HSF_DROME
ID HSF_DROME Reviewed; 691 AA.
AC P22813; Q9V8C1;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Heat shock factor protein;
DE Short=HSF;
DE AltName: Full=Heat shock transcription factor;
DE Short=HSTF;
GN Name=Hsf; ORFNames=CG5748;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2257625; DOI=10.1016/0092-8674(90)90511-c;
RA Clos J., Westwood J.T., Becker P.B., Wilson S., Lambert K., Wu C.;
RT "Molecular cloning and expression of a hexameric Drosophila heat shock
RT factor subject to negative regulation.";
RL Cell 63:1085-1097(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256; THR-258; SER-260;
RP SER-283; SER-299 AND SER-580, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [5]
RP STRUCTURE BY NMR OF 43-150.
RX PubMed=7634100; DOI=10.1038/nsb0994-605;
RA Vuister G.W., Kim S.-J., Orosz A., Marquardt J., Wu C., Bax A.;
RT "Solution structure of the DNA-binding domain of Drosophila heat shock
RT transcription factor.";
RL Nat. Struct. Biol. 1:605-613(1994).
CC -!- FUNCTION: DNA-binding protein that specifically binds heat shock
CC promoter elements (HSE) and activates transcription. In higher
CC eukaryotes, HSF is unable to bind to the HSE unless the cells are heat
CC shocked.
CC -!- SUBUNIT: Homotrimer.
CC -!- INTERACTION:
CC P22813; P22813: Hsf; NbExp=3; IntAct=EBI-130048, EBI-130048;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- PTM: Exhibits temperature-dependent phosphorylation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the HSF family. {ECO:0000305}.
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DR EMBL; M60070; AAA28642.1; -; mRNA.
DR EMBL; AE013599; AAF57749.1; -; Genomic_DNA.
DR PIR; A36295; A36295.
DR RefSeq; NP_476575.1; NM_057227.5.
DR PDB; 1HKS; NMR; -; A=43-148.
DR PDB; 1HKT; NMR; -; A=43-148.
DR PDBsum; 1HKS; -.
DR PDBsum; 1HKT; -.
DR AlphaFoldDB; P22813; -.
DR BMRB; P22813; -.
DR SMR; P22813; -.
DR BioGRID; 62751; 20.
DR DIP; DIP-20041N; -.
DR IntAct; P22813; 4.
DR MINT; P22813; -.
DR STRING; 7227.FBpp0110266; -.
DR iPTMnet; P22813; -.
DR EnsemblMetazoa; FBtr0086782; FBpp0085961; FBgn0001222.
DR GeneID; 37068; -.
DR KEGG; dme:Dmel_CG5748; -.
DR CTD; 37068; -.
DR FlyBase; FBgn0001222; Hsf.
DR VEuPathDB; VectorBase:FBgn0001222; -.
DR eggNOG; KOG0627; Eukaryota.
DR HOGENOM; CLU_025761_0_0_1; -.
DR InParanoid; P22813; -.
DR OMA; HGHLDNM; -.
DR PhylomeDB; P22813; -.
DR Reactome; R-DME-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-DME-3371511; HSF1 activation.
DR Reactome; R-DME-3371568; Attenuation phase.
DR Reactome; R-DME-3371571; HSF1-dependent transactivation.
DR SignaLink; P22813; -.
DR BioGRID-ORCS; 37068; 0 hits in 3 CRISPR screens.
DR EvolutionaryTrace; P22813; -.
DR GenomeRNAi; 37068; -.
DR PRO; PR:P22813; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0001222; Expressed in cleaving embryo and 33 other tissues.
DR ExpressionAtlas; P22813; baseline and differential.
DR Genevisible; P22813; DM.
DR GO; GO:0000785; C:chromatin; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR GO; GO:0003677; F:DNA binding; IDA:FlyBase.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:FlyBase.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:FlyBase.
DR GO; GO:0042742; P:defense response to bacterium; IMP:FlyBase.
DR GO; GO:0050832; P:defense response to fungus; IMP:FlyBase.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:FlyBase.
DR GO; GO:0043388; P:positive regulation of DNA binding; IDA:FlyBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:FlyBase.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0009408; P:response to heat; IDA:FlyBase.
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; Direct protein sequencing; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Stress response; Transcription;
KW Transcription regulation.
FT CHAIN 1..691
FT /note="Heat shock factor protein"
FT /id="PRO_0000124578"
FT DNA_BIND 46..150
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..691
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 258
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 580
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT HELIX 50..57
FT /evidence="ECO:0007829|PDB:1HKS"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:1HKS"
FT TURN 61..65
FT /evidence="ECO:0007829|PDB:1HKS"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:1HKS"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:1HKS"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:1HKT"
FT TURN 82..87
FT /evidence="ECO:0007829|PDB:1HKS"
FT TURN 89..92
FT /evidence="ECO:0007829|PDB:1HKS"
FT HELIX 97..107
FT /evidence="ECO:0007829|PDB:1HKS"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:1HKS"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:1HKT"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:1HKS"
SQ SEQUENCE 691 AA; 76933 MW; E013428B22C98D35 CRC64;
MSRSRSSAKA VQFKHESEEE EEDEEEQLPS RRMHSYGDAA AIGSGVPAFL AKLWRLVDDA
DTNRLICWTK DGQSFVIQNQ AQFAKELLPL NYKHNNMASF IRQLNMYGFH KITSIDNGGL
RFDRDEIEFS HPFFKRNSPF LLDQIKRKIS NNKNGDDKGV LKPEAMSKIL TDVKVMRGRQ
DNLDSRFSAM KQENEVLWRE IASLRQKHAK QQQIVNKLIQ FLITIVQPSR NMSGVKRHVQ
LMINNTPEID RARTTSETES ESGGGPVIHE LREELLDEVM NPSPAGYTAA SHYDQESVSP
PAVERPRSNM SISSHNVDYS NQSVEDLLLQ GNGTAGGNIL VGGAASPMAQ SVSQSPAQHD
VYTVTEAPDS HVQEVPNSPP YYEEQNVLTT PMVREQEQQK RQQLKENNKL RRQAGDVILD
AGDILVDSSS PKAQRTSIQH STQPDVMVQP MIIKSEPENS SGLMDLMTPA NDLYSVNFIS
EDMPTDIFED ALLPDGVEEA AKLDQQQKFG QSTVSSGKFA SNFDVPTNST LLDANQASTS
KAAAKAQASE EEGMAVAKYS GAENGNNRDT NNSQLLRMAS VDELHGHLES MQDELETLKD
LLRGDGVAID QNMLMGLFND SDLMDNYGLS FPNDSISSEK KAPSGSELIS YQPMYDLSDI
LDTDDGNNDQ EASRRQMQTQ SSVLNTPRHE L
