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Q9VMN5 · CH60C_DROME

Function

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

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentmitochondrial inner membrane
Cellular Componentmitochondrial matrix
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular FunctionATP-dependent protein folding chaperone
Molecular Functionprotein-folding chaperone binding
Biological Processapoptotic mitochondrial changes
Biological Processfemale germline ring canal formation
Biological Processfollicle cell of egg chamber development
Biological Processmitochondrial unfolded protein response
Biological Processoogenesis
Biological Processopen tracheal system development
Biological Processprotein folding
Biological Processprotein import into mitochondrial intermembrane space
Biological Processprotein refolding
Biological Processspermatogenesis

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    60 kDa heat shock protein homolog 2, mitochondrial
  • Alternative names
    • 60 kDa chaperonin
    • CPN60
    • Heat shock protein 60 (HSP-60)
    • Hsp60

Gene names

    • Name
      Hsp60C
    • ORF names
      CG7235

Organism names

  • Taxonomic identifier
  • Strain
    • Berkeley
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora

Accessions

  • Primary accession
    Q9VMN5
  • Secondary accessions
    • A4V087
    • Q8IHD0
    • Q8MZB0

Proteomes

Organism-specific databases

Subcellular Location

Phenotypes & Variants

Disruption phenotype

Flies are male and female sterile; reduction in numbers of primary and secondary spermatocytes.

PTM/Processing

Features

Showing features for transit peptide, chain.

Type
IDPosition(s)Description
Transit peptide1-61Mitochondrion
ChainPRO_000000503362-57660 kDa heat shock protein homolog 2, mitochondrial

Proteomic databases

Expression

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.

Developmental stage

Expression first seen in late embryonic stages and continues in larval and adult stages.

Gene expression databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the chaperonin (HSP60) family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    576
  • Mass (Da)
    61,587
  • Last updated
    2004-05-10 v2
  • MD5 Checksum
    7C76E603419A7914D314085B5D337EE0
MMRMFRYTNTLQRTAKISHVLWARNYAKDVRFGPEVRAMMLQGVDVLADAVAVTMGPKGRNVIIEQSWGSPKITKDGVTVAKSIALKDKFQNIGAKLVQDVANNTNEEAGDGTTTATVLARAIAKEGFEKISRGASPVEIRRGVMLAIETVKDNLRRLSRPVNTPEEICQVATISANGDKSVGNLISEAIKKVGRDGVITVKDGKTLCDELEVIEGMKFDRGYISPYFINTSKGAKVEFQDALLLFCEKKIKSAPSIVPALELANAQRKPLVIIAEDLEAEALSTLVVNRLKVGLQVCAVKAPGFGDNRKENLMDMAVATGGIVFGDEANMVRLEDIKMSDFGRVGEVVVSKDDTMLLKGKGQKAEVEKRVEGLREAIKESTSSYEKEKMQERLARLSSGVALLRVGGSSDVEVSEKKDRVIDALNATRAAVEEGIVPGGGTALLRCIQKLNDLKGANEDQNMGIEIIRRALRMPCLTIAKNAGVDGAMVVAKVEILDGDYGYDALKGEYGNMIERGIIDPTKVVRTAISDAAGVASLLTTAEAVVTELPLEEAAAAGAAAGLGALGGMGMGGMGM

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict160in Ref. 3; AAM29278

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE014134
EMBL· GenBank· DDBJ
AAF52277.2
EMBL· GenBank· DDBJ
Genomic DNA
AE014134
EMBL· GenBank· DDBJ
AAN10550.2
EMBL· GenBank· DDBJ
Genomic DNA
AE014134
EMBL· GenBank· DDBJ
AAN10551.2
EMBL· GenBank· DDBJ
Genomic DNA
AY113273
EMBL· GenBank· DDBJ
AAM29278.1
EMBL· GenBank· DDBJ
mRNA
BT001308
EMBL· GenBank· DDBJ
AAN71063.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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