WNK5_ARATH
ID WNK5_ARATH Reviewed; 549 AA.
AC Q9SCU5; Q9XFS5;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Probable serine/threonine-protein kinase WNK5;
DE Short=AtWNK5;
DE EC=2.7.11.1;
DE AltName: Full=Protein kinase with no lysine 5;
GN Name=WNK5; OrderedLocusNames=At3g51630; ORFNames=T18N14.10;
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].
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 [MRNA].
RA Cooke R.M., Laudie M., Berger C., Delseny M.;
RT "Analysis of Arabidopsis thaliana gene structure by cognate cDNA
RT sequencing.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
RP INTERACTION WITH AHK4.
RX PubMed=18642946; DOI=10.1021/pr0703831;
RA Dortay H., Gruhn N., Pfeifer A., Schwerdtner M., Schmuelling T., Heyl A.;
RT "Toward an interaction map of the two-component signaling pathway of
RT Arabidopsis thaliana.";
RL J. Proteome Res. 7:3649-3660(2008).
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).
CC -!- FUNCTION: Regulates flowering time by modulating the photoperiod
CC pathway. {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 -!- SUBUNIT: Interacts with AHK4. {ECO:0000269|PubMed:18642946}.
CC -!- INTERACTION:
CC Q9SCU5; Q9C5U0: AHK4; NbExp=2; IntAct=EBI-1807651, EBI-1100775;
CC Q9SCU5; Q84MC7: PYL9; NbExp=3; IntAct=EBI-1807651, EBI-2349513;
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=BAB91128.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB63149.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB084269; BAB91128.1; ALT_INIT; mRNA.
DR EMBL; AJ238802; CAB43520.1; -; mRNA.
DR EMBL; AL132968; CAB63149.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002686; AEE78815.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78816.1; -; Genomic_DNA.
DR PIR; T46059; T46059.
DR PIR; T51099; T51099.
DR RefSeq; NP_001190056.1; NM_001203127.1.
DR RefSeq; NP_566954.2; NM_115022.3.
DR AlphaFoldDB; Q9SCU5; -.
DR SMR; Q9SCU5; -.
DR BioGRID; 9644; 6.
DR IntAct; Q9SCU5; 2.
DR STRING; 3702.AT3G51630.1; -.
DR iPTMnet; Q9SCU5; -.
DR PaxDb; Q9SCU5; -.
DR PRIDE; Q9SCU5; -.
DR ProteomicsDB; 243083; -.
DR EnsemblPlants; AT3G51630.1; AT3G51630.1; AT3G51630.
DR EnsemblPlants; AT3G51630.2; AT3G51630.2; AT3G51630.
DR GeneID; 824326; -.
DR Gramene; AT3G51630.1; AT3G51630.1; AT3G51630.
DR Gramene; AT3G51630.2; AT3G51630.2; AT3G51630.
DR KEGG; ath:AT3G51630; -.
DR Araport; AT3G51630; -.
DR TAIR; locus:2098242; AT3G51630.
DR eggNOG; KOG0584; Eukaryota.
DR HOGENOM; CLU_000288_142_1_1; -.
DR InParanoid; Q9SCU5; -.
DR OMA; NGQARNI; -.
DR OrthoDB; 695382at2759; -.
DR PhylomeDB; Q9SCU5; -.
DR PRO; PR:Q9SCU5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SCU5; baseline and differential.
DR Genevisible; Q9SCU5; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0043424; F:protein histidine kinase binding; IPI:UniProtKB.
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 ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..549
FT /note="Probable serine/threonine-protein kinase WNK5"
FT /id="PRO_0000351663"
FT DOMAIN 25..283
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 414..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..429
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..487
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..549
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 172
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9JIH7"
FT BINDING 105..108
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9H4A3"
FT BINDING 155
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9H4A3"
FT MOD_RES 504
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LVL5"
SQ SEQUENCE 549 AA; 62658 MW; 54D609DCD6CDC160 CRC64;
MYMEISSASD DSIAYVETDP SGRYGRFREV LGKGAMKTVY KAFDQVLGME VAWNQVKLNE
VFRSPEPLQR LYSEVHLLKN LNHESIIRYC TSWIDVNRRT FNFITELFTS GTLREYRRKY
QKVDIRAIKS WARQILNGLA YLHGHDPPVI HRDLKCDNIF VNGHLGQVKI GDLGLAAILR
GSQNAHSVIG TPEFMAPELY EEDYNELVDI YSFGMCVLEM LTGEYPYSEC TNPAQIYKKV
TSGKLPDSFH LIQHTEAQRF VGKCLETVSR RLPAKELLAD PFLAATDERD LAPLFRLPQQ
LAIQNLAANG TVVEHLPSTT DPTRTTDMSI TGKMNSEDHT IFLQVQILDG DGHMRNIQFP
FNILSDTPLE VALEMVKELE ITDWDPLEIA AMIENEISLL VPNWRANDSS IRHESFGHED
DEDNGDTEGR TRLFSSASSS HDSPVAVREN NDDSSNDVIP DMDDGNRSSN RLLNSSTYHY
SPAIDDDQNQ QQRRRVRLQQ KMRSLVDTRT QVLHRSLMEL INKRRGRGFD PNTNELQPQP
SSTDFIRRC
