Y2921_ARATH
ID Y2921_ARATH Reviewed; 881 AA.
AC O65924;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Putative leucine-rich repeat receptor-like protein kinase At2g19210;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At2g19210; ORFNames=F27F23.1;
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 -!- INTERACTION:
CC O65924; Q9LFS4: NIK1; NbExp=3; IntAct=EBI-20662256, EBI-16146189;
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; AC002392; AAM14837.1; -; Genomic_DNA.
DR EMBL; AC003058; AAC16451.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06857.1; -; Genomic_DNA.
DR PIR; T01269; T01269.
DR RefSeq; NP_179511.1; NM_127478.1.
DR AlphaFoldDB; O65924; -.
DR SMR; O65924; -.
DR BioGRID; 1795; 15.
DR IntAct; O65924; 16.
DR STRING; 3702.AT2G19210.1; -.
DR PaxDb; O65924; -.
DR PRIDE; O65924; -.
DR ProteomicsDB; 234593; -.
DR EnsemblPlants; AT2G19210.1; AT2G19210.1; AT2G19210.
DR GeneID; 816438; -.
DR Gramene; AT2G19210.1; AT2G19210.1; AT2G19210.
DR KEGG; ath:AT2G19210; -.
DR Araport; AT2G19210; -.
DR TAIR; locus:2047675; AT2G19210.
DR eggNOG; ENOG502QQCZ; Eukaryota.
DR HOGENOM; CLU_000288_41_1_1; -.
DR InParanoid; O65924; -.
DR OMA; YAMESIR; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; O65924; -.
DR PRO; PR:O65924; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O65924; baseline and differential.
DR Genevisible; O65924; 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; IPR001611; Leu-rich_rpt.
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 Pfam; PF13855; LRR_8; 1.
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.
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..25
FT /evidence="ECO:0000255"
FT CHAIN 26..881
FT /note="Putative leucine-rich repeat receptor-like protein
FT kinase At2g19210"
FT /id="PRO_0000401335"
FT TOPO_DOM 26..518
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 519..539
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 540..881
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 438..460
FT /note="LRR 1"
FT REPEAT 462..483
FT /note="LRR 2"
FT DOMAIN 576..850
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 851..881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 699
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 582..590
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 603
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 648
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 734
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 739
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 747
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 234
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 310
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 404
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 435
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 462
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 881 AA; 98433 MW; B94105659A923A54 CRC64;
MVHYNFLSLI IFACFFAVFV LLVRAQDQSG FVSIDCGIPE DSSYNDETTD IKYVSDAAFV
ESGTIHSIDP EFQTSSLEKQ FQNVRSFPEG NRNCYDVKPP QGKGFKYLIR TRFMYGNYDN
LGKAPDFDLY LGFNIWDSVT IDNATTIVTK EIIHTLRSDH VHVCLVDKNR GTPFLSALEI
RLLKSNTYET PYDSLILFKR WDLGGLGALP VRYKDDVFDR IWIPLRFPKY TIFNASLTID
SNNNEGFQPA RFVMNTATSP EDLSQDIIFS WEPKDPTWKY FVYMHFAEVV ELPSNETREF
KVLLNEKEIN MSSFSPRYLY TDTLFVQNPV SGPKLEFRLQ QTPRSTLPPI INAIETYRVN
EFLQSPTDQQ DVDAIMRIKS KYGVKKSWLG DPCAPVKYPW KDINCSYVDN ESPRIISVNL
SSSGLTGEID AAFSNLTLLH ILDLSNNSLT GKIPDFLGNL HNLTELNLEG NKLSGAIPVK
LLERSNKKLI LLRIDGNPDL CVSASCQISD EKTKKNVYII PLVASVVGVL GLVLAIALFL
LYKKRHRRGG SGGVRAGPLD TTKRYYKYSE VVKVTNNFER VLGQGGFGKV YHGVLNDDQV
AVKILSESSA QGYKEFRAEV ELLLRVHHKN LTALIGYCHE GKKMALIYEF MANGTLGDYL
SGEKSYVLSW EERLQISLDA AQGLEYLHNG CKPPIVQRDV KPANILINEK LQAKIADFGL
SRSVALDGNN QDTTAVAGTI GYLDPEYHLT QKLSEKSDIY SFGVVLLEVV SGQPVIARSR
TTAENIHITD RVDLMLSTGD IRGIVDPKLG ERFDAGSAWK ITEVAMACAS SSSKNRPTMS
HVVAELKESV SRARAGGGSG ASSVTDPAMT NFDSGMFPQA R
