VQ4_ARATH
ID VQ4_ARATH Reviewed; 247 AA.
AC Q5M750; Q8LDD4; Q94K19; Q9FZA1;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=VQ motif-containing protein 4 {ECO:0000303|PubMed:22535423};
DE Short=AtVQ4 {ECO:0000303|PubMed:22535423};
DE AltName: Full=MPK3/6-targeted VQ-motif-containing protein 1 {ECO:0000303|PubMed:24750137};
GN Name=VQ4 {ECO:0000303|PubMed:22535423};
GN Synonyms=MVQ1 {ECO:0000303|PubMed:24750137};
GN OrderedLocusNames=At1g28280 {ECO:0000312|Araport:AT1G28280};
GN ORFNames=F3H9.7 {ECO:0000312|EMBL:AAF98427.1};
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=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 [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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 107-247.
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 [6]
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 [7]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH MPK3 AND
RP MPK6, AND PHOSPHORYLATION AT SER-16; SER-106; SER-155; SER-194; SER-215 AND
RP THR-219.
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: Acts as negative regulator of WRKY33 transcription factor
CC activity in the promotion of defense gene expression. Acts as a
CC negative regulator of pathogen-associated molecular pattern (PAMP)-
CC induced responses to modulate resistance to pathogens.
CC {ECO:0000269|PubMed:24750137}.
CC -!- SUBUNIT: Interacts with MPK3 and MPK6. {ECO:0000269|PubMed:24750137}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9M9F0}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences. {ECO:0000305};
CC Name=1;
CC IsoId=Q5M750-1; Sequence=Displayed;
CC -!- PTM: Phosphorylated on serine and threonine residues by MPK6 following
CC treatment with the pathogen-associated molecular pattern (PAMP) flg22.
CC MAP kinase-mediated phosphorylation after PAMP elicitation causes
CC degradation of VQ4, allowing WRKY33 to promote transcription from
CC defense genes. {ECO:0000269|PubMed:24750137}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF98427.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC021044; AAF98427.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE30940.1; -; Genomic_DNA.
DR EMBL; AF370468; AAK43845.1; -; mRNA.
DR EMBL; BT020398; AAV97789.1; -; mRNA.
DR EMBL; BT020477; AAW38978.1; -; mRNA.
DR EMBL; AY086070; AAM67358.1; -; mRNA.
DR PIR; A86409; A86409.
DR RefSeq; NP_564303.2; NM_102593.3. [Q5M750-1]
DR AlphaFoldDB; Q5M750; -.
DR STRING; 3702.AT1G28280.1; -.
DR iPTMnet; Q5M750; -.
DR PaxDb; Q5M750; -.
DR PRIDE; Q5M750; -.
DR EnsemblPlants; AT1G28280.1; AT1G28280.1; AT1G28280. [Q5M750-1]
DR GeneID; 839722; -.
DR Gramene; AT1G28280.1; AT1G28280.1; AT1G28280. [Q5M750-1]
DR KEGG; ath:AT1G28280; -.
DR Araport; AT1G28280; -.
DR TAIR; locus:2032200; AT1G28280.
DR eggNOG; ENOG502RIDK; Eukaryota.
DR HOGENOM; CLU_069496_0_0_1; -.
DR InParanoid; Q5M750; -.
DR PRO; PR:Q5M750; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q5M750; baseline and differential.
DR Genevisible; Q5M750; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0051245; P:negative regulation of cellular defense response; IMP:UniProtKB.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IDA:UniProtKB.
DR InterPro; IPR008889; VQ.
DR InterPro; IPR039827; VQ4/VQ13.
DR InterPro; IPR039611; VQ_4/11/13/19/31/33.
DR PANTHER; PTHR33402; PTHR33402; 1.
DR PANTHER; PTHR33402:SF25; PTHR33402:SF25; 1.
DR Pfam; PF05678; VQ; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Nucleus; Phosphoprotein; Plant defense;
KW Reference proteome.
FT CHAIN 1..247
FT /note="VQ motif-containing protein 4"
FT /id="PRO_0000432308"
FT REGION 1..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 67..76
FT /note="VQ"
FT /evidence="ECO:0000305"
FT COMPBIAS 1..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24750137"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24750137"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24750137"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9FHZ3"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LDZ1"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LDZ1"
FT MOD_RES 178
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9LDZ1"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24750137"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24750137"
FT MOD_RES 219
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:24750137"
FT MOD_RES 234
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O23660"
FT MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9LDZ1"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O23660"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O23660"
FT CONFLICT 32..39
FT /note="SESNKPPT -> RESNNPPS (in Ref. 3; AAK43845)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="V -> D (in Ref. 3; AAK43845)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="A -> G (in Ref. 3; AAK43845)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="L -> I (in Ref. 3; AAK43845)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 247 AA; 26863 MW; A130A8F42BB92144 CRC64;
MENSPRYREA TNLIPSPRCH NSNNSCGMSS SSESNKPPTT PTRHVTTRSE SGNPYPTTFV
QADTSSFKQV VQMLTGSAER PKHGSSLKPN PTHHQPDPRS TPSSFSIPPI KAVPNKKQSS
SSASGFRLYE RRNSMKNLKI NPLNPVFNPV NSAFSPRKPE ILSPSILDFP SLVLSPVTPL
IPDPFDRSGS SNQSPNELAA EEKAMKERGF YLHPSPATTP MDPEPRLLPL FPVTSPRVSG
SSSASTS