14337_ARATH
ID 14337_ARATH Reviewed; 265 AA.
AC Q96300;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=14-3-3-like protein GF14 nu;
DE AltName: Full=General regulatory factor 7;
GN Name=GRF7; OrderedLocusNames=At3g02520; ORFNames=F16B3.15;
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=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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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].
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].
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 IDENTIFICATION IN THE SERK1 COMPLEX.
RX PubMed=16473966; DOI=10.1105/tpc.105.039412;
RA Karlova R., Boeren S., Russinova E., Aker J., Vervoort J., de Vries S.C.;
RT "The Arabidopsis SOMATIC EMBRYOGENESIS RECEPTOR-LIKE KINASE1 protein
RT complex includes BRASSINOSTEROID-INSENSITIVE1.";
RL Plant Cell 18:626-638(2006).
RN [8]
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 [9]
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: Component of the SERK1 signaling complex, composed of KAPP,
CC CDC48A, GRF6 or GRF7, SERK1, SERK2, SERK3/BAK1 and BRI1
CC (PubMed:16473966). Interacts with DREB1A and DREB1B in the nucleus
CC (PubMed:28344081). Interacts with CINV1 (PubMed:25256212).
CC {ECO:0000269|PubMed:16473966, ECO:0000269|PubMed:25256212,
CC 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 -!- SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}.
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DR EMBL; U60445; AAB49335.1; -; mRNA.
DR EMBL; AF145299; AAD51782.1; -; Genomic_DNA.
DR EMBL; AC021640; AAF32459.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE73822.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65632.1; -; Genomic_DNA.
DR EMBL; AY065274; AAL38750.1; -; mRNA.
DR EMBL; AY096526; AAM20176.1; -; mRNA.
DR EMBL; AY087723; AAM65260.1; -; mRNA.
DR RefSeq; NP_001327587.1; NM_001337415.1.
DR RefSeq; NP_566174.1; NM_111119.3.
DR AlphaFoldDB; Q96300; -.
DR SMR; Q96300; -.
DR BioGRID; 6393; 56.
DR IntAct; Q96300; 9.
DR STRING; 3702.AT3G02520.1; -.
DR iPTMnet; Q96300; -.
DR PaxDb; Q96300; -.
DR PRIDE; Q96300; -.
DR ProteomicsDB; 244517; -.
DR EnsemblPlants; AT3G02520.1; AT3G02520.1; AT3G02520.
DR EnsemblPlants; AT3G02520.2; AT3G02520.2; AT3G02520.
DR GeneID; 821060; -.
DR Gramene; AT3G02520.1; AT3G02520.1; AT3G02520.
DR Gramene; AT3G02520.2; AT3G02520.2; AT3G02520.
DR KEGG; ath:AT3G02520; -.
DR Araport; AT3G02520; -.
DR TAIR; locus:2076904; AT3G02520.
DR eggNOG; KOG0841; Eukaryota.
DR HOGENOM; CLU_058290_0_0_1; -.
DR OMA; KGCQLAR; -.
DR OrthoDB; 1176818at2759; -.
DR PhylomeDB; Q96300; -.
DR PRO; PR:Q96300; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q96300; baseline and differential.
DR Genevisible; Q96300; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA: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 Cytoplasm; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..265
FT /note="14-3-3-like protein GF14 nu"
FT /id="PRO_0000058669"
FT REGION 242..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48349"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48349"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48349"
FT MOD_RES 211
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P48349"
SQ SEQUENCE 265 AA; 29824 MW; BF76ECB7F76E166A CRC64;
MSSSREENVY LAKLAEQAER YEEMVEFMEK VAKTVDTDEL TVEERNLLSV AYKNVIGARR
ASWRIISSIE QKEESRGNDD HVSIIKDYRG KIETELSKIC DGILNLLDSH LVPTASLAES
KVFYLKMKGD YHRYLAEFKT GAERKEAAES TLVAYKSAQD IALADLAPTH PIRLGLALNF
SVFYYEILNS PDRACSLAKQ AFDEAISELD TLGEESYKDS TLIMQLLRDN LTLWNSDIND
EAGGDEIKEA SKHEPEEGKP AETGQ
