HSC90_DICDI
ID HSC90_DICDI Reviewed; 700 AA.
AC P54651; Q55FQ1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Heat shock cognate 90 kDa protein;
GN Name=hspD; Synonyms=hsc90, hsp90; ORFNames=DDB_G0267400;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=AX3;
RA Boves H., Dittrich W., Mintert U., Lottspeich F., Gerisch G., Faix J.;
RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16512674; DOI=10.1021/pr050350q;
RA Reinders Y., Schulz I., Graef R., Sickmann A.;
RT "Identification of novel centrosomal proteins in Dictyostelium discoideum
RT by comparative proteomic approaches.";
RL J. Proteome Res. 5:589-598(2006).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=AX2;
RX PubMed=16926386; DOI=10.1074/mcp.m600113-mcp200;
RA Gotthardt D., Blancheteau V., Bosserhoff A., Ruppert T., Delorenzi M.,
RA Soldati T.;
RT "Proteomics fingerprinting of phagosome maturation and evidence for the
RT role of a Galpha during uptake.";
RL Mol. Cell. Proteomics 5:2228-2243(2006).
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). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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; L43591; AAA69917.1; -; mRNA.
DR EMBL; AAFI02000003; EAL73152.1; -; Genomic_DNA.
DR RefSeq; XP_647482.1; XM_642390.1.
DR PDB; 4XC0; X-ray; 1.77 A; A=1-223.
DR PDB; 4XCJ; X-ray; 1.75 A; A=1-223.
DR PDB; 4XCL; X-ray; 1.21 A; A=1-223.
DR PDB; 4XD8; X-ray; 1.55 A; A=1-223.
DR PDB; 4XDM; X-ray; 1.50 A; A=1-223.
DR PDB; 4XE2; X-ray; 1.20 A; A=1-223.
DR PDB; 4XKA; X-ray; 2.00 A; A=1-223.
DR PDB; 4XKK; X-ray; 2.70 A; A=1-223.
DR PDB; 4XKO; X-ray; 2.46 A; A=1-223.
DR PDBsum; 4XC0; -.
DR PDBsum; 4XCJ; -.
DR PDBsum; 4XCL; -.
DR PDBsum; 4XD8; -.
DR PDBsum; 4XDM; -.
DR PDBsum; 4XE2; -.
DR PDBsum; 4XKA; -.
DR PDBsum; 4XKK; -.
DR PDBsum; 4XKO; -.
DR AlphaFoldDB; P54651; -.
DR SMR; P54651; -.
DR IntAct; P54651; 2.
DR STRING; 44689.DDB0191163; -.
DR PaxDb; P54651; -.
DR PRIDE; P54651; -.
DR EnsemblProtists; EAL73152; EAL73152; DDB_G0267400.
DR GeneID; 8616289; -.
DR KEGG; ddi:DDB_G0267400; -.
DR dictyBase; DDB_G0267400; hspD.
DR eggNOG; KOG0019; Eukaryota.
DR HOGENOM; CLU_006684_1_3_1; -.
DR InParanoid; P54651; -.
DR OMA; TRMKAEQ; -.
DR PhylomeDB; P54651; -.
DR Reactome; R-DDI-1474151; Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation.
DR Reactome; R-DDI-203615; eNOS activation.
DR Reactome; R-DDI-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-DDI-3371511; HSF1 activation.
DR Reactome; R-DDI-3371571; HSF1-dependent transactivation.
DR Reactome; R-DDI-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR Reactome; R-DDI-844456; The NLRP3 inflammasome.
DR Reactome; R-DDI-8939211; ESR-mediated signaling.
DR Reactome; R-DDI-9009391; Extra-nuclear estrogen signaling.
DR PRO; PR:P54651; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005829; C:cytosol; IDA:dictyBase.
DR GO; GO:0031012; C:extracellular matrix; HDA:dictyBase.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IBA:GO_Central.
DR GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0050821; P:protein stabilization; IMP:dictyBase.
DR GO; GO:0060176; P:regulation of aggregation involved in sorocarp development; IMP:dictyBase.
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 3D-structure; ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding;
KW Reference proteome; Stress response.
FT CHAIN 1..700
FT /note="Heat shock cognate 90 kDa protein"
FT /id="PRO_0000062928"
FT REGION 665..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 696..700
FT /note="TPR repeat-binding"
FT COMPBIAS 665..684
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 95
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 128
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 368
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT CONFLICT 670
FT /note="A -> S (in Ref. 1; AAA69917)"
FT /evidence="ECO:0000305"
FT STRAND 6..10
FT /evidence="ECO:0007829|PDB:4XE2"
FT HELIX 13..23
FT /evidence="ECO:0007829|PDB:4XE2"
FT HELIX 32..54
FT /evidence="ECO:0007829|PDB:4XE2"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:4XE2"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:4XE2"
FT TURN 73..76
FT /evidence="ECO:0007829|PDB:4XE2"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:4XE2"
FT HELIX 89..95
FT /evidence="ECO:0007829|PDB:4XE2"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:4XE2"
FT HELIX 104..113
FT /evidence="ECO:0007829|PDB:4XE2"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:4XE2"
FT HELIX 118..124
FT /evidence="ECO:0007829|PDB:4XE2"
FT HELIX 127..133
FT /evidence="ECO:0007829|PDB:4XE2"
FT STRAND 135..143
FT /evidence="ECO:0007829|PDB:4XE2"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:4XE2"
FT STRAND 159..164
FT /evidence="ECO:0007829|PDB:4XE2"
FT STRAND 171..180
FT /evidence="ECO:0007829|PDB:4XE2"
FT HELIX 182..188
FT /evidence="ECO:0007829|PDB:4XE2"
FT HELIX 190..199
FT /evidence="ECO:0007829|PDB:4XE2"
FT TURN 200..203
FT /evidence="ECO:0007829|PDB:4XKA"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:4XE2"
SQ SEQUENCE 700 AA; 79866 MW; 91D5ECF238088FF2 CRC64;
MAESQVERFT FQAEINQLMS LIINTFYSNK EVFLRELISN ASDALDKIRY QSLTDASVLE
SKTELEIKII PDKTAKTLTL IDSGIGMTKT DMVKNLGTIA RSGTKNFMEQ LQSGAADISM
IGQFGVGFYS AYLVADTVIV HSKNNDDEQY VWESSAGGEF TIALDHTEPL GRGTKIVLHM
KEDQLDYLDE TKIKNLVKKH SEFIQYPISL LTIKEKEVDE ETTAKEGEEE STDAKIEEIE
EEKEKKKVKV QEKEWDVLNK TKPLWTRNPS DVTKEEYNSF YKSISNDWEE PLAVKHFSVE
GQLEFKAILF VPKKAPFDLF ESKKKANNIK LYVKRVFIMD NCADIIPEYL NFVRGIVDSE
DLPLNISRET LQQNKILTVI RKNLVKKCIE LFNEIAENSE DYKKFYEAFS KNLKLGVHED
SQNREKFADL LRYQTSKSGD ELVTLKEYVG RMKEGQNEIY YITGESKKAV ENSPFIEGLK
KKNLEVIYMC DPIDEYAVQQ LKEYDGKKLV SITKEGLKLD ETEDEKKKAE QDKAANEELL
KQVKDVLGDK VEKVVLSTRL ANSPCVLVTS EYGWSANMER IMKAQALRDS SMSSYMSSKK
TLELNPDHPI VRDLAKKAAE KSKTFKDFVY LLYETALLTS GFSLDEPSSF ASRIHRMIKL
GLSIQDDSSA TTEESTNTTT SDDIPPLEEN DEPSEMEKVD
