SRS4_ARATH
ID SRS4_ARATH Reviewed; 222 AA.
AC Q9SI19;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Protein SHI RELATED SEQUENCE 4;
GN Name=SRS4; OrderedLocusNames=At2g18120; ORFNames=F8D23.10;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 FUNCTION, DISRUPTION PHENOTYPE, 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 [4]
RP TISSUE SPECIFICITY, AND 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). {ECO:0000269|PubMed:16740146}.
CC -!- INTERACTION:
CC Q9SI19; O80748: B-box domain protein 26; NbExp=3; IntAct=EBI-15193733, EBI-15191535;
CC Q9SI19; Q94CK9-3: LRP1; NbExp=5; IntAct=EBI-15193733, EBI-15199884;
CC Q9SI19; Q9LXU1: PIM1; NbExp=3; IntAct=EBI-15193733, EBI-15193025;
CC Q9SI19; Q9XGX0: SHI; NbExp=5; IntAct=EBI-15193733, EBI-15205274;
CC Q9SI19; O65517: SRS2; NbExp=5; IntAct=EBI-15193733, EBI-15192995;
CC Q9SI19; Q9M2U4: SRS6; NbExp=4; IntAct=EBI-15193733, EBI-15201394;
CC Q9SI19; Q8LPR5: TCP4; NbExp=3; IntAct=EBI-15193733, EBI-15192325;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in cotyledon tips, leaf primordia,
CC hydathodes, stipules, and lateral root primordia and weakly at the
CC edges of petals and sepals. {ECO:0000269|PubMed:21976484}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:16740146}.
CC -!- SIMILARITY: Belongs to the SHI protein family. {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; AC007212; AAD31354.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06728.1; -; Genomic_DNA.
DR PIR; E84560; E84560.
DR RefSeq; NP_179404.1; NM_127369.3.
DR AlphaFoldDB; Q9SI19; -.
DR BioGRID; 1682; 17.
DR IntAct; Q9SI19; 17.
DR STRING; 3702.AT2G18120.1; -.
DR PaxDb; Q9SI19; -.
DR PRIDE; Q9SI19; -.
DR ProteomicsDB; 226741; -.
DR EnsemblPlants; AT2G18120.1; AT2G18120.1; AT2G18120.
DR GeneID; 816325; -.
DR Gramene; AT2G18120.1; AT2G18120.1; AT2G18120.
DR KEGG; ath:AT2G18120; -.
DR Araport; AT2G18120; -.
DR TAIR; locus:2053134; AT2G18120.
DR eggNOG; ENOG502SSG7; Eukaryota.
DR HOGENOM; CLU_1322507_0_0_1; -.
DR InParanoid; Q9SI19; -.
DR OMA; YPGQINV; -.
DR OrthoDB; 1014431at2759; -.
DR PhylomeDB; Q9SI19; -.
DR PRO; PR:Q9SI19; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SI19; baseline and differential.
DR Genevisible; Q9SI19; 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; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0045893; P:positive regulation of transcription, DNA-templated; IBA:GO_Central.
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; Metal-binding; Nucleus;
KW Reference proteome; Zinc.
FT CHAIN 1..222
FT /note="Protein SHI RELATED SEQUENCE 4"
FT /id="PRO_0000424576"
FT DNA_BIND 72..99
FT /note="Zn(2)-C6 fungal-type; degenerate"
FT /evidence="ECO:0000250"
FT REGION 114..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 191..194
FT /note="Required for homo- and heterodimerization"
FT /evidence="ECO:0000250"
FT COMPBIAS 115..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 222 AA; 24879 MW; 44F61466A36A6ADB CRC64;
MSNFEMAGTG SSRNNEEDNQ QNTNWVWYKH TNNNLSTSHN NQIWQQPSLD LYPGQIDVCD
MTTSSRSLTI SCQECGNQAK KGCTHGRCRT CCKSNGLHCP THVRSTWIPI AKRRERQQQL
QTPTSNPTGG SGRVGKYRDI NQHATLDSSG LEMGETRFPD EVSSDALFRC VRMSGTDDGE
GQYAYQTTVG IAGHLFKGIL YNQGPENKSM RSTQFYENPP RS
