WNK4_ARATH
ID WNK4_ARATH Reviewed; 571 AA.
AC Q9LVL5;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Probable serine/threonine-protein kinase WNK4;
DE Short=AtWNK4;
DE EC=2.7.11.1;
DE AltName: Full=Protein kinase with no lysine 4;
GN Name=WNK4; OrderedLocusNames=At5g58350; ORFNames=MCK7.22;
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], 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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-522, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-522, AND IDENTIFICATION BY
RP 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: May regulate flowering time by modulating the photoperiod
CC pathway. {ECO:0000250}.
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 -!- INDUCTION: Expressed with a circadian rhythm showing a peak before
CC dawn. {ECO:0000269|PubMed:12506983}.
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; AB084268; BAB91127.1; -; mRNA.
DR EMBL; AB019228; BAA96926.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97041.1; -; Genomic_DNA.
DR EMBL; AY039910; AAK64014.1; -; mRNA.
DR EMBL; AY081739; AAL87392.1; -; mRNA.
DR RefSeq; NP_200643.1; NM_125220.4.
DR AlphaFoldDB; Q9LVL5; -.
DR SMR; Q9LVL5; -.
DR BioGRID; 21191; 3.
DR STRING; 3702.AT5G58350.1; -.
DR iPTMnet; Q9LVL5; -.
DR PaxDb; Q9LVL5; -.
DR PRIDE; Q9LVL5; -.
DR ProteomicsDB; 242727; -.
DR DNASU; 835947; -.
DR EnsemblPlants; AT5G58350.1; AT5G58350.1; AT5G58350.
DR GeneID; 835947; -.
DR Gramene; AT5G58350.1; AT5G58350.1; AT5G58350.
DR KEGG; ath:AT5G58350; -.
DR Araport; AT5G58350; -.
DR TAIR; locus:2161278; AT5G58350.
DR eggNOG; KOG0584; Eukaryota.
DR HOGENOM; CLU_000288_142_1_1; -.
DR InParanoid; Q9LVL5; -.
DR OMA; TAMNRTH; -.
DR OrthoDB; 695382at2759; -.
DR PhylomeDB; Q9LVL5; -.
DR PRO; PR:Q9LVL5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LVL5; baseline and differential.
DR Genevisible; Q9LVL5; AT.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; TAS:TAIR.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; HDA:TAIR.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0046777; P:protein autophosphorylation; HDA:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
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; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..571
FT /note="Probable serine/threonine-protein kinase WNK4"
FT /id="PRO_0000351662"
FT DOMAIN 19..277
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 396..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..413
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 166
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9JIH7"
FT BINDING 99..102
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9H4A3"
FT BINDING 149
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9H4A3"
FT MOD_RES 522
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862,
FT ECO:0007744|PubMed:19376835"
SQ SEQUENCE 571 AA; 64914 MW; C90814D4DB44BCBE CRC64;
MNMNQVAEYV ETDPTGRYGR FAEILGRGAM KTVYKAIDEK LGIEVAWSQV KLKEVLRSSV
DLQRLYSEVH LLSTLNHKSI IRFYTSWIDV HNHTLNFITE LFTSGTLRQY KNKYLRIDIR
AIKSWARQIL EGLVYLHEHD PPVIHRDLKC DNIFVNGHLG QVKIGDLGLA RMLRDCHSAH
SIIGTPEFMA PELYEENYNE LIDVYSFGMC FLEMITSEFP YSECNHPAQI YKKVVGGKLP
GAFYRVGDIE AQRFIGKCLV SASKRVSAKE LLQDPFLASD ESWMVYTSGA GNPKPFLNEN
EMDTLKLEDD ELRTEMSIAG KLGAEDNKID LEVQIAYDNG LANNVFFPFD IMNDTSIDVA
KEMVKELEII DWEPVEIAKM IDGAISSLVS DWKYEEDDET PHDHHRHRTD SFHSSSSHAS
SSQASLSNYM ARGLQDWVQD DLHDETYSQS SSHSGSYSNL NYIAVDEYSS QSPVMSRTHN
MTRFCPEESS HLQSGQANAY AASSSTNRSL ASDNRTLTRN RSLVDVQRQL LHRSPGEEAR
KRRLFKTVGD VETVGFQSPY AVSRKPPSSR R
