14331_ARATH
ID 14331_ARATH Reviewed; 267 AA.
AC P42643; Q945M2; Q9M0S7;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 3.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=14-3-3-like protein GF14 chi;
DE AltName: Full=General regulatory factor 1;
GN Name=GRF1; OrderedLocusNames=At4g09000; ORFNames=F23J3.30;
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=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 SEQUENCE REVISION TO N-TERMINUS.
RA Ferl R.J., Lu G.;
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP INTERACTION WITH TPK1.
RX PubMed=17764516; DOI=10.1111/j.1365-313x.2007.03255.x;
RA Latz A., Becker D., Hekman M., Mueller T., Beyhl D., Marten I., Eing C.,
RA Fischer A., Dunkel M., Bertl A., Rapp U.R., Hedrich R.;
RT "TPK1, a Ca(2+)-regulated Arabidopsis vacuole two-pore K(+) channel is
RT activated by 14-3-3 proteins.";
RL Plant J. 52:449-459(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-267, 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 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [14]
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 [15]
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. Involved in the regulation of nutrient metabolism
CC (PubMed:22104211). {ECO:0000269|PubMed:22104211}.
CC -!- SUBUNIT: Interacts with TPK1 (PubMed:17764516). Interacts with the
CC isocitrate dehydrogenase IDH3, and malate dehydrogenases MDH1 and MDH2
CC (PubMed:22104211). Interacts with DREB1A and DREB1B in the nucleus
CC (PubMed:28344081). Interacts with CINV1 (PubMed:25256212).
CC {ECO:0000269|PubMed:17764516, ECO:0000269|PubMed:22104211,
CC ECO:0000269|PubMed:25256212, 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=P42643-1; Sequence=Displayed;
CC -!- DISRUPTION PHENOTYPE: Disturbed levels of several metabolites (e.g.
CC beta-alanine, aspartate, pyroglutamate, glutamate, glutamine, alpha-
CC ketoglutarate, palmitate and shikimate). {ECO:0000269|PubMed:22104211}.
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; L09112; AAA96323.1; -; mRNA.
DR EMBL; U09377; AAA96254.1; -; Genomic_DNA.
DR EMBL; AL161513; CAB78024.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82709.1; -; Genomic_DNA.
DR EMBL; AF412067; AAL06520.1; -; mRNA.
DR EMBL; AY065064; AAL57697.1; -; mRNA.
DR EMBL; AY086143; AAM63348.1; -; mRNA.
DR EMBL; BT024489; ABD19670.1; -; mRNA.
DR PIR; H85090; H85090.
DR PIR; S57276; S57276.
DR RefSeq; NP_567344.1; NM_116969.3. [P42643-1]
DR AlphaFoldDB; P42643; -.
DR SMR; P42643; -.
DR BioGRID; 11778; 230.
DR IntAct; P42643; 7.
DR iPTMnet; P42643; -.
DR PRIDE; P42643; -.
DR ProteomicsDB; 245154; -. [P42643-1]
DR EnsemblPlants; AT4G09000.1; AT4G09000.1; AT4G09000. [P42643-1]
DR GeneID; 826479; -.
DR Gramene; AT4G09000.1; AT4G09000.1; AT4G09000. [P42643-1]
DR KEGG; ath:AT4G09000; -.
DR Araport; AT4G09000; -.
DR HOGENOM; CLU_058290_0_0_1; -.
DR OMA; GDYHCYL; -.
DR PhylomeDB; P42643; -.
DR PRO; PR:P42643; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P42643; baseline and differential.
DR Genevisible; P42643; 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: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 Acetylation; Alternative splicing; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..267
FT /note="14-3-3-like protein GF14 chi"
FT /id="PRO_0000058663"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48349"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48349"
FT MOD_RES 216
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P48349"
FT MOD_RES 267
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT CONFLICT 240
FT /note="T -> A (in Ref. 1; AAA96323 and 3; AAA96254)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 267 AA; 29932 MW; 328FA525D8AE0290 CRC64;
MATPGASSAR DEFVYMAKLA EQAERYEEMV EFMEKVAKAV DKDELTVEER NLLSVAYKNV
IGARRASWRI ISSIEQKEES RGNDDHVSLI RDYRSKIETE LSDICDGILK LLDTILVPAA
ASGDSKVFYL KMKGDYHRYL AEFKSGQERK DAAEHTLTAY KAAQDIANSE LAPTHPIRLG
LALNFSVFYY EILNSPDRAC NLAKQAFDEA IAELDTLGEE SYKDSTLIMQ LLRDNLTLWT
SDMQDDVADD IKEAAPAAAK PADEQQS
