HSF_KLULA
ID HSF_KLULA Reviewed; 677 AA.
AC P22121;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 25-MAY-2022, entry version 142.
DE RecName: Full=Heat shock transcription factor {ECO:0000303|PubMed:1899375};
DE Short=HSTF {ECO:0000305};
DE AltName: Full=Heat shock factor protein {ECO:0000305};
DE Short=HSF {ECO:0000303|PubMed:1899375};
GN Name=HSF {ECO:0000303|PubMed:1899375}; OrderedLocusNames=KLLA0D03322g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP PHOSPHORYLATION.
RX PubMed=1899375; DOI=10.1002/j.1460-2075.1991.tb07958.x;
RA Jakobsen B.K., Pelham H.R.B.;
RT "A conserved heptapeptide restrains the activity of the yeast heat shock
RT transcription factor.";
RL EMBO J. 10:369-375(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
RN [3]
RP SUBUNIT.
RX PubMed=10090742; DOI=10.1021/bi981774j;
RA Peteranderl R., Rabenstein M., Shin Y.K., Liu C.W., Wemmer D.E., King D.S.,
RA Nelson H.C.;
RT "Biochemical and biophysical characterization of the trimerization domain
RT from the heat shock transcription factor.";
RL Biochemistry 38:3559-3569(1999).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 193-281.
RX PubMed=8284672; DOI=10.1126/science.8284672;
RA Harrison C.J., Bohm A.A., Nelson H.C.M.;
RT "Crystal structure of the DNA binding domain of the heat shock
RT transcription factor.";
RL Science 263:224-227(1994).
CC -!- FUNCTION: DNA-binding transcription factor that specifically binds heat
CC shock promoter elements (HSE) and activates transcription.
CC {ECO:0000269|PubMed:1899375}.
CC -!- SUBUNIT: Homotrimer (PubMed:10090742). Homotrimerization increases the
CC affinity of HSF1 to DNA (By similarity). {ECO:0000250|UniProtKB:P10961,
CC ECO:0000269|PubMed:10090742}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:1899375}.
CC -!- PTM: Exhibits temperature-dependent phosphorylation.
CC {ECO:0000305|PubMed:1899375}.
CC -!- SIMILARITY: Belongs to the HSF family. {ECO:0000305}.
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DR EMBL; X55149; CAA38950.1; -; Genomic_DNA.
DR EMBL; CR382124; CAH00310.1; -; Genomic_DNA.
DR PIR; S13365; S13365.
DR RefSeq; XP_453214.1; XM_453214.1.
DR PDB; 1FBQ; X-ray; 2.00 A; A/B=195-281.
DR PDB; 1FBS; X-ray; 2.00 A; A/B=195-281.
DR PDB; 1FBU; X-ray; 2.00 A; A/B=195-281.
DR PDB; 1FYK; X-ray; 2.50 A; A=193-284.
DR PDB; 1FYL; X-ray; 2.10 A; A/B=193-284.
DR PDB; 1FYM; X-ray; 2.20 A; A/B=193-284.
DR PDB; 2HTS; X-ray; 1.83 A; A=193-281.
DR PDB; 3HSF; NMR; -; A=193-281.
DR PDB; 3HTS; X-ray; 1.75 A; B=193-281.
DR PDBsum; 1FBQ; -.
DR PDBsum; 1FBS; -.
DR PDBsum; 1FBU; -.
DR PDBsum; 1FYK; -.
DR PDBsum; 1FYL; -.
DR PDBsum; 1FYM; -.
DR PDBsum; 2HTS; -.
DR PDBsum; 3HSF; -.
DR PDBsum; 3HTS; -.
DR AlphaFoldDB; P22121; -.
DR SMR; P22121; -.
DR STRING; 28985.XP_453214.1; -.
DR EnsemblFungi; CAH00310; CAH00310; KLLA0_D03322g.
DR GeneID; 2893291; -.
DR KEGG; kla:KLLA0_D03322g; -.
DR eggNOG; KOG0627; Eukaryota.
DR HOGENOM; CLU_405993_0_0_1; -.
DR InParanoid; P22121; -.
DR EvolutionaryTrace; P22121; -.
DR Proteomes; UP000000598; Chromosome D.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0032993; C:protein-DNA complex; IMP:CAFA.
DR GO; GO:0003677; F:DNA binding; IMP:CAFA.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR DisProt; DP00036; -.
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 3D-structure; Activator; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Stress response; Transcription;
KW Transcription regulation.
FT CHAIN 1..677
FT /note="Heat shock transcription factor"
FT /id="PRO_0000124579"
FT DNA_BIND 193..297
FT /evidence="ECO:0000255"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 320..373
FT /note="Involved in trimerization"
FT /evidence="ECO:0000305|PubMed:10090742"
FT REGION 400..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..677
FT /note="Activatory"
FT REGION 606..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..648
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..677
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 196..206
FT /evidence="ECO:0007829|PDB:3HTS"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:3HTS"
FT TURN 211..213
FT /evidence="ECO:0007829|PDB:3HTS"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:3HTS"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:1FBQ"
FT STRAND 222..226
FT /evidence="ECO:0007829|PDB:3HTS"
FT HELIX 228..234
FT /evidence="ECO:0007829|PDB:3HTS"
FT HELIX 236..239
FT /evidence="ECO:0007829|PDB:3HTS"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:1FBS"
FT HELIX 245..254
FT /evidence="ECO:0007829|PDB:3HTS"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:3HTS"
FT TURN 266..269
FT /evidence="ECO:0007829|PDB:1FBQ"
FT STRAND 276..280
FT /evidence="ECO:0007829|PDB:3HTS"
SQ SEQUENCE 677 AA; 75420 MW; 0BF03BCF990C210B CRC64;
MGHNDSVETM DEISNPNNIL LPHDGTGLDA TGISGSQEPY GMVDVLNPDS LKDDSNVDEP
LIEDIVNPSL DPEGVVSAEP SNEVGTPLLQ QPISLDHVIT RPASAGGVYS IGNSSTSSAA
KLSDGDLTNA TDPLLNNAHG HGQPSSESQS HSNGYHKQGQ SQQPLLSLNK RKLLAKAHVD
KHHSKKKLST TRARPAFVNK LWSMVNDKSN EKFIHWSTSG ESIVVPNRER FVQEVLPKYF
KHSNFASFVR QLNMYGWHKV QDVKSGSMLS NNDSRWEFEN ENFKRGKEYL LENIVRQKSN
TNILGGTTNA EVDIHILLNE LETVKYNQLA IAEDLKRITK DNEMLWKENM MARERHQSQQ
QVLEKLLRFL SSVFGPNSAK TIGNGFQPDL IHELSDMQVN HMSNNNHNNT GNINPNAYHN
ETDDPMANVF GPLTPTDQGK VPLQDYKLRP RLLLKNRSMS SSSSSNLNQR QSPQNRIVGQ
SPPPQQQQQQ QQQQGQPQGQ QFSYPIQGGN QMMNQLGSPI GTQVGSPVGS QYGNQYGNQY
SNQFGNQLQQ QTSRPALHHG SNGEIRELTP SIVSSDSPDP AFFQDLQNNI DKQEESIQEI
QDWITKLNPG PGEDGNTPIF PELNMPSYFA NTGGSGQSEQ PSDYGDSQIE ELRNSRLHEP
DRSFEEKNNG QKRRRAA
