Y5189_ARATH
ID Y5189_ARATH Reviewed; 876 AA.
AC C0LGG6; Q9FZB0;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 2.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Probable LRR receptor-like protein kinase At1g51890;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At1g51890; ORFNames=T14L22.10;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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 INDUCTION BY PATHOGENS.
RX PubMed=16678099; DOI=10.1016/j.cell.2006.02.047;
RA He P., Shan L., Lin N.-C., Martin G.B., Kemmerling B., Nuemberger T.,
RA Sheen J.;
RT "Specific bacterial suppressors of MAMP signaling upstream of MAPKKK in
RT Arabidopsis innate immunity.";
RL Cell 125:563-575(2006).
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 -!- INTERACTION:
CC C0LGG6-2; Q9M9C5: At1g68400; NbExp=2; IntAct=EBI-20655952, EBI-1238661;
CC C0LGG6-2; Q9M8T0: At3g02880; NbExp=2; IntAct=EBI-20655952, EBI-1238677;
CC C0LGG6-2; Q9C9Y8: At3g08680; NbExp=2; IntAct=EBI-20655952, EBI-16955024;
CC C0LGG6-2; A0A1I9LQ53: At3g50230; NbExp=2; IntAct=EBI-20655952, EBI-20654045;
CC C0LGG6-2; O22138: LRR-RLK; NbExp=2; IntAct=EBI-20655952, EBI-16946020;
CC C0LGG6-2; Q9C9E4: LRR-RLK; NbExp=2; IntAct=EBI-20655952, EBI-20654777;
CC C0LGG6-2; Q9LVI6: RLK902; NbExp=2; IntAct=EBI-20655952, EBI-1626936;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=C0LGG6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=C0LGG6-2; Sequence=VSP_038493;
CC -!- INDUCTION: Transiently by pathogenic bacteria Pseudomonas syringae.
CC Faster level reduction following induction by treatment with the
CC virulent compatible DC3000 strain than with avirulent incompatible
CC strains. {ECO:0000269|PubMed:16678099}.
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; AC015448; AAF99859.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32729.1; -; Genomic_DNA.
DR EMBL; FJ708655; ACN59251.1; -; mRNA.
DR PIR; D96558; D96558.
DR RefSeq; NP_175601.2; NM_104069.3. [C0LGG6-1]
DR AlphaFoldDB; C0LGG6; -.
DR SMR; C0LGG6; -.
DR BioGRID; 26841; 30.
DR IntAct; C0LGG6; 37.
DR STRING; 3702.AT1G51890.1; -.
DR iPTMnet; C0LGG6; -.
DR PaxDb; C0LGG6; -.
DR PRIDE; C0LGG6; -.
DR ProteomicsDB; 243108; -. [C0LGG6-1]
DR EnsemblPlants; AT1G51890.1; AT1G51890.1; AT1G51890. [C0LGG6-1]
DR GeneID; 841616; -.
DR Gramene; AT1G51890.1; AT1G51890.1; AT1G51890. [C0LGG6-1]
DR KEGG; ath:AT1G51890; -.
DR Araport; AT1G51890; -.
DR TAIR; locus:2195845; AT1G51890.
DR HOGENOM; CLU_000288_41_1_1; -.
DR InParanoid; C0LGG6; -.
DR PRO; PR:C0LGG6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; C0LGG6; baseline and differential.
DR Genevisible; C0LGG6; 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:0042742; P:defense response to bacterium; IEP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR025875; Leu-rich_rpt_4.
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; PF12799; LRR_4; 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 Alternative splicing; ATP-binding; Cell membrane; Glycoprotein; Kinase;
KW Leucine-rich repeat; Membrane; Nucleotide-binding; Phosphoprotein;
KW Receptor; Reference proteome; Repeat; Serine/threonine-protein kinase;
KW Signal; Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..876
FT /note="Probable LRR receptor-like protein kinase At1g51890"
FT /id="PRO_0000387529"
FT TOPO_DOM 20..500
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 501..521
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 522..872
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 407..430
FT /note="LRR 1"
FT REPEAT 431..453
FT /note="LRR 2"
FT REPEAT 455..476
FT /note="LRR 3"
FT DOMAIN 570..842
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 694
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 576..584
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 597
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 561
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 642
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 729
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 734
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 742
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 335
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 412
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 455
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 460
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 481
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 494
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 416..463
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:20064227"
FT /id="VSP_038493"
SQ SEQUENCE 876 AA; 98563 MW; 933596B8C2C055FD CRC64;
MRFLSFLIFV FAVLGLVQAQ DQSGFISLDC GLVPTEITYV EKSTNITYRS DATYIDSGVP
GKINEVYRTQ FQQQIWALRS FPEGQRNCYN FSLTAKRKYL IRGTFIYGNY DGLNQLPSFD
LYIGPNKWTS VSIPGVRNGS VSEMIHVLRQ DHLQICLVKT GETTPFISSL ELRPLNNNTY
VTKSGSLIVV ARLYFSPTPP FLRYDEDVHD RIWIPFLDNK NSLLSTELSV DTSNFYNVPQ
TVAKTAAVPL NATQPLKINW SLDDITSQSY IYMHFAEIEN LEANETREFN ITYNGGENWF
SYFRPPKFRI TTVYNPAAVS SLDGNFNFTF SMTGNSTHPP LINGLEIYQV LELPQLDTYQ
DEVSAMMNIK TIYGLSKRSS WQGDPCAPEL YRWEGLNCSY PNFAPPQIIS LNLSGSNLSG
TITSDISKLT HLRELDLSNN DLSGDIPFVF SDMKNLTLIN LSGNKNLNRS VPETLQKRID
NKSLTLIRDE TGKNSTNVVA IAASVASVFA VLVILAIVFV VIRKKQRTNE ASGPRSFTTG
TVKSDARSSS SSIITKERKF TYSEVLKMTK NFERVLGKGG FGTVYHGNLD DTQVAVKMLS
HSSAQGYKEF KAEVELLLRV HHRHLVGLVG YCDDGDNLAL IYEYMEKGDL RENMSGKHSV
NVLSWETRMQ IAVEAAQGLE YLHNGCRPPM VHRDVKPTNI LLNERSQAKL ADFGLSRSFP
VDGESHVMTV VAGTPGYLDP EYYRTNWLSE KSDVYSFGVV LLEIVTNQPV MNKNRERPHI
NEWVMFMLTN GDIKSIVDPK LNEDYDTNGV WKVVELALAC VNPSSSRRPT MPHVVMELNE
CLALEIERKQ GSQATYIKES VEFSPSSASD FSPLAR
