WNK2_ARATH
ID WNK2_ARATH Reviewed; 568 AA.
AC Q8S8Y9; Q9LUV8;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Serine/threonine-protein kinase WNK2;
DE Short=AtWNK2;
DE EC=2.7.11.1;
DE AltName: Full=Protein kinase with no lysine 2;
GN Name=WNK2; OrderedLocusNames=At3g22420; ORFNames=MCB17.15;
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] (ISOFORM 2), INDUCTION, AND AUTOPHOSPHORYLATION.
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=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 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).
CC -!- FUNCTION: Regulates flowering time by modulating the photoperiod
CC pathway. Possesses kinase activity in vitro.
CC {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=2;
CC Name=1;
CC IsoId=Q8S8Y9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8S8Y9-2; Sequence=VSP_035528, VSP_035529;
CC -!- INDUCTION: Expressed with a circadian rhythm showing a peak before
CC dawn. {ECO:0000269|PubMed:12506983}.
CC -!- PTM: Autophosphorylated.
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=BAB01779.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB084267; BAB91126.1; -; mRNA.
DR EMBL; AB022215; BAB01779.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE76633.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76634.1; -; Genomic_DNA.
DR EMBL; BT030355; ABO38768.1; -; mRNA.
DR EMBL; AK227215; BAE99253.1; -; mRNA.
DR EMBL; AY086628; AAM63686.1; -; mRNA.
DR RefSeq; NP_188881.1; NM_113139.3. [Q8S8Y9-1]
DR RefSeq; NP_974354.1; NM_202625.2. [Q8S8Y9-2]
DR AlphaFoldDB; Q8S8Y9; -.
DR SMR; Q8S8Y9; -.
DR BioGRID; 7142; 12.
DR IntAct; Q8S8Y9; 2.
DR STRING; 3702.AT3G22420.2; -.
DR iPTMnet; Q8S8Y9; -.
DR PRIDE; Q8S8Y9; -.
DR ProteomicsDB; 242397; -. [Q8S8Y9-1]
DR EnsemblPlants; AT3G22420.1; AT3G22420.1; AT3G22420. [Q8S8Y9-1]
DR EnsemblPlants; AT3G22420.2; AT3G22420.2; AT3G22420. [Q8S8Y9-2]
DR GeneID; 821810; -.
DR Gramene; AT3G22420.1; AT3G22420.1; AT3G22420. [Q8S8Y9-1]
DR Gramene; AT3G22420.2; AT3G22420.2; AT3G22420. [Q8S8Y9-2]
DR KEGG; ath:AT3G22420; -.
DR Araport; AT3G22420; -.
DR TAIR; locus:2087857; AT3G22420.
DR eggNOG; KOG0584; Eukaryota.
DR HOGENOM; CLU_000288_142_2_1; -.
DR InParanoid; Q8S8Y9; -.
DR PhylomeDB; Q8S8Y9; -.
DR PRO; PR:Q8S8Y9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8S8Y9; baseline and differential.
DR Genevisible; Q8S8Y9; 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; TAS: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: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 Alternative splicing; ATP-binding; Kinase; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..568
FT /note="Serine/threonine-protein kinase WNK2"
FT /id="PRO_0000351660"
FT DOMAIN 24..281
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 453..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..473
FT /note="Basic and acidic residues"
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"
FT VAR_SEQ 189
FT /note="T -> TSKPSHHWNFIALIMFFTTLDLPLLCLCVVKGT (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:12506983, ECO:0000303|Ref.4,
FT ECO:0000303|Ref.5, ECO:0000303|Ref.6"
FT /id="VSP_035528"
FT VAR_SEQ 365
FT /note="G -> GIVSIFFDSFKIIGLKNVTRFRVLGNVG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12506983, ECO:0000303|Ref.4,
FT ECO:0000303|Ref.5, ECO:0000303|Ref.6"
FT /id="VSP_035529"
SQ SEQUENCE 568 AA; 65327 MW; E17CA971FAF9F5A3 CRC64;
MNGEESFVED CSVFVEIDPS GRYGRYDEIL GKGASKTVYR AFDEYEGIEV AWNQVKLRNF
TRNPEELEKF FREIHLLKTL NHQNIMKFYT SWVDTNNLSI NFVTELFTSG TLRQYRLRHR
RVNIRAVKQW CKQILKGLLY LHSRSPPIIH RDLKCDNIFI NGNQGEVKIG DLGLAAILRK
SHAVRCVGTP EFMAPEVYDE EYNELVDVYA FGMCVLEMVT FDYPYSECTH PAQIYKKVTS
GKKPEAFYLV KDPEVREFVE KCLANVTCRL TALELLQDPF LQDDNMDGFV MRPIDYYNGY
DETGVFLRHP LIDDPLYHDQ FESSQICEID LFANDDEDHV DISIKGKRNG DDGIFLRLRI
SDAEGRIRNI YFPFETAIDT AWSVAVEMVS ELDITNQDVA KIAEMIDAEI AALVPDWKND
TESSQNVNNN KNNNTAGFCG ECASNGYIQE TVSSGEKSHH NHHEFDSSED KSCSSVHGRF
ADMWGLRESY SDDGEKQSSR KVRSGRWSEN EMRRELRWLK ARHKIQLMKM RGQTICETPI
EISLTPGTSV SLPLLYRAIS LPVDAVDM
