Y2165_ARATH
ID Y2165_ARATH Reviewed; 915 AA.
AC C0LGK4; Q9SIX4;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Probable LRR receptor-like serine/threonine-protein kinase At2g16250;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At2g16250; ORFNames=F16F14.25;
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 C0LGK4; F4I065: At1g49100; NbExp=2; IntAct=EBI-16943030, EBI-20654598;
CC C0LGK4; Q9FN37: PSKR2; NbExp=2; IntAct=EBI-16943030, EBI-16902047;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I
CC membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD22312.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC007047; AAD22312.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC06478.1; -; Genomic_DNA.
DR EMBL; FJ708694; ACN59289.1; -; mRNA.
DR PIR; C84538; C84538.
DR RefSeq; NP_179220.2; NM_127181.3.
DR AlphaFoldDB; C0LGK4; -.
DR SMR; C0LGK4; -.
DR BioGRID; 1480; 53.
DR IntAct; C0LGK4; 46.
DR STRING; 3702.AT2G16250.1; -.
DR iPTMnet; C0LGK4; -.
DR PaxDb; C0LGK4; -.
DR PRIDE; C0LGK4; -.
DR ProteomicsDB; 243145; -.
DR EnsemblPlants; AT2G16250.1; AT2G16250.1; AT2G16250.
DR GeneID; 816121; -.
DR Gramene; AT2G16250.1; AT2G16250.1; AT2G16250.
DR KEGG; ath:AT2G16250; -.
DR Araport; AT2G16250; -.
DR TAIR; locus:2042599; AT2G16250.
DR eggNOG; ENOG502QR5S; Eukaryota.
DR HOGENOM; CLU_000288_22_6_1; -.
DR InParanoid; C0LGK4; -.
DR OMA; GIQCQNG; -.
DR OrthoDB; 193189at2759; -.
DR PhylomeDB; C0LGK4; -.
DR PRO; PR:C0LGK4; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; C0LGK4; baseline and differential.
DR Genevisible; C0LGK4; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
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; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00369; LRR_TYP; 6.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51450; LRR; 7.
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; Receptor; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..915
FT /note="Probable LRR receptor-like serine/threonine-protein
FT kinase At2g16250"
FT /id="PRO_0000387546"
FT TOPO_DOM 29..451
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 452..472
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 473..915
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 102..125
FT /note="LRR 1"
FT REPEAT 127..150
FT /note="LRR 2"
FT REPEAT 151..174
FT /note="LRR 3"
FT REPEAT 176..198
FT /note="LRR 4"
FT REPEAT 199..223
FT /note="LRR 5"
FT REPEAT 225..247
FT /note="LRR 6"
FT REPEAT 248..271
FT /note="LRR 7"
FT REPEAT 272..295
FT /note="LRR 8"
FT REPEAT 297..320
FT /note="LRR 9"
FT REPEAT 321..344
FT /note="LRR 10"
FT REPEAT 366..390
FT /note="LRR 11"
FT DOMAIN 527..811
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 482..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 851..915
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 870..899
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 657
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 533..541
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 555
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 101
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 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 429
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 437
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 915 AA; 99704 MW; 23AA507095888984 CRC64;
MVDQRRSALG FVLLLLCLVL FFDCVVVGQT QSRFSEKLIL LNLRSSLGLR GTDWPIKGDP
CVDWRGIQCE NGSIIGINIS GFRRTRIGKL NPQFSVDPLR NLTRLSYFNA SGLALPGTIP
EWFGVSLLAL EVLDLSSCSV NGVVPFTLGN LTSLRTLNLS QNSLTSLVPS SLGQLLNLSQ
LDLSRNSFTG VLPQSFSSLK NLLTLDVSSN YLTGPIPPGL GALSKLIHLN FSSNSFSSPI
PSELGDLVNL VDFDLSINSL SGSVPQELRK LSKLQLMAIG DNLLSGTLPV DLFSAESQLQ
TLVLRENGFS GSLPDVCWSL PKLRILDIAK NNFTGLLPYS SYDSDQIAEM VDISSNTFYG
ELTPILRRFR IMDLSGNYFE GKLPDYVTGE NVSVTSNCLR NERRQKPSAI CAAFYKSRGL
DFDDFGRPNL TQPTSKNASS GISRRTVIIL AAVGGGVAFI LLFVILPIIL VLCMRHRRRA
AQRGNNDRPK PAGEASQQPP KGAQTFDLSR LGNAFSYEQL LQATEEFNDA NLIKRGHSGN
LFRGFLENGI PVVIKKIDVR EGKSEGYISE LELFSKAGHQ RLVPFLGHCL ENESQKFLVY
KFMRHGDLAS SLFRKSENEG DGLKSLDWIT RLKIALGAAE GLSYLHHECS PPLVHRDVQA
SSILLDDKFE VRLGSLSEAY AQGDAYQSRI SRLLRLPQSS EPSSSGVTNA ICSYDVYCFG
KVLLELVTGK LGISSPDNAL AKEYMEEALP YISTNEKELV TKILDPSLMV DEDLLEEVWA
MAIIAKSCLN PKPTRRPLMR HIVNALENPL KVVREDTNSG SGSSRLRTNS SRGSWNAAIF
GSWRQSASDV TAVQAGATTS GGGGGGGGNG LRNSGSQGSS GRNNNNNGNS SSSRRRQSSE
IVPEPAAYGV VEDNL
