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Database: UniProt
Entry: Q52L52_MOUSE
LinkDB: Q52L52_MOUSE
Original site: Q52L52_MOUSE 
ID   Q52L52_MOUSE            Unreviewed;       477 AA.
AC   Q52L52;
DT   24-MAY-2005, integrated into UniProtKB/TrEMBL.
DT   24-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 124.
DE   SubName: Full=Heat shock factor 1 {ECO:0000313|Ensembl:ENSMUSP00000154328.2};
DE   SubName: Full=Hsf1 protein {ECO:0000313|EMBL:AAH94064.1};
GN   Name=Hsf1 {ECO:0000313|EMBL:AAH94064.1,
GN   ECO:0000313|Ensembl:ENSMUSP00000154328.2, ECO:0000313|MGI:MGI:96238};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000313|EMBL:AAH94064.1};
RN   [1] {ECO:0000313|EMBL:AAH94064.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N {ECO:0000313|EMBL:AAH94064.1};
RC   TISSUE=Liver {ECO:0000313|EMBL:AAH94064.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RA   Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA   Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA   Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA   Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA   Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA   Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA   Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA   Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA   Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA   Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA   Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA   Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA   Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA   Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA   Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA   Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA   Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA   Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA   Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2] {ECO:0007829|PubMed:19131326}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of electron
RT   capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [3] {ECO:0000313|Ensembl:ENSMUSP00000154328.2, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000154328.2,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4] {ECO:0000313|Ensembl:ENSMUSP00000154328.2}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000154328.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the HSF family. {ECO:0000256|ARBA:ARBA00006403,
CC       ECO:0000256|RuleBase:RU004020}.
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DR   EMBL; BC094064; AAH94064.1; -; mRNA.
DR   RefSeq; NP_001318143.1; NM_001331214.1.
DR   ProteomicsDB; 332401; -.
DR   Antibodypedia; 1848; 2014 antibodies from 50 providers.
DR   DNASU; 15499; -.
DR   Ensembl; ENSMUST00000226872.2; ENSMUSP00000154328.2; ENSMUSG00000022556.12.
DR   GeneID; 15499; -.
DR   UCSC; uc007wki.1; mouse.
DR   AGR; MGI:96238; -.
DR   CTD; 3297; -.
DR   MGI; MGI:96238; Hsf1.
DR   VEuPathDB; HostDB:ENSMUSG00000022556; -.
DR   GeneTree; ENSGT00940000158421; -.
DR   OrthoDB; 1117127at2759; -.
DR   BioGRID-ORCS; 15499; 5 hits in 81 CRISPR screens.
DR   ChiTaRS; Hsf1; mouse.
DR   Proteomes; UP000000589; Chromosome 15.
DR   Bgee; ENSMUSG00000022556; Expressed in animal zygote and 258 other cell types or tissues.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR000232; HSF_DNA-bd.
DR   InterPro; IPR027725; HSF_fam.
DR   InterPro; IPR010542; Vert_HSTF_C.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR10015:SF274; HEAT SHOCK FACTOR PROTEIN 1; 1.
DR   PANTHER; PTHR10015; HEAT SHOCK TRANSCRIPTION FACTOR; 1.
DR   Pfam; PF00447; HSF_DNA-bind; 1.
DR   Pfam; PF06546; Vert_HS_TF; 1.
DR   PRINTS; PR00056; HSFDOMAIN.
DR   SMART; SM00415; HSF; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS00434; HSF_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Activator {ECO:0000256|ARBA:ARBA00023159};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Proteomics identification {ECO:0007829|EPD:Q52L52,
KW   ECO:0007829|MaxQB:Q52L52};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589}.
FT   DOMAIN          57..81
FT                   /note="HSF-type DNA-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS00434"
FT   REGION          272..327
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          340..363
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          444..477
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        340..360
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   477 AA;  51704 MW;  5930E8560A84430B CRC64;
     MDLAVGPGAA GPSNVPAFLT KLWTLVSDPD TDALICWSPS GNSFHVFDQG QFAKEVLPKY
     FKHNNMASFV RQLNMYGFRK VVHIEQGGLV KPERDDTEFQ HPCFLRGQEQ LLENIKRKVT
     SVSTLKSEDI KIRQDSVTRL LTDVQLMKGK QECMDSKLLA MKHENEALWR EVASLRQKHA
     QQQKVVNKLI QFLISLVQSN RILGVKRKIP LMLSDSNSAH SVPKYGRQYS LEHVHGPGPY
     SAPSPAYSSS SLYSSDAVTS SGPIISDITE LAPTSPLASP GRSIDERPLS SSTLVRVKQE
     PPSPPHSPRV LEASPGRPSS MDTPLSPTAF IDSILRESEP TPAASNTAPM DTTGAQAPAL
     PTPSTPEKCL SVACLDNLAR APQMSGVARL FPCPSSFLHG RVQPGNELSD HLDAMDSNLD
     NLQTMLTSHG FSVDTSALLD IQELLSPQEP PRPIEAENSN PDSAGALHGS ASVPAGS
//
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