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SOX7_MOUSE
ID   SOX7_MOUSE              Reviewed;         380 AA.
AC   P40646; Q9R1T6;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2002, sequence version 2.
DT   03-AUG-2022, entry version 153.
DE   RecName: Full=Transcription factor SOX-7;
DE            Short=mSOX7;
GN   Name=Sox7; Synonyms=Sox-7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DNA-BINDING, AND TISSUE SPECIFICITY.
RX   PubMed=10320775; DOI=10.1016/s0167-4781(99)00047-0;
RA   Taniguchi K., Hiraoka Y., Ogawa M., Sakai Y., Kido S., Aiso S.;
RT   "Isolation and characterization of a mouse SRY-related cDNA, mSox7.";
RL   Biochim. Biophys. Acta 1445:225-231(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 56-109.
RC   STRAIN=Parkes; TISSUE=Brain, and Testis;
RX   PubMed=1614875; DOI=10.1093/nar/20.11.2887;
RA   Denny P., Swift S., Brand N., Dabhade N., Barton P., Ashworth A.;
RT   "A conserved family of genes related to the testis determining gene, SRY.";
RL   Nucleic Acids Res. 20:2887-2887(1992).
RN   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP   AND MUTAGENESIS OF 323-GLU--LEU-328.
RX   PubMed=11691915; DOI=10.1093/nar/29.21.4274;
RA   Takash W., Canizares J., Bonneaud N., Poulat F., Mattei M.-G., Jay P.,
RA   Berta P.;
RT   "SOX7 transcription factor: sequence, chromosomal localisation, expression,
RT   transactivation and interference with Wnt signalling.";
RL   Nucleic Acids Res. 29:4274-4283(2001).
RN   [4]
RP   FUNCTION IN FGF3 PROMOTER ACTIVATION.
RX   PubMed=15082719; DOI=10.1074/jbc.m313814200;
RA   Murakami A., Shen H., Ishida S., Dickson C.;
RT   "SOX7 and GATA-4 are competitive activators of Fgf-3 transcription.";
RL   J. Biol. Chem. 279:28564-28573(2004).
RN   [5]
RP   FUNCTION IN HEMOPOIETIC DEVELOPMENT, AND DEVELOPMENTAL STAGE.
RX   PubMed=19801444; DOI=10.1182/blood-2009-06-226290;
RA   Gandillet A., Serrano A.G., Pearson S., Lie-A-Ling M., Lacaud G.,
RA   Kouskoff V.;
RT   "Sox7-sustained expression alters the balance between proliferation and
RT   differentiation of hematopoietic progenitors at the onset of blood
RT   specification.";
RL   Blood 114:4813-4822(2009).
RN   [6]
RP   FUNCTION IN MYOGENIC DIFFERENTIATION, AND DEVELOPMENTAL STAGE.
RX   PubMed=19489079; DOI=10.1002/stem.57;
RA   Savage J., Conley A.J., Blais A., Skerjanc I.S.;
RT   "SOX15 and SOX7 differentially regulate the myogenic program in P19
RT   cells.";
RL   Stem Cells 27:1231-1243(2009).
RN   [7]
RP   FUNCTION IN HEMOPOIETIC DEVELOPMENT, INDUCTION, AND DEVELOPMENTAL STAGE.
RX   PubMed=22492353; DOI=10.1242/dev.071282;
RA   Costa G., Mazan A., Gandillet A., Pearson S., Lacaud G., Kouskoff V.;
RT   "SOX7 regulates the expression of VE-cadherin in the haemogenic endothelium
RT   at the onset of haematopoietic development.";
RL   Development 139:1587-1598(2012).
CC   -!- FUNCTION: Binds to and activates the CDH5 promoter, hence plays a role
CC       in the transcriptional regulation of genes expressed in the hemogenic
CC       endothelium and blocks further differentiation into blood precursors.
CC       May be required for the survival of both hematopoietic and endothelial
CC       precursors during specification. May play a role in skeletal myogenesis
CC       and up-regulate the expression of muscle markers, such as PAX3/PAX7 and
CC       Meox1. Competes with GATA4 for binding and activation of the FGF3
CC       promoter. Represses Wnt/beta-catenin-stimulated transcription. Probably
CC       acts by targeting CTNNB1 to proteasomal degradation. Binds the DNA
CC       sequence 5'-AACAAT-3'. {ECO:0000269|PubMed:10320775,
CC       ECO:0000269|PubMed:11691915, ECO:0000269|PubMed:15082719,
CC       ECO:0000269|PubMed:19489079, ECO:0000269|PubMed:19801444,
CC       ECO:0000269|PubMed:22492353}.
CC   -!- SUBUNIT: Interacts with CTNNB1/beta-catenin; this interaction may lead
CC       to the proteasomal degradation of active CTNNB1 and thus inhibition of
CC       Wnt/beta-catenin-stimulated transcription. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267,
CC       ECO:0000269|PubMed:11691915}. Cytoplasm {ECO:0000269|PubMed:11691915}.
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in ovary, lung and heart.
CC       In the ovary, restricted to oocytes (at protein level). Present both in
CC       mesenchymal and epithelial cells in some adult tissues, including ear.
CC       {ECO:0000269|PubMed:10320775, ECO:0000269|PubMed:11691915}.
CC   -!- DEVELOPMENTAL STAGE: Expressed at least from 7.6 until 17.5 dpc. At 7.5
CC       dpc, expressed in the yolk sac, as well as in the parietal and visceral
CC       endoderm and the embryonic mesoderm. At 8 dpc, expressed in somites and
CC       head region. At 9.5 dpc, expressed throughout vasculature. At 11.5 dpc,
CC       primarily expressed in the intersomitic vasculature. At 17.5 dpc,
CC       predominant expression in heart and lung. At that stage, also expressed
CC       in brain, cochlea, tongue, cartilage, lung, liver and vertebrae. During
CC       hemangioblast differentiation, transiently expressed in hemogenic
CC       endothelium cells and down-regulated in nascent blood precursors. May
CC       be expressed during the precursor stage of myogenic differentiation.
CC       {ECO:0000269|PubMed:11691915, ECO:0000269|PubMed:19489079,
CC       ECO:0000269|PubMed:19801444, ECO:0000269|PubMed:22492353}.
CC   -!- INDUCTION: Up-regulated by VEGFA. {ECO:0000269|PubMed:22492353}.
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DR   EMBL; AB023419; BAA78765.1; -; mRNA.
DR   EMBL; X65660; CAA46611.1; -; mRNA.
DR   CCDS; CCDS27206.1; -.
DR   PIR; S22945; S22945.
DR   RefSeq; NP_035576.1; NM_011446.1.
DR   AlphaFoldDB; P40646; -.
DR   SMR; P40646; -.
DR   STRING; 10090.ENSMUSP00000078597; -.
DR   PhosphoSitePlus; P40646; -.
DR   PaxDb; P40646; -.
DR   PRIDE; P40646; -.
DR   ProteomicsDB; 261616; -.
DR   Antibodypedia; 1821; 223 antibodies from 30 providers.
DR   DNASU; 20680; -.
DR   Ensembl; ENSMUST00000079652; ENSMUSP00000078597; ENSMUSG00000063060.
DR   GeneID; 20680; -.
DR   KEGG; mmu:20680; -.
DR   UCSC; uc007uhy.1; mouse.
DR   CTD; 83595; -.
DR   MGI; MGI:98369; Sox7.
DR   VEuPathDB; HostDB:ENSMUSG00000063060; -.
DR   eggNOG; KOG0527; Eukaryota.
DR   GeneTree; ENSGT00940000161092; -.
DR   HOGENOM; CLU_044994_0_0_1; -.
DR   InParanoid; P40646; -.
DR   OMA; HRTPVDK; -.
DR   OrthoDB; 1042753at2759; -.
DR   PhylomeDB; P40646; -.
DR   Reactome; R-MMU-3769402; Deactivation of the beta-catenin transactivating complex.
DR   BioGRID-ORCS; 20680; 0 hits in 71 CRISPR screens.
DR   PRO; PR:P40646; -.
DR   Proteomes; UP000000589; Chromosome 14.
DR   RNAct; P40646; protein.
DR   Bgee; ENSMUSG00000063060; Expressed in kidney vasculature and 189 other tissues.
DR   ExpressionAtlas; P40646; baseline and differential.
DR   Genevisible; P40646; MM.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:MGI.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:BHF-UCL.
DR   GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0001706; P:endoderm formation; ISO:MGI.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR   GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR   GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; ISO:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR   Gene3D; 1.10.30.10; -; 1.
DR   InterPro; IPR009071; HMG_box_dom.
DR   InterPro; IPR036910; HMG_box_dom_sf.
DR   InterPro; IPR033392; Sox7/17/18_central.
DR   InterPro; IPR021934; Sox_C.
DR   Pfam; PF00505; HMG_box; 1.
DR   Pfam; PF12067; Sox17_18_mid; 1.
DR   SMART; SM00398; HMG; 1.
DR   SUPFAM; SSF47095; SSF47095; 1.
DR   PROSITE; PS50118; HMG_BOX_2; 1.
DR   PROSITE; PS51516; SOX_C; 1.
PE   1: Evidence at protein level;
KW   Activator; Cytoplasm; DNA-binding; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..380
FT                   /note="Transcription factor SOX-7"
FT                   /id="PRO_0000048732"
FT   DOMAIN          260..380
FT                   /note="Sox C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00849"
FT   DNA_BIND        45..113
FT                   /note="HMG box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT   REGION          24..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          139..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          323..328
FT                   /note="Required for beta-catenin-binding"
FT   MUTAGEN         323..328
FT                   /note="Missing: Loss of beta-catenin-binding."
FT                   /evidence="ECO:0000269|PubMed:11691915"
SQ   SEQUENCE   380 AA;  41489 MW;  BE780D7234CB895C CRC64;
     MASLLGAYPW TEGLECPALE AELSDGLSPP AVPRPSGDKS SESRIRRPMN AFMVWAKDER
     KRLAVQNPDL HNAELSKMLG KSWKALTLSQ KRPYVDEAER LRLQHMQDYP NYKYRPRRKK
     QGKRLCKRVD PGFLLSSLSR DQNTLPEKNG IGRGEKEDRG EYSPGATLPG LHSCYREGAA
     AAPGSVDTYP YGLPTPPEMS PLDALEPEQT FFSSSCQEEH GHPHHLPHLP GPPYSPEFTP
     SPLHCSHPLG SLALGQSPGV SMMSSVSGCP PSPAYYSHAT YHPLHPNLQA HLGQLSPPPE
     HPGFDTLDQL SQVELLGDMD RNEFDQYLNT PGHPDSAAGV GTLTGHVPLS QGTPTGPTET
     SLISVLADAT ATYYNSYSVS
 
 
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