SOX15_MOUSE
ID SOX15_MOUSE Reviewed; 231 AA.
AC P43267; O70204; P70418; Q62246; Q91V00; Q91V43; Q920T1; Q9JLG2;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 08-DEC-2000, sequence version 3.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Protein SOX-15;
GN Name=Sox15; Synonyms=Sox-15;
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 [GENOMIC DNA].
RC STRAIN=129;
RX PubMed=10524236; DOI=10.1016/s0378-1119(99)00301-7;
RA Miyashita A., Shimizu N., Endo N., Hanyuu T., Ishii N., Ito K., Itoh Y.,
RA Shirai M., Nakajima T., Odani S., Kuwano R.;
RT "Five different genes, Eif4a1, Cd68, Supl15h, Sox15 and Fxr2h, are
RT clustered in a 40 kb region of mouse chromosome 11.";
RL Gene 237:53-60(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=10821863; DOI=10.1074/jbc.275.21.16103;
RA Beranger F., Mejean C., Moniot B., Berta P., Vandromme M.;
RT "Muscle differentiation is antagonized by SOX15, a new member of the SOX
RT protein family.";
RL J. Biol. Chem. 275:16103-16109(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 8-231.
RC STRAIN=BFM/2Msf, BLG2/Msf, C57BL/10SnJ, CAST/EiJ, HMI/Msf, MSM/Msf,
RC NJL/Msf, pgn2, and SWN/Msf;
RA Liu Y., Kitano T., Koide T., Shiroishi T., Moriwaki K., Saitou N.;
RT "Conspicuous differences among gene genealogies of 21 nuclear genes of five
RT Mus musculus subspecies.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 57-110.
RC STRAIN=Swiss Webster; TISSUE=Embryonic tooth;
RX PubMed=8921394; DOI=10.1006/geno.1996.0548;
RA Stock D.W., Buchanan A.V., Zhao Z., Weiss K.M.;
RT "Numerous members of the Sox family of HMG box-containing genes are
RT expressed in developing mouse teeth.";
RL Genomics 37:234-237(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 58-111.
RC STRAIN=C57BL/6J;
RX PubMed=8479922; DOI=10.1093/nar/21.7.1669;
RA van de Wetering M., Clevers H.;
RT "Sox 15, a novel member of the murine Sox family of HMG box transcription
RT factors.";
RL Nucleic Acids Res. 21:1669-1669(1993).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 92-231.
RC TISSUE=Pancreatic islet;
RA Lim F.L.;
RL Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=15367664; DOI=10.1128/mcb.24.19.8428-8436.2004;
RA Lee H.J., Goering W., Ochs M., Muehlfeld C., Steding G., Paprotta I.,
RA Engel W., Adham I.M.;
RT "Sox15 is required for skeletal muscle regeneration.";
RL Mol. Cell. Biol. 24:8428-8436(2004).
RN [8]
RP FUNCTION, INTERACTION WITH POU5F1, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=15863505; DOI=10.1074/jbc.m501423200;
RA Maruyama M., Ichisaka T., Nakagawa M., Yamanaka S.;
RT "Differential roles for Sox15 and Sox2 in transcriptional control in mouse
RT embryonic stem cells.";
RL J. Biol. Chem. 280:24371-24379(2005).
RN [9]
RP FUNCTION, INTERACTION WITH HAND1, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=16759287; DOI=10.1111/j.1432-0436.2006.00070.x;
RA Yamada K., Kanda H., Tanaka S., Takamatsu N., Shiba T., Ito M.;
RT "Sox15 enhances trophoblast giant cell differentiation induced by Hand1 in
RT mouse placenta.";
RL Differentiation 74:212-221(2006).
RN [10]
RP FUNCTION, INTERACTION WITH FHL3, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=17363903; DOI=10.1038/sj.emboj.7601635;
RA Meeson A.P., Shi X., Alexander M.S., Williams R.S., Allen R.E., Jiang N.,
RA Adham I.M., Goetsch S.C., Hammer R.E., Garry D.J.;
RT "Sox15 and Fhl3 transcriptionally coactivate Foxk1 and regulate myogenic
RT progenitor cells.";
RL EMBO J. 26:1902-1912(2007).
CC -!- FUNCTION: Transcription factor that binds to DNA at the 5'-AACAATG-3'
CC consensus sequence (PubMed:10821863, PubMed:15863505, PubMed:16759287,
CC PubMed:17363903). Acts as a transcriptional activator and repressor
CC (PubMed:10821863, PubMed:15863505, PubMed:16759287). Binds
CC synergistically with POU5F1 (OCT3/4) to gene promoters
CC (PubMed:15863505). Binds to the FOXK1 promoter and recruits FHL3,
CC resulting in transcriptional activation of FOXK1 which leads to
CC myoblast proliferation (PubMed:17363903). Acts as an inhibitor of
CC myoblast differentiation via transcriptional repression which leads to
CC down-regulation of the muscle-specific genes MYOD and MYOG
CC (PubMed:10821863). Involved in trophoblast giant cell differentiation
CC via enhancement of HAND1 transcriptional activity (PubMed:16759287).
CC Regulates transcription of HRC via binding to it proximal enhancer
CC region (PubMed:15863505). Involved in skeletal muscle regeneration
CC (PubMed:15367664, PubMed:17363903). Also plays a role in the
CC development of myogenic precursor cells (PubMed:15367664).
CC {ECO:0000269|PubMed:10821863, ECO:0000269|PubMed:15367664,
CC ECO:0000269|PubMed:15863505, ECO:0000269|PubMed:16759287,
CC ECO:0000269|PubMed:17363903}.
CC -!- SUBUNIT: Interacts with HAND1; the interaction enhances HAND1-induced
CC differentiation of trophoblast giant cells (PubMed:16759287). Interacts
CC with POU5F1 (OCT3/4); binds synergistically with POU5F1 to DNA
CC (PubMed:15863505). Interacts with FHL3; the interaction recruits the
CC transcriptional coactivator FHL3 to the FOXK1 promoter
CC (PubMed:17363903). {ECO:0000269|PubMed:15863505,
CC ECO:0000269|PubMed:16759287, ECO:0000269|PubMed:17363903}.
CC -!- INTERACTION:
CC P43267; Q9R059: Fhl3; NbExp=7; IntAct=EBI-7332587, EBI-7332617;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267,
CC ECO:0000269|PubMed:10821863, ECO:0000269|PubMed:15367664,
CC ECO:0000269|PubMed:17363903}.
CC -!- TISSUE SPECIFICITY: Expressed in myoblasts (at protein level)
CC (PubMed:15367664). Expressed in embryonic stem cells (at protein level)
CC (PubMed:15367664, PubMed:15863505). Expressed in myogenic progenitor
CC cells (at protein level) (PubMed:17363903). Expressed in the ovary
CC (PubMed:15367664). Expressed in kidney, liver, skeletal muscle, and
CC testes (PubMed:10821863, PubMed:15367664). Expressed in lung and skin
CC (PubMed:15863505). Expressed in the brain, heart, diaphragm, and
CC intestines (PubMed:10821863). Expressed in the conceptus tissues of the
CC placenta (PubMed:16759287). {ECO:0000269|PubMed:10821863,
CC ECO:0000269|PubMed:15367664, ECO:0000269|PubMed:15863505,
CC ECO:0000269|PubMed:16759287, ECO:0000269|PubMed:17363903}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in the conceptus ectoplacental
CC cone of the placenta at embryonic day 7.5 dpc (PubMed:16759287).
CC Expressed in the conceptus trophoblast giant cell layer of the placenta
CC (PubMed:16759287). Expressed in the trophoblast giant cells of the
CC placenta from 10 dpc, expression peaks at 14 dpc, then reduces
CC thereafter to 18 dpc (PubMed:16759287). Expression is increased during
CC trophoblast differentiation (PubMed:16759287). Expressed at 8.5 dpc in
CC developing embryos, with increased expression at 9.5 dpc
CC (PubMed:10821863). {ECO:0000269|PubMed:10821863,
CC ECO:0000269|PubMed:16759287}.
CC -!- DISRUPTION PHENOTYPE: Knockout mice are viable, morphologically normal
CC and fertile (PubMed:15367664, PubMed:15863505). Reduced regeneration of
CC damaged skeletal muscle fibers following injury with increased numbers
CC of mononuclear cells and a significant reduction in the number of
CC myofibers (PubMed:15367664, PubMed:17363903). Impaired proliferation of
CC myogenic progenitor cells, reduced number of satellite cells within the
CC tibialis anterior muscles, and a decrease in FOXK1 expression
CC (PubMed:17363903). {ECO:0000269|PubMed:15367664,
CC ECO:0000269|PubMed:15863505, ECO:0000269|PubMed:17363903}.
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DR EMBL; AB014474; BAA28604.1; -; Genomic_DNA.
DR EMBL; AF182945; AAF72108.1; -; mRNA.
DR EMBL; AB039214; BAB68738.1; -; Genomic_DNA.
DR EMBL; AB039215; BAB68739.1; -; Genomic_DNA.
DR EMBL; AB039216; BAB68740.1; -; Genomic_DNA.
DR EMBL; AB039217; BAB68741.1; -; Genomic_DNA.
DR EMBL; AB039218; BAB68742.1; -; Genomic_DNA.
DR EMBL; AB039219; BAB68743.1; -; Genomic_DNA.
DR EMBL; AB039220; BAB68744.1; -; Genomic_DNA.
DR EMBL; AB039221; BAB68745.1; -; Genomic_DNA.
DR EMBL; AB039222; BAB68746.1; -; Genomic_DNA.
DR EMBL; U70443; AAC52861.1; -; mRNA.
DR EMBL; X70909; CAB37848.1; -; Genomic_DNA.
DR EMBL; X98369; CAA67015.1; -; mRNA.
DR CCDS; CCDS24902.1; -.
DR PIR; S33715; S33715.
DR RefSeq; NP_033261.1; NM_009235.2.
DR AlphaFoldDB; P43267; -.
DR SMR; P43267; -.
DR BioGRID; 203402; 5.
DR IntAct; P43267; 4.
DR MINT; P43267; -.
DR STRING; 10090.ENSMUSP00000048524; -.
DR PhosphoSitePlus; P43267; -.
DR PaxDb; P43267; -.
DR PRIDE; P43267; -.
DR ProteomicsDB; 261614; -.
DR Antibodypedia; 12118; 199 antibodies from 33 providers.
DR DNASU; 20670; -.
DR Ensembl; ENSMUST00000047373; ENSMUSP00000048524; ENSMUSG00000041287.
DR GeneID; 20670; -.
DR KEGG; mmu:20670; -.
DR UCSC; uc007jqu.2; mouse.
DR CTD; 6665; -.
DR MGI; MGI:98363; Sox15.
DR VEuPathDB; HostDB:ENSMUSG00000041287; -.
DR eggNOG; KOG0527; Eukaryota.
DR GeneTree; ENSGT00940000162099; -.
DR HOGENOM; CLU_106341_0_0_1; -.
DR InParanoid; P43267; -.
DR OMA; GYGSSHC; -.
DR OrthoDB; 369754at2759; -.
DR PhylomeDB; P43267; -.
DR TreeFam; TF351735; -.
DR BioGRID-ORCS; 20670; 3 hits in 73 CRISPR screens.
DR PRO; PR:P43267; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P43267; protein.
DR Bgee; ENSMUSG00000041287; Expressed in morula and 77 other tissues.
DR ExpressionAtlas; P43267; baseline and differential.
DR Genevisible; P43267; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005667; C:transcription regulator complex; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; 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; IGI:MGI.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IGI:MGI.
DR GO; GO:0048627; P:myoblast development; IMP:MGI.
DR GO; GO:0045843; P:negative regulation of striated muscle tissue development; IDA:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0070318; P:positive regulation of G0 to G1 transition; IMP:BHF-UCL.
DR GO; GO:2000288; P:positive regulation of myoblast proliferation; IMP:BHF-UCL.
DR GO; GO:0014718; P:positive regulation of satellite cell activation involved in skeletal muscle regeneration; IMP:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0043403; P:skeletal muscle tissue regeneration; IMP:MGI.
DR GO; GO:0060707; P:trophoblast giant cell differentiation; IMP:UniProtKB.
DR Gene3D; 1.10.30.10; -; 1.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR031269; SOX15.
DR PANTHER; PTHR10270:SF45; PTHR10270:SF45; 1.
DR Pfam; PF00505; HMG_box; 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 Activator; DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repressor; Transcription; Transcription regulation.
FT CHAIN 1..231
FT /note="Protein SOX-15"
FT /id="PRO_0000048763"
FT DNA_BIND 47..115
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1..45
FT /note="Required to promote HAND1 transcriptional activator
FT activity"
FT /evidence="ECO:0000269|PubMed:16759287"
FT REGION 111..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..181
FT /note="Interaction with FHL3"
FT /evidence="ECO:0000269|PubMed:17363903"
FT REGION 186..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60248"
FT VARIANT 135
FT /note="E -> G (in strain: various strains)"
FT VARIANT 224
FT /note="A -> S (in strain: various strains)"
FT CONFLICT 71
FT /note="K -> E (in Ref. 1; BAA28604)"
FT /evidence="ECO:0000305"
FT CONFLICT 97
FT /note="V -> M (in Ref. 5; CAB37848)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 231 AA; 25311 MW; FCFE87C3BB458645 CRC64;
MALTSSSQAE TWSLHPRAST ASLPLGPQEQ EAGGSPGASG GLPLEKVKRP MNAFMVWSSV
QRRQMAQQNP KMHNSEISKR LGAQWKLLGD EEKRPFVEEA KRLRARHLRD YPDYKYRPRR
KSKNSSTGSV PFSQEGGGLA CGGSHWGPGY TTTQGSRGFG YQPPNYSTAY LPGSYTSSHC
RPEAPLPCTF PQSDPRLQGE LRPSFSPYLS PDSSTPYNTS LAGAPMPVTH L
