TDR_ARATH
ID TDR_ARATH Reviewed; 1041 AA.
AC Q9FII5;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Leucine-rich repeat receptor-like protein kinase TDR;
DE EC=2.7.11.1;
DE AltName: Full=Protein PHLOEM INTERCALATED WITH XYLEM {ECO:0000303|PubMed:17570668};
DE AltName: Full=Tracheary element differentiation inhibitory factor receptor {ECO:0000303|PubMed:18812507};
DE Short=AtTDR {ECO:0000303|PubMed:18812507};
DE Short=TDIF receptor {ECO:0000303|PubMed:18812507};
DE Flags: Precursor;
GN Name=TDR {ECO:0000303|PubMed:18812507};
GN Synonyms=PXY {ECO:0000303|PubMed:17570668};
GN OrderedLocusNames=At5g61480 {ECO:0000312|Araport:AT5G61480};
GN ORFNames=MCI2.4 {ECO:0000312|EMBL:BAB10447.1};
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=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
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=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 [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=17570668; DOI=10.1016/j.cub.2007.05.049;
RA Fisher K., Turner S.;
RT "PXY, a receptor-like kinase essential for maintaining polarity during
RT plant vascular-tissue development.";
RL Curr. Biol. 17:1061-1066(2007).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, INTERACTION WITH
RP CLE41P AND CLE44P, AND TISSUE SPECIFICITY.
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 [7]
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 [8]
RP INTERACTION WITH LURE1.2.
RX PubMed=26863186; DOI=10.1038/nature16975;
RA Wang T., Liang L., Xue Y., Jia P.F., Chen W., Zhang M.X., Wang Y.C.,
RA Li H.J., Yang W.C.;
RT "A receptor heteromer mediates the male perception of female attractants in
RT plants.";
RL Nature 531:241-244(2016).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.77 ANGSTROMS) OF 31-629 IN COMPLEX WITH CLE41,
RP FUNCTION, MUTAGENESIS OF GLY-186; GLY-210; TYR-234; PHE-281; ASP-303;
RP SER-305; ARG-421 AND ARG-423, DISRUPTION PHENOTYPE, GLYCOSYLATION AT
RP ASN-111; ASN-271; ASN-356; ASN-378; ASN-442; ASN-471; ASN-525 AND ASN-542,
RP AND DISULFIDE BONDS.
RX PubMed=27055373; DOI=10.1038/cr.2016.45;
RA Zhang H., Lin X., Han Z., Qu L.-J., Chai J.;
RT "Crystal structure of PXY-TDIF complex reveals a conserved recognition
RT mechanism among CLE peptide-receptor pairs.";
RL Cell Res. 26:543-555(2016).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF 32-629 IN COMPLEX WITH CLE44 AND
RP TDR, GLYCOSYLATION AT ASN-111 AND ASN-322, AND DISULFIDE BONDS.
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).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 31-631 IN COMPLEX WITH CLE41,
RP MUTAGENESIS OF PHE-161; SER-162; ASP-255; ILE-421 AND ARG-423,
RP GLYCOSYLATION AT ASN-111; ASN-258; ASN-271; ASN-322; ASN-356; ASN-378;
RP ASN-430; ASN-442; ASN-471; ASN-525 AND ASN-542, DISULFIDE BONDS, AND
RP SUBCELLULAR LOCATION.
RX PubMed=27498761; DOI=10.1038/ncomms12383;
RA Morita J., Kato K., Nakane T., Kondo Y., Fukuda H., Nishimasu H.,
RA Ishitani R., Nureki O.;
RT "Crystal structure of the plant receptor-like kinase TDR in complex with
RT the TDIF peptide.";
RL Nat. Commun. 7:12383-12383(2016).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 30-642, GLYCOSYLATION AT ASN-111;
RP ASN-356; ASN-378; ASN-471 AND ASN-525, AND DISULFIDE BONDS.
RA Xu G., Li Z.;
RT "Crystal structure of a TDIF-TDR complex.";
RL Submitted (APR-2016) to the PDB data bank.
CC -!- FUNCTION: Acts with CLE41p and CLE44p peptides as a ligand-receptor
CC pair in a signal transduction pathway involved in the regulation of
CC procambium maintenance and polarity during vascular-tissue development
CC (PubMed:17570668, PubMed:18812507, PubMed:27055373). Mediates
CC repression of tracheary element differentiation and the promotion of
CC procambial cells formation and polar division adjacent to phloem cells
CC in the veins (PubMed:17570668, PubMed:18812507, PubMed:27055373).
CC {ECO:0000269|PubMed:17570668, ECO:0000269|PubMed:18812507,
CC ECO:0000269|PubMed:27055373}.
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 -!- 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;
CC -!- SUBUNIT: Interacts specifically with the mature peptides CLE41p and
CC CLE44p, especially in the presence of SERK2 (PubMed:18812507,
CC PubMed:27055373, PubMed:27449136, PubMed:27498761). Interacts with
CC LURE1.2 (PubMed:26863186). {ECO:0000269|PubMed:18812507,
CC ECO:0000269|PubMed:26863186, ECO:0000269|PubMed:27055373,
CC ECO:0000269|PubMed:27449136, ECO:0000269|PubMed:27498761}.
CC -!- INTERACTION:
CC Q9FII5; Q39011: ASK7; NbExp=2; IntAct=EBI-15730235, EBI-1798250;
CC Q9FII5; Q9SUQ3: At4g23740; NbExp=3; IntAct=EBI-15730235, EBI-16912451;
CC Q9FII5; Q9LJY0: PRK4; NbExp=2; IntAct=EBI-15730235, EBI-16914444;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18812507,
CC ECO:0000269|PubMed:27498761}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:18812507}.
CC -!- TISSUE SPECIFICITY: Widely expressed along the vascular strands. In
CC roots and hypocotyls, confined to procambial cells.
CC {ECO:0000269|PubMed:17570668, ECO:0000269|PubMed:18812507}.
CC -!- DISRUPTION PHENOTYPE: Reduced procambial cells number, and adjacent or
CC interspersed xylem and phloem formation. {ECO:0000269|PubMed:17570668,
CC ECO:0000269|PubMed:18812507, ECO:0000269|PubMed:27055373}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; FJ708809; ACN59400.1; -; mRNA.
DR EMBL; AB016887; BAB10447.1; -; Genomic_DNA.
DR EMBL; AB012239; BAB10447.1; JOINED; Genomic_DNA.
DR EMBL; CP002688; AED97473.1; -; Genomic_DNA.
DR RefSeq; NP_200956.1; NM_125541.2.
DR PDB; 5GIJ; X-ray; 3.00 A; B=31-631.
DR PDB; 5GQR; X-ray; 3.50 A; B=32-629.
DR PDB; 5GR9; X-ray; 2.77 A; B=31-629.
DR PDB; 5JFI; X-ray; 2.75 A; A/B=30-642.
DR PDB; 5JFK; X-ray; 2.65 A; A/B=30-642.
DR PDBsum; 5GIJ; -.
DR PDBsum; 5GQR; -.
DR PDBsum; 5GR9; -.
DR PDBsum; 5JFI; -.
DR PDBsum; 5JFK; -.
DR AlphaFoldDB; Q9FII5; -.
DR SMR; Q9FII5; -.
DR BioGRID; 21513; 22.
DR DIP; DIP-46414N; -.
DR IntAct; Q9FII5; 25.
DR STRING; 3702.AT5G61480.1; -.
DR PaxDb; Q9FII5; -.
DR PRIDE; Q9FII5; -.
DR ProteomicsDB; 246433; -.
DR EnsemblPlants; AT5G61480.1; AT5G61480.1; AT5G61480.
DR GeneID; 836269; -.
DR Gramene; AT5G61480.1; AT5G61480.1; AT5G61480.
DR KEGG; ath:AT5G61480; -.
DR Araport; AT5G61480; -.
DR TAIR; locus:2161158; AT5G61480.
DR eggNOG; ENOG502QSRW; Eukaryota.
DR HOGENOM; CLU_000288_22_1_1; -.
DR InParanoid; Q9FII5; -.
DR OMA; FHANYNR; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; Q9FII5; -.
DR PRO; PR:Q9FII5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FII5; baseline and differential.
DR Genevisible; Q9FII5; AT.
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:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IMP:TAIR.
DR GO; GO:0010087; P:phloem or xylem histogenesis; IMP:TAIR.
DR GO; GO:0010067; P:procambium histogenesis; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0010223; P:secondary shoot formation; IMP:TAIR.
DR GO; GO:0010089; P:xylem development; IMP:UniProtKB.
DR Gene3D; 3.80.10.10; -; 3.
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; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00560; LRR_1; 2.
DR Pfam; PF13855; LRR_8; 2.
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; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell membrane; Developmental protein;
KW Disulfide bond; Glycoprotein; Kinase; Leucine-rich repeat; Membrane;
KW Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..1041
FT /note="Leucine-rich repeat receptor-like protein kinase
FT TDR"
FT /id="PRO_0000389463"
FT TOPO_DOM 30..652
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 653..673
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 674..1041
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 80..104
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 105..128
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 130..152
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 154..176
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 177..199
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 200..224
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 225..248
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT REPEAT 250..272
FT /note="LRR 8"
FT /evidence="ECO:0000255"
FT REPEAT 273..296
FT /note="LRR 9"
FT /evidence="ECO:0000255"
FT REPEAT 297..319
FT /note="LRR 10"
FT /evidence="ECO:0000255"
FT REPEAT 321..344
FT /note="LRR 11"
FT /evidence="ECO:0000255"
FT REPEAT 345..368
FT /note="LRR 12"
FT /evidence="ECO:0000255"
FT REPEAT 369..392
FT /note="LRR 13"
FT /evidence="ECO:0000255"
FT REPEAT 394..416
FT /note="LRR 14"
FT /evidence="ECO:0000255"
FT REPEAT 418..439
FT /note="LRR 15"
FT /evidence="ECO:0000255"
FT REPEAT 440..464
FT /note="LRR 16"
FT /evidence="ECO:0000255"
FT REPEAT 466..488
FT /note="LRR 17"
FT /evidence="ECO:0000255"
FT REPEAT 511..535
FT /note="LRR 18"
FT /evidence="ECO:0000255"
FT REPEAT 536..558
FT /note="LRR 19"
FT /evidence="ECO:0000255"
FT REPEAT 559..583
FT /note="LRR 20"
FT /evidence="ECO:0000255"
FT REPEAT 585..607
FT /note="LRR 21"
FT /evidence="ECO:0000255"
FT DOMAIN 719..1001
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 186..188
FT /note="CLE peptide binding"
FT /evidence="ECO:0000269|PubMed:27055373,
FT ECO:0000269|PubMed:27449136, ECO:0000269|PubMed:27498761,
FT ECO:0007744|PDB:5GIJ, ECO:0007744|PDB:5GQR,
FT ECO:0007744|PDB:5GR9"
FT REGION 233..235
FT /note="CLE peptide binding"
FT /evidence="ECO:0000269|PubMed:27055373,
FT ECO:0000269|PubMed:27449136, ECO:0000269|PubMed:27498761,
FT ECO:0007744|PDB:5GIJ, ECO:0007744|PDB:5GQR,
FT ECO:0007744|PDB:5GR9"
FT REGION 303..307
FT /note="CLE peptide binding"
FT /evidence="ECO:0000269|PubMed:27055373,
FT ECO:0000269|PubMed:27449136, ECO:0000269|PubMed:27498761,
FT ECO:0007744|PDB:5GIJ, ECO:0007744|PDB:5GQR,
FT ECO:0007744|PDB:5GR9"
FT REGION 375..377
FT /note="CLE peptide binding"
FT /evidence="ECO:0000269|PubMed:27055373,
FT ECO:0000269|PubMed:27449136, ECO:0000269|PubMed:27498761,
FT ECO:0007744|PDB:5GIJ, ECO:0007744|PDB:5GQR,
FT ECO:0007744|PDB:5GR9"
FT REGION 421..423
FT /note="CLE peptide binding"
FT /evidence="ECO:0000269|PubMed:27055373,
FT ECO:0000269|PubMed:27449136, ECO:0000269|PubMed:27498761,
FT ECO:0007744|PDB:5GIJ, ECO:0007744|PDB:5GQR,
FT ECO:0007744|PDB:5GR9"
FT ACT_SITE 852
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 725..733
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 747
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT SITE 210
FT /note="CLE peptide binding"
FT /evidence="ECO:0000269|PubMed:27055373,
FT ECO:0000269|PubMed:27449136, ECO:0000269|PubMed:27498761,
FT ECO:0007744|PDB:5GIJ, ECO:0007744|PDB:5GQR,
FT ECO:0007744|PDB:5GR9"
FT SITE 255
FT /note="CLE peptide binding"
FT /evidence="ECO:0000269|PubMed:27055373,
FT ECO:0000269|PubMed:27449136, ECO:0000269|PubMed:27498761,
FT ECO:0007744|PDB:5GIJ, ECO:0007744|PDB:5GQR,
FT ECO:0007744|PDB:5GR9"
FT SITE 353
FT /note="CLE peptide binding"
FT /evidence="ECO:0000269|PubMed:27055373,
FT ECO:0000269|PubMed:27449136, ECO:0000269|PubMed:27498761,
FT ECO:0007744|PDB:5GIJ, ECO:0007744|PDB:5GQR,
FT ECO:0007744|PDB:5GR9"
FT MOD_RES 710
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 798
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 839
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 884
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT MOD_RES 892
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 899
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT MOD_RES 900
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:27055373, ECO:0000269|PubMed:27449136,
FT ECO:0000269|PubMed:27498761, ECO:0000269|Ref.12,
FT ECO:0007744|PDB:5GIJ, ECO:0007744|PDB:5GQR,
FT ECO:0007744|PDB:5GR9, ECO:0007744|PDB:5JFI,
FT ECO:0007744|PDB:5JFK"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:27498761, ECO:0007744|PDB:5GIJ"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:27055373, ECO:0000269|PubMed:27498761,
FT ECO:0007744|PDB:5GIJ, ECO:0007744|PDB:5GR9"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:27449136, ECO:0000269|PubMed:27498761,
FT ECO:0007744|PDB:5GIJ, ECO:0007744|PDB:5GQR"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 356
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:27055373, ECO:0000269|PubMed:27449136,
FT ECO:0000269|PubMed:27498761, ECO:0000269|Ref.12,
FT ECO:0007744|PDB:5GIJ, ECO:0007744|PDB:5GQR,
FT ECO:0007744|PDB:5GR9, ECO:0007744|PDB:5JFI,
FT ECO:0007744|PDB:5JFK"
FT CARBOHYD 378
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:27055373, ECO:0000269|PubMed:27449136,
FT ECO:0000269|PubMed:27498761, ECO:0000269|Ref.12,
FT ECO:0007744|PDB:5GIJ, ECO:0007744|PDB:5GQR,
FT ECO:0007744|PDB:5GR9, ECO:0007744|PDB:5JFI,
FT ECO:0007744|PDB:5JFK"
FT CARBOHYD 430
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:27498761, ECO:0007744|PDB:5GIJ"
FT CARBOHYD 442
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:27055373, ECO:0000269|PubMed:27498761,
FT ECO:0007744|PDB:5GIJ, ECO:0007744|PDB:5GR9"
FT CARBOHYD 471
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:27055373, ECO:0000269|PubMed:27498761,
FT ECO:0000269|Ref.12, ECO:0007744|PDB:5GIJ,
FT ECO:0007744|PDB:5GR9, ECO:0007744|PDB:5JFI,
FT ECO:0007744|PDB:5JFK"
FT CARBOHYD 525
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:27055373, ECO:0000269|PubMed:27498761,
FT ECO:0000269|Ref.12, ECO:0007744|PDB:5GIJ,
FT ECO:0007744|PDB:5GR9, ECO:0007744|PDB:5JFI,
FT ECO:0007744|PDB:5JFK"
FT CARBOHYD 542
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:27055373, ECO:0000269|PubMed:27498761,
FT ECO:0007744|PDB:5GIJ, ECO:0007744|PDB:5GR9"
FT CARBOHYD 590
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 69..76
FT /evidence="ECO:0000269|PubMed:27055373,
FT ECO:0000269|PubMed:27449136, ECO:0000269|PubMed:27498761,
FT ECO:0007744|PDB:5GIJ, ECO:0007744|PDB:5GQR,
FT ECO:0007744|PDB:5GR9"
FT DISULFID 390..416
FT /evidence="ECO:0000269|PubMed:27055373,
FT ECO:0000269|PubMed:27449136, ECO:0000269|PubMed:27498761,
FT ECO:0000269|Ref.12, ECO:0007744|PDB:5GIJ,
FT ECO:0007744|PDB:5GQR, ECO:0007744|PDB:5GR9,
FT ECO:0007744|PDB:5JFI, ECO:0007744|PDB:5JFK"
FT DISULFID 511..535
FT /evidence="ECO:0000269|PubMed:27055373,
FT ECO:0000269|PubMed:27449136, ECO:0000269|PubMed:27498761,
FT ECO:0000269|Ref.12, ECO:0007744|PDB:5GIJ,
FT ECO:0007744|PDB:5GQR, ECO:0007744|PDB:5GR9,
FT ECO:0007744|PDB:5JFI, ECO:0007744|PDB:5JFK"
FT DISULFID 620..628
FT /evidence="ECO:0000269|PubMed:27055373,
FT ECO:0000269|PubMed:27449136, ECO:0000269|PubMed:27498761,
FT ECO:0007744|PDB:5GIJ, ECO:0007744|PDB:5GQR,
FT ECO:0007744|PDB:5GR9"
FT MUTAGEN 161
FT /note="F->A: Reduced interaction with CLE41 peptide."
FT /evidence="ECO:0000269|PubMed:27498761"
FT MUTAGEN 162
FT /note="S->A: Reduced interaction with CLE41 peptide."
FT /evidence="ECO:0000269|PubMed:27498761"
FT MUTAGEN 186
FT /note="G->A: Reduced interaction with CLE41 peptide leading
FT to desorganized vascular tissues."
FT /evidence="ECO:0000269|PubMed:27055373"
FT MUTAGEN 210
FT /note="G->A: Reduced interaction with CLE41 peptide leading
FT to desorganized vascular tissues."
FT /evidence="ECO:0000269|PubMed:27055373"
FT MUTAGEN 234
FT /note="Y->A: Reduced interaction with CLE41 peptide leading
FT to desorganized vascular tissues."
FT /evidence="ECO:0000269|PubMed:27055373"
FT MUTAGEN 255
FT /note="D->E: Reduced interaction with CLE41 peptide."
FT /evidence="ECO:0000269|PubMed:27498761"
FT MUTAGEN 281
FT /note="F->A: Reduced interaction with CLE41 peptide."
FT /evidence="ECO:0000269|PubMed:27055373"
FT MUTAGEN 303
FT /note="D->R: Reduced interaction with CLE41 peptide leading
FT to a cambium-defective phenotype and adjacent phloem and
FT xylem cells; when associated with A-305."
FT /evidence="ECO:0000269|PubMed:27055373"
FT MUTAGEN 305
FT /note="S->A: Reduced interaction with CLE41 peptide leading
FT to a cambium-defective phenotype and adjacent phloem and
FT xylem cells; when associated with R-303."
FT /evidence="ECO:0000269|PubMed:27055373"
FT MUTAGEN 421
FT /note="R->A: Slightly reduced interaction with CLE41
FT peptide. Impaired interaction with CLE41 peptide leading to
FT a cambium-defective phenotype and adjacent phloem and xylem
FT cells; when associated with A-423."
FT /evidence="ECO:0000269|PubMed:27055373,
FT ECO:0000269|PubMed:27498761"
FT MUTAGEN 423
FT /note="R->A: Reduced interaction with CLE41 peptide.
FT Impaired interaction with CLE41 peptide leading to a
FT cambium-defective phenotype and adjacent phloem and xylem
FT cells; when associated with A-421."
FT /evidence="ECO:0000269|PubMed:27055373,
FT ECO:0000269|PubMed:27498761"
FT HELIX 34..45
FT /evidence="ECO:0007829|PDB:5GR9"
FT HELIX 50..53
FT /evidence="ECO:0007829|PDB:5GR9"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:5JFK"
FT HELIX 74..77
FT /evidence="ECO:0007829|PDB:5JFK"
FT TURN 78..80
FT /evidence="ECO:0007829|PDB:5GR9"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:5JFK"
FT HELIX 99..103
FT /evidence="ECO:0007829|PDB:5JFK"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:5JFK"
FT STRAND 114..117
FT /evidence="ECO:0007829|PDB:5JFK"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:5GIJ"
FT HELIX 123..127
FT /evidence="ECO:0007829|PDB:5JFK"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:5JFK"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:5JFK"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:5JFK"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:5JFK"
FT STRAND 164..168
FT /evidence="ECO:0007829|PDB:5JFK"
FT HELIX 171..175
FT /evidence="ECO:0007829|PDB:5JFK"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:5JFK"
FT STRAND 186..191
FT /evidence="ECO:0007829|PDB:5GR9"
FT HELIX 195..199
FT /evidence="ECO:0007829|PDB:5JFK"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:5JFK"
FT STRAND 210..216
FT /evidence="ECO:0007829|PDB:5JFK"
FT HELIX 219..223
FT /evidence="ECO:0007829|PDB:5JFK"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:5JFK"
FT STRAND 234..239
FT /evidence="ECO:0007829|PDB:5JFK"
FT HELIX 243..247
FT /evidence="ECO:0007829|PDB:5JFK"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:5GR9"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:5JFK"
FT HELIX 267..271
FT /evidence="ECO:0007829|PDB:5JFK"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:5JFK"
FT STRAND 282..287
FT /evidence="ECO:0007829|PDB:5JFK"
FT HELIX 291..295
FT /evidence="ECO:0007829|PDB:5JFK"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:5JFK"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:5JFK"
FT HELIX 315..319
FT /evidence="ECO:0007829|PDB:5JFK"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:5JFK"
FT STRAND 330..335
FT /evidence="ECO:0007829|PDB:5JFK"
FT HELIX 339..343
FT /evidence="ECO:0007829|PDB:5JFK"
FT STRAND 349..351
FT /evidence="ECO:0007829|PDB:5JFK"
FT STRAND 354..357
FT /evidence="ECO:0007829|PDB:5GR9"
FT TURN 363..368
FT /evidence="ECO:0007829|PDB:5JFK"
FT STRAND 373..375
FT /evidence="ECO:0007829|PDB:5JFK"
FT TURN 387..392
FT /evidence="ECO:0007829|PDB:5JFK"
FT STRAND 397..399
FT /evidence="ECO:0007829|PDB:5JFK"
FT STRAND 402..405
FT /evidence="ECO:0007829|PDB:5GQR"
FT STRAND 406..408
FT /evidence="ECO:0007829|PDB:5JFK"
FT HELIX 411..415
FT /evidence="ECO:0007829|PDB:5JFK"
FT STRAND 421..423
FT /evidence="ECO:0007829|PDB:5JFK"
FT STRAND 426..431
FT /evidence="ECO:0007829|PDB:5JFK"
FT HELIX 437..439
FT /evidence="ECO:0007829|PDB:5JFK"
FT STRAND 445..447
FT /evidence="ECO:0007829|PDB:5JFK"
FT STRAND 450..453
FT /evidence="ECO:0007829|PDB:5JFK"
FT HELIX 459..463
FT /evidence="ECO:0007829|PDB:5JFK"
FT STRAND 469..471
FT /evidence="ECO:0007829|PDB:5GR9"
FT HELIX 485..487
FT /evidence="ECO:0007829|PDB:5JFK"
FT STRAND 492..494
FT /evidence="ECO:0007829|PDB:5JFK"
FT STRAND 502..504
FT /evidence="ECO:0007829|PDB:5GR9"
FT STRAND 516..518
FT /evidence="ECO:0007829|PDB:5JFK"
FT STRAND 521..524
FT /evidence="ECO:0007829|PDB:5JFK"
FT HELIX 532..534
FT /evidence="ECO:0007829|PDB:5JFK"
FT STRAND 540..542
FT /evidence="ECO:0007829|PDB:5JFK"
FT STRAND 545..548
FT /evidence="ECO:0007829|PDB:5GQR"
FT HELIX 554..558
FT /evidence="ECO:0007829|PDB:5JFK"
FT STRAND 564..566
FT /evidence="ECO:0007829|PDB:5JFK"
FT STRAND 569..574
FT /evidence="ECO:0007829|PDB:5JFK"
FT HELIX 578..582
FT /evidence="ECO:0007829|PDB:5JFK"
FT STRAND 588..590
FT /evidence="ECO:0007829|PDB:5JFK"
FT STRAND 593..596
FT /evidence="ECO:0007829|PDB:5JFK"
FT STRAND 597..599
FT /evidence="ECO:0007829|PDB:5GR9"
FT HELIX 604..607
FT /evidence="ECO:0007829|PDB:5GR9"
FT HELIX 610..612
FT /evidence="ECO:0007829|PDB:5JFK"
FT STRAND 619..623
FT /evidence="ECO:0007829|PDB:5JFI"
SQ SEQUENCE 1041 AA; 114678 MW; 92510C0E8C81FABE CRC64;
MKKKNISPSL VLHPLLLLLL PFFAFNSLAL KFSPQLLSLL SLKTSLSGPP SAFQDWKVPV
NGQNDAVWCS WSGVVCDNVT AQVISLDLSH RNLSGRIPIQ IRYLSSLLYL NLSGNSLEGS
FPTSIFDLTK LTTLDISRNS FDSSFPPGIS KLKFLKVFNA FSNNFEGLLP SDVSRLRFLE
ELNFGGSYFE GEIPAAYGGL QRLKFIHLAG NVLGGKLPPR LGLLTELQHM EIGYNHFNGN
IPSEFALLSN LKYFDVSNCS LSGSLPQELG NLSNLETLFL FQNGFTGEIP ESYSNLKSLK
LLDFSSNQLS GSIPSGFSTL KNLTWLSLIS NNLSGEVPEG IGELPELTTL FLWNNNFTGV
LPHKLGSNGK LETMDVSNNS FTGTIPSSLC HGNKLYKLIL FSNMFEGELP KSLTRCESLW
RFRSQNNRLN GTIPIGFGSL RNLTFVDLSN NRFTDQIPAD FATAPVLQYL NLSTNFFHRK
LPENIWKAPN LQIFSASFSN LIGEIPNYVG CKSFYRIELQ GNSLNGTIPW DIGHCEKLLC
LNLSQNHLNG IIPWEISTLP SIADVDLSHN LLTGTIPSDF GSSKTITTFN VSYNQLIGPI
PSGSFAHLNP SFFSSNEGLC GDLVGKPCNS DRFNAGNADI DGHHKEERPK KTAGAIVWIL
AAAIGVGFFV LVAATRCFQK SYGNRVDGGG RNGGDIGPWK LTAFQRLNFT ADDVVECLSK
TDNILGMGST GTVYKAEMPN GEIIAVKKLW GKNKENGKIR RRKSGVLAEV DVLGNVRHRN
IVRLLGCCTN RDCTMLLYEY MPNGSLDDLL HGGDKTMTAA AEWTALYQIA IGVAQGICYL
HHDCDPVIVH RDLKPSNILL DADFEARVAD FGVAKLIQTD ESMSVVAGSY GYIAPEYAYT
LQVDKKSDIY SYGVILLEII TGKRSVEPEF GEGNSIVDWV RSKLKTKEDV EEVLDKSMGR
SCSLIREEMK QMLRIALLCT SRSPTDRPPM RDVLLILQEA KPKRKTVGDN VIVVGDVNDV
NFEDVCSVDV GHDVKCQRIG V
