Y2317_ARATH
ID Y2317_ARATH Reviewed; 1124 AA.
AC O49318;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Probable leucine-rich repeat receptor-like protein kinase At2g33170;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At2g33170; ORFNames=F25I18.9;
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 -!- 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}.
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DR EMBL; AC002334; AAC04906.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08793.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM61424.1; -; Genomic_DNA.
DR EMBL; FJ708708; ACN59303.1; -; mRNA.
DR PIR; B84742; B84742.
DR RefSeq; NP_001323641.1; NM_001336424.1.
DR RefSeq; NP_180875.1; NM_128876.4.
DR AlphaFoldDB; O49318; -.
DR SMR; O49318; -.
DR BioGRID; 3225; 7.
DR IntAct; O49318; 5.
DR STRING; 3702.AT2G33170.1; -.
DR PaxDb; O49318; -.
DR PRIDE; O49318; -.
DR ProteomicsDB; 243063; -.
DR EnsemblPlants; AT2G33170.1; AT2G33170.1; AT2G33170.
DR EnsemblPlants; AT2G33170.2; AT2G33170.2; AT2G33170.
DR GeneID; 817878; -.
DR Gramene; AT2G33170.1; AT2G33170.1; AT2G33170.
DR Gramene; AT2G33170.2; AT2G33170.2; AT2G33170.
DR KEGG; ath:AT2G33170; -.
DR Araport; AT2G33170; -.
DR TAIR; locus:2046525; AT2G33170.
DR eggNOG; ENOG502QPT1; Eukaryota.
DR HOGENOM; CLU_000288_22_1_1; -.
DR InParanoid; O49318; -.
DR OMA; PLKDDTR; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; O49318; -.
DR PRO; PR:O49318; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O49318; baseline and differential.
DR Genevisible; O49318; 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: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; -; 5.
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; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 13.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript 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..32
FT /evidence="ECO:0000255"
FT CHAIN 33..1124
FT /note="Probable leucine-rich repeat receptor-like protein
FT kinase At2g33170"
FT /id="PRO_0000389453"
FT TOPO_DOM 33..752
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 753..773
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 774..1124
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 86..109
FT /note="LRR 1"
FT REPEAT 110..132
FT /note="LRR 2"
FT REPEAT 134..156
FT /note="LRR 3"
FT REPEAT 158..180
FT /note="LRR 4"
FT REPEAT 182..205
FT /note="LRR 5"
FT REPEAT 206..228
FT /note="LRR 6"
FT REPEAT 230..252
FT /note="LRR 7"
FT REPEAT 254..277
FT /note="LRR 8"
FT REPEAT 278..300
FT /note="LRR 9"
FT REPEAT 302..325
FT /note="LRR 10"
FT REPEAT 326..348
FT /note="LRR 11"
FT REPEAT 350..371
FT /note="LRR 12"
FT REPEAT 374..397
FT /note="LRR 13"
FT REPEAT 398..420
FT /note="LRR 14"
FT REPEAT 422..444
FT /note="LRR 15"
FT REPEAT 446..468
FT /note="LRR 16"
FT REPEAT 470..491
FT /note="LRR 17"
FT REPEAT 494..516
FT /note="LRR 18"
FT REPEAT 518..540
FT /note="LRR 19"
FT REPEAT 542..564
FT /note="LRR 20"
FT REPEAT 566..588
FT /note="LRR 21"
FT REPEAT 590..613
FT /note="LRR 22"
FT REPEAT 614..636
FT /note="LRR 23"
FT REPEAT 638..661
FT /note="LRR 24"
FT REPEAT 663..686
FT /note="LRR 25"
FT REPEAT 687..709
FT /note="LRR 26"
FT DOMAIN 819..1100
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 952
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 825..833
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 847
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 808
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 816
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 901
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 939
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 986
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT MOD_RES 994
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 1001
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT MOD_RES 1002
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 314
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 395
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 494
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 547
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 611
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 644
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 684
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 692
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 697
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 710
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1124 AA; 123723 MW; 53018CD2E5966777 CRC64;
MGWWIFEFKK ESKSMFVGVL FLLTLLVWTS ESLNSDGQFL LELKNRGFQD SLNRLHNWNG
IDETPCNWIG VNCSSQGSSS SSNSLVVTSL DLSSMNLSGI VSPSIGGLVN LVYLNLAYNA
LTGDIPREIG NCSKLEVMFL NNNQFGGSIP VEINKLSQLR SFNICNNKLS GPLPEEIGDL
YNLEELVAYT NNLTGPLPRS LGNLNKLTTF RAGQNDFSGN IPTEIGKCLN LKLLGLAQNF
ISGELPKEIG MLVKLQEVIL WQNKFSGFIP KDIGNLTSLE TLALYGNSLV GPIPSEIGNM
KSLKKLYLYQ NQLNGTIPKE LGKLSKVMEI DFSENLLSGE IPVELSKISE LRLLYLFQNK
LTGIIPNELS KLRNLAKLDL SINSLTGPIP PGFQNLTSMR QLQLFHNSLS GVIPQGLGLY
SPLWVVDFSE NQLSGKIPPF ICQQSNLILL NLGSNRIFGN IPPGVLRCKS LLQLRVVGNR
LTGQFPTELC KLVNLSAIEL DQNRFSGPLP PEIGTCQKLQ RLHLAANQFS SNLPNEISKL
SNLVTFNVSS NSLTGPIPSE IANCKMLQRL DLSRNSFIGS LPPELGSLHQ LEILRLSENR
FSGNIPFTIG NLTHLTELQM GGNLFSGSIP PQLGLLSSLQ IAMNLSYNDF SGEIPPEIGN
LHLLMYLSLN NNHLSGEIPT TFENLSSLLG CNFSYNNLTG QLPHTQIFQN MTLTSFLGNK
GLCGGHLRSC DPSHSSWPHI SSLKAGSARR GRIIIIVSSV IGGISLLLIA IVVHFLRNPV
EPTAPYVHDK EPFFQESDIY FVPKERFTVK DILEATKGFH DSYIVGRGAC GTVYKAVMPS
GKTIAVKKLE SNREGNNNNS NNTDNSFRAE ILTLGKIRHR NIVRLYSFCY HQGSNSNLLL
YEYMSRGSLG ELLHGGKSHS MDWPTRFAIA LGAAEGLAYL HHDCKPRIIH RDIKSNNILI
DENFEAHVGD FGLAKVIDMP LSKSVSAVAG SYGYIAPEYA YTMKVTEKCD IYSFGVVLLE
LLTGKAPVQP LEQGGDLATW TRNHIRDHSL TSEILDPYLT KVEDDVILNH MITVTKIAVL
CTKSSPSDRP TMREVVLMLI ESGERAGKVI VSTTCSDLPP PAPP
