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VQ9_ARATH
ID   VQ9_ARATH               Reviewed;         311 AA.
AC   Q9M9F0; Q8LAX9;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=VQ motif-containing protein 9 {ECO:0000303|PubMed:22535423};
DE            Short=AtVQ9 {ECO:0000303|PubMed:22535423};
GN   Name=VQ9 {ECO:0000303|PubMed:22535423};
GN   OrderedLocusNames=At1g78310 {ECO:0000312|Araport:AT1G78310};
GN   ORFNames=F3F9.15 {ECO:0000312|EMBL:AAF71801.1};
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].
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   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   FUNCTION, INTERACTION WITH WRKY8, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP   INDUCTION BY SALT, MUTAGENESIS OF 93-VAL--LYS-96, AND DISRUPTION PHENOTYPE.
RX   PubMed=23451802; DOI=10.1111/tpj.12159;
RA   Hu Y., Chen L., Wang H., Zhang L., Wang F., Yu D.;
RT   "Arabidopsis transcription factor WRKY8 functions antagonistically with its
RT   interacting partner VQ9 to modulate salinity stress tolerance.";
RL   Plant J. 74:730-745(2013).
CC   -!- FUNCTION: Functions as a negative regulator of salt stress response.
CC       Functions as repressor of WRKY8 transcription factor by decreasing the
CC       DNA-binding activity of WRKY8 and acts antagonistically with WRKY8 to
CC       regulate sodium and potassium homeostasis under salt stress.
CC       {ECO:0000269|PubMed:23451802}.
CC   -!- SUBUNIT: Interacts (via N-terminus) with WRKY8.
CC       {ECO:0000269|PubMed:23451802}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23451802}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in roots and at lower levels in
CC       rosette leaves, cauline leaves, stems, flowers and siliques.
CC       {ECO:0000269|PubMed:23451802}.
CC   -!- INDUCTION: By salt stress. {ECO:0000269|PubMed:23451802}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC       conditions, but mutant plants show enhanced resistance to salt stress.
CC       {ECO:0000269|PubMed:23451802}.
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DR   EMBL; AC013430; AAF71801.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE36094.1; -; Genomic_DNA.
DR   EMBL; AY065462; AAL38903.1; -; mRNA.
DR   EMBL; AY117330; AAM51405.1; -; mRNA.
DR   EMBL; AY087538; AAM65080.1; -; mRNA.
DR   RefSeq; NP_565177.1; NM_106480.4.
DR   AlphaFoldDB; Q9M9F0; -.
DR   SMR; Q9M9F0; -.
DR   IntAct; Q9M9F0; 2.
DR   STRING; 3702.AT1G78310.1; -.
DR   PaxDb; Q9M9F0; -.
DR   PRIDE; Q9M9F0; -.
DR   ProteomicsDB; 242647; -.
DR   EnsemblPlants; AT1G78310.1; AT1G78310.1; AT1G78310.
DR   GeneID; 844166; -.
DR   Gramene; AT1G78310.1; AT1G78310.1; AT1G78310.
DR   KEGG; ath:AT1G78310; -.
DR   Araport; AT1G78310; -.
DR   TAIR; locus:2032045; AT1G78310.
DR   eggNOG; ENOG502QV2B; Eukaryota.
DR   HOGENOM; CLU_971171_0_0_1; -.
DR   InParanoid; Q9M9F0; -.
DR   OMA; LAPRWNN; -.
DR   OrthoDB; 1543929at2759; -.
DR   PhylomeDB; Q9M9F0; -.
DR   PRO; PR:Q9M9F0; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9M9F0; baseline and differential.
DR   Genevisible; Q9M9F0; AT.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0030007; P:cellular potassium ion homeostasis; IMP:UniProtKB.
DR   GO; GO:0006883; P:cellular sodium ion homeostasis; IMP:UniProtKB.
DR   GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IDA:UniProtKB.
DR   GO; GO:1901001; P:negative regulation of response to salt stress; IMP:UniProtKB.
DR   InterPro; IPR008889; VQ.
DR   InterPro; IPR039824; VQ9.
DR   InterPro; IPR039612; VQ_5/9/14.
DR   PANTHER; PTHR33783; PTHR33783; 1.
DR   PANTHER; PTHR33783:SF4; PTHR33783:SF4; 1.
DR   Pfam; PF05678; VQ; 1.
PE   1: Evidence at protein level;
KW   Nucleus; Reference proteome; Stress response.
FT   CHAIN           1..311
FT                   /note="VQ motif-containing protein 9"
FT                   /id="PRO_0000432305"
FT   REGION          1..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          103..125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          228..266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          290..311
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           90..99
FT                   /note="VQ"
FT                   /evidence="ECO:0000305"
FT   COMPBIAS        1..33
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..57
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        236..252
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         93..96
FT                   /note="VVQK->EDLE: Loss of interaction with WRKY8 protein."
FT                   /evidence="ECO:0000269|PubMed:23451802"
FT   CONFLICT        18
FT                   /note="A -> V (in Ref. 4; AAM65080)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   311 AA;  33577 MW;  B32D409EA21EF6C2 CRC64;
     MDKSCNSSGD SSAVSASATS STGNNTTNRD HYLRQLNKLS HKISKPTNSS SSVSVANREI
     DLPPPPPLQI NQGNLHQHQP PVYNINKNDF RDVVQKLTGS PAHERISAPP QQPIHHPKPQ
     QSSRLHRIRP PPLVHVINRP PGLLNDALIP QGSHHMNQNW TGVGFNLRPT APLSPLPPLP
     PVHAAAESPV SSYMRYLQNS MFAIDSNRKE FSGLSPLAPL VSPRWYQQQE NAPPSQHNSF
     PPPHPPPPSS AVSQTVPTSI PAPPLFGCSS SPKSPYGLLS PSILLSPSSG QLGFPVSPTT
     VPLPSPKYKG H
 
 
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