Y2241_ARATH
ID Y2241_ARATH Reviewed; 980 AA.
AC Q9ZUI0;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Putative leucine-rich repeat receptor-like serine/threonine-protein kinase At2g24130;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At2g24130; ORFNames=F27D4.4;
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).
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 -!- 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; AC005967; AAD03374.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07532.1; -; Genomic_DNA.
DR PIR; H84632; H84632.
DR RefSeq; NP_179990.1; NM_127974.1.
DR AlphaFoldDB; Q9ZUI0; -.
DR SMR; Q9ZUI0; -.
DR BioGRID; 2299; 9.
DR STRING; 3702.AT2G24130.1; -.
DR PaxDb; Q9ZUI0; -.
DR EnsemblPlants; AT2G24130.1; AT2G24130.1; AT2G24130.
DR GeneID; 816947; -.
DR Gramene; AT2G24130.1; AT2G24130.1; AT2G24130.
DR KEGG; ath:AT2G24130; -.
DR Araport; AT2G24130; -.
DR TAIR; locus:2047525; AT2G24130.
DR eggNOG; ENOG502QPTD; Eukaryota.
DR HOGENOM; CLU_000288_22_0_1; -.
DR InParanoid; Q9ZUI0; -.
DR OMA; RPGMARC; -.
DR PhylomeDB; Q9ZUI0; -.
DR PRO; PR:Q9ZUI0; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZUI0; baseline and differential.
DR Genevisible; Q9ZUI0; 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; -; 3.
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; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00560; LRR_1; 2.
DR Pfam; PF13516; LRR_6; 1.
DR Pfam; PF13855; LRR_8; 3.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 9.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51450; LRR; 17.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..980
FT /note="Putative leucine-rich repeat receptor-like
FT serine/threonine-protein kinase At2g24130"
FT /id="PRO_0000401359"
FT TOPO_DOM 21..593
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 594..614
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 615..980
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 65..89
FT /note="LRR 1"
FT REPEAT 90..113
FT /note="LRR 2"
FT REPEAT 115..138
FT /note="LRR 3"
FT REPEAT 139..162
FT /note="LRR 4"
FT REPEAT 165..189
FT /note="LRR 5"
FT REPEAT 191..214
FT /note="LRR 6"
FT REPEAT 215..238
FT /note="LRR 7"
FT REPEAT 240..263
FT /note="LRR 8"
FT REPEAT 271..295
FT /note="LRR 9"
FT REPEAT 296..320
FT /note="LRR 10"
FT REPEAT 322..344
FT /note="LRR 11"
FT REPEAT 345..370
FT /note="LRR 12"
FT REPEAT 372..391
FT /note="LRR 13"
FT REPEAT 392..416
FT /note="LRR 14"
FT REPEAT 417..440
FT /note="LRR 15"
FT REPEAT 442..463
FT /note="LRR 16"
FT REPEAT 464..490
FT /note="LRR 17"
FT REPEAT 491..514
FT /note="LRR 18"
FT REPEAT 515..537
FT /note="LRR 19"
FT REPEAT 539..563
FT /note="LRR 20"
FT DOMAIN 661..960
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 788
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 667..675
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 689
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 658
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 775
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 841
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 380
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 428
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 497
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 545
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 554
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 980 AA; 107791 MW; A081BD7137A51987 CRC64;
MDYCSLLVVS FLITVMTVLA SKENDHELIK NPQNSLSSWI SSSSSSSSML VDVCNWSGVK
CNKESTQVIE LDISGRDLGG EISPSIANLT GLTVLDLSRN FFVGKIPPEI GSLHETLKQL
SLSENLLHGN IPQELGLLNR LVYLDLGSNR LNGSIPVQLF CNGSSSSLQY IDLSNNSLTG
EIPLNYHCHL KELRFLLLWS NKLTGTVPSS LSNSTNLKWM DLESNMLSGE LPSQVISKMP
QLQFLYLSYN HFVSHNNNTN LEPFFASLAN SSDLQELELA GNSLGGEITS SVRHLSVNLV
QIHLDQNRIH GSIPPEISNL LNLTLLNLSS NLLSGPIPRE LCKLSKLERV YLSNNHLTGE
IPMELGDIPR LGLLDVSRNN LSGSIPDSFG NLSQLRRLLL YGNHLSGTVP QSLGKCINLE
ILDLSHNNLT GTIPVEVVSN LRNLKLYLNL SSNHLSGPIP LELSKMDMVL SVDLSSNELS
GKIPPQLGSC IALEHLNLSR NGFSSTLPSS LGQLPYLKEL DVSFNRLTGA IPPSFQQSST
LKHLNFSFNL LSGNVSDKGS FSKLTIESFL GDSLLCGSIK GMQACKKKHK YPSVLLPVLL
SLIATPVLCV FGYPLVQRSR FGKNLTVYAK EEVEDEEKQN QNDPKYPRIS YQQLIAATGG
FNASSLIGSG RFGHVYKGVL RNNTKVAVKV LDPKTALEFS GSFKRECQIL KRTRHRNLIR
IITTCSKPGF NALVLPLMPN GSLERHLYPG EYSSKNLDLI QLVNICSDVA EGIAYLHHYS
PVKVVHCDLK PSNILLDDEM TALVTDFGIS RLVQGVEETV STDDSVSFGS TDGLLCGSVG
YIAPEYGMGK RASTHGDVYS FGVLLLEIVS GRRPTDVLVN EGSSLHEFMK SHYPDSLEGI
IEQALSRWKP QGKPEKCEKL WREVILEMIE LGLVCTQYNP STRPDMLDVA HEMGRLKEYL
FACPSLLHFS SQETQGEASS
