ID   14339_ARATH             Reviewed;         263 AA.
AC   Q96299; O80367;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   27-MAR-2024, entry version 160.
DE   RecName: Full=14-3-3-like protein GF14 mu;
DE   AltName: Full=General regulatory factor 9;
GN   Name=GRF9; OrderedLocusNames=At2g42590; ORFNames=F14N22.14;
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].
RC   STRAIN=cv. Columbia;
RX   PubMed=9276953; DOI=10.1104/pp.114.4.1421;
RA   Wu K., Rooney M.F., Ferl R.J.;
RT   "The Arabidopsis 14-3-3 multigene family.";
RL   Plant Physiol. 114:1421-1431(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10996255; DOI=10.1016/s0168-9452(00)00320-4;
RA   Kuromori T., Yamamoto M.;
RT   "Members of the Arabidopsis 14-3-3 gene family trans-complement two types
RT   of defects in fission yeast.";
RL   Plant Sci. 158:155-161(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RA   Chung H.-J., Shanker S., Ferl R.J.;
RT   "Sequences of five Arabidopsis general regulatory factor (GRF) genes
RT   encoding 14-3-3 proteins.";
RL   (er) Plant Gene Register PGR99-114(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [5]
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   [6]
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   [7]
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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239, AND IDENTIFICATION BY
RP   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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19376835; DOI=10.1104/pp.109.138677;
RA   Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA   Grossmann J., Gruissem W., Baginsky S.;
RT   "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT   chloroplast kinase substrates and phosphorylation networks.";
RL   Plant Physiol. 150:889-903(2009).
RN   [10]
RP   INTERACTION WITH DREB1A AND DREB1B.
RC   STRAIN=cv. Columbia;
RX   PubMed=28344081; DOI=10.1016/j.molcel.2017.02.016;
RA   Liu Z., Jia Y., Ding Y., Shi Y., Li Z., Guo Y., Gong Z., Yang S.;
RT   "Plasma membrane CRPK1-mediated phosphorylation of 14-3-3 proteins induces
RT   their nuclear import to fine-tune CBF signaling during cold response.";
RL   Mol. Cell 66:117-128(2017).
CC   -!- FUNCTION: Is associated with a DNA binding complex that binds to the G
CC       box, a well-characterized cis-acting DNA regulatory element found in
CC       plant genes.
CC   -!- SUBUNIT: Interacts with DREB1A and DREB1B in the nucleus.
CC       {ECO:0000269|PubMed:28344081}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P48349}. Cytoplasm
CC       {ECO:0000250|UniProtKB:P48349}. Note=Translocates from the cytosol to
CC       the nucleus when phosphorylated. {ECO:0000250|UniProtKB:P48349}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q96299-1; Sequence=Displayed;
CC   -!- SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}.
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DR   EMBL; U60444; AAB49334.2; -; mRNA.
DR   EMBL; AB011545; BAA32735.1; -; mRNA.
DR   EMBL; AF145301; AAD51784.1; -; Genomic_DNA.
DR   EMBL; AC007087; AAD23005.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC10142.1; -; Genomic_DNA.
DR   EMBL; AY093076; AAM13075.1; -; mRNA.
DR   EMBL; AY128764; AAM91164.1; -; mRNA.
DR   EMBL; AY085927; AAM63139.1; -; mRNA.
DR   PIR; T52037; T52037.
DR   RefSeq; NP_565977.1; NM_129820.3. [Q96299-1]
DR   AlphaFoldDB; Q96299; -.
DR   SMR; Q96299; -.
DR   BioGRID; 4196; 6.
DR   IntAct; Q96299; 4.
DR   STRING; 3702.Q96299; -.
DR   iPTMnet; Q96299; -.
DR   PaxDb; 3702-AT2G42590-3; -.
DR   ProteomicsDB; 244502; -. [Q96299-1]
DR   EnsemblPlants; AT2G42590.1; AT2G42590.1; AT2G42590. [Q96299-1]
DR   GeneID; 818859; -.
DR   Gramene; AT2G42590.1; AT2G42590.1; AT2G42590. [Q96299-1]
DR   KEGG; ath:AT2G42590; -.
DR   Araport; AT2G42590; -.
DR   TAIR; AT2G42590; GRF9.
DR   eggNOG; KOG0841; Eukaryota.
DR   InParanoid; Q96299; -.
DR   PhylomeDB; Q96299; -.
DR   PRO; PR:Q96299; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q96299; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   Gene3D; 1.20.190.20; 14-3-3 domain; 1.
DR   InterPro; IPR000308; 14-3-3.
DR   InterPro; IPR023409; 14-3-3_CS.
DR   InterPro; IPR036815; 14-3-3_dom_sf.
DR   InterPro; IPR023410; 14-3-3_domain.
DR   PANTHER; PTHR18860; 14-3-3 PROTEIN; 1.
DR   PANTHER; PTHR18860:SF160; 14-3-3 PROTEIN ZETA; 1.
DR   Pfam; PF00244; 14-3-3; 1.
DR   PIRSF; PIRSF000868; 14-3-3; 1.
DR   PRINTS; PR00305; 1433ZETA.
DR   SMART; SM00101; 14_3_3; 1.
DR   SUPFAM; SSF48445; 14-3-3 protein; 1.
DR   PROSITE; PS00796; 1433_1; 1.
DR   PROSITE; PS00797; 1433_2; 1.
DR   Genevisible; Q96299; AT.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Nucleus; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..263
FT                   /note="14-3-3-like protein GF14 mu"
FT                   /id="PRO_0000058671"
FT   REGION          239..263
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         67
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P48349"
FT   MOD_RES         211
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P48349"
FT   MOD_RES         239
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19245862,
FT                   ECO:0007744|PubMed:19376835"
SQ   SEQUENCE   263 AA;  29520 MW;  B70A45DF64DFD926 CRC64;
     MGSGKERDTF VYLAKLSEQA ERYEEMVESM KSVAKLNVDL TVEERNLLSV GYKNVIGSRR
     ASWRIFSSIE QKEAVKGNDV NVKRIKEYME KVELELSNIC IDIMSVLDEH LIPSASEGES
     TVFFNKMKGD YYRYLAEFKS GNERKEAADQ SLKAYEIATT AAEAKLPPTH PIRLGLALNF
     SVFYYEIMNA PERACHLAKQ AFDEAISELD TLNEESYKDS TLIMQLLRDN LTLWTSDISE
     EGGDDAHKTN GSAKPGAGGD DAE
//