FLZ6_ARATH
ID FLZ6_ARATH Reviewed; 162 AA.
AC Q9SGZ8; Q8L9M2;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 139.
DE RecName: Full=FCS-Like Zinc finger 6 {ECO:0000303|PubMed:24901469};
GN Name=FLZ6 {ECO:0000303|PubMed:24901469};
GN Synonyms=DUF581-6 {ECO:0000303|PubMed:24600465};
GN OrderedLocusNames=At1g78020 {ECO:0000312|Araport:AT1G78020};
GN ORFNames=F28K19.24 {ECO:0000312|EMBL:AAF17687.1};
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 [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 [2]
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 [3]
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 [4]
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
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 [6]
RP GENE FAMILY, INTERACTION WITH KIN10 AND KIN11, SUBCELLULAR LOCATION, AND
RP FUNCTION.
RX PubMed=24600465; DOI=10.3389/fpls.2014.00054;
RA Nietzsche M., Schiessl I., Boernke F.;
RT "The complex becomes more complex: protein-protein interactions of SnRK1
RT with DUF581 family proteins provide a framework for cell- and stimulus
RT type-specific SnRK1 signaling in plants.";
RL Front. Plant Sci. 5:54-54(2014).
RN [7]
RP ERRATUM OF PUBMED:24600465.
RX PubMed=25544057; DOI=10.3389/fpls.2014.00693;
RA Boernke F.;
RT "Corrigendum: The complex becomes more complex: protein-protein
RT interactions of SnRK1 with DUF581 family proteins provide a framework for
RT cell- and stimulus type-specific SnRK1 signaling in plants.";
RL Front. Plant Sci. 5:693-693(2014).
RN [8]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=24901469; DOI=10.1371/journal.pone.0099074;
RA Jamsheer K M., Laxmi A.;
RT "DUF581 is plant specific FCS-like zinc finger involved in protein-protein
RT interaction.";
RL PLoS ONE 9:E99074-E99074(2014).
RN [9]
RP INDUCTION.
RX PubMed=26442059; DOI=10.3389/fpls.2015.00746;
RA Jamsheer K M., Laxmi A.;
RT "Expression of Arabidopsis FCS-Like Zinc finger genes is differentially
RT regulated by sugars, cellular energy level, and abiotic stress.";
RL Front. Plant Sci. 6:746-746(2015).
RN [10]
RP INTERACTION WITH KIN10 AND KIN11.
RX PubMed=29945970; DOI=10.1074/jbc.ra118.002073;
RA Jamsheer K M., Shukla B.N., Jindal S., Gopan N., Mannully C.T., Laxmi A.;
RT "The FCS-like zinc finger scaffold of the kinase SnRK1 is formed by the
RT coordinated actions of the FLZ domain and intrinsically disordered
RT regions.";
RL J. Biol. Chem. 293:13134-13150(2018).
RN [11]
RP TISSUE SPECIFICITY, INTERACTION WITH KIN10 AND KIN11, SUBCELLULAR LOCATION,
RP INDUCTION, DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=29406622; DOI=10.1111/tpj.13854;
RA Jamsheer K M., Sharma M., Singh D., Mannully C.T., Jindal S., Shukla B.N.,
RA Laxmi A.;
RT "FCS-like zinc finger 6 and 10 repress SnRK1 signalling in Arabidopsis.";
RL Plant J. 94:232-245(2018).
CC -!- FUNCTION: May act as an adapter to facilitate the interaction of SnRK1
CC complex with effector proteins, conferring tissue- and stimulus-type
CC specific differences in the SnRK1 regulation pathway (PubMed:24600465).
CC Negatively regulates KIN10 leading to a repression of the SnRK1
CC signaling pathway (PubMed:29406622). {ECO:0000269|PubMed:24600465,
CC ECO:0000269|PubMed:29406622}.
CC -!- SUBUNIT: Interacts with KIN10 and KIN11 via its FLZ-type zinc finger
CC domain. {ECO:0000269|PubMed:24600465, ECO:0000269|PubMed:29406622,
CC ECO:0000269|PubMed:29945970}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24600465,
CC ECO:0000269|PubMed:29406622}. Cytoplasm {ECO:0000269|PubMed:24600465,
CC ECO:0000269|PubMed:29406622}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:29406622}. Note=Shuttles from the cytoplasm to the
CC nucleus when associated with KIN10 (PubMed:24600465). Co-localized with
CC ER marker when associated with KIN11 (PubMed:29406622).
CC {ECO:0000269|PubMed:24600465, ECO:0000269|PubMed:29406622}.
CC -!- TISSUE SPECIFICITY: Early expressed in hypocotyl and cotyledon. Later
CC expressed in old or senescing leaves and in pistil, pollen and filament
CC of open flowers. {ECO:0000269|PubMed:29406622}.
CC -!- INDUCTION: Up-regulated in response to prolonged energy depletion
CC (PubMed:26442059, PubMed:29406622). Up-regulated by the glycolysis
CC inhibitor 2DG (PubMed:26442059). Induced by abscissic acid (ABA)
CC (PubMed:29406622). {ECO:0000269|PubMed:26442059,
CC ECO:0000269|PubMed:29406622}.
CC -!- DISRUPTION PHENOTYPE: Reduced biomass and lateral roots and shorter
CC primary roots. {ECO:0000269|PubMed:29406622}.
CC -!- SIMILARITY: Belongs to the FLZ family. {ECO:0000305}.
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DR EMBL; AC009243; AAF17687.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36058.1; -; Genomic_DNA.
DR EMBL; AY063882; AAL36238.1; -; mRNA.
DR EMBL; AY117331; AAM51406.1; -; mRNA.
DR EMBL; AY088355; AAM65894.1; -; mRNA.
DR PIR; E96809; E96809.
DR RefSeq; NP_565167.1; NM_106451.3.
DR AlphaFoldDB; Q9SGZ8; -.
DR IntAct; Q9SGZ8; 2.
DR iPTMnet; Q9SGZ8; -.
DR PaxDb; Q9SGZ8; -.
DR PRIDE; Q9SGZ8; -.
DR ProteomicsDB; 230014; -.
DR EnsemblPlants; AT1G78020.1; AT1G78020.1; AT1G78020.
DR GeneID; 844137; -.
DR Gramene; AT1G78020.1; AT1G78020.1; AT1G78020.
DR KEGG; ath:AT1G78020; -.
DR Araport; AT1G78020; -.
DR TAIR; locus:2029421; AT1G78020.
DR eggNOG; ENOG502RZVC; Eukaryota.
DR HOGENOM; CLU_085535_1_0_1; -.
DR InParanoid; Q9SGZ8; -.
DR OMA; CSLCERH; -.
DR OrthoDB; 1567352at2759; -.
DR PhylomeDB; Q9SGZ8; -.
DR PRO; PR:Q9SGZ8; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SGZ8; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042594; P:response to starvation; IEP:UniProtKB.
DR GO; GO:0090351; P:seedling development; IMP:TAIR.
DR InterPro; IPR007650; Zf-FLZ_dom.
DR Pfam; PF04570; zf-FLZ; 1.
DR PROSITE; PS51795; ZF_FLZ; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Endoplasmic reticulum; Metal-binding; Nucleus;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..162
FT /note="FCS-Like Zinc finger 6"
FT /id="PRO_0000445497"
FT ZN_FING 88..132
FT /note="FLZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01131"
FT REGION 25..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 87
FT /note="G -> R (in Ref. 4; AAM65894)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 162 AA; 17687 MW; B2EB22EBD9A15083 CRC64;
MLLGKRQRPP INRTTSLSEI KFDLNLPSES EPSNQQKPTV ASPYGSNGQA VTAAVDQNRG
FLDQRLLSMV TPRGNLRRHS GDFSDAGHFL RSCALCERLL VPGRDIYMYR GDKAFCSSEC
RQEQMAQDER KEKGKSAAPA KEPAVTAPAR AKPGKGRAAA AV
