HSP7E_DROME
ID HSP7E_DROME Reviewed; 686 AA.
AC P29845; Q9V6Z7;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Heat shock 70 kDa protein cognate 5;
GN Name=Hsc70-5; Synonyms=Hsc5; ORFNames=CG8542;
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 [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Ovary;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-86, 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; L01502; AAA28628.1; -; mRNA.
DR EMBL; AE013599; AAF58270.1; -; Genomic_DNA.
DR EMBL; AY118844; AAM50704.1; -; mRNA.
DR PIR; JN0667; JN0667.
DR RefSeq; NP_001286414.1; NM_001299485.1.
DR RefSeq; NP_523741.2; NM_079017.2.
DR AlphaFoldDB; P29845; -.
DR SMR; P29845; -.
DR BioGRID; 62333; 23.
DR IntAct; P29845; 1.
DR STRING; 7227.FBpp0086694; -.
DR iPTMnet; P29845; -.
DR PaxDb; P29845; -.
DR PRIDE; P29845; -.
DR DNASU; 36583; -.
DR EnsemblMetazoa; FBtr0087568; FBpp0086694; FBgn0001220.
DR EnsemblMetazoa; FBtr0339969; FBpp0308990; FBgn0001220.
DR GeneID; 36583; -.
DR KEGG; dme:Dmel_CG8542; -.
DR CTD; 36583; -.
DR FlyBase; FBgn0001220; Hsc70-5.
DR VEuPathDB; VectorBase:FBgn0001220; -.
DR eggNOG; KOG0102; Eukaryota.
DR GeneTree; ENSGT00920000149123; -.
DR HOGENOM; CLU_005965_2_1_1; -.
DR InParanoid; P29845; -.
DR OMA; ISIKRHM; -.
DR OrthoDB; 288077at2759; -.
DR PhylomeDB; P29845; -.
DR Reactome; R-DME-3371453; Regulation of HSF1-mediated heat shock response.
DR SignaLink; P29845; -.
DR BioGRID-ORCS; 36583; 0 hits in 1 CRISPR screen.
DR ChiTaRS; Hsc70-5; fly.
DR GenomeRNAi; 36583; -.
DR PRO; PR:P29845; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0001220; Expressed in wing disc and 40 other tissues.
DR ExpressionAtlas; P29845; baseline and differential.
DR Genevisible; P29845; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:FlyBase.
DR GO; GO:0005739; C:mitochondrion; HDA:FlyBase.
DR GO; GO:0001405; C:PAM complex, Tim23 associated import motor; ISS:FlyBase.
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:0030234; F:enzyme regulator activity; ISS:FlyBase.
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:0008566; F:mitochondrial protein-transporting ATPase activity; ISS:FlyBase.
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:0000422; P:autophagy of mitochondrion; IMP:FlyBase.
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:0070584; P:mitochondrion morphogenesis; IMP:FlyBase.
DR GO; GO:0010918; P:positive regulation of mitochondrial membrane potential; IMP:FlyBase.
DR GO; GO:0030150; P:protein import into mitochondrial matrix; ISS:FlyBase.
DR GO; GO:0042026; P:protein refolding; ISS:FlyBase.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 2.60.34.10; -; 1.
DR HAMAP; MF_00332; DnaK; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR012725; Chaperone_DnaK.
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 TIGRFAMs; TIGR02350; prok_dnaK; 1.
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..686
FT /note="Heat shock 70 kDa protein cognate 5"
FT /id="PRO_0000078342"
FT REGION 657..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..675
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 86
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 288
FT /note="A -> V (in Ref. 1; AAA28628)"
FT /evidence="ECO:0000305"
FT CONFLICT 661
FT /note="S -> T (in Ref. 1; AAA28628)"
FT /evidence="ECO:0000305"
FT CONFLICT 678..686
FT /note="GEAKKEEKN -> ASQEGREELN (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 686 AA; 74066 MW; 61A0C0EDA8E74B9E CRC64;
MLRVPKFLPR LARQAGVVPS HMSGASSMFR NLPGASNGIS SQLRYKSGEV KGAVIGIDLG
TTNSCLAVME GKQAKVIENA EGARTTPSHV AFTKDGERLV GMPAKRQAVT NSANTFYATK
RLIGRRFDDP EVKKDITNLS YKVVKASNGD AWVSSTDGKV YSPSQIGAFI LMKMKETAEA
YLNTPVKNAV VTVPAYFNDS QRQATKDAGQ IAGLNVLRVI NEPTAAALAY GMDKTEDKII
AVYDLGGGTF DISILEIQKG VFEVKSTNGD TLLGGEDFDN HIVNFLVAEF KKDSGIDIRK
DNIAMQRLKE AAEKAKCELS SSQQTDINLP YLTMDAAGPQ HMNLKLTRSK LESLVGDLIK
RTIQPCQKAL SDAEVSKSEI GEVLLVGGMT RMPKVQSTVQ ELFGRQPSRS VNPDEAVAVG
AAVQGGVLAG DVTDVLLLDV TPLSLGIETL GGVFTRLISR NTTIPTKKSQ VFSTASDGQT
QVEIKVHQGE REMANDNKLL GSFTLVGIPP APRGVPQIEV VFDIDANGIV HVSAKDKGTG
KEQQIVIQSS GGLSKDEIEN MIKKAEEYAT ADKQKRELIE IVNQGESIVH DTETKMEEFK
SQLPAEECEK LKKEIADLRT LLANKETADL EEVRKATSSL QQSSLKLFEL AYKKMSAERE
SNAGAGSSDS SSSSDTSGEA KKEEKN
