Cytochrome c oxidase subunit 2: Difference between revisions

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{{Short description|Enzyme of the respiratory chain encoded by the mitochondrial genome}}
{{Redirect|COX2|the cyclooxygenase isoenzyme|COX-2}}
{{Redirect|COX2|the cyclooxygenase isoenzyme|Cyclooxygenase-2}}
{{Infobox_gene}}
{{Infobox_gene}}
[[File:Map of the human mitochondrial genome.svg|thumb|320px|Location of the ''MT-CO2'' gene in the human mitochondrial genome. ''MT-CO2'' is one of the three cytochrome c oxidase subunit mitochondrial genes (orange boxes).]]
[[File:Map of the human mitochondrial genome.svg|thumb|320px|Location of the ''MT-CO2'' gene in the human mitochondrial genome. ''MT-CO2'' is one of the three cytochrome c oxidase subunit mitochondrial genes (orange boxes).]]
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| CDD = cd13912
| CDD = cd13912
}}
}}
'''Cytochrome c oxidase subunit 2''', also known as '''cytochrome c oxidase polypeptide II''', is a [[protein]] that in humans is encoded by the MT-CO2 [[gene]].<ref name = "entrez">


{{cite web | title = Entrez Gene: COX2 cytochrome c oxidase subunit II| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4513| access-date = }}{{PD-notice}}
'''Cytochrome c oxidase II''' is a [[protein]] in [[eukaryote]]s that is encoded by the MT-CO2 [[gene]].<ref name = "entrez">{{cite web | title = Entrez Gene: COX2 cytochrome c oxidase subunit II| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4513}}{{PD-notice}}</ref> Cytochrome c oxidase subunit II, abbreviated '''COXII''', '''COX2''', '''COII''', or '''MT-CO2''', is the second subunit of [[cytochrome c oxidase]]. It is also one of the three [[mitochondrial DNA]] (mtDNA) encoded subunits ([[MT-CO1]], MT-CO2, [[MT-CO3]]) of [[Electron transport chain#Complex IV|respiratory complex IV]].

</ref> Cytochrome c oxidase subunit II, abbreviated '''COXII''', '''COX2''', '''COII''', or '''MT-CO2''', is the second subunit of [[cytochrome c oxidase]].


== Structure ==
== Structure ==
The ''MT-CO2'' gene is located on the [[Locus (genetics)|p arm]] of [[mitochondrial DNA]] at position 12 and it spans 683 base pairs.<ref name = entrez /> The ''MT-CO2'' gene produces a 25.6 kDa protein composed of 227 [[amino acids]].<ref name=COPaKB>
In humans, the ''MT-CO2'' gene is located on the [[Locus (genetics)|p arm]] of [[mitochondrial DNA]] at position 12 and it spans 683 base pairs.<ref name = entrez /> The ''MT-CO2'' gene produces a 25.6 kDa protein composed of 227 [[amino acids]].<ref name=COPaKB>


{{cite journal | vauthors = Zong NC, Li H, Li H, Lam MP, Jimenez RC, Kim CS, Deng N, Kim AK, Choi JH, Zelaya I, Liem D, Meyer D, Odeberg J, Fang C, Lu HJ, Xu T, Weiss J, Duan H, Uhlen M, Yates JR, Apweiler R, Ge J, Hermjakob H, Ping P | title = Integration of cardiac proteome biology and medicine by a specialized knowledgebase | journal = Circulation Research | volume = 113 | issue = 9 | pages = 1043–53 | date = October 2013 | pmid = 23965338 | pmc = 4076475 | doi = 10.1161/CIRCRESAHA.113.301151 }}
{{cite journal | vauthors = Zong NC, Li H, Li H, Lam MP, Jimenez RC, Kim CS, Deng N, Kim AK, Choi JH, Zelaya I, Liem D, Meyer D, Odeberg J, Fang C, Lu HJ, Xu T, Weiss J, Duan H, Uhlen M, Yates JR, Apweiler R, Ge J, Hermjakob H, Ping P | title = Integration of cardiac proteome biology and medicine by a specialized knowledgebase | journal = Circulation Research | volume = 113 | issue = 9 | pages = 1043–53 | date = October 2013 | pmid = 23965338 | pmc = 4076475 | doi = 10.1161/CIRCRESAHA.113.301151 }}


⚫
</ref><ref name="url_COPaKB">{{cite web | url = https://amino.heartproteome.org/web/protein/P00403 | work = Cardiac Organellar Protein Atlas Knowledgebase (COPaKB) | title = Cytochrome c oxidase subunit 2 }}{{Dead link|date=August 2020 |bot=InternetArchiveBot |fix-attempted=yes }}</ref> MT-CO2 is a subunit of the enzyme [[Cytochrome c oxidase]] ({{EC number|1.9.3.1}})<ref name="pmid6307356">
</ref><ref name="url_COPaKB">

⚫
{{cite web | url = https://amino.heartproteome.org/web/protein/P00403 | work = Cardiac Organellar Protein Atlas Knowledgebase (COPaKB) | title = Cytochrome c oxidase subunit 2
}}

</ref> MT-CO2 is a subunit of the enzyme [[Cytochrome c oxidase]] ({{EC number|1.9.3.1}})<ref name="pmid6307356">


{{cite journal | vauthors = Capaldi RA, Malatesta F, Darley-Usmar VM | title = Structure of cytochrome c oxidase | journal = Biochimica et Biophysica Acta | volume = 726 | issue = 2 | pages = 135–48 | date = July 1983 | pmid = 6307356 | doi = 10.1016/0304-4173(83)90003-4 }}
{{cite journal | vauthors = Capaldi RA, Malatesta F, Darley-Usmar VM | title = Structure of cytochrome c oxidase | journal = Biochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics | volume = 726 | issue = 2 | pages = 135–48 | date = July 1983 | pmid = 6307356 | doi = 10.1016/0304-4173(83)90003-4 }}


</ref><ref name="pmid8083153">
</ref><ref name="pmid8083153">


{{cite journal | vauthors = García-Horsman JA, Barquera B, Rumbley J, Ma J, Gennis RB | title = The superfamily of heme-copper respiratory oxidases | journal = Journal of Bacteriology | volume = 176 | issue = 18 | pages = 5587–600 | date = September 1994 | pmid = 8083153 | pmc = 196760 | doi = }}
{{cite journal | vauthors = García-Horsman JA, Barquera B, Rumbley J, Ma J, Gennis RB | title = The superfamily of heme-copper respiratory oxidases | journal = Journal of Bacteriology | volume = 176 | issue = 18 | pages = 5587–600 | date = September 1994 | pmid = 8083153 | pmc = 196760 | doi = 10.1128/jb.176.18.5587-5600.1994}}


</ref> (Complex IV), an oligomeric enzymatic [[Protein complex|complex]] of the [[mitochondrial respiratory chain]] involved in the transfer of [[electrons]] from [[cytochrome c]] to [[oxygen]]. In eukaryotes this [[enzyme]] [[Protein complex|complex]] is located in the [[mitochondrial inner membrane]]; in [[Aerobic organism|aerobic]] [[prokaryotes]] it is found in the [[plasma membrane]]. The enzyme complex consists of 3-4 subunits ([[prokaryotes]]) to up to 13 [[polypeptides]] (mammals). The N-terminal domain of cytochrome C oxidase contains two transmembrane alpha-helices.<ref name="pmid8083153"/><ref name="pmid6307356"/> The structure of MT-CO2 is known to contain one redox center and a [[Copper protein|binuclear copper A center (CuA)]]. The [[Copper protein|CuA]] is located in a conserved [[cysteine]] loop at 196 and 200 [[amino acid]] positions and conserved [[histidine]] at 204. Several bacterial MT-CO2 have a C-terminal extension that contains a covalently bound haem c.<ref name ="pmid2165384">{{cite journal | vauthors = Capaldi RA | title = Structure and function of cytochrome c oxidase | journal = Annual Review of Biochemistry | volume = 59 | pages = 569–96 | date = 1990 | pmid = 2165384 | doi = 10.1146/annurev.bi.59.070190.003033 }}</ref><ref name = "pmid8389744">{{cite journal | vauthors = Hill BC | title = The sequence of electron carriers in the reaction of cytochrome c oxidase with oxygen | journal = Journal of Bioenergetics and Biomembranes | volume = 25 | issue = 2 | pages = 115–20 | date = April 1993 | pmid = 8389744 }}</ref>
</ref> (Complex IV), an oligomeric enzymatic [[Protein complex|complex]] of the [[mitochondrial respiratory chain]] involved in the transfer of [[electrons]] from [[cytochrome c]] to [[oxygen]]. In eukaryotes this [[enzyme]] [[Protein complex|complex]] is located in the [[mitochondrial inner membrane]]; in [[Aerobic organism|aerobic]] [[prokaryotes]] it is found in the [[plasma membrane]]. The enzyme complex consists of 3-4 subunits ([[prokaryotes]]) to up to 13 [[polypeptides]] (mammals). The N-terminal domain of cytochrome C oxidase contains two transmembrane alpha-helices.<ref name="pmid8083153"/><ref name="pmid6307356"/> The structure of MT-CO2 is known to contain one redox center and a [[Copper protein|binuclear copper A center (CuA)]]. The [[Copper protein|CuA]] is located in a conserved [[cysteine]] loop at 196 and 200 [[amino acid]] positions and conserved [[histidine]] at 204. Several bacterial MT-CO2 have a C-terminal extension that contains a covalently bound haem c.<ref name ="pmid2165384">{{cite journal | vauthors = Capaldi RA | title = Structure and function of cytochrome c oxidase | journal = Annual Review of Biochemistry | volume = 59 | pages = 569–96 | date = 1990 | pmid = 2165384 | doi = 10.1146/annurev.bi.59.070190.003033 }}</ref><ref name = "pmid8389744">{{cite journal | vauthors = Hill BC | title = The sequence of electron carriers in the reaction of cytochrome c oxidase with oxygen | journal = Journal of Bioenergetics and Biomembranes | volume = 25 | issue = 2 | pages = 115–20 | date = April 1993 | pmid = 8389744 | doi=10.1007/bf00762853| s2cid = 45975377 }}</ref>


== Function ==
== Function ==
The ''MT-CO2'' gene encodes for the second subunit of [[cytochrome c oxidase]] (complex IV), a component of the [[mitochondrial respiratory chain]] that catalyzes the [[reduction (chemistry)|reduction]] of [[oxygen]] to [[water]]. MT-CO2 is one of the three subunits which are responsible for the formation of the functional core of the [[cytochrome c oxidase]]. MT-CO2 plays an essential role in the transfer of electrons from [[cytochrome c]] to the bimetallic center of the [[Cytochrome c oxidase subunit I|catalytic subunit 1]] by utilizing its [[Copper protein|binuclear copper A center]]. It contains two adjacent transmembrane regions in its [[N-terminus]] and the major part of the protein is exposed to the periplasmic or to the mitochondrial [[intermembrane space]], respectively. MT-CO2 provides the substrate-binding site and contains the [[copper proteins|binuclear copper A center]], probably the primary acceptor in cytochrome c oxidase.<ref name = "uniprot">
The ''MT-CO2'' gene encodes for the second subunit of [[cytochrome c oxidase]] (complex IV), a component of the [[mitochondrial respiratory chain]] that catalyzes the [[reduction (chemistry)|reduction]] of [[oxygen]] to [[water]]. MT-CO2 is one of the three subunits which are responsible for the formation of the functional core of the [[cytochrome c oxidase]]. MT-CO2 plays an essential role in the transfer of electrons from [[cytochrome c]] to the bimetallic center of the [[Cytochrome c oxidase subunit I|catalytic subunit 1]] by utilizing its [[Copper protein|binuclear copper A center]]. It contains two adjacent transmembrane regions in its [[N-terminus]] and the major part of the protein is exposed to the periplasmic or to the mitochondrial [[intermembrane space]], respectively. MT-CO2 provides the substrate-binding site and contains the [[copper proteins|binuclear copper A center]], probably the primary acceptor in cytochrome c oxidase.<ref name = "uniprot">


{{Cite web|url=https://www.uniprot.org/uniprot/P00403|title= MT-CO2 - Cytochrome c oxidase subunit 2 - Homo sapiens (Human) - MT-CO2 gene & protein|access-date=2018-08-07}}{{CC-notice|cc=by4 | url=https://www.uniprot.org/uniprot/Q9Y2R0 | work = UniProt }}
{{Cite web|url=https://www.uniprot.org/uniprot/P00403|title= MT-CO2 - Cytochrome c oxidase subunit 2 - Homo sapiens (Human) - MT-CO2 gene & protein|access-date=2018-08-07}}{{CC-notice|cc=by4 | url=https://www.uniprot.org/uniprot/Q9Y2R0 | work = UniProt }}
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</ref><ref name="uniprot0">
</ref><ref name="uniprot0">


{{cite journal | vauthors = | title = UniProt: the universal protein knowledgebase | journal = Nucleic Acids Research | volume = 45 | issue = D1 | pages = D158-D169 | date = January 2017 | pmid = 27899622 | pmc = 5210571 | doi = 10.1093/nar/gkw1099 }}
{{cite journal | title = UniProt: the universal protein knowledgebase | journal = Nucleic Acids Research | volume = 45 | issue = D1 | pages = D158–D169 | date = January 2017 | pmid = 27899622 | pmc = 5210571 | doi = 10.1093/nar/gkw1099 }}


</ref><ref name = "entrez"/>
</ref><ref name = "entrez"/>
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===Mitochondrial complex IV deficiency===
===Mitochondrial complex IV deficiency===
Variants of ''MT-CO2'' have been associated with the [[mitochondria|mitochondrial]] [[cytochrome c oxidase|Complex IV]] deficiency, a deficiency in an enzyme complex of the [[mitochondrial respiratory chain]] that catalyzes the oxidation of [[cytochrome c]] utilizing [[oxygen| molecular oxygen]].<ref name = "hi2">
Variants of ''MT-CO2'' have been associated with the [[mitochondria]]l [[cytochrome c oxidase|Complex IV]] deficiency, a deficiency in an enzyme complex of the [[mitochondrial respiratory chain]] that catalyzes the oxidation of [[cytochrome c]] utilizing [[oxygen|molecular oxygen]].<ref name = "hi2">


{{cite journal | vauthors = Ostergaard E, Weraarpachai W, Ravn K, Born AP, Jønson L, Duno M, Wibrand F, Shoubridge EA, Vissing J | title = Mutations in COA3 cause isolated complex IV deficiency associated with neuropathy, exercise intolerance, obesity, and short stature | journal = Journal of Medical Genetics | volume = 52 | issue = 3 | pages = 203–7 | date = March 2015 | pmid = 25604084 | doi = 10.1136/jmedgenet-2014-102914 }}
{{cite journal | vauthors = Ostergaard E, Weraarpachai W, Ravn K, Born AP, Jønson L, Duno M, Wibrand F, Shoubridge EA, Vissing J | title = Mutations in COA3 cause isolated complex IV deficiency associated with neuropathy, exercise intolerance, obesity, and short stature | journal = Journal of Medical Genetics | volume = 52 | issue = 3 | pages = 203–7 | date = March 2015 | pmid = 25604084 | doi = 10.1136/jmedgenet-2014-102914 | s2cid = 43018915 }}


</ref> The deficiency is characterized by [[heterogeneous]] [[phenotypes]] ranging from isolated [[myopathy]] to severe [[multisystem disease]] affecting several tissues and organs. Other Clinical Manifestations include [[hypertrophic cardiomyopathy]], [[hepatomegaly]] and [[liver dysfunction]], [[hypotonia]], [[muscle weakness]], [[exercise intolerance]], [[developmental delay]], delayed [[motor development]] and [[mental retardation]].<ref>{{cite web |title=Mitochondrial complex IV deficiency |url=https://www.uniprot.org/diseases/DI-01469 |website=www.uniprot.org |language=en}}</ref> Mutations of ''MT-CO2'' is also known to cause [[Leigh's disease]], which may be caused by an abnormality or deficiency of [[cytochrome oxidase]].<ref name="pmid8083153"/><ref name="pmid6307356"/>
</ref> The deficiency is characterized by [[heterogeneous]] [[phenotypes]] ranging from isolated [[myopathy]] to severe [[multisystem disease]] affecting several tissues and organs. Other Clinical Manifestations include [[hypertrophic cardiomyopathy]], [[hepatomegaly]] and [[liver dysfunction]], [[hypotonia]], [[muscle weakness]], [[exercise intolerance]], [[developmental disability]], delayed [[motor development]] and [[mental retardation]].<ref>{{cite web |title=Mitochondrial complex IV deficiency |url=https://www.uniprot.org/diseases/DI-01469 |website=www.uniprot.org |language=en}}</ref> Mutations of ''MT-CO2'' is also known to cause [[Leigh's disease]], which may be caused by an abnormality or deficiency of [[cytochrome oxidase]].<ref name="pmid8083153"/><ref name="pmid6307356"/>


A wide range of symptoms have been found in patients with pathogenic mutations in the ''MT-CO2'' gene with the [[mitochondria|mitochonrdial]] [[cytochrome c oxidase|Complex IV]] deficiency. A [[deletion mutation]] of a single nucleotide (7630delT) in the gene has been found to cause symptoms of reversible [[aphasia]], right [[hemiparesis]], [[hemianopsia]], [[exercise intolerance]], progressive [[mental impairment]], and short [[stature]].<ref>
A wide range of symptoms have been found in patients with pathogenic mutations in the ''MT-CO2'' gene with the [[mitochondria]]l [[cytochrome c oxidase|Complex IV]] deficiency. A [[deletion mutation]] of a single nucleotide (7630delT) in the gene has been found to cause symptoms of reversible [[aphasia]], right [[hemiparesis]], [[hemianopsia]], [[exercise intolerance]], progressive [[mental impairment]], and short [[Human stature|stature]].<ref>


{{cite journal | vauthors = Rossmanith W, Freilinger M, Roka J, Raffelsberger T, Moser-Thier K, Prayer D, Bernert G, Bittner RE | title = Isolated cytochrome c oxidase deficiency as a cause of MELAS | journal = Journal of Medical Genetics | volume = 45 | issue = 2 | pages = 117–21 | date = February 2008 | pmid = 18245391 | doi = 10.1136/jmg.2007.052076 | pmc = 3027970 }}
{{cite journal | vauthors = Rossmanith W, Freilinger M, Roka J, Raffelsberger T, Moser-Thier K, Prayer D, Bernert G, Bittner RE | title = Isolated cytochrome c oxidase deficiency as a cause of MELAS | journal = Journal of Medical Genetics | volume = 45 | issue = 2 | pages = 117–21 | date = February 2008 | pmid = 18245391 | doi = 10.1136/jmg.2007.052076 | pmc = 3027970 }}
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</ref> Furthermore, a patient with a [[nonsense mutation]] (7896G>A) of the gene resulted in phenotypes such as [[short stature]], low [[weight]], [[microcephaly]], [[skin abnormalities]], severe [[hypotonia]], and normal [[reflexes]].<ref>
</ref> Furthermore, a patient with a [[nonsense mutation]] (7896G>A) of the gene resulted in phenotypes such as [[short stature]], low [[weight]], [[microcephaly]], [[skin abnormalities]], severe [[hypotonia]], and normal [[reflexes]].<ref>


{{cite journal | vauthors = Campos Y, García-Redondo A, Fernández-Moreno MA, Martínez-Pardo M, Goda G, Rubio JC, Martín MA, del Hoyo P, Cabello A, Bornstein B, Garesse R, Arenas J | title = Early-onset multisystem mitochondrial disorder caused by a nonsense mutation in the mitochondrial DNA cytochrome C oxidase II gene | journal = Annals of Neurology | volume = 50 | issue = 3 | pages = 409–13 | date = September 2001 | pmid = 11558799 }}
{{cite journal | vauthors = Campos Y, García-Redondo A, Fernández-Moreno MA, Martínez-Pardo M, Goda G, Rubio JC, Martín MA, del Hoyo P, Cabello A, Bornstein B, Garesse R, Arenas J | title = Early-onset multisystem mitochondrial disorder caused by a nonsense mutation in the mitochondrial DNA cytochrome C oxidase II gene | journal = Annals of Neurology | volume = 50 | issue = 3 | pages = 409–13 | date = September 2001 | pmid = 11558799 | doi=10.1002/ana.1141| s2cid = 23891106 }}


</ref> A novel [[heteroplasmic]] mutation (7587T>C) which altered the initiation codon of the ''MT-CO2'' gene in patients have shown clinical manifestations such as progressive gait [[ataxia]], [[cognitive impairment]], bilateral [[optic atrophy]], [[pigmentary retinopathy]], a decrease in [[color vision]], and mild distal-[[muscle wasting]].<ref>{{cite journal | vauthors = Clark KM, Taylor RW, Johnson MA, Chinnery PF, Chrzanowska-Lightowlers ZM, Andrews RM, Nelson IP, Wood NW, Lamont PJ, Hanna MG, Lightowlers RN, Turnbull DM | title = An mtDNA mutation in the initiation codon of the cytochrome C oxidase subunit II gene results in lower levels of the protein and a mitochondrial encephalomyopathy | journal = American Journal of Human Genetics | volume = 64 | issue = 5 | pages = 1330–9 | date = May 1999 | pmid = 10205264 | doi = 10.1086/302361 }}
</ref> A novel [[heteroplasmic]] mutation (7587T>C) which altered the initiation codon of the ''MT-CO2'' gene in patients have shown clinical manifestations such as progressive gait [[ataxia]], [[cognitive impairment]], bilateral [[optic atrophy]], [[pigmentary retinopathy]], a decrease in [[color vision]], and mild distal-[[muscle wasting]].<ref>{{cite journal | vauthors = Clark KM, Taylor RW, Johnson MA, Chinnery PF, Chrzanowska-Lightowlers ZM, Andrews RM, Nelson IP, Wood NW, Lamont PJ, Hanna MG, Lightowlers RN, Turnbull DM | title = An mtDNA mutation in the initiation codon of the cytochrome C oxidase subunit II gene results in lower levels of the protein and a mitochondrial encephalomyopathy | journal = American Journal of Human Genetics | volume = 64 | issue = 5 | pages = 1330–9 | date = May 1999 | pmid = 10205264 | doi = 10.1086/302361 | pmc = 1377869 }}


</ref>
</ref>


===Others===
===Others===
Juvenile [[myopathy]], [[encephalopathy]], [[lactic acidosis]], and [[stroke]] have also been associated with mutations in the ''MT-CO2'' gene.<ref name = entrez />
Juvenile [[myopathy]], [[encephalopathy]], [[lactic acidosis]], and [[stroke]] have also been associated with mutations in the ''MT-CO2'' gene.<ref name = entrez />


== Interactions ==
== Interactions ==


MT-CO2 is known to interact with [[cytochrome c]] by the utilization of a lysine ring around the [[carboxyl]] containing [[Hemeprotein|heme edge]] of [[cytochrome c]] in MT-CO2, including glutamate 129, aspartate 132, and glutamate 19.
MT-CO2 is known to interact with [[cytochrome c]] by the utilization of a lysine ring around the [[carboxyl]] containing [[Hemeprotein|heme edge]] of [[cytochrome c]] in MT-CO2, including glutamate 129, aspartate 132, and glutamate 19.


== References ==
== References ==
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{{refbegin | 2}}
{{refbegin | 2}}
* {{cite journal | vauthors = Torroni A, Achilli A, Macaulay V, Richards M, Bandelt HJ | title = Harvesting the fruit of the human mtDNA tree | journal = Trends in Genetics | volume = 22 | issue = 6 | pages = 339–45 | date = June 2006 | pmid = 16678300 | doi = 10.1016/j.tig.2006.04.001 }}
* {{cite journal | vauthors = Torroni A, Achilli A, Macaulay V, Richards M, Bandelt HJ | title = Harvesting the fruit of the human mtDNA tree | journal = Trends in Genetics | volume = 22 | issue = 6 | pages = 339–45 | date = June 2006 | pmid = 16678300 | doi = 10.1016/j.tig.2006.04.001 }}
* {{cite journal | vauthors = Barrell BG, Bankier AT, Drouin J | title = A different genetic code in human mitochondria | journal = Nature | volume = 282 | issue = 5735 | pages = 189–94 | date = November 1979 | pmid = 226894 | doi = 10.1038/282189a0 }}
* {{cite journal | vauthors = Barrell BG, Bankier AT, Drouin J | title = A different genetic code in human mitochondria | journal = Nature | volume = 282 | issue = 5735 | pages = 189–94 | date = November 1979 | pmid = 226894 | doi = 10.1038/282189a0 | bibcode = 1979Natur.282..189B | s2cid = 4335828 }}
* {{cite journal | vauthors = Bodenteich A, Mitchell LG, Polymeropoulos MH, Merril CR | title = Dinucleotide repeat in the human mitochondrial D-loop | journal = Human Molecular Genetics | volume = 1 | issue = 2 | pages = 140 | date = May 1992 | pmid = 1301157 | doi = 10.1093/hmg/1.2.140-a }}
* {{cite journal | vauthors = Bodenteich A, Mitchell LG, Polymeropoulos MH, Merril CR | title = Dinucleotide repeat in the human mitochondrial D-loop | journal = Human Molecular Genetics | volume = 1 | issue = 2 | pages = 140 | date = May 1992 | pmid = 1301157 | doi = 10.1093/hmg/1.2.140-a | doi-access = free }}
* {{cite journal | vauthors = Lu X, Walker T, MacManus JP, Seligy VL | title = Differentiation of HT-29 human colonic adenocarcinoma cells correlates with increased expression of mitochondrial RNA: effects of trehalose on cell growth and maturation | journal = Cancer Research | volume = 52 | issue = 13 | pages = 3718–25 | date = July 1992 | pmid = 1377597 | doi = }}
* {{cite journal | vauthors = Lu X, Walker T, MacManus JP, Seligy VL | title = Differentiation of HT-29 human colonic adenocarcinoma cells correlates with increased expression of mitochondrial RNA: effects of trehalose on cell growth and maturation | journal = Cancer Research | volume = 52 | issue = 13 | pages = 3718–25 | date = July 1992 | pmid = 1377597 }}
* {{cite journal | vauthors = Marzuki S, Noer AS, Lertrit P, Thyagarajan D, Kapsa R, Utthanaphol P, Byrne E | title = Normal variants of human mitochondrial DNA and translation products: the building of a reference data base | journal = Human Genetics | volume = 88 | issue = 2 | pages = 139–45 | date = December 1991 | pmid = 1757091 | doi = 10.1007/bf00206061 }}
* {{cite journal | vauthors = Marzuki S, Noer AS, Lertrit P, Thyagarajan D, Kapsa R, Utthanaphol P, Byrne E | title = Normal variants of human mitochondrial DNA and translation products: the building of a reference data base | journal = Human Genetics | volume = 88 | issue = 2 | pages = 139–45 | date = December 1991 | pmid = 1757091 | doi = 10.1007/bf00206061 | s2cid = 28048453 }}
* {{cite journal | vauthors = Moraes CT, Andreetta F, Bonilla E, Shanske S, DiMauro S, Schon EA | title = Replication-competent human mitochondrial DNA lacking the heavy-strand promoter region | journal = Molecular and Cellular Biology | volume = 11 | issue = 3 | pages = 1631–7 | date = March 1991 | pmid = 1996112 | pmc = 369459 | doi = }}
* {{cite journal | vauthors = Moraes CT, Andreetta F, Bonilla E, Shanske S, DiMauro S, Schon EA | title = Replication-competent human mitochondrial DNA lacking the heavy-strand promoter region | journal = Molecular and Cellular Biology | volume = 11 | issue = 3 | pages = 1631–7 | date = March 1991 | pmid = 1996112 | pmc = 369459 | doi = 10.1128/MCB.11.3.1631}}
* {{cite journal | vauthors = Power MD, Kiefer MC, Barr PJ, Reeves R | title = Nucleotide sequence of human mitochondrial cytochrome c oxidase II cDNA | journal = Nucleic Acids Research | volume = 17 | issue = 16 | pages = 6734 | date = August 1989 | pmid = 2550900 | pmc = 318375 | doi = 10.1093/nar/17.16.6734 }}
* {{cite journal | vauthors = Power MD, Kiefer MC, Barr PJ, Reeves R | title = Nucleotide sequence of human mitochondrial cytochrome c oxidase II cDNA | journal = Nucleic Acids Research | volume = 17 | issue = 16 | pages = 6734 | date = August 1989 | pmid = 2550900 | pmc = 318375 | doi = 10.1093/nar/17.16.6734 }}
* {{cite journal | vauthors = Attardi G, Chomyn A, Doolittle RF, Mariottini P, Ragan CI | title = Seven unidentified reading frames of human mitochondrial DNA encode subunits of the respiratory chain NADH dehydrogenase | journal = Cold Spring Harbor Symposia on Quantitative Biology | volume = 51 Pt 1 | issue = 1 | pages = 103–14 | year = 1987 | pmid = 3472707 | doi = 10.1101/sqb.1986.051.01.013 }}
* {{cite journal | vauthors = Attardi G, Chomyn A, Doolittle RF, Mariottini P, Ragan CI | title = Seven unidentified reading frames of human mitochondrial DNA encode subunits of the respiratory chain NADH dehydrogenase | journal = Cold Spring Harbor Symposia on Quantitative Biology | volume = 51 | issue = 1 | pages = 103–14 | year = 1987 | pmid = 3472707 | doi = 10.1101/sqb.1986.051.01.013 }}
* {{cite journal | vauthors = Chomyn A, Cleeter MW, Ragan CI, Riley M, Doolittle RF, Attardi G | title = URF6, last unidentified reading frame of human mtDNA, codes for an NADH dehydrogenase subunit | journal = Science | volume = 234 | issue = 4776 | pages = 614–8 | date = October 1986 | pmid = 3764430 | doi = 10.1126/science.3764430 }}
* {{cite journal | vauthors = Chomyn A, Cleeter MW, Ragan CI, Riley M, Doolittle RF, Attardi G | title = URF6, last unidentified reading frame of human mtDNA, codes for an NADH dehydrogenase subunit | journal = Science | volume = 234 | issue = 4776 | pages = 614–8 | date = October 1986 | pmid = 3764430 | doi = 10.1126/science.3764430 | bibcode = 1986Sci...234..614C }}
* {{cite journal | vauthors = Chomyn A, Mariottini P, Cleeter MW, Ragan CI, Matsuno-Yagi A, Hatefi Y, Doolittle RF, Attardi G | title = Six unidentified reading frames of human mitochondrial DNA encode components of the respiratory-chain NADH dehydrogenase | journal = Nature | volume = 314 | issue = 6012 | pages = 592–7 | year = 1985 | pmid = 3921850 | doi = 10.1038/314592a0 }}
* {{cite journal | vauthors = Chomyn A, Mariottini P, Cleeter MW, Ragan CI, Matsuno-Yagi A, Hatefi Y, Doolittle RF, Attardi G | title = Six unidentified reading frames of human mitochondrial DNA encode components of the respiratory-chain NADH dehydrogenase | journal = Nature | volume = 314 | issue = 6012 | pages = 592–7 | year = 1985 | pmid = 3921850 | doi = 10.1038/314592a0 | bibcode = 1985Natur.314..592C | s2cid = 32964006 }}
* {{cite journal | vauthors = Anderson S, Bankier AT, Barrell BG, de Bruijn MH, Coulson AR, Drouin J, Eperon IC, Nierlich DP, Roe BA, Sanger F, Schreier PH, Smith AJ, Staden R, Young IG | title = Sequence and organization of the human mitochondrial genome | journal = Nature | volume = 290 | issue = 5806 | pages = 457–65 | date = April 1981 | pmid = 7219534 | doi = 10.1038/290457a0 }}
* {{cite journal | vauthors = Anderson S, Bankier AT, Barrell BG, de Bruijn MH, Coulson AR, Drouin J, Eperon IC, Nierlich DP, Roe BA, Sanger F, Schreier PH, Smith AJ, Staden R, Young IG | title = Sequence and organization of the human mitochondrial genome | journal = Nature | volume = 290 | issue = 5806 | pages = 457–65 | date = April 1981 | pmid = 7219534 | doi = 10.1038/290457a0 | bibcode = 1981Natur.290..457A | s2cid = 4355527 }}
* {{cite journal | vauthors = Montoya J, Ojala D, Attardi G | title = Distinctive features of the 5'-terminal sequences of the human mitochondrial mRNAs | journal = Nature | volume = 290 | issue = 5806 | pages = 465–70 | date = April 1981 | pmid = 7219535 | doi = 10.1038/290465a0 }}
* {{cite journal | vauthors = Montoya J, Ojala D, Attardi G | title = Distinctive features of the 5'-terminal sequences of the human mitochondrial mRNAs | journal = Nature | volume = 290 | issue = 5806 | pages = 465–70 | date = April 1981 | pmid = 7219535 | doi = 10.1038/290465a0 | bibcode = 1981Natur.290..465M | s2cid = 4358928 }}
* {{cite journal | vauthors = Horai S, Hayasaka K, Kondo R, Tsugane K, Takahata N | title = Recent African origin of modern humans revealed by complete sequences of hominoid mitochondrial DNAs | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 92 | issue = 2 | pages = 532–6 | date = January 1995 | pmid = 7530363 | pmc = 42775 | doi = 10.1073/pnas.92.2.532 }}
* {{cite journal | vauthors = Horai S, Hayasaka K, Kondo R, Tsugane K, Takahata N | title = Recent African origin of modern humans revealed by complete sequences of hominoid mitochondrial DNAs | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 92 | issue = 2 | pages = 532–6 | date = January 1995 | pmid = 7530363 | pmc = 42775 | doi = 10.1073/pnas.92.2.532 | bibcode = 1995PNAS...92..532H | doi-access = free }}
* {{cite journal | vauthors = Ruvolo M, Zehr S, von Dornum M, Pan D, Chang B, Lin J | title = Mitochondrial COII sequences and modern human origins | journal = Molecular Biology and Evolution | volume = 10 | issue = 6 | pages = 1115–35 | date = November 1993 | pmid = 8277847 | doi = 10.1093/oxfordjournals.molbev.a040068 }}
* {{cite journal | vauthors = Ruvolo M, Zehr S, von Dornum M, Pan D, Chang B, Lin J | title = Mitochondrial COII sequences and modern human origins | journal = Molecular Biology and Evolution | volume = 10 | issue = 6 | pages = 1115–35 | date = November 1993 | pmid = 8277847 | doi = 10.1093/oxfordjournals.molbev.a040068 | doi-access = free }}
* {{cite journal | vauthors = Polyak K, Li Y, Zhu H, Lengauer C, Willson JK, Markowitz SD, Trush MA, Kinzler KW, Vogelstein B | title = Somatic mutations of the mitochondrial genome in human colorectal tumours | journal = Nature Genetics | volume = 20 | issue = 3 | pages = 291–3 | date = November 1998 | pmid = 9806551 | doi = 10.1038/3108 }}
* {{cite journal | vauthors = Polyak K, Li Y, Zhu H, Lengauer C, Willson JK, Markowitz SD, Trush MA, Kinzler KW, Vogelstein B | title = Somatic mutations of the mitochondrial genome in human colorectal tumours | journal = Nature Genetics | volume = 20 | issue = 3 | pages = 291–3 | date = November 1998 | pmid = 9806551 | doi = 10.1038/3108 | s2cid = 19786796 }}
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[[Category:Protein domains]]
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Latest revision as of 06:55, 15 April 2024

"COX2" redirects here. For the cyclooxygenase isoenzyme, see Cyclooxygenase-2.
COX2
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesCOX2, mitochondrially encoded cytochrome c oxidase II, COII, MTCO2, Cytochrome c oxidase subunit II, CO II
External IDsOMIM: 516040; MGI: 102503; HomoloGene: 5017; GeneCards: COX2; OMA:COX2 - orthologs
Orthologs
SpeciesHumanMouse
Entrez

4513

17709

Ensembl

ENSG00000198712

ENSMUSG00000064354

UniProt

P00403

P00405

RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

NP_904331

Location (UCSC)Chr M: 0.01 – 0.01 MbChr M: 0.01 – 0.01 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse
Location of the MT-CO2 gene in the human mitochondrial genome. MT-CO2 is one of the three cytochrome c oxidase subunit mitochondrial genes (orange boxes).
Cytochrome c oxidase subunit II, transmembrane domain
Bacterial cytochrome c oxidase complex. Subunit II indicated by blue.
Identifiers
SymbolCOX2_TM
PfamPF02790
InterProIPR011759
PROSITEPDOC00075
SCOP21occ / SCOPe / SUPFAM
TCDB3.D.4
OPM superfamily4
OPM protein1v55
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Cytochrome C oxidase subunit II, periplasmic domain
Identifiers
SymbolCOX2
PfamPF00116
InterProIPR002429
CDDcd13912
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Cytochrome c oxidase II is a protein in eukaryotes that is encoded by the MT-CO2 gene.[5] Cytochrome c oxidase subunit II, abbreviated COXII, COX2, COII, or MT-CO2, is the second subunit 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.

Structure[edit]

In humans, the MT-CO2 gene is located on the p arm of mitochondrial DNA at position 12 and it spans 683 base pairs.[5] The MT-CO2 gene produces a 25.6 kDa protein composed of 227 amino acids.[6][7] MT-CO2 is a subunit of the enzyme Cytochrome c oxidase (EC 1.9.3.1)[8][9] (Complex IV), an oligomeric enzymatic complex of the mitochondrial respiratory chain involved in the transfer of electrons from cytochrome c to oxygen. In eukaryotes this enzyme complex is located in the mitochondrial inner membrane; in aerobic prokaryotes it is found in the plasma membrane. The enzyme complex consists of 3-4 subunits (prokaryotes) to up to 13 polypeptides (mammals). The N-terminal domain of cytochrome C oxidase contains two transmembrane alpha-helices.[9][8] The structure of MT-CO2 is known to contain one redox center and a binuclear copper A center (CuA). The CuA is located in a conserved cysteine loop at 196 and 200 amino acid positions and conserved histidine at 204. Several bacterial MT-CO2 have a C-terminal extension that contains a covalently bound haem c.[10][11]

Function[edit]

The MT-CO2 gene encodes for the second subunit of cytochrome c oxidase (complex IV), a component of the mitochondrial respiratory chain that catalyzes the reduction of oxygen to water. MT-CO2 is one of the three subunits which are responsible for the formation of the functional core of the cytochrome c oxidase. MT-CO2 plays an essential role in the transfer of electrons from cytochrome c to the bimetallic center of the catalytic subunit 1 by utilizing its binuclear copper A center. It contains two adjacent transmembrane regions in its N-terminus and the major part of the protein is exposed to the periplasmic or to the mitochondrial intermembrane space, respectively. MT-CO2 provides the substrate-binding site and contains the binuclear copper A center, probably the primary acceptor in cytochrome c oxidase.[12][13][5]

Clinical significance[edit]

Mitochondrial complex IV deficiency[edit]

Variants of MT-CO2 have been associated with the mitochondrial Complex IV deficiency, a deficiency in an enzyme complex of the mitochondrial respiratory chain that catalyzes the oxidation of cytochrome c utilizing molecular oxygen.[14] The deficiency is characterized by heterogeneous phenotypes ranging from isolated myopathy to severe multisystem disease affecting several tissues and organs. Other Clinical Manifestations include hypertrophic cardiomyopathy, hepatomegaly and liver dysfunction, hypotonia, muscle weakness, exercise intolerance, developmental disability, delayed motor development and mental retardation.[15] Mutations of MT-CO2 is also known to cause Leigh's disease, which may be caused by an abnormality or deficiency of cytochrome oxidase.[9][8]

A wide range of symptoms have been found in patients with pathogenic mutations in the MT-CO2 gene with the mitochondrial Complex IV deficiency. A deletion mutation of a single nucleotide (7630delT) in the gene has been found to cause symptoms of reversible aphasia, right hemiparesis, hemianopsia, exercise intolerance, progressive mental impairment, and short stature.[16] Furthermore, a patient with a nonsense mutation (7896G>A) of the gene resulted in phenotypes such as short stature, low weight, microcephaly, skin abnormalities, severe hypotonia, and normal reflexes.[17] A novel heteroplasmic mutation (7587T>C) which altered the initiation codon of the MT-CO2 gene in patients have shown clinical manifestations such as progressive gait ataxia, cognitive impairment, bilateral optic atrophy, pigmentary retinopathy, a decrease in color vision, and mild distal-muscle wasting.[18]

Others[edit]

Juvenile myopathy, encephalopathy, lactic acidosis, and stroke have also been associated with mutations in the MT-CO2 gene.[5]

Interactions[edit]

MT-CO2 is known to interact with cytochrome c by the utilization of a lysine ring around the carboxyl containing heme edge of cytochrome c in MT-CO2, including glutamate 129, aspartate 132, and glutamate 19.

References[edit]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000198712 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000064354 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ a b c d "Entrez Gene: COX2 cytochrome c oxidase subunit II".Public Domain This article incorporates text from this source, which is in the public domain.
  6. ^ Zong NC, Li H, Li H, Lam MP, Jimenez RC, Kim CS, Deng N, Kim AK, Choi JH, Zelaya I, Liem D, Meyer D, Odeberg J, Fang C, Lu HJ, Xu T, Weiss J, Duan H, Uhlen M, Yates JR, Apweiler R, Ge J, Hermjakob H, Ping P (October 2013). "Integration of cardiac proteome biology and medicine by a specialized knowledgebase". Circulation Research. 113 (9): 1043–53. doi:10.1161/CIRCRESAHA.113.301151. PMC 4076475. PMID 23965338.
  7. ^ "Cytochrome c oxidase subunit 2". Cardiac Organellar Protein Atlas Knowledgebase (COPaKB).[permanent dead link]
  8. ^ a b c Capaldi RA, Malatesta F, Darley-Usmar VM (July 1983). "Structure of cytochrome c oxidase". Biochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics. 726 (2): 135–48. doi:10.1016/0304-4173(83)90003-4. PMID 6307356.
  9. ^ a b c García-Horsman JA, Barquera B, Rumbley J, Ma J, Gennis RB (September 1994). "The superfamily of heme-copper respiratory oxidases". Journal of Bacteriology. 176 (18): 5587–600. doi:10.1128/jb.176.18.5587-5600.1994. PMC 196760. PMID 8083153.
  10. ^ Capaldi RA (1990). "Structure and function of cytochrome c oxidase". Annual Review of Biochemistry. 59: 569–96. doi:10.1146/annurev.bi.59.070190.003033. PMID 2165384.
  11. ^ Hill BC (April 1993). "The sequence of electron carriers in the reaction of cytochrome c oxidase with oxygen". Journal of Bioenergetics and Biomembranes. 25 (2): 115–20. doi:10.1007/bf00762853. PMID 8389744. S2CID 45975377.
  12. ^ "MT-CO2 - Cytochrome c oxidase subunit 2 - Homo sapiens (Human) - MT-CO2 gene & protein". Retrieved 2018-08-07. This article incorporates text available under the CC BY 4.0 license.
  13. ^ "UniProt: the universal protein knowledgebase". Nucleic Acids Research. 45 (D1): D158–D169. January 2017. doi:10.1093/nar/gkw1099. PMC 5210571. PMID 27899622.
  14. ^ Ostergaard E, Weraarpachai W, Ravn K, Born AP, Jønson L, Duno M, Wibrand F, Shoubridge EA, Vissing J (March 2015). "Mutations in COA3 cause isolated complex IV deficiency associated with neuropathy, exercise intolerance, obesity, and short stature". Journal of Medical Genetics. 52 (3): 203–7. doi:10.1136/jmedgenet-2014-102914. PMID 25604084. S2CID 43018915.
  15. ^ "Mitochondrial complex IV deficiency". www.uniprot.org.
  16. ^ Rossmanith W, Freilinger M, Roka J, Raffelsberger T, Moser-Thier K, Prayer D, Bernert G, Bittner RE (February 2008). "Isolated cytochrome c oxidase deficiency as a cause of MELAS". Journal of Medical Genetics. 45 (2): 117–21. doi:10.1136/jmg.2007.052076. PMC 3027970. PMID 18245391.
  17. ^ Campos Y, García-Redondo A, Fernández-Moreno MA, Martínez-Pardo M, Goda G, Rubio JC, Martín MA, del Hoyo P, Cabello A, Bornstein B, Garesse R, Arenas J (September 2001). "Early-onset multisystem mitochondrial disorder caused by a nonsense mutation in the mitochondrial DNA cytochrome C oxidase II gene". Annals of Neurology. 50 (3): 409–13. doi:10.1002/ana.1141. PMID 11558799. S2CID 23891106.
  18. ^ Clark KM, Taylor RW, Johnson MA, Chinnery PF, Chrzanowska-Lightowlers ZM, Andrews RM, Nelson IP, Wood NW, Lamont PJ, Hanna MG, Lightowlers RN, Turnbull DM (May 1999). "An mtDNA mutation in the initiation codon of the cytochrome C oxidase subunit II gene results in lower levels of the protein and a mitochondrial encephalomyopathy". American Journal of Human Genetics. 64 (5): 1330–9. doi:10.1086/302361. PMC 1377869. PMID 10205264.

Further reading[edit]

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

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