KPK2_ARATH
ID KPK2_ARATH Reviewed; 471 AA.
AC Q39030; Q0V851; Q949X5; Q9C5R1;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Serine/threonine-protein kinase AtPK2/AtPK19;
DE EC=2.7.11.1;
DE AltName: Full=Ribosomal-protein S6 kinase homolog 2;
GN Name=ATPK2; Synonyms=ATPK19, S6K2; OrderedLocusNames=At3g08720;
GN ORFNames=F17O14.19;
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. 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 [2]
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 [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=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF Clones.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
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 [8]
RP ACTIVITY REGULATION, AND PHOSPHORYLATION BY PDK1.
RX PubMed=16125835; DOI=10.1016/j.biochi.2005.07.005;
RA Otterhag L., Gustavsson N., Alsterfjord M., Pical C., Lehrach H., Gobom J.,
RA Sommarin M.;
RT "Arabidopsis PDK1: identification of sites important for activity and
RT downstream phosphorylation of S6 kinase.";
RL Biochimie 88:11-21(2006).
RN [9]
RP PHOSPHORYLATION AT THR-455 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 [10]
RP 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 [11]
RP FUNCTION, 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. May be involved
CC in adaptation of plant to cold or high-salt conditions. Mediates the
CC phosphorylation of MRFs (e.g. MRF1) (PubMed:29084871).
CC {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. {ECO:0000269|PubMed:16125835}.
CC -!- SUBUNIT: Interacts with TAP46 (PubMed:25399018). Binds to MRF1
CC (PubMed:29084871). {ECO:0000269|PubMed:25399018,
CC ECO:0000269|PubMed:29084871}.
CC -!- DOMAIN: The activation loop within the kinase domain is the target of
CC phosphorylation. {ECO:0000250}.
CC -!- PTM: Undergoes serine-specific autophosphorylation (By similarity).
CC Phosphorylated at Thr-455 by TOR. {ECO:0000250,
CC ECO:0000269|PubMed:16125835, ECO:0000269|PubMed:22134914}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. S6 kinase subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AY050826; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D42061; BAA07661.1; -; mRNA.
DR EMBL; AC012562; AAG51345.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74669.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74670.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65316.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65317.1; -; Genomic_DNA.
DR EMBL; AF325094; AAK17162.1; -; mRNA.
DR EMBL; AY050826; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK316712; BAH19439.1; -; mRNA.
DR EMBL; BT026369; ABH04476.1; -; mRNA.
DR PIR; S68463; S68463.
DR RefSeq; NP_001327294.1; NM_001337767.1.
DR RefSeq; NP_001327295.1; NM_001337766.1.
DR RefSeq; NP_187484.1; NM_111706.4.
DR RefSeq; NP_850543.1; NM_180212.2.
DR AlphaFoldDB; Q39030; -.
DR SMR; Q39030; -.
DR BioGRID; 5354; 2.
DR STRING; 3702.AT3G08720.2; -.
DR iPTMnet; Q39030; -.
DR PaxDb; Q39030; -.
DR PRIDE; Q39030; -.
DR ProteomicsDB; 250702; -.
DR EnsemblPlants; AT3G08720.1; AT3G08720.1; AT3G08720.
DR EnsemblPlants; AT3G08720.2; AT3G08720.2; AT3G08720.
DR EnsemblPlants; AT3G08720.3; AT3G08720.3; AT3G08720.
DR EnsemblPlants; AT3G08720.4; AT3G08720.4; AT3G08720.
DR GeneID; 820019; -.
DR Gramene; AT3G08720.1; AT3G08720.1; AT3G08720.
DR Gramene; AT3G08720.2; AT3G08720.2; AT3G08720.
DR Gramene; AT3G08720.3; AT3G08720.3; AT3G08720.
DR Gramene; AT3G08720.4; AT3G08720.4; AT3G08720.
DR KEGG; ath:AT3G08720; -.
DR Araport; AT3G08720; -.
DR TAIR; locus:2077843; AT3G08720.
DR eggNOG; KOG0598; Eukaryota.
DR HOGENOM; CLU_000288_63_49_1; -.
DR InParanoid; Q39030; -.
DR OMA; PRANGNI; -.
DR OrthoDB; 1132245at2759; -.
DR PhylomeDB; Q39030; -.
DR BRENDA; 2.7.11.1; 399.
DR PRO; PR:Q39030; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q39030; baseline and differential.
DR Genevisible; Q39030; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
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; IBA:GO_Central.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
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:0009408; P:response to heat; IEP: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; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..471
FT /note="Serine/threonine-protein kinase AtPK2/AtPK19"
FT /id="PRO_0000086162"
FT DOMAIN 140..395
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 396..466
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..307
FT /note="Activation loop"
FT /evidence="ECO:0000250"
FT ACT_SITE 263
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 146..154
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 169
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 296
FT /note="Phosphoserine; by PDPK1"
FT /evidence="ECO:0000250|UniProtKB:P42818"
FT MOD_RES 455
FT /note="Phosphothreonine; by TOR"
FT /evidence="ECO:0000269|PubMed:22134914"
FT CONFLICT 250
FT /note="A -> V (in Ref. 1; BAA07661)"
FT /evidence="ECO:0000305"
FT CONFLICT 359..360
FT /note="LS -> VF (in Ref. 1; BAA07661)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 471 AA; 53037 MW; 95F007B44B58DFB5 CRC64;
MVSSQCSVAN KNQTGKPFQK HLSLSISPPK SVLGDNLELQ FSDVFGPMPE ANSEEACDVA
YDEPAVVYSR SHSLVGPSLV VSHSLKMNKL TLRETEDSVD LVECVEGESI KENDEFSGND
DTDSEKSPEE VSGVVGIEDF EVLKVVGQGA FGKVYQVRKK DTSEIYAMKV MRKDKIVEKN
HAEYMKAERD ILTKIDHPFI VQLKYSFQTK YRLYLVLDFI NGGHLFFQLY HQGLFREDLA
RVYTAEIVSA VSHLHEKGIM HRDLKPENIL MDVDGHVMLT DFGLAKEFEE NTRSNSMCGT
TEYMAPEIVR GKGHDKAADW WSVGILLYEM LTGKPPFLGS KGKIQQKIVK DKIKLPQFLS
NEAHALLKGL LQKEPERRLG SGPSGAEEIK KHKWFKAINW KKLEAREVQP SFKPAVSGRQ
CIANFDKCWT DMSVLDSPAS SPNSDAKANP FTNFTYVRPP HSFLHRTTSN L
