HSF3_MOUSE
ID HSF3_MOUSE Reviewed; 492 AA.
AC D0VYS2; D0VYS3;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Heat shock factor protein 3 {ECO:0000303|PubMed:19864465};
DE Short=HSF 3;
DE AltName: Full=Heat shock transcription factor 3 {ECO:0000303|PubMed:19864465};
DE Short=HSTF 3;
DE Short=mHSF3 {ECO:0000303|PubMed:19864465};
GN Name=Hsf3 {ECO:0000303|PubMed:19864465};
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;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAI50338.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ICR {ECO:0000312|EMBL:BAI50338.1};
RC TISSUE=Brain {ECO:0000312|EMBL:BAI50338.1};
RX PubMed=19864465; DOI=10.1091/mbc.e09-07-0639;
RA Fujimoto M., Hayashida N., Katoh T., Oshima K., Shinkawa T., Prakasam R.,
RA Tan K., Inouye S., Takii R., Nakai A.;
RT "A novel mouse HSF3 has the potential to activate nonclassical heat-shock
RT genes during heat shock.";
RL Mol. Biol. Cell 21:106-116(2010).
CC -!- FUNCTION: DNA-binding protein that specifically binds heat shock
CC promoter elements (HSE) and activates transcription of non-classical
CC heat-shock genes such as PDZD2 and PROM2. Protects cells against heat
CC shock and proteotoxic stress. {ECO:0000269|PubMed:19864465}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm
CC {ECO:0000269|PubMed:19864465}. Nucleus {ECO:0000269|PubMed:19864465}.
CC Note=Cytoplasmic under normal conditions. Translocates to the nucleus
CC in response to heat shock. {ECO:0000269|PubMed:19864465}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000269|PubMed:19864465}. Note=Does not translocate to the nucleus
CC in response to heat shock. {ECO:0000269|PubMed:19864465}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:19864465}; Synonyms=Hsf3a
CC {ECO:0000269|PubMed:19864465};
CC IsoId=D0VYS2-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:19864465}; Synonyms=Hsf3b
CC {ECO:0000269|PubMed:19864465};
CC IsoId=D0VYS2-2; Sequence=VSP_053203, VSP_053204, VSP_053205;
CC -!- SIMILARITY: Belongs to the HSF family. {ECO:0000255}.
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DR EMBL; AB510446; BAI50338.1; -; mRNA.
DR EMBL; AB510447; BAI50339.1; -; mRNA.
DR CCDS; CCDS81156.1; -. [D0VYS2-1]
DR CCDS; CCDS85791.1; -. [D0VYS2-2]
DR RefSeq; NP_001297684.1; NM_001310755.1.
DR AlphaFoldDB; D0VYS2; -.
DR SMR; D0VYS2; -.
DR STRING; 10090.ENSMUSP00000052508; -.
DR iPTMnet; D0VYS2; -.
DR PhosphoSitePlus; D0VYS2; -.
DR PaxDb; D0VYS2; -.
DR PRIDE; D0VYS2; -.
DR ProteomicsDB; 273277; -. [D0VYS2-2]
DR DNASU; 245525; -.
DR GeneID; 245525; -.
DR KEGG; mmu:245525; -.
DR CTD; 245525; -.
DR MGI; MGI:3045337; Hsf3.
DR eggNOG; KOG0627; Eukaryota.
DR InParanoid; D0VYS2; -.
DR BioGRID-ORCS; 245525; 2 hits in 56 CRISPR screens.
DR ChiTaRS; Hsf3; mouse.
DR PRO; PR:D0VYS2; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; D0VYS2; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0031490; F:chromatin DNA binding; IDA:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0034605; P:cellular response to heat; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR027729; HSF3.
DR InterPro; IPR000232; HSF_DNA-bd.
DR InterPro; IPR027725; HSF_fam.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR10015; PTHR10015; 1.
DR PANTHER; PTHR10015:SF148; PTHR10015:SF148; 1.
DR Pfam; PF00447; HSF_DNA-bind; 1.
DR PRINTS; PR00056; HSFDOMAIN.
DR SMART; SM00415; HSF; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
PE 2: Evidence at transcript level;
KW Activator; Alternative splicing; Cytoplasm; DNA-binding; Nucleus;
KW Reference proteome; Stress response; Transcription;
KW Transcription regulation.
FT CHAIN 1..492
FT /note="Heat shock factor protein 3"
FT /id="PRO_0000392634"
FT DNA_BIND 9..114
FT /evidence="ECO:0000250|UniProtKB:P22813"
FT REGION 1..33
FT /note="Required for nuclear translocation in heat-shocked
FT cells"
FT /evidence="ECO:0000269|PubMed:19864465"
FT REGION 260..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..33
FT /note="MEQFRKTMVPHFLTKLWILVDDAVLDHVIRWGK -> MLRPVERGYFYSPDS
FT PNSRRVQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19864465"
FT /id="VSP_053203"
FT VAR_SEQ 377..379
FT /note="SLS -> TII (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19864465"
FT /id="VSP_053204"
FT VAR_SEQ 380..492
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19864465"
FT /id="VSP_053205"
FT CONFLICT 72
FT /note="S -> F (in Ref. 1; BAI50339)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 492 AA; 57302 MW; A63387952609C32F CRC64;
MEQFRKTMVP HFLTKLWILV DDAVLDHVIR WGKDGHSFQI VNEETFAREV LPKYFKHNKI
TSFIRQLNMY GSRKVFALQT EKTSQENKIS IEFQHPLFKR GEACLLANIK RKVPTIKIEG
ASLYSDEFQK IVTEMQEFKD MQRKMDAKYT QMKQDYSNLY HEVTNLRKKY CAQQQLLTRV
LHFILDLMSE NHTVLKKRKR SLSFISEDSD SEWDHQYFRI PEDKKEAMEI LKDGYELVED
KYKSLLDRVM PILKESKKLI SSGDQPSGDD GEHPKVPVQD KPMNEESLTI QLDLTIPVLP
EQITEESVEQ EPKDISLELD LSSQDSILMK DKSDNLYNNI INRDKKDMHH TEGNLLELNS
LLSRKALNYD SDHFSESLSL MKNEEEKSQL DLSGGKDNHM IQCMETPELF LLDEIPMCDF
GENLQDYDRL LEDLKNPPNV ISALCDHDYV TSNISTLQED TIENSIPQLC MEANGESSVF
PFLILNPVTN IF
