SOX2_SHEEP
ID SOX2_SHEEP Reviewed; 320 AA.
AC P54231;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Transcription factor SOX-2;
GN Name=SOX2;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9161426; DOI=10.1016/s0378-1119(96)00782-2;
RA Payen E., Pailhoux E., Gianquinto L., Hayes H., le Pennec N., Bezard J.,
RA Cotinot C.;
RT "The ovine SOX2 gene: sequence, chromosomal localization and gonadal
RT expression.";
RL Gene 189:143-147(1997).
CC -!- FUNCTION: Transcription factor that forms a trimeric complex with OCT4
CC on DNA and controls the expression of a number of genes involved in
CC embryonic development such as YES1, FGF4, UTF1 and ZFP206 (By
CC similarity). Binds to the proximal enhancer region of NANOG (By
CC similarity). Critical for early embryogenesis and for embryonic stem
CC cell pluripotency (By similarity). Downstream SRRT target that mediates
CC the promotion of neural stem cell self-renewal (By similarity). Keeps
CC neural cells undifferentiated by counteracting the activity of
CC proneural proteins and suppresses neuronal differentiation (By
CC similarity). May function as a switch in neuronal development (By
CC similarity). {ECO:0000250|UniProtKB:P48430,
CC ECO:0000250|UniProtKB:P48431, ECO:0000250|UniProtKB:P48432}.
CC -!- SUBUNIT: Interacts with ZSCAN10 (By similarity). Interacts with SOX3
CC and FGFR1 (By similarity). Interacts with GLIS1 (By similarity).
CC Interacts with POU5F1; binds synergistically with POU5F1 to DNA (By
CC similarity). {ECO:0000250|UniProtKB:P48431,
CC ECO:0000250|UniProtKB:P48432}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
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}.
CC -!- PTM: Sumoylation inhibits DNA binding and negatively regulates the FGF4
CC transactivation. {ECO:0000250}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X96997; CAA65725.1; -; Genomic_DNA.
DR RefSeq; NP_001305003.1; NM_001318074.1.
DR AlphaFoldDB; P54231; -.
DR BMRB; P54231; -.
DR SMR; P54231; -.
DR STRING; 9940.ENSOARP00000015658; -.
DR Ensembl; ENSOART00020008872; ENSOARP00020007334; ENSOARG00020005758.
DR GeneID; 101110563; -.
DR KEGG; oas:101110563; -.
DR CTD; 6657; -.
DR eggNOG; KOG0527; Eukaryota.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:Ensembl.
DR GO; GO:0035198; F:miRNA binding; IEA:Ensembl.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0001714; P:endodermal cell fate specification; IEA:Ensembl.
DR GO; GO:0001654; P:eye development; IEA:Ensembl.
DR GO; GO:0048839; P:inner ear development; IEA:Ensembl.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:1902807; P:negative regulation of cell cycle G1/S phase transition; IEA:Ensembl.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0097150; P:neuronal stem cell population maintenance; ISS:UniProtKB.
DR GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0021983; P:pituitary gland development; IEA:Ensembl.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0043281; P:regulation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl.
DR GO; GO:0070848; P:response to growth factor; IEA:Ensembl.
DR GO; GO:0009611; P:response to wounding; IEA:Ensembl.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IEA:Ensembl.
DR Gene3D; 1.10.30.10; -; 1.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR032643; SOX-2.
DR InterPro; IPR022097; SOX_fam.
DR PANTHER; PTHR10270:SF231; PTHR10270:SF231; 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 3: Inferred from homology;
KW Activator; Developmental protein; DNA-binding; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..320
FT /note="Transcription factor SOX-2"
FT /id="PRO_0000048717"
FT DNA_BIND 44..112
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 275..283
FT /note="9aaTAD"
FT /evidence="ECO:0000250|UniProtKB:P41225"
FT COMPBIAS 10..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48431"
FT CROSSLNK 248
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 320 AA; 34481 MW; C6F7BA47AD103B78 CRC64;
MYNMMETELK PPGPQQTSGG GGGGGGNSTA AAAGGNQKNS PDRVKRPMNA FMVWSRGQRR
KMAQENPKMH NSEISKRLGA EWKLLSETEK RPFIDEAKRL RALHMKEHPD YKYRPRRKTK
TLMKKDKYTL PGGLLAPGGN SMASGVGVGA GLGAGVNQRM DSYAHMNGWS NGSYSMMQDQ
LGYPQHPGLN AHGAAQMQPM HRYDVSALQY NSMTSSQTYM NGSPTYSMSY SQQGTPGMAL
GSMGSVVKSE ASSSPPVVTS SSHSRAPCQA GDLRDMISMY LPGAEVPEPA APSRLHMSQH
YQSGPVPGTA INGTLPLSHM
