RLK6_ARATH
ID RLK6_ARATH Reviewed; 899 AA.
AC Q9LIG2;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Receptor-like protein kinase At3g21340;
DE EC=2.7.10.1;
DE EC=2.7.11.1;
DE AltName: Full=Leucine-rich repeat receptor-like protein kinase At3g21340;
DE Flags: Precursor;
GN OrderedLocusNames=At3g21340; ORFNames=MHC9.2;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
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 FUNCTION, AND AUTOPHOSPHORYLATION.
RX PubMed=19124768; DOI=10.1073/pnas.0810249106;
RA Oh M.-H., Wang X., Kota U., Goshe M.B., Clouse S.D., Huber S.C.;
RT "Tyrosine phosphorylation of the BRI1 receptor kinase emerges as a
RT component of brassinosteroid signaling in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:658-663(2009).
CC -!- FUNCTION: Probable receptor with a dual specificity kinase activity
CC acting on both serine/threonine- and tyrosine-containing substrates.
CC {ECO:0000269|PubMed:19124768}.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10027};
CC -!- INTERACTION:
CC Q9LIG2; C0LGI2: At1g67720; NbExp=2; IntAct=EBI-941096, EBI-17070892;
CC Q9LIG2; A0A1I9LQ53: At3g50230; NbExp=2; IntAct=EBI-941096, EBI-20654045;
CC Q9LIG2; Q9FK10: At5g53320; NbExp=2; IntAct=EBI-941096, EBI-20654730;
CC Q9LIG2; O22138: LRR-RLK; NbExp=2; IntAct=EBI-941096, EBI-16946020;
CC Q9LIG2; Q9LVI6: RLK902; NbExp=2; IntAct=EBI-941096, EBI-1626936;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- PTM: Autophosphorylated on Tyr and Thr residues.
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; FJ708725; ACN59320.1; -; mRNA.
DR EMBL; AP001305; BAB03047.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76495.1; -; Genomic_DNA.
DR RefSeq; NP_188771.2; NM_113029.4.
DR AlphaFoldDB; Q9LIG2; -.
DR SMR; Q9LIG2; -.
DR BioGRID; 7020; 30.
DR IntAct; Q9LIG2; 36.
DR STRING; 3702.AT3G21340.1; -.
DR iPTMnet; Q9LIG2; -.
DR PaxDb; Q9LIG2; -.
DR PRIDE; Q9LIG2; -.
DR ProteomicsDB; 228169; -.
DR EnsemblPlants; AT3G21340.1; AT3G21340.1; AT3G21340.
DR GeneID; 821688; -.
DR Gramene; AT3G21340.1; AT3G21340.1; AT3G21340.
DR KEGG; ath:AT3G21340; -.
DR Araport; AT3G21340; -.
DR TAIR; locus:2089483; AT3G21340.
DR eggNOG; ENOG502QQCZ; Eukaryota.
DR HOGENOM; CLU_000288_41_1_1; -.
DR InParanoid; Q9LIG2; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9LIG2; -.
DR PRO; PR:Q9LIG2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LIG2; baseline and differential.
DR Genevisible; Q9LIG2; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_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; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF12819; Malectin_like; 1.
DR Pfam; PF00069; Pkinase; 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; Leucine-rich repeat;
KW Membrane; Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome;
KW Repeat; Serine/threonine-protein kinase; Signal; Transferase;
KW Transmembrane; Transmembrane helix; Tyrosine-protein kinase.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..899
FT /note="Receptor-like protein kinase At3g21340"
FT /id="PRO_0000380728"
FT TOPO_DOM 28..522
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 523..543
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 544..899
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 415..438
FT /note="LRR 1"
FT REPEAT 439..461
FT /note="LRR 2"
FT REPEAT 463..485
FT /note="LRR 3"
FT DOMAIN 592..865
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 717
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 598..606
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 620
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 583
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 665
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 751
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 752
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 757
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 765
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 420
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 436
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 468
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 475
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 899 AA; 100195 MW; 270DCE57E738110D CRC64;
MEYHPQAIRL CALIFISFYA LLHLVEAQDQ KGFISLDCGS LPNEPPYNDP STGLTYSTDD
GFVQSGKTGR IQKAFESIFS KPSLKLRYFP DGFRNCYTLN VTQDTNYLIK AVFVYGNYDG
LNNPPSFDLY LGPNLWVTVD MNGRTNGTIQ EIIHKTISKS LQVCLVKTGT SSPMINTLEL
RPLKNNTYNT QSGSLKYFFR YYFSGSGQNI RYPDDVNDRK WYPFFDAKEW TELTTNLNIN
SSNGYAPPEV VMASASTPIS TFGTWNFSWL LPSSTTQFYV YMHFAEIQTL RSLDTREFKV
TLNGKLAYER YSPKTLATET IFYSTPQQCE DGTCLLELTK TPKSTLPPLM NALEVFTVID
FPQMETNPDD VAAIKSIQST YGLSKISWQG DPCVPKQFLW EGLNCNNLDN STPPIVTSLN
LSSSHLTGII AQGIQNLTHL QELDLSNNNL TGGIPEFLAD IKSLLVINLS GNNFNGSIPQ
ILLQKKGLKL ILEGNANLIC PDGLCVNKAG NGGAKKMNVV IPIVASVAFV VVLGSALAFF
FIFKKKKTSN SQDLGPSSYT QVSEVRTIRS SESAIMTKNR RFTYSEVVTM TNNFERVLGK
GGFGMVYHGT VNNTEQVAVK MLSHSSSQGY KEFKAEVELL LRVHHKNLVG LVGYCDEGEN
LALIYEYMAN GDLREHMSGK RGGSILNWET RLKIVVESAQ GLEYLHNGCK PPMVHRDVKT
TNILLNEHLH AKLADFGLSR SFPIEGETHV STVVAGTPGY LDPEYYRTNW LNEKSDVYSF
GIVLLEIITN QLVINQSREK PHIAEWVGLM LTKGDIQNIM DPKLYGDYDS GSVWRAVELA
MSCLNPSSAR RPTMSQVVIE LNECLSYENA RGGTSQNMNS ESSIEVSMNF DIGATPDAR
