FLZ2_ARATH
ID FLZ2_ARATH Reviewed; 159 AA.
AC Q8VZM9; O23607; Q8L9G6;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=FCS-Like Zinc finger 2 {ECO:0000303|PubMed:24901469};
GN Name=FLZ2 {ECO:0000303|PubMed:24901469};
GN Synonyms=DUF581-12 {ECO:0000303|PubMed:24600465};
GN OrderedLocusNames=At4g17670 {ECO:0000312|Araport:AT4G17670};
GN ORFNames=dl4870c {ECO:0000312|EMBL:AEE83931.1},
GN FCAALL.414 {ECO:0000312|EMBL:AEE83931.1};
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=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [2]
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 [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=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 [5]
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 [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, 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; KIN11; KINB1; KINB2; KINB3 AND SNF4, 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 KINB3 and SNF4 via its N-terminal part (PubMed:29945970). Forms
CC heterodimer with FLZ7, FLZ10, FLZ11, FLZ12, FLZ15, FLZ17 and FLZ18 in
CC vitro (PubMed:29945970). {ECO:0000269|PubMed:24600465,
CC ECO:0000269|PubMed:29945970}.
CC -!- INDUCTION: Down-regulated in response to mild as well as prolonged
CC energy depletion (PubMed:26442059). Down-regulated by the glycolysis
CC inhibitor 2DG (PubMed:26442059). Up-regulated by glucose, sucrose and
CC mannose (PubMed:26442059). {ECO:0000269|PubMed:26442059}.
CC -!- SIMILARITY: Belongs to the FLZ family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB10547.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78770.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; Z97343; CAB10547.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161546; CAB78770.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83931.1; -; Genomic_DNA.
DR EMBL; AY064001; AAL36357.1; -; mRNA.
DR EMBL; AY117186; AAM51261.1; -; mRNA.
DR EMBL; AY088445; AAM65981.1; -; mRNA.
DR PIR; F71446; F71446.
DR RefSeq; NP_567534.1; NM_117875.4.
DR AlphaFoldDB; Q8VZM9; -.
DR STRING; 3702.AT4G17670.1; -.
DR PaxDb; Q8VZM9; -.
DR PRIDE; Q8VZM9; -.
DR ProteomicsDB; 228970; -.
DR EnsemblPlants; AT4G17670.1; AT4G17670.1; AT4G17670.
DR GeneID; 827487; -.
DR Gramene; AT4G17670.1; AT4G17670.1; AT4G17670.
DR KEGG; ath:AT4G17670; -.
DR Araport; AT4G17670; -.
DR TAIR; locus:2129331; AT4G17670.
DR eggNOG; ENOG502RZD3; Eukaryota.
DR HOGENOM; CLU_109662_0_0_1; -.
DR InParanoid; Q8VZM9; -.
DR OMA; PRSGKFH; -.
DR OrthoDB; 1502981at2759; -.
DR PhylomeDB; Q8VZM9; -.
DR PRO; PR:Q8VZM9; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8VZM9; baseline and differential.
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: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 Metal-binding; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..159
FT /note="FCS-Like Zinc finger 2"
FT /id="PRO_0000445493"
FT ZN_FING 75..119
FT /note="FLZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01131"
FT REGION 113..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 148
FT /note="N -> D (in Ref. 5; AAM65981)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 159 AA; 18593 MW; 58ADEFB3F96E564F CRC64;
MEVSMRKPYF IEEEDDGFVS LSEMEAGVSS PSCYNYPQSY YYNHHHHQYS VSSPRSGKFH
DFRFDNSYYG YGQPHFLDSC FLCKKRLGDN RDIFMYRGDT PFCSEECREE QIERDEAKEK
KQSLSTSVKA MRRNEKRSSS SSPTRSRNYA FRTGTVAAA
