ID   14310_ARATH             Reviewed;         254 AA.
AC   P48347; Q9LME5;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 150.
DE   RecName: Full=14-3-3-like protein GF14 epsilon;
DE   AltName: Full=General regulatory factor 10;
GN   Name=GRF10; OrderedLocusNames=At1g22300; ORFNames=T16E15.8;
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   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   [3]
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   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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   [6]
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   [7]
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   [8]
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       (PubMed:28344081). Interacts with CINV1 (PubMed:25256212).
CC       {ECO:0000269|PubMed:25256212, ECO:0000269|PubMed:28344081}.
CC   -!- INTERACTION:
CC       P48347; Q41009: TOC34; Xeno; NbExp=2; IntAct=EBI-1803304, EBI-638506;
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=P48347-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P48347-2; Sequence=VSP_008972;
CC   -!- SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}.
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DR   EMBL; U36446; AAA79699.1; -; mRNA.
DR   EMBL; AF145302; AAD51785.1; -; Genomic_DNA.
DR   EMBL; AC068562; AAF87261.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE30225.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE30226.1; -; Genomic_DNA.
DR   EMBL; AF334382; AAG50088.1; -; mRNA.
DR   EMBL; AY054505; AAK96696.1; -; mRNA.
DR   EMBL; AY058834; AAL24222.1; -; mRNA.
DR   EMBL; AY062838; AAL32916.1; -; mRNA.
DR   EMBL; AY081674; AAM10236.1; -; mRNA.
DR   EMBL; AY087580; AAM65122.1; -; mRNA.
DR   PIR; H86355; H86355.
DR   RefSeq; NP_564167.1; NM_102081.4. [P48347-1]
DR   RefSeq; NP_849698.1; NM_179367.2. [P48347-2]
DR   AlphaFoldDB; P48347; -.
DR   SMR; P48347; -.
DR   BioGRID; 24076; 88.
DR   IntAct; P48347; 4.
DR   MINT; P48347; -.
DR   STRING; 3702.AT1G22300.1; -.
DR   iPTMnet; P48347; -.
DR   PaxDb; P48347; -.
DR   PRIDE; P48347; -.
DR   ProteomicsDB; 244542; -. [P48347-1]
DR   EnsemblPlants; AT1G22300.1; AT1G22300.1; AT1G22300. [P48347-1]
DR   EnsemblPlants; AT1G22300.2; AT1G22300.2; AT1G22300. [P48347-2]
DR   GeneID; 838837; -.
DR   Gramene; AT1G22300.1; AT1G22300.1; AT1G22300. [P48347-1]
DR   Gramene; AT1G22300.2; AT1G22300.2; AT1G22300. [P48347-2]
DR   KEGG; ath:AT1G22300; -.
DR   Araport; AT1G22300; -.
DR   TAIR; locus:2196506; AT1G22300.
DR   eggNOG; KOG0841; Eukaryota.
DR   InParanoid; P48347; -.
DR   OMA; EVEWACC; -.
DR   PhylomeDB; P48347; -.
DR   PRO; PR:P48347; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; P48347; baseline and differential.
DR   Genevisible; P48347; AT.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR   GO; GO:0005634; C:nucleus; HDA:TAIR.
DR   GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; HDA:TAIR.
DR   GO; GO:0009742; P:brassinosteroid mediated signaling pathway; IPI:TAIR.
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   Alternative splicing; Cytoplasm; Nucleus; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..254
FT                   /note="14-3-3-like protein GF14 epsilon"
FT                   /id="PRO_0000058672"
FT   MOD_RES         65
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P48349"
FT   MOD_RES         188
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P48349"
FT   VAR_SEQ         254
FT                   /note="N -> V (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14593172"
FT                   /id="VSP_008972"
SQ   SEQUENCE   254 AA;  28915 MW;  037405C341845C25 CRC64;
     MENEREKQVY LAKLSEQTER YDEMVEAMKK VAQLDVELTV EERNLVSVGY KNVIGARRAS
     WRILSSIEQK EESKGNDENV KRLKNYRKRV EDELAKVCND ILSVIDKHLI PSSNAVESTV
     FFYKMKGDYY RYLAEFSSGA ERKEAADQSL EAYKAAVAAA ENGLAPTHPV RLGLALNFSV
     FYYEILNSPE SACQLAKQAF DDAIAELDSL NEESYKDSTL IMQLLRDNLT LWTSDLNEEG
     DERTKGADEP QDEN