Y2242_ARATH
ID Y2242_ARATH Reviewed; 853 AA.
AC C0LGK9; Q8RWC6; Q9ZUH2;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Probable LRR receptor-like serine/threonine-protein kinase At2g24230;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At2g24230; ORFNames=F27D4.14;
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;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
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 C0LGK9; Q9SHI2: At1g17230; NbExp=3; IntAct=EBI-16965118, EBI-20651261;
CC C0LGK9; Q9SH71: At1g64210; NbExp=2; IntAct=EBI-16965118, EBI-20651385;
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=AAD03384.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC005967; AAD03384.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC07546.1; -; Genomic_DNA.
DR EMBL; AY093187; AAM13186.1; -; mRNA.
DR EMBL; FJ708699; ACN59294.1; -; mRNA.
DR PIR; B84634; B84634.
DR RefSeq; NP_850049.1; NM_179718.2.
DR AlphaFoldDB; C0LGK9; -.
DR SMR; C0LGK9; -.
DR BioGRID; 2309; 25.
DR IntAct; C0LGK9; 25.
DR STRING; 3702.AT2G24230.1; -.
DR PaxDb; C0LGK9; -.
DR PRIDE; C0LGK9; -.
DR ProteomicsDB; 242537; -.
DR EnsemblPlants; AT2G24230.1; AT2G24230.1; AT2G24230.
DR GeneID; 816957; -.
DR Gramene; AT2G24230.1; AT2G24230.1; AT2G24230.
DR KEGG; ath:AT2G24230; -.
DR Araport; AT2G24230; -.
DR TAIR; locus:2047530; AT2G24230.
DR eggNOG; ENOG502QTEF; Eukaryota.
DR HOGENOM; CLU_000288_22_1_1; -.
DR InParanoid; C0LGK9; -.
DR OMA; TLCASEI; -.
DR OrthoDB; 136642at2759; -.
DR PhylomeDB; C0LGK9; -.
DR PRO; PR:C0LGK9; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; C0LGK9; baseline and differential.
DR Genevisible; C0LGK9; 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; -; 2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 6.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51450; LRR; 10.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..853
FT /note="Probable LRR receptor-like serine/threonine-protein
FT kinase At2g24230"
FT /id="PRO_0000387548"
FT TOPO_DOM 24..456
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 457..477
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 478..853
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 91..114
FT /note="LRR 1"
FT REPEAT 116..138
FT /note="LRR 2"
FT REPEAT 139..162
FT /note="LRR 3"
FT REPEAT 163..186
FT /note="LRR 4"
FT REPEAT 188..210
FT /note="LRR 5"
FT REPEAT 212..234
FT /note="LRR 6"
FT REPEAT 235..257
FT /note="LRR 7"
FT REPEAT 259..280
FT /note="LRR 8"
FT REPEAT 281..304
FT /note="LRR 9"
FT REPEAT 305..328
FT /note="LRR 10"
FT REPEAT 329..352
FT /note="LRR 11"
FT REPEAT 354..374
FT /note="LRR 12"
FT REPEAT 375..398
FT /note="LRR 13"
FT REPEAT 400..421
FT /note="LRR 14"
FT DOMAIN 546..853
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 698
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 552..560
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 574
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 535
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 543
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 619
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 738
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 335
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 340
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 386
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 411
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 425
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 328
FT /note="L -> F (in Ref. 3; AAM13186)"
FT /evidence="ECO:0000305"
FT CONFLICT 360
FT /note="V -> I (in Ref. 3; AAM13186)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 853 AA; 94117 MW; 46069C829F9D0070 CRC64;
MGLGLGFWGY ALFLSLFLKQ SHCQEPNTDG FFVSEFYKQM GLSSSQAYNF SAPFCSWQGL
FCDSKNEHVI MLIASGMSLS GQIPDNTIGK LSKLQSLDLS NNKISALPSD FWSLNTLKNL
NLSFNKISGS FSSNVGNFGQ LELLDISYNN FSGAIPEAVD SLVSLRVLKL DHNGFQMSIP
RGLLGCQSLV SIDLSSNQLE GSLPDGFGSA FPKLETLSLA GNKIHGRDTD FADMKSISFL
NISGNQFDGS VTGVFKETLE VADLSKNRFQ GHISSQVDSN WFSLVYLDLS ENELSGVIKN
LTLLKKLKHL NLAWNRFNRG MFPRIEMLSG LEYLNLSNTN LSGHIPREIS KLSDLSTLDV
SGNHLAGHIP ILSIKNLVAI DVSRNNLTGE IPMSILEKLP WMERFNFSFN NLTFCSGKFS
AETLNRSFFG STNSCPIAAN PALFKRKRSV TGGLKLALAV TLSTMCLLIG ALIFVAFGCR
RKTKSGEAKD LSVKEEQSIS GPFSFQTDST TWVADVKQAN AVPVVIFEKP LLNITFSDLL
SATSNFDRDT LLADGKFGPV YRGFLPGGIH VAVKVLVHGS TLSDQEAARE LEFLGRIKHP
NLVPLTGYCI AGDQRIAIYE YMENGNLQNL LHDLPFGVQT TDDWTTDTWE EETDNGTQNI
GTEGPVATWR FRHKIALGTA RALAFLHHGC SPPIIHRDVK ASSVYLDQNW EPRLSDFGLA
KVFGNGLDDE IIHGSPGYLP PEFLQPEHEL PTPKSDVYCF GVVLFELMTG KKPIEDDYLD
EKDTNLVSWV RSLVRKNQAS KAIDPKIQET GSEEQMEEAL KIGYLCTADL PSKRPSMQQV
VGLLKDIEPK SNQ