Protein: HSF1_CAEEL
Sequence: MQPTGNQIQQNQQQQQQLIMRVPKQEVSVSGAARRYVQQAPPNRPPRQNHQNGAIGGKKSSVTIQEVPNNAYLETLNKSGNNKVDDDKLPVFLIKLWNIVEDPNLQSIVHWDDSGASFHISDPYLFGRNVLPHFFKHNNMNSMVRQLNMYGFRKMTPLSQGGLTRTESDQDHLEFSHPCFVQGRPELLSQIKRKQSARTVEDKQVNEQTQQNLEVVMAEMRAMREKAKNMEDKMNKLTKENRDMWTQMGSMRQQHARQQQYFKKLLHFLVSVMQPGLSKRVAKRGVLEIDFCAANGTAGPNSKRARMNSEEGPYKDVCDLLESLQRETQEPFSRRFTNNEGPLISEVTDEFGNSPVGRGSAQDLFGDTFGAQSSRYSDGGATSSREQSPHPIISQPQSNSAGAHGANEQKPDDMYMGSGPLTHENIHRGISALKRDYQGASPASGGPSTSSSAPSGAGAGARMAQKRAAPYKNATRQMAQPQQDYSGGFVNNYSGFMPSDPSMIPYQPSHQYLQPHQKLMAIEDQHHPTTSTSSTNADPHQNLYSPTLGLSPSFDRQLSQELQEYFTGTDTSLESFRDLVSNHNWDDFGNNVPLDDDEEGSEDPLRQLALENAPETSNYDGAEDLLFDNEQQYPENGFDVPDPNYLPLADEEIFPHSPALRTPSPSDPNLV
What is the function of this protein?
Functions as a stress-inducible and DNA-binding transcription factor, playing a central role in the transcriptional activation of the heat shock response (HSR), leading to the expression of a large class of molecular chaperones, heat shock proteins (HSPs), that protect cells from cellular insult damage (PubMed:29042483, PubMed:15611166, PubMed:22265419).  Upon exposure to heat and other stress stimuli, activates gene transcription through binding to site-specific heat shock elements (HSEs) present in the promoter regions of target genes, such as the HSPs (PubMed:29042483, PubMed:27688402, PubMed:15611166, PubMed:22265419).  Binds to inverted 5'-NGAAN-3' pentamer DNA sequences in HSEs (PubMed:29042483, PubMed:27688402).  Involved in positive modulation of expression of heat shock protein hsp-16. 2 in response to heat shock; may act in concert with homeodomain-interacting protein kinase hpk-1 (PubMed:15611166, PubMed:28198373, PubMed:29036198).  In response to heat shock or starvation, required for the modulation of lifespan, and protection against aberrant protein aggregation proteotoxicity; may act in parallel with the Insulin/IGF-1-like signaling (IIS) mediated pathway (PubMed:15611166, PubMed:18331616, PubMed:28198373, PubMed:29036198).  Plays a role in modulating autophagy, in response to a moderate and short-term heat shock, also known as a hormetic heat shock (PubMed:28198373).  Involved in positive modulation of ascaroside pheromone biosynthesis in response to heat shock, perhaps by directly activating transcription of peroxisomal fatty acid beta-oxidation genes (PubMed:26759377).  Required in modulating the response to infection by either Gram-negative or Gram-positive bacteria, perhaps acting via regulation of expression of Hsp90/daf-21 and members of the small heat shock protein (HSP20) family (PubMed:16916933, PubMed:29042483).  May play a role downstream of the daf-16/FOXO and daf-2 signaling pathway in response to bacterial pathogens (PubMed:16916933).  Modulates expression of multiple microRNA genes, in both heat shock-dependent and -independent manner (PubMed:28837599).  Independent of heat shock, required to modulate expression of genes involved in larval development, mainly distinct from HSPs; acts in concert with putative transcription factor efl-1/E2F, which may form part of a multiprotein DRM complex (PubMed:15611166, PubMed:27688402).  Independent of heat shock, involved in promoting death of the linker cell, a male-specific cell which guides the elongation of the gonad; perhaps acting by modulating expression of ubiquitin-conjugating enzyme let-70 (PubMed:26952214).  Plays a role in egg-laying (PubMed:15611166).
What are the official names of this protein?
Heat shock transcription factor hsf-1.
What is the protein family that this protein belongs to?
Belongs to the HSF family.
What are the subcellular locations of this protein?
Nucleus. Cytoplasm. Note=Localizes constitutively to the nucleus (PubMed:23107491, PubMed:29042483). Localization to the nucleus enhanced by heat shock (PubMed:22265419). Localization to nucleus inhibited by the Insulin/IGF-1-like signaling (IIS) mediated pathway (PubMed:22265419). In response to heat shock, forms nuclear stress granules (PubMed:23107491, PubMed:29036198). These structures are dependent upon either heat shock, or can be induced by treatment with sodium azide, which may act by inhibiting ATP production (PubMed:23107491). DNA binding may promote localization to stress granules (PubMed:23107491). Localization to stress granules partially overlaps with sites of active transcription (PubMed:23107491). Other stressors such as osmotic stress, heavy metals, or ethanol do not induce localization to nuclear stress granules (PubMed:23107491).