VQ33_ARATH
ID VQ33_ARATH Reviewed; 243 AA.
AC Q9FHZ3;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=VQ motif-containing protein 33 {ECO:0000303|PubMed:22535423};
DE Short=AtVQ33 {ECO:0000303|PubMed:22535423};
DE AltName: Full=MPK3/6-targeted VQ-motif-containing protein 3 {ECO:0000303|PubMed:24750137};
GN Name=VQ33 {ECO:0000303|PubMed:22535423};
GN Synonyms=MVQ3 {ECO:0000303|PubMed:24750137};
GN OrderedLocusNames=At5g53830 {ECO:0000312|Araport:AT5G53830};
GN ORFNames=MGN6.22 {ECO:0000312|EMBL:BAB09555.1};
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=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(1999).
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;
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).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=22535423; DOI=10.1104/pp.112.196816;
RA Cheng Y., Zhou Y., Yang Y., Chi Y.J., Zhou J., Chen J.Y., Wang F., Fan B.,
RA Shi K., Zhou Y.H., Yu J.Q., Chen Z.;
RT "Structural and functional analysis of VQ motif-containing proteins in
RT Arabidopsis as interacting proteins of WRKY transcription factors.";
RL Plant Physiol. 159:810-825(2012).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND PHOSPHORYLATION AT SER-83;
RP THR-139; SER-148; SER-152; SER-165; SER-178; THR-181; SER-218; SER-221;
RP THR-222 AND SER-238.
RX PubMed=24750137; DOI=10.1111/nph.12817;
RA Pecher P., Eschen-Lippold L., Herklotz S., Kuhle K., Naumann K., Bethke G.,
RA Uhrig J., Weyhe M., Scheel D., Lee J.;
RT "The Arabidopsis thaliana mitogen-activated protein kinases MPK3 and MPK6
RT target a subclass of 'VQ-motif'-containing proteins to regulate immune
RT responses.";
RL New Phytol. 203:592-606(2014).
CC -!- FUNCTION: May modulate WRKY transcription factor activities.
CC {ECO:0000250|UniProtKB:Q9M9F0}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9M9F0}.
CC -!- PTM: Phosphorylated on serine and threonine residues by MPK6.
CC {ECO:0000269|PubMed:24750137}.
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DR EMBL; AB017066; BAB09555.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96411.1; -; Genomic_DNA.
DR EMBL; AF372918; AAK49634.1; -; mRNA.
DR EMBL; AY127951; AAM91050.1; -; mRNA.
DR RefSeq; NP_200194.1; NM_124762.3.
DR AlphaFoldDB; Q9FHZ3; -.
DR STRING; 3702.AT5G53830.1; -.
DR iPTMnet; Q9FHZ3; -.
DR PaxDb; Q9FHZ3; -.
DR PRIDE; Q9FHZ3; -.
DR ProteomicsDB; 242753; -.
DR EnsemblPlants; AT5G53830.1; AT5G53830.1; AT5G53830.
DR GeneID; 835464; -.
DR Gramene; AT5G53830.1; AT5G53830.1; AT5G53830.
DR KEGG; ath:AT5G53830; -.
DR Araport; AT5G53830; -.
DR TAIR; locus:2164022; AT5G53830.
DR eggNOG; ENOG502RIDK; Eukaryota.
DR HOGENOM; CLU_069496_0_0_1; -.
DR InParanoid; Q9FHZ3; -.
DR OMA; NMFAKND; -.
DR OrthoDB; 1494333at2759; -.
DR PhylomeDB; Q9FHZ3; -.
DR PRO; PR:Q9FHZ3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FHZ3; baseline and differential.
DR Genevisible; Q9FHZ3; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR InterPro; IPR008889; VQ.
DR InterPro; IPR039828; VQ33.
DR InterPro; IPR039611; VQ_4/11/13/19/31/33.
DR PANTHER; PTHR33402; PTHR33402; 1.
DR PANTHER; PTHR33402:SF17; PTHR33402:SF17; 1.
DR Pfam; PF05678; VQ; 1.
PE 1: Evidence at protein level;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..243
FT /note="VQ motif-containing protein 33"
FT /id="PRO_0000432322"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 69..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 138..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 59..68
FT /note="VQ"
FT /evidence="ECO:0000305"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24750137"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5M750"
FT MOD_RES 139
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:24750137"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24750137"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24750137"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24750137"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LDZ1"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24750137"
FT MOD_RES 181
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:24750137"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24750137"
FT MOD_RES 221
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24750137"
FT MOD_RES 222
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:24750137"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24750137"
SQ SEQUENCE 243 AA; 26919 MW; C083D926A934C4F9 CRC64;
MEVSTSSMSS KPEQMQNPPP MISSPRFQPQ IISPHHHDQH QHLSNPYPTT FVQADTSTFK
QVVQMLTGSS TDTTTGKHHE APSPVNNNNK GSSFSIPPIK KTNSFKLYER RQNNNNMFAK
NDLMINTLRL QNSQRLMFTG GNSSHHQSPR FSPRNSSSSE NILLSPSMLD FPKLGLNSPV
TPLRSNDDPF NKSSPLSLGN SSEEDKAIAD KGFYLHPSPV STPRDSQPLL LPLFPVASPA
RNS
