HSF2_MOUSE
ID HSF2_MOUSE Reviewed; 535 AA.
AC P38533; Q64157; Q8VEJ0; Q9Z2L8;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Heat shock factor protein 2;
DE Short=HSF 2;
DE AltName: Full=Heat shock transcription factor 2;
DE Short=HSTF 2;
GN Name=Hsf2;
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]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA).
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=1717345; DOI=10.1101/gad.5.10.1902;
RA Sarge K.D., Zimarino V., Holm K., Wu C., Morimoto R.I.;
RT "Cloning and characterization of two mouse heat shock factors with distinct
RT inducible and constitutive DNA-binding ability.";
RL Genes Dev. 5:1902-1911(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM ALPHA).
RC STRAIN=129;
RX PubMed=10333528; DOI=10.1016/s0378-1119(99)00092-x;
RA Manuel M., Sage J., Mattei M.-G., Morange M., Mezger V.;
RT "Genomic structure and chromosomal localization of the mouse Hsf2 gene and
RT promoter sequences.";
RL Gene 232:115-124(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA), TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
RC STRAIN=CBA/J;
RX PubMed=7565677; DOI=10.1128/mcb.15.10.5288;
RA Goodson M.L., Park-Sarge O.-K., Sarge K.D.;
RT "Tissue-dependent expression of heat shock factor 2 isoforms with distinct
RT transcriptional activities.";
RL Mol. Cell. Biol. 15:5288-5293(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
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).
CC -!- FUNCTION: DNA-binding protein that specifically binds heat shock
CC promoter elements (HSE) and activates transcription. In higher
CC eukaryotes, HSF is unable to bind to the HSE unless the cells are heat
CC shocked. HSF2 is expressed in a form that binds DNA constitutively but
CC loses DNA binding by incubation at greater than 41 degrees C.
CC -!- SUBUNIT: DNA-binding homotrimer in stressed or heat shocked cells,
CC otherwise found as a homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Cytoplasmic during
CC normal growth and moves to the nucleus upon activation.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Alpha;
CC IsoId=P38533-1; Sequence=Displayed;
CC Name=Beta;
CC IsoId=P38533-2; Sequence=VSP_002417;
CC -!- TISSUE SPECIFICITY: Isoform alpha is expressed predominantly in testis
CC while isoform beta is expressed predominantly in heart and brain.
CC {ECO:0000269|PubMed:7565677}.
CC -!- DEVELOPMENTAL STAGE: In the 7-day-old testis, isoform beta is expressed
CC at significantly higher levels than isoform alpha. As development
CC proceeds, the levels of isoform alpha gradually increase so that it is
CC the predominant isoform in mature testes. {ECO:0000269|PubMed:7565677}.
CC -!- SIMILARITY: Belongs to the HSF family. {ECO:0000305}.
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; X61754; CAA43893.1; -; mRNA.
DR EMBL; AF045627; AAD02417.1; -; Genomic_DNA.
DR EMBL; AF045615; AAD02417.1; JOINED; Genomic_DNA.
DR EMBL; AF045616; AAD02417.1; JOINED; Genomic_DNA.
DR EMBL; AF045617; AAD02417.1; JOINED; Genomic_DNA.
DR EMBL; AF045618; AAD02417.1; JOINED; Genomic_DNA.
DR EMBL; AF045619; AAD02417.1; JOINED; Genomic_DNA.
DR EMBL; AF045620; AAD02417.1; JOINED; Genomic_DNA.
DR EMBL; AF045621; AAD02417.1; JOINED; Genomic_DNA.
DR EMBL; AF045622; AAD02417.1; JOINED; Genomic_DNA.
DR EMBL; AF045623; AAD02417.1; JOINED; Genomic_DNA.
DR EMBL; AF045624; AAD02417.1; JOINED; Genomic_DNA.
DR EMBL; AF045625; AAD02417.1; JOINED; Genomic_DNA.
DR EMBL; AF045626; AAD02417.1; JOINED; Genomic_DNA.
DR EMBL; S79629; AAB35307.1; -; mRNA.
DR EMBL; BC018414; AAH18414.1; -; mRNA.
DR CCDS; CCDS23852.1; -. [P38533-2]
DR PIR; B40583; B40583.
DR RefSeq; NP_032323.3; NM_008297.3. [P38533-2]
DR AlphaFoldDB; P38533; -.
DR SMR; P38533; -.
DR STRING; 10090.ENSMUSP00000078761; -.
DR iPTMnet; P38533; -.
DR PhosphoSitePlus; P38533; -.
DR MaxQB; P38533; -.
DR PaxDb; P38533; -.
DR PRIDE; P38533; -.
DR ProteomicsDB; 273320; -. [P38533-1]
DR ProteomicsDB; 273321; -. [P38533-2]
DR Antibodypedia; 4231; 724 antibodies from 40 providers.
DR DNASU; 15500; -.
DR Ensembl; ENSMUST00000079833; ENSMUSP00000078761; ENSMUSG00000019878. [P38533-2]
DR GeneID; 15500; -.
DR KEGG; mmu:15500; -.
DR UCSC; uc007fck.2; mouse. [P38533-2]
DR CTD; 3298; -.
DR MGI; MGI:96239; Hsf2.
DR VEuPathDB; HostDB:ENSMUSG00000019878; -.
DR eggNOG; KOG0627; Eukaryota.
DR GeneTree; ENSGT00940000155906; -.
DR HOGENOM; CLU_038829_1_0_1; -.
DR InParanoid; P38533; -.
DR OMA; PTDHDHI; -.
DR OrthoDB; 1154048at2759; -.
DR PhylomeDB; P38533; -.
DR TreeFam; TF330401; -.
DR BioGRID-ORCS; 15500; 2 hits in 77 CRISPR screens.
DR ChiTaRS; Hsf2; mouse.
DR PRO; PR:P38533; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; P38533; protein.
DR Bgee; ENSMUSG00000019878; Expressed in spermatid and 106 other tissues.
DR ExpressionAtlas; P38533; baseline and differential.
DR Genevisible; P38533; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0001162; F:RNA polymerase II intronic transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR027712; HSF2.
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; PTHR10015; 1.
DR PANTHER; PTHR10015:SF185; PTHR10015:SF185; 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; SSF46785; 1.
DR PROSITE; PS00434; HSF_DOMAIN; 1.
PE 2: Evidence at transcript level;
KW Activator; Alternative splicing; Cytoplasm; DNA-binding; Isopeptide bond;
KW Nucleus; Reference proteome; Stress response; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..535
FT /note="Heat shock factor protein 2"
FT /id="PRO_0000124570"
FT DNA_BIND 7..112
FT /evidence="ECO:0000250"
FT REGION 119..192
FT /note="Hydrophobic repeat HR-A/B"
FT REGION 298..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..384
FT /note="Hydrophobic repeat HR-C"
FT REGION 418..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 2
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q03933"
FT CROSSLNK 82
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q03933"
FT CROSSLNK 135
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q03933"
FT CROSSLNK 139
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q03933"
FT CROSSLNK 151
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q03933"
FT CROSSLNK 210
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q03933"
FT CROSSLNK 218
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q03933"
FT CROSSLNK 237
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q03933"
FT VAR_SEQ 392..409
FT /note="Missing (in isoform Beta)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:1717345, ECO:0000303|PubMed:7565677"
FT /id="VSP_002417"
SQ SEQUENCE 535 AA; 60225 MW; 47972520402ABB13 CRC64;
MKQSSNVPAF LSKLWTLVEE THTNEFITWS QNGQSFLVLD EQRFAKEILP KYFKHNNMAS
FVRQLNMYGF RKVVHIESGI IKQERDGPVE FQHPYFKQGQ DDLLENIKRK VSSSKPEENK
IRQEDLTKII SSAQKVQIKQ ETIESRLSEL KSENESLWKE VSELRAKHAQ QQQVIRKIVQ
FIVTLVQNNQ LVSLKRKRPL LLNTNGAPKK NLYQHIVKEP TDNHHHKVPH SRTEGLKSRE
RISDDIIIYD VTDDNVDEEN IPVIPETNED VVVDSSNQYP DIVIVEDDNE DEYAPVIQSG
EQSEPAREPL RVGSAGSSSP LMSSAVQLNG SSSLTSEDPV TMMDSILNDN INLLGKVELL
DYLDSIDCSL EDFQAMLSGR QFSIDPDLLV DLFTSSVQMN PTDNIKYTKS ENKGLEATKS
SVVQHVSEEG RKSKSKPDKQ LIQYTAFPLL AFLDGNSASA IEQGSTTASS EVVPSVDKPI
EVDELLDSSL DPEPTQSKLV RLEPLTEAEA SEATLFYLCE LAPAPLDSDM PLLDS
