HSP7A_DROME
ID HSP7A_DROME Reviewed; 641 AA.
AC P29843; Q9VUA7;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Heat shock 70 kDa protein cognate 1;
DE AltName: Full=Heat shock 70 kDa protein 70C;
GN Name=Hsc70-1; Synonyms=Hsc1; ORFNames=CG8937;
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 [MRNA].
RX PubMed=8514184; DOI=10.1016/0378-1119(93)90558-k;
RA Rubin D.M., Mehta A., Zhu J., Shoham S., Chen X.J., Wells Q., Palter K.B.;
RT "Genomic structure and sequence analysis of Drosophila melanogaster HSC70
RT genes.";
RL Gene 128:155-163(1993).
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 [GENOMIC DNA] OF 1-68.
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).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- DEVELOPMENTAL STAGE: Heat shock cognate proteins are expressed
CC constitutively during normal development.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; L01501; AAA28625.1; -; mRNA.
DR EMBL; AE014296; AAF49782.1; -; Genomic_DNA.
DR EMBL; J01085; AAA28629.1; -; Genomic_DNA.
DR PIR; B03309; B03309.
DR PIR; JN0668; JN0668.
DR RefSeq; NP_524063.1; NM_079339.3.
DR AlphaFoldDB; P29843; -.
DR SMR; P29843; -.
DR BioGRID; 64882; 14.
DR IntAct; P29843; 1.
DR MINT; P29843; -.
DR STRING; 7227.FBpp0075504; -.
DR iPTMnet; P29843; -.
DR PaxDb; P29843; -.
DR PRIDE; P29843; -.
DR DNASU; 39542; -.
DR EnsemblMetazoa; FBtr0075762; FBpp0075504; FBgn0001216.
DR GeneID; 39542; -.
DR KEGG; dme:Dmel_CG8937; -.
DR CTD; 39542; -.
DR FlyBase; FBgn0001216; Hsc70-1.
DR VEuPathDB; VectorBase:FBgn0001216; -.
DR eggNOG; KOG0101; Eukaryota.
DR HOGENOM; CLU_005965_3_0_1; -.
DR InParanoid; P29843; -.
DR OMA; VNEAESY; -.
DR PhylomeDB; P29843; -.
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 SignaLink; P29843; -.
DR BioGRID-ORCS; 39542; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 39542; -.
DR PRO; PR:P29843; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0001216; Expressed in testis and 8 other tissues.
DR ExpressionAtlas; P29843; baseline and differential.
DR Genevisible; P29843; DM.
DR GO; GO:0005737; C:cytoplasm; ISS:FlyBase.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:FlyBase.
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; ISS:FlyBase.
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:0006457; P:protein folding; ISS:FlyBase.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
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; Phosphoprotein; Reference proteome;
KW Stress response.
FT CHAIN 1..641
FT /note="Heat shock 70 kDa protein cognate 1"
FT /id="PRO_0000078337"
FT REGION 612..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
SQ SEQUENCE 641 AA; 70686 MW; DB86DB45E0C4BCA6 CRC64;
MPKLPAVGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTESERL IGDAAKNQVA
MNPNNTIFDA KRLIGRRFDD ATVQSDMKHW PFEVFAENGK PRIRVEYKGE RKSFYPEEVS
SMVLTKMRET AEAYLGGTVT DAVVTVPAYF NDSQRQATKD AGAIAGLNVL RIINEPTAAA
IAYGLDKQGT SERNVLIFDL GGGTFDVSVL TIEDGIFEVK ATAGDTHLGG EDFDNRLVNH
FVQEFQRKHK KDLGQNKRAL RRLRTACERA KRTLSSSTQA SIEIDSLFEG VDFYTSVTRA
RFEELNGDLF RGTMEPVAKA LRDAKMDKGQ IHDIVLVGGS TRIPKVQRLL QDFFNGKELN
KSINPDEAVA YGAAVQAAIL HGDKSEAVQD LLLLDVTPLS LGIETAGGVM TTLIKRNTTI
PTKQTQIFTT YADNQPGVLI QVFEGERAMT RDNNSLGKFE LSAIPPAPRG VPQVEVTFDI
DANGILNVTA LEKSTGKENR ITITNDKGRL SKEDIERMVN DAEAYRQADE QQRDRINAKN
QLESYCFQLR STLDDEHLSS RFSPADRETI QQRSSETIAW LDANQLAERQ EFEHKQQELE
RICSPIITRL YQGAGMAPPP TAGGSNPGAT GGSGPTIEEV D
