FLZ12_ARATH
ID FLZ12_ARATH Reviewed; 228 AA.
AC F4IE21; A0A1P8AT80; Q9LMA6;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2018, sequence version 2.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=FCS-Like Zinc finger 12 {ECO:0000303|PubMed:24901469};
GN Name=FLZ12 {ECO:0000303|PubMed:24901469};
GN Synonyms=DUF581-1 {ECO:0000303|PubMed:24600465};
GN OrderedLocusNames=At1g19200 {ECO:0000312|Araport:AT1G19200};
GN ORFNames=T29M8.7 {ECO:0000312|EMBL:AAF82231.1};
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 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 [4]
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 [5]
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 [6]
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 [7]
RP INTERACTION WITH KIN10; KIN11; KINB1 AND KINB2, 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 and
CC KINB2 via its N-terminal part (PubMed:29945970). Forms homodimer and
CC heterodimer with FLZ2 and FLZ10 in vitro (PubMed:29945970).
CC {ECO:0000269|PubMed:24600465, ECO:0000269|PubMed:29945970}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=F4IE21-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4IE21-2; Sequence=VSP_059891;
CC -!- INDUCTION: Down-regulated by glucose and sucrose but up-regulated by
CC mannose. {ECO:0000269|PubMed:26442059}.
CC -!- SIMILARITY: Belongs to the FLZ family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF82231.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC069143; AAF82231.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002684; ANM59837.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29817.1; -; Genomic_DNA.
DR PIR; E86325; E86325.
DR RefSeq; NP_001322166.1; NM_001332387.1. [F4IE21-1]
DR RefSeq; NP_173354.1; NM_101778.2. [F4IE21-2]
DR AlphaFoldDB; F4IE21; -.
DR STRING; 3702.AT1G19200.1; -.
DR PaxDb; F4IE21; -.
DR PRIDE; F4IE21; -.
DR ProteomicsDB; 228937; -. [F4IE21-1]
DR DNASU; 838503; -.
DR EnsemblPlants; AT1G19200.1; AT1G19200.1; AT1G19200. [F4IE21-2]
DR EnsemblPlants; AT1G19200.2; AT1G19200.2; AT1G19200. [F4IE21-1]
DR GeneID; 838503; -.
DR Gramene; AT1G19200.1; AT1G19200.1; AT1G19200. [F4IE21-2]
DR Gramene; AT1G19200.2; AT1G19200.2; AT1G19200. [F4IE21-1]
DR KEGG; ath:AT1G19200; -.
DR Araport; AT1G19200; -.
DR TAIR; locus:2202195; AT1G19200.
DR HOGENOM; CLU_103134_0_0_1; -.
DR InParanoid; F4IE21; -.
DR OMA; CPRRNQF; -.
DR OrthoDB; 1530874at2759; -.
DR PRO; PR:F4IE21; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4IE21; 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:0071368; P:cellular response to cytokinin stimulus; IEP:TAIR.
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; IPR044604; FLZ12/13/14.
DR InterPro; IPR007650; Zf-FLZ_dom.
DR PANTHER; PTHR47208; PTHR47208; 1.
DR Pfam; PF04570; zf-FLZ; 1.
DR PROSITE; PS51795; ZF_FLZ; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Metal-binding; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..228
FT /note="FCS-Like Zinc finger 12"
FT /id="PRO_0000445502"
FT ZN_FING 162..205
FT /note="FLZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01131"
FT VAR_SEQ 1..13
FT /note="Missing (in isoform 2)"
FT /id="VSP_059891"
SQ SEQUENCE 228 AA; 25380 MW; 7D8B8729442F528E CRC64;
MLSSNPMTWK LSHMVVPGKN STISPDYFTA SQTSPLDMMK FPSPGSSKRY DNGGGIGLGI
VAALEKSSIG INPVCHTGAG SKGFDLARYS KRFQFAAGID LSDSEEYTCV TTRDGLTKVY
YKEEEFEFGH NLLNGDQRWR KPIEIAEESP AKERRVLRDC PDFLTSCCLC KKKLQGKDIY
MYKGDEGFCS KECRSLKIME DSLKEQHKLT SVEVLTGEEI ASPGIFLI
