CH60A_DROME
ID CH60A_DROME Reviewed; 573 AA.
AC O02649; A4V4A0; P35380; Q6NR71; Q95026; Q9VZ31;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 3.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Heat shock protein 60A {ECO:0000312|FlyBase:FBgn0015245};
DE Flags: Precursor;
GN Name=Hsp60A {ECO:0000312|FlyBase:FBgn0015245};
GN Synonyms=hsp60 {ECO:0000303|Ref.1};
GN ORFNames=CG12101 {ECO:0000312|FlyBase:FBgn0015245};
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].
RC STRAIN=Oregon-R;
RA Kozlova T., Reynaud E., Perezgasga L., Zurita M.;
RT "The D. melanogaster homologue of the hsp60 is an essential gene and is
RT differentially expressed during fly development.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
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=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 318-573.
RC TISSUE=Ovary;
RX PubMed=10071211; DOI=10.1007/s004380050942;
RA Caggese C., Ragone G., Perrini B., Moschetti R., de Pinto V., Caizzi R.,
RA Barsanti P.;
RT "Identification of nuclear genes encoding mitochondrial proteins: isolation
RT of a collection of D. melanogaster cDNAs homologous to sequences in the
RT Human Gene Index database.";
RL Mol. Gen. Genet. 261:64-70(1999).
RN [6]
RP PROTEIN SEQUENCE OF 58-68.
RC STRAIN=Vallecas; TISSUE=Wing imaginal disk;
RX PubMed=8500545; DOI=10.1006/excr.1993.1141;
RA Santaren J.F., van Damme J., Puype M., Vandekerckhove J.,
RA Garcia-Bellido A.;
RT "Identification of Drosophila wing imaginal disc proteins by two-
RT dimensional gel analysis and microsequencing.";
RL Exp. Cell Res. 206:220-226(1993).
CC -!- FUNCTION: Prevents misfolding and promotes the refolding and proper
CC assembly of unfolded polypeptides generated under stress conditions.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family. {ECO:0000305}.
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DR EMBL; X99341; CAA67720.1; -; mRNA.
DR EMBL; AE014298; AAF47998.1; -; Genomic_DNA.
DR EMBL; AE014298; AAF47999.1; -; Genomic_DNA.
DR EMBL; BT010206; AAQ23524.1; -; mRNA.
DR EMBL; Y09066; CAA70287.1; -; mRNA.
DR RefSeq; NP_511115.2; NM_078560.3.
DR RefSeq; NP_727489.1; NM_167266.1.
DR AlphaFoldDB; O02649; -.
DR SMR; O02649; -.
DR BioGRID; 58460; 60.
DR DIP; DIP-20404N; -.
DR STRING; 7227.FBpp0073290; -.
DR MoonProt; O02649; -.
DR PaxDb; O02649; -.
DR PRIDE; O02649; -.
DR DNASU; 32045; -.
DR EnsemblMetazoa; FBtr0073434; FBpp0073290; FBgn0015245.
DR EnsemblMetazoa; FBtr0073435; FBpp0073291; FBgn0015245.
DR GeneID; 32045; -.
DR KEGG; dme:Dmel_CG12101; -.
DR CTD; 32045; -.
DR FlyBase; FBgn0015245; Hsp60A.
DR VEuPathDB; VectorBase:FBgn0015245; -.
DR eggNOG; KOG0356; Eukaryota.
DR GeneTree; ENSGT00390000005727; -.
DR HOGENOM; CLU_016503_3_0_1; -.
DR InParanoid; O02649; -.
DR OMA; TDTDKME; -.
DR OrthoDB; 415781at2759; -.
DR PhylomeDB; O02649; -.
DR BioGRID-ORCS; 32045; 0 hits in 1 CRISPR screen.
DR ChiTaRS; Hsp60; fly.
DR GenomeRNAi; 32045; -.
DR PRO; PR:O02649; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0015245; Expressed in oocyte and 41 other tissues.
DR ExpressionAtlas; O02649; baseline and differential.
DR Genevisible; O02649; DM.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:FlyBase.
DR GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0051087; F:chaperone binding; IBA:GO_Central.
DR GO; GO:0008637; P:apoptotic mitochondrial changes; IBA:GO_Central.
DR GO; GO:0034605; P:cellular response to heat; IEP:FlyBase.
DR GO; GO:0034514; P:mitochondrial unfolded protein response; IBA:GO_Central.
DR GO; GO:0007005; P:mitochondrion organization; IMP:FlyBase.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0045041; P:protein import into mitochondrial intermembrane space; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; IEA:InterPro.
DR CDD; cd03344; GroEL; 1.
DR Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR HAMAP; MF_00600; CH60; 1.
DR InterPro; IPR018370; Chaperonin_Cpn60_CS.
DR InterPro; IPR001844; Cpn60/GroEL.
DR InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR InterPro; IPR027413; GROEL-like_equatorial_sf.
DR InterPro; IPR027410; TCP-1-like_intermed_sf.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR PRINTS; PR00298; CHAPERONIN60.
DR SUPFAM; SSF48592; SSF48592; 1.
DR SUPFAM; SSF52029; SSF52029; 1.
DR SUPFAM; SSF54849; SSF54849; 1.
DR TIGRFAMs; TIGR02348; GroEL; 1.
DR PROSITE; PS00296; CHAPERONINS_CPN60; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chaperone; Direct protein sequencing; Mitochondrion;
KW Nucleotide-binding; Reference proteome; Transit peptide.
FT TRANSIT 1..57
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:8500545"
FT CHAIN 58..573
FT /note="Heat shock protein 60A"
FT /id="PRO_0000005031"
FT CONFLICT 261..262
FT /note="NA -> KS (in Ref. 1; CAA67720)"
FT /evidence="ECO:0000305"
FT CONFLICT 318..321
FT /note="GIVF -> ARVG (in Ref. 5; CAA70287)"
FT /evidence="ECO:0000305"
FT CONFLICT 371..373
FT /note="KDQ -> RTK (in Ref. 1; CAA67720)"
FT /evidence="ECO:0000305"
FT CONFLICT 414
FT /note="K -> E (in Ref. 1; CAA67720)"
FT /evidence="ECO:0000305"
FT CONFLICT 439..443
FT /note="ALLRC -> RLVRL (in Ref. 1; CAA67720)"
FT /evidence="ECO:0000305"
FT CONFLICT 468
FT /note="L -> S (in Ref. 1; CAA67720)"
FT /evidence="ECO:0000305"
FT CONFLICT 492
FT /note="N -> T (in Ref. 4; AAQ23524 and 5; CAA70287)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 573 AA; 60809 MW; 7A3792C1D2F3BE4C CRC64;
MFRLPVSLAR SSISRQLAMR GYAKDVRFGP EVRAMMLQGV DVLADAVAVT MGPKGRNVII
EQSWGSPKIT KDGVTVAKSI ELKDKFQNIG AKLVQDVANN TNEEAGDGTT TATVLARAIA
KEGFEKISKG ANPVEIRRGV MLAVETVKDN LKTMSRPVST PEEIAQVATI SANGDQAIGN
LISEAMKKVG RDGVITVKDG KTLTDELEVI EGMKFDRGYI SPYFINSSKG AKVEFQDALL
LLSEKKISSV QSIIPALELA NAQRKPLVII AEDIDGEALS TLVVNRLKIG LQVAAVKAPG
FGDNRKSTLT DMAIASGGIV FGDDADLVKL EDVKVSDLGQ VGEVVITKDD TLLLKGKGKK
DDVLRRANQI KDQIEDTTSE YEKEKLQERL ARLASGVALL RVGGSSEVEV NEKKDRVHDA
LNATRAAVEE GIVPGGGTAL LRCIEKLEGV ETTNEDQKLG VEIVRRALRM PCMTIAKNAG
VDGAMVVAKV ENQAGDYGYD ALKGEYGNLI EKGIIDPTKV VRTAITDASG VASLLTTAEA
VVTEIPKEDG APAMPGMGGM GGMGGMGGMG GMM
