Y2923_ARATH
ID Y2923_ARATH Reviewed; 877 AA.
AC O64556; F4ISF9;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 3.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Putative leucine-rich repeat receptor-like serine/threonine-protein kinase At2g19230;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN OrderedLocusNames=At2g19230; ORFNames=F27F23.3;
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=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 O64556; A0A1I9LQ53: At3g50230; NbExp=2; IntAct=EBI-20662335, EBI-20654045;
CC O64556; Q9FK10: At5g53320; NbExp=4; IntAct=EBI-20662335, EBI-20654730;
CC O64556; Q9LVI6: RLK902; NbExp=4; IntAct=EBI-20662335, EBI-1626936;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AEC06859.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC003058; AAC16453.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06859.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; ANM63021.1; -; Genomic_DNA.
DR PIR; T01271; T01271.
DR RefSeq; NP_001325138.1; NM_001335627.1.
DR RefSeq; NP_179513.4; NM_127480.4.
DR AlphaFoldDB; O64556; -.
DR SMR; O64556; -.
DR BioGRID; 1797; 33.
DR IntAct; O64556; 36.
DR STRING; 3702.AT2G19230.1; -.
DR PaxDb; O64556; -.
DR PRIDE; O64556; -.
DR ProteomicsDB; 232355; -.
DR EnsemblPlants; AT2G19230.2; AT2G19230.2; AT2G19230.
DR GeneID; 816440; -.
DR Gramene; AT2G19230.2; AT2G19230.2; AT2G19230.
DR KEGG; ath:AT2G19230; -.
DR Araport; AT2G19230; -.
DR eggNOG; KOG1091; Eukaryota.
DR HOGENOM; CLU_000288_41_1_1; -.
DR InParanoid; O64556; -.
DR OMA; WQTINIS; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; O64556; -.
DR PRO; PR:O64556; -.
DR Proteomes; UP000006548; Chromosome 2.
DR Genevisible; O64556; 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; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF13855; LRR_8; 1.
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; 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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..877
FT /note="Putative leucine-rich repeat receptor-like
FT serine/threonine-protein kinase At2g19230"
FT /id="PRO_0000403340"
FT TOPO_DOM 25..517
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 518..538
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 539..877
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 439..462
FT /note="LRR 1"
FT REPEAT 463..484
FT /note="LRR 2"
FT DOMAIN 569..842
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 692
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 575..583
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 596
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 641
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 726
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 727
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 732
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 261
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 405
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 420
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 877 AA; 99011 MW; D4D1F3E3DFEB3660 CRC64;
MGNFNFLPLV SFASFVVVLV LVCAQDQSGF VSIDCGIPED SSYYDEKTDI KYISDAAFVE
SGTIHSIDSK FQKKNLEKQF QKVRSFPEGK KNCYDVQPPQ GKGFKYLIRT RFMYGNYDNL
GKAPDFDLYL GVNLWDSVTL ENSTTIVTKE IIYTLRSDKV HVCLVDKERG TPFLSVLELR
LLKNNIYETA SDSLMLYRRW DLGATGDLPA RYKDDIFDRF WMPLMFPNFL ILNTSLMIDP
TSSNGFLPPS VVMSTAVAPM NSSIEQIMVY WEPRDPNWKF YIYIHFAEVE KLPSNETREF
SVFLNKEQID TTSVFRPSYL YTDTLYVQNP VSGPFLEFVL RQGVKSTRPP IMNAIETYRT
NEFLDLPTDQ NDVDAIMKIK TKYKVKKNWL GDPCAPFGYP WQGINCSYTA NNPPRIISVN
LSFSGLTGQI DPVFITLTPL QKLDLSNNRL TGTVPDFLAN LPDLTELNLE ENKLTGILPE
KLLERSKDGS LSLRVGGNPD LCVSDSCRNK KTERKEYIIP SVASVTGLFF LLLALISFWQ
FKKRQQSVKT GPLDTKRYYK YSEIVEITNN FERVLGQGGF GKVYYGVLRG EQVAIKMLSK
SSAQGYKEFR AEVELLLRVH HKNLIALIGY CHEGDQMALI YEYIGNGTLG DYLSGKNSSI
LSWEERLQIS LDAAQGLEYL HNGCKPPIVH RDVKPTNILI NEKLQAKIAD FGLSRSFTLE
GDSQVSTEVA GTIGYLDPEH YSMQQFSEKS DVYSFGVVLL EVITGQPVIS RSRTEENRHI
SDRVSLMLSK GDIKSIVDPK LGERFNAGLA WKITEVALAC ASESTKTRLT MSQVVAELKE
SLCRARTSGD SGDISFSEPT EMNVSMTVDP GVLPQPR
