Y5344_ARATH
ID Y5344_ARATH Reviewed; 1035 AA.
AC C0LGG9; Q9LPG0;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 2.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Probable LRR receptor-like serine/threonine-protein kinase At1g53440;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At1g53440; ORFNames=T3F20.24;
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 2).
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: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=C0LGG9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=C0LGG9-2; Sequence=VSP_038279;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF78445.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC018748; AAF78445.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE32941.1; -; Genomic_DNA.
DR EMBL; FJ708658; ACN59254.1; -; mRNA.
DR PIR; D96574; D96574.
DR RefSeq; NP_175749.1; NM_104222.2. [C0LGG9-1]
DR AlphaFoldDB; C0LGG9; -.
DR SMR; C0LGG9; -.
DR BioGRID; 27004; 12.
DR IntAct; C0LGG9; 11.
DR STRING; 3702.AT1G53440.1; -.
DR iPTMnet; C0LGG9; -.
DR PaxDb; C0LGG9; -.
DR PRIDE; C0LGG9; -.
DR ProteomicsDB; 243017; -. [C0LGG9-1]
DR EnsemblPlants; AT1G53440.1; AT1G53440.1; AT1G53440. [C0LGG9-1]
DR GeneID; 841779; -.
DR Gramene; AT1G53440.1; AT1G53440.1; AT1G53440. [C0LGG9-1]
DR KEGG; ath:AT1G53440; -.
DR Araport; AT1G53440; -.
DR TAIR; locus:2203718; AT1G53440.
DR eggNOG; ENOG502QTCP; Eukaryota.
DR HOGENOM; CLU_000288_114_2_1; -.
DR InParanoid; C0LGG9; -.
DR OMA; NGPEFYQ; -.
DR PhylomeDB; C0LGG9; -.
DR PRO; PR:C0LGG9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; C0LGG9; baseline and differential.
DR Genevisible; C0LGG9; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; 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:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 3.80.10.10; -; 3.
DR InterPro; IPR011009; Kinase-like_dom_sf.
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; 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 2: Evidence at transcript 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..1035
FT /note="Probable LRR receptor-like serine/threonine-protein
FT kinase At1g53440"
FT /id="PRO_0000387532"
FT TOPO_DOM 27..607
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 608..628
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 629..1035
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 87..110
FT /note="LRR 1"
FT REPEAT 111..135
FT /note="LRR 2"
FT REPEAT 137..158
FT /note="LRR 3"
FT REPEAT 160..182
FT /note="LRR 4"
FT REPEAT 183..206
FT /note="LRR 5"
FT REPEAT 208..232
FT /note="LRR 6"
FT REPEAT 234..254
FT /note="LRR 7"
FT REPEAT 278..302
FT /note="LRR 8"
FT REPEAT 303..326
FT /note="LRR 9"
FT REPEAT 328..349
FT /note="LRR 10"
FT REPEAT 350..372
FT /note="LRR 11"
FT DOMAIN 667..948
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 969..1035
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 970..985
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 992..1025
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 793
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 673..681
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 695
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 656
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 740
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 826
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 827
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 832
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 840
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 361
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 469
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 559
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..165
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:20064227"
FT /id="VSP_038279"
SQ SEQUENCE 1035 AA; 114851 MW; FD2E6FB2C1F9DD51 CRC64;
MGFFFSTRKG LLLIIFICLD IFGSNAQLLP EDEVQTLRTI FRKLQNQTVN IERTSCLDRK
WNFVAESTSK LPTSNITCDC TFNASSVCRV TNIQLRGFNL RGIIPPEFGN LTRLTEIDLV
LNFLSGTIPT TLSQIPLEIL AVTGNRLSGP FPPQLGQITT LTDVIMESNL FTGQLPPNLG
NLRSLKRLLI SSNNITGRIP ESLSNLKNLT NFRIDGNSLS GKIPDFIGNW TRLVRLDLQG
TSMEGPIPAS ISNLKNLTEL RITDLRGPTS PFPDLQNMTN MERLVLRNCL IREPIPEYIG
TSMTMLKLLD LSSNMLNGTI PDTFRSLNAF NFMYLNNNSL TGPVPQFILD SKQNIDLSYN
NFTQPPTLSC NQLDVNLISS YPSVTNNSVQ WCLRKDLPCP GDAHHSSLFI NCGGNRLKVD
KDEYADDLNK RGASTFSSVS ERWGYSSSGA WLGNDGATYL ATDTFNLINE STPEYYKTAR
LASQSLKYYG LCMRRGSYKV QLYFAEIMFS NDQTYSSLGR RLFDIYVQGI LLERDFNIAQ
RAGGVGKPFL RQVDEVQVNG STLEIHLKWT GKGTNVIPTR GVYGPLISAI TVTPNFKVDT
GKPLSNGVVA GIVIAACVAF GLLVLVILRL TGYLGGKEVD ENEELRGLDL QTGSFTLKQI
KRATNNFDPE NKIGEGGFGP VYKGVLADGM TIAVKQLSSK SKQGNREFVT EIGMISALQH
PNLVKLYGCC IEGKELLLVY EYLENNSLAR ALFGTEKQRL HLDWSTRNKV CIGIAKGLAY
LHEESRLKIV HRDIKATNVL LDLSLNAKIS DFGLAKLDEE ENTHISTRIA GTIGYMAPEY
AMRGYLTDKA DVYSFGVVCL EIVSGKSNTN YRPKEEFIYL LDWAYVLQEQ GSLLELVDPD
LGTSFSKKEA MRMLNIALLC TNPSPTLRPP MSSVVSMLQG KIKVQPPLVK READPSGSAA
MRFKALEHLS QDSESQVSTY TRNKEHKSSS SMDGPWVDSS FSDPSKDVSL LQQEEGNSSS
SSRRLLDDLT DVEIE
