KPK1_ARATH
ID KPK1_ARATH Reviewed; 465 AA.
AC P42818; Q8LFC1;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Serine/threonine-protein kinase AtPK1/AtPK6 {ECO:0000303|PubMed:7912697};
DE EC=2.7.11.1;
DE AltName: Full=Ribosomal-protein S6 kinase homolog 1 {ECO:0000303|PubMed:7828736};
GN Name=ATPK1 {ECO:0000303|PubMed:7912697};
GN Synonyms=ATPK6, S6K1 {ECO:0000303|PubMed:7828736};
GN OrderedLocusNames=At3g08730 {ECO:0000312|Araport:AT3G08730};
GN ORFNames=F17O14.20 {ECO:0000312|EMBL:AAG51351.1};
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].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=7912697; DOI=10.1016/s0021-9258(17)32481-x;
RA Zhang S.-H., Lawton M.A., Hunter T., Lamb C.J.;
RT "Atpk1, a novel ribosomal protein kinase gene from Arabidopsis. I.
RT Isolation, characterization, and expression.";
RL J. Biol. Chem. 269:17586-17592(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=7828736; DOI=10.1016/0014-5793(94)01423-x;
RA Mizoguchi T., Hayashida N., Yamaguchi-Shinozaki K., Kamada H.,
RA Shinozaki K.;
RT "Two genes that encode ribosomal-protein S6 kinase homologs are induced by
RT cold or salinity stress in Arabidopsis thaliana.";
RL FEBS Lett. 358:199-204(1995).
RN [3]
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 [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP CHARACTERIZATION, AND MUTAGENESIS OF LYS-163.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=8021267; DOI=10.1016/s0021-9258(17)32482-1;
RA Zhang S.-H., Broome M.A., Lawton M.A., Hunter T., Lamb C.J.;
RT "Atpk1, a novel ribosomal protein kinase gene from Arabidopsis. II.
RT Functional and biochemical analysis of the encoded protein.";
RL J. Biol. Chem. 269:17593-17599(1994).
RN [8]
RP GENE FAMILY, AND REVIEW.
RX PubMed=13678909; DOI=10.1016/s1360-1385(03)00188-2;
RA Boegre L., Okresz L., Henriques R., Anthony R.G.;
RT "Growth signalling pathways in Arabidopsis and the AGC protein kinases.";
RL Trends Plant Sci. 8:424-431(2003).
RN [9]
RP ACTIVITY REGULATION, PHOSPHORYLATION AT SER-290 BY PDK1, AND INTERACTION
RP WITH RAPTOR1.
RX PubMed=16377759; DOI=10.1105/tpc.105.035931;
RA Mahfouz M.M., Kim S., Delauney A.J., Verma D.P.;
RT "Arabidopsis TARGET OF RAPAMYCIN interacts with RAPTOR, which regulates the
RT activity of S6 kinase in response to osmotic stress signals.";
RL Plant Cell 18:477-490(2006).
RN [10]
RP FUNCTION, INTERACTION WITH RBR1-E2FB COMPLEX, MUTAGENESIS OF CYS-94, AND
RP SUBCELLULAR LOCATION.
RX PubMed=20683442; DOI=10.1038/emboj.2010.164;
RA Henriques R., Magyar Z., Monardes A., Khan S., Zalejski C., Orellana J.,
RA Szabados L., de la Torre C., Koncz C., Bogre L.;
RT "Arabidopsis S6 kinase mutants display chromosome instability and altered
RT RBR1-E2F pathway activity.";
RL EMBO J. 29:2979-2993(2010).
RN [11]
RP PHOSPHORYLATION AT THR-449 BY TOR.
RX PubMed=22134914; DOI=10.1074/jbc.m111.300749;
RA Xiong Y., Sheen J.;
RT "Rapamycin and glucose-target of rapamycin (TOR) protein signaling in
RT plants.";
RL J. Biol. Chem. 287:2836-2842(2012).
RN [12]
RP MUTAGENESIS OF THR-449, AND INTERACTION WITH TAP46.
RX PubMed=25399018; DOI=10.1093/jxb/eru438;
RA Ahn C.S., Ahn H.K., Pai H.S.;
RT "Overexpression of the PP2A regulatory subunit Tap46 leads to enhanced
RT plant growth through stimulation of the TOR signalling pathway.";
RL J. Exp. Bot. 66:827-840(2015).
RN [13]
RP FUNCTION, MUTAGENESIS OF THR-449, AND INTERACTION WITH MRF1.
RC STRAIN=cv. Columbia;
RX PubMed=29084871; DOI=10.1105/tpc.17.00563;
RA Lee D.-H., Park S.J., Ahn C.S., Pai H.-S.;
RT "MRF family genes are involved in translation control, especially under
RT energy-deficient conditions, and their expression and functions are
RT modulated by the TOR signaling pathway.";
RL Plant Cell 29:2895-2920(2017).
CC -!- FUNCTION: Downstream effector of TOR signaling pathway involved in
CC osmotic stress response (PubMed:20683442). Could be involved in the
CC control of plant growth and development (PubMed:20683442).
CC Phosphorylates the ribosomal proteins P14, P16 and S6
CC (PubMed:20683442). Functions as a repressor of cell proliferation and
CC required for maintenance of chromosome stability and ploidy levels
CC through the RBR1-E2F pathway (PubMed:20683442). Mediates the
CC phosphorylation of MRFs (e.g. MRF1) (PubMed:29084871).
CC {ECO:0000269|PubMed:20683442, ECO:0000269|PubMed:29084871}.
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 -!- ACTIVITY REGULATION: Activated by PDK1. Repressed during osmotic
CC stress. {ECO:0000269|PubMed:16377759}.
CC -!- SUBUNIT: Interacts with RAPTOR1 (PubMed:16377759). Interacts with RBR1-
CC E2FB complex through its LVxCxE motif (PubMed:20683442). Interacts with
CC TAP46 (PubMed:25399018). Binds to MRF1 (PubMed:29084871).
CC {ECO:0000269|PubMed:16377759, ECO:0000269|PubMed:20683442,
CC ECO:0000269|PubMed:25399018, ECO:0000269|PubMed:29084871}.
CC -!- INTERACTION:
CC P42818; Q9FV71: E2FB; NbExp=3; IntAct=EBI-8107038, EBI-1774719;
CC P42818; Q9LKZ3: RBR1; NbExp=2; IntAct=EBI-8107038, EBI-398590;
CC P42818; O49160: TIF3C1; NbExp=2; IntAct=EBI-8107038, EBI-1635551;
CC P42818; Q9C5Z2: TIF3H1; NbExp=3; IntAct=EBI-8107038, EBI-3387106;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20683442}. Nucleus
CC {ECO:0000269|PubMed:20683442}.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues.
CC -!- DEVELOPMENTAL STAGE: Predominates during high metabolic activity in
CC growing buds, root tips, leaf margins and germinating seeds.
CC -!- DOMAIN: The activation loop within the kinase domain is the target of
CC phosphorylation. {ECO:0000250}.
CC -!- PTM: Undergoes serine-specific autophosphorylation. Phosphorylated at
CC Thr-449 by TOR. {ECO:0000269|PubMed:16377759,
CC ECO:0000269|PubMed:22134914}.
CC -!- MISCELLANEOUS: Plants overexpressing KPK1 are hypersensitive to osmotic
CC stress.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. S6 kinase subfamily. {ECO:0000305}.
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DR EMBL; L29030; AAA21142.1; -; mRNA.
DR EMBL; D42056; BAA07656.1; -; mRNA.
DR EMBL; AC012562; AAG51351.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74671.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM64030.1; -; Genomic_DNA.
DR EMBL; AY065230; AAL38706.1; -; mRNA.
DR EMBL; AY096555; AAM20205.1; -; mRNA.
DR EMBL; AY084935; AAM61496.1; -; mRNA.
DR PIR; S68462; S68462.
DR RefSeq; NP_001326081.1; NM_001337768.1.
DR RefSeq; NP_187485.1; NM_111707.4.
DR AlphaFoldDB; P42818; -.
DR SMR; P42818; -.
DR BioGRID; 5355; 12.
DR IntAct; P42818; 14.
DR MINT; P42818; -.
DR STRING; 3702.AT3G08730.1; -.
DR iPTMnet; P42818; -.
DR PaxDb; P42818; -.
DR PRIDE; P42818; -.
DR ProteomicsDB; 238211; -.
DR EnsemblPlants; AT3G08730.1; AT3G08730.1; AT3G08730.
DR EnsemblPlants; AT3G08730.2; AT3G08730.2; AT3G08730.
DR GeneID; 820020; -.
DR Gramene; AT3G08730.1; AT3G08730.1; AT3G08730.
DR Gramene; AT3G08730.2; AT3G08730.2; AT3G08730.
DR KEGG; ath:AT3G08730; -.
DR Araport; AT3G08730; -.
DR TAIR; locus:2077873; AT3G08730.
DR eggNOG; KOG0598; Eukaryota.
DR HOGENOM; CLU_000288_63_49_1; -.
DR InParanoid; P42818; -.
DR OMA; RGCQIMA; -.
DR OrthoDB; 1132245at2759; -.
DR PhylomeDB; P42818; -.
DR BRENDA; 2.7.11.1; 399.
DR PRO; PR:P42818; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; P42818; baseline and differential.
DR Genevisible; P42818; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IDA:TAIR.
DR GO; GO:0004672; F:protein kinase activity; ISS:TAIR.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:TAIR.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0045727; P:positive regulation of translation; TAS:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IDA:TAIR.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR GO; GO:0006970; P:response to osmotic stress; IDA:TAIR.
DR GO; GO:0009651; P:response to salt stress; IEP:TAIR.
DR CDD; cd05123; STKc_AGC; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR045270; STKc_AGC.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 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; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..465
FT /note="Serine/threonine-protein kinase AtPK1/AtPK6"
FT /id="PRO_0000086163"
FT DOMAIN 134..389
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 390..460
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 275..301
FT /note="Activation loop"
FT /evidence="ECO:0000250"
FT MOTIF 91..96
FT /note="LVxCxE motif"
FT /evidence="ECO:0000269|PubMed:20683442"
FT ACT_SITE 257
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 140..148
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 163
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 290
FT /note="Phosphoserine; by PDPK1"
FT /evidence="ECO:0000305|PubMed:16377759"
FT MOD_RES 449
FT /note="Phosphothreonine; by TOR"
FT /evidence="ECO:0000269|PubMed:22134914"
FT MUTAGEN 94
FT /note="C->R: Binding to RBR1 substantially diminished."
FT /evidence="ECO:0000269|PubMed:20683442"
FT MUTAGEN 163
FT /note="K->R: Activity substantially diminished."
FT /evidence="ECO:0000269|PubMed:8021267"
FT MUTAGEN 449
FT /note="T->A: Abrogation of the phosphorylation. Reduced
FT MRF1 phosphorylation activity."
FT /evidence="ECO:0000269|PubMed:25399018,
FT ECO:0000269|PubMed:29084871"
FT MUTAGEN 449
FT /note="T->D: Phosphomimetic. No impact MRF1 phosphorylation
FT activity."
FT /evidence="ECO:0000269|PubMed:29084871"
FT CONFLICT 232
FT /note="D -> N (in Ref. 6; AAM61496)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 465 AA; 52588 MW; 407133D674CA271F CRC64;
MVSSQRPVPN KIQKQQYLSI SPSNSVLKDD VELEFSDVFG PLPEEANDIA YDEPAVVYSR
SHSLVGPCSL DSHSLKLTKL TLLETEDSID LVECLEGESL KENDDFSGND DSDNEKALEG
DLVKVSGVVG IDDFEVMKVV GKGAFGKVYQ VRKKETSEIY AMKVMRKDHI MEKNHAEYMK
AERDILTKID HPFIVQLKYS FQTKYRLYLV LDFINGGHLF FQLYHQGLFR EDLARVYTAE
IVSAVSHLHE KGIMHRDLKP ENILMDTDGH VMLTDFGLAK EFEENTRSNS MCGTTEYMAP
EIVRGKGHDK AADWWSVGIL LYEMLTGKPP FLGSKGKIQQ KIVKDKIKLP QFLSNEAHAI
LKGLLQKEPE RRLGSGLSGA EEIKQHKWFK GINWKKLEAR EVMPSFKPEV SGRQCIANFD
KCWTDMSVLD SPASSPSSDP KANPFTNFTY VRPPPSFLHQ STTTL
