FLZ10_ARATH
ID FLZ10_ARATH Reviewed; 344 AA.
AC Q9LYE4;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=FCS-Like Zinc finger 10 {ECO:0000303|PubMed:24901469};
GN Name=FLZ10 {ECO:0000303|PubMed:24901469};
GN Synonyms=DUF581-14 {ECO:0000303|PubMed:24600465};
GN OrderedLocusNames=At5g11460 {ECO:0000312|Araport:AT5G11460};
GN ORFNames=F15N18.50 {ECO:0000312|EMBL:CAB87706.1};
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF Clones.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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 [6]
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 [7]
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 [8]
RP INTERACTION WITH KIN10; KIN11; KINB1; KINB2 AND KINB3, 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).
RN [9]
RP TISSUE SPECIFICITY, INTERACTION WITH KIN10 AND KIN11, SUBCELLULAR LOCATION,
RP INDUCTION, DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=29406622; DOI=10.1111/tpj.13854;
RA Jamsheer K M., Sharma M., Singh D., Mannully C.T., Jindal S., Shukla B.N.,
RA Laxmi A.;
RT "FCS-like zinc finger 6 and 10 repress SnRK1 signalling in Arabidopsis.";
RL Plant J. 94:232-245(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 (PubMed:24600465).
CC Negatively regulates KIN10 leading to a repression of the SnRK1
CC signaling pathway (PubMed:29406622). {ECO:0000269|PubMed:24600465,
CC ECO:0000269|PubMed:29406622}.
CC -!- SUBUNIT: Interacts with KIN10 and KIN11 via its FLZ-type zinc finger
CC domain (PubMed:24600465, PubMed:29945970, PubMed:29406622). Interacts
CC with KINB1, KINB2 and KINB3 via its N-terminal part (PubMed:29945970).
CC Forms homodimer and heterodimer with FLZ2 and FLZ12 in vitro
CC (PubMed:29945970). {ECO:0000269|PubMed:24600465,
CC ECO:0000269|PubMed:29406622, ECO:0000269|PubMed:29945970}.
CC -!- INTERACTION:
CC Q9LYE4; Q17TI5: BRX; NbExp=3; IntAct=EBI-25519036, EBI-4426649;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29406622}. Nucleus
CC {ECO:0000269|PubMed:29406622}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:29406622}. Note=Co-localized with ER marker when
CC associated with KIN11. {ECO:0000269|PubMed:29406622}.
CC -!- TISSUE SPECIFICITY: Early expressed in hypocotyl and cotyledon and
CC preferentially in the stelar region of the shoot and root. Later
CC expressed in root-shoot junction, lateral root, old or senescing leaves
CC and in pistil and pollen of flower buds or open flowers.
CC {ECO:0000269|PubMed:29406622}.
CC -!- INDUCTION: Up-regulated in response to mild as well as prolonged energy
CC depletion (PubMed:26442059, PubMed:29406622). Up-regulated by the
CC glycolysis inhibitor 2DG (PubMed:29406622). Induced by NaCl
CC (PubMed:26442059). Induced by abscissic acid (ABA) (PubMed:29406622).
CC {ECO:0000269|PubMed:26442059, ECO:0000269|PubMed:29406622}.
CC -!- DISRUPTION PHENOTYPE: Reduced biomass and lateral roots and shorter
CC primary roots. {ECO:0000269|PubMed:29406622}.
CC -!- SIMILARITY: Belongs to the FLZ family. {ECO:0000305}.
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DR EMBL; AL163815; CAB87706.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91682.1; -; Genomic_DNA.
DR EMBL; BT014982; AAT70433.1; -; mRNA.
DR EMBL; BT026508; ABH04615.1; -; mRNA.
DR PIR; T48505; T48505.
DR RefSeq; NP_196707.1; NM_121184.3.
DR AlphaFoldDB; Q9LYE4; -.
DR IntAct; Q9LYE4; 1.
DR PaxDb; Q9LYE4; -.
DR PRIDE; Q9LYE4; -.
DR ProteomicsDB; 228914; -.
DR EnsemblPlants; AT5G11460.1; AT5G11460.1; AT5G11460.
DR GeneID; 831017; -.
DR Gramene; AT5G11460.1; AT5G11460.1; AT5G11460.
DR KEGG; ath:AT5G11460; -.
DR Araport; AT5G11460; -.
DR TAIR; locus:2144246; AT5G11460.
DR eggNOG; ENOG502QWBW; Eukaryota.
DR HOGENOM; CLU_052134_0_0_1; -.
DR InParanoid; Q9LYE4; -.
DR OMA; SCSPIRN; -.
DR OrthoDB; 1196052at2759; -.
DR PhylomeDB; Q9LYE4; -.
DR PRO; PR:Q9LYE4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LYE4; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1902074; P:response to salt; IEP:UniProtKB.
DR GO; GO:0042594; P:response to starvation; IEP:UniProtKB.
DR GO; GO:0090351; P:seedling development; IMP:TAIR.
DR InterPro; IPR044585; FLZ10/11.
DR InterPro; IPR007650; Zf-FLZ_dom.
DR PANTHER; PTHR46868; PTHR46868; 1.
DR Pfam; PF04570; zf-FLZ; 1.
DR PROSITE; PS51795; ZF_FLZ; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Endoplasmic reticulum; Metal-binding; Nucleus;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..344
FT /note="FCS-Like Zinc finger 10"
FT /id="PRO_0000445500"
FT ZN_FING 270..314
FT /note="FLZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01131"
FT REGION 309..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 344 AA; 37869 MW; E816CFDFF8B6165E CRC64;
MSQHSNYQMT TASDYYSTKP VLSAIRSHKL ISSVFEGKCP SDYESAWSPT SPLDFRLFST
LGNPFAASSS RSIWRGKQRS WDSGKVGLSI VHSLVDDHHT DSSATIVLPS PDSKNIIFGS
LMRSGQKPHL LSQPFTKALM PKDVIPNAVF EIGHDVIDVL ELRKSGSVDA AYCSGAENFS
VNNNACQVTK QDPGSLNGGT ESDMEISEDY TCVISHGPNP KTTHFYGDQV MESVEREELK
NRCCKNEKES IFAVAPLDLT TPVDVLPPKD FLSFCYGCSK KLGMGEDIYM YSGYKAFCSS
ECRSKEIDLD EEMEDGDEEE AIKSVSSSDK ESKKKSNGVF FTVG
