FLZ8_ARATH
ID FLZ8_ARATH Reviewed; 267 AA.
AC Q8L471; Q9LJ91;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=FCS-Like Zinc finger 8 {ECO:0000303|PubMed:24901469};
GN Name=FLZ8 {ECO:0000303|PubMed:24901469};
GN Synonyms=DUF581-10 {ECO:0000303|PubMed:24600465};
GN OrderedLocusNames=At3g22550 {ECO:0000312|Araport:AT3G22550};
GN ORFNames=F16J14.11 {ECO:0000312|EMBL:BAB01470.1};
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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 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 [5]
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 [6]
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 [7]
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 [8]
RP INTERACTION WITH HB21.
RX DOI=10.1016/j.cpb.2015.10.004;
RA Nietzsche M., Landgraf R., Tohge T., Boernke F.;
RT "A protein-protein interaction network linking the energy-sensor kinase
RT SnRK1 to multiple signaling pathways in Arabidopsis thaliana.";
RL Curr. Plant Biol. 5:36-44(2016).
RN [9]
RP INTERACTION WITH KIN10; KIN11; KINB1; KINB2; KINB3 AND SNF4.
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). Interacts with KINB1, KINB2, KINB3 and SNF4
CC via its N-terminal part (PubMed:29945970). Interacts with HB21/ZHD3
CC (Ref.8). {ECO:0000269|PubMed:29945970, ECO:0000269|Ref.8}.
CC -!- INDUCTION: Down-regulated in response to mild as well as prolonged
CC energy depletion (PubMed:26442059). Up-regulated by glucose and sucrose
CC (PubMed:26442059). {ECO:0000269|PubMed:26442059}.
CC -!- SIMILARITY: Belongs to the FLZ family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB01470.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AP000731; BAB01470.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002686; AEE76652.1; -; Genomic_DNA.
DR EMBL; AY099714; AAM20565.1; -; mRNA.
DR EMBL; AY128875; AAM91275.1; -; mRNA.
DR RefSeq; NP_188894.2; NM_113154.4.
DR AlphaFoldDB; Q8L471; -.
DR IntAct; Q8L471; 4.
DR STRING; 3702.AT3G22550.1; -.
DR iPTMnet; Q8L471; -.
DR PaxDb; Q8L471; -.
DR PRIDE; Q8L471; -.
DR ProteomicsDB; 230437; -.
DR EnsemblPlants; AT3G22550.1; AT3G22550.1; AT3G22550.
DR GeneID; 821826; -.
DR Gramene; AT3G22550.1; AT3G22550.1; AT3G22550.
DR KEGG; ath:AT3G22550; -.
DR Araport; AT3G22550; -.
DR TAIR; locus:2077031; AT3G22550.
DR eggNOG; ENOG502QS8T; Eukaryota.
DR HOGENOM; CLU_052134_2_1_1; -.
DR InParanoid; Q8L471; -.
DR OMA; GDMLRNR; -.
DR OrthoDB; 1206171at2759; -.
DR PhylomeDB; Q8L471; -.
DR PRO; PR:Q8L471; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8L471; baseline and differential.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0009749; P:response to glucose; IEP:UniProtKB.
DR GO; GO:0042594; P:response to starvation; IEP:UniProtKB.
DR GO; GO:0009744; P:response to sucrose; IEP:UniProtKB.
DR InterPro; IPR044593; FLZ8/MARD1.
DR InterPro; IPR007650; Zf-FLZ_dom.
DR PANTHER; PTHR46443; PTHR46443; 1.
DR Pfam; PF04570; zf-FLZ; 1.
DR PROSITE; PS51795; ZF_FLZ; 1.
PE 1: Evidence at protein level;
KW Metal-binding; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..267
FT /note="FCS-Like Zinc finger 8"
FT /id="PRO_0000445499"
FT ZN_FING 221..265
FT /note="FLZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01131"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 267 AA; 29640 MW; AAB8943EE05557B5 CRC64;
MLKKRSRSKQ ALMAETNQSQ NQKQSKTTPF PRLFTAFSSF KSFTENDAVA SPTSILDTKP
FSVLKNPFGS DNPKTQEPET RLKLEPKRIG LAIVDSLIQD ETPEPGPRSG TILFGSQLRI
RVPDSPISSS DFGIKTRNSQ PETKKPGSES GLGSPRIISG YFPASDMELS EDYTCVTCHG
PNPRTIHIFD NCIVESQPGV VFFRSSDPVN ESDSDYSPPD SFLSCCCNCK KSLGPRDDIF
MYRGDRAFCS SECRSIEMMM SEENDTK
