ID   TOX2_RAT                Reviewed;         473 AA.
AC   Q76IQ7;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=TOX high mobility group box family member 2;
DE   AltName: Full=Granulosa cell HMG box protein 1;
DE            Short=GCX-1;
GN   Name=Tox2; Synonyms=Gcx-1, Gcx1;
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 [MRNA], TISSUE SPECIFICITY, INDUCTION, SUBCELLULAR
RP   LOCATION, NUCLEAR LOCALIZATION SIGNAL, AND FUNCTION.
RC   TISSUE=Ovarian granulosa cell;
RX   PubMed=14764631; DOI=10.1210/en.2003-1343;
RA   Kajitani T., Mizutani T., Yamada K., Yazawa T., Sekiguchi T., Yoshino M.,
RA   Kawata H., Miyamoto K.;
RT   "Cloning and characterization of granulosa cell high-mobility group (HMG)-
RT   box protein-1, a novel HMG-box transcriptional regulator strongly expressed
RT   in rat ovarian granulosa cells.";
RL   Endocrinology 145:2307-2318(2004).
CC   -!- FUNCTION: Putative transcriptional activator involved in the
CC       hypothalamo-pituitary-gonadal system. {ECO:0000269|PubMed:14764631}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267,
CC       ECO:0000269|PubMed:14764631}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in ovary, where it is restricted
CC       to undifferentiated granulosa cells. Expressed in hypothalamus,
CC       pituitary gland, testis and uterus. {ECO:0000269|PubMed:14764631}.
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DR   EMBL; AB096685; BAD02336.1; -; mRNA.
DR   RefSeq; NP_955424.2; NM_199392.2.
DR   RefSeq; XP_017447283.1; XM_017591794.1.
DR   AlphaFoldDB; Q76IQ7; -.
DR   SMR; Q76IQ7; -.
DR   STRING; 10116.ENSRNOP00000061248; -.
DR   PaxDb; Q76IQ7; -.
DR   PRIDE; Q76IQ7; -.
DR   GeneID; 311615; -.
DR   KEGG; rno:311615; -.
DR   UCSC; RGD:735184; rat.
DR   CTD; 84969; -.
DR   RGD; 735184; Tox2.
DR   eggNOG; KOG0381; Eukaryota.
DR   InParanoid; Q76IQ7; -.
DR   OrthoDB; 818359at2759; -.
DR   PhylomeDB; Q76IQ7; -.
DR   PRO; PR:Q76IQ7; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005634; C:nucleus; IDA:RGD.
DR   GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR   GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:RGD.
DR   GO; GO:0003713; F:transcription coactivator activity; ISO:RGD.
DR   GO; GO:0008585; P:female gonad development; IEP:RGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:RGD.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0034698; P:response to gonadotropin; IEP:RGD.
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   DNA-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..473
FT                   /note="TOX high mobility group box family member 2"
FT                   /id="PRO_0000048572"
FT   DNA_BIND        204..272
FT                   /note="HMG box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          25..63
FT                   /note="Required for transcriptional activation"
FT   REGION          139..211
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          277..302
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          340..473
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           172..201
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000269|PubMed:14764631"
FT   COMPBIAS        1..24
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        139..167
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        168..189
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        344..361
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        416..439
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        455..473
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   473 AA;  49876 MW;  5308C8EC52ADDA47 CRC64;
     MSDGNPELLS TSQTYNSQGE SNEDYEIPPI TPPNLPEPSL LHLGDHEAGY HSLCHGLAPN
     GLLPAYSYQA MDLPAIMVSN MLAQDGHLLS GQLPTIQEMV HSEVAAYDSG RPGPLLGRPA
     MLASHMSALS QSQLISQMGL RSGIAHSSPS PPGSKSATPS PSSSTQEEES DAHFKISGEK
     RPSTDPGKKA KNPKKKKKKD PNEPQKPVSA YALFFRDTQA AIKGQNPSAT FGDVSKIVAS
     MWDSLGEEQK QAYKRKTEAA KKEYLKALAA YRASLVSKSP PDQGEAKNAQ ANPPAKMLPP
     KQPMYAMPGL ASFLTPSDLQ AFRSAASPAS LARTLGSKAL LPGLSTSPPP PSFPLSPSLH
     QQLPLPPHAQ GTLLSPPLSM SPAPQPPVLP APMALQVQLA MSPSPPGPQD FPHISDFPSG
     SGSRSPGPSN PSSSGDWDGS YPSGERGLGT CRLCRSSPPP TTSPKNLQEP SAR