ID IDD3_ARATH Reviewed; 506 AA. AC Q9ZWA6; Q700E8; DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 27-MAR-2024, entry version 164. DE RecName: Full=Zinc finger protein MAGPIE {ECO:0000303|PubMed:17785527}; DE AltName: Full=Protein POLLEN SPECIFIC GENE 3 {ECO:0000305}; DE AltName: Full=Protein indeterminate-domain 3 {ECO:0000303|PubMed:16784536}; DE Short=AtIDD3 {ECO:0000303|PubMed:24821766}; GN Name=MGP {ECO:0000303|PubMed:17785527}; GN Synonyms=IDD3 {ECO:0000303|PubMed:16784536}, PSG3 {ECO:0000305}; GN OrderedLocusNames=At1g03840 {ECO:0000312|Araport:AT1G03840}; GN ORFNames=F11M21.23 {ECO:0000312|EMBL:AAD10684.1}; 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 [MRNA] (ISOFORM 2). RX PubMed=15208423; DOI=10.1104/pp.104.042176; RA Gong W., Shen Y.-P., Ma L.-G., Pan Y., Du Y.-L., Wang D.-H., Yang J.-Y., RA Hu L.-D., Liu X.-F., Dong C.-X., Ma L., Chen Y.-H., Yang X.-Y., Gao Y., RA Zhu D., Tan X., Mu J.-Y., Zhang D.-B., Liu Y.-L., Dinesh-Kumar S.P., Li Y., RA Wang X.-P., Gu H.-Y., Qu L.-J., Bai S.-N., Lu Y.-T., Li J.-Y., Zhao J.-D., RA Zuo J., Huang H., Deng X.-W., Zhu Y.-X.; RT "Genome-wide ORFeome cloning and analysis of Arabidopsis transcription RT factor genes."; RL Plant Physiol. 135:773-782(2004). RN [2] 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 [3] 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 [6] 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 [7] 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 [8] RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INTERACTION WITH RP SHR; SCR AND JKD. RX PubMed=17785527; DOI=10.1101/gad.440307; RA Welch D., Hassan H., Blilou I., Immink R., Heidstra R., Scheres B.; RT "Arabidopsis JACKDAW and MAGPIE zinc finger proteins delimit asymmetric RT cell division and stabilize tissue boundaries by restricting SHORT-ROOT RT action."; RL Genes Dev. 21:2196-2204(2007). RN [9] RP DISRUPTION PHENOTYPE. 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 [10] RP INTERACTION WITH SIEL. RX PubMed=21924907; DOI=10.1016/j.cub.2011.08.013; RA Koizumi K., Wu S., MacRae-Crerar A., Gallagher K.L.; RT "An essential protein that interacts with endosomes and promotes movement RT of the SHORT-ROOT transcription factor."; RL Curr. Biol. 21:1559-1564(2011). RN [11] RP FUNCTION, AND INDUCTION. RX PubMed=21935722; DOI=10.1007/s11103-011-9826-5; RA Ogasawara H., Kaimi R., Colasanti J., Kozaki A.; RT "Activity of transcription factor JACKDAW is essential for SHR/SCR- RT dependent activation of SCARECROW and MAGPIE and is modulated by reciprocal RT interactions with MAGPIE, SCARECROW and SHORT ROOT."; RL Plant Mol. Biol. 77:489-499(2011). RN [12] RP FUNCTION, INTERACTION WITH SCL3 AND RGA, AND SUBCELLULAR LOCATION. RX PubMed=24821766; DOI=10.1073/pnas.1321669111; RA Yoshida H., Hirano K., Sato T., Mitsuda N., Nomoto M., Maeo K., Koketsu E., RA Mitani R., Kawamura M., Ishiguro S., Tada Y., Ohme-Takagi M., Matsuoka M., RA Ueguchi-Tanaka M.; RT "DELLA protein functions as a transcriptional activator through the DNA RT binding of the indeterminate domain family proteins."; RL Proc. Natl. Acad. Sci. U.S.A. 111:7861-7866(2014). RN [13] 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 factor that regulates tissue boundaries and CC asymmetric cell division (PubMed:17785527, PubMed:25829440). CC Contributes to the sequestration of 'SHORT-ROOT' to the nucleus CC (PubMed:17785527, PubMed:25829440). Interacts with the SCR and MGP CC promoters (PubMed:21935722). Does not show transcription activity by CC itself, but regulates the transcription of downstream genes through CC interaction with other transcription factors (PubMed:21935722). Binds CC DNA via its zinc fingers (PubMed:24821766). Recognizes and binds to CC SCL3 promoter sequence 5'-AGACAA-3' to promotes its expression when in CC complex with RGA (PubMed:24821766). Positively involved in gibberellic CC acid (GA) signaling (PubMed:24821766). {ECO:0000269|PubMed:17785527, CC ECO:0000269|PubMed:21935722, ECO:0000269|PubMed:24821766, CC ECO:0000269|PubMed:25829440}. CC -!- SUBUNIT: Interacts with SHR, SCR and JKD, but not with itself CC (PubMed:17785527). Interacts with SIEL (PubMed:21924907). Binds to RGA CC and SCL3 competitively in the nucleus (PubMed:24821766). CC {ECO:0000269|PubMed:17785527, ECO:0000269|PubMed:21924907, CC ECO:0000269|PubMed:24821766}. CC -!- INTERACTION: CC Q9ZWA6; Q700D2: JKD; NbExp=3; IntAct=EBI-1568600, EBI-1568562; CC Q9ZWA6; Q9SN22: SCL32; NbExp=3; IntAct=EBI-1568600, EBI-15196807; CC Q9ZWA6; Q9M384: SCR; NbExp=3; IntAct=EBI-1568600, EBI-1250484; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, CC ECO:0000269|PubMed:17785527, ECO:0000269|PubMed:24821766}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9ZWA6-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9ZWA6-2; Sequence=VSP_036332; CC -!- TISSUE SPECIFICITY: Expressed in the ground tissue and stele cells of CC embryos and 2-days post-germination roots but not in the quiescent CC center (PubMed:17785527). Detected only in cells that perform CC asymmetric cell divisions (PubMed:17785527). In roots, present in CC cortex, endodermis, and pericycle layer (PubMed:25829440). CC {ECO:0000269|PubMed:17785527, ECO:0000269|PubMed:25829440}. CC -!- INDUCTION: Up-regulated by the transcription factor JKD, and down- CC regulated by SHR, SCR and itself. {ECO:0000269|PubMed:21935722}. CC -!- DISRUPTION PHENOTYPE: No visible phenotype (PubMed:21265895, CC PubMed:25829440). 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}. CC -!- MISCELLANEOUS: MGP expression is SHR- and SCR-dependent. CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice CC site. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY568648; AAS79538.1; -; mRNA. DR EMBL; AJ630476; CAG25849.1; -; mRNA. DR EMBL; AC003027; AAD10684.1; -; Genomic_DNA. DR EMBL; CP002684; AEE27620.1; -; Genomic_DNA. DR EMBL; CP002684; AEE27621.1; -; Genomic_DNA. DR EMBL; BT006209; AAP12858.1; -; mRNA. DR EMBL; AK227837; BAE99815.1; -; mRNA. DR PIR; A86169; A86169. DR RefSeq; NP_001030951.1; NM_001035874.1. [Q9ZWA6-2] DR RefSeq; NP_171880.1; NM_100263.4. [Q9ZWA6-1] DR AlphaFoldDB; Q9ZWA6; -. DR BioGRID; 24631; 6. DR IntAct; Q9ZWA6; 7. DR STRING; 3702.Q9ZWA6; -. DR iPTMnet; Q9ZWA6; -. DR PaxDb; 3702-AT1G03840-1; -. DR ProteomicsDB; 228784; -. [Q9ZWA6-1] DR EnsemblPlants; AT1G03840.1; AT1G03840.1; AT1G03840. [Q9ZWA6-1] DR EnsemblPlants; AT1G03840.2; AT1G03840.2; AT1G03840. [Q9ZWA6-2] DR GeneID; 839396; -. DR Gramene; AT1G03840.1; AT1G03840.1; AT1G03840. [Q9ZWA6-1] DR Gramene; AT1G03840.2; AT1G03840.2; AT1G03840. [Q9ZWA6-2] DR KEGG; ath:AT1G03840; -. DR Araport; AT1G03840; -. DR TAIR; AT1G03840; MGP. DR eggNOG; KOG1721; Eukaryota. DR HOGENOM; CLU_014578_3_1_1; -. DR InParanoid; Q9ZWA6; -. DR OMA; APQEDYN; -. DR OrthoDB; 5363046at2759; -. DR PhylomeDB; Q9ZWA6; -. DR PRO; PR:Q9ZWA6; -. DR Proteomes; UP000006548; Chromosome 1. DR ExpressionAtlas; Q9ZWA6; baseline and differential. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB. 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:0009740; P:gibberellic acid mediated signaling pathway; IEA:UniProtKB-KW. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0009939; P:positive regulation of gibberellic acid mediated signaling pathway; IMP:UniProtKB. DR GO; GO:0034504; P:protein localization to nucleus; IMP:UniProtKB. DR GO; GO:0006355; P:regulation of DNA-templated transcription; TAS:TAIR. DR GO; GO:0010075; P:regulation of meristem growth; IMP:UniProtKB. DR GO; GO:0048364; P:root development; IGI:TAIR. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 2. DR InterPro; IPR031140; IDD1-16. DR InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR PANTHER; PTHR10593:SF236; PROTEIN INDETERMINATE-DOMAIN 13-RELATED; 1. DR PANTHER; PTHR10593; SERINE/THREONINE-PROTEIN KINASE RIO; 1. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1. DR Genevisible; Q9ZWA6; AT. PE 1: Evidence at protein level; KW Activator; Alternative splicing; DNA-binding; KW Gibberellin signaling pathway; Metal-binding; Nucleus; Phosphoprotein; KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc; KW Zinc-finger. FT CHAIN 1..506 FT /note="Zinc finger protein MAGPIE" FT /id="PRO_0000337841" FT ZN_FING 70..92 FT /note="C2H2-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 111..141 FT /note="C2H2-type 2" FT /evidence="ECO:0000305" FT ZN_FING 146..169 FT /note="C2H2-type 2; degenerate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 173..196 FT /note="CCHC-type 2; atypical" FT /evidence="ECO:0000305" FT REGION 1..53 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 183..195 FT /note="SHR-binding" FT /evidence="ECO:0000250|UniProtKB:Q700D2" FT MOTIF 133..140 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768" FT COMPBIAS 1..20 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 21..39 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 148 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:Q700D2" FT BINDING 151 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 168 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:Q700D2" FT BINDING 175 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:Q700D2" FT BINDING 177 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 BINDING 194 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:Q700D2" FT MOD_RES 60 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8GYC1" FT VAR_SEQ 50..51 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15208423" FT /id="VSP_036332" SQ SEQUENCE 506 AA; 55826 MW; C27006B44C77D1C7 CRC64; MTTEDQTISS SGGYVQSSST TDHVDHHHHD QHESLNPPLV KKKRNLPGNP DPEAEVIALS PKTLMATNRF LCEICGKGFQ RDQNLQLHRR GHNLPWKLKQ RTSKEVRKRV YVCPEKSCVH HHPTRALGDL TGIKKHFCRK HGEKKWKCEK CAKRYAVQSD WKAHSKTCGT REYRCDCGTI FSRRDSFITH RAFCDALAEE TARLNAASHL KSFAATAGSN LNYHYLMGTL IPSPSLPQPP SFPFGPPQPQ HHHHHQFPIT TNNFDHQDVM KPASTLSLWS GGNINHHQQV TIEDRMAPQP HSPQEDYNWV FGNANNHGEL ITTSDSLITH DNNINIVQSK ENANGATSLS VPSLFSSVDQ ITQDANAASV AVANMSATAL LQKAAQMGAT SSTSPTTTIT TDQSAYLQSF ASKSNQIVED GGSDRFFASF GSNSVELMSN NNNGLHEIGN PRNGVTVVSG MGELQNYPWK RRRVDIGNAG GGGQTRDFLG VGVQTICHSS SINGWI //