Y3148_ARATH
ID Y3148_ARATH Reviewed; 1020 AA.
AC C0LGN2; Q94EW5; Q9LH71;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Probable leucine-rich repeat receptor-like serine/threonine-protein kinase At3g14840;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN Name=LRR-RLK; OrderedLocusNames=At3g14840; ORFNames=T21E2.2;
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
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] (ISOFORM 2).
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] (ISOFORM 1).
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).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RX PubMed=17644812; DOI=10.1074/mcp.m700099-mcp200;
RA Marmagne A., Ferro M., Meinnel T., Bruley C., Kuhn L., Garin J.,
RA Barbier-Brygoo H., Ephritikhine G.;
RT "A high content in lipid-modified peripheral proteins and integral receptor
RT kinases features in the arabidopsis plasma membrane proteome.";
RL Mol. Cell. Proteomics 6:1980-1996(2007).
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 C0LGN2; Q9SHI2: At1g17230; NbExp=3; IntAct=EBI-20652801, EBI-20651261;
CC C0LGN2; Q9LP24-3: At1g35710; NbExp=3; IntAct=EBI-20652801, EBI-20651291;
CC C0LGN2; C0LGJ9: At2g02780; NbExp=2; IntAct=EBI-20652801, EBI-20651541;
CC C0LGN2; C0LGU5: At5g45780; NbExp=3; IntAct=EBI-20652801, EBI-16964970;
CC C0LGN2; O65440-2: BAM3; NbExp=3; IntAct=EBI-20652801, EBI-20653325;
CC C0LGN2; Q9LP77: RKL1; NbExp=3; IntAct=EBI-20652801, EBI-1544507;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:17644812};
CC Single-pass type I membrane protein {ECO:0000305|PubMed:17644812}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=C0LGN2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=C0LGN2-2; Sequence=VSP_040160, VSP_040161;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB02650.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP002061; BAB02650.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE75573.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75574.1; -; Genomic_DNA.
DR EMBL; AF389296; AAK63868.1; -; mRNA.
DR EMBL; AY091678; AAM10277.1; -; mRNA.
DR EMBL; FJ708722; ACN59317.1; -; mRNA.
DR RefSeq; NP_188102.5; NM_112345.7. [C0LGN2-1]
DR RefSeq; NP_566494.1; NM_112346.4. [C0LGN2-2]
DR AlphaFoldDB; C0LGN2; -.
DR SMR; C0LGN2; -.
DR BioGRID; 6047; 37.
DR IntAct; C0LGN2; 38.
DR STRING; 3702.AT3G14840.2; -.
DR CAZy; CBM57; Carbohydrate-Binding Module Family 57.
DR iPTMnet; C0LGN2; -.
DR SwissPalm; C0LGN2; -.
DR PaxDb; C0LGN2; -.
DR PRIDE; C0LGN2; -.
DR ProteomicsDB; 242863; -. [C0LGN2-1]
DR EnsemblPlants; AT3G14840.1; AT3G14840.1; AT3G14840. [C0LGN2-2]
DR EnsemblPlants; AT3G14840.2; AT3G14840.2; AT3G14840. [C0LGN2-1]
DR GeneID; 820713; -.
DR Gramene; AT3G14840.1; AT3G14840.1; AT3G14840. [C0LGN2-2]
DR Gramene; AT3G14840.2; AT3G14840.2; AT3G14840. [C0LGN2-1]
DR KEGG; ath:AT3G14840; -.
DR Araport; AT3G14840; -.
DR TAIR; locus:2099352; AT3G14840.
DR eggNOG; ENOG502QVI9; Eukaryota.
DR HOGENOM; CLU_000288_114_2_1; -.
DR InParanoid; C0LGN2; -.
DR OMA; TICHVIH; -.
DR OrthoDB; 130579at2759; -.
DR PhylomeDB; C0LGN2; -.
DR PRO; PR:C0LGN2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; C0LGN2; baseline and differential.
DR Genevisible; C0LGN2; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IBA:GO_Central.
DR GO; GO:0009861; P:jasmonic acid and ethylene-dependent systemic resistance; IMP:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0045088; P:regulation of innate immune response; IMP:TAIR.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR021720; Malectin_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF11721; Malectin; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
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 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell membrane; Glycoprotein; Kinase;
KW Leucine-rich repeat; Membrane; Nucleotide-binding; Phosphoprotein;
KW Receptor; Reference proteome; Repeat; Serine/threonine-protein kinase;
KW Signal; Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..1020
FT /note="Probable leucine-rich repeat receptor-like
FT serine/threonine-protein kinase At3g14840"
FT /id="PRO_0000401333"
FT TOPO_DOM 27..614
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 615..635
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 636..1020
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 86..110
FT /note="LRR 1"
FT REPEAT 111..134
FT /note="LRR 2"
FT REPEAT 136..157
FT /note="LRR 3"
FT REPEAT 158..181
FT /note="LRR 4"
FT REPEAT 182..204
FT /note="LRR 5"
FT REPEAT 206..231
FT /note="LRR 6"
FT REPEAT 253..276
FT /note="LRR 7"
FT REPEAT 277..301
FT /note="LRR 8"
FT REPEAT 302..324
FT /note="LRR 9"
FT REPEAT 326..349
FT /note="LRR 10"
FT REPEAT 479..501
FT /note="LRR 11"
FT DOMAIN 672..949
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 798
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 678..686
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 700
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 745
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 831
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 832
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 837
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 845
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 359
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 389
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 461
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 469
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 498
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 92..112
FT /note="IVLKAQDLQGSLPTDLSGLPF -> MCVLLSFSTSYLFFVKIIINI (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_040160"
FT VAR_SEQ 113..1020
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_040161"
SQ SEQUENCE 1020 AA; 112277 MW; CEE5402B62B931B6 CRC64;
MSLNRQLLFT YYFIVSLILF SDFVSSATLP KEEVDALQSV ATALKKSNWN FSVDPCDETL
SEGGWRNPNA AKGFEDAVTC NCSSVICHVT NIVLKAQDLQ GSLPTDLSGL PFLQELDLTR
NYLNGSIPPE WGASSLLNIS LLGNRISGSI PKELGNLTTL SGLVLEYNQL SGKIPPELGN
LPNLKRLLLS SNNLSGEIPS TFAKLTTLTD LRISDNQFTG AIPDFIQNWK GLEKLVIQAS
GLVGPIPSAI GLLGTLTDLR ITDLSGPESP FPPLRNMTSM KYLILRNCNL TGDLPAYLGQ
NRKLKNLDLS FNKLSGPIPA TYSGLSDVDF IYFTSNMLNG QVPSWMVDQG DTIDITYNNF
SKDKTEECQQ KSVNTFSSTS PLVANNSSNV SCLSKYTCPK TFYGLHINCG GNEITSNETK
YDADTWDTPG YYDSKNGWVS SNTGNFLDDD RTNNGKSKWS NSSELKITNS SIDFRLYTQA
RLSAISLTYQ ALCLGKGNYT VNLHFAEIMF NEKNMYSNLG RRYFDIYVQG KREVKDFNIV
DEAKGVGKAV VKKFPVMVTN GKLEIRLQWA GKGTQAIPVR GVYGPLISAV SVDPDFIPPK
EPGTGTGGGS SVGTVVGSVI ASTVFLVLLI GGILWWRGCL RPKSQMEKDF KNLDFQISSF
SLRQIKVATD NFDPANKIGE GGFGPVHKGI MTDGTVIAVK QLSAKSKQGN REFLNEIAMI
SALQHPHLVK LYGCCVEGDQ LLLVYEYLEN NSLARALFGP QETQIPLNWP MRQKICVGIA
RGLAYLHEES RLKIVHRDIK ATNVLLDKEL NPKISDFGLA KLDEEENTHI STRVAGTYGY
MAPEYAMRGH LTDKADVYSF GVVALEIVHG KSNTSSRSKA DTFYLLDWVH VLREQNTLLE
VVDPRLGTDY NKQEALMMIQ IGMLCTSPAP GDRPSMSTVV SMLEGHSTVN VEKLLEASVN
NEKDEESVRA MKRHYATIGE EEITNTTTTD GPFTSSSTST ANANDLYPVK LDSAYWNTRT
