IDD1_ARATH
ID IDD1_ARATH Reviewed; 500 AA.
AC Q9LVQ7;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Zinc finger protein ENHYDROUS {ECO:0000303|PubMed:21571950};
DE AltName: Full=Protein indeterminate-domain 1 {ECO:0000303|PubMed:16784536};
GN Name=ENY {ECO:0000303|PubMed:21571950};
GN Synonyms=IDD1 {ECO:0000303|PubMed:16784536};
GN OrderedLocusNames=At5g66730 {ECO:0000312|Araport:AT5G66730};
GN ORFNames=MSN2.12 {ECO:0000312|EMBL:BAA97279.1};
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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 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 FUNCTION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, INTERACTION WITH DELLA
RP PROTEINS, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=21571950; DOI=10.1105/tpc.111.085134;
RA Feurtado J.A., Huang D., Wicki-Stordeur L., Hemstock L.E., Potentier M.S.,
RA Tsang E.W., Cutler A.J.;
RT "The Arabidopsis C2H2 zinc finger INDETERMINATE DOMAIN1/ENHYDROUS promotes
RT the transition to germination by regulating light and hormonal signaling
RT during seed maturation.";
RL Plant Cell 23:1772-1794(2011).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH DELLA PROTEINS.
RC STRAIN=cv. Columbia;
RX PubMed=25035403; DOI=10.1105/tpc.114.125690;
RA Fukazawa J., Teramura H., Murakoshi S., Nasuno K., Nishida N., Ito T.,
RA Yoshida M., Kamiya Y., Yamaguchi S., Takahashi Y.;
RT "DELLAs function as coactivators of GAI-ASSOCIATED FACTOR1 in regulation of
RT gibberellin homeostasis and signaling in Arabidopsis.";
RL Plant Cell 26:2920-2938(2014).
CC -!- FUNCTION: Transcription factor promoting the transition to germination
CC by regulating light and hormonal signaling during seed maturation
CC (PubMed:21571950). Acts as a positive regulator of phytochrome and/or
CC gibberellin action (PubMed:21571950, PubMed:25035403).
CC {ECO:0000269|PubMed:21571950, ECO:0000269|PubMed:25035403}.
CC -!- SUBUNIT: Interacts with the DELLA proteins (e.g. GAI/RGA2, RGA, RGL1,
CC RGL2 and RGLG3), acting as coactivators. {ECO:0000269|PubMed:21571950,
CC ECO:0000269|PubMed:25035403}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768,
CC ECO:0000269|PubMed:21571950}.
CC -!- TISSUE SPECIFICITY: At 3 days post anthesis (DPA), expressed in the
CC chalazal endosperm region. By 6 DPA, expressed in the endosperm and
CC embryo. In fully germinated seed, strongest expression in the root tip
CC and not detected in the cotyledons. In 4-days old seedlings, restricted
CC to the vasculature of the cotyledons, the shoot apical meristem region,
CC and the root tip. By 8 days, restricted to newly emerged leaves.
CC {ECO:0000269|PubMed:21571950}.
CC -!- DEVELOPMENTAL STAGE: Strongly up-regulated during seed development.
CC {ECO:0000269|PubMed:21571950}.
CC -!- DISRUPTION PHENOTYPE: Plants lacking both ENY/IDD1 and IDD2/GAF1 have a
CC decreased responsiveness to gibberellic acid (GA).
CC {ECO:0000269|PubMed:25035403}.
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DR EMBL; AB018119; BAA97279.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98257.1; -; Genomic_DNA.
DR EMBL; AY099859; AAM20710.1; -; mRNA.
DR EMBL; BT000310; AAN15629.1; -; mRNA.
DR RefSeq; NP_201474.1; NM_126071.5.
DR AlphaFoldDB; Q9LVQ7; -.
DR IntAct; Q9LVQ7; 29.
DR STRING; 3702.AT5G66730.1; -.
DR iPTMnet; Q9LVQ7; -.
DR PaxDb; Q9LVQ7; -.
DR PRIDE; Q9LVQ7; -.
DR ProteomicsDB; 228782; -.
DR EnsemblPlants; AT5G66730.1; AT5G66730.1; AT5G66730.
DR GeneID; 836806; -.
DR Gramene; AT5G66730.1; AT5G66730.1; AT5G66730.
DR KEGG; ath:AT5G66730; -.
DR Araport; AT5G66730; -.
DR TAIR; locus:2173624; AT5G66730.
DR eggNOG; KOG1721; Eukaryota.
DR HOGENOM; CLU_014578_2_2_1; -.
DR InParanoid; Q9LVQ7; -.
DR OMA; RQQFAPP; -.
DR OrthoDB; 904963at2759; -.
DR PhylomeDB; Q9LVQ7; -.
DR PRO; PR:Q9LVQ7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LVQ7; baseline and differential.
DR Genevisible; Q9LVQ7; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
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:0009740; P:gibberellic acid mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0009937; P:regulation of gibberellic acid mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0010029; P:regulation of seed germination; IMP:TAIR.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:TAIR.
DR GO; GO:0010431; P:seed maturation; IMP:TAIR.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR SMART; SM00355; ZnF_C2H2; 3.
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 DNA-binding; Gibberellin signaling pathway; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..500
FT /note="Zinc finger protein ENHYDROUS"
FT /id="PRO_0000431538"
FT ZN_FING 61..83
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 102..132
FT /note="C2H2-type 2"
FT /evidence="ECO:0000305"
FT ZN_FING 137..160
FT /note="C2H2-type 2; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 164..187
FT /note="CCHC-type 2; atypical"
FT /evidence="ECO:0000305"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..186
FT /note="SHR-binding"
FT /evidence="ECO:0000250|UniProtKB:Q700D2"
FT REGION 196..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 124..131
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 1..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q700D2"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q700D2"
FT BINDING 155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q700D2"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q700D2"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q700D2"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q700D2"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q700D2"
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q700D2"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8GYC1"
SQ SEQUENCE 500 AA; 52626 MW; 3CC0CF7E693B8481 CRC64;
MPVDLDNSST VSGDASVSST GNQNLTPKSV GKKKRNLPGM PDPDAEVIAL SPKTLMATNR
FVCEICNKGF QRDQNLQLHR RGHNLPWKLR QRSTKEVRKK VYVCPVSGCV HHDPSRALGD
LTGIKKHFCR KHGEKKWKCE KCSKKYAVQS DWKAHSKICG TKEYKCDCGT LFSRRDSFIT
HRAFCDALAE ESAKNHTQSK KLYPETVTRK NPEIEQKSPA AVESSPSLPP SSPPSVAIAP
APAISVETES VKIISSSVLP IQNSPESQEN NNHPEVIIEE ASRTIGFNVS SSDLSNDHSN
NNGGYAGLFV SSTASPSLYA SSTASPSLFA PSSSMEPISL CLSTNPSLFG PTIRDPPHFL
TPLPPQPAMS ATALLQKAAQ MGSTGSGGSL LRGLGIVSTT SSSMELSNHD ALSLAPGLGL
GLPCSSGGSG SGLKELMMGN SSVFGPKQTT LDFLGLGRAV GNGGNTGGGL SALLTSIGGG
GGIDLFGSGE FSGKDIGRSS
