FLZ1_ARATH
ID FLZ1_ARATH Reviewed; 177 AA.
AC Q9FGQ9; A0A178U8H3;
DT 05-DEC-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=FCS-Like Zinc finger 1 {ECO:0000303|PubMed:24901469};
GN Name=FLZ1 {ECO:0000303|PubMed:24901469};
GN Synonyms=DUF581-16 {ECO:0000303|PubMed:24600465};
GN OrderedLocusNames=At5g47060 {ECO:0000312|Araport:AT5G47060};
GN ORFNames=MQD22.20 {ECO:0000312|EMBL:BAB10580.1};
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;
RA Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [5]
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP GENE FAMILY, INTERACTION WITH KIN10 AND KIN11, 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 [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, NOMENCLATURE, INTERACTION WITH DSP3 AND BBX21, AND SUBCELLULAR
RP LOCATION.
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; KIN11; KINB1; KINB2 AND KINB3, AND SUBUNIT.
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:24600465, PubMed:29945970). Interacts with KINB1, KINB2
CC and KINB3 via its N-terminal part (PubMed:29945970). Interacts with
CC DSP3 and BBX21 via its FLZ-type zinc finger domain (PubMed:24901469).
CC Forms heterodimer with FLZ7 and FLZ15 in vitro (PubMed:29945970).
CC {ECO:0000269|PubMed:24600465, ECO:0000269|PubMed:24901469,
CC ECO:0000269|PubMed:29945970}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24901469}. Cytoplasm
CC {ECO:0000269|PubMed:24901469}.
CC -!- INDUCTION: Down-regulated in response to mild as well as prolonged
CC energy depletion (PubMed:26442059). Up-regulated by glucose, sucrose
CC and mannose (PubMed:26442059). {ECO:0000269|PubMed:26442059}.
CC -!- SIMILARITY: Belongs to the FLZ family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK230243; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB025609; BAB10580.1; -; Genomic_DNA.
DR EMBL; AB013394; BAB10580.1; JOINED; Genomic_DNA.
DR EMBL; CP002688; AED95462.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM68253.1; -; Genomic_DNA.
DR EMBL; BX841728; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK230243; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_001330022.1; NM_001344706.1.
DR RefSeq; NP_199517.1; NM_124077.5.
DR AlphaFoldDB; Q9FGQ9; -.
DR STRING; 3702.AT5G47060.1; -.
DR iPTMnet; Q9FGQ9; -.
DR PaxDb; Q9FGQ9; -.
DR PRIDE; Q9FGQ9; -.
DR ProteomicsDB; 230107; -.
DR EnsemblPlants; AT5G47060.1; AT5G47060.1; AT5G47060.
DR EnsemblPlants; AT5G47060.2; AT5G47060.2; AT5G47060.
DR GeneID; 834752; -.
DR Gramene; AT5G47060.1; AT5G47060.1; AT5G47060.
DR Gramene; AT5G47060.2; AT5G47060.2; AT5G47060.
DR KEGG; ath:AT5G47060; -.
DR Araport; AT5G47060; -.
DR TAIR; locus:2171047; AT5G47060.
DR eggNOG; ENOG502RZD3; Eukaryota.
DR HOGENOM; CLU_109662_0_0_1; -.
DR InParanoid; Q9FGQ9; -.
DR OMA; DACHRAN; -.
DR OrthoDB; 1502981at2759; -.
DR PhylomeDB; Q9FGQ9; -.
DR PRO; PR:Q9FGQ9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FGQ9; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
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:0019902; F:phosphatase binding; IPI:UniProtKB.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0009749; P:response to glucose; IEP:UniProtKB.
DR GO; GO:1905582; P:response to mannose; IEP:UniProtKB.
DR GO; GO:0042594; P:response to starvation; IEP:UniProtKB.
DR GO; GO:0009744; P:response to sucrose; IEP:UniProtKB.
DR InterPro; IPR044533; FLZ1/2/3.
DR InterPro; IPR007650; Zf-FLZ_dom.
DR PANTHER; PTHR46057; PTHR46057; 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..177
FT /note="FCS-Like Zinc finger 1"
FT /id="PRO_0000445492"
FT ZN_FING 96..140
FT /note="FLZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01131"
FT REGION 22..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 26
FT /note="M -> I (in Ref. 4; BX841728)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 177 AA; 20382 MW; E4664892C2843277 CRC64;
MELSSRKPYF IEEEEEENLA SSLSEMEAGF SGNNNNSNNH GNPQNGVVSS SRFSYGRLNS
LRNSQSYYYN QYSVSSPRSV VSGRFHDFRF DIQQPHFLDS CFLCKKPLGD NRDIYMYRGD
TPFCSEECRQ EQIERDEAKE KKQNLSHSVK SAMRRKEQSS PTRSRDYAFH NGTVAAA
