FLZ11_ARATH
ID FLZ11_ARATH Reviewed; 324 AA.
AC Q9SL94;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=FCS-Like Zinc finger 11 {ECO:0000303|PubMed:24901469};
GN Name=FLZ11 {ECO:0000303|PubMed:24901469};
GN Synonyms=DUF581-8 {ECO:0000303|PubMed:24600465};
GN OrderedLocusNames=At2g25690 {ECO:0000312|Araport:AT2G25690};
GN ORFNames=F3N11.14 {ECO:0000312|EMBL:AAD31369.1};
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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;
RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Carninci P., Hayashizaki Y.,
RA Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA Shinozaki K., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GENE FAMILY, AND 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 [6]
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 [7]
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 [8]
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 [9]
RP INTERACTION WITH KIN10 AND KIN11, SUBUNIT, AND SUBCELLULAR LOCATION.
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).
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.
CC {ECO:0000269|PubMed:24600465}.
CC -!- SUBUNIT: Interacts with KIN10 and KIN11 via its FLZ-type zinc finger
CC domain (PubMed:29945970). Forms heterodimer with FLZ2 in vitro
CC (PubMed:29945970). {ECO:0000269|PubMed:29945970}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29945970}. Nucleus
CC {ECO:0000269|PubMed:29945970}.
CC -!- INDUCTION: Up-regulated in response to mild as well as prolonged energy
CC depletion (PubMed:26442059). Induced by NaCl (PubMed:26442059).
CC {ECO:0000269|PubMed:26442059}.
CC -!- SIMILARITY: Belongs to the FLZ family. {ECO:0000305}.
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DR EMBL; AC006053; AAD31369.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07736.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07737.1; -; Genomic_DNA.
DR EMBL; BT010878; AAR24656.1; -; mRNA.
DR EMBL; AK175432; BAD43195.1; -; mRNA.
DR PIR; E84651; E84651.
DR RefSeq; NP_001031415.1; NM_001036338.1.
DR RefSeq; NP_180140.1; NM_128128.4.
DR AlphaFoldDB; Q9SL94; -.
DR PaxDb; Q9SL94; -.
DR PRIDE; Q9SL94; -.
DR EnsemblPlants; AT2G25690.1; AT2G25690.1; AT2G25690.
DR EnsemblPlants; AT2G25690.2; AT2G25690.2; AT2G25690.
DR GeneID; 817110; -.
DR Gramene; AT2G25690.1; AT2G25690.1; AT2G25690.
DR Gramene; AT2G25690.2; AT2G25690.2; AT2G25690.
DR KEGG; ath:AT2G25690; -.
DR Araport; AT2G25690; -.
DR TAIR; locus:2050271; AT2G25690.
DR eggNOG; ENOG502QWBW; Eukaryota.
DR HOGENOM; CLU_052134_2_0_1; -.
DR InParanoid; Q9SL94; -.
DR OMA; QKDQHQM; -.
DR OrthoDB; 1196052at2759; -.
DR PhylomeDB; Q9SL94; -.
DR PRO; PR:Q9SL94; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SL94; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1902074; P:response to salt; IEP:UniProtKB.
DR GO; GO:0042594; P:response to starvation; IEP:UniProtKB.
DR InterPro; IPR044585; FLZ10/11.
DR InterPro; IPR007650; Zf-FLZ_dom.
DR PANTHER; PTHR46868; PTHR46868; 1.
DR Pfam; PF04570; zf-FLZ; 1.
DR PROSITE; PS51795; ZF_FLZ; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Metal-binding; Nucleus; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..324
FT /note="FCS-Like Zinc finger 11"
FT /id="PRO_0000445501"
FT ZN_FING 266..309
FT /note="FLZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01131"
SQ SEQUENCE 324 AA; 36092 MW; F6C586C170306CA0 CRC64;
MLKTRAMFPH KDQAMSLSLD PQSDLVVGHT NNRPITNPLA LSLLIGLNNK NKCISDSDFV
RSPKSPLEFR VLSTMADSFF LRSPRSSLTA HLNCCCGPAA KVGLSIVDSL GDDRCLLPDI
VFGPALRIKC SEVMDKHPKL LFPVANKSKK IENERSGVVF EIGDNSSETE PVGLRNRSFS
ANDCLRKTRV LSRSKLGQEG DFPGSGSDNA FSSEDDMEDY TCIIAHGPNP KTTHIYGDRV
LECHKNELKG DEDNKEKFGS VFPSDNFLGI CNFCNKKLGG GDDIYMYREK SFCSEECRSE
EMMIDEEDLE EPCIDMHESL KKLF
