysis of leucine-rich repeat receptor-
RT like protein kinase genes in Arabidopsis thaliana.";
RL BMC Genomics 11:19-19(2010).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=16367950; DOI=10.1111/j.1365-313x.2005.02592.x;
RA DeYoung B.J., Bickle K.L., Schrage K.J., Muskett P., Patel K., Clark S.E.;
RT "The CLAVATA1-related BAM1, BAM2 and BAM3 receptor kinase-like proteins are
RT required for meristem function in Arabidopsis.";
RL Plant J. 45:1-16(2006).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY,
RP AND INDUCTION BY CLE45.
RC STRAIN=cv. Columbia;
RX PubMed=23569225; DOI=10.1073/pnas.1222314110;
RA Depuydt S., Rodriguez-Villalon A., Santuari L., Wyser-Rmili C., Ragni L.,
RA Hardtke C.S.;
RT "Suppression of Arabidopsis protophloem differentiation and root meristem
RT growth by CLE45 requires the receptor-like kinase BAM3.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:7074-7079(2013).
RN [7]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=25049386; DOI=10.1073/pnas.1407337111;
RA Rodriguez-Villalon A., Gujas B., Kang Y.H., Breda A.S., Cattaneo P.,
RA Depuydt S., Hardtke C.S.;
RT "Molecular genetic framework for protophloem formation.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:11551-11556(2014).
RN [8]
RP FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=27354416; DOI=10.15252/embr.201642450;
RA Kang Y.H., Hardtke C.S.;
RT "Arabidopsis MAKR5 is a positive effector of BAM3-dependent CLE45
RT signaling.";
RL EMBO Rep. 17:1145-1154(2016).
RN [9]
RP FUNCTION, MUTAGENESIS OF THR-150; 226-GLN--TYR-231; SER-303; GLY-364;
RP PRO-883 AND GLY-901, INTERACTION WITH CLE45, SUBUNIT, SUBCELLULAR LOCATION,
RP AND INDUCTION BY CRN.
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: Necessary for male gametophyte development, as well as ovule
CC specification and function (PubMed:16367950). Required for the
CC development of high-ordered vascular strands within the leaf and a
CC correlated control of leaf shape, size and symmetry (PubMed:16367950).
CC LRR-rich receptor-like kinase (LRR-RLK) involved in the perception of
CC CLE45 peptide ligand which mediates root growth inhibition by
CC repressing protophloem differentiation; this mechanism requires CRN
CC (PubMed:23569225, PubMed:28607033, PubMed:25049386). BRX, BAM3, and
CC CLE45 act together to regulate the transition of protophloem cells from
CC proliferation to differentiation, thus impinging on postembryonic
CC growth capacity of the root meristem (PubMed:23569225,
CC PubMed:25049386). Necessary for CLE45 peptide-triggered accumulation of
CC MAKR5 in developing sieve elements (PubMed:27354416).
CC {ECO:0000269|PubMed:16367950, ECO:0000269|PubMed:23569225,
CC ECO:0000269|PubMed:25049386, ECO:0000269|PubMed:27354416,
CC ECO:0000269|PubMed:28607033}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00159};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU00159};
CC -!- SUBUNIT: Interacts with CLE45, especially in roots (PubMed:28607033).
CC Binds to the dimer CLV2/CRN (PubMed:28607033).
CC {ECO:0000269|PubMed:28607033}.
CC -!- INTERACTION:
CC O65440-2; C0LGR6: At4g29180; NbExp=2; IntAct=EBI-20653325, EBI-20654480;
CC O65440-2; C0LGT1: At5g10290; NbExp=2; IntAct=EBI-20653325, EBI-16954266;
CC O65440-2; Q9ASS4: At5g48380; NbExp=2; IntAct=EBI-20653325, EBI-6298290;
CC O65440-2; Q9LT96: At5g49770; NbExp=4; IntAct=EBI-20653325, EBI-17123993;
CC O65440-2; O65440-2: BAM3; NbExp=2; IntAct=EBI-20653325, EBI-20653325;
CC O65440-2; O22476: BRI1; NbExp=3; IntAct=EBI-20653325, EBI-1797828;
CC O65440-2; Q9ZPS9: BRL2; NbExp=2; IntAct=EBI-20653325, EBI-2292728;
CC O65440-2; Q9FL28: FLS2; NbExp=2; IntAct=EBI-20653325, EBI-1799448;
CC O65440-2; C0LGN2: LRR-RLK; NbExp=3; IntAct=EBI-20653325, EBI-20652801;
CC O65440-2; F4K6B8: RGI4; NbExp=2; IntAct=EBI-20653325, EBI-1238236;
CC O65440-2; Q9FYK0: TMK2; NbExp=3; IntAct=EBI-20653325, EBI-20652836;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28607033};
CC Single-pass type I membrane protein {ECO:0000255}. Endoplasmic
CC reticulum membrane {ECO:0000269|PubMed:28607033}; Single-pass type I
CC membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O65440-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O65440-2; Sequence=VSP_040681;
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, roots, leaves, stems,
CC inflorescences, flowers and siliques (PubMed:16367950). In roots,
CC confined to protophloem and sieve element precursor cells
CC (PubMed:23569225, PubMed:25049386). {ECO:0000269|PubMed:16367950,
CC ECO:0000269|PubMed:23569225, ECO:0000269|PubMed:25049386}.
CC -!- DEVELOPMENTAL STAGE: Expressed in roots developing protophloem, up to
CC the end of the transition zone. {ECO:0000269|PubMed:23569225}.
CC -!- INDUCTION: Accumulates upon CLE45 peptide application
CC (PubMed:23569225). Accumulation is promoted by CRN, especially at later
CC stages of protophloem development (PubMed:28607033).
CC {ECO:0000269|PubMed:23569225, ECO:0000269|PubMed:28607033}.
CC -!- DISRUPTION PHENOTYPE: When associated with BAM1 and BAM2 disruptions,
CC loss of stem cells at the shoot and flower meristems. The disruption of
CC BAM3 restores root protophloem and mersitem phenotypes observed in brx
CC mutants (PubMed:23569225). The bam3 mutant resists to root growth
CC inhibition mediated by CLE45 peptide ligand (PubMed:23569225).
CC {ECO:0000269|PubMed:16367950, ECO:0000269|PubMed:23569225}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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; AL022224; CAA18252.1; -; Genomic_DNA.
DR EMBL; AL161552; CAB79027.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE84297.1; -; Genomic_DNA.
DR EMBL; FJ708747; ACN59341.1; -; mRNA.
DR EMBL; AK229453; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; T05335; T05335.
DR RefSeq; NP_193760.1; NM_118146.5. [O65440-1]
DR AlphaFoldDB; O65440; -.
DR SMR; O65440; -.
DR BioGRID; 13066; 44.
DR IntAct; O65440; 53.
DR STRING; 3702.AT4G20270.1; -.
DR PaxDb; O65440; -.
DR PRIDE; O65440; -.
DR ProteomicsDB; 240771; -. [O65440-1]
DR EnsemblPlants; AT4G20270.1; AT4G20270.1; AT4G20270. [O65440-1]
DR GeneID; 827774; -.
DR Gramene; AT4G20270.1; AT4G20270.1; AT4G20270. [O65440-1]
DR KEGG; ath:AT4G20270; -.
DR Araport; AT4G20270; -.
DR TAIR; locus:2120412; AT4G20270.
DR eggNOG; ENOG502QXPR; Eukaryota.
DR HOGENOM; CLU_000288_114_1_1; -.
DR InParanoid; O65440; -.
DR OMA; KNRRMRK; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; O65440; -.
DR PRO; PR:O65440; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O65440; baseline and differential.
DR Genevisible; O65440; AT.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0042277; F:peptide binding; IPI:UniProtKB.
DR GO; GO:0001653; F:peptide receptor activity; IMP:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0048437; P:floral organ development; IGI:TAIR.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0010078; P:maintenance of root meristem identity; IMP:UniProtKB.
DR GO; GO:0010088; P:phloem development; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0045595; P:regulation of cell differentiation; IMP:UniProtKB.
DR GO; GO:0010075; P:regulation of meristem growth; IGI:TAIR.
DR Gene3D; 3.80.10.10; -; 4.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00560; LRR_1; 3.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 9.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51450; LRR; 13.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell membrane; Developmental protein;
KW Differentiation; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW Kinase; Leucine-rich repeat; Membrane; Nucleotide-binding; Receptor;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Signal;
KW Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..992
FT /note="Leucine-rich repeat receptor-like serine/threonine-
FT protein kinase BAM3"
FT /id="PRO_0000403354"
FT TOPO_DOM 22..656
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 657..677
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 678..992
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 75..99
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 100..124
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 126..148
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 150..173
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 174..199
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 201..221
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 246..270
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 271..294
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 296..320
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 322..342
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 343..366
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 368..391
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 393..414
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 415..438
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 439..462
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 465..489
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REPEAT 491..513
FT /note="LRR 17"
FT /evidence="ECO:0000255"
FT REPEAT 514..536
FT /note="LRR 18"
FT /evidence="ECO:0000255"
FT REPEAT 537..561
FT /note="LRR 19"
FT /evidence="ECO:0000255"
FT REPEAT 563..585
FT /note="LRR 20"
FT /evidence="ECO:0000255"
FT REPEAT 586..610
FT /note="LRR 21"
FT /evidence="ECO:0000255"
FT DOMAIN 710..992
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOTIF 226..231
FT /note="CLE45 peptide binding"
FT /evidence="ECO:0000269|PubMed:28607033"
FT ACT_SITE 836
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 716..724
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 738
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 440
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 472
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 525
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 568
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 575
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 597
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 613
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 631
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 635
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 64..71
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT VAR_SEQ 381..409
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:20064227"
FT /id="VSP_040681"
FT MUTAGEN 150
FT /note="T->I: Insensitivity to root growth inhibition
FT mediated by CLE45 peptide."
FT /evidence="ECO:0000269|PubMed:28607033"
FT MUTAGEN 226..231
FT /note="QLYLGY->AAAAAA: Strongly reduced binding to CLE45
FT and insensitivity to BRX-dependent root growth inhibition
FT mediated by CLE45 peptide."
FT /evidence="ECO:0000269|PubMed:28607033"
FT MUTAGEN 303
FT /note="S->F: Insensitivity to root growth inhibition
FT mediated by CLE45 peptide."
FT /evidence="ECO:0000269|PubMed:28607033"
FT MUTAGEN 364
FT /note="G->R: Insensitivity to root growth inhibition
FT mediated by CLE45 peptide."
FT /evidence="ECO:0000269|PubMed:28607033"
FT MUTAGEN 883
FT /note="P->S: Insensitivity to root growth inhibition
FT mediated by CLE45 peptide."
FT /evidence="ECO:0000269|PubMed:28607033"
FT MUTAGEN 901
FT /note="G->E: Insensitivity to root growth inhibition
FT mediated by CLE45 peptide."
FT /evidence="ECO:0000269|PubMed:28607033"
FT CONFLICT 542
FT /note="Y -> C (in Ref. 4; AK229453)"
FT /evidence="ECO:0000305"
FT CONFLICT 721
FT /note="R -> A (in Ref. 3; ACN59341 and 4; AK229453)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 992 AA; 110283 MW; A394AA19376BDA20 CRC64;
MADKIFTFFL ILSSISPLLC SSLISPLNLS LIRQANVLIS LKQSFDSYDP SLDSWNIPNF
NSLCSWTGVS CDNLNQSITR LDLSNLNISG TISPEISRLS PSLVFLDISS NSFSGELPKE
IYELSGLEVL NISSNVFEGE LETRGFSQMT QLVTLDAYDN SFNGSLPLSL TTLTRLEHLD
LGGNYFDGEI PRSYGSFLSL KFLSLSGNDL RGRIPNELAN ITTLVQLYLG YYNDYRGGIP
ADFGRLINLV HLDLANCSLK GSIPAELGNL KNLEVLFLQT NELTGSVPRE LGNMTSLKTL
DLSNNFLEGE IPLELSGLQK LQLFNLFFNR LHGEIPEFVS ELPDLQILKL WHNNFTGKIP
SKLGSNGNLI EIDLSTNKLT GLIPESLCFG RRLKILILFN NFLFGPLPED LGQCEPLWRF
RLGQNFLTSK LPKGLIYLPN LSLLELQNNF LTGEIPEEEA GNAQFSSLTQ INLSNNRLSG
PIPGSIRNLR SLQILLLGAN RLSGQIPGEI GSLKSLLKID MSRNNFSGKF PPEFGDCMSL
TYLDLSHNQI SGQIPVQISQ IRILNYLNVS WNSFNQSLPN ELGYMKSLTS ADFSHNNFSG
SVPTSGQFSY FNNTSFLGNP FLCGFSSNPC NGSQNQSQSQ LLNQNNARSR GEISAKFKLF
FGLGLLGFFL VFVVLAVVKN RRMRKNNPNL WKLIGFQKLG FRSEHILECV KENHVIGKGG
RGIVYKGVMP NGEEVAVKKL LTITKGSSHD NGLAAEIQTL GRIRHRNIVR LLAFCSNKDV
NLLVYEYMPN GSLGEVLHGK AGVFLKWETR LQIALEAAKG LCYLHHDCSP LIIHRDVKSN
NILLGPEFEA HVADFGLAKF MMQDNGASEC MSSIAGSYGY IAPEYAYTLR IDEKSDVYSF
GVVLLELITG RKPVDNFGEE GIDIVQWSKI QTNCNRQGVV KIIDQRLSNI PLAEAMELFF
VAMLCVQEHS VERPTMREVV QMISQAKQPN TF
