HSF_CRYNH
ID HSF_CRYNH Reviewed; 771 AA.
AC J9VHZ9;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 1.
DT 25-MAY-2022, entry version 51.
DE RecName: Full=Heat shock transcription factor {ECO:0000303|PubMed:27866167};
DE Short=HSTF {ECO:0000305};
DE AltName: Full=Heat shock factor protein {ECO:0000305};
DE Short=HSF {ECO:0000305};
GN Name=HSF1 {ECO:0000303|PubMed:27866167};
GN ORFNames=CNAG_07460 {ECO:0000312|EMBL:AFR93011.1};
OS Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 /
OS CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=235443 {ECO:0000312|Proteomes:UP000010091};
RN [1] {ECO:0000312|Proteomes:UP000010091}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487;
RX PubMed=24743168; DOI=10.1371/journal.pgen.1004261;
RA Janbon G., Ormerod K.L., Paulet D., Byrnes E.J. III, Yadav V.,
RA Chatterjee G., Mullapudi N., Hon C.-C., Billmyre R.B., Brunel F.,
RA Bahn Y.-S., Chen W., Chen Y., Chow E.W.L., Coppee J.-Y., Floyd-Averette A.,
RA Gaillardin C., Gerik K.J., Goldberg J., Gonzalez-Hilarion S., Gujja S.,
RA Hamlin J.L., Hsueh Y.-P., Ianiri G., Jones S., Kodira C.D., Kozubowski L.,
RA Lam W., Marra M., Mesner L.D., Mieczkowski P.A., Moyrand F., Nielsen K.,
RA Proux C., Rossignol T., Schein J.E., Sun S., Wollschlaeger C., Wood I.A.,
RA Zeng Q., Neuveglise C., Newlon C.S., Perfect J.R., Lodge J.K., Idnurm A.,
RA Stajich J.E., Kronstad J.W., Sanyal K., Heitman J., Fraser J.A.,
RA Cuomo C.A., Dietrich F.S.;
RT "Analysis of the genome and transcriptome of Cryptococcus neoformans var.
RT grubii reveals complex RNA expression and microevolution leading to
RT virulence attenuation.";
RL PLoS Genet. 10:E1004261-E1004261(2014).
RN [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, PHOSPHORYLATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=27866167; DOI=10.1534/genetics.116.190595;
RA Yang D.H., Jung K.W., Bang S., Lee J.W., Song M.H., Floyd-Averette A.,
RA Festa R.A., Ianiri G., Idnurm A., Thiele D.J., Heitman J., Bahn Y.S.;
RT "Rewiring of Signaling Networks Modulating Thermotolerance in the Human
RT Pathogen Cryptococcus neoformans.";
RL Genetics 205:201-219(2017).
CC -!- FUNCTION: DNA-binding transcription factor that specifically binds heat
CC shock promoter elements (HSE) and activates transcription
CC (PubMed:27866167). Promotes thermotolerance by transiently regulating a
CC subset of genes (PubMed:27866167). Induces expression of STI, SSA1,
CC SSA2, HSP78 and KAR2 during the heat response (PubMed:27866167).
CC {ECO:0000269|PubMed:27866167}.
CC -!- SUBUNIT: Homotrimer (By similarity). Homotrimerization increases the
CC affinity of HSF1 to DNA (By similarity). Interacts with transcriptional
CC coregulator SSA1 on chromatin (By similarity).
CC {ECO:0000250|UniProtKB:P10961, ECO:0000250|UniProtKB:Q5KMX8}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:27866167}.
CC -!- INDUCTION: Repressed by high temperature (at protein level)
CC (PubMed:27866167). Induced by oxidative stress (PubMed:27866167).
CC {ECO:0000269|PubMed:27866167}.
CC -!- PTM: Phosphorylated at high temperature. {ECO:0000269|PubMed:27866167}.
CC -!- DISRUPTION PHENOTYPE: Inviable vegetative cell population
CC (PubMed:27866167). Inviable spore (PubMed:27866167).
CC {ECO:0000269|PubMed:27866167}.
CC -!- SIMILARITY: Belongs to the HSF family. {ECO:0000255|RuleBase:RU004020}.
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DR EMBL; CP003821; AFR93011.1; -; Genomic_DNA.
DR RefSeq; XP_012047741.1; XM_012192351.1.
DR AlphaFoldDB; J9VHZ9; -.
DR SMR; J9VHZ9; -.
DR EnsemblFungi; AFR93011; AFR93011; CNAG_07460.
DR GeneID; 23890305; -.
DR VEuPathDB; FungiDB:CNAG_07460; -.
DR HOGENOM; CLU_015858_1_0_1; -.
DR Proteomes; UP000010091; Chromosome 2.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IC:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IMP:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0070370; P:cellular heat acclimation; IMP:UniProtKB.
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; DNA-binding; Nucleus; Phosphoprotein; Stress response;
KW Transcription; Transcription regulation.
FT CHAIN 1..771
FT /note="Heat shock transcription factor"
FT /id="PRO_0000452015"
FT DNA_BIND 78..168
FT /evidence="ECO:0000250|UniProtKB:P10961"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..333
FT /note="Involved in trimerization"
FT /evidence="ECO:0000250|UniProtKB:P22121"
FT REGION 350..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 708..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..745
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 771 AA; 80301 MW; D5CD182A3BA94B8C CRC64;
MTTNLYAIAG PSKPTTPTST PSPRSEPPSP LKSLTSLPTN PLNPQGTSTS NALTNQSSST
GIGISKPGLS VDENGEVMKV PAFLNKLYTM VSDPEVDDLI YWGENGDSFF VPNAELFGRE
LLPRWFKHSN FSSFVRQLNM YGFHKVPHLQ SGALKNETPI ELWEFANPYF KRGQPQLLTK
VTRKNNRLSN SGVGSSSSLG GSGAGGGMNT RSASAAAASG SGSGQIQQAI SQGHEAGNHS
TSGKYLITDG TTPGSAPPSH TSAGPLIAPQ TLDLSAINSG IAAIRQTQAS IATDLRKLQA
SNEALWRQAY ETQEKQRKHE ETIDLIVSFL ERLFGTEGEG LKGLKEAMRR GVGVRRDRDG
REGRDSRDAR FADDDDGGQK KRRRVGLDRM IEGGSGDGTG EHGEIESPSS DDRLVEIGSN
SEYSIPSVKR TSSSSHPLSL GQLGSSRFTA LPSEDPSPSG SGLGSTPYEG LRTTQASAHG
AGADVNVTDP TLGMNHLSPL SDTDPLLPSS SNALAPYTSH PSFPSSNPNP SSAWAFNPSQ
PLLSPTSAVA AAHAYNLDPS LLQTTIGSLL QSPAVAQMFL KSLSASAQGQ ALTSHSHPHN
PSLLNPNPNG NASTSASASA HDMNTEGLGT GSGTKDLDPT LALFSPLPSH SSLASQSNDL
LKSYNDALTV GEGVDNLQES IDSLVRSMGL DLPNGGSSSV GVDVGDGSGV GTGTGEGDGE
FNVDEFLQGL AKEGEGEEGE REVGGDGDAS SSGAGAENGR KEDVIAQSGL K
