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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
 
 
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