Y2239_ARATH
ID Y2239_ARATH Reviewed; 634 AA.
AC Q0WVM4; O82223; Q570Q6;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Probable LRR receptor-like serine/threonine-protein kinase At2g23950;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At2g23950; ORFNames=T29E15.15;
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;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 Q0WVM4; A0A178WLG7: At1g51790; NbExp=2; IntAct=EBI-20655099, EBI-20652336;
CC Q0WVM4; C0LGH8: At1g63430; NbExp=3; IntAct=EBI-20655099, EBI-20657656;
CC Q0WVM4; Q9C7T7: CEPR2; NbExp=2; IntAct=EBI-20655099, EBI-16955712;
CC Q0WVM4; O22178: LRR-RLK; NbExp=2; IntAct=EBI-20655099, EBI-20662530;
CC Q0WVM4; Q6R2J8: SRF8; NbExp=2; IntAct=EBI-20655099, EBI-16941202;
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=AAC63680.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC005170; AAC63680.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC07507.1; -; Genomic_DNA.
DR EMBL; AK220652; BAD95153.1; -; mRNA.
DR EMBL; AK226719; BAE98824.1; -; mRNA.
DR EMBL; FJ708698; ACN59293.1; -; mRNA.
DR PIR; G84630; G84630.
DR RefSeq; NP_179973.2; NM_127957.5.
DR AlphaFoldDB; Q0WVM4; -.
DR SMR; Q0WVM4; -.
DR BioGRID; 2280; 47.
DR IntAct; Q0WVM4; 49.
DR STRING; 3702.AT2G23950.1; -.
DR PaxDb; Q0WVM4; -.
DR PRIDE; Q0WVM4; -.
DR ProteomicsDB; 243099; -.
DR EnsemblPlants; AT2G23950.1; AT2G23950.1; AT2G23950.
DR GeneID; 816928; -.
DR Gramene; AT2G23950.1; AT2G23950.1; AT2G23950.
DR KEGG; ath:AT2G23950; -.
DR Araport; AT2G23950; -.
DR TAIR; locus:2061466; AT2G23950.
DR eggNOG; ENOG502QQXY; Eukaryota.
DR HOGENOM; CLU_000288_92_7_1; -.
DR InParanoid; Q0WVM4; -.
DR OMA; QHQKGVM; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q0WVM4; -.
DR PRO; PR:Q0WVM4; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q0WVM4; baseline and differential.
DR Genevisible; Q0WVM4; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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:1901653; P:cellular response to peptide; IMP:TAIR.
DR GO; GO:0007639; P:homeostasis of number of meristem cells; IGI:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
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; 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; PS51450; LRR; 4.
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..27
FT /evidence="ECO:0000255"
FT CHAIN 28..634
FT /note="Probable LRR receptor-like serine/threonine-protein
FT kinase At2g23950"
FT /id="PRO_0000387547"
FT TOPO_DOM 28..236
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 258..634
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 99..121
FT /note="LRR 1"
FT REPEAT 123..145
FT /note="LRR 2"
FT REPEAT 147..167
FT /note="LRR 3"
FT REPEAT 171..193
FT /note="LRR 4"
FT DOMAIN 299..554
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 422
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 305..313
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 327
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 296
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9LSI9"
FT MOD_RES 322
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 383
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LSI9"
FT MOD_RES 395
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 455
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94F62"
FT MOD_RES 456
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94F62"
FT MOD_RES 461
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94F62"
FT MOD_RES 469
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 471
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 472
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 476
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MOD_RES 551
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 634 AA; 69694 MW; A64A416DBD8AF607 CRC64;
MVVMKLITMK IFSVLLLLCF FVTCSLSSEP RNPEVEALIN IKNELHDPHG VFKNWDEFSV
DPCSWTMISC SSDNLVIGLG APSQSLSGTL SGSIGNLTNL RQVSLQNNNI SGKIPPEICS
LPKLQTLDLS NNRFSGEIPG SVNQLSNLQY LRLNNNSLSG PFPASLSQIP HLSFLDLSYN
NLRGPVPKFP ARTFNVAGNP LICKNSLPEI CSGSISASPL SVSLRSSSGR RTNILAVALG
VSLGFAVSVI LSLGFIWYRK KQRRLTMLRI SDKQEEGLLG LGNLRSFTFR ELHVATDGFS
SKSILGAGGF GNVYRGKFGD GTVVAVKRLK DVNGTSGNSQ FRTELEMISL AVHRNLLRLI
GYCASSSERL LVYPYMSNGS VASRLKAKPA LDWNTRKKIA IGAARGLFYL HEQCDPKIIH
RDVKAANILL DEYFEAVVGD FGLAKLLNHE DSHVTTAVRG TVGHIAPEYL STGQSSEKTD
VFGFGILLLE LITGMRALEF GKSVSQKGAM LEWVRKLHKE MKVEELVDRE LGTTYDRIEV
GEMLQVALLC TQFLPAHRPK MSEVVQMLEG DGLAERWAAS HDHSHFYHAN MSYRTITSTD
GNNQTKHLFG SSGFEDEDDN QALDSFAMEL SGPR
