TOX4_RAT
ID TOX4_RAT Reviewed; 619 AA.
AC Q99PM1;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=TOX high mobility group box family member 4;
DE AltName: Full=Epidermal Langerhans cell protein LCP1;
GN Name=Tox4;
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].
RC STRAIN=LEW.AVN; TISSUE=Bone marrow macrophage;
RA Luy M.A., Koehler B.F., Demleitner K., Reske K.;
RT "Cloning of a novel gene expressed differentially in maturing epidermal
RT Langerhans cells.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178 AND SER-182, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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; AF267197; AAK00807.1; -; mRNA.
DR AlphaFoldDB; Q99PM1; -.
DR SMR; Q99PM1; -.
DR STRING; 10116.ENSRNOP00000017476; -.
DR iPTMnet; Q99PM1; -.
DR PhosphoSitePlus; Q99PM1; -.
DR PaxDb; Q99PM1; -.
DR UCSC; RGD:708449; rat.
DR RGD; 708449; Tox4.
DR eggNOG; KOG0381; Eukaryota.
DR InParanoid; Q99PM1; -.
DR PhylomeDB; Q99PM1; -.
DR PRO; PR:Q99PM1; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0000785; C:chromatin; ISO:RGD.
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 1: Evidence at protein 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_0000048570"
FT DNA_BIND 223..291
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 155..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..458
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 310..324
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..451
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:0007744|PubMed:22673903"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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 531
FT /note="Phosphoserine"
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; 66010 MW; EAC7B6C775B2D203 CRC64;
MEFPGGNDNY LTITGPSHPF LSGAETFHTP SLGDEEFEIP PISLDSDPSL AVSDVVAHFD
DLADPSSSQD GSFSAQYGVQ TLDMPVGMTH GLMEQGGGLL SGGLTMDLDH SIGTQYSANP
PVTIDVPMTD MTSGLMGHSQ LTTIDQSELS SQLGLSLGGG TILPPAQSPE DRLSTTPSPT
NSLHEDGVDD FRRQLPAQKT VVVETGKKQK APKKRKKKDP NEPQKPVSAY ALFFRDTQAA
IKGQNPNATF GEVSKIVASM WDSLGEEQKQ VYKRKTEAAK KEYLKALAAY KDNQECQATV
ETVELDPVPQ SQTPSPPPVT TADPASPAPA STESPALSPC IVVNSTLSSY VANQAFSGPG
GQPNITKLII TKQMLPSSIT MSQGGMVTVI PATVVTSRGL QLGQTSTATI QPSQQAQIAT
RSVLQAAAAA AASMQLPPPR LQPPPLQQMP QPPTQQQVTI LQQPPPLQAM QQPPPQKVRI
NLQQQPPPLQ SKIVPPPALK MQATVLPPTV ESSPEQPMNS SPEAHTVEAT SPETICEMIA
DVVPEVESPS QMDVELVSGS PVTLSPQPRC VRSGCENPPV ISKDWDNEYC SNECVVKHCR
DVFLAWVASR NPNSVVLVK
