14335_ARATH
ID 14335_ARATH Reviewed; 268 AA.
AC P42645;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=14-3-3-like protein GF14 upsilon;
DE AltName: Full=General regulatory factor 5;
GN Name=GRF5; OrderedLocusNames=At5g16050; ORFNames=F1N13_190;
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 73; 182 AND C-TERMINUS.
RA Ferl R.J., Lu G.;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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].
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 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 [8]
RP FUNCTION, INTERACTION WITH EDE1, AND SUBCELLULAR LOCATION.
RX PubMed=21558460; DOI=10.1093/aob/mcr050;
RA Pignocchi C., Doonan J.H.;
RT "Interaction of a 14-3-3 protein with the plant microtubule-associated
RT protein EDE1.";
RL Ann. Bot. 107:1103-1109(2011).
RN [9]
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 [10]
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. May be involved in cell cycle regulation by binding to
CC soluble EDE1 and sequestering it in an inactive form during the early
CC stages of mitosis. {ECO:0000269|PubMed:21558460}.
CC -!- SUBUNIT: Interacts with EDE1 (PubMed:21558460). Interacts with DREB1A
CC and DREB1B in the nucleus (PubMed:28344081). Interacts with CINV1
CC (PubMed:25256212). {ECO:0000269|PubMed:21558460,
CC ECO:0000269|PubMed:25256212, ECO:0000269|PubMed:28344081}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21558460}. Nucleus
CC {ECO:0000269|PubMed:21558460}. Note=Not associated with microtubules
CC (PubMed:21558460). Translocates from the cytosol to the nucleus when
CC phosphorylated (By similarity). {ECO:0000250|UniProtKB:P48349,
CC ECO:0000269|PubMed:21558460}.
CC -!- SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}.
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DR EMBL; L09109; AAB06585.1; -; mRNA.
DR EMBL; AF001415; AAB62225.1; -; Genomic_DNA.
DR EMBL; AL391145; CAC01804.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92241.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69323.1; -; Genomic_DNA.
DR EMBL; AY035170; AAK59674.1; -; mRNA.
DR EMBL; AY059115; AAL15221.1; -; mRNA.
DR PIR; S71173; S71173.
DR PIR; T51388; T51388.
DR RefSeq; NP_001331015.1; NM_001343435.1.
DR RefSeq; NP_568325.1; NM_121610.4.
DR AlphaFoldDB; P42645; -.
DR SMR; P42645; -.
DR BioGRID; 16738; 61.
DR IntAct; P42645; 6.
DR MINT; P42645; -.
DR STRING; 3702.AT5G16050.1; -.
DR iPTMnet; P42645; -.
DR PaxDb; P42645; -.
DR PRIDE; P42645; -.
DR ProteomicsDB; 244541; -.
DR EnsemblPlants; AT5G16050.1; AT5G16050.1; AT5G16050.
DR EnsemblPlants; AT5G16050.2; AT5G16050.2; AT5G16050.
DR GeneID; 831462; -.
DR Gramene; AT5G16050.1; AT5G16050.1; AT5G16050.
DR Gramene; AT5G16050.2; AT5G16050.2; AT5G16050.
DR KEGG; ath:AT5G16050; -.
DR Araport; AT5G16050; -.
DR TAIR; locus:2146147; AT5G16050.
DR eggNOG; KOG0841; Eukaryota.
DR HOGENOM; CLU_058290_0_0_1; -.
DR OMA; NSDHVSI; -.
DR OrthoDB; 1176818at2759; -.
DR PhylomeDB; P42645; -.
DR PRO; PR:P42645; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P42645; baseline and differential.
DR Genevisible; P42645; 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:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; 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..268
FT /note="14-3-3-like protein GF14 upsilon"
FT /id="PRO_0000058667"
FT REGION 243..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48349"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48349"
FT MOD_RES 213
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P48349"
FT MOD_RES 267
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19376835"
SQ SEQUENCE 268 AA; 30182 MW; ECB35B7E53F688FF CRC64;
MSSDSSREEN VYLAKLAEQA ERYEEMVEFM EKVAKTVETE ELTVEERNLL SVAYKNVIGA
RRASWRIISS IEQKEDSRGN SDHVSIIKDY RGKIETELSK ICDGILNLLE AHLIPAASLA
ESKVFYLKMK GDYHRYLAEF KTGAERKEAA ESTLVAYKSA QDIALADLAP THPIRLGLAL
NFSVFYYEIL NSSDRACSLA KQAFDEAISE LDTLGEESYK DSTLIMQLLR DNLTLWTSDL
NDEAGDDIKE APKEVQKVDE QAQPPPSQ
