SRS7_ARATH
ID SRS7_ARATH Reviewed; 345 AA.
AC Q9FXH7; Q5Q0G2; Q5Q0G3;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Protein SHI RELATED SEQUENCE 7;
GN Name=SRS7; OrderedLocusNames=At1g19790; ORFNames=F6F9.16;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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] (ISOFORMS 1 AND 2).
RC STRAIN=cv. Columbia;
RX PubMed=16244158; DOI=10.1104/pp.105.063479;
RA Xiao Y.-L., Smith S.R., Ishmael N., Redman J.C., Kumar N., Monaghan E.L.,
RA Ayele M., Haas B.J., Wu H.C., Town C.D.;
RT "Analysis of the cDNAs of hypothetical genes on Arabidopsis chromosome 2
RT reveals numerous transcript variants.";
RL Plant Physiol. 139:1323-1337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Underwood B.A., Xiao Y.-L., Moskal W.A. Jr., Monaghan E.L., Wang W.,
RA Redman J.C., Wu H.C., Utterback T., Town C.D.;
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=20706774; DOI=10.1007/s11103-010-9677-5;
RA Kim S.G., Lee S., Kim Y.S., Yun D.J., Woo J.C., Park C.M.;
RT "Activation tagging of an Arabidopsis SHI-RELATED SEQUENCE gene produces
RT abnormal anther dehiscence and floral development.";
RL Plant Mol. Biol. 74:337-351(2010).
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). Regulates anther dehiscence and
CC floral development. {ECO:0000269|PubMed:16740146,
CC ECO:0000269|PubMed:20706774}.
CC -!- INTERACTION:
CC Q9FXH7; Q9C9L2: TCP15; NbExp=3; IntAct=EBI-15194151, EBI-4426144;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20706774}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9FXH7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FXH7-2; Sequence=VSP_053446, VSP_053447;
CC -!- TISSUE SPECIFICITY: Mainly expressed in the filaments of flowers, the
CC shoot apex regions and pollen. Also present in leaves.
CC {ECO:0000269|PubMed:20706774}.
CC -!- DEVELOPMENTAL STAGE: In young plants, detected at a low level only in
CC the root tips and lateral root primordia. In fully open flowers,
CC primarily observed in the filaments and anthers.
CC {ECO:0000269|PubMed:20706774}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:16740146, ECO:0000269|PubMed:20706774}.
CC -!- SIMILARITY: Belongs to the SHI protein family. {ECO:0000305}.
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DR EMBL; AC007797; AAG12552.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29897.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29898.1; -; Genomic_DNA.
DR EMBL; AY800588; AAV68824.1; -; mRNA.
DR EMBL; AY800589; AAV68825.1; -; mRNA.
DR EMBL; AY924676; AAX23751.1; -; mRNA.
DR PIR; A86331; A86331.
DR RefSeq; NP_001031069.1; NM_001035992.4. [Q9FXH7-1]
DR RefSeq; NP_173409.1; NM_101835.3. [Q9FXH7-1]
DR AlphaFoldDB; Q9FXH7; -.
DR BioGRID; 23806; 16.
DR IntAct; Q9FXH7; 14.
DR STRING; 3702.AT1G19790.2; -.
DR PaxDb; Q9FXH7; -.
DR PRIDE; Q9FXH7; -.
DR ProteomicsDB; 226742; -. [Q9FXH7-1]
DR EnsemblPlants; AT1G19790.1; AT1G19790.1; AT1G19790. [Q9FXH7-1]
DR EnsemblPlants; AT1G19790.2; AT1G19790.2; AT1G19790. [Q9FXH7-1]
DR GeneID; 838567; -.
DR Gramene; AT1G19790.1; AT1G19790.1; AT1G19790. [Q9FXH7-1]
DR Gramene; AT1G19790.2; AT1G19790.2; AT1G19790. [Q9FXH7-1]
DR KEGG; ath:AT1G19790; -.
DR Araport; AT1G19790; -.
DR TAIR; locus:2013109; AT1G19790.
DR eggNOG; ENOG502QQ15; Eukaryota.
DR HOGENOM; CLU_041493_1_0_1; -.
DR InParanoid; Q9FXH7; -.
DR OMA; LGGRENN; -.
DR OrthoDB; 1014431at2759; -.
DR PhylomeDB; Q9FXH7; -.
DR PRO; PR:Q9FXH7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FXH7; baseline and differential.
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; 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:0009299; P:mRNA transcription; IDA:UniProtKB.
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; Alternative splicing; Auxin biosynthesis;
KW Auxin signaling pathway; Developmental protein; DNA-binding; Metal-binding;
KW Nucleus; Reference proteome; Zinc.
FT CHAIN 1..345
FT /note="Protein SHI RELATED SEQUENCE 7"
FT /id="PRO_0000424579"
FT DNA_BIND 119..146
FT /note="Zn(2)-C6 fungal-type; degenerate"
FT /evidence="ECO:0000250"
FT REGION 7..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 256..259
FT /note="Required for homo- and heterodimerization"
FT /evidence="ECO:0000250"
FT COMPBIAS 10..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT VAR_SEQ 218..234
FT /note="LETSHLPPEISSPAVFR -> MTMSFQLINIEKKFQQI (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:16244158"
FT /id="VSP_053446"
FT VAR_SEQ 235..345
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16244158"
FT /id="VSP_053447"
SQ SEQUENCE 345 AA; 37928 MW; B783F9408126A696 CRC64;
MAGLFYLGGR DHNKQDHHQE KDHNEDKSNN YLYLYKDEIY NNNKGFEIFP PQYFQQQQQQ
NHAAAPTNLY SFGMVPSGGN INNNRSTNRS LYFNVVSDHE PVRSSTGGFT VTRQGNMNCQ
DCGNQAKKDC PHMRCRTCCK SRGFDCQTHV KSTWVSAAKR RERQAQLAVL PAKRIRDANS
RGGGDDDDDD KEDEKNDSCG GGSALACTRV VNASSSGLET SHLPPEISSP AVFRCMRVSS
IDDEDEEYAY QTAVSIGGHV FKGILYDQGP SSDHHRYSSS LNGETSHQHH LNLMDSTPSA
ATTNAVTAVN TNNGSIDPSS LYTAVATPFN AFVAGGTPFF ASSRC
