HSP7F_SCHPO
ID HSP7F_SCHPO Reviewed; 720 AA.
AC O59838; Q9UU58;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Heat shock protein homolog pss1;
GN Name=pss1; Synonyms=ssp1; ORFNames=SPAC110.04c, SPAP14E8.01c;
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], FUNCTION, AND INDUCTION.
RX PubMed=9524252; DOI=10.1016/s0378-1119(98)00061-4;
RA Chung K.-S., Hoe K.-L., Kim K.-W., Yoo H.-S.;
RT "Isolation of a novel heat shock protein 70-like gene, pss1+ of
RT Schizosaccharomyces pombe homologous to hsp110/SSE subfamily.";
RL Gene 210:143-150(1998).
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 129-306, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38 AND THR-39, AND
RP IDENTIFICATION BY 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: Required for normal growth at various temperatures.
CC {ECO:0000269|PubMed:9524252}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10759889}.
CC -!- INDUCTION: Increases a few-fold upon upshift to 42 degrees Celsius.
CC {ECO:0000269|PubMed:9524252}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; U59434; AAC18441.1; -; mRNA.
DR EMBL; CU329670; CAC08562.1; -; Genomic_DNA.
DR EMBL; AB027800; BAA87104.1; -; Genomic_DNA.
DR PIR; JC6562; JC6562.
DR RefSeq; XP_001713060.1; XM_001713008.2.
DR AlphaFoldDB; O59838; -.
DR SMR; O59838; -.
DR BioGRID; 280590; 10.
DR IntAct; O59838; 1.
DR STRING; 4896.SPAC110.04c.1; -.
DR iPTMnet; O59838; -.
DR MaxQB; O59838; -.
DR PaxDb; O59838; -.
DR PRIDE; O59838; -.
DR EnsemblFungi; SPAC110.04c.1; SPAC110.04c.1:pep; SPAC110.04c.
DR PomBase; SPAC110.04c; pss1.
DR VEuPathDB; FungiDB:SPAC110.04c; -.
DR eggNOG; KOG0103; Eukaryota.
DR HOGENOM; CLU_005965_5_1_1; -.
DR InParanoid; O59838; -.
DR OMA; AYDRHFG; -.
DR PhylomeDB; O59838; -.
DR PRO; PR:O59838; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; ISO:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; ISO:PomBase.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 2.60.34.10; -; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029048; HSP70_C_sf.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR Pfam; PF00012; HSP70; 1.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF100934; SSF100934; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS01036; HSP70_3; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Stress response.
FT CHAIN 1..720
FT /note="Heat shock protein homolog pss1"
FT /id="PRO_0000078382"
FT REGION 658..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..686
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 39
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 573
FT /note="V -> E (in Ref. 1; AAC18441)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 720 AA; 80375 MW; 7F14E05ABAC154C9 CRC64;
MSSRTNVVGI DFGNSKTVIA VARNRAIDVI VNEVSNRSTP SLVSYGERSR FLGEAAKSAE
ASNFRNTVGS LKRLAGRTYD DPEIKDIESN FISAKLTEVD GFVGAKVQYL NEETAFSNIQ
LIAAYFTKIK AIAEAELIGS VSDVVISIPA WFTDIQRRAL LEAANIAGLN PLRLMNDNAA
AALTYGITKT DLPEPESPRR VAIVDFGHSN YSVSIVEFSR GQFHIKSTVC DRNLGSRNMD
KALIDYFAAE FKEKYKIDVL SNPKATFRLA TAVERLKKVL SANANAPLNV EMIMNDIDAS
SFIKRSDFEE LIKPLLERLT PPIEKALELA GIKKEDLYSI EMVGGCTRVP IVKEVIANYF
GKGLSFTLNQ DEAVARGCAL SCAILSPVFR VREFHVHDVT TYPITFSWEP IPENPEEDSS
LEVFSEGNPI PSTKILTFYR KAPFKLLAAY SKEAQLPGSI KQNIAQYLIN DVVPNKDGDL
SIVKIKVRLD LHGILVVEQA YIVEEQEVEE PVETSPEEEA EKKTDEPVKM RKVKKLVKVA
DLSVSVQEDR LPTEVLEKYR EAEHQMIATD KLVAETVDRK NALEEYIYDT RAKLDDIYAP
FTNEEESSKF KEMLTKAEDW LYEEGEDTTK AVYTAKLEDL MRVGGPIRQR YLDAEEAKRQ
KVQAEREAAK AATKSEAEKQ KPSGKFEEGT GGRAPPPPPA EEVAPENEEV ETMEIDEQKE
