RLK0_ARATH
ID RLK0_ARATH Reviewed; 868 AA.
AC Q9FN94;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Receptor-like protein kinase At5g59670;
DE EC=2.7.10.1;
DE EC=2.7.11.1;
DE AltName: Full=Leucine-rich repeat receptor-like protein kinase At5g59670;
DE Flags: Precursor;
GN OrderedLocusNames=At5g59670; ORFNames=MTH12.12;
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=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(1997).
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 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 -!- 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; FJ708807; ACN59398.1; -; mRNA.
DR EMBL; AB006705; BAB09505.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97218.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM68447.1; -; Genomic_DNA.
DR EMBL; AY099606; AAM20457.1; -; mRNA.
DR EMBL; BT008803; AAP68242.1; -; mRNA.
DR RefSeq; NP_001318840.1; NM_001345366.1.
DR RefSeq; NP_200775.2; NM_125359.4.
DR AlphaFoldDB; Q9FN94; -.
DR SMR; Q9FN94; -.
DR BioGRID; 21332; 38.
DR IntAct; Q9FN94; 37.
DR STRING; 3702.AT5G59670.1; -.
DR iPTMnet; Q9FN94; -.
DR PaxDb; Q9FN94; -.
DR PRIDE; Q9FN94; -.
DR ProteomicsDB; 228090; -.
DR EnsemblPlants; AT5G59670.1; AT5G59670.1; AT5G59670.
DR EnsemblPlants; AT5G59670.2; AT5G59670.2; AT5G59670.
DR GeneID; 836088; -.
DR Gramene; AT5G59670.1; AT5G59670.1; AT5G59670.
DR Gramene; AT5G59670.2; AT5G59670.2; AT5G59670.
DR KEGG; ath:AT5G59670; -.
DR Araport; AT5G59670; -.
DR TAIR; locus:2174294; AT5G59670.
DR eggNOG; ENOG502QQCZ; Eukaryota.
DR HOGENOM; CLU_000288_41_1_1; -.
DR InParanoid; Q9FN94; -.
DR OMA; PRTCNGG; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9FN94; -.
DR PRO; PR:Q9FN94; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FN94; baseline and differential.
DR Genevisible; Q9FN94; 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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF13855; LRR_8; 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; 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..22
FT /evidence="ECO:0000255"
FT CHAIN 23..868
FT /note="Receptor-like protein kinase At5g59670"
FT /id="PRO_0000380729"
FT TOPO_DOM 23..500
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 501..521
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 522..868
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 409..432
FT /note="LRR 1"
FT REPEAT 433..459
FT /note="LRR 2"
FT REPEAT 461..481
FT /note="LRR 3"
FT DOMAIN 564..834
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 689
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 570..578
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 592
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 555
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 637
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 723
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 724
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 729
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 372
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 405
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 416
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 423
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 445
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 464
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 471
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 868 AA; 97032 MW; 3A2C4E66C2BC582D CRC64;
MESSFGLLLA LLTLTIIHIV QAQDPQGFIS LDCGLPANET SPYTETQTGL LFSSDATFIQ
SGKTGRVQAN QESKFLKPYR TLRYFPEGVR NCYNLSVFKE RKYLIAASFL YGNYDGHNIA
PVFDLYLGPN LWAKIDLQDV NGTGEEILHI PTSNSLQICL VQTGETTPLI SSLELRPMRT
GSYTTVSGSL KTYRRLYFKK SGSRLRYSKD VYDRSWFPRF MDEWTQISTA LGVINTNIYQ
PPEDALKNAA TPTDASAPLT FKWNSEKLDV QYYFYAHYAE IQDLQANDTR EFNILLNGQN
LSVTGPEVPD KLSIKTFQSS SPISCNGWAC NFQLIRTKRS TLPPLLNALE VYTVIQFPRS
ETDESDVVAM KNISASYGLS RINWQGDPCF PQQLRWDALD CTNRNISQPP RITSLNLSSS
RLNGTIAAAI QSITQLETLD LSYNNLTGEV PEFLGKMKSL SVINLSGNNL NGSIPQALRK
KRLKLYLEGN PRLIKPPKKE FPVAIVTLVV FVTVIVVLFL VFRKKMSTIV KGLRLPPRTS
MVDVTFSNKK SKRFTYSEVV QVTKNFQRVL GKGGFGMVYH GTVKGSEQVA VKVLSQSSTQ
GSKEFKAEVD LLLRVHHTNL VSLVGYCCEG DYLALVYEFL PNGDLKQHLS GKGGNSIINW
SIRLRIALEA ALGLEYLHIG CTPPMVHRDV KTANILLDEN FKAKLADFGL SRSFQGEGES
QESTTIAGTL GYLDPECYHS GRLGEKSDVY SFGIVLLEMI TNQPVINQTS GDSHITQWVG
FQMNRGDILE IMDPNLRKDY NINSAWRALE LAMSCAYPSS SKRPSMSQVI HELKECIACE
NTGISKNRSL EYQEMNVSLD TTAVPMAR
