ID   FLZ5_ARATH              Reviewed;         147 AA.
AC   Q8VY80; Q9LM43;
DT   10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=FCS-Like Zinc finger 5 {ECO:0000303|PubMed:24901469};
GN   Name=FLZ5 {ECO:0000303|PubMed:24901469};
GN   Synonyms=DUF581-2 {ECO:0000303|PubMed:24600465};
GN   OrderedLocusNames=At1g22160 {ECO:0000312|Araport:AT1G22160};
GN   ORFNames=F2E2.23 {ECO:0000312|EMBL:AAF86553.1};
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=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=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   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   [5]
RP   GENE FAMILY, INTERACTION WITH KIN10 AND KIN11, SUBCELLULAR LOCATION, AND
RP   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   [6]
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   [7]
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   [8]
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   [9]
RP   INTERACTION WITH GAI AND RGA.
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   [10]
RP   INTERACTION WITH KIN10; KIN11 AND KINB3.
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). Interacts with DELLA proteins GAI
CC       and RGA (Ref.9). {ECO:0000269|PubMed:24600465,
CC       ECO:0000269|PubMed:29945970, ECO:0000269|Ref.9}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24600465}. Cytoplasm
CC       {ECO:0000269|PubMed:24600465}. Note=Shuttles from the cytoplasm to the
CC       nucleus when associated with KIN10. {ECO:0000269|PubMed:24600465}.
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=AAF86553.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC069252; AAF86553.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE30204.1; -; Genomic_DNA.
DR   EMBL; AY072370; AAL62362.1; -; mRNA.
DR   EMBL; AY114615; AAM47934.1; -; mRNA.
DR   EMBL; AY086318; AAM64388.1; -; mRNA.
DR   RefSeq; NP_564160.1; NM_102066.3.
DR   AlphaFoldDB; Q8VY80; -.
DR   IntAct; Q8VY80; 3.
DR   STRING; 3702.AT1G22160.1; -.
DR   iPTMnet; Q8VY80; -.
DR   PaxDb; Q8VY80; -.
DR   PRIDE; Q8VY80; -.
DR   ProteomicsDB; 230108; -.
DR   EnsemblPlants; AT1G22160.1; AT1G22160.1; AT1G22160.
DR   GeneID; 838821; -.
DR   Gramene; AT1G22160.1; AT1G22160.1; AT1G22160.
DR   KEGG; ath:AT1G22160; -.
DR   Araport; AT1G22160; -.
DR   TAIR; locus:2030611; AT1G22160.
DR   eggNOG; ENOG502RZVC; Eukaryota.
DR   HOGENOM; CLU_085535_1_0_1; -.
DR   InParanoid; Q8VY80; -.
DR   OMA; TISPRNH; -.
DR   OrthoDB; 1567352at2759; -.
DR   PhylomeDB; Q8VY80; -.
DR   PRO; PR:Q8VY80; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q8VY80; baseline and differential.
DR   GO; GO:0005829; C:cytosol; 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:0042594; P:response to starvation; 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..147
FT                   /note="FCS-Like Zinc finger 5"
FT                   /id="PRO_0000445496"
FT   ZN_FING         77..121
FT                   /note="FLZ-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01131"
SQ   SEQUENCE   147 AA;  16964 MW;  CEA922C4688BECB0 CRC64;
     MLLGKRQRPP IKRTTSLSEI KFDLNQPSEQ EPSDHQIQLV NVDEHRQVHQ RLLDQRLLAM
     VSPRGTQRRH SSDYSEDFLR SCSLCKRLLV HGRDIYMYRG DRAFCSLECR QQQITVDERK
     EKKKGSVRST IVVATGTTTG ERVSAAV