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Y5374_ARATH
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   03-AUG-2022, entry version 82.
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.AT5G37450.1; -.
DR   iPTMnet; C0LGU1; -.
DR   PRIDE; C0LGU1; -.
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   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: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; -; 3.
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   Pfam; PF13855; LRR_8; 1.
DR   Pfam; PF08263; LRRNT_2; 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; 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
 
 
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