WNK7_ARATH
ID WNK7_ARATH Reviewed; 557 AA.
AC Q8LST2; Q9C5N1; Q9M9B6;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Probable serine/threonine-protein kinase WNK7;
DE Short=AtWNK7;
DE EC=2.7.11.1;
DE AltName: Full=Protein kinase with no lysine 7;
GN Name=WNK7; OrderedLocusNames=At1g49160; ORFNames=F27J15.7;
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).
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
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=Q8LST2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8LST2-2; Sequence=VSP_035531;
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to exon skipping. {ECO:0000305}.
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; AB085617; BAB92986.1; -; mRNA.
DR EMBL; AC016041; AAF69698.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE32397.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32398.1; -; Genomic_DNA.
DR EMBL; AF360136; AAK25846.1; -; mRNA.
DR RefSeq; NP_564541.1; NM_103806.2. [Q8LST2-2]
DR RefSeq; NP_849787.1; NM_179456.3. [Q8LST2-1]
DR AlphaFoldDB; Q8LST2; -.
DR SMR; Q8LST2; -.
DR STRING; 3702.AT1G49160.2; -.
DR iPTMnet; Q8LST2; -.
DR PaxDb; Q8LST2; -.
DR ProteomicsDB; 242790; -. [Q8LST2-1]
DR EnsemblPlants; AT1G49160.1; AT1G49160.1; AT1G49160. [Q8LST2-2]
DR EnsemblPlants; AT1G49160.2; AT1G49160.2; AT1G49160. [Q8LST2-1]
DR GeneID; 841339; -.
DR Gramene; AT1G49160.1; AT1G49160.1; AT1G49160. [Q8LST2-2]
DR Gramene; AT1G49160.2; AT1G49160.2; AT1G49160. [Q8LST2-1]
DR KEGG; ath:AT1G49160; -.
DR Araport; AT1G49160; -.
DR TAIR; locus:2028521; AT1G49160.
DR eggNOG; KOG0584; Eukaryota.
DR HOGENOM; CLU_000288_142_0_1; -.
DR InParanoid; Q8LST2; -.
DR PhylomeDB; Q8LST2; -.
DR PRO; PR:Q8LST2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8LST2; baseline and differential.
DR Genevisible; Q8LST2; 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; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..557
FT /note="Probable serine/threonine-protein kinase WNK7"
FT /id="PRO_0000351665"
FT DOMAIN 28..285
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 451..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..495
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..517
FT /note="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 MOD_RES 505
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LVL5"
FT VAR_SEQ 1..42
FT /note="MEGSEDASAIVEPPDPEVLEIDPTCRYIRYKEVIGKGASKTV -> MLLQLL
FT NHLTQKFLKSTQLVDIFG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_035531"
SQ SEQUENCE 557 AA; 63480 MW; 18146529E2E307F5 CRC64;
MEGSEDASAI VEPPDPEVLE IDPTCRYIRY KEVIGKGASK TVFKGFDEVD GIEVAWNQVR
IDDLLQSPDC LERLYSEVRL LKSLKHKNII RFYNSWIDDK NKTVNIITEL FTSGSLRQYR
KKHRKVNMKA VKCWARQILT GLKYLHSQDP PIIHRDIKCD NIFINGNHGE VKIGDLGLAT
VMEQANAKSV IGTPEFMAPE LYDENYNELA DIYSFGMCML EMVTFEYPYC ECRNSAQIYK
KVSSGIKPAS LSKVKDPEVM KFIEKCLLPA SERLSAEELL LDSFLNVNGL VMNNPLPLPD
IVMPKEGSFG ERCLMSEGPP NARNRTMSMN LDEDNNLPIV ISSNNSGTNC IEVRRAKRGN
FFVLKGEEND ENSVSLILRI VDENGRVRNI HFLFFQEGDT ASNVSSEMVE QLELTDKNVK
FIAELIDVLL VNLIPNWKTD VAVDHLIHPQ QNQSSKDNHQ NGASSQAGES ISHSLSSDYC
PRSDDEANPT VAATTEDQEA EKPGSLEEEE EDERLKEELE KIEERFREEM KEITRKREEA
TMETKNRFFE KKMQQVE
