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Protein

60 kDa heat shock protein, mitochondrial

Gene

Hsp60

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.By similarity

GO - Molecular functioni

GO - Biological processi

  • 'de novo' protein folding Source: FlyBase
  • cellular response to heat Source: FlyBase
  • mitochondrion organization Source: FlyBase
  • protein refolding Source: InterPro
  • protein targeting to mitochondrion Source: FlyBase
  • response to heat Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
60 kDa heat shock protein, mitochondrial
Alternative name(s):
60 kDa chaperonin
CPN60
Heat shock protein 60
Short name:
HSP-60
Hsp60
Mitochondrial matrix protein P1
Gene namesi
Name:Hsp60
Synonyms:Mmp-P1
ORF Names:CG12101
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0015245. Hsp60.

Subcellular locationi

GO - Cellular componenti

  • lipid particle Source: FlyBase
  • microtubule associated complex Source: FlyBase
  • mitochondrial inner membrane Source: FlyBase
  • mitochondrial matrix Source: FlyBase
  • mitochondrion Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5757Mitochondrion1 PublicationAdd
BLAST
Chaini58 – 57351660 kDa heat shock protein, mitochondrialPRO_0000005031Add
BLAST

Proteomic databases

PaxDbiO02649.
PRIDEiO02649.

Expressioni

Gene expression databases

BgeeiO02649.
ExpressionAtlasiO02649. differential.
GenevisibleiO02649. DM.

Interactioni

GO - Molecular functioni

Protein-protein interaction databases

BioGridi58460. 49 interactions.
DIPiDIP-20404N.
MINTiMINT-1555277.
STRINGi7227.FBpp0073290.

Structurei

3D structure databases

ProteinModelPortaliO02649.
SMRiO02649. Positions 21-546.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the chaperonin (HSP60) family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0356. Eukaryota.
COG0459. LUCA.
GeneTreeiENSGT00390000005727.
InParanoidiO02649.
KOiK04077.
OMAiSNAMKKV.
OrthoDBiEOG7HTHGJ.
PhylomeDBiO02649.

Family and domain databases

Gene3Di1.10.560.10. 2 hits.
3.50.7.10. 1 hit.
HAMAPiMF_00600. CH60.
InterProiIPR018370. Chaperonin_Cpn60_CS.
IPR001844. Chaprnin_Cpn60.
IPR002423. Cpn60/TCP-1.
IPR027409. GroEL-like_apical_dom.
IPR027413. GROEL-like_equatorial.
[Graphical view]
PfamiPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSiPR00298. CHAPERONIN60.
SUPFAMiSSF52029. SSF52029. 1 hit.
TIGRFAMsiTIGR02348. GroEL. 1 hit.
PROSITEiPS00296. CHAPERONINS_CPN60. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O02649-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFRLPVSLAR SSISRQLAMR GYAKDVRFGP EVRAMMLQGV DVLADAVAVT
60 70 80 90 100
MGPKGRNVII EQSWGSPKIT KDGVTVAKSI ELKDKFQNIG AKLVQDVANN
110 120 130 140 150
TNEEAGDGTT TATVLARAIA KEGFEKISKG ANPVEIRRGV MLAVETVKDN
160 170 180 190 200
LKTMSRPVST PEEIAQVATI SANGDQAIGN LISEAMKKVG RDGVITVKDG
210 220 230 240 250
KTLTDELEVI EGMKFDRGYI SPYFINSSKG AKVEFQDALL LLSEKKISSV
260 270 280 290 300
QSIIPALELA NAQRKPLVII AEDIDGEALS TLVVNRLKIG LQVAAVKAPG
310 320 330 340 350
FGDNRKSTLT DMAIASGGIV FGDDADLVKL EDVKVSDLGQ VGEVVITKDD
360 370 380 390 400
TLLLKGKGKK DDVLRRANQI KDQIEDTTSE YEKEKLQERL ARLASGVALL
410 420 430 440 450
RVGGSSEVEV NEKKDRVHDA LNATRAAVEE GIVPGGGTAL LRCIEKLEGV
460 470 480 490 500
ETTNEDQKLG VEIVRRALRM PCMTIAKNAG VDGAMVVAKV ENQAGDYGYD
510 520 530 540 550
ALKGEYGNLI EKGIIDPTKV VRTAITDASG VASLLTTAEA VVTEIPKEDG
560 570
APAMPGMGGM GGMGGMGGMG GMM
Length:573
Mass (Da):60,809
Last modified:December 1, 2000 - v3
Checksum:i7A3792C1D2F3BE4C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti261 – 2622NA → KS in CAA67720 (Ref. 1) Curated
Sequence conflicti318 – 3214GIVF → ARVG in CAA70287 (PubMed:10071211).Curated
Sequence conflicti371 – 3733KDQ → RTK in CAA67720 (Ref. 1) Curated
Sequence conflicti414 – 4141K → E in CAA67720 (Ref. 1) Curated
Sequence conflicti439 – 4435ALLRC → RLVRL in CAA67720 (Ref. 1) Curated
Sequence conflicti468 – 4681L → S in CAA67720 (Ref. 1) Curated
Sequence conflicti492 – 4921N → T in AAQ23524 (Ref. 4) Curated
Sequence conflicti492 – 4921N → T in CAA70287 (PubMed:10071211).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X99341 mRNA. Translation: CAA67720.1.
AE014298 Genomic DNA. Translation: AAF47998.1.
AE014298 Genomic DNA. Translation: AAF47999.1.
BT010206 mRNA. Translation: AAQ23524.1.
Y09066 mRNA. Translation: CAA70287.1.
RefSeqiNP_511115.2. NM_078560.3.
NP_727489.1. NM_167266.1.
UniGeneiDm.313.

Genome annotation databases

EnsemblMetazoaiFBtr0073434; FBpp0073290; FBgn0015245.
FBtr0073435; FBpp0073291; FBgn0015245.
GeneIDi32045.
KEGGidme:Dmel_CG12101.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X99341 mRNA. Translation: CAA67720.1.
AE014298 Genomic DNA. Translation: AAF47998.1.
AE014298 Genomic DNA. Translation: AAF47999.1.
BT010206 mRNA. Translation: AAQ23524.1.
Y09066 mRNA. Translation: CAA70287.1.
RefSeqiNP_511115.2. NM_078560.3.
NP_727489.1. NM_167266.1.
UniGeneiDm.313.

3D structure databases

ProteinModelPortaliO02649.
SMRiO02649. Positions 21-546.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi58460. 49 interactions.
DIPiDIP-20404N.
MINTiMINT-1555277.
STRINGi7227.FBpp0073290.

Proteomic databases

PaxDbiO02649.
PRIDEiO02649.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0073434; FBpp0073290; FBgn0015245.
FBtr0073435; FBpp0073291; FBgn0015245.
GeneIDi32045.
KEGGidme:Dmel_CG12101.

Organism-specific databases

CTDi32045.
FlyBaseiFBgn0015245. Hsp60.

Phylogenomic databases

eggNOGiKOG0356. Eukaryota.
COG0459. LUCA.
GeneTreeiENSGT00390000005727.
InParanoidiO02649.
KOiK04077.
OMAiSNAMKKV.
OrthoDBiEOG7HTHGJ.
PhylomeDBiO02649.

Miscellaneous databases

ChiTaRSiHsp60. fly.
GenomeRNAii32045.
PROiO02649.

Gene expression databases

BgeeiO02649.
ExpressionAtlasiO02649. differential.
GenevisibleiO02649. DM.

Family and domain databases

Gene3Di1.10.560.10. 2 hits.
3.50.7.10. 1 hit.
HAMAPiMF_00600. CH60.
InterProiIPR018370. Chaperonin_Cpn60_CS.
IPR001844. Chaprnin_Cpn60.
IPR002423. Cpn60/TCP-1.
IPR027409. GroEL-like_apical_dom.
IPR027413. GROEL-like_equatorial.
[Graphical view]
PfamiPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSiPR00298. CHAPERONIN60.
SUPFAMiSSF52029. SSF52029. 1 hit.
TIGRFAMsiTIGR02348. GroEL. 1 hit.
PROSITEiPS00296. CHAPERONINS_CPN60. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The D. melanogaster homologue of the hsp60 is an essential gene and is differentially expressed during fly development."
    Kozlova T., Reynaud E., Perezgasga L., Zurita M.
    Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Oregon-R.
  2. "The genome sequence of Drosophila melanogaster."
    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.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  5. "Identification of nuclear genes encoding mitochondrial proteins: isolation of a collection of D. melanogaster cDNAs homologous to sequences in the Human Gene Index database."
    Caggese C., Ragone G., Perrini B., Moschetti R., de Pinto V., Caizzi R., Barsanti P.
    Mol. Gen. Genet. 261:64-70(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 318-573.
    Tissue: Ovary.
  6. "Identification of Drosophila wing imaginal disc proteins by two-dimensional gel analysis and microsequencing."
    Santaren J.F., van Damme J., Puype M., Vandekerckhove J., Garcia-Bellido A.
    Exp. Cell Res. 206:220-226(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 58-68.
    Strain: Vallecas.
    Tissue: Wing imaginal disk.

Entry informationi

Entry nameiCH60_DROME
AccessioniPrimary (citable) accession number: O02649
Secondary accession number(s): A4V4A0
, P35380, Q6NR71, Q95026, Q9VZ31
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: December 1, 2000
Last modified: June 8, 2016
This is version 127 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.