IDD8_ARATH
ID IDD8_ARATH Reviewed; 466 AA.
AC Q9FFH3;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Zinc finger protein NUTCRACKER {ECO:0000303|PubMed:25829440};
DE AltName: Full=Protein indeterminate-domain 8 {ECO:0000303|PubMed:16784536};
GN Name=NUC {ECO:0000303|PubMed:25829440};
GN Synonyms=IDD8 {ECO:0000303|PubMed:16784536}; OrderedLocusNames=At5g44160;
GN ORFNames=MLN1.8;
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=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
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 GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16784536; DOI=10.1186/1471-2164-7-158;
RA Colasanti J., Tremblay R., Wong A.Y., Coneva V., Kozaki A., Mable B.K.;
RT "The maize INDETERMINATE1 flowering time regulator defines a highly
RT conserved zinc finger protein family in higher plants.";
RL BMC Genomics 7:158-158(2006).
RN [5]
RP INDUCTION BY SHR.
RX PubMed=16640459; DOI=10.1371/journal.pbio.0040143;
RA Levesque M.P., Vernoux T., Busch W., Cui H., Wang J.Y., Blilou I.,
RA Hassan H., Nakajima K., Matsumoto N., Lohmann J.U., Scheres B.,
RA Benfey P.N.;
RT "Whole-genome analysis of the SHORT-ROOT developmental pathway in
RT Arabidopsis.";
RL PLoS Biol. 4:739-752(2006).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE,
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=21265895; DOI=10.1111/j.1365-313x.2010.04432.x;
RA Seo P.J., Ryu J., Kang S.K., Park C.M.;
RT "Modulation of sugar metabolism by an INDETERMINATE DOMAIN transcription
RT factor contributes to photoperiodic flowering in Arabidopsis.";
RL Plant J. 65:418-429(2011).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, PHOSPHORYLATION AT THR-98; SER-178 AND
RP SER-182, INTERACTION WITH KIN10, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP THR-98; SER-178 AND SER-182.
RC STRAIN=cv. Columbia;
RX PubMed=25929516; DOI=10.1186/s12870-015-0503-8;
RA Jeong E.-Y., Seo P.J., Woo J.C., Park C.-M.;
RT "AKIN10 delays flowering by inactivating IDD8 transcription factor through
RT protein phosphorylation in Arabidopsis.";
RL BMC Plant Biol. 15:110-110(2015).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=25829440; DOI=10.1105/tpc.114.132407;
RA Long Y., Smet W., Cruz-Ramirez A., Castelijns B., de Jonge W.,
RA Maehoenen A.P., Bouchet B.P., Perez G.S., Akhmanova A., Scheres B.,
RA Blilou I.;
RT "Arabidopsis BIRD zinc finger proteins jointly stabilize tissue boundaries
RT by confining the cell fate regulator SHORT-ROOT and contributing to fate
RT specification.";
RL Plant Cell 27:1185-1199(2015).
CC -!- FUNCTION: Transcription activator that binds to the DNA sequence 5'-
CC CTTTTGTCC-3' (PubMed:21265895, PubMed:25929516). Regulates
CC photoperiodic flowering by modulating sugar transport and metabolism
CC (PubMed:21265895, PubMed:25929516). Regulates SUS1 and SUS4
CC (PubMed:21265895). Transcription factor that regulates tissue
CC boundaries and asymmetric cell division (PubMed:25829440). Contributes
CC to the sequestration of 'SHORT-ROOT' to the nucleus (PubMed:25829440).
CC {ECO:0000269|PubMed:21265895, ECO:0000269|PubMed:25829440,
CC ECO:0000269|PubMed:25929516}.
CC -!- SUBUNIT: Interacts with AKIN10. {ECO:0000269|PubMed:25929516}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768,
CC ECO:0000269|PubMed:21265895, ECO:0000269|PubMed:25929516}.
CC -!- TISSUE SPECIFICITY: Highly expressed in vegetative organs and at lower
CC levels in flowers and siliques. Expressed predominantly in roots. In
CC roots, present in cortex, endodermis, and pericycle layer
CC (PubMed:25829440). {ECO:0000269|PubMed:21265895,
CC ECO:0000269|PubMed:25829440, ECO:0000305|PubMed:21265895}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development.
CC {ECO:0000269|PubMed:21265895}.
CC -!- INDUCTION: Up-regulated by 'SHORT-ROOT' (SHR)(PubMed:16640459).
CC Strongly down-regulated by sugar deprivation, but not regulated by day-
CC length. {ECO:0000269|PubMed:16640459}.
CC -!- PTM: Inhibition of transcription factor activity by KIN10-mediated
CC phosphorylation at Thr-98, Ser-178 and Ser-182 under sugar deprivation
CC conditions, thus delaying flowering. {ECO:0000269|PubMed:25929516}.
CC -!- DISRUPTION PHENOTYPE: Delayed flowering (PubMed:21265895,
CC PubMed:25929516). Roots of the triple mutant jkd mgp nuc contain
CC patches of undivided ground tissue (GT), indicating that cortex and
CC endodermis layers are not fully separated. The quadruple mutant line
CC jkd mgp nuc scr has short root meristems, lacks endodermis and miss
CC Casparian strip (PubMed:25829440). {ECO:0000269|PubMed:21265895,
CC ECO:0000269|PubMed:25829440, ECO:0000269|PubMed:25929516}.
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DR EMBL; AB005239; BAB10983.1; -; Genomic_DNA.
DR EMBL; CP002688; AED95068.1; -; Genomic_DNA.
DR EMBL; AY037202; AAK59787.1; -; mRNA.
DR EMBL; BT002685; AAO11601.1; -; mRNA.
DR RefSeq; NP_199229.1; NM_123783.4.
DR AlphaFoldDB; Q9FFH3; -.
DR BioGRID; 19689; 5.
DR IntAct; Q9FFH3; 3.
DR STRING; 3702.AT5G44160.1; -.
DR iPTMnet; Q9FFH3; -.
DR PaxDb; Q9FFH3; -.
DR PRIDE; Q9FFH3; -.
DR ProteomicsDB; 228789; -.
DR EnsemblPlants; AT5G44160.1; AT5G44160.1; AT5G44160.
DR GeneID; 834439; -.
DR Gramene; AT5G44160.1; AT5G44160.1; AT5G44160.
DR KEGG; ath:AT5G44160; -.
DR Araport; AT5G44160; -.
DR TAIR; locus:2167608; AT5G44160.
DR eggNOG; KOG1721; Eukaryota.
DR HOGENOM; CLU_014578_3_1_1; -.
DR InParanoid; Q9FFH3; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9FFH3; -.
DR PRO; PR:Q9FFH3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FFH3; baseline and differential.
DR Genevisible; Q9FFH3; AT.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; 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:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0008356; P:asymmetric cell division; IMP:TAIR.
DR GO; GO:0010150; P:leaf senescence; IMP:TAIR.
DR GO; GO:0048573; P:photoperiodism, flowering; IMP:TAIR.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0034504; P:protein localization to nucleus; IMP:UniProtKB.
DR GO; GO:0010075; P:regulation of meristem growth; IMP:UniProtKB.
DR GO; GO:0048510; P:regulation of timing of transition from vegetative to reproductive phase; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:TAIR.
DR GO; GO:0048364; P:root development; IGI:TAIR.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..466
FT /note="Zinc finger protein NUTCRACKER"
FT /id="PRO_0000337842"
FT ZN_FING 66..88
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 107..137
FT /note="C2H2-type 2"
FT /evidence="ECO:0000305"
FT ZN_FING 142..165
FT /note="C2H2-type 2; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 169..192
FT /note="CCHC-type 2; atypical"
FT /evidence="ECO:0000305"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..191
FT /note="SHR-binding"
FT /evidence="ECO:0000250|UniProtKB:Q700D2"
FT MOTIF 134..141
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 1..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 144
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q700D2"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q700D2"
FT BINDING 160
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q700D2"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q700D2"
FT BINDING 171
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q700D2"
FT BINDING 173
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q700D2"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q700D2"
FT BINDING 190
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q700D2"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8GYC1"
FT MOD_RES 98
FT /note="Phosphothreonine; by KIN10"
FT /evidence="ECO:0000269|PubMed:25929516"
FT MOD_RES 178
FT /note="Phosphoserine; by KIN10"
FT /evidence="ECO:0000269|PubMed:25929516"
FT MOD_RES 182
FT /note="Phosphoserine; by KIN10"
FT /evidence="ECO:0000269|PubMed:25929516"
FT MUTAGEN 98
FT /note="T->A: Reduction of KIN10-mediated phosphorylation."
FT /evidence="ECO:0000269|PubMed:25929516"
FT MUTAGEN 178
FT /note="S->A: Reduction of KIN10-mediated phosphorylation.
FT Constitutive transcription factor activity."
FT /evidence="ECO:0000269|PubMed:25929516"
FT MUTAGEN 182
FT /note="S->A: Strong reduction of KIN10-mediated
FT phosphorylation. Constitutive transcription factor
FT activity."
FT /evidence="ECO:0000269|PubMed:25929516"
SQ SEQUENCE 466 AA; 51189 MW; 4B8C618EA9CFE666 CRC64;
MTSEVLQTIS SGSGFAQPQS SSTLDHDESL INPPLVKKKR NLPGNPDPEA EVIALSPTTL
MATNRFLCEV CGKGFQRDQN LQLHRRGHNL PWKLKQRTSK EVRKRVYVCP EKTCVHHHSS
RALGDLTGIK KHFCRKHGEK KWTCEKCAKR YAVQSDWKAH SKTCGTREYR CDCGTIFSRR
DSFITHRAFC DALAEETAKI NAVSHLNGLA AAGAPGSVNL NYQYLMGTFI PPLQPFVPQP
QTNPNHHHQH FQPPTSSSLS LWMGQDIAPP QPQPDYDWVF GNAKAASACI DNNNTHDEQI
TQNANASLTT TTTLSAPSLF SSDQPQNANA NSNVNMSATA LLQKAAEIGA TSTTTAATND
PSTFLQSFPL KSTDQTTSYD SGEKFFALFG SNNNIGLMSR SHDHQEIENA RNDVTVASAL
DELQNYPWKR RRVDGGGEVG GGGQTRDFLG VGVQTLCHPS SINGWI
