RBK1_ARATH
ID RBK1_ARATH Reviewed; 467 AA.
AC Q8H1D6; Q93ZZ8; Q9LXA4;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Receptor-like cytosolic serine/threonine-protein kinase RBK1;
DE EC=2.7.11.1;
DE AltName: Full=Protein ROP BINDING PROTEIN KINASES 1;
GN Name=RBK1; OrderedLocusNames=At5g10520; ORFNames=F12B17.130;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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].
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 [4]
RP INTERACTION WITH ARAC5 AND ARAC10, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INDUCTION BY PATHOGENS AND ETHYLENE.
RX PubMed=18088316; DOI=10.1111/j.1365-313x.2007.03384.x;
RA Molendijk A.J., Ruperti B., Singh M.K., Dovzhenko A., Ditengou F.A.,
RA Milia M., Westphal L., Rosahl S., Soellick T.R., Uhrig J., Weingarten L.,
RA Huber M., Palme K.;
RT "A cysteine-rich receptor-like kinase NCRK and a pathogen-induced protein
RT kinase RBK1 are Rop GTPase interactors.";
RL Plant J. 53:909-923(2008).
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 -!- SUBUNIT: Interacts with ARAC5 and ARAC10.
CC {ECO:0000269|PubMed:18088316}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18088316}.
CC Endomembrane system {ECO:0000269|PubMed:18088316}; Peripheral membrane
CC protein {ECO:0000269|PubMed:18088316}. Nucleus
CC {ECO:0000269|PubMed:18088316}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in vasculature, hydathode
CC endothem, leaf mesophyll cells and trichomes.
CC {ECO:0000269|PubMed:18088316}.
CC -!- INDUCTION: By fungal pathogens such as Phytophthora infestans and
CC Botrytis cinerea. Promoted by ethylene in the vascular cylinder of
CC primary roots and in the root cortex in the root/hypocotyl junction
CC zone. {ECO:0000269|PubMed:18088316}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB89391.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL353995; CAB89391.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED91559.1; -; Genomic_DNA.
DR EMBL; AY056156; AAL07235.1; -; mRNA.
DR EMBL; AY150507; AAN13023.1; -; mRNA.
DR PIR; T49987; T49987.
DR RefSeq; NP_568231.1; NM_121090.4.
DR AlphaFoldDB; Q8H1D6; -.
DR SMR; Q8H1D6; -.
DR BioGRID; 16195; 10.
DR IntAct; Q8H1D6; 8.
DR STRING; 3702.AT5G10520.1; -.
DR PaxDb; Q8H1D6; -.
DR PRIDE; Q8H1D6; -.
DR ProteomicsDB; 225909; -.
DR EnsemblPlants; AT5G10520.1; AT5G10520.1; AT5G10520.
DR GeneID; 830917; -.
DR Gramene; AT5G10520.1; AT5G10520.1; AT5G10520.
DR KEGG; ath:AT5G10520; -.
DR Araport; AT5G10520; -.
DR TAIR; locus:2142514; AT5G10520.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_155_1_1; -.
DR InParanoid; Q8H1D6; -.
DR OMA; HISHPNA; -.
DR OrthoDB; 684563at2759; -.
DR PhylomeDB; Q8H1D6; -.
DR PRO; PR:Q8H1D6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8H1D6; baseline and differential.
DR Genevisible; Q8H1D6; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0012505; C:endomembrane system; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0051020; F:GTPase binding; IPI:UniProtKB.
DR GO; GO:0016301; F: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:0071369; P:cellular response to ethylene stimulus; IEP:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IEP:UniProtKB.
DR GO; GO:0098542; P:defense response to other organism; IEP:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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 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; Cytoplasm; Kinase; Membrane; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..467
FT /note="Receptor-like cytosolic serine/threonine-protein
FT kinase RBK1"
FT /id="PRO_0000403330"
FT DOMAIN 153..430
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 278
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 159..167
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 181
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 142
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 282
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 318
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 326
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT CONFLICT 56
FT /note="D -> N (in Ref. 3; AAL07235)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 467 AA; 52652 MW; E4610F132762F620 CRC64;
MAVEDNKNSE SKNHQEVELH RNDLGLEDSS SPRGVLGMVS DSDNSSSSCS SCSSDDKSSS
TSSPFSNTTK TVSSSHHGLQ WNKMIESIKK KSMRRFSVIP LLASYELTRK NLRRKQPKLT
PSESAFTCEA FFMAKPSWRN FTYEELAVAT DYFNPENMIG KGGHAEVYKG VLINGETVAI
KKLMSHAKEE EERVSDFLSE LGIIAHVNHP NAARLRGFSS DRGLHFVLEY APYGSLASML
FGSEECLEWK IRYKVALGIA DGLSYLHNAC PRRIIHRDIK ASNILLNHDY EAQISDFGLA
KWLPENWPHH VVFPIEGTFG YLAPEYFMHG IVDEKIDVFA FGVLLLEIIT SRRAVDTASR
QSIVAWAKPF LEKNSMEDIV DPRLGNMFNP TEMQRVMLTA SMCVHHIAAM RPDMTRLVQL
LRGEDGPAEL QQKAGERTMS VNACDLQDHT SSSYLNELRR HRQLLME
