WNK8_ARATH
ID WNK8_ARATH Reviewed; 563 AA.
AC Q944Q0; Q8S8Y7; Q9FHY4;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Serine/threonine-protein kinase WNK8;
DE Short=AtWNK8;
DE EC=2.7.11.1;
DE AltName: Full=Protein kinase with no lysine 8;
GN Name=WNK8; OrderedLocusNames=At5g41990; ORFNames=MJC20.9;
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=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(1999).
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 NUCLEOTIDE SEQUENCE [MRNA] OF 14-563.
RC STRAIN=cv. Columbia;
RX PubMed=12506983; DOI=10.1271/bbb.66.2429;
RA Nakamichi N., Murakami-Kojima M., Sato E., Kishi Y., Yamashino T.,
RA Mizuno T.;
RT "Compilation and characterization of a novel WNK family of protein kinases
RT in Arabiodpsis thaliana with reference to circadian rhythms.";
RL Biosci. Biotechnol. Biochem. 66:2429-2436(2002).
RN [5]
RP FUNCTION, AUTOPHOSPHORYLATION, AND MUTAGENESIS OF LYS-41 AND ASP-157.
RX PubMed=16427632; DOI=10.1016/j.febslet.2006.01.018;
RA Hong-Hermesdorf A., Bruex A., Grueber A., Grueber G., Schumacher K.;
RT "A WNK kinase binds and phosphorylates V-ATPase subunit C.";
RL FEBS Lett. 580:932-939(2006).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18761494; DOI=10.1111/j.1438-8677.2008.00072.x;
RA Wang Y., Liu K., Liao H., Zhuang C., Ma H., Yan X.;
RT "The plant WNK gene family and regulation of flowering time in
RT Arabidopsis.";
RL Plant Biol. 10:548-562(2008).
RN [7]
RP FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=20840782; DOI=10.1186/1471-2229-10-203;
RA Tsuchiya T., Eulgem T.;
RT "Co-option of EDM2 to distinct regulatory modules in Arabidopsis thaliana
RT development.";
RL BMC Plant Biol. 10:203-203(2010).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH EDM2, AND
RP AUTOPHOSPHORYLATION.
RC STRAIN=cv. Columbia;
RX PubMed=20149132; DOI=10.1111/j.1365-313x.2010.04169.x;
RA Tsuchiya T., Eulgem T.;
RT "The Arabidopsis defense component EDM2 affects the floral transition in an
RT FLC-dependent manner.";
RL Plant J. 62:518-528(2010).
RN [9]
RP INTERACTION WITH RGS1.
RX PubMed=21952135; DOI=10.1038/msb.2011.66;
RA Klopffleisch K., Phan N., Augustin K., Bayne R.S., Booker K.S.,
RA Botella J.R., Carpita N.C., Carr T., Chen J.G., Cooke T.R., Frick-Cheng A.,
RA Friedman E.J., Fulk B., Hahn M.G., Jiang K., Jorda L., Kruppe L., Liu C.,
RA Lorek J., McCann M.C., Molina A., Moriyama E.N., Mukhtar M.S., Mudgil Y.,
RA Pattathil S., Schwarz J., Seta S., Tan M., Temp U., Trusov Y., Urano D.,
RA Welter B., Yang J., Panstruga R., Uhrig J.F., Jones A.M.;
RT "Arabidopsis G-protein interactome reveals connections to cell wall
RT carbohydrates and morphogenesis.";
RL Mol. Syst. Biol. 7:532-532(2011).
RN [10]
RP INTERACTION WITH RGS1 AND GB1.
RX PubMed=22940907; DOI=10.1038/ncb2568;
RA Urano D., Phan N., Jones J.C., Yang J., Huang J., Grigston J., Taylor J.P.,
RA Jones A.M.;
RT "Endocytosis of the seven-transmembrane RGS1 protein activates G-protein-
RT coupled signalling in Arabidopsis.";
RL Nat. Cell Biol. 14:1079-1088(2012).
CC -!- FUNCTION: Regulates flowering time by modulating the photoperiod
CC pathway. Phosphorylates the vacuolar ATPase subunit C (VATC) and RGS1
CC (PubMed:16427632, PubMed:18761494). Regulates EDM2 that, in turn,
CC modulates development processes (PubMed:20840782, PubMed:20149132).
CC {ECO:0000269|PubMed:16427632, ECO:0000269|PubMed:18761494,
CC ECO:0000269|PubMed:20149132, ECO:0000269|PubMed:20840782}.
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 RGS1 and GB1, but not with GPA1. The
CC association with RGS1 at the plasma membrane is triggered by induction
CC of glucose (PubMed:21952135, PubMed:22940907). Binds to EDM2 in nucleus
CC (PubMed:20149132). {ECO:0000269|PubMed:20149132,
CC ECO:0000269|PubMed:21952135, ECO:0000269|PubMed:22940907}.
CC -!- INTERACTION:
CC Q944Q0; Q9SDS7: VHA-C; NbExp=4; IntAct=EBI-4441446, EBI-1794418;
CC Q944Q0; Q944Q0: WNK8; NbExp=2; IntAct=EBI-4441446, EBI-4441446;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20149132}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:16427632,
CC ECO:0000269|PubMed:20149132}.
CC -!- DISRUPTION PHENOTYPE: Plants display early flowering and altered
CC expression of genes involved in the photoperiod flowering pathway, such
CC as ELF4, TOC1, CO and FT. {ECO:0000269|PubMed:18761494}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. WNK subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- CAUTION: Was named WNK/'with no lysine(K)' because key residues for
CC catalysis, including the lysine involved in ATP binding, are either not
CC conserved or differ compared to the residues described in other kinase
CC family proteins. {ECO:0000250|UniProtKB:Q9H4A3}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB08432.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB017067; BAB08432.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED94750.1; -; Genomic_DNA.
DR EMBL; AF424629; AAL11622.1; -; mRNA.
DR EMBL; AY113042; AAM47350.1; -; mRNA.
DR EMBL; AB084271; BAB91130.1; -; mRNA.
DR RefSeq; NP_568599.1; NM_123564.3.
DR AlphaFoldDB; Q944Q0; -.
DR SMR; Q944Q0; -.
DR BioGRID; 19454; 7.
DR IntAct; Q944Q0; 3.
DR MINT; Q944Q0; -.
DR STRING; 3702.AT5G41990.1; -.
DR PaxDb; Q944Q0; -.
DR PRIDE; Q944Q0; -.
DR ProteomicsDB; 242452; -.
DR EnsemblPlants; AT5G41990.1; AT5G41990.1; AT5G41990.
DR GeneID; 834204; -.
DR Gramene; AT5G41990.1; AT5G41990.1; AT5G41990.
DR KEGG; ath:AT5G41990; -.
DR Araport; AT5G41990; -.
DR TAIR; locus:2165790; AT5G41990.
DR eggNOG; KOG0584; Eukaryota.
DR HOGENOM; CLU_000288_142_0_1; -.
DR InParanoid; Q944Q0; -.
DR OMA; KRKWITK; -.
DR OrthoDB; 695382at2759; -.
DR PhylomeDB; Q944Q0; -.
DR PRO; PR:Q944Q0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q944Q0; baseline and differential.
DR Genevisible; Q944Q0; 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: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; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0048573; P:photoperiodism, flowering; IMP:TAIR.
DR GO; GO:0009911; P:positive regulation of flower development; IMP:TAIR.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IDA:TAIR.
DR GO; GO:0009909; P:regulation of flower development; IMP:TAIR.
DR GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IMP:TAIR.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
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; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..563
FT /note="Serine/threonine-protein kinase WNK8"
FT /id="PRO_0000351666"
FT DOMAIN 29..286
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 426..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..449
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 176
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9JIH7"
FT BINDING 109..112
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9H4A3"
FT BINDING 159
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9H4A3"
FT MOD_RES 509
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LVL5"
FT MUTAGEN 41
FT /note="K->M: Loss of autophosphorylation."
FT /evidence="ECO:0000269|PubMed:16427632"
FT MUTAGEN 157
FT /note="D->A: Loss of autophosphorylation."
FT /evidence="ECO:0000269|PubMed:16427632"
SQ SEQUENCE 563 AA; 63803 MW; 0342EE9FDB5A0F54 CRC64;
MASGSGFLGQ ISSMEEADFA EKDPSGRYIR YDDVLGRGAF KTVYKAFDEV DGIEVAWNLV
SIEDVMQMPG QLERLYSEVH LLKALKHENI IKLFYSWVDE KNKTINMITE LFTSGSLRVY
RKKHRKVDPK AIKNWARQIL KGLNYLHSQN PPVIHRDLKC DNIFVNGNTG EVKIGDLGLA
TVLQQPTARS VIGTPEFMAP ELYEEEYNEL VDIYSFGMCM LEMVTCEYPY NECRNQAQIY
KKVTSNIKPQ SLGKVDDPQV RQFIEKCLLP ASSRPTALEL SKDPFLARDG GKDSALLASS
STSSKYVRPP QLEHLPMDVD HNENKSVSSN EDYPWSQTIE LQRIAENKEF RLRGERSDDV
TASMVLRIAD PSGKCRIVHF AFYLESDTAT AIAEEMVEEL HLTSQEVVVI ADMIDDFIMQ
LLSDRTSSHH NQNSPRLTHE DHEAANQQTV NSKDEEAAGQ SMKSDISADY YFPYSANDGN
AAMEAGRDAE SMSSYLDSCS MMSTIYNLSI SDNDYPEDLK TELNLIESQF NQSFQDLLKL
KEDAIENAKR KWITKKQKAV NIS
