HSP83_DROPS
ID HSP83_DROPS Reviewed; 717 AA.
AC P04809; O16059; O16060; O16061; O16062; O16063; O16064; O16065; O16066;
AC O16067; O18670; Q2M0F2;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Heat shock protein 83;
DE AltName: Full=HSP 82;
GN Name=Hsp83; Synonyms=Hsp82; ORFNames=GA11622;
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MV2-25 / Tucson 14011-0121.94;
RX PubMed=15632085; DOI=10.1101/gr.3059305;
RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA Weinstock G.M., Gibbs R.A.;
RT "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT gene, and cis-element evolution.";
RL Genome Res. 15:1-18(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-375.
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-269, AND VARIANTS.
RC STRAIN=pseudo1, pseudo10, pseudo11, pseudo2, pseudo3, pseudo4, pseudo5,
RC pseudo6, pseudo7, pseudo8, and pseudo9;
RX PubMed=9383055; DOI=10.1093/genetics/147.3.1091;
RA Wang R.L., Wakeley J., Hey J.;
RT "Gene flow and natural selection in the origin of Drosophila pseudoobscura
RT and close relatives.";
RL Genetics 147:1091-1106(1997).
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 -!- 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAL30982.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH379069; EAL30982.1; ALT_SEQ; Genomic_DNA.
DR EMBL; X03812; CAA27439.1; -; Genomic_DNA.
DR EMBL; AF006529; AAC07914.1; -; Genomic_DNA.
DR EMBL; AF006530; AAC07915.1; -; Genomic_DNA.
DR EMBL; AF006531; AAC07916.1; -; Genomic_DNA.
DR EMBL; AF006532; AAC07917.1; -; Genomic_DNA.
DR EMBL; AF006533; AAC07918.1; -; Genomic_DNA.
DR EMBL; AF006534; AAC07919.1; -; Genomic_DNA.
DR EMBL; AF006535; AAC07920.1; -; Genomic_DNA.
DR EMBL; AF006536; AAC07921.1; -; Genomic_DNA.
DR EMBL; AF006537; AAC07922.1; -; Genomic_DNA.
DR EMBL; AF006538; AAC07923.1; -; Genomic_DNA.
DR EMBL; AF006539; AAC07924.1; -; Genomic_DNA.
DR PIR; C24827; C24827.
DR RefSeq; XP_001353471.1; XM_001353435.3.
DR AlphaFoldDB; P04809; -.
DR SMR; P04809; -.
DR STRING; 7237.FBpp0274520; -.
DR PRIDE; P04809; -.
DR EnsemblMetazoa; FBtr0276082; FBpp0274520; FBgn0012701.
DR GeneID; 4813013; -.
DR KEGG; dpo:Dpse_GA11622; -.
DR eggNOG; KOG0019; Eukaryota.
DR HOGENOM; CLU_006684_1_3_1; -.
DR InParanoid; P04809; -.
DR OMA; MRRMKEM; -.
DR PhylomeDB; P04809; -.
DR ChiTaRS; Hsp83; fly.
DR Proteomes; UP000001819; Chromosome X.
DR Bgee; FBgn0012701; Expressed in female reproductive system 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; 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 3: Inferred from homology;
KW ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Reference proteome;
KW Stress response.
FT CHAIN 1..717
FT /note="Heat shock protein 83"
FT /id="PRO_0000062934"
FT REGION 213..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 687..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 713..717
FT /note="TPR repeat-binding"
FT COMPBIAS 227..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 BINDING 385
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT VARIANT 171
FT /note="G -> S (in strain: pseudo8 and pseudo9)"
SQ SEQUENCE 717 AA; 81771 MW; BF46AF2207322273 CRC64;
MPEEAETFAF QAEIAQLMSL IINTFYSNKE IFLRELISNA SDALDKIRYE SLTDPSKLDS
GKELYIKLIP NKTAGTLTII DTGIGMTKSD LVNNLGTIAK SGTKAFMEAL QAGADISMIG
QFGVGFYSAY LIADRVTVTS KNNDDEQYVW ESSAGGSFTV KADNSEPLGR GTKIVLYIKE
DQTDYLEESK IKEIVNKHSQ FIGYPIKLLV EKEREKEVSD DEADDEKKDD EAKKDMDTDE
PKIEDVGEDE DADKKDKDGK KKKTIKEKYT EDEELNKTKP IWTRNPDDIS QEEYGEFYKS
LTNDWEDHLC VKHFSVEGQL EFRALLFIPR RTPFDLFENQ KKRNNIKLYV RRVFIMDNCE
DLIPEYLNFI KGVVDSEDLP LNISREMLQQ NKVLKVIRKN LVKKTMELIE ELTEDKENYK
KFYEQFSKNL KLGVHEDSNN RAKLADFLRF HTSASGDDFC SLSDYVSRMK ENQKHVYFIT
GESKDQVSNS AFVERVKARG FEVVYMTEPI DEYVIQHLKE YKGKQLVSVT KEGLELPEDE
AEKKKREEDK AKFEGLCKLM KSILDSKVEK VVVSNRLVDS PCCIVTSQFG WSANMERIMK
AQALRDTATM GYMAGKKQLE INPDHPIVEA LRQKADADKN DKAVKDLVIL LFETSLLSSG
FSLDSPQVHA SRIYRMIKLG LGIDEDEPMT TEDAHSGGDA PGLVEDTEDA SHMEEVD
