SOX3A_XENLA
ID SOX3A_XENLA Reviewed; 309 AA.
AC P55863; A7VJ96; P40648; Q6INQ2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Transcription factor Sox-3-A;
DE Short=xSox3;
DE AltName: Full=xSox-B1;
GN Name=sox3-a; Synonyms=sox3;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC TISSUE=Ovary;
RX PubMed=9328277; DOI=10.1006/abbi.1997.0283;
RA Sakai Y., Hiraoka Y., Konishi M., Ogawa M., Aiso S.;
RT "Isolation and Characterization of Xenopus laevis xSox-B1 cDNA.";
RL Arch. Biochem. Biophys. 346:1-6(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Ovary;
RX PubMed=9099866; DOI=10.1016/s0378-1119(96)00790-1;
RA Koyano S., Ito M., Takamatsu N., Takiguchi S., Shiba T.;
RT "The Xenopus Sox3 gene expressed in oocytes of early stages.";
RL Gene 188:101-107(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=9415486;
RA Penzel R., Oschwald R., Chen Y., Tacke L., Grunz H.;
RT "Characterization and early embryonic expression of a neural specific
RT transcription factor xSOX3 in Xenopus laevis.";
RL Int. J. Dev. Biol. 41:667-677(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastrula;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP INTERACTION WITH CTNNB1.
RX PubMed=10549281; DOI=10.1016/s1097-2765(00)80200-2;
RA Zorn A.M., Barish G.D., Williams B.O., Lavender P., Klymkowsky M.W.,
RA Varmus H.E.;
RT "Regulation of Wnt signaling by Sox proteins: XSox17 alpha/beta and XSox3
RT physically interact with beta-catenin.";
RL Mol. Cell 4:487-498(1999).
RN [6]
RP FUNCTION, INTERACTION WITH CTNNB1, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF MET-44; ASN-45;
RP ARG-55; TRP-78; ALA-93 AND PRO-105.
RX PubMed=14522872; DOI=10.1242/dev.00798;
RA Zhang C., Basta T., Jensen E.D., Klymkowsky M.W.;
RT "The beta-catenin/VegT-regulated early zygotic gene Xnr5 is a direct target
RT of SOX3 regulation.";
RL Development 130:5609-5624(2003).
RN [7]
RP FUNCTION.
RX PubMed=15302595; DOI=10.1016/j.ydbio.2004.05.019;
RA Zhang C., Basta T., Hernandez-Lagunas L., Simpson P., Stemple D.L.,
RA Artinger K.B., Klymkowsky M.W.;
RT "Repression of nodal expression by maternal B1-type SOXs regulates germ
RT layer formation in Xenopus and zebrafish.";
RL Dev. Biol. 273:23-37(2004).
RN [8]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=17056008; DOI=10.1016/j.bbrc.2006.10.040;
RA Nitta K.R., Takahashi S., Haramoto Y., Fukuda M., Onuma Y., Asashima M.;
RT "Expression of Sox1 during Xenopus early embryogenesis.";
RL Biochem. Biophys. Res. Commun. 351:287-293(2006).
RN [9]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RA Ma L., Zhao S.-H., Kong Q.-H., Mao B.-Y.;
RT "Temporal and spatial expression patterns of Sox1 gene in Xenopus laevis
RT embryo.";
RL Dong Wu Xue Yan Jiu 28:403-408(2007).
RN [10]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=18031719; DOI=10.1016/j.ydbio.2007.10.023;
RA Rogers C.D., Archer T.C., Cunningham D.D., Grammer T.C., Silva Casey E.M.;
RT "Sox3 expression is maintained by FGF signaling and restricted to the
RT neural plate by Vent proteins in the Xenopus embryo.";
RL Dev. Biol. 313:307-319(2008).
RN [11]
RP FUNCTION.
RX PubMed=17608734; DOI=10.1111/j.1432-0436.2007.00190.x;
RA Zhang C., Klymkowsky M.W.;
RT "The Sox axis, Nodal signaling, and germ layer specification.";
RL Differentiation 75:536-545(2007).
CC -!- FUNCTION: Transcription factor with sequence-specific DNA binding
CC activity. Binds to the consensus sequence 5'-[AT][AT]CAA[AT]G-3',
CC showing a preference for 5'-AACAAT-3' and 5'-AACAAAG-3'. Inhibits beta-
CC catenin-mediated dorsal axis specification by binding to sites within
CC the promoter of the beta-catenin-regulated gene nodal5. Acts maternally
CC as a transcriptional repressor of nodal5 and nodal6 to restrict their
CC expression to the vegetal hemisphere of early embryos and thus
CC establish germ layer formation. Acts at multiple points to inhibit
CC nodal signaling, repressing the expression of the other mesoderm-
CC inducing nodal genes nodal, nodal2 and nodal4, and also acting
CC downstream to induce expression of genes including trim33/ectodermin,
CC ema and coco, whose products repress nodal signaling.
CC {ECO:0000269|PubMed:14522872, ECO:0000269|PubMed:15302595,
CC ECO:0000269|PubMed:17608734, ECO:0000269|PubMed:9099866,
CC ECO:0000269|PubMed:9328277}.
CC -!- SUBUNIT: Interacts with ctnnb1. {ECO:0000269|PubMed:10549281,
CC ECO:0000269|PubMed:14522872}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267,
CC ECO:0000269|PubMed:14522872}. Cytoplasm {ECO:0000269|PubMed:14522872}.
CC Note=Primarily cytoplasmic in early embryos. Nuclear localization
CC becomes more pronounced as development proceeds.
CC -!- TISSUE SPECIFICITY: Expression is restricted to the animal hemisphere
CC of the uncleaved egg and early cleavage embryos. In late blastula and
CC gastrula stages, expressed in the dorsal animal and marginal zone. In
CC neurula stages, expressed in the developing central nervous system
CC including the otic vesicles, branchial arches and the lens epithelium
CC of the developing eye. At stage 23 (early tail bud), expressed in the
CC neural tube and around the anterior neural plate. Throughout tail bud
CC stages, expressed in the brain, and in the otic vesicle and branchial
CC arches. Weakly expressed in the eye lens at stage 30 (late tailbud). In
CC adults, mainly expressed in the ovary, with faint expression in the
CC brain, testis, muscle and skin. {ECO:0000269|PubMed:14522872,
CC ECO:0000269|PubMed:17056008, ECO:0000269|PubMed:18031719,
CC ECO:0000269|PubMed:9099866, ECO:0000269|PubMed:9328277,
CC ECO:0000269|PubMed:9415486, ECO:0000269|Ref.9}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically. Most
CC abundant in stage I oocytes. Expression fades away at stage 7 and then
CC is elevated at the late blastula stage (stage 9), which continues
CC during neurulation. From stage 25 onwards, expression levels decrease.
CC {ECO:0000269|PubMed:14522872, ECO:0000269|PubMed:17056008,
CC ECO:0000269|PubMed:18031719, ECO:0000269|PubMed:9099866,
CC ECO:0000269|PubMed:9328277, ECO:0000269|PubMed:9415486,
CC ECO:0000269|Ref.9}.
CC -!- INDUCTION: By bmp-antagonism. Fgf is required for maintenance of
CC expression, but not for induction. {ECO:0000269|PubMed:17056008,
CC ECO:0000269|PubMed:18031719}.
CC -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large
CC number of yeast and animal transcription factors.
CC {ECO:0000250|UniProtKB:P41225}.
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DR EMBL; AB000825; BAF76379.1; -; mRNA.
DR EMBL; Y07542; CAA68828.1; -; mRNA.
DR EMBL; BC072222; AAH72222.1; -; mRNA.
DR PIR; S22946; S22946.
DR RefSeq; NP_001084148.1; NM_001090679.1.
DR AlphaFoldDB; P55863; -.
DR SMR; P55863; -.
DR BioGRID; 100660; 1.
DR PRIDE; P55863; -.
DR DNASU; 399335; -.
DR GeneID; 399335; -.
DR KEGG; xla:399335; -.
DR CTD; 399335; -.
DR Xenbase; XB-GENE-484819; sox3.S.
DR OMA; ANAGGGX; -.
DR OrthoDB; 1161594at2759; -.
DR Proteomes; UP000186698; Chromosome 8S.
DR Bgee; 399335; Expressed in blastula and 13 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0008013; F:beta-catenin binding; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0001704; P:formation of primary germ layer; IMP:UniProtKB.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; IMP:UniProtKB.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR Gene3D; 1.10.30.10; -; 1.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR029550; SOX-3.
DR InterPro; IPR022097; SOX_fam.
DR PANTHER; PTHR10270:SF111; PTHR10270:SF111; 1.
DR Pfam; PF00505; HMG_box; 1.
DR Pfam; PF12336; SOXp; 1.
DR SMART; SM00398; HMG; 1.
DR SUPFAM; SSF47095; SSF47095; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Developmental protein; DNA-binding; Gastrulation; Nucleus;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..309
FT /note="Transcription factor Sox-3-A"
FT /id="PRO_0000048723"
FT DNA_BIND 40..108
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 260..271
FT /note="9aaTAD"
FT /evidence="ECO:0000250|UniProtKB:P41225"
FT COMPBIAS 276..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 44
FT /note="M->L: Abolishes binding to 5'-ATTGTT-3' DNA
FT sequence. Does not affect ctnnb1-binding."
FT /evidence="ECO:0000269|PubMed:14522872"
FT MUTAGEN 45
FT /note="N->I: Abolishes binding to 5'-ATTGTT-3' DNA
FT sequence. Reduces binding to the nodal5 promoter. Does not
FT affect ctnnb1-binding."
FT /evidence="ECO:0000269|PubMed:14522872"
FT MUTAGEN 55
FT /note="R->G: Abolishes binding to 5'-ATTGTT-3' DNA
FT sequence."
FT /evidence="ECO:0000269|PubMed:14522872"
FT MUTAGEN 78
FT /note="W->R: Abolishes binding to 5'-ATTGTT-3' DNA
FT sequence."
FT /evidence="ECO:0000269|PubMed:14522872"
FT MUTAGEN 93
FT /note="A->S: Does not abolish binding to 5'-ATTGTT-3' DNA
FT sequence."
FT /evidence="ECO:0000269|PubMed:14522872"
FT MUTAGEN 105
FT /note="P->A: Abolishes binding to 5'-ATTGTT-3' DNA
FT sequence."
FT /evidence="ECO:0000269|PubMed:14522872"
FT CONFLICT 96
FT /note="L -> K (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 309 AA; 34035 MW; 89E401E6BB9EAE03 CRC64;
MYSMLDTDIK SPVQQSNAPI GGPATPGGKG NASTLDQDRV KRPMNAFMVW SRGQRRKMAQ
ENPKMHNSEI SKRLGADWKL LSDSDKRPFI DEAKRLRAVH MKDYPDYKYR PRRKTKTLLK
KDKYSLPGNL LAPGVSPVAS SVGVGQRIDT YAHMNGWTNG AYSLMQDQLG YSQHPAMNSP
QMQQIQHRYD MSGLQYNPMM TSAQNAYMNA AASTYSMSPA YNQQSSTVMS LASMGSVVKS
EPSSPPPAIT SHTQRACLGD LRDMISMYLP PGGDASDPSL QNSRLHSVHQ HYQSAAGPGV
NGTVPLTHI
