Y5182_ARATH
ID Y5182_ARATH Reviewed; 885 AA.
AC C0LGG3; Q9C8I9; Q9FZB7;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Probable LRR receptor-like serine/threonine-protein kinase At1g51820;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At1g51820; ORFNames=F19C24.23, T14L22.3;
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;
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].
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).
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 C0LGG3; A0A178VQN9: At2g42290; NbExp=2; IntAct=EBI-17066817, EBI-20655829;
CC C0LGG3; A0A178UFM8: AXX17_At5g50380; NbExp=3; IntAct=EBI-17066817, EBI-20653342;
CC C0LGG3; Q9SYQ8: CLV1; NbExp=3; IntAct=EBI-17066817, EBI-1646111;
CC C0LGG3; Q9FRI1: LRR-RLK; NbExp=3; IntAct=EBI-17066817, EBI-17071528;
CC C0LGG3; Q9LZV7: PXC2; NbExp=3; IntAct=EBI-17066817, EBI-1238200;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF99853.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG50887.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC015448; AAF99853.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC025294; AAG50887.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE32721.1; -; Genomic_DNA.
DR EMBL; FJ708652; ACN59248.1; -; mRNA.
DR PIR; E96557; E96557.
DR RefSeq; NP_175594.2; NM_104062.3.
DR AlphaFoldDB; C0LGG3; -.
DR SMR; C0LGG3; -.
DR BioGRID; 26834; 27.
DR IntAct; C0LGG3; 32.
DR STRING; 3702.AT1G51820.1; -.
DR PaxDb; C0LGG3; -.
DR PRIDE; C0LGG3; -.
DR ProteomicsDB; 243012; -.
DR EnsemblPlants; AT1G51820.1; AT1G51820.1; AT1G51820.
DR GeneID; 841609; -.
DR Gramene; AT1G51820.1; AT1G51820.1; AT1G51820.
DR KEGG; ath:AT1G51820; -.
DR Araport; AT1G51820; -.
DR TAIR; locus:2017647; AT1G51820.
DR eggNOG; ENOG502QQCZ; Eukaryota.
DR HOGENOM; CLU_000288_41_1_1; -.
DR InParanoid; C0LGG3; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; C0LGG3; -.
DR PRO; PR:C0LGG3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; C0LGG3; baseline and differential.
DR Genevisible; C0LGG3; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0006468; P:protein phosphorylation; IEA:InterPro.
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; 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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..885
FT /note="Probable LRR receptor-like serine/threonine-protein
FT kinase At1g51820"
FT /id="PRO_0000387528"
FT TOPO_DOM 21..509
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 510..530
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 531..885
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 403..424
FT /note="LRR 1"
FT REPEAT 427..447
FT /note="LRR 2"
FT REPEAT 451..473
FT /note="LRR 3"
FT DOMAIN 578..851
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 703
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 584..592
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 606
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 651
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 737
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 738
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 743
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 751
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 22
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 281
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 424
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 437
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 456
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 461
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 885 AA; 98098 MW; B58500016F524685 CRC64;
MERHFVFIAT YLLIFHLVQA QNQTGFISVD CGLSLLESPY DAPQTGLTYT SDADLVASGK
TGRLAKEFEP LVDKPTLTLR YFPEGVRNCY NLNVTSDTNY LIKATFVYGN YDGLNVGPNF
NLYLGPNLWT TVSSNDTIEE IILVTRSNSL QVCLVKTGIS IPFINMLELR PMKKNMYVTQ
SGSLKYLFRG YISNSSTRIR FPDDVYDRKW YPLFDDSWTQ VTTNLKVNTS ITYELPQSVM
AKAATPIKAN DTLNITWTVE PPTTQFYSYV HIAEIQALRA NETREFNVTL NGEYTFGPFS
PIPLKTASIV DLSPGQCDGG RCILQVVKTL KSTLPPLLNA IEAFTVIDFP QMETNENDVA
GIKNVQGTYG LSRISWQGDP CVPKQLLWDG LNCKNSDIST PPIITSLDLS SSGLTGIITQ
AIKNLTHLQI LDLSDNNLTG EVPEFLADIK SLLVINLSGN NLSGSVPPSL LQKKGMKLNV
EGNPHILCTT GSCVKKKEDG HKKKSVIVPV VASIASIAVL IGALVLFLIL RKKRSPKVEG
PPPSYMQASD GRLPRSSEPA IVTKNRRFSY SQVVIMTNNF QRILGKGGFG MVYHGFVNGT
EQVAVKILSH SSSQGYKQFK AEVELLLRVH HKNLVGLVGY CDEGDNLALI YEYMANGDLK
EHMSGTRNRF ILNWGTRLKI VIESAQGLEY LHNGCKPPMV HRDVKTTNIL LNEHFEAKLA
DFGLSRSFLI EGETHVSTVV AGTPGYLDPE YHRTNWLTEK SDVYSFGILL LEIITNRHVI
DQSREKPHIG EWVGVMLTKG DIQSIMDPSL NEDYDSGSVW KAVELAMSCL NHSSARRPTM
SQVVIELNEC LASENARGGA SRDMESKSSI EVSLTFGTEV SPNAR
