SRS2_ARATH
ID SRS2_ARATH Reviewed; 322 AA.
AC O65517;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Protein SHI RELATED SEQUENCE 2;
DE AltName: Full=Protein STYLISH 2;
GN Name=SRS2; Synonyms=STY2; OrderedLocusNames=At4g36260; ORFNames=F23E13.150;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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, 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 [4]
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 [5]
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 [6]
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 [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 influence 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}.
CC -!- INTERACTION:
CC O65517; Q9SI19: SRS4; NbExp=5; IntAct=EBI-15192995, EBI-15193733;
CC O65517; O82277: TCP10; NbExp=3; IntAct=EBI-15192995, EBI-3133327;
CC O65517; Q93Z00: TCP14; NbExp=3; IntAct=EBI-15192995, EBI-4424563;
CC O65517; Q8LPR5: TCP4; NbExp=3; IntAct=EBI-15192995, EBI-15192325;
CC O65517; O64647: TCP9; NbExp=3; IntAct=EBI-15192995, EBI-9838721;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, roots, cauline leaves,
CC flowers and siliques. {ECO:0000269|PubMed:12361963}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the apical parts of the developing
CC gynoecium. In carpels, first observed at late development stage in the
CC most apical parts of the open-ended gynoecium. Accumulates in
CC differentiating style and stigmatic tissues. Not expressed in the
CC stigma after fertilization but remains in the style until full silique
CC maturation. Also detected in anthers. In seedlings, present in the
CC shoot apex and in cotyledons, leaf primordia, stipules, hydathodes and
CC in primordia of lateral roots. Detected in developing trichomes and in
CC leaf and pedicel attachment sites. {ECO:0000269|PubMed:12361963}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. The double mutant sty1-1
CC and sty2-1 has a reduction in the amount of stylar and stigmatic
CC tissues and decreased proliferation of stylar xylem, as well as shorter
CC siliques and rosette and cauline leaves with a higher degree of
CC serration. Hypersensitive to 1-N-naphthylphtalamic acid (NPA), but
CC 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}.
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DR EMBL; AL022141; CAA18132.1; -; Genomic_DNA.
DR EMBL; AL161589; CAB80297.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86640.1; -; Genomic_DNA.
DR PIR; T04595; T04595.
DR RefSeq; NP_195349.1; NM_119794.3.
DR AlphaFoldDB; O65517; -.
DR BioGRID; 15065; 17.
DR IntAct; O65517; 18.
DR STRING; 3702.AT4G36260.1; -.
DR PaxDb; O65517; -.
DR PRIDE; O65517; -.
DR ProteomicsDB; 226566; -.
DR EnsemblPlants; AT4G36260.1; AT4G36260.1; AT4G36260.
DR GeneID; 829783; -.
DR Gramene; AT4G36260.1; AT4G36260.1; AT4G36260.
DR KEGG; ath:AT4G36260; -.
DR Araport; AT4G36260; -.
DR TAIR; locus:2122234; AT4G36260.
DR eggNOG; ENOG502SSG7; Eukaryota.
DR HOGENOM; CLU_041493_1_0_1; -.
DR InParanoid; O65517; -.
DR OMA; MGEASFP; -.
DR OrthoDB; 1014431at2759; -.
DR PhylomeDB; O65517; -.
DR PRO; PR:O65517; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O65517; baseline and differential.
DR Genevisible; O65517; 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: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; 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..322
FT /note="Protein SHI RELATED SEQUENCE 2"
FT /id="PRO_0000424574"
FT DNA_BIND 94..121
FT /note="Zn(2)-C6 fungal-type; degenerate"
FT /evidence="ECO:0000250"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 132..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 231..234
FT /note="Required for homo- and heterodimerization"
FT /evidence="ECO:0000250"
FT COMPBIAS 247..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 322 AA; 34144 MW; 37CC1C12892C7279 CRC64;
MAGIFSLGGN NNNNGDEEEE NQQQQKTNWV WYRSNANTNN INPSSSQQVW QIPPEQMLMH
HHSHPQQQSL DLYPGHQIDV SDLATSSRSI TISCRDCGNQ AKKDCTHMRC RTCCKSRGFD
CSTHVRSTWI PVARRRERQQ QLHMSTSGGG GGSGSGGAGG GGSSIPKRHR DPTLPGTSSS
SRLPSHSAGL EMGEASFPGE VSSDALFRCV KMSGVDDGGD GQYAYQTTVN IGGHLFKGIL
YDQGPESSYM SGGSGGSDHQ SSSAGGGGGG HPFNPPVVTD GGGGVSSAMF VDPNSGGYYS
SNMTTSVFMP PGTQFYQNPP RS
