Y5343_ARATH
ID Y5343_ARATH Reviewed; 1038 AA.
AC C0LGG8; F4HRH3; Q8H7G0; Q9LPF9;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Probable LRR receptor-like serine/threonine-protein kinase At1g53430;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At1g53430; ORFNames=T3F20.25;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-182 (ISOFORM 1).
RA Stracke R., Palme K.;
RT "Signal peptide selection derived cDNAs from Arabidopsis thaliana leaves
RT and guard cells.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
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 C0LGG8; A0A1I9LQ53: At3g50230; NbExp=2; IntAct=EBI-20656135, EBI-20654045;
CC C0LGG8; Q9LVI6: RLK902; NbExp=2; IntAct=EBI-20656135, EBI-1626936;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I
CC membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=C0LGG8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=C0LGG8-2; Sequence=VSP_038281, VSP_038282;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF78446.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC018748; AAF78446.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE32939.2; -; Genomic_DNA.
DR EMBL; FJ708657; ACN59253.1; -; mRNA.
DR EMBL; AF083693; AAN60252.1; -; mRNA.
DR PIR; C96574; C96574.
DR RefSeq; NP_001319214.1; NM_001333594.1. [C0LGG8-1]
DR AlphaFoldDB; C0LGG8; -.
DR SMR; C0LGG8; -.
DR BioGRID; 27003; 17.
DR IntAct; C0LGG8; 18.
DR STRING; 3702.AT1G53430.1; -.
DR iPTMnet; C0LGG8; -.
DR PaxDb; C0LGG8; -.
DR PRIDE; C0LGG8; -.
DR ProteomicsDB; 243015; -. [C0LGG8-1]
DR EnsemblPlants; AT1G53430.1; AT1G53430.1; AT1G53430. [C0LGG8-1]
DR GeneID; 841778; -.
DR Gramene; AT1G53430.1; AT1G53430.1; AT1G53430. [C0LGG8-1]
DR KEGG; ath:AT1G53430; -.
DR Araport; AT1G53430; -.
DR eggNOG; ENOG502QTCP; Eukaryota.
DR InParanoid; C0LGG8; -.
DR OMA; DSIEQRS; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; C0LGG8; -.
DR PRO; PR:C0LGG8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; C0LGG8; baseline and differential.
DR Genevisible; C0LGG8; 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; IBA:GO_Central.
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; 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; PF13855; LRR_8; 1.
DR Pfam; PF11721; Malectin; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00369; LRR_TYP; 3.
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; 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..28
FT /evidence="ECO:0000255"
FT CHAIN 29..1038
FT /note="Probable LRR receptor-like serine/threonine-protein
FT kinase At1g53430"
FT /id="PRO_0000387534"
FT TOPO_DOM 29..609
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 610..630
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 631..1038
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 113..137
FT /note="LRR 1"
FT REPEAT 139..160
FT /note="LRR 2"
FT REPEAT 161..184
FT /note="LRR 3"
FT REPEAT 185..208
FT /note="LRR 4"
FT REPEAT 210..234
FT /note="LRR 5"
FT REPEAT 236..256
FT /note="LRR 6"
FT REPEAT 259..281
FT /note="LRR 7"
FT REPEAT 282..305
FT /note="LRR 8"
FT REPEAT 306..328
FT /note="LRR 9"
FT REPEAT 330..351
FT /note="LRR 10"
FT REPEAT 352..374
FT /note="LRR 11"
FT DOMAIN 669..950
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 984..1038
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 984..1000
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1007..1022
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1023..1038
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 795
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 675..683
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 697
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 658
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 742
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 828
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 829
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 834
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 842
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 339
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 363
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 471
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 561
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..33
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_038281"
FT VAR_SEQ 34..36
FT /note="DEV -> MAI (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_038282"
SQ SEQUENCE 1038 AA; 114945 MW; 84608C486633F9D0 CRC64;
MGFIFSTEKV VYVLLLIFVC LENFGSNAQL LPEDEVQTLR TIFRKLQNQT VNIERTSCSD
QNWNFVVESA SNSPTSNITC DCTFNASSVC RVTNIQLKSF SLPGIFPPEF GNLTRLREID
LSRNFLNGTI PTTLSQIPLE ILSVIGNRLS GPFPPQLGDI TTLTDVNLET NLFTGPLPRN
LGNLRSLKEL LLSANNFTGQ IPESLSNLKN LTEFRIDGNS LSGKIPDFIG NWTLLERLDL
QGTSMEGPIP PSISNLTNLT ELRITDLRGQ AAFSFPDLRN LMKMKRLVLR NCLIRGPIPE
YIGSMSELKT LDLSSNMLTG VIPDTFRNLD AFNFMFLNNN SLTGPVPQFI INSKENLDLS
DNNFTQPPTL SCNQLDVNLI SSYPSVTDNS VQWCLREGLP CPEDAKQSSL FINCGGSRLK
IGKDTYTDDL NSRGQSTFSS VSERWGYSSS GVWLGKEDAG YLATDRFNLI NGSTPEYYKT
ARLSPQSLKY YGLCLRRGSY KLQLHFAEIM FSNDQTFNSL GRRIFDIYVQ GNLLERDFNI
AERAGGVGKP FIRQIDGVQV NGSTLEIHLQ WTGKGTNVIP TRGVYGPLIS AITITPNFKV
DTGKPLSNGA VAGIVIAACA VFGLLVLVIL RLTGYLGGKE VDENEELRGL DLQTGSFTLK
QIKRATNNFD PENKIGEGGF GPVYKGVLAD GMTIAVKQLS SKSKQGNREF VTEIGMISAL
QHPNLVKLYG CCIEGKELLL VYEYLENNSL ARALFGTEKQ RLHLDWSTRN KICIGIAKGL
AYLHEESRLK IVHRDIKATN VLLDLSLNAK ISDFGLAKLN DDENTHISTR IAGTIGYMAP
EYAMRGYLTD KADVYSFGVV CLEIVSGKSN TNYRPKEEFV YLLDWAYVLQ EQGSLLELVD
PDLGTSFSKK EAMRMLNIAL LCTNPSPTLR PPMSSVVSML EGKIKVQPPL VKREADPSGS
AAMRFKALEL LSQDSESQVS TYARNREQDI SSSSMDGPWV DSSFSEPGKD VSLQQQEEGR
SSSSSRKLLD DLTDVKIE
