SHI1_ORYSJ
ID SHI1_ORYSJ Reviewed; 315 AA.
AC Q652K4; A0A0P0XQ70; A3C0W6; Q0J046;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Protein SHORT INTERNODES 1 {ECO:0000303|PubMed:30914468};
DE Short=OsSHI1 {ECO:0000303|PubMed:30914468};
GN Name=SHI1 {ECO:0000303|PubMed:30914468};
GN OrderedLocusNames=Os09g0531600 {ECO:0000312|EMBL:BAT09102.1},
GN LOC_Os09g36160 {ECO:0000305};
GN ORFNames=OJ1254_E07.16 {ECO:0000312|EMBL:BAD46263.1},
GN OsJ_30107 {ECO:0000312|EMBL:EAZ45455.1},
GN P0515E01.1 {ECO:0000312|EMBL:BAD46016.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RG The rice full-length cDNA consortium;
RT "Oryza sativa full length cDNA.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, HOMODIMERIZATION, INTERACTION WITH SPL14, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=30914468; DOI=10.1105/tpc.19.00023;
RA Duan E., Wang Y., Li X., Lin Q., Zhang T., Wang Y., Zhou C., Zhang H.,
RA Jiang L., Wang J., Lei C., Zhang X., Guo X., Wang H., Wan J.;
RT "OsSHI1 regulates plant architecture through modulating the transcriptional
RT activity of IPA1 in rice.";
RL Plant Cell 31:1026-1042(2019).
CC -!- FUNCTION: Regulates tillering and panicle branching by modulating
CC SPL14/IPA1 transcriptional activity on the downstream TB1 and DEP1
CC target genes (PubMed:30914468). Binds directly to the 5'-T/GCTCTAC-3'
CC DNA motif found in the promoter regions of both TB1 and DEP1
CC (PubMed:30914468). Represses the DNA binding activity of SPL14/IPA1
CC toward the promoters of both TB1 and DEP1 (PubMed:30914468). Exhibits
CC weak transcriptional activation activity in yeast cells
CC (PubMed:30914468). {ECO:0000269|PubMed:30914468}.
CC -!- SUBUNIT: Forms homodimers (via C-terminus) (PubMed:30914468). Interacts
CC with SPL14/IPA1 (via C-terminus) (PubMed:30914468).
CC {ECO:0000269|PubMed:30914468}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:30914468}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in axillary buds and young
CC panicles. {ECO:0000269|PubMed:30914468}.
CC -!- DISRUPTION PHENOTYPE: Significant reduced tiller number, enhanced culm
CC strength, increased panicle branch numbers and reduced grain size.
CC {ECO:0000269|PubMed:30914468}.
CC -!- SIMILARITY: Belongs to the SHI protein family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF25669.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP005314; BAD46016.1; -; Genomic_DNA.
DR EMBL; AP005567; BAD46263.1; -; Genomic_DNA.
DR EMBL; AP008215; BAF25669.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014965; BAT09102.1; -; Genomic_DNA.
DR EMBL; CM000146; EAZ45455.1; -; Genomic_DNA.
DR EMBL; AK241285; BAH00998.1; -; mRNA.
DR RefSeq; XP_015611315.1; XM_015755829.1.
DR AlphaFoldDB; Q652K4; -.
DR STRING; 4530.OS09T0531600-01; -.
DR PaxDb; Q652K4; -.
DR PRIDE; Q652K4; -.
DR EnsemblPlants; Os09t0531600-01; Os09t0531600-01; Os09g0531600.
DR GeneID; 4347669; -.
DR Gramene; Os09t0531600-01; Os09t0531600-01; Os09g0531600.
DR KEGG; osa:4347669; -.
DR eggNOG; ENOG502QQ15; Eukaryota.
DR HOGENOM; CLU_041493_1_0_1; -.
DR InParanoid; Q652K4; -.
DR OMA; AGAPFFH; -.
DR OrthoDB; 1014431at2759; -.
DR Proteomes; UP000000763; Chromosome 9.
DR Proteomes; UP000007752; Chromosome 9.
DR Proteomes; UP000059680; Chromosome 9.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
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:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0048450; P:floral organ structural organization; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
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; DNA-binding; Metal-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Zinc.
FT CHAIN 1..315
FT /note="Protein SHORT INTERNODES 1"
FT /id="PRO_0000453484"
FT DNA_BIND 97..124
FT /note="Zn(2)-C6 fungal-type; degenerate"
FT /evidence="ECO:0000305|PubMed:30914468"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 64..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 227..230
FT /note="Required for homo- and heterodimerization"
FT /evidence="ECO:0000305|PubMed:30914468"
FT COMPBIAS 69..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04386"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04386"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04386"
FT BINDING 108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04386"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04386"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04386"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04386"
FT BINDING 124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04386"
FT CONFLICT 120
FT /note="R -> P (in Ref. 4; EAZ45455)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="A -> D (in Ref. 4; EAZ45455)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 315 AA; 32022 MW; 381842CBE74ACC50 CRC64;
MAGFPLGGGS HSRDNPAPPV PPVHPADAAS FLYATRGGSF QLWQQQEQQP FYASNIIRFA
DDAPPAPSLA GASSSSSSRG MRSSGGGGGG GGGGISCQDC GNQAKKDCTH MRCRTCCKSR
GFACATHVKS TWVPAAKRRE RQQQLAALAA SAAATAGGAG PSRDPTKRPR ARPSATTPTT
SSGDQQMVTV AERFPREVSS EAVFRCVRLG PVDQAEAEVA YQTAVSIGGH VFKGILHDVG
PEALAVAGGG GASEYHFRLT GDGSSPSTAA AGEAGSGGGG NIIVSSAVVM DPYPTPGPYG
AFPAGTPFFH GHPRP
