HSF_SCHPO
ID HSF_SCHPO Reviewed; 609 AA.
AC Q02953; Q9USC6;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Heat shock factor protein;
DE Short=HSF;
DE AltName: Full=Heat shock transcription factor;
DE Short=HSTF;
GN Name=hsf1; Synonyms=hsf; ORFNames=SPAC2E12.02;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8423799; DOI=10.1128/mcb.13.2.749-761.1993;
RA Gallo G.J., Prentice H., Kingston R.E.;
RT "Heat shock factor is required for growth at normal temperatures in the
RT fission yeast Schizosaccharomyces pombe.";
RL Mol. Cell. Biol. 13:749-761(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 111-222, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: DNA-binding protein that specifically binds heat shock
CC promoter elements (HSE) and activates transcription. Also required for
CC growth at normal temperatures.
CC -!- SUBUNIT: Homotrimer.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10759889,
CC ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the HSF family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M94683; AAA35313.1; -; mRNA.
DR EMBL; CU329670; CAA93546.1; -; Genomic_DNA.
DR EMBL; AB027865; BAA87169.1; -; Genomic_DNA.
DR PIR; A48070; A48070.
DR RefSeq; NP_594846.1; NM_001020275.2.
DR AlphaFoldDB; Q02953; -.
DR SMR; Q02953; -.
DR BioGRID; 278378; 6.
DR STRING; 4896.SPAC2E12.02.1; -.
DR iPTMnet; Q02953; -.
DR MaxQB; Q02953; -.
DR PaxDb; Q02953; -.
DR PRIDE; Q02953; -.
DR EnsemblFungi; SPAC2E12.02.1; SPAC2E12.02.1:pep; SPAC2E12.02.
DR GeneID; 2541888; -.
DR KEGG; spo:SPAC2E12.02; -.
DR PomBase; SPAC2E12.02; hsf1.
DR VEuPathDB; FungiDB:SPAC2E12.02; -.
DR eggNOG; KOG0627; Eukaryota.
DR HOGENOM; CLU_443554_0_0_1; -.
DR InParanoid; Q02953; -.
DR OMA; QSDSPNE; -.
DR PhylomeDB; Q02953; -.
DR Reactome; R-SPO-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-SPO-3371511; HSF1 activation.
DR Reactome; R-SPO-3371568; Attenuation phase.
DR Reactome; R-SPO-3371571; HSF1-dependent transactivation.
DR PRO; PR:Q02953; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IMP:PomBase.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:PomBase.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:PomBase.
DR GO; GO:0034605; P:cellular response to heat; IMP:PomBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:PomBase.
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; DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Stress response; Transcription; Transcription regulation.
FT CHAIN 1..609
FT /note="Heat shock factor protein"
FT /id="PRO_0000124580"
FT DNA_BIND 50..156
FT /evidence="ECO:0000250"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 310..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 567..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..596
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 29
FT /note="N -> H (in Ref. 1; AAA35313)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 609 AA; 66947 MW; CE1F7A87D8CBF50A CRC64;
MIQTASTISS NGGTNQGMES SSANSPEMNG TQNSMSVGMS GSGSSQNRKI TQFSNKLYNM
VNDSSTDSLI RWSDRGDSFL VIGHEDFAKL VLPRYFKHNN FSSFVRQLNM YGFHKVPHIQ
QGVLQSDSPN ELLEFANPNF QRDQPELLCL VTRKKAGSQP VEESNTSLDM STISSELQNI
RIQQMNLSNE LSRIQVDNAA LWQENMENRE RQRRHQETID KILRFLASVY LDGKQKPPSK
VMPKSRRLLL EAKYPTVSPT NEPSAHSRPS PQGTTANSSS ASISSLHNTT PDGEGKYRSV
QNGRALNYVS SFNSDSHSPK DYISQSYTNE PGLKKESADS FNNSIDSYIS PNQSPNTDVP
SLNRDDTTDP KVVNTGDIIN MLDDANSIEG SNMNSLSPLL FDYPNSLYPV NNTSSEQHHN
SYRGSVSNSQ PSGNLSESTN LQPVQPVDYM SNSNPSYGSY NAEDQLTNFH PGYAMDQKRI
SKLSDGITKQ DQNIQALADI LGIPLGDGKI DDAGFSANSP TNLNLPVSSD LDSVLNIPPN
EDVFPDSNPV FDEFTNISNL TSPIEASNGN TFGSNPVSLP NQQKSVNPSL MTVSSPRQVR
KKRKSSIGA
