ID Y5374_ARATH Reviewed; 959 AA.
AC C0LGU1; F4K767; Q9FG43;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 89.
DE RecName: Full=Probable LRR receptor-like serine/threonine-protein kinase At5g37450;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At5g37450; ORFNames=T25O11.15;
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;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
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 C0LGU1; C0LGJ9: At2g02780; NbExp=2; IntAct=EBI-20661217, EBI-20651541;
CC C0LGU1; Q8W4S5: At5g63710; NbExp=3; IntAct=EBI-20661217, EBI-16934827;
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=AED94189.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAB10966.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP000607; BAB10966.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED94189.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; ANM71165.1; -; Genomic_DNA.
DR EMBL; FJ708785; ACN59376.1; -; mRNA.
DR RefSeq; NP_001332713.1; NM_001344198.1.
DR RefSeq; NP_198561.1; NM_123104.1.
DR AlphaFoldDB; C0LGU1; -.
DR SMR; C0LGU1; -.
DR BioGRID; 18973; 16.
DR IntAct; C0LGU1; 18.
DR STRING; 3702.C0LGU1; -.
DR iPTMnet; C0LGU1; -.
DR PaxDb; 3702-AT5G37450-1; -.
DR ProteomicsDB; 242833; -.
DR EnsemblPlants; AT5G37450.3; AT5G37450.3; AT5G37450.
DR GeneID; 833722; -.
DR Gramene; AT5G37450.3; AT5G37450.3; AT5G37450.
DR KEGG; ath:AT5G37450; -.
DR Araport; AT5G37450; -.
DR TAIR; AT5G37450; -.
DR eggNOG; ENOG502QTAM; Eukaryota.
DR InParanoid; C0LGU1; -.
DR OMA; LNIARFC; -.
DR PhylomeDB; C0LGU1; -.
DR PRO; PR:C0LGU1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; C0LGU1; baseline and differential.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14066; STKc_IRAK; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 3.
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; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR45974:SF23; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR45974; RECEPTOR-LIKE PROTEIN 55; 1.
DR Pfam; PF00560; LRR_1; 4.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 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; Receptor; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..959
FT /note="Probable LRR receptor-like serine/threonine-protein
FT kinase At5g37450"
FT /id="PRO_0000387562"
FT TOPO_DOM 25..565
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 566..586
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 587..959
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 79..100
FT /note="LRR 1"
FT REPEAT 101..124
FT /note="LRR 2"
FT REPEAT 125..148
FT /note="LRR 3"
FT REPEAT 149..172
FT /note="LRR 4"
FT REPEAT 173..198
FT /note="LRR 5"
FT REPEAT 200..220
FT /note="LRR 6"
FT REPEAT 221..244
FT /note="LRR 7"
FT REPEAT 246..268
FT /note="LRR 8"
FT REPEAT 269..292
FT /note="LRR 9"
FT REPEAT 294..314
FT /note="LRR 10"
FT REPEAT 315..338
FT /note="LRR 11"
FT REPEAT 341..366
FT /note="LRR 12"
FT DOMAIN 631..906
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 755
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 637..645
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 659
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 311
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 358
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 369
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 510
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 959 AA; 106058 MW; 697F74DC06B3277E CRC64;
MKEMMGVVGI ILVVSSCCLS LLDAQEITHP TDVSALQYVH RKLKDPLNHL QDWKKTDPCA
SNWTGVICIP DPSDGFLHVK ELRLLNMNLT GQLAPELGLL SNLTILNFMW NDLTGQIPPE
LGNLTHLIFL LLSGNQLTGS LPQELGSLSN LLILQIDYNE ISGKLPTSLA NLKKLKHFHM
NNNSITGQIP PEYSTLTNVL HFLMDNNKLT GNLPPELAQM PSLRILQLDG SNFDGTEIPS
SYGSIPNLVK LSLRNCNLEG PIPDLSKSLV LYYLDISSNK LTGEIPKNKF SANITTINLY
NNLLSGSIPS NFSGLPRLQR LQVQNNNLSG EIPVIWENRI LKAEEKLILD LRNNMFSNVS
SVLLNPPSNV TVKLYGNPVC ANVNAGKLAD LCGISTLEVE SPATSSETIS TGDCKRQSCP
VSENYDYVIG SPVACFCAAP LGIDLRLRSP SFSDFRPYKV SYMLDVASPK NLGINPYQIS
IDTFAWQSGP RLFMNMKIFP EYSELNSKFN STEVQRIVDF FATFTLNTDD SLGPYEIISI
NTGAYKDVTI IFPKKSGMSI GVSVGIIIGA IAFFLVLSSL ALVFFIKRSK RKRKTREVDM
EQEHPLPKPP MNMESVKGYN FTELDSATSS FSDLSQIGRG GYGKVYKGHL PGGLVVAVKR
AEQGSLQGQK EFFTEIELLS RLHHRNLVSL LGYCDQKGEQ MLVYEYMPNG SLQDALSARF
RQPLSLALRL RIALGSARGI LYLHTEADPP IIHRDIKPSN ILLDSKMNPK VADFGISKLI
ALDGGGVQRD HVTTIVKGTP GYVDPEYYLS HRLTEKSDVY SLGIVFLEIL TGMRPISHGR
NIVREVNEAC DAGMMMSVID RSMGQYSEEC VKRFMELAIR CCQDNPEARP WMLEIVRELE
NIYGLIPKEE KPYSSPSVQS SASGMSGFAV ASPRSSYTTF SEFTANQLVS GVIPSIAPR
//
