Y5977_ARATH
ID Y5977_ARATH Reviewed; 946 AA.
AC Q9LT96;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Probable leucine-rich repeat receptor-like protein kinase At5g49770;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At5g49770; ORFNames=K2I5.14;
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;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
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 Q9LT96; Q9SHI2: At1g17230; NbExp=3; IntAct=EBI-17123993, EBI-20651261;
CC Q9LT96; Q9LP24-3: At1g35710; NbExp=3; IntAct=EBI-17123993, EBI-20651291;
CC Q9LT96; Q9SH71: At1g64210; NbExp=2; IntAct=EBI-17123993, EBI-20651385;
CC Q9LT96; O65440-2: BAM3; NbExp=4; IntAct=EBI-17123993, EBI-20653325;
CC Q9LT96; Q9M0G7: MIK1; NbExp=2; IntAct=EBI-17123993, EBI-16196224;
CC Q9LT96; Q9LJY0: PRK4; NbExp=2; IntAct=EBI-17123993, EBI-16914444;
CC Q9LT96; Q9LHP4: RGI1; NbExp=2; IntAct=EBI-17123993, EBI-20660903;
CC Q9LT96; Q9LP77: RKL1; NbExp=3; IntAct=EBI-17123993, EBI-1544507;
CC Q9LT96; F4I2N7-2: RLK7; NbExp=3; IntAct=EBI-17123993, EBI-20651307;
CC Q9LT96; Q9LVI6: RLK902; NbExp=2; IntAct=EBI-17123993, EBI-1626936;
CC Q9LT96; Q9LK43: TMK4; NbExp=4; IntAct=EBI-17123993, EBI-20664575;
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 ---------------------------------------------------------------------------
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; AB025613; BAA98165.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95855.1; -; Genomic_DNA.
DR EMBL; FJ708798; ACN59389.1; -; mRNA.
DR RefSeq; NP_199788.1; NM_124355.3.
DR AlphaFoldDB; Q9LT96; -.
DR SMR; Q9LT96; -.
DR BioGRID; 20286; 30.
DR IntAct; Q9LT96; 40.
DR STRING; 3702.AT5G49770.1; -.
DR iPTMnet; Q9LT96; -.
DR PaxDb; Q9LT96; -.
DR PRIDE; Q9LT96; -.
DR ProteomicsDB; 243143; -.
DR EnsemblPlants; AT5G49770.1; AT5G49770.1; AT5G49770.
DR GeneID; 835040; -.
DR Gramene; AT5G49770.1; AT5G49770.1; AT5G49770.
DR KEGG; ath:AT5G49770; -.
DR Araport; AT5G49770; -.
DR TAIR; locus:2156992; AT5G49770.
DR eggNOG; ENOG502QQH6; Eukaryota.
DR HOGENOM; CLU_000288_14_1_1; -.
DR InParanoid; Q9LT96; -.
DR OMA; MLADNQV; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9LT96; -.
DR PRO; PR:Q9LT96; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LT96; baseline and differential.
DR Genevisible; Q9LT96; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009536; C:plastid; 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; 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; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
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; PF13855; LRR_8; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
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; Receptor; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..946
FT /note="Probable leucine-rich repeat receptor-like protein
FT kinase At5g49770"
FT /id="PRO_0000389462"
FT TOPO_DOM 26..561
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 562..582
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 583..946
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 67..91
FT /note="LRR 1"
FT REPEAT 92..116
FT /note="LRR 2"
FT REPEAT 118..140
FT /note="LRR 3"
FT REPEAT 141..164
FT /note="LRR 4"
FT REPEAT 166..191
FT /note="LRR 5"
FT REPEAT 195..219
FT /note="LRR 6"
FT REPEAT 221..244
FT /note="LRR 7"
FT REPEAT 245..268
FT /note="LRR 8"
FT REPEAT 269..293
FT /note="LRR 9"
FT REPEAT 295..314
FT /note="LRR 10"
FT REPEAT 316..340
FT /note="LRR 11"
FT REPEAT 342..365
FT /note="LRR 12"
FT REPEAT 367..387
FT /note="LRR 13"
FT REPEAT 389..407
FT /note="LRR 14"
FT DOMAIN 634..908
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 919..946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 758
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 640..648
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 662
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 415
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 460
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 489
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 514
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 946 AA; 104523 MW; A4BD1F3AD67B8DC0 CRC64;
MKMSSRIGLF KLLILLFFQI YSVYAFTDGS DFTALQALKN EWDTLSKSWK SSDPCGTEWV
GITCNNDNRV VSISLTNRNL KGKLPTEIST LSELQTLDLT GNPELSGPLP ANIGNLRKLT
FLSLMGCAFN GPIPDSIGNL EQLTRLSLNL NKFSGTIPAS MGRLSKLYWF DIADNQLEGK
LPVSDGASLP GLDMLLQTGH FHFGNNKLSG EIPEKLFSSE MTLLHVLFDG NQFTGSIPES
LGLVQNLTVL RLDRNRLSGD IPSSLNNLTN LQELHLSDNK FTGSLPNLTS LTSLYTLDVS
NNPLALSPVP SWIPFLNSLS TLRLEDIQLD GPVPTSLFSP LQLQTVSLKH NLINTTLDLG
TNYSKQLDFV DLRDNFITGY KSPANNPVNV MLADNQVCQD PANQLSGYCN AVQPNSTFST
LTKCGNHCGK GKEPNQGCHC VYPLTGVFTL RSPSFSGFSN NSNFLKFGES LMTFFKNGKY
PVDSVAMRNI SENPTDYHLL INLLIFPSGR DRFNQTEMDS INSAFTIQDY KPPPRFGPYI
FVADQYKTFS DLEDSKTVSM KVIIGVVVGV VVLLLLLALA GIYALRQKKR AQRATDQMNP
FAKWDAGKNE MDAPQLMGTK AFTFEELSKC TNNFSDANDV GGGGYGQVYK GTLPNGQVIA
IKRAQQGSMQ GAFEFKTEIE LLSRVHHKNV VKLLGFCFDQ KEQMLVYEYI PNGSLRDGLS
GKNGVKLDWT RRLKIALGSG KGLAYLHELA DPPIIHRDVK SNNILLDEHL TAKVADFGLS
KLVGDPEKAH VTTQVKGTMG YLDPEYYMTN QLTEKSDVYG FGVVMLELLT GKSPIDRGSY
VVKEVKKKMD KSRNLYDLQE LLDTTIIQNS GNLKGFEKYV DVALQCVEPE GVNRPTMSEV
VQELESILRL VGLNPNADSA TYEEASGDPY GRDSFEYTGV FPTPKP
