ID Y2289_ARATH Reviewed; 880 AA.
AC C0LGL4; O81066;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE RecName: Full=Probable LRR receptor-like serine/threonine-protein kinase At2g28960;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At2g28960; ORFNames=T9I4.4;
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=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 C0LGL4; C0LGE4: At1g12460; NbExp=3; IntAct=EBI-16946048, EBI-17126713;
CC C0LGL4; Q9LRT1: At3g28040; NbExp=2; IntAct=EBI-16946048, EBI-16956175;
CC C0LGL4; C0LGR6: At4g29180; NbExp=2; IntAct=EBI-16946048, EBI-20654480;
CC C0LGL4; C0LGS2: At4g36180; NbExp=2; IntAct=EBI-16946048, EBI-16955302;
CC C0LGL4; C0LGS3: At4g37250; NbExp=2; IntAct=EBI-16946048, EBI-16955335;
CC C0LGL4; Q0WR59: At5g10020; NbExp=2; IntAct=EBI-16946048, EBI-16945916;
CC C0LGL4; C0LGQ9: GHR1; NbExp=2; IntAct=EBI-16946048, EBI-16939160;
CC C0LGL4; Q9FRI1: LRR-RLK; NbExp=3; IntAct=EBI-16946048, EBI-17071528;
CC C0LGL4; Q93ZS4: NIK3; NbExp=2; IntAct=EBI-16946048, EBI-17121474;
CC C0LGL4; Q9LZV7: PXC2; NbExp=2; IntAct=EBI-16946048, EBI-1238200;
CC C0LGL4; P43298: TMK1; NbExp=2; IntAct=EBI-16946048, EBI-2023970;
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=AAC33224.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC005315; AAC33224.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; ANM62343.1; -; Genomic_DNA.
DR EMBL; FJ708704; ACN59299.1; -; mRNA.
DR PIR; T02728; T02728.
DR RefSeq; NP_180462.2; NM_128455.3.
DR AlphaFoldDB; C0LGL4; -.
DR SMR; C0LGL4; -.
DR BioGRID; 2795; 80.
DR IntAct; C0LGL4; 80.
DR STRING; 3702.C0LGL4; -.
DR PaxDb; 3702-AT2G28960-1; -.
DR ProteomicsDB; 243101; -.
DR EnsemblPlants; AT2G28960.2; AT2G28960.2; AT2G28960.
DR GeneID; 817445; -.
DR Gramene; AT2G28960.2; AT2G28960.2; AT2G28960.
DR KEGG; ath:AT2G28960; -.
DR Araport; AT2G28960; -.
DR TAIR; AT2G28960; -.
DR eggNOG; ENOG502QQCZ; Eukaryota.
DR HOGENOM; CLU_000288_41_1_1; -.
DR InParanoid; C0LGL4; -.
DR OrthoDB; 673883at2759; -.
DR PhylomeDB; C0LGL4; -.
DR PRO; PR:C0LGL4; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; C0LGL4; baseline and differential.
DR Genevisible; C0LGL4; AT.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd14066; STKc_IRAK; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
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; IPR024788; Malectin-like_Carb-bd_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR45631; OS07G0107800 PROTEIN-RELATED; 1.
DR PANTHER; PTHR45631:SF133; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF12819; Malectin_like; 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; Phosphoprotein; 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..880
FT /note="Probable LRR receptor-like serine/threonine-protein
FT kinase At2g28960"
FT /id="PRO_0000387550"
FT TOPO_DOM 25..511
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 512..532
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 533..880
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 409..430
FT /note="LRR 1"
FT REPEAT 433..455
FT /note="LRR 2"
FT REPEAT 457..476
FT /note="LRR 3"
FT DOMAIN 573..846
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 854..880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 862..880
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 698
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 579..587
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 601
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 564
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 646
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 732
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 733
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 738
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 746
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 403
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 430
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 441
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 505
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 880 AA; 98965 MW; 3D50E57749FA8D23 CRC64;
MEGRRQRLLV FIFGALAITH LVQAQPPDQR GFISLDCGLP VNESPYTDPR TGLTFSSDAD
FILSGLRGEA GDDNTYIYRQ YKDLRYFPDG IRNCYNLKVE QGINYLIRAG FGYGNYDGLN
VYPKFDLHVG PNMWIAVDLE FGKDREIIYM TTSNLLQICL VKTGSTIPMI STLELRPLRN
DSYLTQFGPL DLIYRRAYSS NSTGFIRYPD DIFDRKWDRY NEFETDVNTT LNVRSSSPFQ
VPEAVSRMGI TPENASLPLR FYVSLDDDSD KVNVYFHFAE IQALRGNETR EFDIELEEDI
IQSAYSPTML QSDTKYNLSP HKCSSGLCYL KLVRTPRSTL PPLISAIEAF KVVDFPYAET
NPNDVAAMKD IEAFYGLKMI SWQGDPCVPE LLKWEDLKCS YTNKSTPPRI ISLDLSSRGL
KGVIAPAFQN LTELRKLDLS NNSFTGGVPE FLASMKSLSI INLNWNDLTG PLPKLLLDRE
KNGLKLTIQG NPKLCNDASC KNNNNQTYIV PVVASVASVL IIIAVLILIL VFKKRRPTQV
DSLPTVQHGL PNRPSIFTQT KRFTYSEVEA LTDNFERVLG EGGFGVVYHG ILNGTQPIAV
KLLSQSSVQG YKEFKAEVEL LLRVHHVNLV SLVGYCDEES NLALLYEYAP NGDLKQHLSG
ERGGSPLKWS SRLKIVVETA QGLEYLHTGC KPPMVHRDVK TTNILLDEHF QAKLADFGLS
RSFPVGGETH VSTAVAGTPG YLDPEYYRTN RLNEKSDVYS FGIVLLEIIT SRPVIQQTRE
KPHIAAWVGY MLTKGDIENV VDPRLNRDYE PTSVWKALEI AMSCVNPSSE KRPTMSQVTN
ELKQCLTLEN SKRGVREDMG SRSSVEMSTS FTTEINPKAR
//
