O75880 · SCO1_HUMAN

  • Protein
    Protein SCO1 homolog, mitochondrial
  • Gene
    SCO1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Copper metallochaperone essential for the maturation of cytochrome c oxidase subunit II (MT-CO2/COX2). Not required for the synthesis of MT-CO2/COX2 but plays a crucial role in stabilizing MT-CO2/COX2 during its subsequent maturation. Involved in transporting copper to the Cu(A) site on MT-CO2/COX2 (PubMed:15229189, PubMed:15659396, PubMed:16735468, PubMed:17189203, PubMed:19336478).
Plays an important role in the regulation of copper homeostasis by controlling the abundance and cell membrane localization of copper transporter CTR1 (By similarity).

Features

Showing features for binding site.

130120406080100120140160180200220240260280300
TypeIDPosition(s)Description
Binding site169Cu cation (UniProtKB | ChEBI)
Binding site173Cu cation (UniProtKB | ChEBI)
Binding site260Cu 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
Cellular Componentmitochondrion
Cellular Componentmyofibril
Molecular Functioncopper chaperone activity
Molecular Functioncopper ion binding
Biological Processintracellular copper ion homeostasis
Biological Processmitochondrial cytochrome c oxidase assembly

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Protein SCO1 homolog, mitochondrial

Gene names

    • Name
      SCO1
    • Synonyms
      SCOD1

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    O75880
  • Secondary accessions
    • B2RDM0

Proteomes

Organism-specific databases

Subcellular Location

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain68-92Mitochondrial matrix
Transmembrane93-111Helical
Topological domain112-301Mitochondrial intermembrane

Keywords

Disease & Variants

Involvement in disease

Mitochondrial complex IV deficiency, nuclear type 4 (MC4DN4)

  • Note
    • The disease is caused by variants affecting the gene represented in this entry
  • Description
    An autosomal recessive mitochondrial disorder characterized by hypotonia, encephalopathy, metabolic acidosis, poor feeding, hepatomegaly, and hypertrophic cardiomyopathy in some patients. Death occurs in infancy. Patient tissues show decreased levels and activity of mitochondrial respiratory complex IV.
  • See also
    MIM:619048
Natural variants in MC4DN4
Variant IDPosition(s)ChangeDescription
VAR_012109174P>Lin MC4DN4; no effect on synthesis of cytochrome c oxidase subunit II; reduced stability of newly synthesized cytochrome c oxidase subunit II; reduced copper-binding; dbSNP:rs104894630

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_01453758in dbSNP:rs1802083
Natural variantVAR_012109174in MC4DN4; no effect on synthesis of cytochrome c oxidase subunit II; reduced stability of newly synthesized cytochrome c oxidase subunit II; reduced copper-binding; dbSNP:rs104894630

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 375 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Keywords

Organism-specific databases

Miscellaneous

Chemistry

Genetic variation databases

PTM/Processing

Features

Showing features for transit peptide, chain, disulfide bond.

TypeIDPosition(s)Description
Transit peptide1-67Mitochondrion
ChainPRO_000003192168-301Protein SCO1 homolog, mitochondrial
Disulfide bond169↔173Redox-active

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Predominantly expressed in tissues characterized by high rates of oxidative phosphorylation (OxPhos), including muscle, heart, and brain.

Gene expression databases

Organism-specific databases

Interaction

Subunit

Homodimer (PubMed:15229189, PubMed:16735468).
Interacts with COA6 (PubMed:26160915).
Found in a complex with TMEM177, COX20, COA6, MT-CO2/COX2, COX18 and SCO2 (PubMed:29154948).
Interacts with TMEM177 in a COX20-dependent manner (PubMed:29154948).
Interacts with COX20 in a MT-CO2/COX2- and COX18-dependent manner (PubMed:24403053, PubMed:28330871, PubMed:29154948).
Interacts with COX16 (PubMed:29381136).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY O75880CIDEB Q9UHD43EBI-6656171, EBI-7062247
BINARY O75880COMT P21964-23EBI-6656171, EBI-10200977
BINARY O75880COX17 Q140613EBI-6656171, EBI-711311

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region63-91Disordered
Region118-131Important for dimerization

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
    301
  • Mass (Da)
    33,814
  • Last updated
    1998-11-01 v1
  • Checksum
    C4A0F35A1741894F
MAMLVLVPGRVMRPLGGQLWRFLPRGLEFWGPAEGTARVLLRQFCARQAEAWRASGRPGYCLGTRPLSTARPPPPWSQKGPGDSTRPSKPGPVSWKSLAITFAIGGALLAGMKHVKKEKAEKLEKERQRHIGKPLLGGPFSLTTHTGERKTDKDYLGQWLLIYFGFTHCPDVCPEELEKMIQVVDEIDSITTLPDLTPLFISIDPERDTKEAIANYVKEFSPKLVGLTGTREEVDQVARAYRVYYSPGPKDEDEDYIVDHTIIMYLIGPDGEFLDYFGQNKRKGEIAASIATHMRPYRKKS

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
J3QL56J3QL56_HUMANSCO1270
J3QR42J3QR42_HUMANSCO191

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF026852
EMBL· GenBank· DDBJ
AAD08641.1
EMBL· GenBank· DDBJ
mRNA
AF295386
EMBL· GenBank· DDBJ
AAG23836.1
EMBL· GenBank· DDBJ
Genomic DNA
AF295381
EMBL· GenBank· DDBJ
AAG23836.1
EMBL· GenBank· DDBJ
Genomic DNA
AF295382
EMBL· GenBank· DDBJ
AAG23836.1
EMBL· GenBank· DDBJ
Genomic DNA
AF295383
EMBL· GenBank· DDBJ
AAG23836.1
EMBL· GenBank· DDBJ
Genomic DNA
AF295384
EMBL· GenBank· DDBJ
AAG23836.1
EMBL· GenBank· DDBJ
Genomic DNA
AF295385
EMBL· GenBank· DDBJ
AAG23836.1
EMBL· GenBank· DDBJ
Genomic DNA
AF183424
EMBL· GenBank· DDBJ
AAG09693.1
EMBL· GenBank· DDBJ
mRNA
AK315595
EMBL· GenBank· DDBJ
BAG37967.1
EMBL· GenBank· DDBJ
mRNA
CH471108
EMBL· GenBank· DDBJ
EAW89997.1
EMBL· GenBank· DDBJ
Genomic DNA
BC015504
EMBL· GenBank· DDBJ
AAH15504.1
EMBL· GenBank· DDBJ
mRNA
AF131816
EMBL· GenBank· DDBJ
AAD20051.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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