RPK2_ARATH
ID RPK2_ARATH Reviewed; 1151 AA.
AC Q9S7I6; C0LGM5; Q8GYR1;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=LRR receptor-like serine/threonine-protein kinase RPK2;
DE EC=2.7.11.1;
DE AltName: Full=Protein TOADSTOOL 2;
DE AltName: Full=Receptor-like protein kinase 2;
DE Flags: Precursor;
GN Name=RPK2; Synonyms=TOAD2; OrderedLocusNames=At3g02130;
GN ORFNames=F14P3.22, F1C9.8;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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] OF 166-1151.
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 167-1151.
RC STRAIN=cv. Columbia;
RX PubMed=20064227; DOI=10.1186/1471-2164-11-19;
RA Gou X., He K., Yang H., Yuan T., Lin H., Clouse S.D., Li J.;
RT "Genome-wide cloning and sequence analysis of leucine-rich repeat receptor-
RT like protein kinase genes in Arabidopsis thaliana.";
RL BMC Genomics 11:19-19(2010).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=17543866; DOI=10.1016/j.devcel.2007.04.003;
RA Nodine M.D., Yadegari R., Tax F.E.;
RT "RPK1 and TOAD2 are two receptor-like kinases redundantly required for
RT arabidopsis embryonic pattern formation.";
RL Dev. Cell 12:943-956(2007).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY,
RP INDUCTION BY DEHYDRATION AND LOW TEMPERATURE, AND DISRUPTION PHENOTYPE.
RX PubMed=17419837; DOI=10.1111/j.1365-313x.2007.03083.x;
RA Mizuno S., Osakabe Y., Maruyama K., Ito T., Osakabe K., Sato T.,
RA Shinozaki K., Yamaguchi-Shinozaki K.;
RT "Receptor-like protein kinase 2 (RPK 2) is a novel factor controlling
RT anther development in Arabidopsis thaliana.";
RL Plant J. 50:751-766(2007).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=18158146; DOI=10.1016/j.ydbio.2007.11.021;
RA Nodine M.D., Tax F.E.;
RT "Two receptor-like kinases required together for the establishment of
RT Arabidopsis cotyledon primordia.";
RL Dev. Biol. 314:161-170(2008).
CC -!- FUNCTION: Key regulator of anther development (e.g. lignification
CC pattern), including tapetum degradation during pollen maturation (e.g.
CC germination capacity). Together with RPK1, required for pattern
CC formation along the radial axis (e.g. the apical embryonic domain cell
CC types that generate cotyledon primordia), and the apical-basal axis
CC (e.g. differentiation of the basal pole during early embryogenesis).
CC {ECO:0000269|PubMed:17419837, ECO:0000269|PubMed:17543866,
CC ECO:0000269|PubMed:18158146}.
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 Q9S7I6; Q9SUQ3: At4g23740; NbExp=4; IntAct=EBI-16940204, EBI-16912451;
CC Q9S7I6; O22476: BRI1; NbExp=2; IntAct=EBI-16940204, EBI-1797828;
CC Q9S7I6; Q9FL28: FLS2; NbExp=2; IntAct=EBI-16940204, EBI-1799448;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17419837,
CC ECO:0000269|PubMed:17543866, ECO:0000269|PubMed:18158146}; Single-pass
CC type I membrane protein {ECO:0000269|PubMed:17419837,
CC ECO:0000269|PubMed:17543866, ECO:0000269|PubMed:18158146}.
CC -!- TISSUE SPECIFICITY: Expressed in root tips, flowers, leaf meristems,
CC and the bottom parts of the surrounding young leaves and trichomes.
CC {ECO:0000269|PubMed:17419837}.
CC -!- DEVELOPMENTAL STAGE: First detected in the central domain protodermal
CC cells when cotyledon primordia become recognizable, at the early
CC globular stage. Later observed throughout the central domain and basal
CC domain of the embryo proper. After bolting, localized in axillary buds
CC and premature anthers. Abundant in the tapetum of wild-type anthers
CC during microspore maturation. {ECO:0000269|PubMed:17419837,
CC ECO:0000269|PubMed:17543866, ECO:0000269|PubMed:18158146}.
CC -!- INDUCTION: Slightly by dehydration and low temperature.
CC {ECO:0000269|PubMed:17419837}.
CC -!- DISRUPTION PHENOTYPE: Impaired central domain protoderm patterning
CC defects, and defective cotyledon primordia cell types. Enhanced shoot
CC growth, and male sterility due to defects in anther dehiscence and
CC pollen maturation. {ECO:0000269|PubMed:17419837,
CC ECO:0000269|PubMed:18158146}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC42107.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC42107.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC009755; AAF02124.1; -; Genomic_DNA.
DR EMBL; AC011664; AAF14849.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73767.1; -; Genomic_DNA.
DR EMBL; FJ708715; ACN59310.1; -; mRNA.
DR EMBL; AK117442; BAC42107.1; ALT_SEQ; mRNA.
DR RefSeq; NP_186862.3; NM_111080.4.
DR AlphaFoldDB; Q9S7I6; -.
DR SMR; Q9S7I6; -.
DR BioGRID; 6573; 56.
DR IntAct; Q9S7I6; 42.
DR STRING; 3702.AT3G02130.1; -.
DR PaxDb; Q9S7I6; -.
DR PRIDE; Q9S7I6; -.
DR ProteomicsDB; 227959; -.
DR EnsemblPlants; AT3G02130.1; AT3G02130.1; AT3G02130.
DR GeneID; 821240; -.
DR Gramene; AT3G02130.1; AT3G02130.1; AT3G02130.
DR KEGG; ath:AT3G02130; -.
DR Araport; AT3G02130; -.
DR TAIR; locus:2076512; AT3G02130.
DR eggNOG; ENOG502QSHG; Eukaryota.
DR HOGENOM; CLU_000288_114_2_1; -.
DR InParanoid; Q9S7I6; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; Q9S7I6; -.
DR PRO; PR:Q9S7I6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9S7I6; baseline and differential.
DR Genevisible; Q9S7I6; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
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:0048653; P:anther development; IMP:UniProtKB.
DR GO; GO:0048508; P:embryonic meristem development; IMP:UniProtKB.
DR GO; GO:0009808; P:lignin metabolic process; IMP:TAIR.
DR GO; GO:0009942; P:longitudinal axis specification; IMP:UniProtKB.
DR GO; GO:0010073; P:meristem maintenance; IMP:TAIR.
DR GO; GO:0009846; P:pollen germination; IMP:UniProtKB.
DR GO; GO:0010152; P:pollen maturation; IMP:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0009945; P:radial axis specification; IMP:UniProtKB.
DR GO; GO:0009409; P:response to cold; IEP:UniProtKB.
DR GO; GO:0009414; P:response to water deprivation; IEP:UniProtKB.
DR Gene3D; 3.80.10.10; -; 4.
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; IPR013210; LRR_N_plant-typ.
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; 1.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 9.
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; Developmental protein; Glycoprotein; Kinase;
KW Leucine-rich repeat; Membrane; Nucleotide-binding; Phosphoprotein;
KW Receptor; Reference proteome; Repeat; Serine/threonine-protein kinase;
KW Signal; Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..1151
FT /note="LRR receptor-like serine/threonine-protein kinase
FT RPK2"
FT /id="PRO_0000387523"
FT TOPO_DOM 36..811
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 812..832
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 833..1151
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 85..108
FT /note="LRR 1"
FT REPEAT 143..167
FT /note="LRR 2"
FT REPEAT 168..190
FT /note="LRR 3"
FT REPEAT 192..215
FT /note="LRR 4"
FT REPEAT 216..241
FT /note="LRR 5"
FT REPEAT 261..285
FT /note="LRR 6"
FT REPEAT 287..308
FT /note="LRR 7"
FT REPEAT 309..333
FT /note="LRR 8"
FT REPEAT 341..368
FT /note="LRR 9"
FT REPEAT 387..410
FT /note="LRR 10"
FT REPEAT 411..435
FT /note="LRR 11"
FT REPEAT 436..459
FT /note="LRR 12"
FT REPEAT 461..481
FT /note="LRR 13"
FT REPEAT 542..565
FT /note="LRR 14"
FT REPEAT 567..581
FT /note="LRR 15"
FT REPEAT 585..608
FT /note="LRR 16"
FT REPEAT 610..633
FT /note="LRR 17"
FT REPEAT 634..657
FT /note="LRR 18"
FT REPEAT 658..681
FT /note="LRR 19"
FT REPEAT 682..706
FT /note="LRR 20"
FT REPEAT 707..729
FT /note="LRR 21"
FT REPEAT 731..752
FT /note="LRR 22"
FT DOMAIN 874..1146
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 772..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 996
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 880..888
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 902
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 863
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 871
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 947
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 983
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 1038
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 1046
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 481
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 540
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 591
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 640
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 670
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 708
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 718
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 734
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 739
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1151 AA; 125230 MW; 86DECE2E18F11326 CRC64;
MTSLPSSVIK WRFFRRQMPS DVVFSLCLLC FASCLAGKIT VLADSDKSVL LRFKKTVSDP
GSILASWVEE SEDYCSWFGV SCDSSSRVMA LNISGSGSSE ISRNRFTCGD IGKFPLYGFG
VRRDCTGNHG ALAGNLPSVI MSLTGLRVLS LPFNSFSGEI PVGIWGMEKL EVLDLEGNLM
TGSLPDQFTG LRNLRVMNLG FNRVSGEIPN SLQNLTKLEI LNLGGNKLNG TVPGFVGRFR
VLHLPLNWLQ GSLPKDIGDS CGKLEHLDLS GNFLTGRIPE SLGKCAGLRS LLLYMNTLEE
TIPLEFGSLQ KLEVLDVSRN TLSGPLPVEL GNCSSLSVLV LSNLYNVYED INSVRGEADL
PPGADLTSMT EDFNFYQGGI PEEITRLPKL KILWVPRATL EGRFPGDWGS CQNLEMVNLG
QNFFKGEIPV GLSKCKNLRL LDLSSNRLTG ELLKEISVPC MSVFDVGGNS LSGVIPDFLN
NTTSHCPPVV YFDRFSIESY SDPSSVYLSF FTEKAQVGTS LIDLGSDGGP AVFHNFADNN
FTGTLKSIPL AQERLGKRVS YIFSAGGNRL YGQFPGNLFD NCDELKAVYV NVSFNKLSGR
IPQGLNNMCT SLKILDASVN QIFGPIPTSL GDLASLVALN LSWNQLQGQI PGSLGKKMAA
LTYLSIANNN LTGQIPQSFG QLHSLDVLDL SSNHLSGGIP HDFVNLKNLT VLLLNNNNLS
GPIPSGFATF AVFNVSSNNL SGPVPSTNGL TKCSTVSGNP YLRPCHVFSL TTPSSDSRDS
TGDSITQDYA SSPVENAPSQ SPGKGGFNSL EIASIASASA IVSVLIALVI LFFYTRKWHP
KSKIMATTKR EVTMFMDIGV PITFDNVVRA TGNFNASNLI GNGGFGATYK AEISQDVVVA
IKRLSIGRFQ GVQQFHAEIK TLGRLRHPNL VTLIGYHASE TEMFLVYNYL PGGNLEKFIQ
ERSTRDWRVL HKIALDIARA LAYLHDQCVP RVLHRDVKPS NILLDDDCNA YLSDFGLARL
LGTSETHATT GVAGTFGYVA PEYAMTCRVS DKADVYSYGV VLLELLSDKK ALDPSFVSYG
NGFNIVQWAC MLLRQGRAKE FFTAGLWDAG PHDDLVEVLH LAVVCTVDSL STRPTMKQVV
RRLKQLQPPS C
