ID   SOX5_XENTR              Reviewed;         753 AA.
AC   B3DM43;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Transcription factor Sox-5 {ECO:0000250|UniProtKB:P35710};
DE   AltName: Full=SRY (sex determining region Y)-box 5;
GN   Name=sox5 {ECO:0000312|EMBL:AAI67694.1};
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1] {ECO:0000312|EMBL:AAI67694.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Tadpole {ECO:0000312|EMBL:AAI67694.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transcription factor involved in chondrocytes differentiation
CC       and cartilage formation. Specifically binds the 5'-AACAAT-3' DNA motif
CC       present in enhancers and super-enhancers and promotes expression of
CC       genes important for chondrogenesis. Required for overt chondrogenesis
CC       when condensed prechondrocytes differentiate into early stage
CC       chondrocytes: sox5 and sox6 cooperatively bind with sox9 on active
CC       enhancers and super-enhancers associated with cartilage-specific genes,
CC       and thereby potentiate sox9's ability to transactivate. Not involved in
CC       precartilaginous condensation, the first step in chondrogenesis, during
CC       which skeletal progenitors differentiate into prechondrocytes.
CC       {ECO:0000250|UniProtKB:P35710}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P35710}.
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DR   EMBL; BC167694; AAI67694.1; -; mRNA.
DR   RefSeq; NP_001122130.1; NM_001128658.1.
DR   AlphaFoldDB; B3DM43; -.
DR   BMRB; B3DM43; -.
DR   SMR; B3DM43; -.
DR   STRING; 8364.ENSXETP00000055793; -.
DR   PaxDb; B3DM43; -.
DR   PRIDE; B3DM43; -.
DR   GeneID; 100038209; -.
DR   KEGG; xtr:100038209; -.
DR   CTD; 6660; -.
DR   Xenbase; XB-GENE-487032; sox5.
DR   eggNOG; KOG0528; Eukaryota.
DR   InParanoid; B3DM43; -.
DR   OrthoDB; 465521at2759; -.
DR   Proteomes; UP000008143; Chromosome 3.
DR   Proteomes; UP000790000; Unplaced.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0001502; P:cartilage condensation; ISS:UniProtKB.
DR   GO; GO:0051216; P:cartilage development; ISS:UniProtKB.
DR   GO; GO:0045165; P:cell fate commitment; IBA:GO_Central.
DR   GO; GO:0002062; P:chondrocyte differentiation; ISS:UniProtKB.
DR   GO; GO:0032332; P:positive regulation of chondrocyte differentiation; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 1.10.30.10; -; 1.
DR   InterPro; IPR009071; HMG_box_dom.
DR   InterPro; IPR036910; HMG_box_dom_sf.
DR   Pfam; PF00505; HMG_box; 1.
DR   SMART; SM00398; HMG; 1.
DR   SUPFAM; SSF47095; SSF47095; 1.
DR   PROSITE; PS50118; HMG_BOX_2; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Differentiation; DNA-binding; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..753
FT                   /note="Transcription factor Sox-5"
FT                   /id="PRO_0000378066"
FT   DNA_BIND        557..625
FT                   /note="HMG box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          357..418
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          679..753
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          453..487
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        362..417
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        683..698
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        707..725
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        726..741
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   753 AA;  83100 MW;  CDC07323325AAA8A CRC64;
     MLTDPDLPPE FERMSSKRPA SPYGEADGEV AMVTSRQKME DDGGDGLPAF HLPLHVGFKP
     HSEEFQAVSL LTQEGCDRRS PSYQHNTMEL DCNKMPPFAL HNAATSPIKA EELGRQSGES
     LANAMLGTPE RRKGSLADVV DTLKQRKMEE LIKSEPEETP SIEKLLSKDW KDKLLAMGSG
     NLGDVKGTPE SLAEKERQLM AMINQLTSLR EQLLAAHDEQ KKLAASQIEK QRQQMELAKQ
     QQEQIARQQQ QLLQQQHKIN LLQQQIQVQG QLPPLMIPVF PPDQRTLAAA AAAQQGFLIP
     PGFSYKPGCS DPYPVQLIPT TMAAAAAATP GLAPLQLQQL YAAQLAAMQV SPGAKLPGVP
     PSNLSNAVSP SSIHTDKSTS SPPPKTKDDV TQPLNLSAKP KGSDSKSPSS PTSPHIPRLS
     SALAHKPICS TSASTPLRVN SIDILSSITS PGYLNDHDAV TKAIQEARQM KEQLRREQQA
     LDGKVVNSLG LNNCRTDKDK SSLESLTQQL TGKPNEDKFS HAMMDFNLSG DSDGSAGISE
     SRIYRESRGR GSNEPHIKRP MNAFMVWAKD ERRKILQAFP DMHNSNISKI LGSRWKAMTN
     LEKQPYYEEQ ARLSKQHLEK YPDYKYKPRP KRTCLVDGKK LRIGEYKAIM RSRRQQAQIP
     ISTAGVVYPG AIAMAGMPSP HLPSEHSSVS SSPEPGMPVI QSTYGIKEEE PHIKEEIHRE
     DINGEMYDEY DEDDDPDVDY ASDSENLSAE QAN