SHI_ARATH
ID SHI_ARATH Reviewed; 331 AA.
AC Q9XGX0;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Protein SHORT INTERNODES;
GN Name=SHI; OrderedLocusNames=At5g66350;
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], FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=10368174; DOI=10.2307/3870795;
RA Fridborg I., Kuusk S., Moritz T., Sundberg E.;
RT "The Arabidopsis dwarf mutant shi exhibits reduced gibberellin responses
RT conferred by overexpression of a new putative zinc finger protein.";
RL Plant Cell 11:1019-1032(1999).
RN [2]
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 [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].
RA Fujita M., Mizukado S., Seki M., Shinozaki K., Mitsuda N., Takiguchi Y.,
RA Takagi M.;
RT "ORF cloning and analysis of Arabidopsis transcription factor genes.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=11706176; DOI=10.1104/pp.010388;
RA Fridborg I., Kuusk S., Robertson M., Sundberg E.;
RT "The Arabidopsis protein SHI represses gibberellin responses in Arabidopsis
RT and barley.";
RL Plant Physiol. 127:937-948(2001).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, INTERACTION WITH LRP1,
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16740146; DOI=10.1111/j.1365-313x.2006.02774.x;
RA Kuusk S., Sohlberg J.J., Magnus Eklund D., Sundberg E.;
RT "Functionally redundant SHI family genes regulate Arabidopsis gynoecium
RT development in a dose-dependent manner.";
RL Plant J. 47:99-111(2006).
RN [7]
RP GENE FAMILY.
RX PubMed=21976484; DOI=10.1104/pp.111.182253;
RA Eklund D.M., Cierlik I., Staaldal V., Claes A.R., Vestman D., Chandler J.,
RA Sundberg E.;
RT "Expression of Arabidopsis SHORT INTERNODES/STYLISH family genes in auxin
RT biosynthesis zones of aerial organs is dependent on a GCC box-like
RT regulatory element.";
RL Plant Physiol. 157:2069-2080(2011).
CC -!- FUNCTION: Transcription activator that binds DNA on 5'-ACTCTAC-3' and
CC promotes auxin homeostasis-regulating gene expression (e.g. YUC genes),
CC as well as genes affecting stamen development, cell expansion and
CC timing of flowering. Synergistically with other SHI-related proteins,
CC regulates gynoecium, stamen and leaf development in a dose-dependent
CC manner, controlling apical-basal patterning. Promotes style and stigma
CC formation, and influences vascular development during gynoecium
CC development. May also have a role in the formation and/or maintenance
CC of the shoot apical meristem (SAM). Suppressor of the gibberellin (GA)
CC signal transduction. {ECO:0000269|PubMed:10368174,
CC ECO:0000269|PubMed:11706176, ECO:0000269|PubMed:16740146}.
CC -!- SUBUNIT: Forms a heterodimer with LRP1.
CC -!- INTERACTION:
CC Q9XGX0; O04292: ATHB-9; NbExp=3; IntAct=EBI-15205274, EBI-1536772;
CC Q9XGX0; O80748: B-box domain protein 26; NbExp=3; IntAct=EBI-15205274, EBI-15191535;
CC Q9XGX0; Q9C5X0: IAA34; NbExp=3; IntAct=EBI-15205274, EBI-3946459;
CC Q9XGX0; Q9SI19: SRS4; NbExp=5; IntAct=EBI-15205274, EBI-15193733;
CC Q9XGX0; Q8LPR5: TCP4; NbExp=3; IntAct=EBI-15205274, EBI-15192325;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in young organs such as shoot apices and
CC root tips. Present in roots, stems, flowers, leaves, hydathodes and
CC siliques. {ECO:0000269|PubMed:10368174, ECO:0000269|PubMed:11706176}.
CC -!- DEVELOPMENTAL STAGE: In germinating seeds, first detected at about 48 h
CC after imbibition. In young seedlings grown in continuous light, present
CC in the root/shoot transition zone, in the apex, and in the apical
CC region of the cotyledons. Later observed in lateral root primordia and
CC in emerging lateral roots, particularly in the root tips, as well as in
CC the shoot apex and in the new leaves, especially in the apical and
CC lateral hydathodes. In adult plants, accumulates in lateral root tips,
CC lateral root primordia, and axillary shoot primordia. In flowers,
CC expressed in the style and stigmatic surface of the pistil and in the
CC receptacle (base) of the flower throughout the development of the
CC pistil until anthesis and later in the silique. Fades out after
CC fertilization. {ECO:0000269|PubMed:11706176,
CC ECO:0000269|PubMed:16740146}.
CC -!- DISRUPTION PHENOTYPE: High gibberellin (GA) levels associated with
CC dwarfism, short hypocotyl, narrow leaves, reduced apical dominance, and
CC late flowering, but more flowers. {ECO:0000269|PubMed:10368174,
CC ECO:0000269|PubMed:11706176, ECO:0000269|PubMed:16740146}.
CC -!- SIMILARITY: Belongs to the SHI protein family. {ECO:0000305}.
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DR EMBL; AF152555; AAD34162.1; -; mRNA.
DR EMBL; AB022211; BAB10714.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98202.1; -; Genomic_DNA.
DR EMBL; AB493816; BAH30654.1; -; mRNA.
DR RefSeq; NP_201436.1; NM_126033.2.
DR AlphaFoldDB; Q9XGX0; -.
DR BioGRID; 22009; 16.
DR IntAct; Q9XGX0; 16.
DR STRING; 3702.AT5G66350.1; -.
DR PaxDb; Q9XGX0; -.
DR ProteomicsDB; 234492; -.
DR EnsemblPlants; AT5G66350.1; AT5G66350.1; AT5G66350.
DR GeneID; 836767; -.
DR Gramene; AT5G66350.1; AT5G66350.1; AT5G66350.
DR KEGG; ath:AT5G66350; -.
DR Araport; AT5G66350; -.
DR TAIR; locus:2155021; AT5G66350.
DR eggNOG; ENOG502QQ15; Eukaryota.
DR HOGENOM; CLU_041493_1_0_1; -.
DR InParanoid; Q9XGX0; -.
DR OMA; GLECPTH; -.
DR PhylomeDB; Q9XGX0; -.
DR PRO; PR:Q9XGX0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9XGX0; baseline and differential.
DR Genevisible; Q9XGX0; AT.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:TAIR.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IPI:TAIR.
DR GO; GO:0048653; P:anther development; IGI:TAIR.
DR GO; GO:0009851; P:auxin biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0009740; P:gibberellic acid mediated signaling pathway; TAS:TAIR.
DR GO; GO:0009938; P:negative regulation of gibberellic acid mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0009555; P:pollen development; IGI:TAIR.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0009739; P:response to gibberellin; IMP:TAIR.
DR InterPro; IPR007818; SHI.
DR InterPro; IPR006511; SHI_C.
DR InterPro; IPR006510; Znf_LRP1.
DR PANTHER; PTHR31604; PTHR31604; 1.
DR TIGRFAMs; TIGR01624; LRP1_Cterm; 1.
DR TIGRFAMs; TIGR01623; put_zinc_LRP1; 1.
PE 1: Evidence at protein level;
KW Activator; Auxin biosynthesis; Auxin signaling pathway;
KW Developmental protein; DNA-binding; Gibberellin signaling pathway;
KW Metal-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Zinc.
FT CHAIN 1..331
FT /note="Protein SHORT INTERNODES"
FT /id="PRO_0000424581"
FT DNA_BIND 120..147
FT /note="Zn(2)-C6 fungal-type; degenerate"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 158..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 247..250
FT /note="Required for homo- and heterodimerization"
FT /evidence="ECO:0000250"
FT COMPBIAS 15..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 120
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 331 AA; 35377 MW; F28CD990008EA387 CRC64;
MAGFFSLGHG GGGNTPDNHR TNTNNPSSSG TESWLWCRNP NSNADGGEAG PSYKGTLELW
QHPNNQEIIF QQQQQQQQRL DLYTSAAGLG VGPSNRSLIE TSGGALMMMR SGSGSGGPSC
QDCGNQSKKD CSHMRCRTCC KSRGLDCPTH VKSTWVPAAK RRERQQQLST GQQPQQLGGS
VPKRQRERIP ARSTSMAYTR IPSNNTSGLE VGNFPPEVSS SAVFRCVRVS SVDDEEEEYA
YKTAVSIGGH VFKGVLYDQG PAERSSSGGG SQPLNLITAG PSASSSSPNV SCNNGVVGST
SDHYIDPASL NYPTPINTFM TGTHFFSNSR S
