WAG2_ARATH
ID WAG2_ARATH Reviewed; 480 AA.
AC Q9LUL2;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Serine/threonine-protein kinase WAG2;
DE EC=2.7.11.1;
GN Name=WAG2; OrderedLocusNames=At3g14370; ORFNames=MLN21.15;
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=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 [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 Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF Clones.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=16460509; DOI=10.1111/j.1365-313x.2005.02641.x;
RA Santner A.A., Watson J.C.;
RT "The WAG1 and WAG2 protein kinases negatively regulate root waving in
RT Arabidopsis.";
RL Plant J. 45:752-764(2006).
RN [6]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=19075219; DOI=10.1073/pnas.0809761106;
RA Cheng Y., Qin G., Dai X., Zhao Y.;
RT "NPY genes and AGC kinases define two key steps in auxin-mediated
RT organogenesis in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:21017-21022(2008).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20823065; DOI=10.1242/dev.052456;
RA Dhonukshe P., Huang F., Galvan-Ampudia C.S., Mahonen A.P., Kleine-Vehn J.,
RA Xu J., Quint A., Prasad K., Friml J., Scheres B., Offringa R.;
RT "Plasma membrane-bound AGC3 kinases phosphorylate PIN auxin carriers at
RT TPRXS(N/S) motifs to direct apical PIN recycling.";
RL Development 137:3245-3255(2010).
CC -!- FUNCTION: Serine/threonine-protein kinase involved in the regulation of
CC auxin signaling. Acts as a positive regulator of cellular auxin efflux
CC and regulates organ development by enhancing PIN-mediated polar auxin
CC transport. Phosphorylates conserved serine residues in the PIN auxin
CC efflux carriers. Phosphorylation of PIN proteins is required and
CC sufficient for apical-basal PIN polarity that enables directional
CC intercellular auxin fluxes, which mediate differential growth, tissue
CC patterning and organogenesis. Acts as suppressors of root waving.
CC {ECO:0000269|PubMed:16460509, ECO:0000269|PubMed:19075219,
CC ECO:0000269|PubMed:20823065}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:20823065}.
CC Note=Targeted to the cell periphery.
CC -!- TISSUE SPECIFICITY: Expressed in root tips, lateral root primordia and
CC emerging true leaf primordia. {ECO:0000269|PubMed:16460509}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout embryogenesis with higher
CC expression in the cotyledon primordia at heart stages.
CC {ECO:0000269|PubMed:19075219}.
CC -!- DISRUPTION PHENOTYPE: Enhanced root waving when grown on agar plates.
CC {ECO:0000269|PubMed:16460509}.
CC -!- MISCELLANEOUS: Over-expression of WAG1 induces a basal-to-apical shift
CC in PIN1, PIN2 and PIN4 localization, resulting in the loss of auxin
CC gradients and strong defects in embryo and seedling roots.
CC {ECO:0000305|PubMed:20823065}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; AB022220; BAB01042.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75509.1; -; Genomic_DNA.
DR EMBL; BT029242; ABJ98574.1; -; mRNA.
DR EMBL; AY088832; AAM67139.1; -; mRNA.
DR RefSeq; NP_188054.1; NM_112295.4.
DR AlphaFoldDB; Q9LUL2; -.
DR SMR; Q9LUL2; -.
DR IntAct; Q9LUL2; 1.
DR STRING; 3702.AT3G14370.1; -.
DR iPTMnet; Q9LUL2; -.
DR PaxDb; Q9LUL2; -.
DR PRIDE; Q9LUL2; -.
DR ProteomicsDB; 242781; -.
DR EnsemblPlants; AT3G14370.1; AT3G14370.1; AT3G14370.
DR GeneID; 820658; -.
DR Gramene; AT3G14370.1; AT3G14370.1; AT3G14370.
DR KEGG; ath:AT3G14370; -.
DR Araport; AT3G14370; -.
DR TAIR; locus:2091035; AT3G14370.
DR eggNOG; KOG0610; Eukaryota.
DR HOGENOM; CLU_000288_63_30_1; -.
DR InParanoid; Q9LUL2; -.
DR OMA; NHRRHDP; -.
DR OrthoDB; 799520at2759; -.
DR PhylomeDB; Q9LUL2; -.
DR PRO; PR:Q9LUL2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LUL2; baseline and differential.
DR Genevisible; Q9LUL2; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; ISS:TAIR.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:TAIR.
DR GO; GO:0009926; P:auxin polar transport; IMP:TAIR.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0048825; P:cotyledon development; IGI:TAIR.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 2.
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; Auxin signaling pathway; Cytoplasm; Developmental protein;
KW Growth regulation; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..480
FT /note="Serine/threonine-protein kinase WAG2"
FT /id="PRO_0000425535"
FT DOMAIN 88..396
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 213
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 94..102
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 117
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 480 AA; 54427 MW; 54430F8E84319A4D CRC64;
MEQEDFYFPD TDLDLSFTST TTDRTFASSS ARTSLTLSFN DRLSTSSAVT TSSTSSSSVN
HRRHDPHWSA IKSAKLLSSD GNIHLRHLKL IRHLGTGNLG RVFLCNLRDS SARFALKVID
RNCLTTEKKL SQVETEAEIL SLLDHPFLPT LYARIDESHY TCLLIDYAPN GDLHSLLRKQ
PGNRLPIQPV RFFAAEVLVA LEYLHAMGIV YRDLKPENVL LREDGHVMLS DFDLCFKSDV
VPTFKSRRYR RSSSSPSLRR RRSGCFSVAA EKKYEREEIV SEFAAEPVTA FSRSCVGTHE
YLAPELVSGN GHGSGVDWWA FGIFLYELLY GTTPFKGESK EQTLRNIVST TKTASFHMDG
DLDEARDLIE KLLVKDPRKR LGCARGAQDI KRHPFFDGIK WPLIRHYKPP EEVRGLVIKK
STRPHASHVI AVSPRRRKSF LWRALSYLLR GKSSSGGSKN QSNSNYYHYV GKSYASRKRV
