Y2451_ARATH
ID Y2451_ARATH Reviewed; 868 AA.
AC Q9ZQR3;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Leucine-rich repeat receptor-like serine/threonine-protein kinase At2g14510;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At2g14510; ORFNames=T13P21.11;
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).
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 Q9ZQR3; C0LGI5: At1g69990; NbExp=2; IntAct=EBI-20651957, EBI-20651225;
CC Q9ZQR3; Q8VYT3: At4g30520; NbExp=2; IntAct=EBI-20651957, EBI-16902452;
CC Q9ZQR3; Q9ASS4: At5g48380; NbExp=2; IntAct=EBI-20651957, EBI-6298290;
CC Q9ZQR3; A0A178UFM8: AXX17_At5g50380; NbExp=2; IntAct=EBI-20651957, EBI-20653342;
CC Q9ZQR3; Q94F62: BAK1; NbExp=2; IntAct=EBI-20651957, EBI-617138;
CC Q9ZQR3; Q6XAT2: ERL2; NbExp=2; IntAct=EBI-20651957, EBI-16895926;
CC Q9ZQR3; Q9ZRF9: RPK1; NbExp=2; IntAct=EBI-20651957, EBI-1238953;
CC Q9ZQR3; Q8RWZ1: SUB; NbExp=2; IntAct=EBI-20651957, EBI-17072125;
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; AC006067; AAD15465.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06307.1; -; Genomic_DNA.
DR EMBL; FJ708693; ACN59288.1; -; mRNA.
DR PIR; A84518; A84518.
DR RefSeq; NP_179057.1; NM_127014.2.
DR AlphaFoldDB; Q9ZQR3; -.
DR SMR; Q9ZQR3; -.
DR BioGRID; 1297; 26.
DR IntAct; Q9ZQR3; 31.
DR STRING; 3702.AT2G14510.1; -.
DR PaxDb; Q9ZQR3; -.
DR PRIDE; Q9ZQR3; -.
DR EnsemblPlants; AT2G14510.1; AT2G14510.1; AT2G14510.
DR GeneID; 815938; -.
DR Gramene; AT2G14510.1; AT2G14510.1; AT2G14510.
DR KEGG; ath:AT2G14510; -.
DR Araport; AT2G14510; -.
DR TAIR; locus:2055165; AT2G14510.
DR eggNOG; ENOG502QQCZ; Eukaryota.
DR HOGENOM; CLU_000288_41_1_1; -.
DR InParanoid; Q9ZQR3; -.
DR OMA; AKSMIAN; -.
DR PhylomeDB; Q9ZQR3; -.
DR PRO; PR:Q9ZQR3; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZQR3; baseline and differential.
DR Genevisible; Q9ZQR3; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..868
FT /note="Leucine-rich repeat receptor-like serine/threonine-
FT protein kinase At2g14510"
FT /id="PRO_0000403344"
FT TOPO_DOM 24..510
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 511..531
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 532..868
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..482
FT /note="LRR 3"
FT DOMAIN 563..832
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 687
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 569..577
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 590
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 635
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 721
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 722
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 727
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 735
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 48
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 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 433
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 446
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 495
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 868 AA; 97635 MW; D4FA7FEEE96F2928 CRC64;
METRNKFMLL ACATFSIMSL VKSQNQQGFI SLDCGLPSKE SYIEPSSNLT FISDVNFIRG
GKTGNIQNNS RTNFIFKPFK VLRYFPDGIR NCYSLSVKQG TKYLIRTLFY YGNYDGLNTS
PRFDLFLGPN IWTSVDVLIA DVGDGVVEEI VHVTRSNILD ICLVKTGTST PMISAIELRP
LRYDTYTART GSLKSMAHFY FTNSDEAIRY PEDVYDRVWM PYSQPEWTQI NTTRNVSGFS
DGYNPPQGVI QTASIPTNGS EPLTFTWNLE SSDDETYAYL FFAEIQQLKV NETREFKILA
NGVDYIDYTP WKFEARTLSN PAPLKCEGGV CRVQLSKTPK STLPPLMNAI EIFSVIQFPQ
SDTNTDEVIA IKKIQSTYQL SRISWQGDPC VPKQFSWMGV SCNVIDISTP PRIISLDLSL
SGLTGVISPS IQNLTMLREL DLSNNNLTGE VPEFLATIKP LLVIHLRGNN LRGSVPQALQ
DREKNDGLKL FVDPNITRRG KHQPKSWLVA IVASISCVAV TIIVLVLIFI FRRRKSSTRK
VIRPSLEMKN RRFKYSEVKE MTNNFEVVLG KGGFGVVYHG FLNNEQVAVK VLSQSSTQGY
KEFKTEVELL LRVHHVNLVS LVGYCDEGID LALIYEFMEN GNLKEHLSGK RGGSVLNWSS
RLKIAIESAL GIEYLHIGCQ PPMVHRDVKS TNILLGLRFE AKLADFGLSR SFLVGSQAHV
STNVAGTLGY LDPEYYLKNW LTEKSDVYSF GIVLLESITG QPVIEQSRDK SYIVEWAKSM
LANGDIESIM DPNLHQDYDS SSSWKALELA MLCINPSSTQ RPNMTRVAHE LNECLEIYNL
TKIRSQDQNS SKSLGHTVTF ISDIPSAR
