ID Y5457_ARATH Reviewed; 614 AA.
AC C0LGU5; Q9FK65;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 97.
DE RecName: Full=Probable LRR receptor-like serine/threonine-protein kinase At5g45780;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At5g45780; ORFNames=MRA19.22;
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=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
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 C0LGU5; A0A178WK49: At1g62950; NbExp=3; IntAct=EBI-16964970, EBI-20657508;
CC C0LGU5; C0LGH8: At1g63430; NbExp=3; IntAct=EBI-16964970, EBI-20657656;
CC C0LGU5; A0A178UAF6: AXX17_At5g67350; NbExp=2; IntAct=EBI-16964970, EBI-20661274;
CC C0LGU5; C0LGN2: LRR-RLK; NbExp=3; IntAct=EBI-16964970, EBI-20652801;
CC C0LGU5; O22178: LRR-RLK; NbExp=2; IntAct=EBI-16964970, EBI-20662530;
CC C0LGU5; Q9FZ59: PEPR2; NbExp=3; IntAct=EBI-16964970, EBI-20652612;
CC C0LGU5; Q9FN37: PSKR2; NbExp=3; IntAct=EBI-16964970, EBI-16902047;
CC C0LGU5; Q9C8M9: SRF6; NbExp=3; IntAct=EBI-16964970, EBI-16954301;
CC C0LGU5; P43298: TMK1; NbExp=3; IntAct=EBI-16964970, EBI-2023970;
CC C0LGU5; Q8GY50: VRLK1; NbExp=3; IntAct=EBI-16964970, EBI-20658163;
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=BAB09221.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB012245; BAB09221.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED95298.1; -; Genomic_DNA.
DR EMBL; FJ708789; ACN59380.1; -; mRNA.
DR RefSeq; NP_199390.2; NM_123946.4.
DR AlphaFoldDB; C0LGU5; -.
DR SMR; C0LGU5; -.
DR BioGRID; 19867; 82.
DR IntAct; C0LGU5; 90.
DR STRING; 3702.C0LGU5; -.
DR PaxDb; 3702-AT5G45780-1; -.
DR ProteomicsDB; 243019; -.
DR EnsemblPlants; AT5G45780.1; AT5G45780.1; AT5G45780.
DR GeneID; 834618; -.
DR Gramene; AT5G45780.1; AT5G45780.1; AT5G45780.
DR KEGG; ath:AT5G45780; -.
DR Araport; AT5G45780; -.
DR TAIR; AT5G45780; CIK4.
DR eggNOG; ENOG502QU0U; Eukaryota.
DR HOGENOM; CLU_000288_92_7_1; -.
DR InParanoid; C0LGU5; -.
DR OrthoDB; 460883at2759; -.
DR PhylomeDB; C0LGU5; -.
DR PRO; PR:C0LGU5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; C0LGU5; baseline and differential.
DR Genevisible; C0LGU5; AT.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0015026; F:coreceptor activity; IGI:TAIR.
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:0048653; P:anther development; IGI:TAIR.
DR GO; GO:0007639; P:homeostasis of number of meristem cells; IGI:TAIR.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
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; PTHR47988:SF83; OS02G0236100 PROTEIN; 1.
DR PANTHER; PTHR47988; SOMATIC EMBRYOGENESIS RECEPTOR KINASE 1; 1.
DR Pfam; PF00560; LRR_1; 3.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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..26
FT /evidence="ECO:0000255"
FT CHAIN 27..614
FT /note="Probable LRR receptor-like serine/threonine-protein
FT kinase At5g45780"
FT /id="PRO_0000387563"
FT TOPO_DOM 27..242
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 264..614
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 104..126
FT /note="LRR 1"
FT REPEAT 128..151
FT /note="LRR 2"
FT REPEAT 152..174
FT /note="LRR 3"
FT REPEAT 176..197
FT /note="LRR 4"
FT DOMAIN 300..576
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 426
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 306..314
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 328
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 297
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9LSI9"
FT MOD_RES 323
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94F62"
FT MOD_RES 380
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 459
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94F62"
FT MOD_RES 460
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94F62"
FT MOD_RES 465
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94F62"
FT MOD_RES 473
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 475
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 476
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 480
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 555
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 224
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 614 AA; 68206 MW; 3B2460D71C8CCE09 CRC64;
MEISLMKFLF LGIWVYYYSV LDSVSAMDSL LSPKGVNYEV AALMSVKNKM KDEKEVLSGW
DINSVDPCTW NMVGCSSEGF VVSLEMASKG LSGILSTSIG ELTHLHTLLL QNNQLTGPIP
SELGQLSELE TLDLSGNRFS GEIPASLGFL THLNYLRLSR NLLSGQVPHL VAGLSGLSFL
DLSFNNLSGP TPNISAKDYR IVGNAFLCGP ASQELCSDAT PVRNATGLSE KDNSKHHSLV
LSFAFGIVVA FIISLMFLFF WVLWHRSRLS RSHVQQDYEF EIGHLKRFSF REIQTATSNF
SPKNILGQGG FGMVYKGYLP NGTVVAVKRL KDPIYTGEVQ FQTEVEMIGL AVHRNLLRLF
GFCMTPEERM LVYPYMPNGS VADRLRDNYG EKPSLDWNRR ISIALGAARG LVYLHEQCNP
KIIHRDVKAA NILLDESFEA IVGDFGLAKL LDQRDSHVTT AVRGTIGHIA PEYLSTGQSS
EKTDVFGFGV LILELITGHK MIDQGNGQVR KGMILSWVRT LKAEKRFAEM VDRDLKGEFD
DLVLEEVVEL ALLCTQPHPN LRPRMSQVLK VLEGLVEQCE GGYEARAPSV SRNYSNGHEE
QSFIIEAIEL SGPR
//
