Y2899_ARATH
ID Y2899_ARATH Reviewed; 884 AA.
AC O81069;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Probable leucine-rich repeat receptor-like protein kinase At2g28990;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At2g28990; ORFNames=T9I4.7;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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).
RN [4]
RP INTERACTION WITH AMT1-1.
RX PubMed=21423366; DOI=10.3389/fphys.2010.00024;
RA Lalonde S., Sero A., Pratelli R., Pilot G., Chen J., Sardi M.I.,
RA Parsa S.A., Kim D.Y., Acharya B.R., Stein E.V., Hu H.C., Villiers F.,
RA Takeda K., Yang Y., Han Y.S., Schwacke R., Chiang W., Kato N., Loque D.,
RA Assmann S.M., Kwak J.M., Schroeder J.I., Rhee S.Y., Frommer W.B.;
RT "A membrane protein/signaling protein interaction network for Arabidopsis
RT version AMPv2.";
RL Front. Physiol. 1:24-24(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 -!- SUBUNIT: Binds to the ammonium transporter AMT1-1.
CC {ECO:0000269|PubMed:21423366}.
CC -!- INTERACTION:
CC O81069; A0A178VQN9: At2g42290; NbExp=2; IntAct=EBI-16887698, EBI-20655829;
CC O81069; C0LGS2: At4g36180; NbExp=2; IntAct=EBI-16887698, EBI-16955302;
CC O81069; C0LGS3: At4g37250; NbExp=2; IntAct=EBI-16887698, EBI-16955335;
CC O81069; Q9FRI1: LRR-RLK; NbExp=3; IntAct=EBI-16887698, EBI-17071528;
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}.
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DR EMBL; AC005315; AAC33227.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08197.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM63285.1; -; Genomic_DNA.
DR EMBL; FJ708706; ACN59301.1; -; mRNA.
DR PIR; T02731; T02731.
DR RefSeq; NP_001318310.1; NM_001336195.1.
DR RefSeq; NP_180465.1; NM_128458.2.
DR AlphaFoldDB; O81069; -.
DR SMR; O81069; -.
DR BioGRID; 2798; 48.
DR IntAct; O81069; 45.
DR STRING; 3702.AT2G28990.1; -.
DR PaxDb; O81069; -.
DR PRIDE; O81069; -.
DR ProteomicsDB; 232400; -.
DR EnsemblPlants; AT2G28990.1; AT2G28990.1; AT2G28990.
DR EnsemblPlants; AT2G28990.2; AT2G28990.2; AT2G28990.
DR GeneID; 817448; -.
DR Gramene; AT2G28990.1; AT2G28990.1; AT2G28990.
DR Gramene; AT2G28990.2; AT2G28990.2; AT2G28990.
DR KEGG; ath:AT2G28990; -.
DR Araport; AT2G28990; -.
DR TAIR; locus:2066158; AT2G28990.
DR eggNOG; ENOG502QQCZ; Eukaryota.
DR HOGENOM; CLU_000288_41_1_1; -.
DR InParanoid; O81069; -.
DR OMA; ESKGSME; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; O81069; -.
DR PRO; PR:O81069; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O81069; baseline and differential.
DR Genevisible; O81069; 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; IPR008271; Ser/Thr_kinase_AS.
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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..884
FT /note="Probable leucine-rich repeat receptor-like protein
FT kinase At2g28990"
FT /id="PRO_0000389456"
FT TOPO_DOM 20..508
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 509..529
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 530..884
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 404..427
FT /note="LRR 1"
FT REPEAT 428..451
FT /note="LRR 2"
FT REPEAT 452..476
FT /note="LRR 3"
FT DOMAIN 577..850
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 535..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 418
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 427
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 438
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 459
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 464
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 884 AA; 98756 MW; E354E899EAAE48BE CRC64;
MKIHLLLAMI GTFVVIIGAQ DQEGFISLDC GLPSDESPYD DSFNGLTFTS DSTFIQTGKI
DSVDKDLNIN LSKQYLTLRY FPEGKRNCYS LDVKRGTTYL IVVSFVYGNY DGLNRDPNFD
IHLGPNKWKR IDLDGEKEGT REEIIHKARS NSLDICLVKT GETLPIISAI EIRPLRNNTY
VTQSGSLMMS FRVYLSNSDA SIRYADDVHD RIWSPFNGSS HTHITTDLNI NNSNAYEIPK
NILQTAAIPR NASAPLIITW DPLPINAEVY LYMHFAEIQT LEANETRQFD VILRGNFNHS
GFSPTKLKVF TLYTEEPMKC GSEGCYLQLV KTPNSTLPPL INAIEAYSVI EFSQLETSLS
DVDAIKNIKN TYKLNKITWQ GDPCLPQDLS WESIRCTYVD GSTSPTIISL DLSKSGLNGS
IPQILQNFTQ LQELDLSNNS LTGPVPIFLA NMKTLSLINL SGNNLSGSVP QALLDKEKEG
LVLKLEGNPD LCKSSFCNTE KKNKFLLPVI ASAASLVIVV VVVALFFVFR KKKASPSNLH
APPSMPVSNP GHNSQSESSF TSKKIRFTYS EVQEMTNNFD KALGEGGFGV VYHGFVNVIE
QVAVKLLSQS SSQGYKHFKA EVELLMRVHH INLVSLVGYC DEGEHLALIY EYMPNGDLKQ
HLSGKHGGFV LSWESRLKIV LDAALGLEYL HTGCVPPMVH RDIKTTNILL DQHLQAKLAD
FGLSRSFPIG NEKNVSTVVA GTPGYLDPEY YQTNWLTEKS DIYSFGIVLL EIISNRPIIQ
QSREKPHIVE WVSFMITKGD LRSIMDPNLH QDYDIGSVWK AIELAMSCVS LSSARRPNMS
RVVNELKECL ISETSRIGEG RDMESKGSME FSRDIYNEVI PQAR
