SOX5_RAT
ID SOX5_RAT Reviewed; 763 AA.
AC F1M8W4; F1LQN4; Q5U1X4;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2015, sequence version 2.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Transcription factor SOX-5;
GN Name=Sox5 {ECO:0000312|RGD:620471}; Synonyms=Sox-5;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=26150426; DOI=10.1093/nar/gkv688;
RA Liu C.F., Lefebvre V.;
RT "The transcription factors SOX9 and SOX5/SOX6 cooperate genome-wide through
RT super-enhancers to drive chondrogenesis.";
RL Nucleic Acids Res. 43:8183-8203(2015).
CC -!- FUNCTION: Transcription factor involved in chondrocytes differentiation
CC and cartilage formation (By similarity). Specifically binds the 5'-
CC AACAAT-3' DNA motif present in enhancers and super-enhancers and
CC promotes expression of genes important for chondrogenesis, including
CC cartilage matrix protein-coding genes, such as COL2A1 and AGC1 (By
CC similarity). Required for overt chondrogenesis when condensed
CC prechondrocytes differentiate into early stage chondrocytes: SOX5 and
CC SOX6 cooperatively bind with SOX9 on active enhancers and super-
CC enhancers associated with cartilage-specific genes, and thereby
CC potentiate SOX9's ability to transactivate (PubMed:26150426). Not
CC involved in precartilaginous condensation, the first step in
CC chondrogenesis, during which skeletal progenitors differentiate into
CC prechondrocytes (By similarity). Together with SOX6, required to form
CC and maintain a pool of highly proliferating chondroblasts between
CC epiphyses and metaphyses, to form columnar chondroblasts, delay
CC chondrocyte prehypertrophy but promote hypertrophy, and to delay
CC terminal differentiation of chondrocytes on contact with ossification
CC fronts (By similarity). Binds to the proximal promoter region of the
CC myelin protein MPZ gene (By similarity). {ECO:0000250|UniProtKB:P35710,
CC ECO:0000269|PubMed:26150426}.
CC -!- SUBUNIT: Forms homodimers and heterodimers with SOX6.
CC {ECO:0000250|UniProtKB:P35710}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P35710}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=F1M8W4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F1M8W4-2; Sequence=VSP_060587, VSP_060588;
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DR EMBL; AABR07062459; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07062460; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07062461; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07062462; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07062463; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07062464; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07073087; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC121477; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC086415; AAH86415.1; -; mRNA.
DR RefSeq; NP_001258196.1; NM_001271267.1. [F1M8W4-1]
DR RefSeq; XP_008761572.1; XM_008763350.1. [F1M8W4-2]
DR AlphaFoldDB; F1M8W4; -.
DR SMR; F1M8W4; -.
DR STRING; 10116.ENSRNOP00000052404; -.
DR PaxDb; F1M8W4; -.
DR Ensembl; ENSRNOT00000055542; ENSRNOP00000052404; ENSRNOG00000027869. [F1M8W4-1]
DR GeneID; 140587; -.
DR KEGG; rno:140587; -.
DR UCSC; RGD:1359322; rat.
DR CTD; 6660; -.
DR RGD; 620471; Sox5.
DR eggNOG; KOG0528; Eukaryota.
DR GeneTree; ENSGT00940000156122; -.
DR HOGENOM; CLU_018522_0_1_1; -.
DR InParanoid; F1M8W4; -.
DR OMA; PPPKSKX; -.
DR OrthoDB; 465521at2759; -.
DR TreeFam; TF320471; -.
DR PRO; PR:F1M8W4; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000027869; Expressed in testis and 16 other tissues.
DR ExpressionAtlas; F1M8W4; baseline and differential.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005667; C:transcription regulator complex; ISO:RGD.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:RGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:RGD.
DR GO; GO:0055059; P:asymmetric neuroblast division; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; ISO:RGD.
DR GO; GO:0021953; P:central nervous system neuron differentiation; ISO:RGD.
DR GO; GO:0002062; P:chondrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0048709; P:oligodendrocyte differentiation; ISO:RGD.
DR GO; GO:0061036; P:positive regulation of cartilage development; ISO:RGD.
DR GO; GO:0032332; P:positive regulation of chondrocyte differentiation; ISO:RGD.
DR GO; GO:2000741; P:positive regulation of mesenchymal stem cell differentiation; ISO:RGD.
DR GO; GO:0060164; P:regulation of timing of neuron differentiation; ISO:RGD.
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 1: Evidence at protein level;
KW Activator; Alternative splicing; Coiled coil; Differentiation; DNA-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..763
FT /note="Transcription factor SOX-5"
FT /id="PRO_0000450216"
FT DNA_BIND 556..624
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 77..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 714..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 195..268
FT /evidence="ECO:0000255"
FT COMPBIAS 88..127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 731..750
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35711"
FT MOD_RES 131
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P35711"
FT MOD_RES 370
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35711"
FT MOD_RES 372
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P35711"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35711"
FT MOD_RES 414
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35711"
FT MOD_RES 439
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35711"
FT VAR_SEQ 1..322
FT /note="Missing (in isoform 2)"
FT /id="VSP_060587"
FT VAR_SEQ 338..388
FT /note="LQQFYAAQLAAMQVSPGGKLLGLPQGNLGAAVSPTSIHTDKSTNSPPPKSK
FT -> LQ (in isoform 2)"
FT /id="VSP_060588"
SQ SEQUENCE 763 AA; 83971 MW; 386ABEAF673AFE43 CRC64;
MLTDPDLPQE FERMSSKRPA SPYGETDGEV AMVTSRQKVE EEESERLPAF HLPLHVSFPN
KPHSEEFQPV SLLTQEACGP RTPAAQHSTM EVDGNKVMSS LAPYNSSTSP QKAEEGGRQS
GESVSSAALG TPERRKGSLA DVVDTLKQRK MEELIKNEPE DTPSIEKLLS KDWKDKLLAM
GSGNFGEIKG TPESLAEKER QLMGMINQLT SLREQLLAAH DEQKKLAASQ IEKQRQQMEL
AKQQQEQIAR QQQQLLQQQH KINLLQQQIQ VQGQLPPLMI PVFPPDQRTL AAAAQQGFLL
PPGFSYKAGC SDPYPVQLIP TTMAAAAAAT PGLGPLQLQQ FYAAQLAAMQ VSPGGKLLGL
PQGNLGAAVS PTSIHTDKST NSPPPKSKDE VAQPLNLSAK PKTSDGKSPA SPTSPHMPAL
RINSGAGPLK ASVPAALASP SARVSTIGYL NDHDAVTKAI QEARQMKEQL RREQQALDGK
VAVVNSIGIS NCRTEKEKTT LESLTQQLAV KQNEEGKFSH GMMDFNMSGD SDGSAGVSES
RIYRESRGRG SNEPHIKRPM NAFMVWAKDE RRKILQAFPD MHNSNISKIL GSRWKAMTNL
EKQPYYEEQA RLSKQHLEKY PDYKYKPRPK RTCLVDGKKL RIGEYKAIMR NRRQEMRQYF
NVGQQAQIPI ATAGVVYPGA IAMAGMPSPH LPSEHSSVSS SPEPGMPVIQ STYGVKGEEP
HIKEEIQAED INGEIYEEYE EEEEDPDVDY GSDSENHIAG QAN
