Y2559_ARATH
ID Y2559_ARATH Reviewed; 683 AA.
AC O64639;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Receptor-like serine/threonine-protein kinase At2g45590;
DE EC=2.7.11.1;
GN OrderedLocusNames=At2g45590; ORFNames=F17K2.12;
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=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
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 membrane
CC 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; AC003680; AAC06160.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10574.1; -; Genomic_DNA.
DR EMBL; BT002788; AAO22616.1; -; mRNA.
DR EMBL; BT005124; AAO50657.1; -; mRNA.
DR PIR; T00872; T00872.
DR RefSeq; NP_182083.1; NM_130121.4.
DR AlphaFoldDB; O64639; -.
DR SMR; O64639; -.
DR STRING; 3702.AT2G45590.1; -.
DR iPTMnet; O64639; -.
DR PaxDb; O64639; -.
DR PRIDE; O64639; -.
DR ProteomicsDB; 242359; -.
DR EnsemblPlants; AT2G45590.1; AT2G45590.1; AT2G45590.
DR GeneID; 819167; -.
DR Gramene; AT2G45590.1; AT2G45590.1; AT2G45590.
DR KEGG; ath:AT2G45590; -.
DR Araport; AT2G45590; -.
DR TAIR; locus:2043629; AT2G45590.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_011728_0_0_1; -.
DR InParanoid; O64639; -.
DR OMA; GESPEKM; -.
DR OrthoDB; 337129at2759; -.
DR PhylomeDB; O64639; -.
DR PRO; PR:O64639; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O64639; baseline and differential.
DR Genevisible; O64639; 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 InterPro; IPR044576; At4g25390-like.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR46821; PTHR46821; 1.
DR Pfam; PF00069; Pkinase; 2.
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 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding; Receptor;
KW Reference proteome; Serine/threonine-protein kinase; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..683
FT /note="Receptor-like serine/threonine-protein kinase
FT At2g45590"
FT /id="PRO_0000403334"
FT TOPO_DOM 1..30
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 52..683
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 92..664
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 223
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 98..106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 683 AA; 75554 MW; FA195E4C898FBEFA CRC64;
MPSRLSPPDI PPLQPTPTVS DGHHRFQTLP LIIAGSLTLT GVLLILVTLL IYRRLYRNRT
APSDLISNSK SPQHYQCRRF SYSQLRRATN SFSESTHLGH GGFGSVYKAD FPSGGDSLAV
KVMDTSAGSL QGEREFHNEL SLSSHLIGSP HVVSLLGFSS DRRGRKLILV YELMANRSLQ
DALLDRKCVE LMDWNKRFEI ATDIAKGIEF LHHCCDPIII HGDIKPSNIL LDSDFKAKIG
DFGLARVKSE DFDTRILIEE EDKSKDVVED NGSILEETES VITVFEEGNN VVNLSPETCG
ISVLTETVAS PGEKSGLSPE NCAVSILTVE VGAASPAMAS IPSPETCAIS VLTDTGLSPE
SSKLKVGSKR DWWWKQDNNG GSRGGIESGS VKDYVMEWIG SEIKKERPSN NKEWINNGDG
SSSVSKKKKK EKKRKPREWW KEEFCEELTR KKRKKKKKKK RGLSSISSID SWFHRDDGAS
SVHDHNLNPT KRKKRNSIDW WVDGLSGELK SVMGKKNSQD SGLWCDVNVQ KSGGVSSTPS
MRGTVCYIAP ECGGGGVLSE KCDVYSFGVL LLVLVSGRRP LQVTASPMSE FERANLISWA
KQLACNGKLL ELVDKSIHSL EKEQAVLCIT IALLCLQRSP VKRPTMKEIV EMLSGVSEPP
HLPFEFSPSP PMGFPFKSRK KAR
