ID   TOX4_PONAB              Reviewed;         621 AA.
AC   Q5R6A9; Q5R4X6;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 2.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=TOX high mobility group box family member 4;
GN   Name=TOX4;
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=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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; CR860582; CAH92707.1; -; mRNA.
DR   EMBL; CR861113; CAH93190.1; -; mRNA.
DR   RefSeq; NP_001126876.1; NM_001133404.1.
DR   RefSeq; NP_001128875.1; NM_001135403.1.
DR   AlphaFoldDB; Q5R6A9; -.
DR   SMR; Q5R6A9; -.
DR   STRING; 9601.ENSPPYP00000006367; -.
DR   Ensembl; ENSPPYT00000006622; ENSPPYP00000006367; ENSPPYG00000005598.
DR   GeneID; 100173889; -.
DR   GeneID; 100189804; -.
DR   KEGG; pon:100173889; -.
DR   CTD; 9878; -.
DR   eggNOG; KOG0381; Eukaryota.
DR   GeneTree; ENSGT00940000154888; -.
DR   InParanoid; Q5R6A9; -.
DR   OrthoDB; 1465513at2759; -.
DR   Proteomes; UP000001595; Chromosome 14.
DR   GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0072357; C:PTW/PP1 phosphatase complex; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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..621
FT                   /note="TOX high mobility group box family member 4"
FT                   /id="PRO_0000364349"
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          305..333
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          510..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..333
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         481
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:O94842"
FT   MOD_RES         533
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         552
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         562
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O94842"
FT   MOD_RES         567
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O94842"
FT   CONFLICT        157
FT                   /note="L -> P (in Ref. 1; CAH93190)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        161
FT                   /note="T -> A (in Ref. 1; CAH93190)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        215
FT                   /note="R -> E (in Ref. 1; CAH92707)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        362
FT                   /note="Q -> R (in Ref. 1; CAH93190)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        402
FT                   /note="L -> P (in Ref. 1; CAH92707)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   621 AA;  66199 MW;  D5EAEA6BE43168F5 CRC64;
     MEFPGGNDNY LTITGPSHPF LSGAETFHTP SLGDEEFEIP PISLDSDPSL AVSDVVGHFD
     DLADPSSSQD GSFSAQYGVQ TLDMPVGMTH GLMEQGGGLL SGGLTMDLDH SIGTQYSANP
     PVTIDVPMTD MTSGLMGHSQ LTTIDQSELS SQLGLSLGGG TILPPAQSPE DRLSTTPSPT
     SSLHEDGVED FRRQLPSQKT VVVEAGKKQK APKKRKKKDP NEPQKPVSAY ALFFRDTQAA
     IKGQNPNATF GEVSKIVASM WDSLGEEQKQ VYKRKTEAAK KEYLKALAAY KDNQECQATV
     ETVELDPAPP SQTPSPPPMA TVDPASPAPA SIEPPALSPS IVVNSTLSSY VANQASSGAG
     GQPNITKLII TKQMLPSSIT MSQGGMVTVI PATVVTSRGL QLGQTSTATI QPSQQAQIVT
     RSVLQAAAAA AAAASMQLPP PRLQPPPLQQ MPQPPTQQQV TILQQPPPLQ AMQQPPPQKV
     RINLQQQPPP LQIKSVPLPT LKMQTTLVPP TVESSPERPM NNSPEAHTVE ATSPETICEM
     ITDVVPEVES PSQMDVELVS GSPVALSPQP RCVRSGCENP PIVSKDWDNE YCSNECVVKH
     CRDVFLAWVA SRNSNTVVFV K