COX4I2: Difference between revisions

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{{Infobox_gene}}
{{PBB_Controls
'''Cytochrome c oxidase subunit 4 isoform 2, mitochondrial''' is an [[enzyme]] that in humans is encoded by the ''COX4I2'' [[gene]].<ref name="pmid11311561">{{cite journal | vauthors = Hüttemann M, Kadenbach B, Grossman LI | title = Mammalian subunit IV isoforms of cytochrome c oxidase | journal = Gene | volume = 267 | issue = 1 | pages = 111–23 | date = Apr 2001 | pmid = 11311561 | pmc =  | doi = 10.1016/S0378-1119(01)00385-7 }}</ref><ref name="pmid17937768">{{cite journal | vauthors = Hüttemann M, Lee I, Liu J, Grossman LI | title = Transcription of mammalian cytochrome c oxidase subunit IV-2 is controlled by a novel conserved oxygen responsive element | journal = The FEBS Journal | volume = 274 | issue = 21 | pages = 5737–48 | date = Nov 2007 | pmid = 17937768 | pmc = | doi = 10.1111/j.1742-4658.2007.06093.x }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: COX4I2 cytochrome c oxidase subunit IV isoform 2 (lung)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=84701| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Cytochrome c oxidase subunit IV isoform 2 (lung)
| HGNCid = 16232
| Symbol = COX4I2
| AltSymbols =; COX4; COX4-2; COX4B; COX4L2; COXIV-2; dJ857M17.2
| OMIM = 607976
| ECnumber = 
| Homologene = 13082
| MGIid = 2135755
| GeneAtlas_image1 = PBB_GE_COX4I2_gnf1h00848_at_tn.png
| Function = {{GNF_GO|id=GO:0004129 |text = cytochrome-c oxidase activity}} {{GNF_GO|id=GO:0016491 |text = oxidoreductase activity}}
| Component = {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005751 |text = mitochondrial respiratory chain complex IV}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006118 |text = electron transport}} {{GNF_GO|id=GO:0045333 |text = cellular respiration}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 84701
    | Hs_Ensembl = ENSG00000131055
    | Hs_RefseqProtein = NP_115998
    | Hs_RefseqmRNA = NM_032609
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 20
    | Hs_GenLoc_start = 29689352
    | Hs_GenLoc_end = 29696470
    | Hs_Uniprot = Q96KJ9
    | Mm_EntrezGene = 84682
    | Mm_Ensembl = ENSMUSG00000009876
    | Mm_RefseqmRNA = NM_053091
    | Mm_RefseqProtein = NP_444321
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 2
    | Mm_GenLoc_start = 152446596
    | Mm_GenLoc_end = 152456322
    | Mm_Uniprot = Q91W29
  }}
}}
'''Cytochrome c oxidase subunit IV isoform 2 (lung)''', also known as '''COX4I2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: COX4I2 cytochrome c oxidase subunit IV isoform 2 (lung)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=84701| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
[[Cytochrome c oxidase]] (COX), the terminal enzyme of the [[mitochondrial respiratory chain]], catalyzes the electron transfer from reduced cytochrome c to oxygen. It 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 be involved in the regulation and assembly of the complex. This nuclear gene encodes isoform 2 of subunit IV. Isoform 1 of subunit IV is encoded by a different gene, however, the two genes show a similar structural organization. Subunit IV is the largest nuclear encoded subunit which plays a pivotal role in COX regulation.<ref name="entrez" />
{{PBB_Summary
| section_title =
| summary_text = Cytochrome c oxidase (COX), the terminal enzyme of the mitochondrial respiratory chain, catalyzes the electron transfer from reduced cytochrome c to oxygen. It 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 be involved in the regulation and assembly of the complex. This nuclear gene encodes isoform 2 of subunit IV. Isoform 1 of subunit IV is encoded by a different gene, however, the two genes show a similar structural organization. Subunit IV is the largest nuclear encoded subunit which plays a pivotal role in COX regulation.<ref name="entrez">{{cite web | title = Entrez Gene: COX4I2 cytochrome c oxidase subunit IV isoform 2 (lung)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=84701| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
 
==Further reading==
COX4I2 has been shown to [[Protein-protein interaction|interact]] with [[Cytochrome c]].<ref name=pmid6088481>{{cite journal | vauthors = Michel B, Bosshard HR | title = Spectroscopic analysis of the interaction between cytochrome c and cytochrome c oxidase | journal = The Journal of Biological Chemistry | volume = 259 | issue = 16 | pages = 10085–91 | date = Aug 1984 | pmid = 6088481 }}</ref><ref name=pmid10683230>{{cite journal | vauthors = Wiedemann FR, Vielhaber S, Schröder R, Elger CE, Kunz WS | title = Evaluation of methods for the determination of mitochondrial respiratory chain enzyme activities in human skeletal muscle samples | journal = Analytical Biochemistry | volume = 279 | issue = 1 | pages = 55–60 | date = Mar 2000 | pmid = 10683230 | doi = 10.1006/abio.1999.4434 }}</ref><ref name=pmid11737208>{{cite journal | vauthors = Sampson V, Alleyne T | title = Cytochrome c/cytochrome c oxidase interaction. Direct structural evidence for conformational changes during enzyme turnover | journal = European Journal of Biochemistry / FEBS | volume = 268 | issue = 24 | pages = 6534–44 | date = Dec 2001 | pmid = 11737208 | doi = 10.1046/j.0014-2956.2001.02608.x }}</ref><ref name=pmid1309738>{{cite journal | vauthors = Lynch SR, Sherman D, Copeland RA | title = Cytochrome c binding affects the conformation of cytochrome a in cytochrome c oxidase | journal = The Journal of Biological Chemistry | volume = 267 | issue = 1 | pages = 298–302 | date = Jan 1992 | pmid = 1309738 }}</ref>
 
== References ==
{{reflist}}
 
==External links==
* {{UCSC gene info|COX4I2}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Lynch SR, Sherman D, Copeland RA | title = Cytochrome c binding affects the conformation of cytochrome a in cytochrome c oxidase | journal = The Journal of Biological Chemistry | volume = 267 | issue = 1 | pages = 298–302 | date = Jan 1992 | pmid = 1309738 | doi =  }}
| citations =
* {{cite journal | vauthors = Garber EA, Margoliash E | title = Interaction of cytochrome c with cytochrome c oxidase: an understanding of the high- to low-affinity transition | journal = Biochimica et Biophysica Acta | volume = 1015 | issue = 2 | pages = 279–87 | date = Feb 1990 | pmid = 2153405 | doi = 10.1016/0005-2728(90)90032-Y }}
*{{cite journal | author=Lynch SR, Sherman D, Copeland RA |title=Cytochrome c binding affects the conformation of cytochrome a in cytochrome c oxidase. |journal=J. Biol. Chem. |volume=267 |issue= 1 |pages= 298-302 |year= 1992 |pmid= 1309738 |doi=  }}
* {{cite journal | vauthors = Bolli R, Nałecz KA, Azzi A | title = The interconversion between monomeric and dimeric bovine heart cytochrome c oxidase | journal = Biochimie | volume = 67 | issue = 1 | pages = 119–28 | date = Jan 1985 | pmid = 2986725 | doi = 10.1016/S0300-9084(85)80237-6 }}
*{{cite journal | author=Garber EA, Margoliash E |title=Interaction of cytochrome c with cytochrome c oxidase: an understanding of the high- to low-affinity transition. |journal=Biochim. Biophys. Acta |volume=1015 |issue= 2 |pages= 279-87 |year= 1990 |pmid= 2153405 |doi= }}
* {{cite journal | vauthors = Michel B, Bosshard HR | title = Spectroscopic analysis of the interaction between cytochrome c and cytochrome c oxidase | journal = The Journal of Biological Chemistry | volume = 259 | issue = 16 | pages = 10085–91 | date = Aug 1984 | pmid = 6088481 | doi =  }}
*{{cite journal | author=Bolli R, Nałecz KA, Azzi A |title=The interconversion between monomeric and dimeric bovine heart cytochrome c oxidase. |journal=Biochimie |volume=67 |issue= 1 |pages= 119-28 |year= 1985 |pmid= 2986725 |doi= }}
* {{cite journal | vauthors = Hare JF, Ching E, Attardi G | title = Isolation, subunit composition, and site of synthesis of human cytochrome c oxidase | journal = Biochemistry | volume = 19 | issue = 10 | pages = 2023–30 | date = May 1980 | pmid = 6246917 | doi = 10.1021/bi00551a003 }}
*{{cite journal | author=Michel B, Bosshard HR |title=Spectroscopic analysis of the interaction between cytochrome c and cytochrome c oxidase. |journal=J. Biol. Chem. |volume=259 |issue= 16 |pages= 10085-91 |year= 1984 |pmid= 6088481 |doi=  }}
* {{cite journal | vauthors = Papadopoulou LC, Tsiftsoglou AS | title = Effects of hemin on apoptosis, suppression of cytochrome c oxidase gene expression, and bone-marrow toxicity induced by doxorubicin (adriamycin) | journal = Biochemical Pharmacology | volume = 52 | issue = 5 | pages = 713–22 | date = Sep 1996 | pmid = 8765469 | doi = 10.1016/0006-2952(96)00349-8 }}
*{{cite journal | author=Hare JF, Ching E, Attardi G |title=Isolation, subunit composition, and site of synthesis of human cytochrome c oxidase. |journal=Biochemistry |volume=19 |issue= 10 |pages= 2023-30 |year= 1980 |pmid= 6246917 |doi= }}
* {{cite journal | vauthors = Wiedemann FR, Vielhaber S, Schröder R, Elger CE, Kunz WS | title = Evaluation of methods for the determination of mitochondrial respiratory chain enzyme activities in human skeletal muscle samples | journal = Analytical Biochemistry | volume = 279 | issue = 1 | pages = 55–60 | date = Mar 2000 | pmid = 10683230 | doi = 10.1006/abio.1999.4434 }}
*{{cite journal | author=Papadopoulou LC, Tsiftsoglou AS |title=Effects of hemin on apoptosis, suppression of cytochrome c oxidase gene expression, and bone-marrow toxicity induced by doxorubicin (adriamycin). |journal=Biochem. Pharmacol. |volume=52 |issue= 5 |pages= 713-22 |year= 1996 |pmid= 8765469 |doi= }}
* {{cite journal | vauthors = Sampson V, Alleyne T | title = Cytochrome c/cytochrome c oxidase interaction. Direct structural evidence for conformational changes during enzyme turnover | journal = European Journal of Biochemistry / FEBS | volume = 268 | issue = 24 | pages = 6534–44 | date = Dec 2001 | pmid = 11737208 | doi = 10.1046/j.0014-2956.2001.02608.x }}
*{{cite journal | author=Wiedemann FR, Vielhaber S, Schröder R, ''et al.'' |title=Evaluation of methods for the determination of mitochondrial respiratory chain enzyme activities in human skeletal muscle samples. |journal=Anal. Biochem. |volume=279 |issue= 1 |pages= 55-60 |year= 2000 |pmid= 10683230 |doi= 10.1006/abio.1999.4434 }}
* {{cite journal | vauthors = Vizirianakis IS, Pappas IS, Tsiftsoglou AS | title = Differentiation-dependent repression of c-myc, B22, COX II and COX IV genes in murine erythroleukemia (MEL) cells | journal = Biochemical Pharmacology | volume = 63 | issue = 5 | pages = 1009–17 | date = Mar 2002 | pmid = 11911854 | doi = 10.1016/S0006-2952(01)00937-6 }}
*{{cite journal | author=Hüttemann M, Kadenbach B, Grossman LI |title=Mammalian subunit IV isoforms of cytochrome c oxidase. |journal=Gene |volume=267 |issue= 1 |pages= 111-23 |year= 2001 |pmid= 11311561 |doi=  }}
* {{cite journal | vauthors = Fukuda R, Zhang H, Kim JW, Shimoda L, Dang CV, Semenza GL | title = HIF-1 regulates cytochrome oxidase subunits to optimize efficiency of respiration in hypoxic cells | journal = Cell | volume = 129 | issue = 1 | pages = 111–22 | date = Apr 2007 | pmid = 17418790 | doi = 10.1016/j.cell.2007.01.047 }}
*{{cite journal  | author=Sampson V, Alleyne T |title=Cytochrome c/cytochrome c oxidase interaction. Direct structural evidence for conformational changes during enzyme turnover. |journal=Eur. J. Biochem. |volume=268 |issue= 24 |pages= 6534-44 |year= 2002 |pmid= 11737208 |doi= }}
*{{cite journal  | author=Deloukas P, Matthews LH, Ashurst J, ''et al.'' |title=The DNA sequence and comparative analysis of human chromosome 20. |journal=Nature |volume=414 |issue= 6866 |pages= 865-71 |year= 2002 |pmid= 11780052 |doi= 10.1038/414865a }}
*{{cite journal | author=Vizirianakis IS, Pappas IS, Tsiftsoglou AS |title=Differentiation-dependent repression of c-myc, B22, COX II and COX IV genes in murine erythroleukemia (MEL) cells. |journal=Biochem. Pharmacol. |volume=63 |issue= 5 |pages= 1009-17 |year= 2002 |pmid= 11911854 |doi=  }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |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 }}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |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 }}
*{{cite journal | author=Fukuda R, Zhang H, Kim JW, ''et al.'' |title=HIF-1 regulates cytochrome oxidase subunits to optimize efficiency of respiration in hypoxic cells. |journal=Cell |volume=129 |issue= 1 |pages= 111-22 |year= 2007 |pmid= 17418790 |doi= 10.1016/j.cell.2007.01.047 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
 
{{WikiDoc Sources}}
{{gene-20-stub}}

Revision as of 02:30, 27 October 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Cytochrome c oxidase subunit 4 isoform 2, mitochondrial is an enzyme that in humans is encoded by the COX4I2 gene.[1][2][3]

Function

Cytochrome c oxidase (COX), the terminal enzyme of the mitochondrial respiratory chain, catalyzes the electron transfer from reduced cytochrome c to oxygen. It 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 be involved in the regulation and assembly of the complex. This nuclear gene encodes isoform 2 of subunit IV. Isoform 1 of subunit IV is encoded by a different gene, however, the two genes show a similar structural organization. Subunit IV is the largest nuclear encoded subunit which plays a pivotal role in COX regulation.[3]

Interactions

COX4I2 has been shown to interact with Cytochrome c.[4][5][6][7]

References

  1. ↑ Hüttemann M, Kadenbach B, Grossman LI (Apr 2001). "Mammalian subunit IV isoforms of cytochrome c oxidase". Gene. 267 (1): 111–23. doi:10.1016/S0378-1119(01)00385-7. PMID 11311561.
  2. ↑ Hüttemann M, Lee I, Liu J, Grossman LI (Nov 2007). "Transcription of mammalian cytochrome c oxidase subunit IV-2 is controlled by a novel conserved oxygen responsive element". The FEBS Journal. 274 (21): 5737–48. doi:10.1111/j.1742-4658.2007.06093.x. PMID 17937768.
  3. ↑ 3.0 3.1 "Entrez Gene: COX4I2 cytochrome c oxidase subunit IV isoform 2 (lung)".
  4. ↑ Michel B, Bosshard HR (Aug 1984). "Spectroscopic analysis of the interaction between cytochrome c and cytochrome c oxidase". The Journal of Biological Chemistry. 259 (16): 10085–91. PMID 6088481.
  5. ↑ Wiedemann FR, Vielhaber S, Schröder R, Elger CE, Kunz WS (Mar 2000). "Evaluation of methods for the determination of mitochondrial respiratory chain enzyme activities in human skeletal muscle samples". Analytical Biochemistry. 279 (1): 55–60. doi:10.1006/abio.1999.4434. PMID 10683230.
  6. ↑ Sampson V, Alleyne T (Dec 2001). "Cytochrome c/cytochrome c oxidase interaction. Direct structural evidence for conformational changes during enzyme turnover". European Journal of Biochemistry / FEBS. 268 (24): 6534–44. doi:10.1046/j.0014-2956.2001.02608.x. PMID 11737208.
  7. ↑ Lynch SR, Sherman D, Copeland RA (Jan 1992). "Cytochrome c binding affects the conformation of cytochrome a in cytochrome c oxidase". The Journal of Biological Chemistry. 267 (1): 298–302. PMID 1309738.

External links

Further reading

  • Lynch SR, Sherman D, Copeland RA (Jan 1992). "Cytochrome c binding affects the conformation of cytochrome a in cytochrome c oxidase". The Journal of Biological Chemistry. 267 (1): 298–302. PMID 1309738.
  • Garber EA, Margoliash E (Feb 1990). "Interaction of cytochrome c with cytochrome c oxidase: an understanding of the high- to low-affinity transition". Biochimica et Biophysica Acta. 1015 (2): 279–87. doi:10.1016/0005-2728(90)90032-Y. PMID 2153405.
  • Bolli R, Nałecz KA, Azzi A (Jan 1985). "The interconversion between monomeric and dimeric bovine heart cytochrome c oxidase". Biochimie. 67 (1): 119–28. doi:10.1016/S0300-9084(85)80237-6. PMID 2986725.
  • Michel B, Bosshard HR (Aug 1984). "Spectroscopic analysis of the interaction between cytochrome c and cytochrome c oxidase". The Journal of Biological Chemistry. 259 (16): 10085–91. PMID 6088481.
  • Hare JF, Ching E, Attardi G (May 1980). "Isolation, subunit composition, and site of synthesis of human cytochrome c oxidase". Biochemistry. 19 (10): 2023–30. doi:10.1021/bi00551a003. PMID 6246917.
  • Papadopoulou LC, Tsiftsoglou AS (Sep 1996). "Effects of hemin on apoptosis, suppression of cytochrome c oxidase gene expression, and bone-marrow toxicity induced by doxorubicin (adriamycin)". Biochemical Pharmacology. 52 (5): 713–22. doi:10.1016/0006-2952(96)00349-8. PMID 8765469.
  • Wiedemann FR, Vielhaber S, Schröder R, Elger CE, Kunz WS (Mar 2000). "Evaluation of methods for the determination of mitochondrial respiratory chain enzyme activities in human skeletal muscle samples". Analytical Biochemistry. 279 (1): 55–60. doi:10.1006/abio.1999.4434. PMID 10683230.
  • Sampson V, Alleyne T (Dec 2001). "Cytochrome c/cytochrome c oxidase interaction. Direct structural evidence for conformational changes during enzyme turnover". European Journal of Biochemistry / FEBS. 268 (24): 6534–44. doi:10.1046/j.0014-2956.2001.02608.x. PMID 11737208.
  • Vizirianakis IS, Pappas IS, Tsiftsoglou AS (Mar 2002). "Differentiation-dependent repression of c-myc, B22, COX II and COX IV genes in murine erythroleukemia (MEL) cells". Biochemical Pharmacology. 63 (5): 1009–17. doi:10.1016/S0006-2952(01)00937-6. PMID 11911854.
  • Fukuda R, Zhang H, Kim JW, Shimoda L, Dang CV, Semenza GL (Apr 2007). "HIF-1 regulates cytochrome oxidase subunits to optimize efficiency of respiration in hypoxic cells". Cell. 129 (1): 111–22. doi:10.1016/j.cell.2007.01.047. PMID 17418790.


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