ID HSP83_BOMMO Reviewed; 716 AA.
AC Q9BLC5; D6N7U7;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 24-JAN-2024, entry version 123.
DE RecName: Full=Heat shock protein 83;
DE Short=BmHSP90;
GN Name=Hsp83; Synonyms=Hsp90;
OS Bombyx mori (Silk moth).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC Bombycidae; Bombycinae; Bombyx.
OX NCBI_TaxID=7091;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C108; TISSUE=Wing imaginal disk;
RX PubMed=11418243; DOI=10.1016/s0378-1119(01)00523-6;
RA Landais I., Pommet J., Mita K., Nohata J., Gimenez S., Fournier P.,
RA Devauchelle G., Duonor-Cerutti M., Ogliastro M.;
RT "Characterization of the cDNA encoding the 90 kDa heat-shock protein in the
RT Lepidoptera Bombyx mori and Spodoptera frugiperda.";
RL Gene 271:223-231(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=p50T;
RX PubMed=19121390; DOI=10.1016/j.ibmb.2008.11.004;
RG International Silkworm Genome Consortium;
RT "The genome of a lepidopteran model insect, the silkworm Bombyx mori.";
RL Insect Biochem. Mol. Biol. 38:1036-1045(2008).
RN [3]
RP INTERACTION WITH SHU.
RX PubMed=22902560; DOI=10.1016/j.molcel.2012.07.019;
RA Xiol J., Cora E., Koglgruber R., Chuma S., Subramanian S., Hosokawa M.,
RA Reuter M., Yang Z., Berninger P., Palencia A., Benes V., Penninger J.,
RA Sachidanandam R., Pillai R.S.;
RT "A role for Fkbp6 and the chaperone machinery in piRNA amplification and
RT transposon silencing.";
RL Mol. Cell 47:970-979(2012).
RN [4]
RP FUNCTION.
RX PubMed=23681506; DOI=10.1261/rna.037200.112;
RA Izumi N., Kawaoka S., Yasuhara S., Suzuki Y., Sugano S., Katsuma S.,
RA Tomari Y.;
RT "Hsp90 facilitates accurate loading of precursor piRNAs into PIWI
RT proteins.";
RL RNA 19:896-901(2013).
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). Required for piRNA biogenesis by
CC facilitating loading of piRNAs into PIWI proteins. {ECO:0000250,
CC ECO:0000269|PubMed:23681506}.
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 (By similarity). Interacts with shu.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family. {ECO:0000305}.
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DR EMBL; AB060275; BAB41209.1; -; mRNA.
DR EMBL; GU324473; ADG57739.1; -; Genomic_DNA.
DR EMBL; HQ437671; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001036876.1; NM_001043411.1.
DR AlphaFoldDB; Q9BLC5; -.
DR SMR; Q9BLC5; -.
DR STRING; 7091.Q9BLC5; -.
DR PaxDb; 7091-BGIBMGA004612-TA; -.
DR EnsemblMetazoa; NM_001043411.1; NP_001036876.1; GeneID_692420.
DR GeneID; 692420; -.
DR KEGG; bmor:692420; -.
DR CTD; 692420; -.
DR eggNOG; KOG0019; Eukaryota.
DR HOGENOM; CLU_006684_1_3_1; -.
DR InParanoid; Q9BLC5; -.
DR OMA; MRRMKEM; -.
DR OrthoDB; 547579at2759; -.
DR Proteomes; UP000005204; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR CDD; cd16927; HATPase_Hsp90-like; 1.
DR Gene3D; 3.30.230.80; -; 1.
DR Gene3D; 3.40.50.11260; -; 1.
DR Gene3D; 1.20.120.790; Heat shock protein 90, C-terminal domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 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_Su5_D2-typ_SF.
DR PANTHER; PTHR11528:SF34; HEAT SHOCK PROTEIN 83; 1.
DR PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR Pfam; PF13589; HATPase_c_3; 1.
DR Pfam; PF00183; HSP90; 1.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF110942; HSP90 C-terminal domain; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS00298; HSP90; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Stress response.
FT CHAIN 1..716
FT /note="Heat shock protein 83"
FT /id="PRO_0000428731"
FT REGION 221..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 688..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 712..716
FT /note="TPR repeat-binding"
FT BINDING 46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 133
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"
SQ SEQUENCE 716 AA; 82422 MW; 92E15A7F466D1AE9 CRC64;
MPEEMETQPA EVETFAFQAE IAQLMSLIIN TFYSNKEIFL RELISNSSDA LDKIRYESLT
DPSKLDSGKE LYIKIIPNKN EGTLTIIDTG IGMTKADLVN NLGTIAKSGT KAFMEALQAG
ADISMIGQFG VGFYSSYLVA DRVTVHSKHN DDEQYVWESS AGGSFTVRPD SGEPLGRGTK
IVLHVKEDLA EFMEEHKIKE IVKKHSQFIG YPIKLMVEKE REKELSDDEA EEEKKEEEDE
KPKIEDVGED EDEDKKDTKK KKKTIKEKYT EDEELNKTKP IWTRNADDIT QDEYGDFYKS
LTNDWEDHLA VKHFSVEGQL EFRALLFVPR RAPFDLFENK KRKNNIKLYV RRVFIMDNCE
DLIPEYLNFI RGVVDSEDLP LNISREMLQQ NKILKVIRKN LVKKCLELFE ELAEDKENYK
KYYEQFSKNL KLGIHEDSQN RAKLSELLRY HTSASGDEAC SLKEYVSRMK ENQKHIYYIT
GENRDQVANS SFVERVKKRG YEVVYMTEPI DEYVVQQMRE YDGKTLVSVT KEGLELPEDE
EEKKKREEDK VKFEGLCKVM KNILDNKVEK VVVSNRLVES PCCIVTAQYG WSANMERIMK
AQALRDTSTM GYMAAKKHLE INPDHSIVET LRQKAEADKN DKAVKDLVIL LYETALLSSG
FTLDEPQVHA SRIYRMIKLG LGIDEDEPIQ VEEPASGDVP PLEGDADDAS RMEEVD
//
