Q06474 · COX2_SYNY3

Function

function

Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).

Catalytic activity

Cofactor

Cu cation (UniProtKB | Rhea| CHEBI:23378 )
Note: Binds a copper A center.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site214Cu cation A (UniProtKB | ChEBI)
Binding site249Cu cation A (UniProtKB | ChEBI)
Binding site253Cu cation A (UniProtKB | ChEBI)
Binding site257Cu cation A (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 Componentplasma membrane
Cellular Componentrespirasome
Molecular Functioncopper ion binding
Molecular Functioncytochrome-c oxidase activity
Biological ProcessATP synthesis coupled electron transport

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Cytochrome c oxidase subunit 2
  • EC number
  • Alternative names
    • Cytochrome aa3 subunit 2
    • Cytochrome c oxidase polypeptide II
    • Oxidase aa(3) subunit 2

Gene names

    • Name
      ctaC
    • Synonyms
      coxB
    • Ordered locus names
      slr1136

Organism names

Accessions

  • Primary accession
    Q06474
  • Secondary accessions
    • P77963

Proteomes

Subcellular Location

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane48-68Helical
Transmembrane87-107Helical

Keywords

PTM/Processing

Features

Showing features for signal, chain.

TypeIDPosition(s)Description
Signal1-20
ChainPRO_000000606521-332Cytochrome c oxidase subunit 2

Proteomic databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    332
  • Mass (Da)
    35,917
  • Last updated
    1997-11-01 v2
  • Checksum
    314F15C8F8D4AD26
MKIPGSVITLLIGVVITVVSLWYGQNHGLMPVAASADAEKVDGIFNYMMTIATGLFLLVEGVLVYCLIRFRRRKDDQTDGPPIEGNVPLEILWTAIPTVIVFTLAVYSFEVYNNLGGLDPTISRDNAGQQMAHNHMGHMGSMGNMVAMAGDGDVALGIGLDSEEQGVNPLMVDVKGIQYAWIFTYPETGIISGELHAPIDRPVQLNMEAGDVIHAFWIPQLRLKQDVIPGRGSTLVFNASTPGQYPVICAELCGAYHGGMKSVFYAHTPEEYDDWVAANAPAPTESMAMTLPKATTAMTPNEYLAPYAKEMGVQTEALAQLKDQTSPVGDLL

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict240-244in Ref. 1 and 2
Sequence conflict320-332in Ref. 1 and 2

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X53746
EMBL· GenBank· DDBJ
CAA37776.1
EMBL· GenBank· DDBJ
Genomic DNA
BA000022
EMBL· GenBank· DDBJ
BAA17288.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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