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60 kDa heat shock protein homolog 2, mitochondrial (60 kDa chaperonin) (CPN60) (Heat shock protein 60) (HSP-60) (Hsp60)

 CH60C_DROME             Reviewed;         576 AA.
Q9VMN5; A4V087; Q8IHD0; Q8MZB0;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
10-MAY-2004, sequence version 2.
23-MAY-2018, entry version 146.
RecName: Full=60 kDa heat shock protein homolog 2, mitochondrial;
AltName: Full=60 kDa chaperonin;
AltName: Full=CPN60;
AltName: Full=Heat shock protein 60;
Short=HSP-60;
AltName: Full=Hsp60;
Flags: Precursor;
Name=Hsp60C; ORFNames=CG7235;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[2]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Testis;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[4]
FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
PHENOTYPE.
PubMed=16385159; DOI=10.1007/BF02715797;
Sarkar S., Lakhotia S.C.;
"The Hsp60C gene in the 25F cytogenetic region in Drosophila
melanogaster is essential for tracheal development and fertility.";
J. Genet. 84:265-281(2005).
-!- FUNCTION: Prevents misfolding and promotes the refolding and
proper assembly of unfolded polypeptides generated under stress
conditions (By similarity). Essential for proper development of
trachea, spermatogonia and spermatocytes. {ECO:0000250,
ECO:0000269|PubMed:16385159}.
-!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
-!- TISSUE SPECIFICITY: First detectable expression is seen in the
posterior part of the dorsal tracheal trunk at stage 14-15, which
marks the beginning of terminal tracheation. In the larval gut,
expression in proventriculus is stronger than in midgut and
hindgut. Malpighian tubules shows low expression and late third
instar larval imaginal disks and brain showed moderate expression.
In larval ovary and testis, expression is strong in the posterior
region. {ECO:0000269|PubMed:16385159}.
-!- DEVELOPMENTAL STAGE: Expression first seen in late embryonic
stages and continues in larval and adult stages.
{ECO:0000269|PubMed:16385159}.
-!- DISRUPTION PHENOTYPE: Flies are male and female sterile; reduction
in numbers of primary and secondary spermatocytes.
{ECO:0000269|PubMed:16385159}.
-!- SIMILARITY: Belongs to the chaperonin (HSP60) family.
{ECO:0000305}.
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; AE014134; AAF52277.2; -; Genomic_DNA.
EMBL; AE014134; AAN10550.2; -; Genomic_DNA.
EMBL; AE014134; AAN10551.2; -; Genomic_DNA.
EMBL; AY113273; AAM29278.1; -; mRNA.
EMBL; BT001308; AAN71063.1; -; mRNA.
RefSeq; NP_608948.2; NM_135104.5.
RefSeq; NP_723104.2; NM_164654.2.
RefSeq; NP_723105.2; NM_164655.3.
UniGene; Dm.6406; -.
ProteinModelPortal; Q9VMN5; -.
SMR; Q9VMN5; -.
BioGrid; 59964; 15.
DIP; DIP-20697N; -.
IntAct; Q9VMN5; 14.
STRING; 7227.FBpp0078742; -.
PaxDb; Q9VMN5; -.
PRIDE; Q9VMN5; -.
EnsemblMetazoa; FBtr0079110; FBpp0078742; FBgn0031728.
EnsemblMetazoa; FBtr0079111; FBpp0078743; FBgn0031728.
EnsemblMetazoa; FBtr0079112; FBpp0078744; FBgn0031728.
GeneID; 33796; -.
KEGG; dme:Dmel_CG7235; -.
UCSC; CG7235-RA; d. melanogaster.
CTD; 33796; -.
FlyBase; FBgn0031728; Hsp60C.
eggNOG; KOG0356; Eukaryota.
eggNOG; COG0459; LUCA.
GeneTree; ENSGT00390000005727; -.
InParanoid; Q9VMN5; -.
KO; K04077; -.
OMA; CVIKVGA; -.
OrthoDB; EOG091G04JM; -.
PhylomeDB; Q9VMN5; -.
ChiTaRS; Hsp60C; fly.
GenomeRNAi; 33796; -.
PRO; PR:Q9VMN5; -.
Proteomes; UP000000803; Chromosome 2L.
Bgee; FBgn0031728; -.
Genevisible; Q9VMN5; DM.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0005759; C:mitochondrial matrix; ISS:FlyBase.
GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0044183; F:protein binding involved in protein folding; IBA:GO_Central.
GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
GO; GO:0006458; P:'de novo' protein folding; ISS:FlyBase.
GO; GO:0008637; P:apoptotic mitochondrial changes; IBA:GO_Central.
GO; GO:0061077; P:chaperone-mediated protein folding; IBA:GO_Central.
GO; GO:0007301; P:female germline ring canal formation; IMP:FlyBase.
GO; GO:0048477; P:oogenesis; IMP:FlyBase.
GO; GO:0007424; P:open tracheal system development; IMP:FlyBase.
GO; GO:0030707; P:ovarian follicle cell development; IMP:FlyBase.
GO; GO:0045041; P:protein import into mitochondrial intermembrane space; IBA:GO_Central.
GO; GO:0042026; P:protein refolding; IEA:InterPro.
GO; GO:0006626; P:protein targeting to mitochondrion; ISS:FlyBase.
GO; GO:0007283; P:spermatogenesis; IMP:FlyBase.
CDD; cd03344; GroEL; 1.
Gene3D; 1.10.560.10; -; 2.
Gene3D; 3.30.260.10; -; 2.
Gene3D; 3.50.7.10; -; 1.
HAMAP; MF_00600; CH60; 1.
InterPro; IPR018370; Chaperonin_Cpn60_CS.
InterPro; IPR001844; Chaprnin_Cpn60.
InterPro; IPR002423; Cpn60/TCP-1.
InterPro; IPR027409; GroEL-like_apical_dom_sf.
InterPro; IPR027413; GROEL-like_equatorial_sf.
InterPro; IPR027410; TCP-1-like_intermed_sf.
Pfam; PF00118; Cpn60_TCP1; 1.
PRINTS; PR00298; CHAPERONIN60.
SUPFAM; SSF48592; SSF48592; 2.
SUPFAM; SSF52029; SSF52029; 1.
SUPFAM; SSF54849; SSF54849; 1.
TIGRFAMs; TIGR02348; GroEL; 1.
PROSITE; PS00296; CHAPERONINS_CPN60; 1.
2: Evidence at transcript level;
ATP-binding; Chaperone; Complete proteome; Developmental protein;
Differentiation; Mitochondrion; Nucleotide-binding; Oogenesis;
Reference proteome; Spermatogenesis; Transit peptide.
TRANSIT 1 61 Mitochondrion. {ECO:0000250}.
CHAIN 62 576 60 kDa heat shock protein homolog 2,
mitochondrial.
/FTId=PRO_0000005033.
CONFLICT 160 160 R -> Q (in Ref. 3; AAM29278).
{ECO:0000305}.
SEQUENCE 576 AA; 61587 MW; 7FB52C049E9A5F79 CRC64;
MMRMFRYTNT LQRTAKISHV LWARNYAKDV RFGPEVRAMM LQGVDVLADA VAVTMGPKGR
NVIIEQSWGS PKITKDGVTV AKSIALKDKF QNIGAKLVQD VANNTNEEAG DGTTTATVLA
RAIAKEGFEK ISRGASPVEI RRGVMLAIET VKDNLRRLSR PVNTPEEICQ VATISANGDK
SVGNLISEAI KKVGRDGVIT VKDGKTLCDE LEVIEGMKFD RGYISPYFIN TSKGAKVEFQ
DALLLFCEKK IKSAPSIVPA LELANAQRKP LVIIAEDLEA EALSTLVVNR LKVGLQVCAV
KAPGFGDNRK ENLMDMAVAT GGIVFGDEAN MVRLEDIKMS DFGRVGEVVV SKDDTMLLKG
KGQKAEVEKR VEGLREAIKE STSSYEKEKM QERLARLSSG VALLRVGGSS DVEVSEKKDR
VIDALNATRA AVEEGIVPGG GTALLRCIQK LNDLKGANED QNMGIEIIRR ALRMPCLTIA
KNAGVDGAMV VAKVEILDGD YGYDALKGEY GNMIERGIID PTKVVRTAIS DAAGVASLLT
TAEAVVTELP LEEAAAAGAA AGLGALGGMG MGGMGM


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