Y2232_ARATH
ID Y2232_ARATH Reviewed; 834 AA.
AC O22187;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Probable receptor-like protein kinase At2g23200;
DE EC=2.7.11.-;
DE Flags: Precursor;
GN OrderedLocusNames=At2g23200; ORFNames=T20D16.17;
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 GENE FAMILY.
RX PubMed=19529822; DOI=10.1093/mp/ssn083;
RA Chae L., Sudat S., Dudoit S., Zhu T., Luan S.;
RT "Diverse transcriptional programs associated with environmental stress and
RT hormones in the Arabidopsis receptor-like kinase gene family.";
RL Mol. Plant 2:84-107(2009).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
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; AC002391; AAB87113.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07428.1; -; Genomic_DNA.
DR PIR; T00512; T00512.
DR RefSeq; NP_179901.1; NM_127884.4.
DR AlphaFoldDB; O22187; -.
DR SMR; O22187; -.
DR BioGRID; 2205; 2.
DR IntAct; O22187; 2.
DR STRING; 3702.AT2G23200.1; -.
DR iPTMnet; O22187; -.
DR PaxDb; O22187; -.
DR PRIDE; O22187; -.
DR ProteomicsDB; 243060; -.
DR EnsemblPlants; AT2G23200.1; AT2G23200.1; AT2G23200.
DR GeneID; 816852; -.
DR Gramene; AT2G23200.1; AT2G23200.1; AT2G23200.
DR KEGG; ath:AT2G23200; -.
DR Araport; AT2G23200; -.
DR TAIR; locus:2058636; AT2G23200.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_42_1_1; -.
DR InParanoid; O22187; -.
DR OMA; TAQQPNY; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; O22187; -.
DR PRO; PR:O22187; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O22187; baseline and differential.
DR Genevisible; O22187; 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:0005773; C:vacuole; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:InterPro.
DR GO; GO:0046777; P:protein autophosphorylation; IBA:GO_Central.
DR InterPro; IPR045272; ANXUR1-like.
DR InterPro; IPR011009; Kinase-like_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 PANTHER; PTHR27003; PTHR27003; 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.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding; Glycoprotein; Kinase; Membrane; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Signal; Transferase;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..834
FT /note="Probable receptor-like protein kinase At2g23200"
FT /id="PRO_0000386553"
FT TOPO_DOM 29..405
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 427..834
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 488..761
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 613
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 494..502
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 516
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 314
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 834 AA; 93379 MW; 17C311B80AED7ED4 CRC64;
MENFCFQDSV SLFITIMVLV LLPRLSLSDT STYTRPENFY VNCGSDSNVF YGGQTFVGDT
NSSTNSVSFT NKGTEVINDQ SSVAPEIYRT VRIFRHPSSY KFKLDSLGLH FVRLHFSVVF
SRADLLTARF TVSATSGSNH HLKSFSPQNL TNTPRVEEFL LMMNSLEFEI RFVPDHSSLA
LINAIEVFSA PDDLEIPSAS DKNLHTIYRL NVGGEKITPD NDTLGRTWLP DDDDFLYRKD
SARNINSTQT PNYVGGLSSA TDSTAPDFVY KTAKAMNRSS NEQVGMLMNV TWSFKVKSNH
RHFIRIHFSD ILSNLSNSDS DFYLFVNGYW RVDVKPSEQP RLASPFFKDV VNVSDGSGLL
NISIGTKEAN KDAGFLNGLE MMEVLSKSGS DYSNRSSSRV HIITGCAVAA AAASALVFSL
LFMVFLKRRR SKKTKPEVEG TVWSPLPLHR GGSSDNRPIS QYHNSPLRNL HLGLTIPFTD
ILSATNNFDE QLLIGKGGFG YVYKAILPDG TKAAIKRGKT GSGQGILEFQ TEIQVLSRIR
HRHLVSLTGY CEENSEMILV YEFMEKGTLK EHLYGSNLPS LTWKQRLEIC IGAARGLDYL
HSSGSEGAII HRDVKSTNIL LDEHNIAKVA DFGLSKIHNQ DESNISINIK GTFGYLDPEY
LQTHKLTEKS DVYAFGVVLL EVLFARPAID PYLPHEEVNL SEWVMFCKSK GTIDEILDPS
LIGQIETNSL KKFMEIAEKC LKEYGDERPS MRDVIWDLEY VLQLQMMTNR REAHEEDSTA
INSGGSLVAP RLMVSDSFST NSIFQNGDES KNRFGFTDSS ETRVFSQLKI SDAR
