WNK1_ARATH
ID WNK1_ARATH Reviewed; 700 AA.
AC Q9CAV6;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Serine/threonine-protein kinase WNK1;
DE Short=AtWNK1;
DE EC=2.7.11.1;
DE AltName: Full=Protein kinase with no lysine 1;
GN Name=WNK1; OrderedLocusNames=At3g04910; ORFNames=T9J14.14;
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], FUNCTION, AND INDUCTION.
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 [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 FUNCTION, INDUCTION, AND AUTOPHOSPHORYLATION.
RX PubMed=12091722; DOI=10.1093/pcp/pcf084;
RA Murakami-Kojima M., Nakamichi N., Yamashino T., Mizuno T.;
RT "The APRR3 component of the clock-associated APRR1/TOC1 quintet is
RT phosphorylated by a novel protein kinase belonging to the WNK family, the
RT gene for which is also transcribed rhythmically in Arabidopsis thaliana.";
RL Plant Cell Physiol. 43:675-683(2002).
RN [5]
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- FUNCTION: Regulates flowering time by modulating the photoperiod
CC pathway. Phosphorylates APRR3. {ECO:0000269|PubMed:12091722,
CC ECO:0000269|PubMed:12506983, ECO:0000269|PubMed:18761494}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9CAV6-1; Sequence=Displayed;
CC -!- INDUCTION: Expressed with a circadian rhythm showing a peak in the
CC evening. {ECO:0000269|PubMed:12091722, ECO:0000269|PubMed:12506983}.
CC -!- PTM: Autophosphorylated.
CC -!- DISRUPTION PHENOTYPE: Plants display delayed 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}.
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DR EMBL; AB084266; BAB91125.1; -; mRNA.
DR EMBL; AC009465; AAG51416.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74155.1; -; Genomic_DNA.
DR RefSeq; NP_187142.1; NM_111363.4. [Q9CAV6-1]
DR AlphaFoldDB; Q9CAV6; -.
DR SMR; Q9CAV6; -.
DR BioGRID; 4986; 2.
DR STRING; 3702.AT3G04910.1; -.
DR iPTMnet; Q9CAV6; -.
DR PaxDb; Q9CAV6; -.
DR PRIDE; Q9CAV6; -.
DR ProteomicsDB; 242677; -. [Q9CAV6-1]
DR EnsemblPlants; AT3G04910.1; AT3G04910.1; AT3G04910. [Q9CAV6-1]
DR GeneID; 819651; -.
DR Gramene; AT3G04910.1; AT3G04910.1; AT3G04910. [Q9CAV6-1]
DR KEGG; ath:AT3G04910; -.
DR Araport; AT3G04910; -.
DR TAIR; locus:2114845; AT3G04910.
DR eggNOG; KOG0584; Eukaryota.
DR HOGENOM; CLU_000288_142_2_1; -.
DR InParanoid; Q9CAV6; -.
DR OMA; HCEVDAQ; -.
DR OrthoDB; 695382at2759; -.
DR PhylomeDB; Q9CAV6; -.
DR PRO; PR:Q9CAV6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9CAV6; baseline and differential.
DR Genevisible; Q9CAV6; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; ISS:TAIR.
DR GO; GO:0007623; P:circadian rhythm; IEP:TAIR.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IDA: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 Alternative splicing; ATP-binding; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..700
FT /note="Serine/threonine-protein kinase WNK1"
FT /id="PRO_0000351659"
FT DOMAIN 24..281
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 314..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 647..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 171
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9JIH7"
FT BINDING 104..107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9H4A3"
FT BINDING 154
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9H4A3"
SQ SEQUENCE 700 AA; 80208 MW; C950FA6761A386D9 CRC64;
MNNLSYLEPD YSEFVEVDPT GRYGRYNEVL GKGASKTVYR AFDEYEGIEV AWNQVKLYDF
LQSPEDLERL YCEIHLLKTL KHKNIMKFYT SWVDTANRNI NFVTELFTSG TLRQYRLRHK
RVNIRAMKHW CRQILRGLHY LHSHDPPVIH RDLKCDNIFV NGNQGEVKIG DLGLAAILRK
SHAAHCVGTP EFMAPEVYEE AYNELVDIYS FGMCILEMVT FDYPYSECTH PAQIYKKVMS
GKKPDALYKV KDPEVKCFIE KCLATVSLRV SARELLDDPF LRIDDGEFDL RSVDMEDSVG
PLYRQPHHLP DYYNYPSNSS SLNRQYSNGN YPSNSSSLNR QYSNGYNSHH EYQNGWAYNP
AETEETHGIE LFESRNNDDQ EEEKKSGNVD ITIKGKRRDD GGLFLRLRIA DKEGRVRNIY
FPFDIETDTA LSVATEMVAE LDMDDHGVTK IANMIDGEIS SLVPSWRPGP EFEECLAAAA
AANAASICNN CVSNRTSMGS VMDFLRTNPG ANVIQCCRNG CGETHGRFEE ITIRETEVRL
RELWKLQQQQ ESRELSSIDS GHNHSEEEEE EEVLYEDPEN MFSCEAGNEI NHISGSGSFS
FMPSKYCDEP SEKTENQVQQ ELRWLKAKCQ IELRDIQDEQ LKTRWPESGE EVEISPKDGF
LGSVSGLGRE EDTVKEMFGE RLVPKCLKRT TSLPVDAIDS
