SRS1_ARATH
ID SRS1_ARATH Reviewed; 370 AA.
AC Q9SD40; F4J383;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 11-DEC-2013, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Protein SHI RELATED SEQUENCE 1;
DE AltName: Full=Protein STYLISH 1;
GN Name=SRS1; Synonyms=STY1; OrderedLocusNames=At3g51060; ORFNames=F24M12.100;
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] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [6]
RP FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=12361963; DOI=10.1242/dev.129.20.4707;
RA Kuusk S., Sohlberg J.J., Long J.A., Fridborg I., Sundberg E.;
RT "STY1 and STY2 promote the formation of apical tissues during Arabidopsis
RT gynoecium development.";
RL Development 129:4707-4717(2002).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH LRP1, GENE FAMILY, AND
RP 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 [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16740145; DOI=10.1111/j.1365-313x.2006.02775.x;
RA Sohlberg J.J., Myrenaas M., Kuusk S., Lagercrantz U., Kowalczyk M.,
RA Sandberg G., Sundberg E.;
RT "STY1 regulates auxin homeostasis and affects apical-basal patterning of
RT the Arabidopsis gynoecium.";
RL Plant J. 47:112-123(2006).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=18811619; DOI=10.1111/j.1469-8137.2008.02625.x;
RA Staaldal V., Sohlberg J.J., Eklund D.M., Ljung K., Sundberg E.;
RT "Auxin can act independently of CRC, LUG, SEU, SPT and STY1 in style
RT development but not apical-basal patterning of the Arabidopsis gynoecium.";
RL New Phytol. 180:798-808(2008).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, DIMERIZATION, AND HOMODIMER.
RX PubMed=20154152; DOI=10.1105/tpc.108.064816;
RA Eklund D.M., Staaldal V., Valsecchi I., Cierlik I., Eriksson C.,
RA Hiratsu K., Ohme-Takagi M., Sundstroem J.F., Thelander M., Ezcurra I.,
RA Sundberg E.;
RT "The Arabidopsis thaliana STYLISH1 protein acts as a transcriptional
RT activator regulating auxin biosynthesis.";
RL Plant Cell 22:349-363(2010).
RN [11]
RP INDUCTION BY ESR1 AND ESR2, 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).
RN [12]
RP FUNCTION.
RX PubMed=22318676; DOI=10.1007/s11103-012-9888-z;
RA Staaldal V., Cierlik I., Chen S., Landberg K., Baylis T., Myrenaas M.,
RA Sundstroem J.F., Eklund D.M., Ljung K., Sundberg E.;
RT "The Arabidopsis thaliana transcriptional activator STYLISH1 regulates
RT genes affecting stamen development, cell expansion and timing of
RT flowering.";
RL Plant Mol. Biol. 78:545-559(2012).
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:12361963,
CC ECO:0000269|PubMed:16740145, ECO:0000269|PubMed:16740146,
CC ECO:0000269|PubMed:18811619, ECO:0000269|PubMed:20154152,
CC ECO:0000269|PubMed:22318676}.
CC -!- SUBUNIT: Forms homodimers and heterodimers with LRP1.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20154152}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9SD40-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9SD40-2; Sequence=VSP_053445;
CC -!- TISSUE SPECIFICITY: Expressed in flowers, seeds and seedlings.
CC {ECO:0000269|PubMed:12361963}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the apical parts of the developing
CC gynoecium. Detected throughout the youngest flower primordium. Later
CC relocalizes towards the regions of the presumptive sepal anlagen and
CC remains in sepal primordia until just after their emergence. Also
CC observed on the abaxial side of the young floral meristem. Present in
CC the newly arisen gynoecial primordium. Restricted to the apical parts
CC of the carpels as the open-ended gynoecial cylinder elongates
CC vertically. In the apical regions of the gynoecium, confined to a zone
CC in the interphase between the style and the stigma and fades out later.
CC Within the gynoecium, accumulates in ovule primordia, and, as the
CC ovules developed, restricted to the epidermis of the developing
CC funiculi, to the outer, but not the inner, integuments and to the tip
CC of the nucellus. Also present in the cell layer of the septum that
CC faces the ovary. In the embryo, detected in the cotyledon primordia
CC during late globular to mid heart stage. In addition, transiently
CC expressed in petal and stamen primordia and in the tapetum of the
CC anthers. {ECO:0000269|PubMed:12361963}.
CC -!- INDUCTION: Regulated by ESR1 and ESR2. {ECO:0000269|PubMed:21976484}.
CC -!- DISRUPTION PHENOTYPE: Gynoecia with aberrant style morphology. The
CC double mutant sty1-1 and sty2-1 has a reduction in the amount of stylar
CC and stigmatic tissues and decreased proliferation of stylar xylem, as
CC well as shorter siliques and rosette and cauline leaves with a higher
CC degree of serration. Hypersensitive to 1-N-naphthylphtalamic acid
CC (NPA), but restored by exogenous application of auxin.
CC {ECO:0000269|PubMed:12361963, ECO:0000269|PubMed:16740145,
CC ECO:0000269|PubMed:16740146, ECO:0000269|PubMed:18811619}.
CC -!- SIMILARITY: Belongs to the SHI protein family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BX824145; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AL132980; CAB62628.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78745.1; -; Genomic_DNA.
DR EMBL; BX824145; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BT029509; ABL66765.1; -; mRNA.
DR EMBL; AB493645; BAH30483.1; -; mRNA.
DR PIR; T45737; T45737.
DR RefSeq; NP_190675.4; NM_114966.6. [Q9SD40-1]
DR AlphaFoldDB; Q9SD40; -.
DR BioGRID; 9588; 8.
DR IntAct; Q9SD40; 8.
DR STRING; 3702.AT3G51060.1; -.
DR PaxDb; Q9SD40; -.
DR PRIDE; Q9SD40; -.
DR ProteomicsDB; 226565; -. [Q9SD40-1]
DR EnsemblPlants; AT3G51060.1; AT3G51060.1; AT3G51060. [Q9SD40-1]
DR GeneID; 824270; -.
DR Gramene; AT3G51060.1; AT3G51060.1; AT3G51060. [Q9SD40-1]
DR KEGG; ath:AT3G51060; -.
DR Araport; AT3G51060; -.
DR TAIR; locus:2080818; AT3G51060.
DR eggNOG; ENOG502QQ15; Eukaryota.
DR HOGENOM; CLU_041493_1_0_1; -.
DR OMA; CTRIPTH; -.
DR OrthoDB; 1014431at2759; -.
DR PRO; PR:Q9SD40; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SD40; baseline and differential.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003677; F:DNA binding; IDA:TAIR.
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:0046982; F:protein heterodimerization activity; 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:0009555; P:pollen development; IGI:TAIR.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA: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; Alternative splicing; Auxin biosynthesis;
KW Auxin signaling pathway; Developmental protein; DNA-binding; Metal-binding;
KW Nucleus; Reference proteome; Zinc.
FT CHAIN 1..370
FT /note="Protein SHI RELATED SEQUENCE 1"
FT /id="PRO_0000424573"
FT DNA_BIND 144..171
FT /note="Zn(2)-C6 fungal-type; degenerate"
FT /evidence="ECO:0000250"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 271..274
FT /note="Required for homo- and heterodimerization"
FT BINDING 144
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 144
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="1"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 160
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 160
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 171
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT VAR_SEQ 248..370
FT /note="FRCVRVSSVEDGEEEFAYQTAVSIGGHIFKGILYDLGPGSSGGGGYNVVAAG
FT ESSSGGGGAQQLNLITAGSVTVATASSSTPNLGGIGSSSAAAATYIDPAALYPTPINTF
FT MAGTQFFPNPRS -> LGACV (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4, ECO:0000303|Ref.5"
FT /id="VSP_053445"
SQ SEQUENCE 370 AA; 38352 MW; F759B42BD06F2D30 CRC64;
MAGFFSLDGG GGGGGGGGNN QEDHRSNTNP PPPVSEAWLW YRNPNVNANA NTNVNANAPS
SSNAALGTLE LWQNHNQQEI MFQHQQHQQR LDLYSSAAGL GVGPSNHNQF DISGETSTAG
AGRAAAMMMI RSGGSGGGSG GVSCQDCGNQ AKKDCSHMRC RTCCKSRGFE CSTHVRSTWV
PAAKRRERQQ QLATVQPQTQ LPRGESVPKR HRENLPATSS SLVCTRIPSH SGLEVGNFPA
EVSSSAVFRC VRVSSVEDGE EEFAYQTAVS IGGHIFKGIL YDLGPGSSGG GGYNVVAAGE
SSSGGGGAQQ LNLITAGSVT VATASSSTPN LGGIGSSSAA AATYIDPAAL YPTPINTFMA
GTQFFPNPRS
