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WNK6_ARATH
ID   WNK6_ARATH              Reviewed;         567 AA.
AC   Q8S8Y8; Q2V3U7; Q9LSA2;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Probable serine/threonine-protein kinase WNK6;
DE            Short=AtWNK6;
DE            EC=2.7.11.1;
DE   AltName: Full=Protein kinase with no lysine 6;
GN   Name=WNK6; OrderedLocusNames=At3g18750; ORFNames=MVE11.20;
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 1), 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=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 1).
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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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.
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8S8Y8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8S8Y8-2; Sequence=VSP_035530;
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB01801.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB084270; BAB91129.1; -; mRNA.
DR   EMBL; AB026654; BAB01801.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002686; AEE76139.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE76140.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE76141.1; -; Genomic_DNA.
DR   EMBL; CP002686; ANM64345.1; -; Genomic_DNA.
DR   EMBL; CP002686; ANM64346.1; -; Genomic_DNA.
DR   EMBL; AK175997; BAD43760.1; -; mRNA.
DR   EMBL; BT030341; ABO38754.1; -; mRNA.
DR   RefSeq; NP_001030723.1; NM_001035646.2. [Q8S8Y8-2]
DR   RefSeq; NP_001189928.1; NM_001202999.2. [Q8S8Y8-1]
DR   RefSeq; NP_001319584.1; NM_001338354.1. [Q8S8Y8-2]
DR   RefSeq; NP_001326380.1; NM_001338356.1. [Q8S8Y8-1]
DR   RefSeq; NP_188505.1; NM_112761.3. [Q8S8Y8-1]
DR   AlphaFoldDB; Q8S8Y8; -.
DR   SMR; Q8S8Y8; -.
DR   STRING; 3702.AT3G18750.3; -.
DR   PaxDb; Q8S8Y8; -.
DR   PRIDE; Q8S8Y8; -.
DR   ProteomicsDB; 243084; -. [Q8S8Y8-1]
DR   EnsemblPlants; AT3G18750.1; AT3G18750.1; AT3G18750. [Q8S8Y8-1]
DR   EnsemblPlants; AT3G18750.2; AT3G18750.2; AT3G18750. [Q8S8Y8-2]
DR   EnsemblPlants; AT3G18750.3; AT3G18750.3; AT3G18750. [Q8S8Y8-1]
DR   EnsemblPlants; AT3G18750.5; AT3G18750.5; AT3G18750. [Q8S8Y8-1]
DR   EnsemblPlants; AT3G18750.6; AT3G18750.6; AT3G18750. [Q8S8Y8-2]
DR   GeneID; 821406; -.
DR   Gramene; AT3G18750.1; AT3G18750.1; AT3G18750. [Q8S8Y8-1]
DR   Gramene; AT3G18750.2; AT3G18750.2; AT3G18750. [Q8S8Y8-2]
DR   Gramene; AT3G18750.3; AT3G18750.3; AT3G18750. [Q8S8Y8-1]
DR   Gramene; AT3G18750.5; AT3G18750.5; AT3G18750. [Q8S8Y8-1]
DR   Gramene; AT3G18750.6; AT3G18750.6; AT3G18750. [Q8S8Y8-2]
DR   KEGG; ath:AT3G18750; -.
DR   Araport; AT3G18750; -.
DR   TAIR; locus:2093994; AT3G18750.
DR   eggNOG; KOG0584; Eukaryota.
DR   HOGENOM; CLU_000288_142_0_1; -.
DR   InParanoid; Q8S8Y8; -.
DR   OMA; FINGHRG; -.
DR   OrthoDB; 695382at2759; -.
DR   PhylomeDB; Q8S8Y8; -.
DR   PRO; PR:Q8S8Y8; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q8S8Y8; baseline and differential.
DR   Genevisible; Q8S8Y8; 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: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   2: Evidence at transcript level;
KW   Alternative splicing; ATP-binding; Coiled coil; Kinase; Nucleotide-binding;
KW   Reference proteome; Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..567
FT                   /note="Probable serine/threonine-protein kinase WNK6"
FT                   /id="PRO_0000351664"
FT   DOMAIN          28..285
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          499..528
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          519..553
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        499..513
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        175
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9JIH7"
FT   BINDING         108..111
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H4A3"
FT   BINDING         158
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H4A3"
FT   VAR_SEQ         192..258
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_035530"
SQ   SEQUENCE   567 AA;  64866 MW;  9D0AB562D4E94BB2 CRC64;
     MEGTDDASAL QEPPDPEVLE VDPTFRYIRY KEVIGKGAFK TVYKAFDEVD GIEVAWNQVR
     IDDVLQSPNC LERLYSEVRL LKSLKHNNII RFYNSWIDDK NKTVNIITEL FTSGSLRHYR
     KKHRKVNMKA VKNWARQILM GLRYLHGQEP PIIHRDLKCD NIFINGNHGE VKIGDLGLAT
     VMEQANAKSV IGTPEFMAPE LYDENYNELA DIYSFGMCML EMVTFDYPYC ECKNSAQIYK
     KVSSGIKPAS LSRVKDPEVK QFIEKCLLPA SERLSAKELL LDPFLQLNGL TMNNPLPLPD
     IVMPKEGAFG DRCLMSEGPP TTRPSKTLSI DLDEDSNLPI VTFSDNSGSR CIEVRRAKRG
     NFFVLKGEEN DEQSVSLILR IVDENGRVRN IHFLFYQEGD TASKVSSEMV EQLELTDQNV
     TFIAELIDIL LVNMIPTWKT DVTVDHLIHS QLNQNSRSHH NEAKPQKQEE TVFHDTCELV
     SHSCNSDCPR SDEEDKQCVD ATKGEDKSSI QEVEEATEPV SLEEEERLRQ ELEEIEAKYQ
     EDMKEIATKR EEAIMETKKK LSLMKLK
 
 
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