| Identification |
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| Name | Cytochrome c oxidase subunit 2 |
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| Synonyms | - Cytochrome c oxidase polypeptide II
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| Gene Name | COX2 |
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| Enzyme Class | |
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| Biological Properties |
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| General Function | Involved in copper ion binding |
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| Specific Function | Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1- 3 form the functional core of the enzyme complex. Subunit 2 transfers the electrons from cytochrome c via its binuclear copper A center to the bimetallic center of the catalytic subunit 1 |
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| Cellular Location | Mitochondrion inner membrane; Multi-pass membrane protein |
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| SMPDB Pathways | |
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| KEGG Pathways | |
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| SMPDB Reactions | Not Available |
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| KEGG Reactions | Not Available |
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| Metabolites | | YMDB ID | Name | View |
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| YMDB00862 | hydron | Show |
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| GO Classification | | Component |
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| cell part | | membrane | | membrane part | | intrinsic to membrane | | integral to membrane | | Function |
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| ion binding | | cation binding | | metal ion binding | | transition metal ion binding | | iron ion binding | | oxidoreductase activity | | heme binding | | electron carrier activity | | catalytic activity | | heme-copper terminal oxidase activity | | cytochrome-c oxidase activity | | copper ion binding | | binding | | Process |
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| generation of precursor metabolites and energy | | metabolic process | | electron transport chain | | respiratory electron transport chain | | cellular metabolic process |
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| Gene Properties |
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| Chromosome Location | chromosome 17 |
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| Locus | Q0250 |
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| Gene Sequence | >756 bp
ATGTTAGATTTATTAAGATTACAATTAACAACATTCATTATGAATGATGTACCAACACCT
TATGCATGTTATTTTCAGGATTCAGCAACACCAAATCAAGAAGGTATTTTAGAATTACAT
GATAATATTATGTTTTATTTATTAGTTATTTTAGGTTTAGTATCTTGAATGTTATATACA
ATTGTTATAACATATTCAAAAAATCCTATTGCATATAAATATATTAAACATGGACAAACT
ATTGAAGTTATTTGAACAATTTTTCCAGCTGTAATTTTATTAATTATTGCTTTTCCTTCA
TTTATTTTATTATATTTATGTGATGAAGTTATTTCACCAGCTATAACTATTAAAGCTATT
GGATATCAATGATATTGAAAATATGAATATTCAGATTTTATTAATGATAGTGGTGAAACT
GTTGAATTTGAATCATATGTTATTCCTGATGAATTATTAGAAGAAGGTCAATTAAGATTA
TTAGATACTGATACTTCTATAGTTGTACCTGTAGATACACATATTAGATTCGTTGTAACA
GCTGCTGATGTTATTCATGATTTTGCTATTCCAAGTTTAGGTATTAAAGTTGATGCTACT
CCTGGTAGATTAAATCAAGTTTCTGCTTTAATTCAAAGAGAAGGTGTCTTCTATGGAGCA
TGTTCTGAGTTGTGTGGGACAGGTCATGCAAATATGCCAATTAAGATCGAAGCAGTATCA
TTACCTAAATTTTTGGAATGATTAAATGAACAATAA |
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| Protein Properties |
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| Pfam Domain Function | |
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| Protein Residues | 251 |
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| Protein Molecular Weight | 28566.90039 |
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| Protein Theoretical pI | 4.2 |
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| Signalling Regions | |
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| Transmembrane Regions | |
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| Protein Sequence | >Cytochrome c oxidase subunit 2
MLDLLRLQLTTFIMNDVPTPYACYFQDSATPNQEGILELHDNIMFYLLVILGLVSWMLYT
IVMTYSKNPIAYKYIKHGQTIEVIWTIFPAVILLIIAFPSFILLYLCDEVISPAMTIKAI
GYQWYWKYEYSDFINDSGETVEFESYVIPDELLEEGQLRLLDTDTSMVVPVDTHIRFVVT
AADVIHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGACSELCGTGHANMPIKIEAVS
LPKFLEWLNEQ |
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| References |
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| External Links | |
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| General Reference | - Coruzzi, G., Tzagoloff, A. (1979). "Assembly of the mitochondrial membrane system. DNA sequence of subunit 2 of yeast cytochrome oxidase." J Biol Chem 254:9324-9330.225327
- Fox, T. D. (1979). "Five TGA "stop" codons occur within the translated sequence of the yeast mitochondrial gene for cytochrome c oxidase subunit II." Proc Natl Acad Sci U S A 76:6534-6538.230513
- Foury, F., Roganti, T., Lecrenier, N., Purnelle, B. (1998). "The complete sequence of the mitochondrial genome of Saccharomyces cerevisiae." FEBS Lett 440:325-331.9872396
- Cameron, V. L., Fox, T. D., Poyton, R. O. (1989). "Isolation and characterization of a yeast strain carrying a mutation in the mitochondrial promoter for COX2." J Biol Chem 264:13391-13394.2547760
- Macino, G., Coruzzi, G., Nobrega, F. G., Li, M., Tzagoloff, A. (1979). "Use of the UGA terminator as a tryptophan codon in yeast mitochondria." Proc Natl Acad Sci U S A 76:3784-3785.226981
- Geier, B. M., Schagger, H., Ortwein, C., Link, T. A., Hagen, W. R., Brandt, U., Von Jagow, G. (1995). "Kinetic properties and ligand binding of the eleven-subunit cytochrome-c oxidase from Saccharomyces cerevisiae isolated with a novel large-scale purification method." Eur J Biochem 227:296-302.7851399
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