RPK1_ARATH
ID RPK1_ARATH Reviewed; 540 AA.
AC Q9ZRF9; Q9LQ97;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Probable LRR receptor-like serine/threonine-protein kinase RPK1;
DE EC=2.7.11.1;
DE AltName: Full=Protein TOADSTOOL 1;
DE AltName: Full=Receptor-like protein kinase 1;
DE Flags: Precursor;
GN Name=RPK1; Synonyms=TOAD1; OrderedLocusNames=At1g69270;
GN ORFNames=F23O10.15, F4N2.23;
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 [MRNA], TISSUE SPECIFICITY, AND INDUCTION BY ABA;
RP DEHYDRATION; HIGH SALT AND LOW TEMPERATURE.
RC STRAIN=cv. Columbia; TISSUE=Flower;
RX PubMed=9112773; DOI=10.1104/pp.113.4.1203;
RA Hong S.W., Jon J.H., Kwak J.M., Nam H.G.;
RT "Identification of a receptor-like protein kinase gene rapidly induced by
RT abscisic acid, dehydration, high salt, and cold treatments in Arabidopsis
RT thaliana.";
RL Plant Physiol. 113:1203-1212(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
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 [4]
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).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND INDUCTION BY
RP ABSCISIC ACID.
RX PubMed=15772289; DOI=10.1105/tpc.104.027474;
RA Osakabe Y., Maruyama K., Seki M., Satou M., Shinozaki K.,
RA Yamaguchi-Shinozaki K.;
RT "Leucine-rich repeat receptor-like kinase1 is a key membrane-bound
RT regulator of abscisic acid early signaling in Arabidopsis.";
RL Plant Cell 17:1105-1119(2005).
RN [7]
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 [8]
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: Involved in the main abscisic acid-mediated (ABA) signaling
CC pathway and in early ABA perception. Together with RPK2, required for
CC pattern formation along the radial axis (e.g. the apical embryonic
CC domain cell types that generate cotyledon primordia), and the apical-
CC basal axis (e.g. differentiation of the basal pole during early
CC embryogenesis). {ECO:0000269|PubMed:15772289,
CC ECO:0000269|PubMed:17543866, 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 Q9ZRF9; O04567: At1g27190; NbExp=2; IntAct=EBI-1238953, EBI-1238687;
CC Q9ZRF9; C0LGI5: At1g69990; NbExp=3; IntAct=EBI-1238953, EBI-20651225;
CC Q9ZRF9; Q9ZQR3: At2g14510; NbExp=2; IntAct=EBI-1238953, EBI-20651957;
CC Q9ZRF9; Q8VYT3: At4g30520; NbExp=4; IntAct=EBI-1238953, EBI-16902452;
CC Q9ZRF9; Q9ASS4: At5g48380; NbExp=2; IntAct=EBI-1238953, EBI-6298290;
CC Q9ZRF9; Q94F62: BAK1; NbExp=4; IntAct=EBI-1238953, EBI-617138;
CC Q9ZRF9; Q9LJF3: BRL3; NbExp=2; IntAct=EBI-1238953, EBI-20651413;
CC Q9ZRF9; Q42371: ERECTA; NbExp=3; IntAct=EBI-1238953, EBI-16940407;
CC Q9ZRF9; C0LGW6: ERL1; NbExp=3; IntAct=EBI-1238953, EBI-16914248;
CC Q9ZRF9; Q6XAT2: ERL2; NbExp=3; IntAct=EBI-1238953, EBI-16895926;
CC Q9ZRF9; C0LGX3: HSL2; NbExp=2; IntAct=EBI-1238953, EBI-16904927;
CC Q9ZRF9; Q9C8I6: IOS1; NbExp=4; IntAct=EBI-1238953, EBI-16924837;
CC Q9ZRF9; Q9ZVD4: LRR-RLK; NbExp=2; IntAct=EBI-1238953, EBI-20651739;
CC Q9ZRF9; Q9LFS4: NIK1; NbExp=4; IntAct=EBI-1238953, EBI-16146189;
CC Q9ZRF9; Q9C7S5: PSY1R; NbExp=2; IntAct=EBI-1238953, EBI-16904988;
CC Q9ZRF9; Q9ZRF9: RPK1; NbExp=2; IntAct=EBI-1238953, EBI-1238953;
CC Q9ZRF9; Q8LPS5: SERK5; NbExp=2; IntAct=EBI-1238953, EBI-16887868;
CC Q9ZRF9; Q9C8M9: SRF6; NbExp=2; IntAct=EBI-1238953, EBI-16954301;
CC Q9ZRF9; Q8RWZ1: SUB; NbExp=2; IntAct=EBI-1238953, EBI-17072125;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15772289,
CC ECO:0000269|PubMed:17543866, ECO:0000269|PubMed:18158146}; Single-pass
CC type I membrane protein {ECO:0000269|PubMed:15772289,
CC ECO:0000269|PubMed:17543866, ECO:0000269|PubMed:18158146}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, and flowers.
CC {ECO:0000269|PubMed:9112773}.
CC -!- DEVELOPMENTAL STAGE: First detected in the suspensor cells of octant-
CC stage embryos, in the basal plasma membrane of the basal-most cell of
CC the suspensor, which is in direct contact with maternal tissue.
CC Expressed in the central domain protodermal cells when cotyledon
CC primordia become recognizable. Later observed throughout the central
CC domain and basal domain of the embryo proper, as well as the suspensor.
CC {ECO:0000269|PubMed:17543866, ECO:0000269|PubMed:18158146}.
CC -!- INDUCTION: By ABA (at protein level), dehydration, high salt levels,
CC and low temperature. {ECO:0000269|PubMed:15772289,
CC ECO:0000269|PubMed:9112773}.
CC -!- DISRUPTION PHENOTYPE: Decreased sensitivity to ABA during germination,
CC growth, and stomatal closure. Impaired central domain protoderm
CC patterning defects, and defective cotyledon primordia cell types.
CC {ECO:0000269|PubMed:15772289, 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=AAF27063.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U55875; AAD11518.1; -; mRNA.
DR EMBL; AC008262; AAF27063.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC018364; AAG52484.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34904.1; -; Genomic_DNA.
DR EMBL; AY099858; AAM20709.1; -; mRNA.
DR EMBL; BT008896; AAP68335.1; -; mRNA.
DR EMBL; FJ708674; ACN59269.1; -; mRNA.
DR PIR; G96716; G96716.
DR RefSeq; NP_177087.1; NM_105594.3.
DR AlphaFoldDB; Q9ZRF9; -.
DR SMR; Q9ZRF9; -.
DR BioGRID; 28479; 25.
DR IntAct; Q9ZRF9; 43.
DR STRING; 3702.AT1G69270.1; -.
DR PaxDb; Q9ZRF9; -.
DR PRIDE; Q9ZRF9; -.
DR ProteomicsDB; 228237; -.
DR EnsemblPlants; AT1G69270.1; AT1G69270.1; AT1G69270.
DR GeneID; 843258; -.
DR Gramene; AT1G69270.1; AT1G69270.1; AT1G69270.
DR KEGG; ath:AT1G69270; -.
DR Araport; AT1G69270; -.
DR TAIR; locus:2026408; AT1G69270.
DR eggNOG; ENOG502QTCP; Eukaryota.
DR HOGENOM; CLU_000288_92_6_1; -.
DR InParanoid; Q9ZRF9; -.
DR OMA; DECNPRI; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q9ZRF9; -.
DR PRO; PR:Q9ZRF9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9ZRF9; baseline and differential.
DR Genevisible; Q9ZRF9; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005777; C:peroxisome; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0004672; F:protein kinase activity; IDA:TAIR.
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:0009738; P:abscisic acid-activated signaling pathway; IMP:TAIR.
DR GO; GO:0048508; P:embryonic meristem development; IMP:UniProtKB.
DR GO; GO:0009942; P:longitudinal axis specification; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0009945; P:radial axis specification; IMP:UniProtKB.
DR GO; GO:0009737; P:response to abscisic acid; IEP:UniProtKB.
DR GO; GO:0009409; P:response to cold; IEP:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IEP:UniProtKB.
DR GO; GO:0009414; P:response to water deprivation; IEP:UniProtKB.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
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; PF08263; LRRNT_2; 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 Abscisic acid signaling pathway; ATP-binding; Cell membrane;
KW Developmental protein; Kinase; Leucine-rich repeat; Membrane;
KW Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..540
FT /note="Probable LRR receptor-like serine/threonine-protein
FT kinase RPK1"
FT /id="PRO_0000387522"
FT TOPO_DOM 20..198
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 220..540
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 118..142
FT /note="LRR 1"
FT REPEAT 144..169
FT /note="LRR 2"
FT DOMAIN 261..535
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 385
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 267..275
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 289
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 250
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 258
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 334
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O22476"
FT MOD_RES 372
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 427
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:C0LGT6"
FT MOD_RES 435
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9M0G7"
SQ SEQUENCE 540 AA; 59742 MW; 6560AEBEB506A724 CRC64;
MKLLGLVFLL FNLFMFSFSR KLLTESGGGL HDEAALLKLK SSFLDPNGVL SSWVSDSSSN
HCSWYGVSCN SDSRVVSLIL RGCDELEGSG VLHLPDLSSC SSSKRRLGGV ISPVVGDLSE
IRVLSLSFND LRGEIPKEIW GLEKLEILDL KGNNFIGGIR VVDNVVLRKL MSFEDEDEIG
PSSADDDSPG KSGLYPIEIA SIVSASVIVF VLLVLVILFI YTRKWKRNSQ VQVDEIKEIK
VFVDIGIPLT YEIIVRATGY FSNSNCIGHG GFGSTYKAEV SPTNVFAVKR LSVGRFQGDQ
QFHAEISALE MVRHPNLVML IGYHASETEM FLIYNYLSGG NLQDFIKERS KAAIEWKVLH
KIALDVARAL SYLHEQCSPK VLHRDIKPSN ILLDNNYNAY LSDFGLSKLL GTSQSHVTTG
VAGTFGYVAP EYAMTCRVSE KADVYSYGIV LLELISDKRA LDPSFSSHEN GFNIVSWAHM
MLSQGKAKEV FTTGLWETGP PDDLVEVLHL ALKCTVDSLS IRPTMKQAVR LLKRIQPSRL
