HSP70_DROME
ID HSP70_DROME Reviewed; 642 AA.
AC P82910; Q5BI85; Q8MT04; Q95NG7; Q9BIS5;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Major heat shock 70 kDa protein Aa;
DE Short=Heat shock protein 70Aa;
DE AltName: Full=HSP70-87A7;
GN Name=Hsp70Aa; Synonyms=Hsp70A; ORFNames=CG31366;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=122, 3CPA126, 3CPA2, 3CPA35, 3CPA43, 3CPA47, 3CPA61, 3CPA81, 3CPA86,
RC AUS, B28, FrV3-1, QD18, and Z(H)1;
RX PubMed=11965431; DOI=10.1007/s00239-001-0044-7;
RA Bettencourt B.R., Feder M.E.;
RT "Rapid concerted evolution via gene conversion at the Drosophila hsp70
RT genes.";
RL J. Mol. Evol. 54:569-586(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Testis;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Larva, and Pupae;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INTERACTION WITH DPIT47 AND HSP83.
RX PubMed=11493638; DOI=10.1242/jcs.114.11.2015;
RA Crevel G., Bates H., Huikeshoven H., Cotterill S.;
RT "The Drosophila Dpit47 protein is a nuclear Hsp90 co-chaperone that
RT interacts with DNA polymerase alpha.";
RL J. Cell Sci. 114:2015-2025(2001).
CC -!- SUBUNIT: Forms a complex with Hsp83 and Dpit47.
CC {ECO:0000269|PubMed:11493638}.
CC -!- INDUCTION: Heat shock induces the synthesis of seven proteins at five
CC otherwise inactive sites in the polytene chromosomes of fruit fly
CC larvae. Two separate sites, producing two and three copies,
CC respectively, code for the 70 kDa protein.
CC -!- MISCELLANEOUS: There are two copies of the gene coding for this protein
CC at chromosome locus 87A7.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM49826.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF295933; AAG26887.1; -; Genomic_DNA.
DR EMBL; AF295934; AAG26888.1; -; Genomic_DNA.
DR EMBL; AF295935; AAG26889.1; -; Genomic_DNA.
DR EMBL; AF295936; AAG26890.1; -; Genomic_DNA.
DR EMBL; AF295937; AAG26891.1; -; Genomic_DNA.
DR EMBL; AF295938; AAG26892.1; -; Genomic_DNA.
DR EMBL; AF350452; AAK30209.1; -; Genomic_DNA.
DR EMBL; AF350453; AAK30210.1; -; Genomic_DNA.
DR EMBL; AF350454; AAK30211.1; -; Genomic_DNA.
DR EMBL; AF350455; AAK30212.1; -; Genomic_DNA.
DR EMBL; AF350456; AAK30213.1; -; Genomic_DNA.
DR EMBL; AF350457; AAK30214.1; -; Genomic_DNA.
DR EMBL; AF350458; AAK30215.1; -; Genomic_DNA.
DR EMBL; AF350459; AAK30216.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13535.1; -; Genomic_DNA.
DR EMBL; AY118457; AAM49826.1; ALT_FRAME; mRNA.
DR EMBL; BT021339; AAX33487.1; -; mRNA.
DR RefSeq; NP_524798.2; NM_080059.3.
DR RefSeq; NP_731651.1; NM_169441.2.
DR AlphaFoldDB; P82910; -.
DR SMR; P82910; -.
DR BioGRID; 69381; 50.
DR BioGRID; 71511; 62.
DR DIP; DIP-19548N; -.
DR STRING; 7227.FBpp0081956; -.
DR PaxDb; P82910; -.
DR DNASU; 48581; -.
DR EnsemblMetazoa; FBtr0082482; FBpp0081956; FBgn0013276.
DR EnsemblMetazoa; FBtr0082512; FBpp0081986; FBgn0013275.
DR GeneID; 44920; -.
DR GeneID; 48581; -.
DR KEGG; dme:Dmel_CG18743; -.
DR KEGG; dme:Dmel_CG31366; -.
DR CTD; 44920; -.
DR CTD; 48581; -.
DR FlyBase; FBgn0013275; Hsp70Aa.
DR VEuPathDB; VectorBase:FBgn0013275; -.
DR VEuPathDB; VectorBase:FBgn0013276; -.
DR eggNOG; KOG0101; Eukaryota.
DR GeneTree; ENSGT00940000154813; -.
DR HOGENOM; CLU_005965_3_0_1; -.
DR InParanoid; P82910; -.
DR OrthoDB; 288077at2759; -.
DR PhylomeDB; P82910; -.
DR Reactome; R-DME-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-DME-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-DME-3371571; HSF1-dependent transactivation.
DR PRO; PR:P82910; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0013275; Expressed in seminal fluid secreting gland and 9 other tissues.
DR ExpressionAtlas; P82910; baseline and differential.
DR Genevisible; P82910; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0031072; F:heat shock protein binding; IBA:GO_Central.
DR GO; GO:0051787; F:misfolded protein binding; IBA:GO_Central.
DR GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0034620; P:cellular response to unfolded protein; IBA:GO_Central.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR GO; GO:0035080; P:heat shock-mediated polytene chromosome puffing; IMP:FlyBase.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0009408; P:response to heat; IMP:FlyBase.
DR GO; GO:0001666; P:response to hypoxia; IMP:FlyBase.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 2.60.34.10; -; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029048; HSP70_C_sf.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR PANTHER; PTHR19375; PTHR19375; 1.
DR Pfam; PF00012; HSP70; 1.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF100934; SSF100934; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Nucleotide-binding; Reference proteome; Stress response.
FT CHAIN 1..642
FT /note="Major heat shock 70 kDa protein Aa"
FT /id="PRO_0000078329"
FT REGION 609..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 69
FT /note="R -> G (in strain: 3CPA2)"
FT VARIANT 441
FT /note="Y -> S (in strain: FrV3-1)"
FT VARIANT 495
FT /note="K -> T (in strain: QD18)"
FT VARIANT 593
FT /note="L -> M (in strain: 122)"
FT VARIANT 615
FT /note="Missing (in strain: 122)"
FT VARIANT 636
FT /note="P -> R (in strain: QD18)"
FT CONFLICT 139..143
FT /note="Missing (in Ref. 4; AAM49826)"
FT /evidence="ECO:0000305"
FT CONFLICT 371
FT /note="A -> P (in Ref. 4; AAM49826)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 642 AA; 70160 MW; EC08E94412E27F84 CRC64;
MPAIGIDLGT TYSCVGVYQH GKVEIIANDQ GNRTTPSYVA FTDSERLIGD PAKNQVAMNP
RNTVFDAKRL IGRKYDDPKI AEDMKHWPFK VVSDGGKPKI GVEYKGESKR FAPEEISSMV
LTKMKETAEA YLGESITDAV ITVPAYFNDS QRQATKDAGH IAGLNVLRII NEPTAAALAY
GLDKNLKGER NVLIFDLGGG TFDVSILTID EGSLFEVRST AGDTHLGGED FDNRLVTHLA
DEFKRKYKKD LRSNPRALRR LRTAAERAKR TLSSSTEATI EIDALFEGQD FYTKVSRARF
EELCADLFRN TLQPVEKALN DAKMDKGQIH DIVLVGGSTR IPKVQSLLQD FFHGKNLNLS
INPDEAVAYG AAVQAAILSG DQSGKIQDVL LVDVAPLSLG IETAGGVMTK LIERNCRIPC
KQTKTFSTYA DNQPGVSIQV YEGERAMTKD NNALGTFDLS GIPPAPRGVP QIEVTFDLDA
NGILNVSAKE MSTGKAKNIT IKNDKGRLSQ AEIDRMVNEA EKYADEDEKH RQRITSRNAL
ESYVFNVKQA VEQAPAGKLD EADKNSVLDK CNDTIRWLDS NTTAEKEEFD HKLEELTRHC
SPIMTKMHQQ GAGAGAGGPG ANCGQQAGGF GGYSGPTVEE VD
