SRS8_ARATH
ID SRS8_ARATH Reviewed; 173 AA.
AC F4KH89;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Protein SHI RELATED SEQUENCE 8;
GN Name=SRS8; OrderedLocusNames=At5g33210;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 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 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) (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=F4KH89-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the SHI protein family. {ECO:0000305}.
CC -!- CAUTION: May be the product of a pseudogene. {ECO:0000305}.
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DR EMBL; AC069557; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED93889.1; -; Genomic_DNA.
DR RefSeq; NP_198306.1; NM_122845.1. [F4KH89-1]
DR AlphaFoldDB; F4KH89; -.
DR STRING; 3702.AT5G33210.1; -.
DR PaxDb; F4KH89; -.
DR PRIDE; F4KH89; -.
DR ProteomicsDB; 226569; -. [F4KH89-1]
DR EnsemblPlants; AT5G33210.1; AT5G33210.1; AT5G33210. [F4KH89-1]
DR GeneID; 833279; -.
DR Gramene; AT5G33210.1; AT5G33210.1; AT5G33210. [F4KH89-1]
DR KEGG; ath:AT5G33210; -.
DR Araport; AT5G33210; -.
DR TAIR; locus:2183078; AT5G33210.
DR eggNOG; ENOG502QQ15; Eukaryota.
DR HOGENOM; CLU_1549735_0_0_1; -.
DR OrthoDB; 1014431at2759; -.
DR PhylomeDB; F4KH89; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4KH89; baseline and differential.
DR Genevisible; F4KH89; 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; IPR006510; Znf_LRP1.
DR PANTHER; PTHR31604; PTHR31604; 1.
DR TIGRFAMs; TIGR01623; put_zinc_LRP1; 1.
PE 3: Inferred from homology;
KW Activator; Alternative splicing; Auxin biosynthesis;
KW Auxin signaling pathway; Developmental protein; DNA-binding; Metal-binding;
KW Nucleus; Reference proteome; Zinc.
FT CHAIN 1..173
FT /note="Protein SHI RELATED SEQUENCE 8"
FT /id="PRO_0000424580"
FT DNA_BIND 52..79
FT /note="Zn(2)-C6 fungal-type; degenerate"
FT /evidence="ECO:0000250"
FT REGION 100..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 52
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 52
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
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 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 173 AA; 19543 MW; 7A3419FEC844BDF8 CRC64;
MDMNMEKIFE DSVPCRVRAK RGCATHPRSI AERAAMMMIR SGGSGGSGGV SCQDFGNQAK
KDCSHMRCRT CCKSRGFECS THVRSTWVPA TKRRERQQQL ATVQPQTQLP RGESVPKRHR
ENLPATSSSL VCTRIPFHSG ICHCNVKYLF MCIYICLLLY GREIYNEMQA AFL
