HSP83_DROVI
ID HSP83_DROVI Reviewed; 374 AA.
AC P04811;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Heat shock protein 83;
DE AltName: Full=HSP 82;
DE Flags: Fragment;
GN Name=Hsp83; Synonyms=Hsp82;
OS Drosophila virilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7244;
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}.
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DR EMBL; X03813; CAA27441.1; -; Genomic_DNA.
DR PIR; D24827; D24827.
DR AlphaFoldDB; P04811; -.
DR SMR; P04811; -.
DR STRING; 7244.FBpp0227597; -.
DR EnsemblMetazoa; FBtr0229105; FBpp0227597; FBgn0013086.
DR eggNOG; KOG0019; Eukaryota.
DR OrthoDB; 924636at2759; -.
DR ChiTaRS; Hsp83; fly.
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..>374
FT /note="Heat shock protein 83"
FT /id="PRO_0000062936"
FT REGION 213..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..262
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 374
SQ SEQUENCE 374 AA; 42814 MW; AA896438B4FB4CB1 CRC64;
MPEEAETFAF QAEIAQLMSL IINTFYSNKE IFLRELISNA SDALDKIRYE SLTDPSKLDS
GKELYIKLIP NKTAGTLTII DTGIGMTKSD LVNNLGTIAK SGTKAFMEAL QAGADISMIG
QFGVGFYSAY LVADKVTVTS KNNDDEQYVW ESSAGGSFTV RADNSEPLGR GTKIVLFIKE
DQTDYLEESK IKEIVNKHSQ FIGYPIKLLV EKEREKEVSD DEDDEKKEGD EKKEMDTDEP
KIEDVGEDED ADKKDKDAKK KKTIKEKYTE DEELNKTKPI WTRNPDDISQ EEYGEFYKSL
TNDWEDHLAV KHFSVEGQLE FRALLFIPRR TPFDLFENQK KRNNIKLYVR RVFIMDNCED
LIPEYLNFIK GVVD
