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Identification
NameCytochrome c oxidase subunit 2
Synonyms
  • Cytochrome c oxidase polypeptide II
Gene NameCOX2
Enzyme Class
Biological Properties
General FunctionInvolved in copper ion binding
Specific FunctionCytochrome 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
Cellular LocationMitochondrion inner membrane; Multi-pass membrane protein
SMPDB Pathways
Oxidative phosphorylationPW002461 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Oxidative phosphorylationec00190 Map00190
SMPDB ReactionsNot Available
KEGG ReactionsNot Available
Metabolites
YMDB IDNameView
YMDB00862hydronShow
GO Classification
Component
cell part
membrane
membrane part
intrinsic to membrane
integral to membrane
Function
binding
heme-copper terminal oxidase activity
ion binding
cytochrome-c oxidase activity
cation binding
catalytic activity
metal ion binding
copper ion binding
transition metal ion binding
iron ion binding
oxidoreductase activity
heme binding
electron carrier activity
Process
electron transport chain
respiratory electron transport chain
metabolic process
generation of precursor metabolites and energy
cellular metabolic process
Gene Properties
Chromosome Locationchromosome 17
LocusQ0250
Gene Sequence>756 bp ATGTTAGATTTATTAAGATTACAATTAACAACATTCATTATGAATGATGTACCAACACCT TATGCATGTTATTTTCAGGATTCAGCAACACCAAATCAAGAAGGTATTTTAGAATTACAT GATAATATTATGTTTTATTTATTAGTTATTTTAGGTTTAGTATCTTGAATGTTATATACA ATTGTTATAACATATTCAAAAAATCCTATTGCATATAAATATATTAAACATGGACAAACT ATTGAAGTTATTTGAACAATTTTTCCAGCTGTAATTTTATTAATTATTGCTTTTCCTTCA TTTATTTTATTATATTTATGTGATGAAGTTATTTCACCAGCTATAACTATTAAAGCTATT GGATATCAATGATATTGAAAATATGAATATTCAGATTTTATTAATGATAGTGGTGAAACT GTTGAATTTGAATCATATGTTATTCCTGATGAATTATTAGAAGAAGGTCAATTAAGATTA TTAGATACTGATACTTCTATAGTTGTACCTGTAGATACACATATTAGATTCGTTGTAACA GCTGCTGATGTTATTCATGATTTTGCTATTCCAAGTTTAGGTATTAAAGTTGATGCTACT CCTGGTAGATTAAATCAAGTTTCTGCTTTAATTCAAAGAGAAGGTGTCTTCTATGGAGCA TGTTCTGAGTTGTGTGGGACAGGTCATGCAAATATGCCAATTAAGATCGAAGCAGTATCA TTACCTAAATTTTTGGAATGATTAAATGAACAATAA
Protein Properties
Pfam Domain Function
Protein Residues251
Protein Molecular Weight28566.90039
Protein Theoretical pI4.2
Signalling Regions
  • 1-15
Transmembrane Regions
  • 43-64
  • 83-107
Protein Sequence>Cytochrome c oxidase subunit 2 MLDLLRLQLTTFIMNDVPTPYACYFQDSATPNQEGILELHDNIMFYLLVILGLVSWMLYT IVMTYSKNPIAYKYIKHGQTIEVIWTIFPAVILLIIAFPSFILLYLCDEVISPAMTIKAI GYQWYWKYEYSDFINDSGETVEFESYVIPDELLEEGQLRLLDTDTSMVVPVDTHIRFVVT AADVIHDFAIPSLGIKVDATPGRLNQVSALIQREGVFYGACSELCGTGHANMPIKIEAVS LPKFLEWLNEQ
References
External Links
ResourceLink
Saccharomyces Genome Database COX2
Uniprot IDP00410
Uniprot NameCOX2_YEAST
GenBank Gene IDAJ011856
Genebank Protein ID4160387
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