COX7B: Difference between revisions

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Latest revision as of 17:14, 8 September 2018

Cytochrome c oxidase subunit 7B, mitochondrial (COX7B) is an enzyme that in humans is encoded by the COX7B gene.^[1] COX7B is a nuclear-encoded subunit of cytochrome c oxidase (COX). Cytochrome c oxidase (complex IV) is a multi-subunit enzyme complex that couples the transfer of electrons from cytochrome c to molecular oxygen and contributes to a proton electrochemical gradient across the inner mitochondrial membrane, acting as the terminal enzyme of the mitochondrial respiratory chain.^[2] Work with Oryzias latices has linked disruptions in COX7B with microphthalmia with linear skin lesions (MLS), microcephaly, and mitochondrial disease. Clinically, mutations in COX7B have been associated with linear skin defects with multiple congenital anomalies.^[3]

Structure

COX7B is located on the q arm of the X chromosome in position 21.1 and has 3 exons.^[2] The COX7B gene produces a 9.2 kDa protein composed of 80 amino acids.^[4]^[5] COX7B is one of the nuclear-encoded polypeptide chains of cytochrome c oxidase (COX), a heteromeric complex consisting of 3 catalytic subunits encoded by mitochondrial genes and multiple structural subunits encoded by nuclear genes. The protein encoded by COX7B belongs to the cytochrome c oxidase VIIb family. COX7B has a 24 amino acid transit peptide domain from positions 1-24, an 8 amino acid topological mitochondrial matrix domain from positions 25-32, a helical, 27 amino acid transmembrane domain from positions 33-59, and a 21 amino acid topological intermembrane domain from positions 60-80.^[6]^[7]^[8]^[3] COX7B may also have several pseudogenes on chromosomes 1, 2, 20 and 22.^[2]

Function

Cytochrome c oxidase (COX), the terminal enzyme of the mitochondrial respiratory chain, catalyzes the electron transfer from reduced cytochrome c to oxygen. The mitochondrially-encoded subunits of COX function in electron transfer, while the nuclear-encoded subunits may be involved in the regulation and assembly of the complex. The COX7B nuclear gene encodes subunit 7B, which is located on the inner mitochondrial membrane in association with several other proteins encompassing the COX complex. It is found in all tissues and has been shown to be highly similar to bovine COX VIIb protein.^[2] COX7B is believed to be important for COX assembly and activity, the function of mitochondrial respiratory chain, and the proper development of the central nervous system in vertebrates.^[3]^[6]^[7]

Model organisms

Oryzias latices (also known as medaka) is a Japanese rice fish that has been used as a model organism in COX7B studies. By using a morpholino knockdown technique, COX7B has been shown to be indispensable for COX assembly, COX activity, and mitochondrial respiration. Additionally, the down-regulation of an ortholog of COX7B has suggested that there may be an association between COX7B disfunction and microphthalmia with linear skin lesions (MLS), microcephaly, and mitochondrial disease. Work with Oryzias latices could also indicate an evolutionary conserved role for the mitochondrial respiratory chain complexes in central nervous system development.^[3]

Clinical significance

Mutations in COX7B have been associated with linear skin defects with multiple congenital anomalies. This disorder is a distinct form of aplasia cutis congenita presenting as multiple linear skin defects on the face and neck associated with poor growth and short stature, microcephaly, and facial dysmorphism. Additional clinical features include intellectual disability, nail dystrophy, cardiac abnormalities, diaphragmatic hernia, genitourinary abnormalities, pale optic discs and altered visual-evoked potentials, agenesis of the corpus callosum, and other central nervous system abnormalities.^[6]^[7] The COX7B mutations associated with disease include c.196delC, a heterozygous mutation leading to a frameshift in exon 3, c.41-2A>G, a heterozygous splice mutation in a novel acceptor site in intron 1, and c.55C>T, a heterozygous nonsense mutation in exon 2. Additionally, experiments with Oryzias latices suggest COX7B may be associated with microphthalmia with linear skin lesions (MLS), an X-linked, dominant, male-lethal mitochondrial disorder.^[3]

Interactions

COX7B has been shown to have 6 binary protein-protein interactions including 3 co-complex interactions. GNMT, MYB, MT-CO1, HSCB, and SLC25A13 have all been found to interact with COX7B.^[9]

References

↑ Sadlock JE, Lightowlers RN, Capaldi RA, Schon EA (February 1993). "Isolation of a cDNA specifying subunit VIIb of human cytochrome c oxidase". Biochimica et Biophysica Acta. 1172 (1–2): 223–5. doi:10.1016/0167-4781(93)90301-s. PMID 8382530.
↑ ^2.0 ^2.1 ^2.2 ^2.3 "Entrez Gene: COX7B cytochrome c oxidase subunit VIIb". This article incorporates text from this source, which is in the public domain.
↑ ^3.0 ^3.1 ^3.2 ^3.3 ^3.4 Indrieri A, van Rahden VA, Tiranti V, Morleo M, Iaconis D, Tammaro R, D'Amato I, Conte I, Maystadt I, Demuth S, Zvulunov A, Kutsche K, Zeviani M, Franco B (November 2012). "Mutations in COX7B cause microphthalmia with linear skin lesions, an unconventional mitochondrial disease". American Journal of Human Genetics. 91 (5): 942–9. doi:10.1016/j.ajhg.2012.09.016. PMC 3487127. PMID 23122588.
↑ Yao, Daniel. "Cardiac Organellar Protein Atlas Knowledgebase (COPaKB) —— Protein Information". amino.heartproteome.org. Retrieved 2018-08-06.
↑ 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.
↑ ^6.0 ^6.1 ^6.2 "COX7B - Cytochrome c oxidase subunit 7B, mitochondrial precursor - Homo sapiens (Human) - COX7B gene & protein". uniprot.org. Retrieved 2018-08-06.File:CC-BY-icon-80x15.png This article incorporates text available under the CC BY 4.0 license.
↑ ^7.0 ^7.1 ^7.2 "UniProt: the universal protein knowledgebase". Nucleic Acids Research. 45 (D1): D158–D169. January 2017. doi:10.1093/nar/gkw1099. PMC 5210571. PMID 27899622.
↑ Van Kuilenburg AB, Van Beeumen JJ, Van der Meer NM, Muijsers AO (January 1992). "Subunits VIIa,b,c of human cytochrome c oxidase. Identification of both 'heart-type' and 'liver-type' isoforms of subunit VIIa in human heart". European Journal of Biochemistry. 203 (1–2): 193–9. PMID 1309697.
↑ "6 binary interactions found for search term COX7B". IntAct Molecular Interaction Database. EMBL-EBI. Retrieved 2018-08-25.

External links

Human COX7B genome location and COX7B gene details page in the UCSC Genome Browser.

@@ Line 1: / Line 1: @@
 {{Infobox_gene}}
-'''Cytochrome c oxidase subunit 7B, mitochondrial''' is an [[enzyme]] that in humans is encoded by the ''COX7B'' [[gene]].<ref name="pmid8382530">{{cite journal | vauthors = Sadlock JE, Lightowlers RN, Capaldi RA, Schon EA | title = Isolation of a cDNA specifying subunit VIIb of human cytochrome c oxidase | journal = Biochim Biophys Acta | volume = 1172 | issue = 1–2 | pages = 223–5 |date=Mar 1993 | pmid = 8382530 | pmc =  | doi =  10.1016/0167-4781(93)90301-s}}</ref><ref name="entrez">{{cite web | title = Entrez Gene: COX7B cytochrome c oxidase subunit VIIb| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1349| accessdate = }}</ref>
+'''Cytochrome c oxidase subunit 7B, mitochondrial (COX7B)''' is an [[enzyme]] that in humans is encoded by the ''COX7B'' [[gene]].<ref name="pmid8382530">{{cite journal | vauthors = Sadlock JE, Lightowlers RN, Capaldi RA, Schon EA | title = Isolation of a cDNA specifying subunit VIIb of human cytochrome c oxidase | journal = Biochimica et Biophysica Acta | volume = 1172 | issue = 1–2 | pages = 223–5 | date = February 1993 | pmid = 8382530 | pmc =  | doi = 10.1016/0167-4781(93)90301-s }}</ref> COX7B is a [[Nuclear gene|nuclear]]-encoded subunit of [[cytochrome c oxidase]] (COX). Cytochrome c oxidase ([[Cytochrome c oxidase|complex IV]]) is a multi-subunit enzyme complex that couples the transfer of [[electron]]s from [[cytochrome c]] to molecular [[oxygen]] and contributes to a [[hydronium|proton]] [[electrochemical gradient]] across the [[inner mitochondrial membrane]], acting as the terminal enzyme of the [[Mitochondrion|mitochondrial]] [[electron transport chain|respiratory chain]].<ref name="entrez">{{cite web | title = Entrez Gene: COX7B cytochrome c oxidase subunit VIIb| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1349| access-date = }}{{PD-notice}}</ref> Work with [[Japanese rice fish|Oryzias latices]] has linked disruptions in COX7B with [[microphthalmia]] with linear [[skin lesions]] (MLS), [[microcephaly]], and [[mitochondrial disease]]. Clinically, [[mutation]]s in ''COX7B'' have been associated with linear skin defects with multiple [[congenital anomalies]].<ref name=":0">{{cite journal | vauthors = Indrieri A, van Rahden VA, Tiranti V, Morleo M, Iaconis D, Tammaro R, D'Amato I, Conte I, Maystadt I, Demuth S, Zvulunov A, Kutsche K, Zeviani M, Franco B | title = Mutations in COX7B cause microphthalmia with linear skin lesions, an unconventional mitochondrial disease | journal = American Journal of Human Genetics | volume = 91 | issue = 5 | pages = 942–9 | date = November 2012 | pmid = 23122588 | pmc = 3487127 | doi = 10.1016/j.ajhg.2012.09.016 }}</ref>
-<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
+== Structure ==
-{{PBB Summary
+''COX7B'' is located on the [[Locus (genetics)|q arm]] of the [[X chromosome]] in position 21.1 and has 3 [[exon]]s.<ref name="entrez" /> The ''COX7B'' gene produces a 9.2 kDa [[protein]] composed of 80 [[amino acid]]s.<ref>{{Cite web|url=https://amino.heartproteome.org/web/protein/P24311|title=Cardiac Organellar Protein Atlas Knowledgebase (COPaKB) —— Protein Information|last=Yao|first=Daniel|website=amino.heartproteome.org|access-date=2018-08-06}}</ref><ref>{{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> COX7B is one of the nuclear-encoded polypeptide chains of [[cytochrome c oxidase]] (COX), a [[heteromer]]ic complex consisting of 3 catalytic subunits encoded by [[Mitochondrial DNA|mitochondrial genes]] and multiple structural subunits encoded by [[nuclear gene]]s. The protein encoded by ''COX7B'' belongs to the cytochrome c oxidase VIIb family. ''COX7B'' has a 24 amino acid [[Signal peptide|transit peptide]] domain from positions 1-24, an 8 amino acid topological [[mitochondrial matrix]] domain from positions 25-32, a helical, 27 amino acid [[transmembrane domain]] from positions 33-59, and a 21 amino acid topological [[Mitochondrial intermembrane space|intermembrane]] domain from positions 60-80.<ref name=":1">{{Cite web|url=https://www.uniprot.org/uniprot/P24311|title=COX7B - Cytochrome c oxidase subunit 7B, mitochondrial precursor - Homo sapiens (Human) - COX7B gene & protein|website=uniprot.org|language=en|access-date=2018-08-06}}{{CC-notice|cc=by4}}</ref><ref name=":3">{{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 }}</ref><ref>{{cite journal | vauthors = Van Kuilenburg AB, Van Beeumen JJ, Van der Meer NM, Muijsers AO | title = Subunits VIIa,b,c of human cytochrome c oxidase. Identification of both 'heart-type' and 'liver-type' isoforms of subunit VIIa in human heart | journal = European Journal of Biochemistry | volume = 203 | issue = 1–2 | pages = 193–9 | date = January 1992 | pmid = 1309697 }}</ref><ref name=":0" /> ''COX7B'' may also have several [[pseudogene]]s on chromosomes [[Chromosome 1|1]], [[Chromosome 2|2]], [[Chromosome 20|20]] and [[Chromosome 22|22]].<ref name="entrez" />
-| section_title =
-| summary_text = [[Cytochrome c oxidase]] (COX), the terminal component of the mitochondrial [[respiratory]] chain, catalyzes the electron transfer from reduced [[cytochrome c]] to [[oxygen]]. This component is a heteromeric complex consisting of 3 catalytic subunits encoded by mitochondrial genes and multiple structural subunits encoded by nuclear genes. The mitochondrially-encoded subunits function in electron transfer, and the nuclear-encoded subunits may function in the regulation and assembly of the complex. This nuclear gene encodes subunit VIIb, which is highly similar to bovine COX VIIb protein and is found in all tissues. This gene may have several pseudogenes on chromosomes 1, 2, 20 and 22, respectively.<ref name="entrez" />
-}}
-==References==
+== Function ==
+[[Cytochrome c oxidase]] (COX), the terminal enzyme of the [[mitochondrial respiratory chain]], catalyzes the electron transfer from reduced [[cytochrome c]] to [[oxygen]]. The mitochondrially-encoded subunits of COX function in [[electron transfer]], while the nuclear-encoded subunits may be involved in the regulation and assembly of the complex. The ''COX7B'' nuclear gene encodes subunit 7B, which is located on the [[inner mitochondrial membrane]] in association with several other proteins encompassing the COX complex. It is found in all tissues and has been shown to be highly similar to bovine COX VIIb protein.<ref name="entrez" /> COX7B is believed to be important for COX assembly and activity, the function of [[Electron transport chain|mitochondrial respiratory chain]], and the proper development of the [[central nervous system]] in [[vertebrate]]s.<ref name=":0" /><ref name=":1" /><ref name=":3" />
+== Model organisms ==
+[[Japanese rice fish|Oryzias latices]] (also known as [[Japanese rice fish|medaka]]) is a Japanese rice fish that has been used as a [[model organism]] in COX7B studies. By using a [[morpholino]] knockdown technique, COX7B has been shown to be indispensable for COX assembly, COX activity, and mitochondrial respiration. Additionally, the [[down-regulation]] of an [[ortholog]] of COX7B has suggested that there may be an association between COX7B disfunction and [[microphthalmia]] with linear [[skin lesions]] (MLS), [[microcephaly]], and [[mitochondrial disease]]. Work with Oryzias latices could also indicate an evolutionary conserved role for the mitochondrial respiratory chain complexes in [[central nervous system]] development.<ref name=":0" />
+== Clinical significance ==
+Mutations in ''COX7B'' have been associated with linear skin defects with multiple [[congenital anomalies]]. This disorder is a distinct form of [[aplasia cutis congenita]] presenting as multiple linear skin defects on the face and neck associated with poor growth and [[short stature]], [[microcephaly]], and [[facial dysmorphism]]. Additional clinical features include [[intellectual disability]], [[Nail disease|nail dystrophy]], cardiac abnormalities, [[diaphragmatic hernia]], [[Genitourinary system|genitourinary]] abnormalities, [[Optic disc pallor|pale optic discs]] and altered [[Visual evoked potentials|visual-evoked potentials]], [[agenesis of the corpus callosum]], and other [[central nervous system]] abnormalities.<ref name=":1" /><ref name=":3" /> The ''COX7B'' mutations associated with disease include c.196delC, a [[Zygosity|heterozygous]] mutation leading to a [[Frameshift mutation|frameshift]] in exon 3, c.41-2A>G, a heterozygous [[Splice site mutation|splice mutation]] in a novel acceptor site in [[intron]] 1, and c.55C>T, a heterozygous [[nonsense mutation]] in exon 2. Additionally, experiments with [[Japanese rice fish|Oryzias latices]] suggest ''COX7B'' may be associated with [[microphthalmia]] with linear skin lesions (MLS), an [[X-linked dominant inheritance|X-linked, dominant]], male-lethal [[Mitochondrial disease|mitochondrial disorder]].<ref name=":0" />
+== Interactions ==
+COX7B has been shown to have 6 binary [[Protein–protein interaction|protein-protein interactions]] including 3 co-complex interactions. [[GNMT]], [[MYB (gene)|MYB]], [[Cytochrome c oxidase subunit I|MT-CO1]], HSCB, and [[Citrin|SLC25A13]] have all been found to interact with COX7B.<ref>{{cite web | url = https://www.ebi.ac.uk/intact/interactions?conversationContext=3&query=COX7B | title = 6 binary interactions found for search term COX7B | website = IntAct Molecular Interaction Database | publisher = EMBL-EBI | access-date = 2018-08-25 }}</ref>
+== References ==
 {{reflist}}
-==External links==
+== External links ==
 * {{UCSC gene info|COX7B}}
-==Further reading==
+== Further reading ==
 {{refbegin | 2}}
-{{PBB_Further_reading
+* {{Cite book | vauthors = Lenka N, Vijayasarathy C, Mullick J, Avadhani NG | title = Structural organization and transcription regulation of nuclear genes encoding the mammalian cytochrome c oxidase complex | volume = 61 | issue =  | pages = 309–44 | year = 1998 | pmid = 9752724 | doi = 10.1016/S0079-6603(08)60830-2 | isbn = 978-0-12-540061-9 | series = Progress in Nucleic Acid Research and Molecular Biology }}
-| citations =
+* {{cite journal | vauthors = Stroh A, Kadenbach B | title = Tissue-specific and species-specific distribution of -SH groups in cytochrome c oxidase subunits | journal = European Journal of Biochemistry | volume = 156 | issue = 1 | pages = 199–204 | date = April 1986 | pmid = 3007143 | doi = 10.1111/j.1432-1033.1986.tb09568.x }}
-*{{cite journal  | vauthors=Lenka N, Vijayasarathy C, Mullick J, Avadhani NG |title=Structural organization and transcription regulation of nuclear genes encoding the mammalian cytochrome c oxidase complex |journal=Prog. Nucleic Acid Res. Mol. Biol. |volume=61 |issue=  |pages= 309–44 |year= 1998 |pmid= 9752724 |doi=10.1016/S0079-6603(08)60830-2  | series=Progress in Nucleic Acid Research and Molecular Biology  | isbn=978-0-12-540061-9  }}
+* {{cite journal | vauthors = Possekel S, Marsac C, Kadenbach B | title = Biochemical analysis of fibroblasts from patients with cytochrome c oxidase-associated Leigh syndrome | journal = Biochimica et Biophysica Acta | volume = 1316 | issue = 3 | pages = 153–9 | date = August 1996 | pmid = 8781533 | doi = 10.1016/0925-4439(96)00005-1 }}
-*{{cite journal  | vauthors=Van Kuilenburg AB, Van Beeumen JJ, Van der Meer NM, Muijsers AO |title=Subunits VIIa,b,c of human cytochrome c oxidase. Identification of both 'heart-type' and 'liver-type' isoforms of subunit VIIa in human heart |journal=Eur. J. Biochem. |volume=203 |issue= 1–2 |pages= 193–9 |year= 1992 |pmid= 1309697 |doi=10.1111/j.1432-1033.1992.tb19847.x  }}
+* {{cite journal | vauthors = Nijtmans LG, Taanman JW, Muijsers AO, Speijer D, Van den Bogert C | title = Assembly of cytochrome-c oxidase in cultured human cells | journal = European Journal of Biochemistry | volume = 254 | issue = 2 | pages = 389–94 | date = June 1998 | pmid = 9660196 | doi = 10.1046/j.1432-1327.1998.2540389.x }}
-*{{cite journal  | vauthors=Stroh A, Kadenbach B |title=Tissue-specific and species-specific distribution of -SH groups in cytochrome c oxidase subunits |journal=Eur. J. Biochem. |volume=156 |issue= 1 |pages= 199–204 |year= 1986 |pmid= 3007143 |doi=10.1111/j.1432-1033.1986.tb09568.x  }}
-*{{cite journal  | vauthors=Possekel S, Marsac C, Kadenbach B |title=Biochemical analysis of fibroblasts from patients with cytochrome c oxidase-associated Leigh syndrome |journal=Biochim. Biophys. Acta |volume=1316 |issue= 3 |pages= 153–9 |year= 1996 |pmid= 8781533 |doi=  10.1016/0925-4439(96)00005-1}}
-*{{cite journal  | author=Nijtmans LG |title=Assembly of cytochrome-c oxidase in cultured human cells |journal=Eur. J. Biochem. |volume=254 |issue= 2 |pages= 389–94 |year= 1998 |pmid= 9660196 |doi=10.1046/j.1432-1327.1998.2540389.x  |name-list-format=vanc| author2=Taanman JW  | author3=Muijsers AO  | display-authors=3  | last4=Speijer  | first4=Dave  | last5=Van Den Bogert  | first5=Coby  }}
-*{{cite journal  | author=Strausberg RL |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241  |name-list-format=vanc| author2=Feingold EA  | author3=Grouse LH  | display-authors=3  | last4=Derge  | first4=JG  | last5=Klausner  | first5=RD  | last6=Collins  | first6=FS  | last7=Wagner  | first7=L  | last8=Shenmen  | first8=CM  | last9=Schuler  | first9=GD }}
-*{{cite journal  | author=Gerhard DS |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504  | pmc=528928  |name-list-format=vanc| author2=Wagner L  | author3=Feingold EA  | display-authors=3  | last4=Shenmen  | first4=CM  | last5=Grouse  | first5=LH  | last6=Schuler  | first6=G  | last7=Klein  | first7=SL  | last8=Old  | first8=S  | last9=Rasooly  | first9=R }}
-*{{cite journal  | author=Ross MT |title=The DNA sequence of the human X chromosome |journal=Nature |volume=434 |issue= 7031 |pages= 325–37 |year= 2005 |pmid= 15772651 |doi= 10.1038/nature03440  | pmc=2665286  |name-list-format=vanc| author2=Grafham DV  | author3=Coffey AJ  | display-authors=3  | last4=Scherer  | first4=Steven  | last5=McLay  | first5=Kirsten  | last6=Muzny  | first6=Donna  | last7=Platzer  | first7=Matthias  | last8=Howell  | first8=Gareth R.  | last9=Burrows  | first9=Christine }}
-}}
 {{refend}}
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