WNK3_ARATH
ID WNK3_ARATH Reviewed; 516 AA.
AC Q9STK6;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Probable serine/threonine-protein kinase WNK3;
DE Short=AtWNK3;
DE EC=2.7.11.1;
DE AltName: Full=Protein kinase with no lysine 3;
GN Name=WNK3; OrderedLocusNames=At3g48260; ORFNames=T29H11_220;
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 [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).
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 -!- 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; AB085616; BAB92985.1; -; mRNA.
DR EMBL; AL049659; CAB41172.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78392.1; -; Genomic_DNA.
DR PIR; T06716; T06716.
DR RefSeq; NP_680105.1; NM_148852.2.
DR AlphaFoldDB; Q9STK6; -.
DR SMR; Q9STK6; -.
DR BioGRID; 9303; 28.
DR IntAct; Q9STK6; 28.
DR STRING; 3702.AT3G48260.1; -.
DR PaxDb; Q9STK6; -.
DR PRIDE; Q9STK6; -.
DR ProteomicsDB; 242786; -.
DR EnsemblPlants; AT3G48260.1; AT3G48260.1; AT3G48260.
DR GeneID; 823984; -.
DR Gramene; AT3G48260.1; AT3G48260.1; AT3G48260.
DR KEGG; ath:AT3G48260; -.
DR Araport; AT3G48260; -.
DR TAIR; locus:504955638; AT3G48260.
DR eggNOG; KOG0584; Eukaryota.
DR HOGENOM; CLU_000288_142_3_1; -.
DR InParanoid; Q9STK6; -.
DR OMA; SWIDSKS; -.
DR OrthoDB; 695382at2759; -.
DR PhylomeDB; Q9STK6; -.
DR PRO; PR:Q9STK6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9STK6; baseline and differential.
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; IPR024678; Kinase_OSR1/WNK_CCT.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF12202; OSR1_C; 1.
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 ATP-binding; Coiled coil; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..516
FT /note="Probable serine/threonine-protein kinase WNK3"
FT /id="PRO_0000351661"
FT DOMAIN 22..280
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 426..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 457..490
FT /evidence="ECO:0000255"
FT ACT_SITE 169
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9JIH7"
FT BINDING 102..105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9H4A3"
FT BINDING 152
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9H4A3"
SQ SEQUENCE 516 AA; 58949 MW; AC46D0C2C4A67B64 CRC64;
MRQDENNSEE EFVEIDPTGR YGRYKEVLGK GAFKEVYRAF DQLEGIEVAW NQVKLDDKFC
SSEDLDRLYS EVHLLKTLKH KSIIKFYTSW IDHQHMTINL ITEVFTSGNL RQYRKKHKCV
DLRALKKWSR QILEGLVYLH SHDPPVIHRD LKCDNIFING NQGEVKIGDL GLAAILHRAR
SAHSVIGTPE FMAPELYEED YNVLVDIYAF GMCLLELVTF EYPYSECTNA AQIYRKVTSG
IKPAALLNVT DPQVRAFIEK CIAKVSQRLS AKELLDDPFL KCYKENTENV SSHKENGYNG
NGIVDKLSDS EVGLLTVEGQ RKDLNTIFLK LRITDSKGQI RNIHFPFNIE TDTSFSVAIE
MVEELDLTDD QDISTIAKMI DTEIHSHIPD WTPSRLIGDD SAVQKCLSSP ETLHLDRFPS
GRKFWSSPKA GAGDSRSPFA PRSNSKLSSA QGPINQEVGV IVEKLESLLR KQREEIEEMQ
RDQERIVTEF LKEFPPEICE EALVRLQVKD SDNLLC
