THE1_ARATH
ID THE1_ARATH Reviewed; 855 AA.
AC Q9LK35;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Receptor-like protein kinase THESEUS 1;
DE EC=2.7.11.-;
DE Flags: Precursor;
GN Name=THE1; OrderedLocusNames=At5g54380; ORFNames=GA469.3;
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;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. La-0;
RX PubMed=14506206; DOI=10.1074/mcp.t300006-mcp200;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Large-scale analysis of in vivo phosphorylated membrane proteins by
RT immobilized metal ion affinity chromatography and mass spectrometry.";
RL Mol. Cell. Proteomics 2:1234-1243(2003).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15308754; DOI=10.1105/tpc.104.023150;
RA Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT "Phosphoproteomics of the Arabidopsis plasma membrane and a new
RT phosphorylation site database.";
RL Plant Cell 16:2394-2405(2004).
RN [5]
RP FUNCTION, MUTAGENESIS OF GLY-37 AND GLU-150, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AUTOPHOSPHORYLATION, AND DISRUPTION PHENOTYPE.
RX PubMed=17540573; DOI=10.1016/j.cub.2007.05.018;
RA Hematy K., Sado P.-E., Van Tuinen A., Rochange S., Desnos T., Balzergue S.,
RA Pelletier S., Renou J.-P., Hoefte H.;
RT "A receptor-like kinase mediates the response of Arabidopsis cells to the
RT inhibition of cellulose synthesis.";
RL Curr. Biol. 17:922-931(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=17644812; DOI=10.1074/mcp.m700099-mcp200;
RA Marmagne A., Ferro M., Meinnel T., Bruley C., Kuhn L., Garin J.,
RA Barbier-Brygoo H., Ephritikhine G.;
RT "A high content in lipid-modified peripheral proteins and integral receptor
RT kinases features in the arabidopsis plasma membrane proteome.";
RL Mol. Cell. Proteomics 6:1980-1996(2007).
RN [7]
RP GENE FAMILY.
RX PubMed=19529822; DOI=10.1093/mp/ssn083;
RA Chae L., Sudat S., Dudoit S., Zhu T., Luan S.;
RT "Diverse transcriptional programs associated with environmental stress and
RT hormones in the Arabidopsis receptor-like kinase gene family.";
RL Mol. Plant 2:84-107(2009).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND INDUCTION BY
RP BRASSINOSTEROIDS.
RX PubMed=19383785; DOI=10.1073/pnas.0812346106;
RA Guo H., Li L., Ye H., Yu X., Algreen A., Yin Y.;
RT "Three related receptor-like kinases are required for optimal cell
RT elongation in Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:7648-7653(2009).
CC -!- FUNCTION: Receptor-like protein kinase required for cell elongation
CC during vegetative growth, mostly in a brassinosteroid-(BR-) independent
CC manner. Mediates the response of growing plant cells to the
CC perturbation of cellulose synthesis and may act as a cell-wall-
CC integrity sensor. Controls ectopic-lignin accumulation in cellulose-
CC deficient mutant backgrounds. {ECO:0000269|PubMed:17540573,
CC ECO:0000269|PubMed:19383785}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17540573,
CC ECO:0000305|PubMed:17644812}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:17540573, ECO:0000305|PubMed:17644812}.
CC -!- TISSUE SPECIFICITY: Expressed in most vegetative tissues, including
CC leaves, stems and roots, primarily in expanding cells and vascular
CC tissue. {ECO:0000269|PubMed:17540573, ECO:0000269|PubMed:19383785}.
CC -!- INDUCTION: By brassinosteroids (BR). {ECO:0000269|PubMed:19383785}.
CC -!- PTM: Autophosphorylated.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype; due to redundancy with
CC HERK1. Herk1 and the1 double mutants are stunted. In the1-4, shorter
CC hypocotyls without brassinolide (BL) treatment. In the1-3, partially
CC restored hypocotyl growth defect of prc1-8 and of other cellulose-
CC deficient mutants. {ECO:0000269|PubMed:17540573,
CC ECO:0000269|PubMed:19383785}.
CC -!- MISCELLANEOUS: Semidominant suppressor of the cellulose-deficient
CC mutant procuste1-1.
CC -!- MISCELLANEOUS: This protein was called 'Theseus' after the Greek
CC mythological figure Theseus, who slew the brigand Procustes.
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; AP000380; BAA98098.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96490.1; -; Genomic_DNA.
DR RefSeq; NP_200249.1; NM_124818.4.
DR AlphaFoldDB; Q9LK35; -.
DR SMR; Q9LK35; -.
DR BioGRID; 20770; 1.
DR STRING; 3702.AT5G54380.1; -.
DR iPTMnet; Q9LK35; -.
DR SwissPalm; Q9LK35; -.
DR PaxDb; Q9LK35; -.
DR PRIDE; Q9LK35; -.
DR ProteomicsDB; 246404; -.
DR EnsemblPlants; AT5G54380.1; AT5G54380.1; AT5G54380.
DR GeneID; 835526; -.
DR Gramene; AT5G54380.1; AT5G54380.1; AT5G54380.
DR KEGG; ath:AT5G54380; -.
DR Araport; AT5G54380; -.
DR TAIR; locus:2151349; AT5G54380.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_42_2_1; -.
DR InParanoid; Q9LK35; -.
DR OMA; DQIMDPN; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9LK35; -.
DR PRO; PR:Q9LK35; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LK35; baseline and differential.
DR Genevisible; Q9LK35; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:TAIR.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:InterPro.
DR GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:TAIR.
DR GO; GO:0009741; P:response to brassinosteroid; IGI:TAIR.
DR GO; GO:0009826; P:unidimensional cell growth; IGI:TAIR.
DR InterPro; IPR045272; ANXUR1-like.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR024788; Malectin-like_Carb-bd_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR27003; PTHR27003; 1.
DR Pfam; PF12819; Malectin_like; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
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 ATP-binding; Cell membrane; Glycoprotein; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..855
FT /note="Receptor-like protein kinase THESEUS 1"
FT /id="PRO_0000385336"
FT TOPO_DOM 23..415
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 416..436
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 437..855
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 510..783
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 822..855
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 834..848
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 634
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 516..524
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 538
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 376
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 37
FT /note="G->D: In the1-1; partially restored hypocotyl growth
FT defect of prc1-8."
FT /evidence="ECO:0000269|PubMed:17540573"
FT MUTAGEN 150
FT /note="E->K: In the1-2; partially restored hypocotyl growth
FT defect of prc1-8."
FT /evidence="ECO:0000269|PubMed:17540573"
SQ SEQUENCE 855 AA; 93295 MW; 169CBF02D001D9B0 CRC64;
MVFTKSLLVL LWFLSCYTTT TSSALFNPPD NYLISCGSSQ NITFQNRIFV PDSLHSSLVL
KIGNSSVATS TTSNNSTNSI YQTARVFSSL ASYRFKITSL GRHWIRLHFS PINNSTWNLT
SASITVVTED FVLLNNFSFN NFNGSYIFKE YTVNVTSEFL TLSFIPSNNS VVFVNAIEVV
SVPDNLIPDQ ALALNPSTPF SGLSLLAFET VYRLNMGGPL LTSQNDTLGR QWDNDAEYLH
VNSSVLVVTA NPSSIKYSPS VTQETAPNMV YATADTMGDA NVASPSFNVT WVLPVDPDFR
YFVRVHFCDI VSQALNTLVF NLYVNDDLAL GSLDLSTLTN GLKVPYFKDF ISNGSVESSG
VLTVSVGPDS QADITNATMN GLEVLKISNE AKSLSGVSSV KSLLPGGSGS KSKKKAVIIG
SLVGAVTLIL LIAVCCYCCL VASRKQRSTS PQEGGNGHPW LPLPLYGLSQ TLTKSTASHK
SATASCISLA STHLGRCFMF QEIMDATNKF DESSLLGVGG FGRVYKGTLE DGTKVAVKRG
NPRSEQGMAE FRTEIEMLSK LRHRHLVSLI GYCDERSEMI LVYEYMANGP LRSHLYGADL
PPLSWKQRLE ICIGAARGLH YLHTGASQSI IHRDVKTTNI LLDENLVAKV ADFGLSKTGP
SLDQTHVSTA VKGSFGYLDP EYFRRQQLTE KSDVYSFGVV LMEVLCCRPA LNPVLPREQV
NIAEWAMAWQ KKGLLDQIMD SNLTGKVNPA SLKKFGETAE KCLAEYGVDR PSMGDVLWNL
EYALQLEETS SALMEPDDNS TNHIPGIPMA PMEPFDNSMS IIDRGGVNSG TGTDDDAEDA
TTSAVFSQLV HPRGR
