HSF_CANAL
ID HSF_CANAL Reviewed; 760 AA.
AC Q5AQ33; A0A1D8PEH8; Q5APJ0;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Heat shock transcription factor {ECO:0000303|PubMed:19818013};
DE Short=HSTF {ECO:0000305};
DE AltName: Full=Heat shock factor protein {ECO:0000305};
DE Short=HSF {ECO:0000305};
GN Name=CTA8 {ECO:0000312|CGD:CAL0000175059};
GN Synonyms=HSF1 {ECO:0000303|PubMed:19818013};
GN OrderedLocusNames=CAALFM_C109170WA {ECO:0000312|CGD:CAL0000175059};
GN ORFNames=CaO19.12238 {ECO:0000312|CGD:CAL0000175059},
GN CaO19.4775 {ECO:0000312|CGD:CAL0000175059};
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP IDENTIFICATION.
RX PubMed=10341421;
RX DOI=10.1002/(sici)1097-0061(199905)15:7<585::aid-yea401>3.0.co;2-9;
RA Kaiser B., Munder T., Saluz H.P., Kuenkel W., Eck R.;
RT "Identification of a gene encoding the pyruvate decarboxylase gene
RT regulator CaPdc2p from Candida albicans.";
RL Yeast 15:585-591(1999).
RN [5]
RP INDUCTION.
RX PubMed=18653474; DOI=10.1091/mbc.e07-09-0946;
RA Ramsdale M., Selway L., Stead D., Walker J., Yin Z., Nicholls S.M.,
RA Crowe J., Sheils E.M., Brown A.J.;
RT "MNL1 regulates weak acid-induced stress responses of the fungal pathogen
RT Candida albicans.";
RL Mol. Biol. Cell 19:4393-4403(2008).
RN [6]
RP FUNCTION, PHOSPHORYLATION, AND DISRUPTION PHENOTYPE.
RX PubMed=19818013; DOI=10.1111/j.1365-2958.2009.06883.x;
RA Nicholls S., Leach M.D., Priest C.L., Brown A.J.;
RT "Role of the heat shock transcription factor, Hsf1, in a major fungal
RT pathogen that is obligately associated with warm-blooded animals.";
RL Mol. Microbiol. 74:844-861(2009).
RN [7]
RP FUNCTION, PHOSPHORYLATION AT SER-570; THR-574; SER-576 AND THR-577, AND
RP MUTAGENESIS OF SER-570; THR-574; SER-576 AND THR-577.
RX PubMed=20817114; DOI=10.1016/j.fgb.2010.08.010;
RA Nicholls S., MacCallum D.M., Kaffarnik F.A., Selway L., Peck S.C.,
RA Brown A.J.;
RT "Activation of the heat shock transcription factor Hsf1 is essential for
RT the full virulence of the fungal pathogen Candida albicans.";
RL Fungal Genet. Biol. 48:297-305(2011).
RN [8]
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=22448221; DOI=10.1371/journal.pone.0032467;
RA Leach M.D., Tyc K.M., Brown A.J., Klipp E.;
RT "Modelling the regulation of thermal adaptation in Candida albicans, a
RT major fungal pathogen of humans.";
RL PLoS ONE 7:E32467-E32467(2012).
RN [9]
RP FUNCTION, AND INTERACTION WITH HSP90.
RX PubMed=23300438; DOI=10.1371/journal.ppat.1003069;
RA Leach M.D., Budge S., Walker L., Munro C., Cowen L.E., Brown A.J.;
RT "Hsp90 orchestrates transcriptional regulation by Hsf1 and cell wall
RT remodelling by MAPK signalling during thermal adaptation in a pathogenic
RT yeast.";
RL PLoS Pathog. 8:E1003069-E1003069(2012).
CC -!- FUNCTION: DNA-binding transcription factor that specifically binds heat
CC shock promoter elements (HSE) and activates transcription. With HSP90,
CC is required for the modulation of the chaperone levels in response to
CC growth temperature, rather than the activation of acute responses to
CC sudden thermal transitions. Activated during infection and contributes
CC to full virulence. {ECO:0000269|PubMed:19818013,
CC ECO:0000269|PubMed:20817114, ECO:0000269|PubMed:22448221,
CC ECO:0000269|PubMed:23300438}.
CC -!- SUBUNIT: Homotrimer (By similarity). Homotrimerization increases the
CC affinity of HSF1 to DNA (By similarity). Interacts with HSP90
CC (PubMed:23300438). {ECO:0000250|UniProtKB:P10961,
CC ECO:0000269|PubMed:23300438}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P10961}.
CC -!- INDUCTION: Induced during exposure to the weak acid stress of acetic
CC acid, through the regulation by the transcription factor MNL1.
CC {ECO:0000269|PubMed:18653474}.
CC -!- PTM: Activated by phosphorylation of at least Ser-570, Thr-574, Ser-576
CC and Thr-577 in response to heat shock. Additional unidentified residues
CC are also phosphorylated in response to heat shock.
CC {ECO:0000269|PubMed:19818013, ECO:0000269|PubMed:20817114,
CC ECO:0000269|PubMed:22448221}.
CC -!- DISRUPTION PHENOTYPE: Leads to lethality.
CC {ECO:0000269|PubMed:19818013}.
CC -!- SIMILARITY: Belongs to the HSF family. {ECO:0000305}.
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DR EMBL; CP017623; AOW26551.1; -; Genomic_DNA.
DR RefSeq; XP_723461.2; XM_718368.2.
DR AlphaFoldDB; Q5AQ33; -.
DR SMR; Q5AQ33; -.
DR BioGRID; 1218041; 2.
DR STRING; 237561.Q5AQ33; -.
DR iPTMnet; Q5AQ33; -.
DR PRIDE; Q5AQ33; -.
DR GeneID; 3634947; -.
DR KEGG; cal:CAALFM_C109170WA; -.
DR CGD; CAL0000175059; CTA8.
DR VEuPathDB; FungiDB:C1_09170W_A; -.
DR eggNOG; KOG0627; Eukaryota.
DR HOGENOM; CLU_366803_0_0_1; -.
DR InParanoid; Q5AQ33; -.
DR OrthoDB; 1154048at2759; -.
DR PHI-base; PHI:2565; -.
DR PRO; PR:Q5AQ33; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0044182; P:filamentous growth of a population of unicellular organisms; IEA:UniProt.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 1.
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 Pfam; PF00447; HSF_DNA-bind; 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; Coiled coil; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Stress response; Transcription;
KW Transcription regulation; Virulence.
FT CHAIN 1..760
FT /note="Heat shock transcription factor"
FT /id="PRO_0000426084"
FT DNA_BIND 276..385
FT /evidence="ECO:0000255"
FT REGION 1..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..467
FT /note="Involved in trimerization"
FT /evidence="ECO:0000250|UniProtKB:P22121"
FT REGION 492..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 674..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 646..684
FT /evidence="ECO:0000255"
FT COMPBIAS 18..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..742
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..760
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 570
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:20817114"
FT MOD_RES 574
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:20817114"
FT MOD_RES 576
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:20817114"
FT MOD_RES 577
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:20817114"
FT MUTAGEN 570
FT /note="S->A: Decreases thermotolerance; when associated
FT with A-574, A-576 and A-577."
FT /evidence="ECO:0000269|PubMed:20817114"
FT MUTAGEN 570
FT /note="S->E: Mimics phosphorylation and increases
FT thermotolerance; when associated with E-574, E-576 and E-
FT 577."
FT /evidence="ECO:0000269|PubMed:20817114"
FT MUTAGEN 574
FT /note="T->A: Decreases thermotolerance; when associated
FT with A-570, A-576 and A-577."
FT /evidence="ECO:0000269|PubMed:20817114"
FT MUTAGEN 574
FT /note="T->E: Mimics phosphorylation and increases
FT thermotolerance; when associated with E-570, E-576 and E-
FT 577."
FT /evidence="ECO:0000269|PubMed:20817114"
FT MUTAGEN 576
FT /note="S->A: Decreases thermotolerance; when associated
FT with A-570, A-556 and A-577."
FT /evidence="ECO:0000269|PubMed:20817114"
FT MUTAGEN 576
FT /note="S->E: Mimics phosphorylation and increases
FT thermotolerance; when associated with E-570, E-556 and E-
FT 577."
FT /evidence="ECO:0000269|PubMed:20817114"
FT MUTAGEN 577
FT /note="T->A: Decreases thermotolerance; when associated
FT with A-570, A-574 and A-576."
FT /evidence="ECO:0000269|PubMed:20817114"
FT MUTAGEN 577
FT /note="T->E: Mimics phosphorylation and increases
FT thermotolerance; when associated with E-570, E-574 and E-
FT 576."
FT /evidence="ECO:0000269|PubMed:20817114"
SQ SEQUENCE 760 AA; 86197 MW; FABFFE4657C80BB9 CRC64;
MIMNMTTDYR DPLLDLFGTE SNSGNETSSP SDIPVINRSG TFNQQQFSPL LTQQSLYNTP
NSGSTPNIFD PNYTQMQEEQ TSPSSNKLQP EDPPRKKRNT RSQTKIHQQS EGDEYNSNDY
KDSIDLDKPP VVEPSPPFFV ESDTTPEFVI PTPTSEQQQQ QHHELIAQDY QRSNNSNQFG
NLTHYEPNLP PLPPLSESIL PQTNTFHPLV LPHDPRHAIT AGPANNSQQQ QQQQQQDSSI
PSDGISSKIQ QLHAPSLSNN QSASQRKKKE SSGPKTRPAF VMKIWSMVND PANHEYIRWN
DDGKTFQVFH REDFMKVILP KYFKHNNFAS FVRQLNMYGW HKVQDVANGT LNQNSDKNGQ
DEIWQFENPN FIKDREDLLD KIVRNKSSSN QDDVSGVSFN GINNSANLSL ILQELETIKM
NQYVISEDLR RVRQDNKMLW QENYLNRERN QVQGRTLDKI LKFLSVVYGN NANKILNGHG
FADFNDSNNI MTQYRPSPMG SPLLSRPQTQ PPPSNSRFAR DNNQTAQPTY ESPLSTSDTN
NNNNNTFEYQ QAVNRPRLML TNRAHSRRPS MSRTKSTPEG SIEEIIRSYS NDKAAESNVN
RMYEQLVGHQ PGATTNNNNH SSSTAISAPS PRHSFLQELN LPGTPRNLDD LEKHINKEGQ
SIQQVQDWID KLAQEQHEKQ QQQQGNDDDD DFDVNEFLKD ATTTPSSNVP NGGHYNNGNI
SFVGSPIAMT PGSNVSSNIN DSDGNEKKSK KRSIEEVSDH
