IDD2_ARATH
ID IDD2_ARATH Reviewed; 452 AA.
AC Q9SCQ6;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Zinc finger protein GAI-ASSOCIATED FACTOR 1 {ECO:0000303|PubMed:25035403};
DE AltName: Full=Protein indeterminate-domain 2 {ECO:0000303|PubMed:16784536};
GN Name=GAF1 {ECO:0000303|PubMed:25035403};
GN Synonyms=IDD2 {ECO:0000303|PubMed:16784536};
GN OrderedLocusNames=At3g50700 {ECO:0000312|Araport:AT3G50700};
GN ORFNames=T3A5.80 {ECO:0000312|EMBL:CAB62439.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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].
RA Kim C.J., Chen H., Cheuk R., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
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 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 [6]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF 367-PRO--LEU-384,
RP INTERACTION WITH TPR1; TPR4 AND DELLA PROTEINS, TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, AND ACTIVITY REGULATION.
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 that acts as a positive regulator of
CC gibberellin (GA) action, homeostasis and signaling. GA converts the
CC GAF1 complex from transcriptional activator to repressor via the
CC degradation of DELLA proteins. {ECO:0000269|PubMed:25035403}.
CC -!- ACTIVITY REGULATION: Transcription activation is repressed by
CC gibberellic acid GA(3) in the presence of TPR4.
CC {ECO:0000269|PubMed:25035403}.
CC -!- SUBUNIT: Interacts with the DELLA proteins (e.g. GAI/RGA2, RGA, RGL1,
CC RGL2 and RGLG3), acting as coactivators and with TPR1 and TPR4, acting
CC as a corepressors, at the promoter of GA20OX2 gene.
CC {ECO:0000269|PubMed:25035403}.
CC -!- INTERACTION:
CC Q9SCQ6; Q9SN22: SCL32; NbExp=4; IntAct=EBI-15200862, EBI-15196807;
CC Q9SCQ6; Q93Z00: TCP14; NbExp=3; IntAct=EBI-15200862, EBI-4424563;
CC Q9SCQ6; Q8LPR5: TCP4; NbExp=3; IntAct=EBI-15200862, EBI-15192325;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768,
CC ECO:0000269|PubMed:25035403}.
CC -!- TISSUE SPECIFICITY: Observed in vegetative tissues. Mainly expressed in
CC hypocotyls, petioles, shoot apices, root tips, and trichomes, and, at
CC low levels, in leaves, stems and flowers.
CC {ECO:0000269|PubMed:25035403}.
CC -!- DISRUPTION PHENOTYPE: Plants lacking both ENY/IDD1 and GAF1/IDD2 have a
CC decreased responsiveness to gibberellic acid (GA).
CC {ECO:0000269|PubMed:25035403}.
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DR EMBL; AL132979; CAB62439.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78699.1; -; Genomic_DNA.
DR EMBL; BT014947; AAT47798.1; -; mRNA.
DR EMBL; BT015836; AAU94399.1; -; mRNA.
DR EMBL; AK226933; BAE99004.1; -; mRNA.
DR PIR; T46147; T46147.
DR RefSeq; NP_190639.1; NM_114930.6.
DR AlphaFoldDB; Q9SCQ6; -.
DR IntAct; Q9SCQ6; 14.
DR STRING; 3702.AT3G50700.1; -.
DR iPTMnet; Q9SCQ6; -.
DR PaxDb; Q9SCQ6; -.
DR PRIDE; Q9SCQ6; -.
DR ProteomicsDB; 228783; -.
DR EnsemblPlants; AT3G50700.1; AT3G50700.1; AT3G50700.
DR GeneID; 824234; -.
DR Gramene; AT3G50700.1; AT3G50700.1; AT3G50700.
DR KEGG; ath:AT3G50700; -.
DR Araport; AT3G50700; -.
DR TAIR; locus:2101739; AT3G50700.
DR eggNOG; KOG1721; Eukaryota.
DR HOGENOM; CLU_014578_2_2_1; -.
DR InParanoid; Q9SCQ6; -.
DR OMA; HTHGKKQ; -.
DR OrthoDB; 904963at2759; -.
DR PhylomeDB; Q9SCQ6; -.
DR PRO; PR:Q9SCQ6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SCQ6; baseline and differential.
DR Genevisible; Q9SCQ6; AT.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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:0010336; P:gibberellic acid homeostasis; IDA:UniProtKB.
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:0006355; P:regulation of transcription, DNA-templated; TAS:TAIR.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 1.
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..452
FT /note="Zinc finger protein GAI-ASSOCIATED FACTOR 1"
FT /id="PRO_0000431539"
FT ZN_FING 63..85
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 104..134
FT /note="C2H2-type 2"
FT /evidence="ECO:0000305"
FT ZN_FING 139..162
FT /note="C2H2-type 2; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 166..189
FT /note="CCHC-type 2; atypical"
FT /evidence="ECO:0000305"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..188
FT /note="SHR-binding"
FT /evidence="ECO:0000250|UniProtKB:Q700D2"
FT REGION 196..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 126..133
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 1..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 141
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q700D2"
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 157
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q700D2"
FT BINDING 161
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
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 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q700D2"
FT BINDING 183
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q700D2"
FT BINDING 187
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q700D2"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8GYC1"
FT MUTAGEN 367..384
FT /note="Missing: Impaired DELLA proteins binding."
FT /evidence="ECO:0000269|PubMed:25035403"
SQ SEQUENCE 452 AA; 47943 MW; 15F4FB9E50A67731 CRC64;
MPVDLDNSST VSGEASVSIS STGNQNPLPN STGKKKRNLP GMPDPESEVI ALSPKTLLAT
NRFVCEICNK GFQRDQNLQL HRRGHNLPWK LRQKSNKEVK KKVYVCPEVS CVHHDPSRAL
GDLTGIKKHF CRKHGEKKWK CDKCSKKYAV QSDWKAHSKI CGTKEYKCDC GTLFSRRDSF
ITHRAFCDAL AEENARSHHS QSKKQNPEIL TRKNPVPNPV PAPVDTESAK IKSSSTLTIK
QSESPKTPPE IVQEAPKPTS LNVVTSNGVF AGLFESSSAS PSIYTTSSSS KSLFASSSSI
EPISLGLSTS HGSSFLGSNR FHAQPAMSAT ALLQKAAQMG AASSGGSLLH GLGIVSSTST
SIDAIVPHGL GLGLPCGGES SSGLKELMMG NSSVFGPKQT TLDFLGLGRA VGNGNGPSNG
LSTLVGGGTG IDMATTFGSG EFSGKDISRR KS
