oxidoreduction-driven active transmembrane transporter activity
Cellular component
integral component of membrane
mitochondrial inner membrane
respiratory chain complex IV
membrane
mitochondrion
mitochondrial respiratory chain complex IV
Biological process
proton transmembrane transport
aerobic electron transport chain
respiratory chain complex IV assembly
respiratory electron transport chain
mitochondrial electron transport, cytochrome c to oxygen
aerobic respiration
transmembrane transport
Sources:Amigo / QuickGO
Orthologs
Species
Human
Mouse
Entrez
4514
17710
Ensembl
ENSG00000198938
ENSMUSG00000064358
UniProt
P00414
P00416
RefSeq (mRNA)
n/a
n/a
RefSeq (protein)
n/a
NP_904334
Location (UCSC)
Chr M: 0.01 – 0.01 Mb
Chr M: 0.01 – 0.01 Mb
PubMed search
[3]
[4]
Wikidata
View/Edit Human
View/Edit Mouse
Cytochrome c oxidase subunit III
Structure of the 13-subunit oxidized cytochrome c oxidase.[5]
Identifiers
Symbol
COX3
Pfam
PF00510
InterPro
IPR000298
PROSITE
PDOC50253
SCOP2
1occ / SCOPe / SUPFAM
TCDB
3.D.4
OPM superfamily
4
OPM protein
1v55
CDD
cd01665
Available protein structures:
Pfam
structures / ECOD
PDB
RCSB PDB; PDBe; PDBj
PDBsum
structure summary
Cytochrome c oxidase subunit III (COX3) is an enzyme that in humans is encoded by the MT-CO3 gene.[6] It is one of main transmembrane subunits of cytochrome c oxidase. It is also one of the three mitochondrial DNA (mtDNA) encoded subunits (MT-CO1, MT-CO2, MT-CO3) of respiratory complex IV. Variants of it have been associated with isolated myopathy, severe encephalomyopathy, Leber hereditary optic neuropathy, mitochondrial complex IV deficiency, and recurrent myoglobinuria .[7][8][9]
^ abcGRCh38: Ensembl release 89: ENSG00000198938 – Ensembl, May 2017
^ abcGRCm38: Ensembl release 89: ENSMUSG00000064358 – Ensembl, May 2017
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Miki K, Sogabe S, Uno A, Ezoe T, Kasai N, Saeda M, Matsuura Y, Miki M (May 1994). "Application of an automatic molecular-replacement procedure to crystal structure analysis of cytochrome c2 from Rhodopseudomonas viridis". Acta Crystallographica Section D. 50 (Pt 3): 271–5. Bibcode:1994AcCrD..50..271M. doi:10.1107/S0907444993013952. PMID 15299438.
^"Entrez Gene: COX3 cytochrome c oxidase subunit III". This article incorporates text from this source, which is in the public domain.
^Cite error: The named reference :1 was invoked but never defined (see the help page).
^"MT-CO3 - Cytochrome c oxidase subunit 3 - Homo sapiens (Human) - MT-CO3 gene & protein". www.uniprot.org. Retrieved 2018-08-21. This article incorporates text available under the CC BY 4.0 license.
^"UniProt: the universal protein knowledgebase". Nucleic Acids Research. 45 (D1): D158–D169. January 2017. doi:10.1093/nar/gkw1099. PMC 5210571. PMID 27899622.
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Yaono R, Yoshikawa S (1996). "The whole structure of the 13-subunit oxidized cytochromecoxidase at 2.8 A". Science. 272 (5265): 1136–44. Bibcode:1996Sci...
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1985). "Isolation of ubiquinol oxidase from Paracoccus denitrificans and resolution into cytochrome bc1 and cytochromec-aa3 complexes". The Journal of...
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daunorubicin into DXR. By 1999, they produced recombinant Dox A, a Cytochrome P450 oxidase, and found that it catalyzes multiple steps in DXR biosynthesis...
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