Y5181_ARATH
ID Y5181_ARATH Reviewed; 871 AA.
AC Q9FZB8; Q9C8I8;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Probable LRR receptor-like serine/threonine-protein kinase At1g51810;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At1g51810; ORFNames=F19C24.1, T14L22.2;
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=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=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [4]
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 -!- INTERACTION:
CC Q9FZB8-2; Q93ZS4: NIK3; NbExp=2; IntAct=EBI-20653376, EBI-17121474;
CC Q9FZB8-2; Q9LZV7: PXC2; NbExp=2; IntAct=EBI-20653376, EBI-1238200;
CC Q9FZB8-2; Q9FYK0: TMK2; NbExp=2; IntAct=EBI-20653376, EBI-20652836;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9FZB8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FZB8-2; Sequence=VSP_038278;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AC015448; AAF99852.1; -; Genomic_DNA.
DR EMBL; AC025294; AAG50867.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32720.1; -; Genomic_DNA.
DR EMBL; DQ459169; ABE97168.1; -; mRNA.
DR EMBL; FJ708651; ACN59247.1; -; mRNA.
DR PIR; D96557; D96557.
DR RefSeq; NP_175593.2; NM_104061.3. [Q9FZB8-2]
DR AlphaFoldDB; Q9FZB8; -.
DR SMR; Q9FZB8; -.
DR BioGRID; 26833; 22.
DR IntAct; Q9FZB8; 25.
DR STRING; 3702.AT1G51810.1; -.
DR PaxDb; Q9FZB8; -.
DR PeptideAtlas; Q9FZB8; -.
DR PRIDE; Q9FZB8; -.
DR ProteomicsDB; 243011; -. [Q9FZB8-1]
DR EnsemblPlants; AT1G51810.1; AT1G51810.1; AT1G51810. [Q9FZB8-2]
DR GeneID; 841608; -.
DR Gramene; AT1G51810.1; AT1G51810.1; AT1G51810. [Q9FZB8-2]
DR KEGG; ath:AT1G51810; -.
DR Araport; AT1G51810; -.
DR TAIR; locus:2017537; AT1G51810.
DR eggNOG; ENOG502QQCZ; Eukaryota.
DR HOGENOM; CLU_000288_41_1_1; -.
DR InParanoid; Q9FZB8; -.
DR OMA; ITIMLHQ; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9FZB8; -.
DR PRO; PR:Q9FZB8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FZB8; baseline and differential.
DR Genevisible; Q9FZB8; 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 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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..871
FT /note="Probable LRR receptor-like serine/threonine-protein
FT kinase At1g51810"
FT /id="PRO_0000387530"
FT TOPO_DOM 21..512
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 513..533
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 534..871
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 405..426
FT /note="LRR 1"
FT REPEAT 429..449
FT /note="LRR 2"
FT REPEAT 453..474
FT /note="LRR 3"
FT DOMAIN 577..850
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 702
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 583..591
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 605
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 568
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 650
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 736
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 737
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 742
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 750
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 179
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 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 396
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 439
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 458
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 463
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 489
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..127
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17147637,
FT ECO:0000303|PubMed:20064227"
FT /id="VSP_038278"
SQ SEQUENCE 871 AA; 97230 MW; B1EE894F31F07F84 CRC64;
MERHCLFFVI FSLILHLVQA QDPIGFINLD CGLSIQGSPY KESSTGLTYT SDDGFVQSGK
IGKITKELES LYKKPERTLR YFPDGVRNCF SLNVTRGTKY LIKPTFLYGN YDGRNVIPDF
DLYIGPNMWI TVNTDNTIKE ILHVSKSNTL QVCLVKTGTS IPYINTLELR PLADDIYTNE
SGSLNYLFRV YYSNLKGYIE YPDDVHDRIW KQILPYQDWQ ILTTNLQINV SNDYDLPQRV
MKTAVTPIKA STTTMEFPWN LEPPTSQFYL FLHFAELQSL QANETREFNV VLNGNVTFKS
YSPKFLEMQT VYSTAPKQCD GGKCLLQLVK TSRSTLPPLI NAMEAYTVLD FPQIETNVDE
VIAIKNIQST YGLSKTTWQG DPCVPKKFLW DGLNCNNSDD STPPIITSLN LSSSGLTGII
VLTIQNLANL QELDLSNNNL SGGVPEFLAD MKSLLVINLS GNNLSGVVPQ KLIEKKMLKL
NIEGNPKLNC TVESCVNKDE EGGRQIKSMT IPIVASIGSV VAFTVALMIF CVVRKNNPSN
DEAPTSCMLP ADSRSSEPTI VTKNKKFTYA EVLTMTNNFQ KILGKGGFGI VYYGSVNGTE
QVAVKMLSHS SAQGYKQFKA EVELLLRVHH KNLVGLVGYC EEGDKLALIY EYMANGDLDE
HMSGKRGGSI LNWGTRLKIA LEAAQGLEYL HNGCKPLMVH RDVKTTNILL NEHFDTKLAD
FGLSRSFPIE GETHVSTVVA GTIGYLDPEY YRTNWLTEKS DVYSFGVVLL VMITNQPVID
QNREKRHIAE WVGGMLTKGD IKSITDPNLL GDYNSGSVWK AVELAMSCMN PSSMTRPTMS
QVVFELKECL ASESSREVSM TFGTEVAPMA R
