14333_ARATH
ID 14333_ARATH Reviewed; 255 AA.
AC P42644; F4KBI7; Q945L2;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=14-3-3-like protein GF14 psi {ECO:0000303|PubMed:7972511};
DE AltName: Full=General regulatory factor 3 {ECO:0000303|PubMed:7870824};
DE AltName: Full=Protein RARE COLD INDUCIBLE 1A {ECO:0000303|PubMed:7520301};
GN Name=GRF3 {ECO:0000303|PubMed:7870824};
GN Synonyms=RCI1A {ECO:0000303|PubMed:7520301};
GN OrderedLocusNames=At5g38480 {ECO:0000312|Araport:AT5G38480};
GN ORFNames=MXI10.21 {ECO:0000312|EMBL:BAB10138.1};
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 [MRNA] (ISOFORM 1), AND FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=7972511; DOI=10.1104/pp.105.4.1459;
RA Lu G., Rooney M.F., Wu K., Ferl R.J.;
RT "Five cDNAs encoding Arabidopsis GF14 proteins.";
RL Plant Physiol. 105:1459-1460(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INDUCTION BY COLD.
RX PubMed=7520301; DOI=10.1007/bf00029607;
RA Jarillo J.A., Capel J., Leyva A., Martinez Zapater J.M., Salinas J.;
RT "Two related low-temperature-inducible genes of Arabidopsis encode proteins
RT showing high homology to 14-3-3 proteins, a family of putative kinase
RT regulators.";
RL Plant Mol. Biol. 25:693-704(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=7870824; DOI=10.1104/pp.107.1.283;
RA Rooney M.F., Ferl R.J.;
RT "Sequences of three Arabidopsis general regulatory factor genes encoding
RT GF14 (14-3-3) proteins.";
RL Plant Physiol. 107:283-284(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
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 1).
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 GENE FAMILY.
RX PubMed=11351068; DOI=10.1104/pp.126.1.35;
RA DeLille J.M., Sehnke P.C., Ferl R.J.;
RT "The arabidopsis 14-3-3 family of signaling regulators.";
RL Plant Physiol. 126:35-38(2001).
RN [9]
RP FUNCTION, AND SUBUNIT.
RX PubMed=16407442; DOI=10.1104/pp.105.073916;
RA Sehnke P.C., Laughner B., Cardasis H., Powell D., Ferl R.J.;
RT "Exposed loop domains of complexed 14-3-3 proteins contribute to structural
RT diversity and functional specificity.";
RL Plant Physiol. 140:647-660(2006).
RN [10]
RP REGULATION BY PHOSPHATE DEPRIVATION.
RX PubMed=17598127; DOI=10.1007/s00425-007-0569-0;
RA Cao A., Jain A., Baldwin J.C., Raghothama K.G.;
RT "Phosphate differentially regulates 14-3-3 family members and GRF9 plays a
RT role in Pi-starvation induced responses.";
RL Planta 226:1219-1230(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-238, 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 [12]
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 [13]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY DEPRIVATION OF PHOSPHATE;
RP POTASSIUM AND NITROGEN, AND INTERACTION WITH AGT3; GLN1-1; GLN1-2; GLN1-4;
RP SAM1; SAM2 AND METK3.
RX PubMed=21094157; DOI=10.1016/j.febslet.2010.11.025;
RA Shin R., Jez J.M., Basra A., Zhang B., Schachtman D.P.;
RT "14-3-3 proteins fine-tune plant nutrient metabolism.";
RL FEBS Lett. 585:143-147(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-162, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22092075; DOI=10.1021/pr200917t;
RA Aryal U.K., Krochko J.E., Ross A.R.;
RT "Identification of phosphoproteins in Arabidopsis thaliana leaves using
RT polyethylene glycol fractionation, immobilized metal-ion affinity
RT chromatography, two-dimensional gel electrophoresis and mass
RT spectrometry.";
RL J. Proteome Res. 11:425-437(2012).
RN [15]
RP FUNCTION, DISRUPTION PHENOTYPE, AND REGULATION BY MIR396.
RX PubMed=22751317; DOI=10.4161/psb.20420;
RA Hewezi T., Baum T.J.;
RT "Complex feedback regulations govern the expression of miRNA396 and its GRF
RT target genes.";
RL Plant Signal. Behav. 7:749-751(2012).
RN [16]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY COLD, SUBCELLULAR LOCATION,
RP AND INTERACTION WITH ACS2; ACS5; ACS6; ACS8 AND ACS11.
RX PubMed=25122152; DOI=10.1105/tpc.114.127605;
RA Catala R., Lopez-Cobollo R., Mar Castellano M., Angosto T., Alonso J.M.,
RA Ecker J.R., Salinas J.;
RT "The Arabidopsis 14-3-3 protein RARE COLD INDUCIBLE 1A links low-
RT temperature response and ethylene biosynthesis to regulate freezing
RT tolerance and cold acclimation.";
RL Plant Cell 26:3326-3342(2014).
RN [17]
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 [18]
RP INTERACTION WITH FD.
RX PubMed=25661797; DOI=10.1038/srep08341;
RA Kawamoto N., Sasabe M., Endo M., Machida Y., Araki T.;
RT "Calcium-dependent protein kinases responsible for the phosphorylation of a
RT bZIP transcription factor FD crucial for the florigen complex formation.";
RL Sci. Rep. 5:8341-8341(2015).
RN [19]
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 (PubMed:7972511, PubMed:7870824, PubMed:16407442). Involved
CC in the regulation of nutrient metabolism (PubMed:22104211,
CC PubMed:21094157). Reciprocal negative transcription regulation of
CC miR396 (PubMed:22751317). Negative regulator of constitutive freezing
CC tolerance and cold acclimation by controlling cold-induced gene
CC expression partially through an ethylene (ET)-dependent pathway;
CC prevents ethylene (ET) biosynthesis, probably by binding 1-
CC aminocyclopropane-1-carboxylate synthases (ACS) to reduce their
CC stability, thus contributing to establish adequate ET levels under both
CC standard and low-temperature conditions (PubMed:25122152).
CC {ECO:0000269|PubMed:16407442, ECO:0000269|PubMed:21094157,
CC ECO:0000269|PubMed:22104211, ECO:0000269|PubMed:22751317,
CC ECO:0000269|PubMed:25122152, ECO:0000303|PubMed:7870824,
CC ECO:0000303|PubMed:7972511}.
CC -!- SUBUNIT: Component of a DNA binding complex that binds to the G box
CC (PubMed:16407442). Interacts with IDH3, AGT3, GLN1-1, GLN1-2, GLN1-4,
CC SAM1, SAM2, MDH1, METK3 and MDH2 (PubMed:22104211, PubMed:21094157).
CC Binds to 1-aminocyclopropane-1-carboxylate synthases (ACS) such as
CC ACS2, ACS5, ACS6, ACS8, and ACS11 (PubMed:25122152). Interacts with FD
CC (PubMed:25661797). Interacts with DREB1A and DREB1B in the nucleus
CC (PubMed:28344081). Interacts with CINV1 (PubMed:25256212).
CC {ECO:0000269|PubMed:16407442, ECO:0000269|PubMed:21094157,
CC ECO:0000269|PubMed:22104211, ECO:0000269|PubMed:25122152,
CC ECO:0000269|PubMed:25256212, ECO:0000269|PubMed:25661797,
CC ECO:0000269|PubMed:28344081}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25122152}. Nucleus
CC {ECO:0000269|PubMed:25122152}. 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=P42644-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P42644-2; Sequence=VSP_057062;
CC -!- INDUCTION: By cold in an abscisic acid- (ABA-) independent manner (at
CC protein level) (PubMed:7520301, PubMed:25122152). Repressed by
CC phosphate (Pi) deprivation (PubMed:17598127). Induced by nitrogen (N)
CC and phosphate (P) deprivation in leaves, but repressed by potassium (K)
CC and N deprivation in roots (PubMed:21094157). Repressed by miR396
CC (PubMed:22751317). {ECO:0000269|PubMed:17598127,
CC ECO:0000269|PubMed:21094157, ECO:0000269|PubMed:22751317,
CC ECO:0000269|PubMed:25122152, ECO:0000269|PubMed:7520301}.
CC -!- DISRUPTION PHENOTYPE: Short primary roots and reduced size, with
CC smaller cells (PubMed:21094157, PubMed:25122152). Disturbed levels of
CC several metabolites (e.g. beta-alanine, threonic acid, phenylalanine,
CC 1,3-diaminopropane dihydrochloride, citrate, glycine, aspartate,
CC glucose, 1,4-diaminobutane, proline, palmitate and shikimate)
CC (PubMed:22104211). Increased miR396 levels in plants lacking
CC simultaneously GRF1, GRF2 and GRF3 (PubMed:22751317). Higher freezing
CC tolerance, and greater levels of cold-inducible genes and
CC ethylene- (ET-) inducible genes leading to higher ET levels, as well as
CC slightly enhanced expression of ACS6 (PubMed:25122152).
CC {ECO:0000269|PubMed:21094157, ECO:0000269|PubMed:22104211,
CC ECO:0000269|PubMed:22751317, ECO:0000269|PubMed:25122152}.
CC -!- SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}.
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DR EMBL; L09110; AAA32799.1; -; mRNA.
DR EMBL; X74140; CAA52237.1; -; mRNA.
DR EMBL; U09375; AAA96252.1; -; Genomic_DNA.
DR EMBL; AB005231; BAB10138.1; -; Genomic_DNA.
DR EMBL; AB005248; BAB10138.1; JOINED; Genomic_DNA.
DR EMBL; CP002688; AED94323.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94324.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM71068.1; -; Genomic_DNA.
DR EMBL; AF412093; AAL06546.1; -; mRNA.
DR EMBL; AY093976; AAM16237.1; -; mRNA.
DR EMBL; AK226217; BAE98382.1; -; mRNA.
DR EMBL; AK228478; BAF00404.1; -; mRNA.
DR PIR; S47969; S47969.
DR PIR; S57277; S57277.
DR RefSeq; NP_001318697.1; NM_001344251.1. [P42644-2]
DR RefSeq; NP_001332624.1; NM_001344252.1. [P42644-2]
DR RefSeq; NP_568557.1; NM_123209.4. [P42644-1]
DR AlphaFoldDB; P42644; -.
DR SMR; P42644; -.
DR BioGRID; 19087; 275.
DR IntAct; P42644; 9.
DR STRING; 3702.AT5G38480.1; -.
DR iPTMnet; P42644; -.
DR PaxDb; P42644; -.
DR PRIDE; P42644; -.
DR ProteomicsDB; 243289; -. [P42644-1]
DR EnsemblPlants; AT5G38480.1; AT5G38480.1; AT5G38480. [P42644-1]
DR EnsemblPlants; AT5G38480.2; AT5G38480.2; AT5G38480. [P42644-2]
DR EnsemblPlants; AT5G38480.3; AT5G38480.3; AT5G38480. [P42644-2]
DR GeneID; 833836; -.
DR Gramene; AT5G38480.1; AT5G38480.1; AT5G38480. [P42644-1]
DR Gramene; AT5G38480.2; AT5G38480.2; AT5G38480. [P42644-2]
DR Gramene; AT5G38480.3; AT5G38480.3; AT5G38480. [P42644-2]
DR KEGG; ath:AT5G38480; -.
DR Araport; AT5G38480; -.
DR TAIR; locus:2177386; AT5G38480.
DR eggNOG; KOG0841; Eukaryota.
DR HOGENOM; CLU_058290_0_0_1; -.
DR OMA; STRIVEW; -.
DR PhylomeDB; P42644; -.
DR PRO; PR:P42644; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P42644; baseline and differential.
DR Genevisible; P42644; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; HDA:TAIR.
DR GO; GO:0006995; P:cellular response to nitrogen starvation; IEP:UniProtKB.
DR GO; GO:0016036; P:cellular response to phosphate starvation; IEP:UniProtKB.
DR GO; GO:0051365; P:cellular response to potassium ion starvation; IEP:UniProtKB.
DR GO; GO:0009631; P:cold acclimation; IMP:UniProtKB.
DR GO; GO:0009873; P:ethylene-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0019222; P:regulation of metabolic process; IMP:UniProtKB.
DR GO; GO:0009409; P:response to cold; IEP: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; Ethylene signaling pathway; Nucleus;
KW Phosphoprotein; Reference proteome; Stress response.
FT CHAIN 1..255
FT /note="14-3-3-like protein GF14 psi"
FT /id="PRO_0000058665"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48349"
FT MOD_RES 162
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22092075"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48349"
FT MOD_RES 210
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P48349"
FT MOD_RES 238
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT VAR_SEQ 239..241
FT /note="DEA -> VT (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_057062"
FT CONFLICT 90
FT /note="K -> E (in Ref. 1; AAA32799 and 3; AAA96252)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 255 AA; 28606 MW; 51E018F146ED2A0F CRC64;
MSTREENVYM AKLAEQAERY EEMVEFMEKV AKTVDVEELS VEERNLLSVA YKNVIGARRA
SWRIISSIEQ KEESKGNEDH VAIIKDYRGK IESELSKICD GILNVLEAHL IPSASPAESK
VFYLKMKGDY HRYLAEFKAG AERKEAAEST LVAYKSASDI ATAELAPTHP IRLGLALNFS
VFYYEILNSP DRACSLAKQA FDDAIAELDT LGEESYKDST LIMQLLRDNL TLWTSDMTDE
AGDEIKEASK PDGAE
