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SRS3_ARATH
ID   SRS3_ARATH              Reviewed;         174 AA.
AC   Q9SJT8; Q8GUY8;
DT   11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Protein SHI RELATED SEQUENCE 3;
GN   Name=SRS3; OrderedLocusNames=At2g21400; ORFNames=F3K23.16;
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=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 13-174.
RC   STRAIN=cv. Columbia;
RX   PubMed=12481096; DOI=10.1104/pp.010207;
RA   Xiao Y.-L., Malik M., Whitelaw C.A., Town C.D.;
RT   "Cloning and sequencing of cDNAs for hypothetical genes from chromosome 2
RT   of Arabidopsis.";
RL   Plant Physiol. 130:2118-2128(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   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   -!- 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; AC006841; AAD23685.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC07174.1; -; Genomic_DNA.
DR   EMBL; AY163777; AAN85201.1; -; mRNA.
DR   PIR; G84600; G84600.
DR   RefSeq; NP_179735.1; NM_127712.3.
DR   AlphaFoldDB; Q9SJT8; -.
DR   SMR; Q9SJT8; -.
DR   BioGRID; 2032; 7.
DR   IntAct; Q9SJT8; 7.
DR   STRING; 3702.AT2G21400.1; -.
DR   PaxDb; Q9SJT8; -.
DR   PRIDE; Q9SJT8; -.
DR   EnsemblPlants; AT2G21400.1; AT2G21400.1; AT2G21400.
DR   GeneID; 816679; -.
DR   Gramene; AT2G21400.1; AT2G21400.1; AT2G21400.
DR   KEGG; ath:AT2G21400; -.
DR   Araport; AT2G21400; -.
DR   TAIR; locus:2050074; AT2G21400.
DR   eggNOG; ENOG502QQ15; Eukaryota.
DR   HOGENOM; CLU_041493_3_1_1; -.
DR   InParanoid; Q9SJT8; -.
DR   PhylomeDB; Q9SJT8; -.
DR   PRO; PR:Q9SJT8; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9SJT8; baseline.
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; 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   2: Evidence at transcript level;
KW   Activator; Auxin biosynthesis; Auxin signaling pathway;
KW   Developmental protein; DNA-binding; Metal-binding; Nucleus;
KW   Reference proteome; Zinc.
FT   CHAIN           1..174
FT                   /note="Protein SHI RELATED SEQUENCE 3"
FT                   /id="PRO_0000424575"
FT   DNA_BIND        9..36
FT                   /note="Zn(2)-C6 fungal-type; degenerate"
FT                   /evidence="ECO:0000250"
FT   MOTIF           110..113
FT                   /note="Required for homo- and heterodimerization"
FT                   /evidence="ECO:0000250"
FT   BINDING         9
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         9
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         12
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         20
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         25
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         25
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         29
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         36
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        41
FT                   /note="K -> E (in Ref. 3; AAN85201)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   174 AA;  19814 MW;  ABC062FA0F9F9C93 CRC64;
     MMMIMGRKCE DCGNQAKKDC VYMRCRTCCK SKAFHCQTHI KSTWVPAYRR SHHKHQSQPL
     STSIPKGVQI HTTPGHFPAE LSSLADFRCV KVSSIDDGKE QYAYQTTVNI GGHVFRGILH
     DQGLHKVMVD HHYNKNSNNH QELLTPSTSS CPLKITSPFT DFMFGTRFSS VLRR
 
 
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