HSP90_SCHPO
ID HSP90_SCHPO Reviewed; 704 AA.
AC P41887; Q9UUG4;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Heat shock protein 90 homolog;
GN Name=swo1; Synonyms=hsp90; ORFNames=SPAC926.04c;
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 [GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=7813446; DOI=10.1002/j.1460-2075.1994.tb06956.x;
RA Aligue R., Akhavan-Niaki H., Russell P.;
RT "A role for Hsp90 in cell cycle control: Wee1 tyrosine kinase activity
RT requires interaction with Hsp90.";
RL EMBO J. 13:6099-6106(1994).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245; SER-277 AND SER-286, 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: Molecular chaperone that promotes the maturation, structural
CC maintenance and proper regulation of specific target proteins involved
CC for instance in cell cycle control and signal transduction. Undergoes a
CC functional cycle that is linked to its ATPase activity. This cycle
CC probably induces conformational changes in the client proteins, thereby
CC causing their activation. Interacts dynamically with various co-
CC chaperones that modulate its substrate recognition, ATPase cycle and
CC chaperone function (By similarity). Interacts with the wee1 protein
CC kinase; which requires swo1 for its activation. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DOMAIN: The TPR repeat-binding motif mediates interaction with TPR
CC repeat-containing proteins. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family. {ECO:0000305}.
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DR EMBL; L35550; AAC41646.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB54152.1; -; Genomic_DNA.
DR PIR; S51795; S51795.
DR PIR; T39202; T39202.
DR RefSeq; NP_594365.1; NM_001019786.2.
DR AlphaFoldDB; P41887; -.
DR SMR; P41887; -.
DR BioGRID; 279956; 30.
DR IntAct; P41887; 1.
DR STRING; 4896.SPAC926.04c.1; -.
DR iPTMnet; P41887; -.
DR MaxQB; P41887; -.
DR PaxDb; P41887; -.
DR PRIDE; P41887; -.
DR EnsemblFungi; SPAC926.04c.1; SPAC926.04c.1:pep; SPAC926.04c.
DR GeneID; 2543539; -.
DR KEGG; spo:SPAC926.04c; -.
DR PomBase; SPAC926.04c; -.
DR VEuPathDB; FungiDB:SPAC926.04c; -.
DR eggNOG; KOG0019; Eukaryota.
DR HOGENOM; CLU_006684_1_3_1; -.
DR InParanoid; P41887; -.
DR OMA; MRRMKEM; -.
DR PhylomeDB; P41887; -.
DR Reactome; R-SPO-1474151; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
DR Reactome; R-SPO-203615; eNOS activation.
DR Reactome; R-SPO-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-SPO-3371511; HSF1 activation.
DR Reactome; R-SPO-3371571; HSF1-dependent transactivation.
DR Reactome; R-SPO-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-SPO-6798695; Neutrophil degranulation.
DR Reactome; R-SPO-844456; The NLRP3 inflammasome.
DR Reactome; R-SPO-9009391; Extra-nuclear estrogen signaling.
DR PRO; PR:P41887; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005739; C:mitochondrion; ISO:PomBase.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0140453; C:protein aggregate center; IDA:PomBase.
DR GO; GO:0032991; C:protein-containing complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IDA:PomBase.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:CACAO.
DR GO; GO:0044183; F:protein folding chaperone; EXP:PomBase.
DR GO; GO:0051082; F:unfolded protein binding; IDA:PomBase.
DR GO; GO:0006458; P:'de novo' protein folding; ISO:PomBase.
DR GO; GO:0010619; P:adenylate cyclase-activating glucose-activated G protein-coupled receptor signaling pathway; IMP:PomBase.
DR GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IDA:CACAO.
DR GO; GO:0031048; P:heterochromatin assembly by small RNA; IMP:PomBase.
DR GO; GO:0006457; P:protein folding; IDA:PomBase.
DR GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
DR Gene3D; 1.20.120.790; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR HAMAP; MF_00505; HSP90; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR019805; Heat_shock_protein_90_CS.
DR InterPro; IPR037196; HSP90_C.
DR InterPro; IPR001404; Hsp90_fam.
DR InterPro; IPR020575; Hsp90_N.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR PANTHER; PTHR11528; PTHR11528; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00183; HSP90; 1.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF110942; SSF110942; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS00298; HSP90; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..704
FT /note="Heat shock protein 90 homolog"
FT /id="PRO_0000062963"
FT REGION 213..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 678..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 700..704
FT /note="TPR repeat-binding"
FT COMPBIAS 230..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 38
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 80
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 375
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 10..11
FT /note="EA -> DW (in Ref. 1; AAC41646)"
FT /evidence="ECO:0000305"
FT CONFLICT 77
FT /note="S -> T (in Ref. 1; AAC41646)"
FT /evidence="ECO:0000305"
FT CONFLICT 591..594
FT /note="AQAL -> LKPS (in Ref. 1; AAC41646)"
FT /evidence="ECO:0000305"
FT CONFLICT 655
FT /note="D -> H (in Ref. 1; AAC41646)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 704 AA; 80596 MW; 4E18B95722840768 CRC64;
MSNTETFKFE AEISQLMSLI INTVYSNKEI FLRELISNAS DALDKIRYQS LSDPHALDAE
KDLFIRITPD KENKILSIRD TGIGMTKNDL INNLGVIAKS GTKQFMEAAA SGADISMIGQ
FGVGFYSAYL VADKVQVVSK HNDDEQYIWE SSAGGSFTVT LDTDGPRLLR GTEIRLFMKE
DQLQYLEEKT IKDTVKKHSE FISYPIQLVV TREVEKEVPE EEETEEVKNE EDDKAPKIEE
VDDESEKKEK KTKKVKETTT ETEELNKTKP IWTRNPSEVT KEEYASFYKS LTNDWEDHLA
VKHFSVEGQL EFRAILFVPR RAPMDLFEAK RKKNNIKLYV RRVFITDDCE ELIPEWLGFI
KGVVDSEDLP LNLSREMLQQ NKIMKVIRKN LVRRCLDMFN EIAEDKENFK TFYDAFSKNL
KLGIHEDAAN RPALAKLLRY NSLNSPDDLI SLEDYITKMP EHQKNIYFIT GESKQAVENS
PFLEIFRAKK FDVLFMVDPI DEYAVTQLKE FEGKKLVNIT KDGLELEETD EEKAAREKLE
KEYEEFAKQL KTILGDKVEK VVVSNKIVGS PCLLTTGQYG WSANMERIMK AQALRDTSMS
AYMSSRKTFE INPKSPIIAE LKKKVEENGA EDRSVKDLAT ILYETALLSS GFTLDDPSAY
AQRINRLISL GLSIDEEEEA PIEEISTESV AAENNAESKM EEVD
