ID WNK9_ARATH Reviewed; 492 AA.
AC Q2V338; Q5XF58;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 134.
DE RecName: Full=Probable serine/threonine-protein kinase WNK9;
DE Short=AtWNK9;
DE EC=2.7.11.1;
DE AltName: Full=Protein kinase with no lysine 9;
GN Name=WNK9; OrderedLocusNames=At5g28080; ORFNames=T24G3.10;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-492.
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Cheuk R.F., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (NOV-2004) 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=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q2V338-1; Sequence=Displayed;
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=AAU90048.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AC006192; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED93774.1; -; Genomic_DNA.
DR EMBL; AK228774; BAF00673.1; -; mRNA.
DR EMBL; BT015758; AAU90048.1; ALT_INIT; mRNA.
DR EMBL; BT020173; AAV43775.1; -; mRNA.
DR RefSeq; NP_001031960.1; NM_001036883.2. [Q2V338-1]
DR RefSeq; NP_001332380.1; NM_001344062.1.
DR RefSeq; NP_001332381.1; NM_001344063.1.
DR RefSeq; NP_001332382.1; NM_001344060.1.
DR RefSeq; NP_001332383.1; NM_001344061.1.
DR RefSeq; NP_001332384.1; NM_001344059.1.
DR AlphaFoldDB; Q2V338; -.
DR SMR; Q2V338; -.
DR STRING; 3702.Q2V338; -.
DR PaxDb; 3702-AT5G28080-2; -.
DR EnsemblPlants; AT5G28080.2; AT5G28080.2; AT5G28080. [Q2V338-1]
DR GeneID; 832881; -.
DR Gramene; AT5G28080.2; AT5G28080.2; AT5G28080. [Q2V338-1]
DR KEGG; ath:AT5G28080; -.
DR Araport; AT5G28080; -.
DR TAIR; AT5G28080; WNK9.
DR eggNOG; KOG0584; Eukaryota.
DR HOGENOM; CLU_000288_142_2_1; -.
DR InParanoid; Q2V338; -.
DR OMA; HRPSSIC; -.
DR OrthoDB; 53548at2759; -.
DR PhylomeDB; Q2V338; -.
DR PRO; PR:Q2V338; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q2V338; baseline and differential.
DR Genevisible; Q2V338; AT.
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; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; TAS:TAIR.
DR CDD; cd13983; STKc_WNK; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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 PANTHER; PTHR13902; SERINE/THREONINE-PROTEIN KINASE WNK WITH NO LYSINE -RELATED; 1.
DR PANTHER; PTHR13902:SF116; SERINE_THREONINE-PROTEIN KINASE WNK9-RELATED; 1.
DR Pfam; PF12202; OSR1_C; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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; Kinase; Nucleotide-binding;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..492
FT /note="Probable serine/threonine-protein kinase WNK9"
FT /id="PRO_0000351667"
FT DOMAIN 25..282
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
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"
SQ SEQUENCE 492 AA; 56915 MW; 1B386EB19477E0C5 CRC64;
MMNNLSHLES DYSEYVEVDP TGRYGRYNEV LGKGSSKTVY RGFDEYQGIE VAWNQVKLYD
FLQSPQELER LYCEIHLLKT LKHKSIMKFY ASWVDTDNRN INFVTEMFTS GTLRQYRLKH
KRVNIRAVKN WCRQILRGLN YLHTHDPPVI HRDLKCDNIF INGNQGEVKI GDLGLAACLQ
HSHAAHCVGT PEFMAPEVYK EEYNQLVDIY SFGMCVLEMV TFDYPYSECS HPAQIYKRVI
SGKKPDGLDK VKDPEVRGFI EKCLATVSLR LSACELLDDH FLCIDESDMR RVESEKGLID
EAGTPLRHSY HIPHYSNGYY SLYNQNQWDY NGDETVESHE IDLLEFQNDD DEEEEDKRFG
SVDISIKGKR RDNGDGLFLR LKTVNKEGCV RNIYFPFDIE TDTAISVARE MVEELEMDDR
DVTKIANMID GEIASLVPNW SIFCSSESNR SSVGSVMDFN EMQCGRDGCE EKHGRFEEIT
FEITVNDSDE ED
//
