HSF1_CHICK
ID HSF1_CHICK Reviewed; 491 AA.
AC P38529; I7GGU6;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Heat shock factor protein 1 {ECO:0000250|UniProtKB:Q00613};
DE Short=HSF 1;
DE AltName: Full=HSF 3A;
DE AltName: Full=HSTF 3A;
DE AltName: Full=Heat shock transcription factor 1 {ECO:0000250|UniProtKB:Q00613};
DE Short=HSTF 1;
GN Name=HSF1 {ECO:0000250|UniProtKB:Q00613};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DNA-BINDING.
RC TISSUE=Blood;
RX PubMed=8455593; DOI=10.1128/mcb.13.4.1983-1997.1993;
RA Nakai A., Morimoto R.I.;
RT "Characterization of a novel chicken heat shock transcription factor, heat
RT shock factor 3, suggests a new regulatory pathway.";
RL Mol. Cell. Biol. 13:1983-1997(1993).
CC -!- FUNCTION: Functions as a stress-inducible and DNA-binding transcription
CC factor that plays a central role in the transcriptional activation of
CC the heat shock response (HSR), leading to the expression of a large
CC class of molecular chaperones heat shock proteins (HSPs) that protect
CC cells from cellular insults' damage (PubMed:8455593). In unstressed
CC cells, is present in a HSP90-containing multichaperone complex that
CC maintains it in a non-DNA-binding inactivated monomeric form. Upon
CC exposure to heat and other stress stimuli, undergoes homotrimerization
CC and activates HSP gene transcription through binding to site-specific
CC heat shock elements (HSEs) present in the promoter regions of HSP
CC genes. Upon heat shock stress, forms a chromatin-associated complex
CC with TTC5/STRAP and p300/EP300 to stimulate HSR transcription,
CC therefore increasing cell survival (By similarity). Activation is
CC reversible, and during the attenuation and recovery phase period of the
CC HSR, returns to its unactivated form. Binds to inverted 5'-NGAAN-3'
CC pentamer DNA sequences. Binds to chromatin at heat shock gene
CC promoters. Also serves several other functions independently of its
CC transcriptional activity. Involved in the repression of Ras-induced
CC transcriptional activation of the c-fos gene in heat-stressed cells.
CC Positively regulates pre-mRNA 3'-end processing and polyadenylation of
CC HSP70 mRNA upon heat-stressed cells. Plays a role in nuclear export of
CC stress-induced mRNA. Plays a role in the regulation of mitotic
CC progression. Also plays a role as a negative regulator of non-
CC homologous end joining (NHEJ) repair activity in a DNA damage-dependent
CC manner. Involved in stress-induced cancer cell proliferation.
CC {ECO:0000250|UniProtKB:Q00613, ECO:0000269|PubMed:8455593}.
CC -!- SUBUNIT: Monomer; cytoplasmic latent and transcriptionally inactive
CC monomeric form in unstressed cells. Homotrimer; in response to stress,
CC such as heat shock, homotrimerizes and translocates into the nucleus,
CC binds to heat shock element (HSE) sequences in promoter of heat shock
CC protein (HSP) genes and acquires transcriptional ability.
CC {ECO:0000250|UniProtKB:Q00613}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q00613}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q00613}. Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q00613}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q00613}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000250|UniProtKB:Q00613}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:Q00613}.
CC Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q00613}.
CC -!- TISSUE SPECIFICITY: Low expression found in most tissues with the
CC exception of blood and liver. Highest levels are found in the pigmental
CC layer of retina and in the lymphoblastoid cell line MSB-1.
CC {ECO:0000269|PubMed:8455593}.
CC -!- DEVELOPMENTAL STAGE: Expressed during development.
CC {ECO:0000269|PubMed:8455593}.
CC -!- DOMAIN: In unstressed cells, spontaneous homotrimerization is
CC inhibited. Intramolecular interactions between the hydrophobic repeat
CC HR-A/B and HR-C regions are necessary to maintain HSF1 in the inactive,
CC monomeric conformation. In heat stressed cells, HSF1 homotrimerization
CC occurs through formation of a three-stranded coiled-coil structure
CC generated by intermolecular interactions between HR-A/B regions
CC allowing DNA-binding activity. The D domain is necessary for
CC translocation to the nucleus. 9aaTAD is a transactivation motif present
CC in a large number of yeast and animal transcription factors.
CC {ECO:0000250|UniProtKB:Q00613}.
CC -!- SIMILARITY: Belongs to the HSF family. {ECO:0000305}.
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DR EMBL; L06098; AFP54343.1; -; mRNA.
DR RefSeq; NP_001292185.1; NM_001305256.1.
DR AlphaFoldDB; P38529; -.
DR SMR; P38529; -.
DR STRING; 9031.ENSGALP00000026456; -.
DR PaxDb; P38529; -.
DR GeneID; 420362; -.
DR KEGG; gga:420362; -.
DR VEuPathDB; HostDB:LOC420362; -.
DR eggNOG; KOG0627; Eukaryota.
DR InParanoid; P38529; -.
DR OrthoDB; 1154048at2759; -.
DR PhylomeDB; P38529; -.
DR PRO; PR:P38529; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0101031; C:chaperone complex; ISS:UniProtKB.
DR GO; GO:0000785; C:chromatin; IDA:ARUK-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:AgBase.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0097431; C:mitotic spindle pole; ISS:UniProtKB.
DR GO; GO:0097165; C:nuclear stress granule; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:AgBase.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0016605; C:PML body; ISS:UniProtKB.
DR GO; GO:0031490; F:chromatin DNA binding; ISS:UniProtKB.
DR GO; GO:0001046; F:core promoter sequence-specific DNA binding; IDA:AgBase.
DR GO; GO:0003677; F:DNA binding; IDA:AgBase.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:ARUK-UCL.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0031072; F:heat shock protein binding; ISS:UniProtKB.
DR GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:AgBase.
DR GO; GO:0043621; F:protein self-association; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:ARUK-UCL.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:AgBase.
DR GO; GO:0071276; P:cellular response to cadmium ion; ISS:UniProtKB.
DR GO; GO:0071480; P:cellular response to gamma radiation; ISS:UniProtKB.
DR GO; GO:0034605; P:cellular response to heat; IDA:AgBase.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0000165; P:MAPK cascade; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:2001033; P:negative regulation of double-strand break repair via nonhomologous end joining; ISS:UniProtKB.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:1902808; P:positive regulation of cell cycle G1/S phase transition; IMP:AgBase.
DR GO; GO:1902751; P:positive regulation of cell cycle G2/M phase transition; IMP:AgBase.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:AgBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:AgBase.
DR GO; GO:0045931; P:positive regulation of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:1900365; P:positive regulation of mRNA polyadenylation; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:ARUK-UCL.
DR GO; GO:0061408; P:positive regulation of transcription from RNA polymerase II promoter in response to heat stress; ISS:UniProtKB.
DR GO; GO:0070207; P:protein homotrimerization; IDA:AgBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0009408; P:response to heat; IDA:AgBase.
DR GO; GO:0009416; P:response to light stimulus; IDA:AgBase.
DR Gene3D; 1.10.10.10; -; 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; PTHR10015; 2.
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 1: Evidence at protein level;
KW Activator; Centromere; Chromosome; Cytoplasm; Cytoskeleton; DNA damage;
KW DNA repair; DNA-binding; Kinetochore; mRNA processing; mRNA transport;
KW Nucleus; Reference proteome; Stress response; Transcription;
KW Transcription regulation; Transport.
FT CHAIN 1..491
FT /note="Heat shock factor protein 1"
FT /id="PRO_0000124574"
FT REGION 20..125
FT /note="DNA-binding domain"
FT /evidence="ECO:0000250|UniProtKB:Q00613"
FT REGION 135..208
FT /note="Hydrophobic repeat HR-A/B"
FT /evidence="ECO:0000250|UniProtKB:Q00613"
FT REGION 208..229
FT /note="D domain"
FT /evidence="ECO:0000250|UniProtKB:Q00613"
FT REGION 275..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..491
FT /note="Transactivation domain"
FT /evidence="ECO:0000250|UniProtKB:Q00613"
FT REGION 346..371
FT /note="Hydrophobic repeat HR-C"
FT /evidence="ECO:0000250|UniProtKB:Q00613"
FT REGION 464..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 374..382
FT /note="9aaTAD"
FT /evidence="ECO:0000250|UniProtKB:Q00613"
FT COMPBIAS 275..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..308
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 491 AA; 53599 MW; D605CEB368A0B3B8 CRC64;
MEGPGAAAAA VGAGPGGSNV SAFLTKLWTL VEDPETDPLI CWSPSGNSFH VFDQGQFAKE
VLPKYFKHNN MASFVRQLNM YGFRKVVHIE QGGLVKPEKD DTEFQHPYFI RGQEHLLENI
KRKVTSVSSI KNEDIKVRQD NVTKLLTDIQ VMKGKQESMD SKLIAMKHEN EALWREVASL
RQKHAQQQKV VNKLIQFLIS LVQSNRILGV KRKIPLMLND SSSAHSMPKY SRQYSLEHVH
GSSPYAASSP AYSGSNIYSP DSSTNSGPII SDVTELAQSS PSASPSGSLD ERSSPVVRIK
EEPPSPSRSP KENEPSTTTA AAGNSTEQPQ PQEKCLSVAC LDKNELNDHL DTIDSNLDNL
QTMLSTHGFS VDTTALLDLF SPSMTVTDMN LPDLDSSLAS IQDLLSSQEQ QKPSEADAAA
ADTGKQLVHY TAQPLFLVDS SAVDVGSGDL PIFFELGEGS YFTDGDEYNE DPTISLLSGT
EQPKPKDPTV S
