Y5487_ARATH
ID Y5487_ARATH Reviewed; 895 AA.
AC C0LGV0; Q9FKC2;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Probable LRR receptor-like serine/threonine-protein kinase At5g48740;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At5g48740; ORFNames=K24G6.7;
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=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
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 C0LGV0; Q93ZS4: NIK3; NbExp=2; IntAct=EBI-17091250, EBI-17121474;
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=BAB09427.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB012242; BAB09427.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED95718.1; -; Genomic_DNA.
DR EMBL; FJ708794; ACN59385.1; -; mRNA.
DR RefSeq; NP_199685.2; NM_124251.4.
DR AlphaFoldDB; C0LGV0; -.
DR SMR; C0LGV0; -.
DR BioGRID; 20178; 19.
DR IntAct; C0LGV0; 18.
DR STRING; 3702.AT5G48740.1; -.
DR PaxDb; C0LGV0; -.
DR PRIDE; C0LGV0; -.
DR ProteomicsDB; 243138; -.
DR EnsemblPlants; AT5G48740.1; AT5G48740.1; AT5G48740.
DR GeneID; 834932; -.
DR Gramene; AT5G48740.1; AT5G48740.1; AT5G48740.
DR KEGG; ath:AT5G48740; -.
DR Araport; AT5G48740; -.
DR TAIR; locus:2156549; AT5G48740.
DR eggNOG; ENOG502QW5Y; Eukaryota.
DR HOGENOM; CLU_000288_41_3_1; -.
DR InParanoid; C0LGV0; -.
DR OMA; WQDDPCS; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; C0LGV0; -.
DR PRO; PR:C0LGV0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; C0LGV0; baseline and differential.
DR Genevisible; C0LGV0; 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; -; 2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
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; SM00369; LRR_TYP; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51450; LRR; 4.
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..16
FT /evidence="ECO:0000255"
FT CHAIN 17..895
FT /note="Probable LRR receptor-like serine/threonine-protein
FT kinase At5g48740"
FT /id="PRO_0000387565"
FT TOPO_DOM 17..544
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 545..565
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 566..895
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 385..407
FT /note="LRR 1"
FT REPEAT 408..430
FT /note="LRR 2"
FT REPEAT 431..453
FT /note="LRR 3"
FT REPEAT 454..477
FT /note="LRR 4"
FT REPEAT 478..500
FT /note="LRR 5"
FT REPEAT 511..532
FT /note="LRR 6"
FT DOMAIN 606..888
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 732
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 612..620
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 634
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 679
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 767
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 772
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 780
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 50
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 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 234
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 416
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 436
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 462
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 498
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 521
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 895 AA; 99613 MW; 12CF391F473F6FD6 CRC64;
MLFWVLLSSF CVFCFSSPDG FLSLSCGGSS YTAAYNISWV SDNDYIETGN TTTVTYAEGN
STSSVPIRLF PDPQGRQCYK LPVRKDLSSV LIRATFVYRN YDSQNSPPAF HVSLGRRITS
TVDLRTNDPW IEELVWPVNN DSLLLCLLAV KGRGIPVISS LEVRPLPLGS YKYSLEGSPD
IILRRSYRIN SGYTNGTIRY PSDPFDRIWD PDQSYSPFHA SWSFNGLTKL NSFNITENPP
ASVLKTARIL ARKESLSYTL SLHTPGDYYI ILYFAGILSL SPSFSVTIND EVKQSDYTVT
SSEAGTLYFT QKGISKLNIT LRKIKFNPQV SALEVYEILQ IPPEASSTTV SALKVIEQFT
GQDLGWQDDP CTPLPWNHIE CEGNRVTSLF LSKINLRSIS PTFGDLLDLK TLDLHNTSLT
GAIQNVGSLK DLQKLNLSFN QLESFGSELE DLVNLEVLDL QNNSLQGSVP ETLGKLKKLR
LLNLENNNLV GPLPQSLNIT GLEVRITGNP CLSFSSISCN NVSSTIDTPQ VTIPINKKQR
KQNRIAILLG VSGGALFATF LVFVFMSIFT RRQRNKERDI TRAQLKMQNW NASRIFSHKE
IKSATRNFKE VIGRGSFGAV YRGKLPDGKQ VAVKVRFDRT QLGADSFINE VHLLSQIRHQ
NLVSFEGFCY EPKRQILVYE YLSGGSLADH LYGPRSKRHS LNWVSRLKVA VDAAKGLDYL
HNGSEPRIIH RDVKSSNILL DKDMNAKVSD FGLSKQFTKA DASHITTVVK GTAGYLDPEY
YSTLQLTEKS DVYSFGVVLL ELICGREPLS HSGSPDSFNL VLWARPNLQA GAFEIVDDIL
KETFDPASMK KAASIAIRCV GRDASGRPSI AEVLTKLKEA YSLQLSYLAA SAHTD
