UniProt: D3ZBQ1

Database: UniProt
Entry: D3ZBQ1_RAT

LinkDB:  D3ZBQ1_RAT 
Original site:  D3ZBQ1_RAT

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Ontology (69)   
   GO (69)   
Gene (6)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   ENSEMBL-UP (3)   
   RGD (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
Protein domain (12)   
   InterPro (6)   
   Pfam (3)   
   PROSITE (2)   
   SMART (1)   
Literature (2)   
   PubMed (2)   
All databases (90)   

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ID   D3ZBQ1_RAT              Unreviewed;       672 AA.
AC   D3ZBQ1;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   27-MAR-2024, entry version 123.
DE   SubName: Full=Forkhead box O3 {ECO:0000313|Ensembl:ENSRNOP00000000327.3};
GN   Name=Foxo3 {ECO:0000313|Ensembl:ENSRNOP00000000327.3,
GN   ECO:0000313|RGD:1309196};
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 {ECO:0000313|Ensembl:ENSRNOP00000000327.3, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000000327.3, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000000327.3,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0007829|PubMed:22673903}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903;
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).
RN   [3] {ECO:0000313|Ensembl:ENSRNOP00000000327.3}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000000327.3};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00089}.
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DR   RefSeq; NP_001099865.1; NM_001106395.1.
DR   AlphaFoldDB; D3ZBQ1; -.
DR   SMR; D3ZBQ1; -.
DR   IntAct; D3ZBQ1; 1.
DR   MINT; D3ZBQ1; -.
DR   STRING; 10116.ENSRNOP00000000327; -.
DR   PhosphoSitePlus; D3ZBQ1; -.
DR   PaxDb; 10116-ENSRNOP00000000327; -.
DR   Ensembl; ENSRNOT00000000327.6; ENSRNOP00000000327.3; ENSRNOG00000000299.6.
DR   GeneID; 294515; -.
DR   KEGG; rno:294515; -.
DR   AGR; RGD:1309196; -.
DR   CTD; 2309; -.
DR   RGD; 1309196; Foxo3.
DR   eggNOG; KOG2294; Eukaryota.
DR   GeneTree; ENSGT00940000159826; -.
DR   HOGENOM; CLU_023456_1_0_1; -.
DR   OMA; TGGMMQR; -.
DR   OrthoDB; 5385885at2759; -.
DR   TreeFam; TF315583; -.
DR   Reactome; R-RNO-1181150; Signaling by NODAL.
DR   Reactome; R-RNO-198693; AKT phosphorylates targets in the nucleus.
DR   Reactome; R-RNO-5687128; MAPK6/MAPK4 signaling.
DR   Reactome; R-RNO-9607240; FLT3 Signaling.
DR   Reactome; R-RNO-9614399; Regulation of localization of FOXO transcription factors.
DR   Reactome; R-RNO-9617629; Regulation of FOXO transcriptional activity by acetylation.
DR   Reactome; R-RNO-9617828; FOXO-mediated transcription of cell cycle genes.
DR   Reactome; R-RNO-9634638; Estrogen-dependent nuclear events downstream of ESR-membrane signaling.
DR   Proteomes; UP000002494; Chromosome 20.
DR   Bgee; ENSRNOG00000000299; Expressed in jejunum and 18 other cell types or tissues.
DR   ExpressionAtlas; D3ZBQ1; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR   GO; GO:0005829; C:cytosol; ISO:RGD.
DR   GO; GO:0016020; C:membrane; ISO:RGD.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:Ensembl.
DR   GO; GO:0005741; C:mitochondrial outer membrane; ISO:RGD.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR   GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR   GO; GO:0090571; C:RNA polymerase II transcription repressor complex; ISO:RGD.
DR   GO; GO:0008013; F:beta-catenin binding; ISO:RGD.
DR   GO; GO:0031490; F:chromatin DNA binding; ISO:RGD.
DR   GO; GO:0003677; F:DNA binding; ISO:RGD.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:RGD.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:RGD.
DR   GO; GO:0034246; F:mitochondrial transcription factor activity; ISO:RGD.
DR   GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR   GO; GO:0043565; F:sequence-specific DNA binding; ISO:RGD.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:RGD.
DR   GO; GO:0001221; F:transcription coregulator binding; IPI:RGD.
DR   GO; GO:0001547; P:antral ovarian follicle growth; ISO:RGD.
DR   GO; GO:0048854; P:brain morphogenesis; ISO:RGD.
DR   GO; GO:0060070; P:canonical Wnt signaling pathway; ISO:RGD.
DR   GO; GO:1904646; P:cellular response to amyloid-beta; IEP:RGD.
DR   GO; GO:0071386; P:cellular response to corticosterone stimulus; IEP:RGD.
DR   GO; GO:0042149; P:cellular response to glucose starvation; ISO:RGD.
DR   GO; GO:0071333; P:cellular response to glucose stimulus; IEP:RGD.
DR   GO; GO:0071456; P:cellular response to hypoxia; IEP:RGD.
DR   GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEP:RGD.
DR   GO; GO:0034599; P:cellular response to oxidative stress; ISO:RGD.
DR   GO; GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; ISO:RGD.
DR   GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; ISO:RGD.
DR   GO; GO:0042593; P:glucose homeostasis; ISO:RGD.
DR   GO; GO:0001544; P:initiation of primordial ovarian follicle growth; ISO:RGD.
DR   GO; GO:0006390; P:mitochondrial transcription; ISO:RGD.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISO:RGD.
DR   GO; GO:0030336; P:negative regulation of cell migration; ISO:RGD.
DR   GO; GO:0045665; P:negative regulation of neuron differentiation; IMP:RGD.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0097150; P:neuronal stem cell population maintenance; ISO:RGD.
DR   GO; GO:0001556; P:oocyte maturation; ISO:RGD.
DR   GO; GO:0001542; P:ovulation from ovarian follicle; ISO:RGD.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; ISO:RGD.
DR   GO; GO:0010508; P:positive regulation of autophagy; ISO:RGD.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISO:RGD.
DR   GO; GO:2000353; P:positive regulation of endothelial cell apoptotic process; IMP:RGD.
DR   GO; GO:0045648; P:positive regulation of erythrocyte differentiation; ISO:RGD.
DR   GO; GO:1901300; P:positive regulation of hydrogen peroxide-mediated programmed cell death; IMP:RGD.
DR   GO; GO:1902895; P:positive regulation of miRNA transcription; ISO:RGD.
DR   GO; GO:0014737; P:positive regulation of muscle atrophy; ISO:RGD.
DR   GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISO:RGD.
DR   GO; GO:1903428; P:positive regulation of reactive oxygen species biosynthetic process; IMP:RGD.
DR   GO; GO:0045591; P:positive regulation of regulatory T cell differentiation; ISO:RGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; ISO:RGD.
DR   GO; GO:2000177; P:regulation of neural precursor cell proliferation; ISO:RGD.
DR   GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; ISO:RGD.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0006417; P:regulation of translation; ISO:RGD.
DR   GO; GO:0071548; P:response to dexamethasone; IEP:RGD.
DR   GO; GO:0070542; P:response to fatty acid; ISO:RGD.
DR   GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
DR   GO; GO:0042594; P:response to starvation; ISO:RGD.
DR   GO; GO:1990785; P:response to water-immersion restraint stress; IEP:RGD.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR   GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; ISO:RGD.
DR   CDD; cd20061; FH_FOXO3; 1.
DR   Gene3D; 6.10.250.1690; -; 2.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR001766; Fork_head_dom.
DR   InterPro; IPR032067; FOXO-TAD.
DR   InterPro; IPR032068; FOXO_KIX-bd.
DR   InterPro; IPR030456; TF_fork_head_CS_2.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR45767; FORKHEAD BOX PROTEIN O; 1.
DR   PANTHER; PTHR45767:SF4; FORKHEAD BOX PROTEIN O3; 1.
DR   Pfam; PF00250; Forkhead; 1.
DR   Pfam; PF16676; FOXO-TAD; 1.
DR   Pfam; PF16675; FOXO_KIX_bdg; 1.
DR   PRINTS; PR00053; FORKHEAD.
DR   SMART; SM00339; FH; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS00658; FORK_HEAD_2; 1.
DR   PROSITE; PS50039; FORK_HEAD_3; 1.
PE   1: Evidence at protein level;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW   ProRule:PRU00089}; Nucleus {ECO:0000256|PROSITE-ProRule:PRU00089};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494}.
FT   DNA_BIND        156..250
FT                   /note="Fork-head"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00089"
SQ   SEQUENCE   672 AA;  71198 MW;  488905ADCB3A7A2A CRC64;
     MAEAPASPVP LSPLEVELDP EFEPQSRPRS CTWPLQRPEL QASPAKPSGE TAADSMIPEE
     DDDEDDEDSG GRGSSAMVIG GGVSSALGSG LLLEDSARLL SPGGQDLGTG PASSAGALSG
     GTQTQLQPQQ PLPPPQPGAA GGSGQPRKCS SRRNAWGNLS YADLITRAIE SSPDKRLTLS
     QIYEWMVRCV PYFKDKGDSN SSAGWKNSIR HNLSLHSRFM RVQNEGTGKS SWWIINPDGG
     KSGKAPRRRA VSMDNSNKYT KSRGRAAKKK AALQAAPESA DDSPSQLSKW PGSPTSRSSD
     ELDAWTDFRS RTNSNASTVS GRLSPILAST ELDDVQDDDG PLSPMLYSSS ASLSPSVSKP
     CTVELPRLTD MAGTMNLNDG LAENLMDDLL DNIALPPSQA SPPGGLMQRS SSFPYTAKSS
     GLGSPTSSFN STVFGPASLN SLRQSPMQTI QENRPATFSS VSHYGNQTLQ DLLTSDSLSH
     SDVMMTQSDP LMSQASTAVS AQNARRNVML RNDPMMSFAA QPTQGSLVNQ NLLHHQHQTQ
     GALGGSRALS NSVSNMGLSD SSSLGSAKHQ QQSPVSQSMQ TLSDSLSGSS LYSASANLPV
     MGHDKFPSDL DLDMFNGSLE CDMESIIRSE LMDADGLDFN FDSLISTQNV VGLNVGNFTG
     AKQASSQSWV PG
//

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