ID   FLZ3_ARATH              Reviewed;          93 AA.
AC   O80506;
DT   10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=FCS-Like Zinc finger 3 {ECO:0000303|PubMed:24901469};
GN   Name=FLZ3 {ECO:0000303|PubMed:24901469};
GN   Synonyms=DUF581-9 {ECO:0000303|PubMed:24600465};
GN   OrderedLocusNames=At2g44670 {ECO:0000312|Araport:AT2G44670};
GN   ORFNames=F16B22.16 {ECO:0000312|EMBL:AEC10453.1};
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=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(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;
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].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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, SUBCELLULAR LOCATION,
RP   MUTAGENESIS OF CYS-47, 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; TCP3; TCP13 AND CSN5B.
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   [11]
RP   INTERACTION WITH KIN10; KIN11 AND KINB3, 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). {ECO:0000269|PubMed:24600465,
CC       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: Down-regulated in response to mild as well as prolonged
CC       energy depletion. {ECO:0000269|PubMed:26442059}.
CC   -!- SIMILARITY: Belongs to the FLZ family. {ECO:0000305}.
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DR   EMBL; AC003672; AAC27469.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC10453.1; -; Genomic_DNA.
DR   EMBL; AF325088; AAK17156.1; -; mRNA.
DR   EMBL; AY048280; AAK82542.1; -; mRNA.
DR   EMBL; BT001142; AAN64533.1; -; mRNA.
DR   EMBL; AK228057; BAF00018.1; -; mRNA.
DR   EMBL; AY088046; AAM65592.1; -; mRNA.
DR   PIR; T01594; T01594.
DR   RefSeq; NP_566023.1; NM_130031.3.
DR   AlphaFoldDB; O80506; -.
DR   IntAct; O80506; 1.
DR   STRING; 3702.AT2G44670.1; -.
DR   PaxDb; O80506; -.
DR   PRIDE; O80506; -.
DR   ProteomicsDB; 230525; -.
DR   EnsemblPlants; AT2G44670.1; AT2G44670.1; AT2G44670.
DR   GeneID; 819075; -.
DR   Gramene; AT2G44670.1; AT2G44670.1; AT2G44670.
DR   KEGG; ath:AT2G44670; -.
DR   Araport; AT2G44670; -.
DR   TAIR; locus:2042416; AT2G44670.
DR   eggNOG; ENOG502RZD3; Eukaryota.
DR   HOGENOM; CLU_121190_1_1_1; -.
DR   InParanoid; O80506; -.
DR   OMA; DQQIEPH; -.
DR   OrthoDB; 1567308at2759; -.
DR   PhylomeDB; O80506; -.
DR   PRO; PR:O80506; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; O80506; 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:0019900; F:kinase binding; IPI:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042594; P:response to starvation; 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   Cytoplasm; Metal-binding; Nucleus; Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..93
FT                   /note="FCS-Like Zinc finger 3"
FT                   /id="PRO_0000445494"
FT   ZN_FING         15..59
FT                   /note="FLZ-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01131"
FT   REGION          54..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        54..74
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         47
FT                   /note="C->S: Abolishes its ability to interact with KIN10."
FT                   /evidence="ECO:0000269|PubMed:24600465"
SQ   SEQUENCE   93 AA;  10522 MW;  2C740531787EBD82 CRC64;
     MASYYSGFLG CEEPHFLESC SLCRKHLGLN SDIFMYRGDK AFCSNECREE QIESDEAKER
     KWKKSSRSLR KNSSETKESA AGNTVRTGTL VVA