FLZ7_ARATH
ID FLZ7_ARATH Reviewed; 126 AA.
AC F4JW68; Q52KA1;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=FCS-Like Zinc finger 7 {ECO:0000303|PubMed:24901469};
GN Name=FLZ7 {ECO:0000303|PubMed:24901469};
GN Synonyms=DUF581-13 {ECO:0000303|PubMed:24600465};
GN OrderedLocusNames=At4g39795 {ECO:0000312|Araport:AT4G39795};
GN ORFNames=T19P19 {ECO:0000312|EMBL:AL022605},
GN T5J17 {ECO:0000312|EMBL:AL035708};
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [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 KIN10; KIN11 AND KINB3, 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:24600465, PubMed:29945970). Interacts with KINB3 via its
CC N-terminal part (PubMed:29945970). Forms homodimer and heterodimer with
CC FLZ1, FLZ2 and FLZ15 in vitro (PubMed:29945970).
CC {ECO:0000269|PubMed:24600465, ECO:0000269|PubMed:29945970}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29945970}. Nucleus
CC {ECO:0000269|PubMed:29945970}.
CC -!- INDUCTION: Down-regulated by glucose, sucrose and mannose.
CC {ECO:0000269|PubMed:26442059}.
CC -!- SIMILARITY: Belongs to the FLZ family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAY17404.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAY57309.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL022605; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL035708; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL161595; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL161596; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002687; AEE87120.1; -; Genomic_DNA.
DR EMBL; BT021967; AAY17404.1; ALT_INIT; mRNA.
DR EMBL; BT023470; AAY57309.1; ALT_INIT; mRNA.
DR RefSeq; NP_680776.2; NM_148410.3.
DR AlphaFoldDB; F4JW68; -.
DR PaxDb; F4JW68; -.
DR PRIDE; F4JW68; -.
DR EnsemblPlants; AT4G39795.1; AT4G39795.1; AT4G39795.
DR GeneID; 830138; -.
DR Gramene; AT4G39795.1; AT4G39795.1; AT4G39795.
DR KEGG; ath:AT4G39795; -.
DR Araport; AT4G39795; -.
DR TAIR; locus:504955245; AT4G39795.
DR eggNOG; ENOG502R1MU; Eukaryota.
DR HOGENOM; CLU_085535_1_0_1; -.
DR InParanoid; F4JW68; -.
DR OMA; MEHDEGK; -.
DR OrthoDB; 1567352at2759; -.
DR PRO; PR:F4JW68; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JW68; 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:0009749; P:response to glucose; IEP:UniProtKB.
DR GO; GO:1905582; P:response to mannose; IEP:UniProtKB.
DR GO; GO:0009744; P:response to sucrose; IEP:UniProtKB.
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; Metal-binding; Nucleus; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..126
FT /note="FCS-Like Zinc finger 7"
FT /id="PRO_0000445498"
FT ZN_FING 72..116
FT /note="FLZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01131"
SQ SEQUENCE 126 AA; 14104 MW; 8D3C4ED2780A7CA1 CRC64;
MLLGNRPRPQ MQRTASITRI TIEVDGDQTA GQDSDVSMTV VDGGENYAQR FLSPVNHQRN
ERKYGGRSSP SSFLVNCGFC KRGLAPGRDI YMYKGDAAFC SIECREQQME HDEGKTRNRV
VLSPSK
