14334_ARATH
ID 14334_ARATH Reviewed; 267 AA.
AC P46077;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=14-3-3-like protein GF14 phi;
DE AltName: Full=General regulatory factor 4;
GN Name=GRF4; OrderedLocusNames=At1g35160; ORFNames=T32G9.30;
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 23 AND 245.
RA Ferl R.J.;
RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 [4]
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 [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].
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, 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 [9]
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 [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 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).
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 FD (PubMed:25661797). Interacts with CINV1
CC (PubMed:25256212). {ECO:0000269|PubMed:25256212,
CC ECO:0000269|PubMed:25661797}.
CC -!- INTERACTION:
CC P46077; Q00403: GTF2B; Xeno; NbExp=2; IntAct=EBI-637479, EBI-389564;
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=P46077-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}.
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DR EMBL; L09111; AAB06231.1; -; mRNA.
DR EMBL; AF001414; AAB62224.1; -; Genomic_DNA.
DR EMBL; AC079605; AAG50610.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE31760.1; -; Genomic_DNA.
DR EMBL; AY084342; AAM60925.1; -; mRNA.
DR PIR; C86472; C86472.
DR RefSeq; NP_564453.1; NM_103213.3. [P46077-1]
DR AlphaFoldDB; P46077; -.
DR SMR; P46077; -.
DR BioGRID; 25635; 26.
DR IntAct; P46077; 8.
DR MINT; P46077; -.
DR STRING; 3702.AT1G35160.2; -.
DR iPTMnet; P46077; -.
DR PRIDE; P46077; -.
DR ProteomicsDB; 244516; -. [P46077-1]
DR EnsemblPlants; AT1G35160.1; AT1G35160.1; AT1G35160. [P46077-1]
DR GeneID; 840403; -.
DR Gramene; AT1G35160.1; AT1G35160.1; AT1G35160. [P46077-1]
DR KEGG; ath:AT1G35160; -.
DR Araport; AT1G35160; -.
DR eggNOG; KOG0841; Eukaryota.
DR HOGENOM; CLU_058290_0_0_1; -.
DR OMA; FKTAGER; -.
DR PhylomeDB; P46077; -.
DR PRO; PR:P46077; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P46077; baseline and differential.
DR Genevisible; P46077; 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: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 phi"
FT /id="PRO_0000058666"
FT REGION 244..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48349"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48349"
FT MOD_RES 217
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P48349"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19245862,
FT ECO:0007744|PubMed:19376835"
SQ SEQUENCE 267 AA; 30194 MW; 18FA010F752CC134 CRC64;
MAAPPASSSA REEFVYLAKL AEQAERYEEM VEFMEKVAEA VDKDELTVEE RNLLSVAYKN
VIGARRASWR IISSIEQKEE SRGNDDHVTT IRDYRSKIES ELSKICDGIL KLLDTRLVPA
SANGDSKVFY LKMKGDYHRY LAEFKTGQER KDAAEHTLTA YKAAQDIANA ELAPTHPIRL
GLALNFSVFY YEILNSPDRA CNLAKQAFDE AIAELDTLGE ESYKDSTLIM QLLRDNLTLW
TSDMQDESPE EIKEAAAPKP AEEQKEI
