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Forkhead box protein O4 (Afxh) (Fork head domain transcription factor AFX1)

 FOXO4_MOUSE             Reviewed;         505 AA.
Q9WVH3;
11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
12-SEP-2018, entry version 152.
RecName: Full=Forkhead box protein O4;
AltName: Full=Afxh;
AltName: Full=Fork head domain transcription factor AFX1;
Name=Foxo4; Synonyms=Afx, Afx1, Fkhr3, Mllt7;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Embryo;
PubMed=11353388; DOI=10.1007/s003350020002;
Biggs W.H. III, Cavenee W.K., Arden K.C.;
"Identification and characterization of members of the FKHR (FOX O)
subclass of winged-helix transcription factors in the mouse.";
Mamm. Genome 12:416-425(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Furuyama T., Nakazawa T., Mori N.;
"Mouse AFX, a forkhead type transcription factor.";
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
[3]
FUNCTION, AND INDUCTION.
PubMed=16054032; DOI=10.1016/j.devcel.2005.05.017;
Liu Z.-P., Wang Z., Yanagisawa H., Olson E.N.;
"Phenotypic modulation of smooth muscle cells through interaction of
Foxo4 and myocardin.";
Dev. Cell 9:261-270(2005).
[4]
TISSUE SPECIFICITY.
PubMed=22510882; DOI=10.1038/emboj.2012.97;
Nakae J., Cao Y., Hakuno F., Takemori H., Kawano Y., Sekioka R.,
Abe T., Kiyonari H., Tanaka T., Sakai J., Takahashi S., Itoh H.;
"Novel repressor regulates insulin sensitivity through interaction
with Foxo1.";
EMBO J. 31:2275-2295(2012).
[5]
INTERACTION WITH FOXK1.
PubMed=22956541; DOI=10.1242/jcs.105239;
Shi X., Wallis A.M., Gerard R.D., Voelker K.A., Grange R.W.,
DePinho R.A., Garry M.G., Garry D.J.;
"Foxk1 promotes cell proliferation and represses myogenic
differentiation by regulating Foxo4 and Mef2.";
J. Cell Sci. 125:5329-5337(2012).
-!- FUNCTION: Transcription factor involved in the regulation of the
insulin signaling pathway. Binds to insulin-response elements
(IREs) and can activate transcription of IGFBP1. Down-regulates
expression of HIF1A and suppresses hypoxia-induced transcriptional
activation of HIF1A-modulated genes. Also involved in negative
regulation of the cell cycle. Involved in increased proteasome
activity in embryonic stem cells (ESCs) by activating expression
of PSMD11 in ESCs, leading to enhanced assembly of the 26S
proteasome, followed by higher proteasome activity (By
similarity). Represses smooth muscle cell differentiation by
inhibiting the transcriptional coactivator activity of myocardin.
{ECO:0000250|UniProtKB:P98177, ECO:0000269|PubMed:16054032}.
-!- SUBUNIT: Interacts with CREBBP/CBP, MYOCD, SIRT1, SRF and YWHAZ.
Acetylated by CREBBP/CBP and deacetylated by SIRT1. Binding of
YWHAZ inhibits DNA-binding. Interacts with USP7; the interaction
is enhanced in presence of hydrogen peroxide and occurs
independently of TP53. Interacts with NLK, and this inhibits
monoubiquitination and transcriptional activity (By similarity).
Interacts with FOXK1; the interaction inhibits MEF2C
transactivation activity (PubMed:22956541).
{ECO:0000250|UniProtKB:P98177, ECO:0000269|PubMed:22956541}.
-!- INTERACTION:
P56558:Ogt (xeno); NbExp=2; IntAct=EBI-4567305, EBI-7614183;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=When
phosphorylated, translocated from nucleus to cytoplasm.
Dephosphorylation triggers nuclear translocation.
Monoubiquitination increases nuclear localization. When
deubiquitinated, translocated from nucleus to cytoplasm (By
similarity). {ECO:0000250|UniProtKB:P98177}.
-!- TISSUE SPECIFICITY: Strongly expressed in brown adipose tissue and
weakly in white adipose tissue (at protein level). Expressed in
skeletal muscle. {ECO:0000269|PubMed:11353388,
ECO:0000269|PubMed:22510882}.
-!- INDUCTION: By artery ligation in proliferating neointimal smooth
muscle cells. {ECO:0000269|PubMed:16054032}.
-!- PTM: Acetylation by CREBBP/CBP is induced by oxidative stress and
inhibits transcriptional activity. Deacetylation by SIRT1 is NAD-
dependent and stimulates transcriptional activity (By similarity).
{ECO:0000250|UniProtKB:P98177}.
-!- PTM: Phosphorylation by PKB/AKT1 inhibits transcriptional activity
and is responsible for cytoplasmic localization. May be
phosphorylated at multiple sites by NLK (By similarity).
{ECO:0000250|UniProtKB:P98177}.
-!- PTM: Monoubiquitinated; monoubiquitination is induced by oxidative
stress and reduced by deacetylase inhibitors; results in its
relocalization to the nucleus and its increased transcriptional
activity. Deubiquitinated by USP7; deubiquitination is induced by
oxidative stress; enhances its interaction with USP7 and
consequently, deubiquitination; increases its translocation to the
cytoplasm and inhibits its transcriptional activity. Hydrogene-
peroxide-induced ubiquitination and USP7-mediated deubiquitination
have no major effect on its protein stability (By similarity).
{ECO:0000250|UniProtKB:P98177}.
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EMBL; AF114260; AAD42108.1; -; mRNA.
EMBL; AB032770; BAA86199.1; -; mRNA.
CCDS; CCDS41077.1; -.
RefSeq; NP_061259.1; NM_018789.2.
UniGene; Mm.240299; -.
ProteinModelPortal; Q9WVH3; -.
SMR; Q9WVH3; -.
BioGrid; 207680; 1.
CORUM; Q9WVH3; -.
IntAct; Q9WVH3; 3.
MINT; Q9WVH3; -.
STRING; 10090.ENSMUSP00000059420; -.
iPTMnet; Q9WVH3; -.
PhosphoSitePlus; Q9WVH3; -.
MaxQB; Q9WVH3; -.
PaxDb; Q9WVH3; -.
PRIDE; Q9WVH3; -.
Ensembl; ENSMUST00000062000; ENSMUSP00000059420; ENSMUSG00000042903.
GeneID; 54601; -.
KEGG; mmu:54601; -.
UCSC; uc009twz.2; mouse.
CTD; 4303; -.
MGI; MGI:1891915; Foxo4.
eggNOG; KOG2294; Eukaryota.
eggNOG; COG5025; LUCA.
GeneTree; ENSGT00920000149005; -.
HOGENOM; HOG000251635; -.
HOVERGEN; HBG057789; -.
InParanoid; Q9WVH3; -.
KO; K12358; -.
OMA; ENLECDM; -.
OrthoDB; EOG091G06K3; -.
PhylomeDB; Q9WVH3; -.
TreeFam; TF315583; -.
Reactome; R-MMU-198693; AKT phosphorylates targets in the nucleus.
Reactome; R-MMU-5689880; Ub-specific processing proteases.
ChiTaRS; Foxo4; mouse.
PRO; PR:Q9WVH3; -.
Proteomes; UP000000589; Chromosome X.
Bgee; ENSMUSG00000042903; Expressed in 227 organ(s), highest expression level in placenta.
CleanEx; MM_FOXO4; -.
ExpressionAtlas; Q9WVH3; baseline and differential.
Genevisible; Q9WVH3; MM.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0016607; C:nuclear speck; ISO:MGI.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0008013; F:beta-catenin binding; ISO:MGI.
GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
GO; GO:0019899; F:enzyme binding; ISS:UniProtKB.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:1990841; F:promoter-specific chromatin binding; ISO:MGI.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
GO; GO:0008134; F:transcription factor binding; ISS:UniProtKB.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
GO; GO:0007050; P:cell cycle arrest; ISS:UniProtKB.
GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
GO; GO:0008286; P:insulin receptor signaling pathway; ISS:UniProtKB.
GO; GO:0007095; P:mitotic G2 DNA damage checkpoint; IDA:MGI.
GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
GO; GO:0016525; P:negative regulation of angiogenesis; ISS:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:MGI.
GO; GO:0070317; P:negative regulation of G0 to G1 transition; ISS:UniProtKB.
GO; GO:0051151; P:negative regulation of smooth muscle cell differentiation; ISS:UniProtKB.
GO; GO:0071158; P:positive regulation of cell cycle arrest; ISO:MGI.
GO; GO:0014911; P:positive regulation of smooth muscle cell migration; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl.
GO; GO:1990785; P:response to water-immersion restraint stress; IEA:Ensembl.
GO; GO:0048863; P:stem cell differentiation; ISS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd00059; FH; 1.
Gene3D; 1.10.10.10; -; 1.
InterPro; IPR001766; Fork_head_dom.
InterPro; IPR032067; FOXO-TAD.
InterPro; IPR030456; TF_fork_head_CS_2.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
Pfam; PF00250; Forkhead; 1.
Pfam; PF16676; FOXO-TAD; 1.
PRINTS; PR00053; FORKHEAD.
SMART; SM00339; FH; 1.
SUPFAM; SSF46785; SSF46785; 1.
PROSITE; PS00658; FORK_HEAD_2; 1.
PROSITE; PS50039; FORK_HEAD_3; 1.
1: Evidence at protein level;
Acetylation; Activator; Cell cycle; Complete proteome; Cytoplasm;
Developmental protein; Differentiation; DNA-binding; Myogenesis;
Nucleus; Phosphoprotein; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 505 Forkhead box protein O4.
/FTId=PRO_0000091876.
DNA_BIND 100 188 Fork-head. {ECO:0000255|PROSITE-
ProRule:PRU00089}.
REGION 97 215 Required for interaction with FOXK1.
{ECO:0000269|PubMed:22956541}.
MOD_RES 32 32 Phosphothreonine; by PKB/AKT1.
{ECO:0000250|UniProtKB:P98177}.
MOD_RES 197 197 Phosphoserine; by PKB/AKT1.
{ECO:0000250|UniProtKB:P98177}.
MOD_RES 262 262 Phosphoserine; by PKB/AKT1.
{ECO:0000250|UniProtKB:P98177}.
SEQUENCE 505 AA; 53649 MW; ABB99B54807C7CE5 CRC64;
MDPENKKSAT GAAAILDLDP DFEPQSRPRS CTWPLPRPDL ATEPHEPSEV EPSLGQKVPT
EGHSEPILLP SRLPEPAGGP QPGILGAVTG PRKGGSRRNA WGNQSYAELI SQAIESAPEK
RLTLAQIYEW MVRTVPYFKD KGDSNSSAGW KNSIRHNLSL HSKFIKVHNE ATGKSSWWML
NPDGGKGGKA PRRRAASMDS SSKLLRGRSK GPKKKPSVLP APPEGATPRS PLGHFAKWSS
SPCPRNREEA DVWTTFRPRS SSNASTVSTR LSPMRPESEV LAEEEMPASA SSYAGGVPPT
LSEDLELLDG LNLASPHSLL SRSGLSGFSL QHPGLAGPLH SYGASLFGPI DGSLSAGEGC
FSSSQSLEAL LTSDTPPPPA DVLMTQVDPI LSQAPTLLLL GGMPSSSKLG TGVSLCPTPL
EGPGPSNLVP NLSVMAPPPV MAGAPIPKVL GTPVLASPTE DSSHDRMPQD LDLDMYMENL
ECDMDNIISD LMDGEGLDFN FEPDP


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