14338_ARATH
ID 14338_ARATH Reviewed; 248 AA.
AC P48348; Q0WSB7; Q9SWP7;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=14-3-3-like protein GF14 kappa;
DE AltName: Full=General regulatory factor 8;
GN Name=GRF8; OrderedLocusNames=At5g65430; ORFNames=MNA5.16;
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] (ISOFORM 1).
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 SEQUENCE REVISION TO 53; 72; 121 AND 154.
RA Reyes M., Ferl R.J.;
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
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=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
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] (ISOFORM 1).
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] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [9]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH IDH3; MDH1 AND MDH2.
RX PubMed=22104211; DOI=10.1186/1752-0509-5-192;
RA Diaz C., Kusano M., Sulpice R., Araki M., Redestig H., Saito K., Stitt M.,
RA Shin R.;
RT "Determining novel functions of Arabidopsis 14-3-3 proteins in central
RT metabolic processes.";
RL BMC Syst. Biol. 5:192-192(2011).
RN [10]
RP INTERACTION WITH CINV1.
RX PubMed=25256212; DOI=10.1111/tpj.12677;
RA Gao J., van Kleeff P.J., Oecking C., Li K.W., Erban A., Kopka J.,
RA Hincha D.K., de Boer A.H.;
RT "Light modulated activity of root alkaline/neutral invertase involves the
RT interaction with 14-3-3 proteins.";
RL Plant J. 80:785-796(2014).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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. Involved in the regulation of nutrient metabolism
CC (PubMed:22104211). Negative regulator of freezing tolerance that
CC modulates cold-responsive C-repeat-binding factors (CBF) DREB1A AND
CC DREB1B proteins stability by facilitating their ubiquitin-mediated
CC degradation (PubMed:28344081). {ECO:0000269|PubMed:22104211,
CC ECO:0000269|PubMed:28344081}.
CC -!- SUBUNIT: Interacts with the isocitrate dehydrogenase IDH3, and malate
CC dehydrogenases MDH1 and MDH2 (PubMed:22104211). Interacts with CINV1
CC (PubMed:25256212). {ECO:0000269|PubMed:22104211,
CC ECO:0000269|PubMed:25256212}.
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=2;
CC Name=1;
CC IsoId=P48348-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P48348-2; Sequence=VSP_008971;
CC -!- DISRUPTION PHENOTYPE: Disturbed levels of several metabolites (e.g.
CC beta-alanine, ribose, aspartate, pyroglutamate, glutamate, asparagine,
CC fructose-6-phosphate, myo-inositol, 1,4-diaminobutane, palmitate and
CC shikimate). Enhanced freezing tolerance associated with enhanced cold
CC induction of cold-responsive C-repeat-binding factor (CBF) target genes
CC in the double mutant lacking both GRF6 and GRF8, probably due to the
CC suppression of ubiquitin-mediated degradation DREB1A and DREB1B
CC degradation by the 26S proteasome pathway (PubMed:28344081).
CC {ECO:0000269|PubMed:22104211, ECO:0000269|PubMed:28344081}.
CC -!- SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U36447; AAA79700.2; -; mRNA.
DR EMBL; AF145300; AAD51783.1; -; Genomic_DNA.
DR EMBL; AB011479; BAB11565.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98052.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98053.1; -; Genomic_DNA.
DR EMBL; AY050996; AAK93673.1; -; mRNA.
DR EMBL; AY079350; AAL85081.1; -; mRNA.
DR EMBL; AK228019; BAE99981.1; -; mRNA.
DR EMBL; AY085088; AAM61642.1; -; mRNA.
DR RefSeq; NP_569012.2; NM_125941.2. [P48348-2]
DR RefSeq; NP_851274.1; NM_180943.2. [P48348-1]
DR AlphaFoldDB; P48348; -.
DR SMR; P48348; -.
DR BioGRID; 21910; 196.
DR IntAct; P48348; 4.
DR MINT; P48348; -.
DR STRING; 3702.AT5G65430.3; -.
DR iPTMnet; P48348; -.
DR MetOSite; P48348; -.
DR PaxDb; P48348; -.
DR PRIDE; P48348; -.
DR ProteomicsDB; 244525; -. [P48348-1]
DR EnsemblPlants; AT5G65430.1; AT5G65430.1; AT5G65430. [P48348-1]
DR EnsemblPlants; AT5G65430.2; AT5G65430.2; AT5G65430. [P48348-2]
DR GeneID; 836668; -.
DR Gramene; AT5G65430.1; AT5G65430.1; AT5G65430. [P48348-1]
DR Gramene; AT5G65430.2; AT5G65430.2; AT5G65430. [P48348-2]
DR KEGG; ath:AT5G65430; -.
DR Araport; AT5G65430; -.
DR eggNOG; KOG0841; Eukaryota.
DR OMA; FEMATTI; -.
DR PhylomeDB; P48348; -.
DR PRO; PR:P48348; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P48348; baseline and differential.
DR Genevisible; P48348; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0019222; P:regulation of metabolic process; IMP:UniProtKB.
DR GO; GO:0050826; P:response to freezing; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR Gene3D; 1.20.190.20; -; 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; PTHR18860; 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; SSF48445; 1.
DR PROSITE; PS00796; 1433_1; 1.
DR PROSITE; PS00797; 1433_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..248
FT /note="14-3-3-like protein GF14 kappa"
FT /id="PRO_0000058670"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48349"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48349"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48349"
FT MOD_RES 214
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P48349"
FT VAR_SEQ 243..244
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.7"
FT /id="VSP_008971"
SQ SEQUENCE 248 AA; 28029 MW; 848897CE6DB6BA37 CRC64;
MATTLSRDQY VYMAKLAEQA ERYEEMVQFM EQLVSGATPA GELTVEERNL LSVAYKNVIG
SLRAAWRIVS SIEQKEESRK NEEHVSLVKD YRSKVETELS SICSGILRLL DSHLIPSATA
SESKVFYLKM KGDYHRYLAE FKSGDERKTA AEDTMIAYKA AQDVAVADLA PTHPIRLGLA
LNFSVFYYEI LNSSEKACSM AKQAFEEAIA ELDTLGEESY KDSTLIMQLL RDNLTLWTSD
MQEQMDEA
