Y5614_ARATH
ID Y5614_ARATH Reviewed; 1033 AA.
AC C0LGH3; Q0WRM0; Q6NLS4; Q9C7J2; Q9SGU0;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Probable LRR receptor-like serine/threonine-protein kinase At1g56140;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At1g56140; ORFNames=F14G9.24, T6H22.8.1;
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 3).
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
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: Membrane {ECO:0000255}; Single-pass type I
CC membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=C0LGH3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=C0LGH3-2; Sequence=VSP_038288, VSP_038289;
CC Name=3;
CC IsoId=C0LGH3-3; Sequence=VSP_038286, VSP_038287;
CC Name=4;
CC IsoId=C0LGH3-4; Sequence=VSP_038285;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF02840.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAG50909.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=ACN59258.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC009894; AAF02840.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC069159; AAG50909.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33348.1; -; Genomic_DNA.
DR EMBL; BT011697; AAS49060.1; -; mRNA.
DR EMBL; BT012256; AAS76743.1; -; mRNA.
DR EMBL; AK228283; BAF00229.1; -; mRNA.
DR EMBL; FJ708663; ACN59258.1; ALT_FRAME; mRNA.
DR PIR; G96602; G96602.
DR RefSeq; NP_564709.2; NM_104492.4. [C0LGH3-1]
DR AlphaFoldDB; C0LGH3; -.
DR SMR; C0LGH3; -.
DR BioGRID; 27291; 19.
DR STRING; 3702.AT1G56140.1; -.
DR iPTMnet; C0LGH3; -.
DR PaxDb; C0LGH3; -.
DR PRIDE; C0LGH3; -.
DR ProteomicsDB; 242906; -. [C0LGH3-1]
DR EnsemblPlants; AT1G56140.1; AT1G56140.1; AT1G56140. [C0LGH3-1]
DR GeneID; 842066; -.
DR Gramene; AT1G56140.1; AT1G56140.1; AT1G56140. [C0LGH3-1]
DR KEGG; ath:AT1G56140; -.
DR Araport; AT1G56140; -.
DR TAIR; locus:2011816; AT1G56140.
DR eggNOG; ENOG502QUW9; Eukaryota.
DR HOGENOM; CLU_000288_114_2_1; -.
DR InParanoid; C0LGH3; -.
DR OMA; ISIFRQW; -.
DR OrthoDB; 146580at2759; -.
DR PhylomeDB; C0LGH3; -.
DR PRO; PR:C0LGH3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; C0LGH3; baseline and differential.
DR Genevisible; C0LGH3; 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; -; 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; PF13855; LRR_8; 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 2: Evidence at transcript 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..1033
FT /note="Probable LRR receptor-like serine/threonine-protein
FT kinase At1g56140"
FT /id="PRO_0000387536"
FT TOPO_DOM 29..636
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 637..657
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 658..1033
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 97..121
FT /note="LRR 1"
FT REPEAT 122..145
FT /note="LRR 2"
FT REPEAT 147..169
FT /note="LRR 3"
FT REPEAT 170..193
FT /note="LRR 4"
FT REPEAT 195..217
FT /note="LRR 5"
FT REPEAT 241..264
FT /note="LRR 6"
FT REPEAT 265..288
FT /note="LRR 7"
FT REPEAT 289..313
FT /note="LRR 8"
FT REPEAT 314..337
FT /note="LRR 9"
FT REPEAT 339..361
FT /note="LRR 10"
FT REPEAT 363..382
FT /note="LRR 11"
FT REPEAT 383..406
FT /note="LRR 12"
FT REPEAT 422..445
FT /note="LRR 13"
FT DOMAIN 693..951
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1012..1033
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 817
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 699..707
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 721
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 682
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 766
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 821
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 850
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 851
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 856
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 864
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 301
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 393
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 579
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 96..988
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_038285"
FT VAR_SEQ 173..184
FT /note="RLLSISSNNFSG -> MTPQPPQSAAFH (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_038286"
FT VAR_SEQ 185..1033
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_038287"
FT VAR_SEQ 508..521
FT /note="YYGLGLENGGYTVT -> FYFQHLERFRKTTF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:20064227"
FT /id="VSP_038288"
FT VAR_SEQ 522..1033
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:20064227"
FT /id="VSP_038289"
FT CONFLICT 275
FT /note="D -> E (in Ref. 3; ACN59258)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1033 AA; 113754 MW; 2F091890AF9C8467 CRC64;
MLRLWRYLCL LLTVWFLCNF GPVYVVRAQN RTGATTHPDE ALALNSIFAA WRIRAPREWN
ISGELCSGAA IDASVLDSNP AYNPLIKCDC SFENSTICRI TNIKVYAMEV VGSIPQQLWT
LEYLTNLNLG QNVLTGSLPP ALGNLTRMRW MTFGINALSG PIPKEIGLLT DLRLLSISSN
NFSGSIPDEI GRCTKLQQIY IDSSGLSGGL PVSFANLVEL EQAWIADMEL TGQIPDFIGD
WTKLTTLRIL GTGLSGPIPA SFSNLTSLTE LRLGDISNGN SSLEFIKDMK SLSILVLRNN
NLTGTIPSNI GEYSSLRQLD LSFNKLHGTI PASLFNLRQL THLFLGNNTL NGSLPTQKGQ
SLSNVDVSYN DLSGSLPSWV SLPNLNLNLV ANNFTLEGLD NRVLSGLNCL QKNFPCNRGK
GIYSDFSINC GGPEIRSVTE AVFEREDEDL GPASFVVSAG QRWAASSVGL FAGSSNNIYI
STSQSQFVNT LDSELFQSAR LSASSLRYYG LGLENGGYTV TLQFAEIQIL GSTSNTWRGL
GRRRFDIYVQ GRLVEKDFDV RRTAGDSTVR AVQREYKANV SQNHLEIHLF WAGKGTCCIP
IQGAYGPLIS AVGATPDFTP TVGNRPPSKG KSMTGTIVGV IVGVGLLSII SGVVIFIIRK
RRKRYTDDEE ILSMDVKPYT FTYSELKSAT QDFDPSNKLG EGGFGPVYKG KLNDGREVAV
KLLSVGSRQG KGQFVAEIVA ISAVQHRNLV KLYGCCYEGE HRLLVYEYLP NGSLDQALFG
EKTLHLDWST RYEICLGVAR GLVYLHEEAR LRIVHRDVKA SNILLDSKLV PKVSDFGLAK
LYDDKKTHIS TRVAGTIGYL APEYAMRGHL TEKTDVYAFG VVALELVSGR PNSDENLEDE
KRYLLEWAWN LHEKGREVEL IDHQLTEFNM EEGKRMIGIA LLCTQTSHAL RPPMSRVVAM
LSGDVEVSDV TSKPGYLTDW RFDDTTASSI SGFPLRNTQA SESFTSFVAP RSEISPRNND
ARPMLGAQMN EGR
