Y1518_ARATH
ID Y1518_ARATH Reviewed; 890 AA.
AC C0LGG4; Q9FZB3;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2009, sequence version 2.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Probable LRR receptor-like serine/threonine-protein kinase At1g51860;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At1g51860; ORFNames=T14L22.7;
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] OF 243-890.
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: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=AAF99856.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC015448; AAF99856.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE32726.1; -; Genomic_DNA.
DR EMBL; FJ708653; ACN59249.1; -; mRNA.
DR PIR; A96558; A96558.
DR RefSeq; NP_175598.1; NM_104066.2.
DR AlphaFoldDB; C0LGG4; -.
DR SMR; C0LGG4; -.
DR STRING; 3702.AT1G51860.1; -.
DR iPTMnet; C0LGG4; -.
DR PaxDb; C0LGG4; -.
DR PRIDE; C0LGG4; -.
DR ProteomicsDB; 242984; -.
DR EnsemblPlants; AT1G51860.1; AT1G51860.1; AT1G51860.
DR GeneID; 841613; -.
DR Gramene; AT1G51860.1; AT1G51860.1; AT1G51860.
DR KEGG; ath:AT1G51860; -.
DR Araport; AT1G51860; -.
DR TAIR; locus:2195850; AT1G51860.
DR HOGENOM; CLU_000288_41_1_1; -.
DR InParanoid; C0LGG4; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; C0LGG4; -.
DR PRO; PR:C0LGG4; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; C0LGG4; baseline and differential.
DR Genevisible; C0LGG4; 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; 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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF12819; Malectin_like; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 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 2: Evidence at transcript 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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..890
FT /note="Probable LRR receptor-like serine/threonine-protein
FT kinase At1g51860"
FT /id="PRO_0000387527"
FT TOPO_DOM 24..513
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 514..534
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 535..890
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 412..435
FT /note="LRR 1"
FT REPEAT 436..458
FT /note="LRR 2"
FT REPEAT 460..481
FT /note="LRR 3"
FT DOMAIN 584..856
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 708
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 590..598
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 611
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 575
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 656
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 742
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 743
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 748
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 756
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 142
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 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 289
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 312
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 340
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 465
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 473
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 497
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 890 AA; 99234 MW; 374CE5857EEB15F5 CRC64;
MKSLHWFLHL LIIAFTVLRS VEAQNQAGFI SLDCGLVPKE TTYTEKSTNI TYKSDVDYID
SGLVGKINDA YKTQFQQQVW AVRSFPVGQR NCYNVNLTAN NKYLIRGTFV YGNYDGLNQF
PSFDLHIGPN KWSSVKILGV TNTSMHEIIH VVPQDSLEVC LVKTGPTTPF ISSLEVRPLN
NESYLTQSGS LMLFARVYFP SSSSSFIRYD EDIHDRVWNS FTDDETVWIS TDLPIDTSNS
YDMPQSVMKT AAVPKNASEP WLLWWTLDEN TAQSYVYMHF AEVQNLTANE TREFNITYNG
GLRWFSYLRP PNLSISTIFN PRAVSSSNGI FNFTFAMTGN STLPPLLNAL EIYTVVDILQ
LETNKDEVSA MMNIKETYGL SKKISWQGDP CAPQLYRWEG LNCSYPDSEG SRIISLNLNG
SELTGSITSD ISKLTLLTVL DLSNNDLSGD IPTFFAEMKS LKLINLSGNP NLNLTAIPDS
LQQRVNSKSL TLILGENLTL TPKKESKKVP MVAIAASVAG VFALLVILAI FFVIKRKNVK
AHKSPGPPPL VTPGIVKSET RSSNPSIITR ERKITYPEVL KMTNNFERVL GKGGFGTVYH
GNLDGAEVAV KMLSHSSAQG YKEFKAEVEL LLRVHHRHLV GLVGYCDDGD NLALIYEYMA
NGDLRENMSG KRGGNVLTWE NRMQIAVEAA QGLEYLHNGC RPPMVHRDVK TTNILLNERC
GAKLADFGLS RSFPIDGECH VSTVVAGTPG YLDPEYYRTN WLSEKSDVYS FGVVLLEIVT
NQPVIDKTRE RPHINDWVGF MLTKGDIKSI VDPKLMGDYD TNGAWKIVEL ALACVNPSSN
RRPTMAHVVM ELNDCVALEN ARRQGSEEMY SMGSVDYSLS STSDFAPGAR
