SOX6_PONAB
ID SOX6_PONAB Reviewed; 787 AA.
AC Q5RCU4;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Transcription factor SOX-6 {ECO:0000305};
GN Name=SOX6 {ECO:0000250|UniProtKB:P35712};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transcription factor that plays a key role in several
CC developmental processes, including neurogenesis, chondrocytes
CC differentiation and cartilage formation. Specifically binds the 5'-
CC AACAAT-3' DNA motif present in enhancers and super-enhancers and
CC promotes expression of genes important for chondrogenesis. Required for
CC overt chondrogenesis when condensed prechondrocytes differentiate into
CC early stage chondrocytes: SOX5 and SOX6 cooperatively bind with SOX9 on
CC active enhancers and super-enhancers associated with cartilage-specific
CC genes, and thereby potentiate SOX9's ability to transactivate. Not
CC involved in precartilaginous condensation, the first step in
CC chondrogenesis, during which skeletal progenitors differentiate into
CC prechondrocytes. Together with SOX5, required to form and maintain a
CC pool of highly proliferating chondroblasts between epiphyses and
CC metaphyses, to form columnar chondroblasts, delay chondrocyte
CC prehypertrophy but promote hypertrophy, and to delay terminal
CC differentiation of chondrocytes on contact with ossification fronts.
CC Binds to the proximal promoter region of the myelin protein MPZ gene,
CC and is thereby involved in the differentiation of oligodendroglia in
CC the developing spinal tube. Binds to the gene promoter of MBP and acts
CC as a transcriptional repressor. {ECO:0000250|UniProtKB:P40645}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with DAZAP2 (By
CC similarity). May interact with CENPK (By similarity).
CC {ECO:0000250|UniProtKB:P40645}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P40645,
CC ECO:0000255|PROSITE-ProRule:PRU00267}. Cytoplasm
CC {ECO:0000250|UniProtKB:P40645}.
CC -!- PTM: Sumoylation inhibits the transcriptional activity. {ECO:0000250}.
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DR EMBL; CR858174; CAH90413.1; -; mRNA.
DR RefSeq; NP_001125207.1; NM_001131735.1.
DR AlphaFoldDB; Q5RCU4; -.
DR SMR; Q5RCU4; -.
DR STRING; 9601.ENSPPYP00000003973; -.
DR GeneID; 100172098; -.
DR KEGG; pon:100172098; -.
DR CTD; 55553; -.
DR eggNOG; KOG0528; Eukaryota.
DR InParanoid; Q5RCU4; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0001217; F:DNA-binding transcription repressor activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0007420; P:brain development; ISS:UniProtKB.
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:0021529; P:spinal cord oligodendrocyte cell differentiation; ISS:UniProtKB.
DR Gene3D; 1.10.30.10; -; 1.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR027153; SOX-6.
DR PANTHER; PTHR45789:SF1; PTHR45789:SF1; 2.
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 Activator; Coiled coil; Cytoplasm; Developmental protein; Differentiation;
KW DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Repressor; Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..787
FT /note="Transcription factor SOX-6"
FT /id="PRO_0000310865"
FT DNA_BIND 580..648
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 712..787
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 184..262
FT /evidence="ECO:0000255"
FT COMPBIAS 21..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 712..744
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 757..772
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 119
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P35712"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35712"
FT MOD_RES 360
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P40645"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35712"
FT MOD_RES 401
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40645"
FT CROSSLNK 363
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 376
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 787 AA; 87307 MW; 0AA531989BD660D6 CRC64;
MSSKQATSPF ACAADGEDAM TQDLTSREKE EGSDQHVASH LPLHPIMHNK PHSEELPTLV
NTIQQDADWD SVLSSQQRME SENNKLCSLY SFRNTSTSPH KPDEGSRDRE IMTSVTFGTP
ERRKGSLADV VDTLKQKKLE EMTRTEQEDP SCMEKLLSKD WKEKMERLNT SELLGEIKGT
PESLAEKERQ LSTMITQLIS LREQLLAAHD EQKKLAASQI EKQRQQMDLA RQQQEQIARQ
QQQLLQQQHK INLLQQQIQV QGHMPPLMIP IFPHDQRTLA AAAAAQQGFL FPPGITYKPG
DNYPVQFIPS TMAAAAASGL SPLQLQQLYA AQLASMQVSP GAKMPSTPQP PNTAGTVSPT
GIKNEKRGTS PVTQVKDEAA AQPLNLSSRP KTAEPVKSPT SPTQNLFPAS KTSPVNLPNK
SSIPSPIGGS LGRGSSLDIL SSLNSPALFG DQDTVMKAIQ EARKMREQIQ REQQQQQPHG
VDGKLSSINN MGLNNCRNEK ERTRFENLGP QLTGKSNEDG KLGPGVIDLT RPEDAEGSKA
MNGSAAKLQQ YYCWPTGGAT VAEARVYRDA RGRASSEPHI KRPMNAFMVW AKDERRKILQ
AFPDMHNSNI SKILGSRWKS MSNQEKQPYY EEQARLSKIH LEKYPNYKYK PRPKRTCIVD
GKKLRIGEYK QLMRSRRQEM RQFFTVGQQP QIPITTGTGV VYPGAITMAT TTPSPQMTSD
CSSTSASPEP SLPVIQSTYG MKTDGGSLAG NEMINGEDEM EMYDDYEDDP KSDYSSENEA
PEAVSAN
