HSP71_DROME
ID HSP71_DROME Reviewed; 642 AA.
AC P02825; Q95NG7;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 3.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Major heat shock 70 kDa protein Ab;
DE Short=Heat shock protein 70Ab;
DE AltName: Full=HSP70-87A7;
GN Name=Hsp70Ab; Synonyms=Hsp70A; ORFNames=CG18743;
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].
RX PubMed=6795353; DOI=10.1016/0022-2836(81)90536-2;
RA Karch F., Toeroek I., Tissieres A.;
RT "Extensive regions of homology in front of the two hsp70 heat shock variant
RT genes in Drosophila melanogaster.";
RL J. Mol. Biol. 148:219-230(1981).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLY-189; ASN-194; GLY-262;
RP ARG-489; ASP-567; GLY-573 AND ARG-636.
RC STRAIN=122, 3CPA126, 3CPA2, 3CPA35, 3CPA43, 3CPA47, 3CPA61, 3CPA81, 3CPA86,
RC 56H8, 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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-135 AND 445-642.
RX PubMed=6255408; DOI=10.1093/nar/8.14.3105;
RA Toeroek I., Karch F.;
RT "Nucleotide sequences of heat shock activated genes in Drosophila
RT melanogaster. I. Sequences in the regions of the 5' and 3' ends of the hsp
RT 70 gene in the hybrid plasmid 56H8.";
RL Nucleic Acids Res. 8:3105-3123(1980).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-100.
RX PubMed=6804941; DOI=10.1073/pnas.79.2.525;
RA Ingolia T.D., Craig E.A.;
RT "Drosophila gene related to the major heat shock-induced gene is
RT transcribed at normal temperatures and not induced by heat shock.";
RL Proc. Natl. Acad. Sci. U.S.A. 79:525-529(1982).
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=CAA23495.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA23495.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA23496.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA23496.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; J01103; AAA28640.1; -; Genomic_DNA.
DR EMBL; AF295939; AAG26893.1; -; Genomic_DNA.
DR EMBL; AF295940; AAG26894.1; -; Genomic_DNA.
DR EMBL; AF295941; AAG26895.1; -; Genomic_DNA.
DR EMBL; AF295942; AAG26896.1; -; Genomic_DNA.
DR EMBL; AF295943; AAG26897.1; -; Genomic_DNA.
DR EMBL; AF295944; AAG26898.1; -; Genomic_DNA.
DR EMBL; AF295945; AAG26899.1; -; Genomic_DNA.
DR EMBL; AF350460; AAK30217.1; -; Genomic_DNA.
DR EMBL; AF350461; AAK30218.1; -; Genomic_DNA.
DR EMBL; AF350462; AAK30219.1; -; Genomic_DNA.
DR EMBL; AF350463; AAK30220.1; -; Genomic_DNA.
DR EMBL; AF350464; AAK30221.1; -; Genomic_DNA.
DR EMBL; AF350465; AAK30222.1; -; Genomic_DNA.
DR EMBL; AF350466; AAK30223.1; -; Genomic_DNA.
DR EMBL; AF350467; AAK30224.1; -; Genomic_DNA.
DR EMBL; AE014297; AAG22148.2; -; Genomic_DNA.
DR EMBL; V00213; CAA23495.1; ALT_SEQ; Genomic_DNA.
DR EMBL; V00214; CAA23496.1; ALT_SEQ; Genomic_DNA.
DR PIR; A03308; A03308.
DR RefSeq; NP_524798.2; NM_080059.3.
DR RefSeq; NP_731651.1; NM_169441.2.
DR AlphaFoldDB; P02825; -.
DR SMR; P02825; -.
DR BioGRID; 69381; 50.
DR BioGRID; 71511; 62.
DR IntAct; P02825; 5.
DR PRIDE; P02825; -.
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; FBgn0013276; Hsp70Ab.
DR VEuPathDB; VectorBase:FBgn0013275; -.
DR VEuPathDB; VectorBase:FBgn0013276; -.
DR HOGENOM; CLU_005965_3_0_1; -.
DR InParanoid; P02825; -.
DR OrthoDB; 288077at2759; -.
DR PhylomeDB; P02825; -.
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 SignaLink; P02825; -.
DR PRO; PR:P02825; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0013275; Expressed in seminal fluid secreting gland and 9 other tissues.
DR ExpressionAtlas; P02825; baseline and differential.
DR Genevisible; P02825; 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..642
FT /note="Major heat shock 70 kDa protein Ab"
FT /id="PRO_0000078330"
FT REGION 609..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 189
FT /note="E -> G (in strain: B28)"
FT /evidence="ECO:0000269|PubMed:11965431"
FT VARIANT 194
FT /note="I -> N (in strain: Z(H)1)"
FT /evidence="ECO:0000269|PubMed:11965431"
FT VARIANT 262
FT /note="R -> G (in strain: 122)"
FT /evidence="ECO:0000269|PubMed:11965431"
FT VARIANT 489
FT /note="K -> R (in strain: FrV3-1)"
FT /evidence="ECO:0000269|PubMed:11965431"
FT VARIANT 567
FT /note="V -> D (in strain: 56H8)"
FT /evidence="ECO:0000269|PubMed:11965431"
FT VARIANT 573
FT /note="D -> G (in strain: 122)"
FT /evidence="ECO:0000269|PubMed:11965431"
FT VARIANT 636
FT /note="P -> R (in strain: B28)"
FT /evidence="ECO:0000269|PubMed:11965431"
FT CONFLICT 50
FT /note="D -> E (in Ref. 1; AAA28640)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="A -> AA (in Ref. 1; AAA28640 and 5; CAA23495)"
FT /evidence="ECO:0000305"
FT CONFLICT 530
FT /note="H -> R (in Ref. 1; AAA28640 and 5; CAA23496)"
FT /evidence="ECO:0000305"
FT CONFLICT 534
FT /note="I -> V (in Ref. 1; AAA28640 and 5; CAA23496)"
FT /evidence="ECO:0000305"
FT CONFLICT 543..545
FT /note="YVF -> HVL (in Ref. 1; AAA28640 and 5; CAA23496)"
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
