HSP83_DROSI
ID HSP83_DROSI Reviewed; 375 AA.
AC P04810;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Heat shock protein 83;
DE AltName: Full=HSP 82;
DE Flags: Fragment;
GN Name=Hsp83; Synonyms=Hsp82;
OS Drosophila simulans (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7240;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2426456; DOI=10.1016/s0022-2836(86)80001-8;
RA Blackman R.K., Meselson M.;
RT "Interspecific nucleotide sequence comparisons used to identify regulatory
RT and structural features of the Drosophila hsp82 gene.";
RL J. Mol. Biol. 188:499-515(1986).
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. Required for piRNA biogenesis by facilitating
CC loading of piRNAs into PIWI proteins (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Interacts with shu (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 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; X03811; CAA27438.1; -; Genomic_DNA.
DR PIR; B24827; B24827.
DR AlphaFoldDB; P04810; -.
DR SMR; P04810; -.
DR EnsemblMetazoa; FBtr0213649; FBpp0212141; FBgn0012840.
DR ChiTaRS; Hsp83; fly.
DR Bgee; FBgn0012840; Expressed in embryo and 3 other tissues.
DR GO; GO:0005813; C:centrosome; IEA:EnsemblMetazoa.
DR GO; GO:0101031; C:chaperone complex; IEA:EnsemblMetazoa.
DR GO; GO:0034663; C:endoplasmic reticulum chaperone complex; IEA:EnsemblMetazoa.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:EnsemblMetazoa.
DR GO; GO:0005705; C:polytene chromosome interband; IEA:EnsemblMetazoa.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0005158; F:insulin receptor binding; IEA:EnsemblMetazoa.
DR GO; GO:0030911; F:TPR domain binding; IEA:EnsemblMetazoa.
DR GO; GO:0051082; F:unfolded protein binding; IEA:EnsemblMetazoa.
DR GO; GO:0007098; P:centrosome cycle; IEA:EnsemblMetazoa.
DR GO; GO:0009631; P:cold acclimation; IEA:EnsemblMetazoa.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:EnsemblMetazoa.
DR GO; GO:0010529; P:negative regulation of transposition; IEA:EnsemblMetazoa.
DR GO; GO:0019094; P:pole plasm mRNA localization; IEA:EnsemblMetazoa.
DR GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IEA:EnsemblMetazoa.
DR GO; GO:0002052; P:positive regulation of neuroblast proliferation; IEA:EnsemblMetazoa.
DR GO; GO:0043248; P:proteasome assembly; IEA:EnsemblMetazoa.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR GO; GO:0045187; P:regulation of circadian sleep/wake cycle, sleep; IEA:EnsemblMetazoa.
DR GO; GO:0009408; P:response to heat; IEA:EnsemblMetazoa.
DR GO; GO:0070922; P:RISC complex assembly; IEA:EnsemblMetazoa.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR019805; Heat_shock_protein_90_CS.
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 PRINTS; PR00775; HEATSHOCK90.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS00298; HSP90; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Stress response.
FT CHAIN 1..>375
FT /note="Heat shock protein 83"
FT /id="PRO_0000062935"
FT REGION 213..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 126
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT NON_TER 375
SQ SEQUENCE 375 AA; 42933 MW; 42D83FF07E4828A1 CRC64;
MPEEAETFAF QAEIAQLMSL IINTFYSNKE IFLRELISNA SDALDKIRYE SLTDPSKLDS
GKELYIKLIP NKTAGTLTII DTGIGMTKSD LVNNLGTIAK SGTKAFMEAL QAGADISMIG
QFGVGFYSAY LVADKVTVTS KNNDDEQYVW ESSAGGSFTV RADNSEPLGR GTKIVLYIKE
DQTDYLEESK IKEIVNKHSQ FIGYPIKLLV EKEREKEVSD DEADDEKKEG DEKKEMETDE
PKIEDVGEDE DADKKDKDAK KKKTIKEKYT EDEELNKTKP IWTRNPDDIS QEEYGEFYKS
LTNDWEDHLA VKHFSVEGQL EFRALLFIPR RTPFDLFENQ KKRNNIKLYV RRVFIMDNCE
DLIPEYLNFM KGVVD
