HSP72_DROME
ID HSP72_DROME Reviewed; 641 AA.
AC Q8INI8; P02824; Q95NK0; Q95W08; Q9BIS1; Q9BIS3; Q9BIS4; Q9I7J6;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Major heat shock 70 kDa protein Ba;
DE Short=Heat shock protein 70Ba;
DE AltName: Full=HSP70-87C1;
GN Name=Hsp70Ba; ORFNames=CG31449;
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=NFS97, and SFS97;
RX PubMed=11687637; DOI=10.1073/pnas.231478298;
RA Michalak P., Minkov I., Helin A., Lerman D.N., Bettencourt B.R.,
RA Feder M.E., Korol A.B., Nevo E.;
RT "Genetic evidence for adaptation-driven incipient speciation of Drosophila
RT melanogaster along a microclimatic contrast in 'Evolution Canyon,'
RT Israel.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:13195-13200(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=T32;
RX PubMed=11441029; DOI=10.1242/jeb.204.11.1869;
RA Zatsepina O.G., Velikodvorskaia V.V., Molodtsov V.B., Garbuz D.,
RA Lerman D.N., Bettencourt B.R., Feder M.E., Evgenev M.B.;
RT "A Drosophila melanogaster strain from sub-equatorial Africa has
RT exceptional thermotolerance but decreased Hsp70 expression.";
RL J. Exp. Biol. 204:1869-1881(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=3CPA126, 3CPA2, 3CPA35, 3CPA43, 3CPA47, 3CPA61, 3CPA81, 3CPA86, A28,
RC AUS, 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 [4]
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 [5]
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).
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: Most strains have three copies of the gene coding for
CC this protein at chromosome locus 87C1; two tandemly repeated Hsp70
CC genes (Hsp70Bb and Hsp70Bc) and one in reverse orientation (Hsp70Ba).
CC Some strains, including that sequenced in the Drosophila genome project
CC have three tandemly repeated Hsp70 genes (Hsp70Bb, Hsp70Bbb and
CC Hsp70Bc).
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; AF385405; AAK67154.1; -; Genomic_DNA.
DR EMBL; AF385406; AAK67155.1; -; Genomic_DNA.
DR EMBL; AF385407; AAK67156.1; -; Genomic_DNA.
DR EMBL; AF385408; AAK67157.1; -; Genomic_DNA.
DR EMBL; AY032740; AAK62472.1; -; Genomic_DNA.
DR EMBL; AF295946; AAG26900.1; -; Genomic_DNA.
DR EMBL; AF295947; AAG26901.1; -; Genomic_DNA.
DR EMBL; AF295948; AAG26902.1; -; Genomic_DNA.
DR EMBL; AF295949; AAG26903.1; -; Genomic_DNA.
DR EMBL; AF295950; AAG26904.1; -; Genomic_DNA.
DR EMBL; AF350468; AAK30225.1; -; Genomic_DNA.
DR EMBL; AF350469; AAK30226.1; -; Genomic_DNA.
DR EMBL; AF350470; AAK30227.1; -; Genomic_DNA.
DR EMBL; AF350471; AAK30228.1; -; Genomic_DNA.
DR EMBL; AF350472; AAK30229.1; -; Genomic_DNA.
DR EMBL; AF350473; AAK30230.1; -; Genomic_DNA.
DR EMBL; AF350474; AAK30231.1; -; Genomic_DNA.
DR EMBL; AF350475; AAK30232.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13545.1; -; Genomic_DNA.
DR RefSeq; NP_524927.2; NM_080188.3.
DR RefSeq; NP_650209.1; NM_141952.2.
DR RefSeq; NP_731716.1; NM_169469.2.
DR AlphaFoldDB; Q8INI8; -.
DR SMR; Q8INI8; -.
DR BioGRID; 69382; 51.
DR BioGRID; 71512; 47.
DR BioGRID; 71513; 47.
DR ELM; Q8INI8; -.
DR STRING; 7227.FBpp0082106; -.
DR PaxDb; Q8INI8; -.
DR PRIDE; Q8INI8; -.
DR DNASU; 44921; -.
DR DNASU; 48582; -.
DR DNASU; 48583; -.
DR EnsemblMetazoa; FBtr0082637; FBpp0082106; FBgn0013278.
DR EnsemblMetazoa; FBtr0082638; FBpp0082107; FBgn0013279.
DR GeneID; 44921; -.
DR GeneID; 48582; -.
DR GeneID; 48583; -.
DR KEGG; dme:Dmel_CG31359; -.
DR KEGG; dme:Dmel_CG31449; -.
DR KEGG; dme:Dmel_CG6489; -.
DR CTD; 44921; -.
DR CTD; 48582; -.
DR CTD; 48583; -.
DR FlyBase; FBgn0013277; Hsp70Ba.
DR VEuPathDB; VectorBase:FBgn0013278; -.
DR VEuPathDB; VectorBase:FBgn0013279; -.
DR eggNOG; KOG0101; Eukaryota.
DR HOGENOM; CLU_005965_3_0_1; -.
DR InParanoid; Q8INI8; -.
DR OMA; ECEACIK; -.
DR OrthoDB; 288077at2759; -.
DR PhylomeDB; Q8INI8; -.
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 Reactome; R-DME-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR SignaLink; Q8INI8; -.
DR BioGRID-ORCS; 44921; 0 hits in 3 CRISPR screens.
DR BioGRID-ORCS; 48582; 0 hits in 3 CRISPR screens.
DR BioGRID-ORCS; 48583; 0 hits in 3 CRISPR screens.
DR PRO; PR:Q8INI8; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0013278; Expressed in imaginal disc and 11 other tissues.
DR ExpressionAtlas; Q8INI8; baseline and differential.
DR Genevisible; Q8INI8; 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:0006986; P:response to unfolded protein; NAS:UniProtKB.
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 2: Evidence at transcript level;
KW ATP-binding; Nucleotide-binding; Reference proteome; Stress response.
FT CHAIN 1..641
FT /note="Major heat shock 70 kDa protein Ba"
FT /id="PRO_0000078332"
FT REGION 609..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 2
FT /note="P -> H (in strain: NFS97)"
FT VARIANT 43
FT /note="D -> E (in strain: 3CPA86 and T32)"
FT VARIANT 129
FT /note="E -> D (in strain: 3CPA86 and 3CPA126)"
FT VARIANT 138
FT /note="D -> E (in strain: 3CPA86 and 3CPA126)"
FT VARIANT 195
FT /note="F -> L (in strain: QD18)"
FT VARIANT 241
FT /note="E -> D (in strain: Z(H)1)"
FT VARIANT 350
FT /note="E -> D (in strain: Z(H)1)"
FT VARIANT 430
FT /note="S -> A (in strain: Z(H)1)"
FT VARIANT 516
FT /note="M -> I (in strain: A28)"
FT VARIANT 524
FT /note="A -> V (in strain: A28)"
FT VARIANT 545
FT /note="F -> Y (in strain: AUS and Berkeley)"
FT VARIANT 555
FT /note="P -> T (in strain: AUS)"
FT VARIANT 573
FT /note="E -> D (in strain: A28)"
FT VARIANT 606
FT /note="K -> T (in strain: 3CPA126 and QD18)"
FT CONFLICT 196
FT /note="D -> E (in Ref. 2; AAK67154)"
FT /evidence="ECO:0000305"
FT CONFLICT 333
FT /note="V -> L (in Ref. 2; AAK67154)"
FT /evidence="ECO:0000305"
FT CONFLICT 597
FT /note="T -> A (in Ref. 4; AAN13545)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 641 AA; 70195 MW; F2C9C204F67EBB59 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
EEFKRKYKKD LRSNPRALRR LRTAAERAKR TLSSSTEATI EIDALFEGQD FYTKVSRARF
EELCADLFRN TLQPVEKALN DAKMDKGQIH DIVLVGGSTR IPKVQSLLQE FFHGKNLNLS
INPDEAVAYG AAVQAAILSG DQSGKIQDVL LVDVAPLSLG IETAGGVMTK LIERNCRIPC
KQTKTFSTYS DNQPGVSIQV YEGERAMTKD NNALGTFDLS GIPPAPRGVP QIEVTFDLDA
NGILNVSAKE MSTGKAKNIT IKNDKGRLSQ AEIDRMVNEA EKYADEDEKH RQRITSRNAL
ESYVFNVKQS VEQAPAGKLD EADKNSVLDK CNETIRWLDS NTTAEKEEFD HKMEELTRHC
SPIMTKMHQQ GAGAAGGPGA NCGQQAGGFG GYSGPTVEEV D
