Y1756_ARATH
ID Y1756_ARATH Reviewed; 871 AA.
AC C0LGD9; Q9LNX9;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Probable LRR receptor-like serine/threonine-protein kinase At1g07560;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At1g07560; ORFNames=F22G5.6;
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].
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 -!- INTERACTION:
CC C0LGD9; C0LGI5: At1g69990; NbExp=2; IntAct=EBI-16902423, EBI-20651225;
CC C0LGD9; C0LGW2: PAM74; NbExp=2; IntAct=EBI-16902423, EBI-16888393;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF79578.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC022464; AAF79578.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28142.1; -; Genomic_DNA.
DR EMBL; FJ708628; ACN59224.1; -; mRNA.
DR PIR; B86210; B86210.
DR RefSeq; NP_172236.2; NM_100630.3.
DR AlphaFoldDB; C0LGD9; -.
DR SMR; C0LGD9; -.
DR BioGRID; 22511; 53.
DR IntAct; C0LGD9; 53.
DR STRING; 3702.AT1G07560.1; -.
DR PaxDb; C0LGD9; -.
DR PRIDE; C0LGD9; -.
DR ProteomicsDB; 243056; -.
DR EnsemblPlants; AT1G07560.1; AT1G07560.1; AT1G07560.
DR GeneID; 837270; -.
DR Gramene; AT1G07560.1; AT1G07560.1; AT1G07560.
DR KEGG; ath:AT1G07560; -.
DR Araport; AT1G07560; -.
DR TAIR; locus:2024972; AT1G07560.
DR eggNOG; ENOG502QQCZ; Eukaryota.
DR HOGENOM; CLU_000288_41_1_1; -.
DR InParanoid; C0LGD9; -.
DR OMA; NTSPVKC; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; C0LGD9; -.
DR PRO; PR:C0LGD9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; C0LGD9; baseline and differential.
DR Genevisible; C0LGD9; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR024788; Malectin-like_Carb-bd_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF12819; Malectin_like; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein 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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..871
FT /note="Probable LRR receptor-like serine/threonine-protein
FT kinase At1g07560"
FT /id="PRO_0000387544"
FT TOPO_DOM 25..515
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 516..536
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 537..871
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 413..436
FT /note="LRR 1"
FT REPEAT 437..459
FT /note="LRR 2"
FT REPEAT 461..482
FT /note="LRR 3"
FT DOMAIN 570..837
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 692
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 576..584
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 598
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 561
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 643
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 696
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 726
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 727
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 732
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 740
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 236
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 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 407
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 434
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 447
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 466
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 471
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 871 AA; 96926 MW; C56478E3E029ED5F CRC64;
MKNLRGLLLA FLVLSLGISD FLRAQDQQGF ISLDCGLQAD ESPYTEPLTK LTFTSDADFI
KSGKSGKIQN VPGMEYIKPY TVLRYFPDGV RNCYTLIVIQ GTNYLIVAMF TYGNYDNLNT
HPKFDLYLGP NIWTTVDLQR NVNGTRAEII HIPRSTSLQI CLVKTGTTTP LISALELRPL
RNNTYIPQSG SLKTLFRVHL TDSKETVRYP EDVHDRLWSP FFMPEWRLLR TSLTVNTSDD
NGYDIPEDVV VTAATPANVS SPLTISWNLE TPDDLVYAYL HVAEIQSLRE NDTREFNISA
GQDVNYGPVS PDEFLVGTLF NTSPVKCEGG TCHLQLIKTP KSTLPPLLNA IEAFITVEFP
QSETNANDVL AIKSIETSYG LSRISWQGDP CVPQQLLWDG LTCEYTNMST PPRIHSLDLS
SSELTGIIVP EIQNLTELKK LDFSNNNLTG GVPEFLAKMK SLLVINLSGN NLSGSVPQAL
LNKVKNGLKL NIQGNPNLCF SSSCNKKKNS IMLPVVASLA SLAAIIAMIA LLFVCIKRRS
SSRKGPSPSQ QSIETIKKRY TYAEVLAMTK KFERVLGKGG FGMVYHGYIN GTEEVAVKLL
SPSSAQGYKE FKTEVELLLR VYHTNLVSLV GYCDEKDHLA LIYQYMVNGD LKKHFSGSSI
ISWVDRLNIA VDAASGLEYL HIGCKPLIVH RDVKSSNILL DDQLQAKLAD FGLSRSFPIG
DESHVSTLVA GTFGYLDHEY YQTNRLSEKS DVYSFGVVLL EIITNKPVID HNRDMPHIAE
WVKLMLTRGD ISNIMDPKLQ GVYDSGSAWK ALELAMTCVN PSSLKRPNMS HVVHELKECL
VSENNRTRDI DTSRSMDINL SFGTDVNPKA R
