Q5RH02 · SCO2_DANRE

Function

function

Copper metallochaperone essential for the synthesis and maturation of cytochrome c oxidase subunit II (MT-CO2/COX2). Involved in transporting copper to the Cu(A) site on MT-CO2/COX2. Also acts as a thiol-disulfide oxidoreductase to regulate the redox state of the cysteines in SCO1 during maturation of MT-CO2/COX2.

Features

Showing features for binding site.

127920406080100120140160180200220240260
TypeIDPosition(s)Description
Binding site145Cu cation (UniProtKB | ChEBI)
Binding site149Cu cation (UniProtKB | ChEBI)
Binding site236Cu cation (UniProtKB | ChEBI)

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
Molecular Functioncopper chaperone activity
Molecular Functioncopper ion binding
Molecular Functionprotein-disulfide reductase activity
Biological Processeye development
Biological Processintracellular copper ion homeostasis
Biological Processmitochondrial cytochrome c oxidase assembly

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Protein SCO2 homolog, mitochondrial

Gene names

    • Name
      sco2
    • ORF names
      si:dkey-202b22.3

Organism names

  • Taxonomic identifier
  • Strain
    • Tuebingen
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Ostariophysi > Cypriniformes > Danionidae > Danioninae > Danio

Accessions

  • Primary accession
    Q5RH02

Proteomes

Organism-specific databases

Subcellular Location

Mitochondrion inner membrane
; Single-pass membrane protein

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain?-72Mitochondrial matrix
Transmembrane73-90Helical
Topological domain91-279Mitochondrial intermembrane

Keywords

PTM/Processing

Features

Showing features for chain, transit peptide, disulfide bond.

TypeIDPosition(s)Description
ChainPRO_0000354069?-279Protein SCO2 homolog, mitochondrial
Transit peptide1-?Mitochondrion
Disulfide bond145↔149Redox-active

Keywords

Proteomic databases

Expression

Gene expression databases

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain97-271Thioredoxin

Sequence similarities

Belongs to the SCO1/2 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
    279
  • Mass (Da)
    32,111
  • Last updated
    2004-12-21 v1
  • Checksum
    79D2DEA5420A1827
MLRLRVFDRHKRLWSVLQSTIRGNNISNHIPNTTCRSSAPPHLCARQRAFYSQNSPKTPNPGSSAGIKLRTRLVVTLLFGGGIIGTWWYVHQEKEKRIQMQRLEQLRKVALGQGDFHLLDHTGQRRTKRDFLGHWVLLYFGFTHCPDICPDELEKLTSVVHILDKDPSLPSVQPLFITVDPERDDVSAMARYVKDFHPRLVGLTGSAEEVKQAGRDFRVYASNGPKDEDGDYIVDHSIVIYLVNPDGLFIDYYNRMKNDTQIAESIRNHMKTFVRLFPD

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BX649398
EMBL· GenBank· DDBJ
CAI20823.1
EMBL· GenBank· DDBJ
Genomic DNA

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.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp