SRS5_ARATH
ID SRS5_ARATH Reviewed; 346 AA.
AC Q9LQZ5;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Protein SHI RELATED SEQUENCE 5;
GN Name=SRS5; OrderedLocusNames=At1g75520; ORFNames=F1B16.17;
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].
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 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 Q9LQZ5; Q9S7W5: TCP13; NbExp=3; IntAct=EBI-15194925, EBI-4424877;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:16740146}.
CC -!- SIMILARITY: Belongs to the SHI protein family. {ECO:0000305}.
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DR EMBL; AC006434; AAF87119.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35729.1; -; Genomic_DNA.
DR EMBL; AY800620; AAV68856.1; -; mRNA.
DR EMBL; AY924730; AAX23805.1; -; mRNA.
DR PIR; F96785; F96785.
DR RefSeq; NP_177684.1; NM_106205.3.
DR AlphaFoldDB; Q9LQZ5; -.
DR BioGRID; 29107; 24.
DR IntAct; Q9LQZ5; 24.
DR STRING; 3702.AT1G75520.1; -.
DR PaxDb; Q9LQZ5; -.
DR PRIDE; Q9LQZ5; -.
DR ProteomicsDB; 226567; -.
DR EnsemblPlants; AT1G75520.1; AT1G75520.1; AT1G75520.
DR GeneID; 843888; -.
DR Gramene; AT1G75520.1; AT1G75520.1; AT1G75520.
DR KEGG; ath:AT1G75520; -.
DR Araport; AT1G75520; -.
DR TAIR; locus:2005659; AT1G75520.
DR eggNOG; ENOG502QQ15; Eukaryota.
DR HOGENOM; CLU_041493_1_0_1; -.
DR InParanoid; Q9LQZ5; -.
DR OMA; YAYHTAV; -.
DR OrthoDB; 1014431at2759; -.
DR PhylomeDB; Q9LQZ5; -.
DR PRO; PR:Q9LQZ5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LQZ5; baseline and differential.
DR Genevisible; Q9LQZ5; AT.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA: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:0009640; P:photomorphogenesis; IGI:TAIR.
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..346
FT /note="Protein SHI RELATED SEQUENCE 5"
FT /id="PRO_0000424577"
FT DNA_BIND 125..152
FT /note="Zn(2)-C6 fungal-type; degenerate"
FT /evidence="ECO:0000250"
FT REGION 7..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 269..272
FT /note="Required for homo- and heterodimerization"
FT /evidence="ECO:0000250"
FT COMPBIAS 15..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..206
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 141
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 141
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 152
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 346 AA; 38554 MW; DF63B573D28CAC9E CRC64;
MAGFFYLGGR DNNSNNNKQD HHQVDKDHHH QDKSNYLYLY KDEIYNNNKG FEIWPPQYFQ
QQEHQQQQQQ QQHASAPANF YSFGMVPSGS SSNNNNNRSR SLYFNVVSDH EPGGFTVTRQ
GGMNCQDCGN QAKKDCPHMR CRTCCKSRGF HCQTHVKSTW VPAAKRRERL AQLASLQHHS
ASSRETQNAK RLREASGGDN NDDKDHSGGG GSALANTRVV NANSNSGLEV SQHLPPEVNS
PAIFRCVRVS SIEEDEDDQA YAYQTAVNIG GHIFKGILYD QGPEHQDNHH LNLLASTATT
TNVEETATKT VTGNNNNGLM LDPSSLYPAQ LNSFIAGTPF FTPPRS
