14336_ARATH
ID 14336_ARATH Reviewed; 248 AA.
AC P48349; P42647; Q9LX97;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=14-3-3-like protein GF14 lambda;
DE AltName: Full=14-3-3-like protein AFT1;
DE AltName: Full=14-3-3-like protein RCI2;
DE AltName: Full=General regulatory factor 6;
GN Name=GRF6; Synonyms=AFT1, RCI2; OrderedLocusNames=At5g10450;
GN ORFNames=F12B17_200;
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].
RX PubMed=7520301; DOI=10.1007/bf00029607;
RA Jarillo J.A., Capel J., Leyva A., Martinez Zapater J.M., Salinas J.;
RT "Two related low-temperature-inducible genes of Arabidopsis encode proteins
RT showing high homology to 14-3-3 proteins, a family of putative kinase
RT regulators.";
RL Plant Mol. Biol. 25:693-704(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=7718616; DOI=10.1016/0167-4889(95)00006-e;
RA Zhang H., Wang J., Hwang I., Goodman H.M.;
RT "Isolation and expression of an Arabidopsis 14-3-3-like protein gene.";
RL Biochim. Biophys. Acta 1266:113-116(1995).
RN [3]
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 [4]
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 [5]
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 [6]
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 [7]
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 [8]
RP INTERACTION WITH SERK1, PHOSPHORYLATION, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION IN THE SERK1 COMPLEX.
RX PubMed=15592873; DOI=10.1007/s00425-004-1447-7;
RA Rienties I.M., Vink J., Borst J.W., Russinova E., de Vries S.C.;
RT "The Arabidopsis SERK1 protein interacts with the AAA-ATPase AtCDC48, the
RT 14-3-3 protein GF14lambda and the PP2C phosphatase KAPP.";
RL Planta 221:394-405(2005).
RN [9]
RP FUNCTION, AND 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 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 FUNCTION, INTERACTION WITH ADF1, AND DISRUPTION PHENOTYPE.
RX PubMed=26345162; DOI=10.1007/s11427-015-4897-1;
RA Zhao S., Zhao Y., Guo Y.;
RT "14-3-3 lambda protein interacts with ADF1 to regulate actin cytoskeleton
RT dynamics in Arabidopsis.";
RL Sci. China Life Sci. 58:1142-1150(2015).
RN [12]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF SER-61; SER-70; SER-112;
RP SER-193 AND THR-214, INTERACTION WITH CRPK1; DREB1A AND DREB1B, SUBCELLULAR
RP LOCATION, PHOSPHORYLATION AT SER-70; SER-112; SER-193 AND THR-214 BY CRPK1,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
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 (By similarity). Specific negative regulator of slow-
CC vacuolar (SV) ion channel. Mediates F-actin dynamics possibly through
CC inhibiting ADF1 phosphorylation (PubMed:26345162). Negative regulator
CC of freezing tolerance that modulates cold-responsive C-repeat-binding
CC factors (CBF) DREB1A AND DREB1B proteins stability by facilitating
CC their ubiquitin-mediated degradation when activated by CRPK1-mediated
CC phosophorylation in freezing conditions (PubMed:28344081).
CC {ECO:0000250, ECO:0000269|PubMed:17764516, ECO:0000269|PubMed:26345162,
CC ECO:0000269|PubMed:28344081}.
CC -!- SUBUNIT: Interacts with SERK1 in the cell membrane. Component of the
CC SERK1 signaling complex, composed of KAPP, CDC48A, GRF6 or GRF7, SERK1,
CC SERK2, SERK3/BAK1 and BRI1 (PubMed:15592873). Interacts with TPK1
CC (PubMed:17764516). Interacts with ADF1 (PubMed:26345162). Binds to
CC CRPK1 at the plasma membrane. Interacts with DREB1A and DREB1B in the
CC nucleus when activated by CRPK1-mediated phosophorylation upon freezing
CC (PubMed:28344081). Interacts with CINV1 (PubMed:25256212).
CC {ECO:0000269|PubMed:15592873, ECO:0000269|PubMed:17764516,
CC ECO:0000269|PubMed:25256212, ECO:0000269|PubMed:26345162,
CC ECO:0000269|PubMed:28344081}.
CC -!- INTERACTION:
CC P48349; Q8S307: BZR1; NbExp=5; IntAct=EBI-1633785, EBI-1803261;
CC P48349; O48963: PHOT1; NbExp=6; IntAct=EBI-1633785, EBI-1553849;
CC P48349; Q9C5Z6: RPW8.2; NbExp=4; IntAct=EBI-1633785, EBI-2460628;
CC P48349; Q94AG2: SERK1; NbExp=6; IntAct=EBI-1633785, EBI-1555537;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15592873,
CC ECO:0000269|PubMed:28344081}. Cell membrane
CC {ECO:0000269|PubMed:15592873}. Cytoplasm {ECO:0000269|PubMed:28344081}.
CC Note=Translocates from the cytosol to the nucleus when phosphorylated
CC by CRPK1 in response to cold stress. {ECO:0000269|PubMed:28344081}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P48349-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P48349-2; Sequence=VSP_041594;
CC -!- INDUCTION: By cold.
CC -!- PTM: Transphosphorylated by SERK1.
CC -!- PTM: Phosphorylated by CRPK1 in response to cold.
CC {ECO:0000269|PubMed:28344081}.
CC -!- DISRUPTION PHENOTYPE: Increased length of hypocotyls under dark-grown
CC conditions. Altered actin arrays in hypocotyl cells. Enhanced freezing
CC tolerance associated with enhanced cold induction of cold-responsive C-
CC repeat-binding factor (CBF) target genes in the double mutant lacking
CC both GRF6 and GRF8, probably due to the suppression of ubiquitin-
CC mediated degradation DREB1A and DREB1B degradation by the 26S
CC proteasome pathway (PubMed:28344081). {ECO:0000269|PubMed:26345162,
CC ECO:0000269|PubMed:28344081}.
CC -!- SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}.
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DR EMBL; X74141; CAA52238.1; -; mRNA.
DR EMBL; U02565; AAA74737.1; -; mRNA.
DR EMBL; U68545; AAB08482.1; -; mRNA.
DR EMBL; AF145298; AAD51781.1; -; Genomic_DNA.
DR EMBL; AL353995; CAB89398.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91541.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91544.1; -; Genomic_DNA.
DR EMBL; AY052293; AAK96486.1; -; mRNA.
DR EMBL; AY061918; AAL31245.1; -; mRNA.
DR PIR; S47970; S47970.
DR PIR; S53727; S53727.
DR PIR; T49994; T49994.
DR RefSeq; NP_001190276.1; NM_001203347.1. [P48349-2]
DR RefSeq; NP_568229.1; NM_121083.4. [P48349-1]
DR AlphaFoldDB; P48349; -.
DR SMR; P48349; -.
DR BioGRID; 16187; 39.
DR IntAct; P48349; 13.
DR MINT; P48349; -.
DR STRING; 3702.AT5G10450.4; -.
DR TCDB; 8.A.98.1.8; the 14-3-3 protein (14-3-3) family.
DR iPTMnet; P48349; -.
DR SwissPalm; P48349; -.
DR PaxDb; P48349; -.
DR PRIDE; P48349; -.
DR ProteomicsDB; 245171; -. [P48349-1]
DR EnsemblPlants; AT5G10450.1; AT5G10450.1; AT5G10450. [P48349-1]
DR EnsemblPlants; AT5G10450.4; AT5G10450.4; AT5G10450. [P48349-2]
DR GeneID; 830909; -.
DR Gramene; AT5G10450.1; AT5G10450.1; AT5G10450. [P48349-1]
DR Gramene; AT5G10450.4; AT5G10450.4; AT5G10450. [P48349-2]
DR KEGG; ath:AT5G10450; -.
DR Araport; AT5G10450; -.
DR TAIR; locus:2142489; AT5G10450.
DR eggNOG; KOG0841; Eukaryota.
DR InParanoid; P48349; -.
DR OrthoDB; 1176818at2759; -.
DR PhylomeDB; P48349; -.
DR PRO; PR:P48349; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P48349; baseline and differential.
DR Genevisible; P48349; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0009742; P:brassinosteroid mediated signaling pathway; IPI:TAIR.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IMP:TAIR.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0009409; P:response to cold; IGI:TAIR.
DR GO; GO:0050826; P:response to freezing; 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 Alternative splicing; Cell membrane; Cytoplasm; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome; Stress response.
FT CHAIN 1..248
FT /note="14-3-3-like protein GF14 lambda"
FT /id="PRO_0000058668"
FT MOD_RES 70
FT /note="Phosphoserine; by CRPK1"
FT /evidence="ECO:0000269|PubMed:28344081"
FT MOD_RES 112
FT /note="Phosphoserine; by CRPK1"
FT /evidence="ECO:0000269|PubMed:28344081"
FT MOD_RES 193
FT /note="Phosphoserine; by CRPK1"
FT /evidence="ECO:0000269|PubMed:28344081"
FT MOD_RES 214
FT /note="Phosphothreonine; by CRPK1"
FT /evidence="ECO:0000269|PubMed:28344081"
FT VAR_SEQ 243..248
FT /note="EQMDEA -> TNQMHHIRDIKEHVKTEITAKPCVLSYYYSM (in
FT isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_041594"
FT MUTAGEN 61
FT /note="S->A: Normal phosphorylation."
FT /evidence="ECO:0000269|PubMed:28344081"
FT MUTAGEN 70
FT /note="S->A: Reduced phosphorylation by CRPK1. Impaired
FT phosphorylation and loss of translocation from cytoplasm to
FT the nucleus in response to cold; when associated with A-
FT 112; A-193 and A-214."
FT /evidence="ECO:0000269|PubMed:28344081"
FT MUTAGEN 112
FT /note="S->A: Reduced phosphorylation by CRPK1. Impaired
FT phosphorylation and loss of translocation from cytoplasm to
FT the nucleus in response to cold; when associated with A-70;
FT A-193 and A-214."
FT /evidence="ECO:0000269|PubMed:28344081"
FT MUTAGEN 193
FT /note="S->A: Reduced phosphorylation by CRPK1. Impaired
FT phosphorylation and loss of translocation from cytoplasm to
FT the nucleus in response to cold; when associated with A-70;
FT A-112 and A-214."
FT /evidence="ECO:0000269|PubMed:28344081"
FT MUTAGEN 214
FT /note="T->A: Reduced phosphorylation by CRPK1. Impaired
FT phosphorylation and loss of translocation from cytoplasm to
FT the nucleus in response to cold; when associated with A-70;
FT A-112 and A-193."
FT /evidence="ECO:0000269|PubMed:28344081"
FT CONFLICT 241..248
FT /note="MQEQMDEA -> YAGADGRGLRI (in Ref. 1; CAA52238)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 248 AA; 27976 MW; 4017D23098E74891 CRC64;
MAATLGRDQY VYMAKLAEQA ERYEEMVQFM EQLVTGATPA EELTVEERNL LSVAYKNVIG
SLRAAWRIVS SIEQKEESRK NDEHVSLVKD YRSKVESELS SVCSGILKLL DSHLIPSAGA
SESKVFYLKM KGDYHRYMAE FKSGDERKTA AEDTMLAYKA AQDIAAADMA PTHPIRLGLA
LNFSVFYYEI LNSSDKACNM AKQAFEEAIA ELDTLGEESY KDSTLIMQLL RDNLTLWTSD
MQEQMDEA
