Y5639_ARATH
ID Y5639_ARATH Reviewed; 1102 AA.
AC Q9LVP0;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Probable leucine-rich repeat receptor-like protein kinase At5g63930;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At5g63930; ORFNames=MBM17.3;
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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].
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 Q9LVP0; F4I2N7-2: RLK7; NbExp=2; IntAct=EBI-16955586, EBI-20651307;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
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; AB019227; BAA96896.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97817.1; -; Genomic_DNA.
DR EMBL; FJ708814; ACN59405.1; -; mRNA.
DR RefSeq; NP_201198.1; NM_125789.3.
DR AlphaFoldDB; Q9LVP0; -.
DR SMR; Q9LVP0; -.
DR BioGRID; 21756; 41.
DR IntAct; Q9LVP0; 29.
DR STRING; 3702.AT5G63930.1; -.
DR PaxDb; Q9LVP0; -.
DR ProteomicsDB; 242896; -.
DR EnsemblPlants; AT5G63930.1; AT5G63930.1; AT5G63930.
DR GeneID; 836514; -.
DR Gramene; AT5G63930.1; AT5G63930.1; AT5G63930.
DR KEGG; ath:AT5G63930; -.
DR Araport; AT5G63930; -.
DR TAIR; locus:2160791; AT5G63930.
DR eggNOG; ENOG502QPT1; Eukaryota.
DR HOGENOM; CLU_000288_22_1_1; -.
DR InParanoid; Q9LVP0; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; Q9LVP0; -.
DR PRO; PR:Q9LVP0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LVP0; baseline and differential.
DR Genevisible; Q9LVP0; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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; -; 5.
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; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF13855; LRR_8; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 8.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Glycoprotein; Kinase; Leucine-rich repeat;
KW Membrane; Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome;
KW Repeat; Serine/threonine-protein kinase; Signal; Transferase;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..1102
FT /note="Probable leucine-rich repeat receptor-like protein
FT kinase At5g63930"
FT /id="PRO_0000401350"
FT TOPO_DOM 27..737
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 738..758
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 759..1102
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 72..96
FT /note="LRR 1"
FT REPEAT 97..120
FT /note="LRR 2"
FT REPEAT 122..144
FT /note="LRR 3"
FT REPEAT 145..170
FT /note="LRR 4"
FT REPEAT 172..192
FT /note="LRR 5"
FT REPEAT 193..216
FT /note="LRR 6"
FT REPEAT 217..241
FT /note="LRR 7"
FT REPEAT 243..264
FT /note="LRR 8"
FT REPEAT 265..288
FT /note="LRR 9"
FT REPEAT 289..312
FT /note="LRR 10"
FT REPEAT 314..336
FT /note="LRR 11"
FT REPEAT 337..360
FT /note="LRR 12"
FT REPEAT 361..383
FT /note="LRR 13"
FT REPEAT 385..408
FT /note="LRR 14"
FT REPEAT 409..432
FT /note="LRR 15"
FT REPEAT 433..456
FT /note="LRR 16"
FT REPEAT 458..480
FT /note="LRR 17"
FT REPEAT 481..504
FT /note="LRR 18"
FT REPEAT 505..528
FT /note="LRR 19"
FT REPEAT 529..552
FT /note="LRR 20"
FT REPEAT 554..576
FT /note="LRR 21"
FT REPEAT 577..602
FT /note="LRR 22"
FT REPEAT 604..624
FT /note="LRR 23"
FT REPEAT 625..649
FT /note="LRR 24"
FT REPEAT 651..672
FT /note="LRR 25"
FT REPEAT 674..700
FT /note="LRR 26"
FT DOMAIN 804..1091
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 932
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 810..818
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 832
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 793
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 801
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 882
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 919
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 966
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT MOD_RES 974
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 981
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT MOD_RES 982
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 302
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 311
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 444
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 482
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 503
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 535
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 564
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 588
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 599
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 614
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 632
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 661
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 672
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 680
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 695
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1102 AA; 120477 MW; 6CDF852ADD32D54D CRC64;
MVKEMMKLAV FFISLLLILL ISETTGLNLE GQYLLEIKSK FVDAKQNLRN WNSNDSVPCG
WTGVMCSNYS SDPEVLSLNL SSMVLSGKLS PSIGGLVHLK QLDLSYNGLS GKIPKEIGNC
SSLEILKLNN NQFDGEIPVE IGKLVSLENL IIYNNRISGS LPVEIGNLLS LSQLVTYSNN
ISGQLPRSIG NLKRLTSFRA GQNMISGSLP SEIGGCESLV MLGLAQNQLS GELPKEIGML
KKLSQVILWE NEFSGFIPRE ISNCTSLETL ALYKNQLVGP IPKELGDLQS LEFLYLYRNG
LNGTIPREIG NLSYAIEIDF SENALTGEIP LELGNIEGLE LLYLFENQLT GTIPVELSTL
KNLSKLDLSI NALTGPIPLG FQYLRGLFML QLFQNSLSGT IPPKLGWYSD LWVLDMSDNH
LSGRIPSYLC LHSNMIILNL GTNNLSGNIP TGITTCKTLV QLRLARNNLV GRFPSNLCKQ
VNVTAIELGQ NRFRGSIPRE VGNCSALQRL QLADNGFTGE LPREIGMLSQ LGTLNISSNK
LTGEVPSEIF NCKMLQRLDM CCNNFSGTLP SEVGSLYQLE LLKLSNNNLS GTIPVALGNL
SRLTELQMGG NLFNGSIPRE LGSLTGLQIA LNLSYNKLTG EIPPELSNLV MLEFLLLNNN
NLSGEIPSSF ANLSSLLGYN FSYNSLTGPI PLLRNISMSS FIGNEGLCGP PLNQCIQTQP
FAPSQSTGKP GGMRSSKIIA ITAAVIGGVS LMLIALIVYL MRRPVRTVAS SAQDGQPSEM
SLDIYFPPKE GFTFQDLVAA TDNFDESFVV GRGACGTVYK AVLPAGYTLA VKKLASNHEG
GNNNNVDNSF RAEILTLGNI RHRNIVKLHG FCNHQGSNLL LYEYMPKGSL GEILHDPSCN
LDWSKRFKIA LGAAQGLAYL HHDCKPRIFH RDIKSNNILL DDKFEAHVGD FGLAKVIDMP
HSKSMSAIAG SYGYIAPEYA YTMKVTEKSD IYSYGVVLLE LLTGKAPVQP IDQGGDVVNW
VRSYIRRDAL SSGVLDARLT LEDERIVSHM LTVLKIALLC TSVSPVARPS MRQVVLMLIE
SERSEGEQEH LDTEELTQTT TP
