位置:首页 > 蛋白库 > FX1AA_DANRE
FX1AA_DANRE
ID   FX1AA_DANRE             Reviewed;         652 AA.
AC   A3RK74; F1RBQ1; F8W360;
DT   03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Forkhead box protein O1-A;
GN   Name=foxo1a; Synonyms=foxo1, foxO1a.1;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RX   PubMed=17993506; DOI=10.1093/hmg/ddm326;
RA   Berry F.B., Skarie J.M., Mirzayans F., Fortin Y., Hudson T.J., Raymond V.,
RA   Link B.A., Walter M.A.;
RT   "FOXC1 is required for cell viability and resistance to oxidative stress in
RT   the eye through the transcriptional regulation of FOXO1A.";
RL   Hum. Mol. Genet. 17:490-505(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
CC   -!- FUNCTION: Transcription factor that regulates metabolic homeostasis in
CC       response to oxidative stress (By similarity). Binds to the consensus
CC       sequence 5'-TT[G/A]TTTTG-3' and the related Daf-16 family binding
CC       element (DBE) with consensus sequence 5'-TT[G/A]TTTAC-3' (By
CC       similarity). Main regulator of redox balance and osteoblast numbers and
CC       controls bone mass. Orchestrates the endocrine function of the skeleton
CC       in regulating glucose metabolism (By similarity). May be involved in
CC       regulating cellular homeostasis in the eye (PubMed:17993506).
CC       {ECO:0000250|UniProtKB:Q9R1E0, ECO:0000269|PubMed:17993506}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9R1E0}. Nucleus
CC       {ECO:0000250|UniProtKB:Q9R1E0}. Note=Shuttles between the cytoplasm and
CC       nucleus. {ECO:0000250|UniProtKB:Q9R1E0}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the developing eye. In 48h embryos,
CC       enriched within the periocular mesenchyme (POM), in the branchial arch
CC       region and in the developing pancreas. {ECO:0000269|PubMed:17993506}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; EF421424; ABO10192.1; -; mRNA.
DR   EMBL; BX649258; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001070725.2; NM_001077257.2.
DR   RefSeq; XP_009289702.1; XM_009291427.2.
DR   AlphaFoldDB; A3RK74; -.
DR   SMR; A3RK74; -.
DR   STRING; 7955.ENSDARP00000087386; -.
DR   PaxDb; A3RK74; -.
DR   Ensembl; ENSDART00000171723; ENSDARP00000134884; ENSDARG00000099555.
DR   Ensembl; ENSDART00000179778; ENSDARP00000155088; ENSDARG00000099555.
DR   GeneID; 768121; -.
DR   KEGG; dre:768121; -.
DR   CTD; 768121; -.
DR   ZFIN; ZDB-GENE-061013-59; foxo1a.
DR   eggNOG; KOG2294; Eukaryota.
DR   GeneTree; ENSGT00940000161558; -.
DR   HOGENOM; CLU_023456_1_1_1; -.
DR   InParanoid; A3RK74; -.
DR   OMA; MNGCGLI; -.
DR   OrthoDB; 1160384at2759; -.
DR   PhylomeDB; A3RK74; -.
DR   Reactome; R-DRE-198693; AKT phosphorylates targets in the nucleus.
DR   Reactome; R-DRE-211163; AKT-mediated inactivation of FOXO1A.
DR   Reactome; R-DRE-5687128; MAPK6/MAPK4 signaling.
DR   Reactome; R-DRE-9614399; Regulation of localization of FOXO transcription factors.
DR   Reactome; R-DRE-9617629; Regulation of FOXO transcriptional activity by acetylation.
DR   Reactome; R-DRE-9617828; FOXO-mediated transcription of cell cycle genes.
DR   PRO; PR:A3RK74; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 15.
DR   Bgee; ENSDARG00000099555; Expressed in cardiac ventricle and 21 other tissues.
DR   ExpressionAtlas; A3RK74; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0006094; P:gluconeogenesis; IGI:ZFIN.
DR   GO; GO:0001945; P:lymph vessel development; IGI:ZFIN.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0048659; P:smooth muscle cell proliferation; IMP:ZFIN.
DR   GO; GO:0048745; P:smooth muscle tissue development; IMP:ZFIN.
DR   CDD; cd00059; FH; 1.
DR   Gene3D; 1.10.10.10; -; 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   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; SSF46785; 1.
DR   PROSITE; PS00658; FORK_HEAD_2; 1.
DR   PROSITE; PS50039; FORK_HEAD_3; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; DNA-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..652
FT                   /note="Forkhead box protein O1-A"
FT                   /id="PRO_0000419246"
FT   DNA_BIND        134..228
FT                   /note="Fork-head"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00089"
FT   REGION          1..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          208..277
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          359..406
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..57
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   652 AA;  69348 MW;  CC2103BAAB1083AA CRC64;
     MADAAQNQMV EIDPDFEPLS RPRSCTWPLP RPEFPNPAAA DSNTSSPAPS VKQEPSSTAD
     FINNLSLLEE NEDYPDQKPL MLCSEFQCQE NCIHQQQIPS QQQQVPVLSS PVAAAAAAAA
     AAQRKSSSSR RNAWGNMSYA DLITKAIESS PEKRLTLSQI YDWMVKSVPY FKDKGDSNSS
     AGWKNSIRHN LSLHSRFIRV QNEGTGKSSW WMLNPEGGKS GKSPRRRAAS MDNNSKFAKS
     RGRAAKKKLA LQGGPEGGAD SPGSQYGKWP GSPNSHSNDD FEAWTAFRPR TSSNASTLSG
     RLSPFIDDEL GDSDVHMVYP GPGSGTKMTS TLPSLSEMAG SLGHSGSENV MENLLDNLNL
     LSPKNPSTGG PGSGSNQSSP SSLMQASPGY SPYSSPGLSA VSQQTQQDFR KCLYGQAGMG
     SMSPMPMQPL PESKPSFGPG GGTMGQFNCT AGLLKELLTS DGEPGDLMPS VDTVVSQSAG
     GSGCMLPPYS SGRNELMGGG PTHSHTLSHP HNMHGQAPPT SVALNGRSLH PLTAIGHSSV
     GGRLGSGKSP MQMQYGGSGH LGGGLPPYCS MSSNGYGRGP GMMAHQQLQH LEKLPSDLDG
     MPIERFECDV ESILHDTLMD GESLDFNFDP MNSQQGFVPH SVKTTTHSWV SG
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024