ID   TOX4_BOVIN              Reviewed;         619 AA.
AC   Q0P5K4;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=TOX high mobility group box family member 4;
GN   Name=TOX4;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal skin;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transcription factor that modulates cell fate reprogramming
CC       from the somatic state to the pluripotent and neuronal fate (By
CC       similarity). Component of the PTW/PP1 phosphatase complex, which plays
CC       a role in the control of chromatin structure and cell cycle progression
CC       during the transition from mitosis into interphase (By similarity). In
CC       liver, controls the expression of hormone-regulated gluconeogenic genes
CC       such as G6PC1 and PCK1. This regulation is independent of the insulin
CC       receptor activation (By similarity). {ECO:0000250|UniProtKB:O94842,
CC       ECO:0000250|UniProtKB:Q8BU11}.
CC   -!- ACTIVITY REGULATION: In liver, recruited to target gene promoters
CC       following treatment with dexamethasone and cAMP. Binding is decreased
CC       in presence of insulin. {ECO:0000250|UniProtKB:Q8BU11}.
CC   -!- SUBUNIT: Component of the PTW/PP1 phosphatase complex, composed of
CC       PPP1R10/PNUTS, TOX4, WDR82 and PPP1CA or PPP1CB or PPP1CC. Interacts
CC       with PPP1R10/PNUTS (By similarity). Interacts with FOXO1 and CREB1
CC       (increased by cAMP); FOXO1 and CREB1 are required for full induction of
CC       TOX4-dependent activity and the interactions are inhibited by insulin
CC       (By similarity). {ECO:0000250|UniProtKB:O94842,
CC       ECO:0000250|UniProtKB:Q8BU11}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8BU11}.
CC       Note=Associated with chromatin. {ECO:0000250|UniProtKB:Q8BU11}.
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DR   EMBL; BC119929; AAI19930.1; -; mRNA.
DR   RefSeq; NP_001069175.1; NM_001075707.1.
DR   AlphaFoldDB; Q0P5K4; -.
DR   SMR; Q0P5K4; -.
DR   STRING; 9913.ENSBTAP00000020149; -.
DR   PaxDb; Q0P5K4; -.
DR   PRIDE; Q0P5K4; -.
DR   Ensembl; ENSBTAT00000020149; ENSBTAP00000020149; ENSBTAG00000015146.
DR   GeneID; 515314; -.
DR   KEGG; bta:515314; -.
DR   CTD; 9878; -.
DR   VEuPathDB; HostDB:ENSBTAG00000015146; -.
DR   VGNC; VGNC:36230; TOX4.
DR   eggNOG; KOG0381; Eukaryota.
DR   GeneTree; ENSGT00940000154888; -.
DR   HOGENOM; CLU_030650_0_0_1; -.
DR   InParanoid; Q0P5K4; -.
DR   OMA; WCSIKNQ; -.
DR   OrthoDB; 1465513at2759; -.
DR   TreeFam; TF106481; -.
DR   Proteomes; UP000009136; Chromosome 10.
DR   Bgee; ENSBTAG00000015146; Expressed in semen and 107 other tissues.
DR   GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0072357; C:PTW/PP1 phosphatase complex; ISS:UniProtKB.
DR   GO; GO:0031490; F:chromatin DNA binding; 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   InterPro; IPR037985; TOX4.
DR   PANTHER; PTHR45781:SF2; PTHR45781:SF2; 1.
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; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..619
FT                   /note="TOX high mobility group box family member 4"
FT                   /id="PRO_0000364348"
FT   DNA_BIND        223..291
FT                   /note="HMG box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT   REGION          153..227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          304..337
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          507..529
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           213..218
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        168..183
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        309..334
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         176
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BU11"
FT   MOD_RES         178
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O94842"
FT   MOD_RES         181
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O94842"
FT   MOD_RES         182
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O94842"
FT   MOD_RES         313
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O94842"
FT   MOD_RES         315
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O94842"
FT   MOD_RES         479
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:O94842"
FT   MOD_RES         548
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O94842"
FT   MOD_RES         550
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O94842"
FT   MOD_RES         558
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O94842"
FT   MOD_RES         560
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O94842"
FT   MOD_RES         565
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O94842"
SQ   SEQUENCE   619 AA;  66087 MW;  AB3B7D2EF6485295 CRC64;
     MEFPGGNDNY LTITGPSHPF LSGAETFHTP SLGDEEFEIP PISLDSDPSL AVSDVVGHFD
     DLADPSSSQD GSFSAQYGVQ TLDMPVGMTH GLMEQGGGLL SGGLTMDLDH SIGTQYSANP
     PVTIDVPMTD MTSGLMGHSQ LTTIDQSELS SQLGLSLGGG TILPPAQSPE DRLSTTPSPT
     SSLHEDGVEE FRRQPPSQKT VVVEAGKKQK APKKRKKKDP NEPQKPVSAY ALFFRDTQAA
     IKGQNPNATF GEVSKIVASM WDSLGEEQKQ VYKRKTEAAK KEYLKALAAY KDNQECQATV
     ETVDMDPAPP SQTPSPPPVA AADPASPAPA STEPPALSPS IVVNSTLSSY VANQASSGAG
     GQPNITKLII TKQMLPSSIT MSQGGMVTVI PATVVTSRGL QLGQTSTATI QPSQQAQIVT
     RSVLQAAAAA AASMQLPPPR LQPPPLQQMP QPPTQQQVTI LQQPPPLQAM QQPPPQKFRI
     NLQQQPPPLQ VKIVPPPTLK MQTTLVPPPV ESSPEQPVNN SPETHTVEET TPETICEMIT
     DVVPEVESPS QMDVELVSGS PMTLSPQPRC VRSGCENPPV VSKDWDNEYC SNECVVKHCR
     DVFLAWVASR NSNTVVFVK