SOX5_XENLA
ID SOX5_XENLA Reviewed; 757 AA.
AC P40647; A5PKN9;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Transcription factor Sox-5;
DE Short=xSox-5 {ECO:0000303|PubMed:1614875};
DE AltName: Full=SRY (sex determining region Y)-box 5 {ECO:0000303|PubMed:1614875};
GN Name=sox5 {ECO:0000303|PubMed:1614875};
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 [LARGE SCALE MRNA].
RC TISSUE=Neurula;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 570-623.
RC TISSUE=Oocyte;
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 TISSUE SPECIFICITY.
RX PubMed=11784034; DOI=10.1006/dbio.2001.0434;
RA Martin B.L., Harland R.M.;
RT "Hypaxial muscle migration during primary myogenesis in Xenopus laevis.";
RL Dev. Biol. 239:270-280(2001).
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}.
CC -!- TISSUE SPECIFICITY: Expressed in migrating myoblasts during ventral
CC body wall formation. {ECO:0000269|PubMed:11784034}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI42560.1; Type=Miscellaneous discrepancy; Note=Deletion of C-terminal sequence resulting in a frameshift at position 667.; Evidence={ECO:0000305};
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DR EMBL; BC142559; AAI42560.1; ALT_SEQ; mRNA.
DR EMBL; DR718509; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; X65653; CAA46604.1; -; mRNA.
DR PIR; S22949; S22949.
DR RefSeq; NP_001167508.1; NM_001174037.1.
DR AlphaFoldDB; P40647; -.
DR BMRB; P40647; -.
DR SMR; P40647; -.
DR MaxQB; P40647; -.
DR PRIDE; P40647; -.
DR GeneID; 100381154; -.
DR KEGG; xla:100381154; -.
DR CTD; 100381154; -.
DR Xenbase; XB-GENE-865667; sox5.S.
DR OrthoDB; 465521at2759; -.
DR Proteomes; UP000186698; Chromosome 3S.
DR Bgee; 100381154; Expressed in neurula embryo and 15 other tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0001502; P:cartilage condensation; ISS:UniProtKB.
DR GO; GO:0051216; P:cartilage development; ISS:UniProtKB.
DR GO; GO:0002062; P:chondrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IDA:UniProtKB.
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..757
FT /note="Transcription factor Sox-5"
FT /id="PRO_0000048728"
FT DNA_BIND 559..627
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 113..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 719..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 457..489
FT /evidence="ECO:0000255"
FT COMPBIAS 359..388
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..436
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..745
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 757 AA; 83508 MW; 6ACC3D5192597C8A CRC64;
MLTEPELPPD INRMSSKRPA SPYGEADGEV AMATSRQKME DEGSDGLPAF HLPLHVGFPS
KPHSEEFQAV SLLTQESCDR RSPSYQLNSM ELDCNKMSAF ALHNVATSPM KAEEVGRQSG
DSLSNSMLGT PERRKGSLAD VVDTLKQRKM EELIKSEPEE TPTIEKLLSK DWKDKLLAMG
SGNLADVKGT PESLAEKERQ LMTMINQLTS LREQLLAAHD EQKKLAASQI EKQRQQMELA
KQQQEQIARQ QQQLLQQQHK INLLQQQIQV QGQLPPLMIP VFPPDQRTLA AAAAAQQGFL
IPPGFSYKPG CSDPYPLQLI PTTMAAAAAA TPGLAPLQLQ QLYAAQLAAM QVSPGAKLPG
VPQNNLSNSI SPSSVHTDKS TSSPPPKSKD DVAQPLNLSA KPKGSDSRSS SSPTSPHIQR
LSSGSTHKPI SSTSASTPIR LNSIDILSSL TSPGYLNDHD AVTKAIHEAR QMKEQLRREQ
QALDGKVVNS LGLNNCRTEK DKSSLDALTQ QLTGKPNEDK FSHAMMDFNL SGDSDGSAGI
SESRIYREAR GRGSNEPHIK RPMNAFMVWA KDERRKILQA FPDMHNSNIS KILGSRWKSM
TNLEKQPYYE EQARLSKQHL EKYPDYKYKP RPKRTCLVDG KKLRIGEYKA IMRSRRQGQQ
TQIPISTAGV VYPGAIAMAG MPSPHLPSEH SSVSSSPEPG MPVIQSTYGI KQEELHIKEE
IRGDNINGEM YDEYDEEDDP DIDYGSDSEN PSATQAN
