ID   FLZ17_ARATH             Reviewed;         126 AA.
AC   P0DO11; Q8GWT6;
DT   10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2018, sequence version 1.
DT   25-MAY-2022, entry version 16.
DE   RecName: Full=FCS-Like Zinc finger 17 {ECO:0000303|PubMed:24901469};
GN   Name=FLZ17 {ECO:0000303|PubMed:24901469};
GN   Synonyms=DUF581-3 {ECO:0000303|PubMed:24600465};
GN   OrderedLocusNames=At1g53885 {ECO:0000312|Araport:AT1G53885};
GN   ORFNames=T18A20 {ECO:0000312|EMBL:AC009324};
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=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(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=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
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   INDUCTION BY CYTOKININ.
RX   PubMed=16832061; DOI=10.1073/pnas.0602038103;
RA   Rashotte A.M., Mason M.G., Hutchison C.E., Ferreira F.J., Schaller G.E.,
RA   Kieber J.J.;
RT   "A subset of Arabidopsis AP2 transcription factors mediates cytokinin
RT   responses in concert with a two-component pathway.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:11081-11085(2006).
RN   [6]
RP   GENE FAMILY, SUBCELLULAR LOCATION, 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 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: Nucleus {ECO:0000269|PubMed:24600465,
CC       ECO:0000269|PubMed:29945970}. Cytoplasm {ECO:0000269|PubMed:24600465,
CC       ECO:0000269|PubMed:29945970}. Note=Shuttles from the cytoplasm to the
CC       nucleus when associated with KIN10. {ECO:0000269|PubMed:24600465}.
CC   -!- INDUCTION: Up-regulated in response to prolonged energy depletion
CC       (PubMed:26442059). Down-regulated by glucose, sucrose and mannose
CC       (PubMed:26442059). Induced by NaCl and abscissic acid (ABA)
CC       (PubMed:26442059). Induced by cytokinin (PubMed:26442059).
CC       {ECO:0000269|PubMed:26442059}.
CC   -!- SIMILARITY: Belongs to the FLZ family. {ECO:0000305}.
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DR   EMBL; AC009324; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CP002684; AEE33015.1; -; Genomic_DNA.
DR   EMBL; AK118646; BAC43242.1; -; mRNA.
DR   EMBL; BT004725; AAO42971.1; -; mRNA.
DR   RefSeq; NP_001117487.1; NM_001124015.2.
DR   RefSeq; NP_564644.1; NM_104266.3.
DR   AlphaFoldDB; P0DO11; -.
DR   STRING; 3702.AT1G53885.1; -.
DR   iPTMnet; P0DO11; -.
DR   EnsemblPlants; AT1G53885.1; AT1G53885.1; AT1G53885.
DR   EnsemblPlants; AT1G53903.1; AT1G53903.1; AT1G53903.
DR   GeneID; 6241094; -.
DR   GeneID; 841826; -.
DR   Gramene; AT1G53885.1; AT1G53885.1; AT1G53885.
DR   Gramene; AT1G53903.1; AT1G53903.1; AT1G53903.
DR   KEGG; ath:AT1G53885; -.
DR   KEGG; ath:AT1G53903; -.
DR   Araport; AT1G53885; -.
DR   OMA; ILMDEMR; -.
DR   PRO; PR:P0DO11; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; P0DO11; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009737; P:response to abscisic acid; IEP:UniProtKB.
DR   GO; GO:0034097; P:response to cytokine; IEP:UniProtKB.
DR   GO; GO:0009749; P:response to glucose; IEP:UniProtKB.
DR   GO; GO:1905582; P:response to mannose; IEP:UniProtKB.
DR   GO; GO:1902074; P:response to salt; IEP:UniProtKB.
DR   GO; GO:0042594; P:response to starvation; IEP:UniProtKB.
DR   GO; GO:0009744; P:response to sucrose; IEP:UniProtKB.
DR   InterPro; IPR044181; FLZ17/18.
DR   InterPro; IPR007650; Zf-FLZ_dom.
DR   PANTHER; PTHR47847; PTHR47847; 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..126
FT                   /note="FCS-Like Zinc finger 17"
FT                   /id="PRO_0000445507"
FT   ZN_FING         41..85
FT                   /note="FLZ-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01131"
SQ   SEQUENCE   126 AA;  14761 MW;  8E6A0F2561630421 CRC64;
     MTKISVGLQL VTRDSREKLN NIVIKSSLRL NRSNPNISEL CFLKTCHLCN KQLHQDKDVY
     MYRGDLGFCS RECRESQMLI DDRKELEAST KMMLASYRRC NNGAGKSESR NLFDDLRRRR
     QLFIVP