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{{Technical|date=October 2010}}
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{{Infobox_gene}}
| require_manual_inspection = no
'''Cytochrome c oxidase copper chaperone''' is a [[protein]] that in humans is encoded by the ''COX17'' [[gene]].<ref name="pmid9050918">{{cite journal | vauthors = Amaravadi R, Glerum DM, Tzagoloff A | title = Isolation of a cDNA encoding the human homolog of COX17, a yeast gene essential for mitochondrial copper recruitment | journal = Hum Genet | volume = 99 | issue = 3 | pages = 329–33 |date=Mar 1997 | pmid = 9050918 | pmc =  | doi =10.1007/s004390050367  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: COX17 COX17 cytochrome c oxidase assembly homolog (S. cerevisiae)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10063| accessdate = }}</ref>
| update_protein_box = 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 = COX17 cytochrome c oxidase assembly homolog (S. cerevisiae)
| HGNCid = 2264
| Symbol = COX17
| AltSymbols =; MGC104397; MGC117386
| OMIM = 604813
| ECnumber = 
| Homologene = 38089
| MGIid = 1333806
| GeneAtlas_image1 = PBB_GE_COX17_203880_at_tn.png
| Function = {{GNF_GO|id=GO:0005507 |text = copper ion binding}} {{GNF_GO|id=GO:0016531 |text = copper chaperone activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005758 |text = mitochondrial intermembrane space}}
| Process = {{GNF_GO|id=GO:0006091 |text = generation of precursor metabolites and energy}} {{GNF_GO|id=GO:0006457 |text = protein folding}} {{GNF_GO|id=GO:0006825 |text = copper ion transport}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 10063
    | Hs_Ensembl = ENSG00000138495
    | Hs_RefseqProtein = NP_005685
    | Hs_RefseqmRNA = NM_005694
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 3
    | Hs_GenLoc_start = 120871062
    | Hs_GenLoc_end = 120878933
    | Hs_Uniprot = Q14061
    | Mm_EntrezGene = 12856
    | Mm_Ensembl = ENSMUSG00000046516
    | Mm_RefseqmRNA = NM_001017429
    | Mm_RefseqProtein = NP_001017429
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 16
    | Mm_GenLoc_start = 38266238
    | Mm_GenLoc_end = 38272002
    | Mm_Uniprot = Q3UJM3
  }}
}}
'''COX17 cytochrome c oxidase assembly homolog (S. cerevisiae)''', also known as '''COX17''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: COX17 COX17 cytochrome c oxidase assembly homolog (S. cerevisiae)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10063| 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 component of the [[electron transport chain|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 a protein which is not a structural subunit, but may be involved in the recruitment of copper to mitochondria for incorporation into the COX [[Enzyme#Cofactors|apoenzyme]]. This protein shares 92% amino acid sequence identity with mouse and rat Cox17 proteins. This gene is no longer considered to be a candidate gene for COX deficiency. A pseudogene COX17P has been found on chromosome 13.<ref name="entrez"/>
{{PBB_Summary
| 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 a protein which is not a structural subunit, but may be involved in the recruitment of copper to mitochondria for incorporation into the COX apoenzyme. This protein shares 92% amino acid sequence identity with mouse and rat Cox17 proteins. This gene is no longer considered to be a candidate gene for COX deficiency. A pseudogene COX17P has been found on chromosome 13.<ref name="entrez">{{cite web | title = Entrez Gene: COX17 COX17 cytochrome c oxidase assembly homolog (S. cerevisiae)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10063| accessdate = }}</ref>
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Amaravadi R, Glerum DM, Tzagoloff A |title=Isolation of a cDNA encoding the human homolog of COX17, a yeast gene essential for mitochondrial copper recruitment. |journal=Hum. Genet. |volume=99 |issue= 3 |pages= 329-33 |year= 1997 |pmid= 9050918 |doi=  }}
*{{cite journal  | vauthors=Punter FA, Adams DL, Glerum DM |title=Characterization and localization of human COX17, a gene involved in mitochondrial copper transport. |journal=Hum. Genet. |volume=107 |issue= 1 |pages= 69–74 |year= 2000 |pmid= 10982038 |doi=10.1007/s004390050013 }}
*{{cite journal  | author=Punter FA, Adams DL, Glerum DM |title=Characterization and localization of human COX17, a gene involved in mitochondrial copper transport. |journal=Hum. Genet. |volume=107 |issue= 1 |pages= 69-74 |year= 2000 |pmid= 10982038 |doi= }}
*{{cite journal  | author=Horvath R |title=Characterization of human SCO1 and COX17 genes in mitochondrial cytochrome-c-oxidase deficiency |journal=Biochem. Biophys. Res. Commun. |volume=276 |issue= 2 |pages= 530–3 |year= 2000 |pmid= 11027508 |doi= 10.1006/bbrc.2000.3495 |name-list-format=vanc| author2=Lochmüller H | author3=Stucka R | display-authors=3  | last4=Yao  | first4=J  | last5=Shoubridge  | first5=EA  | last6=Kim  | first6=SH  | last7=Gerbitz  | first7=KD  | last8=Jaksch  | first8=M }}
*{{cite journal | author=Horvath R, Lochmüller H, Stucka R, ''et al.'' |title=Characterization of human SCO1 and COX17 genes in mitochondrial cytochrome-c-oxidase deficiency. |journal=Biochem. Biophys. Res. Commun. |volume=276 |issue= 2 |pages= 530-3 |year= 2000 |pmid= 11027508 |doi= 10.1006/bbrc.2000.3495 }}
*{{cite journal  | author=Kako K |title=The expression of Cox17p in rodent tissues and cells |journal=Eur. J. Biochem. |volume=267 |issue= 22 |pages= 6699–707 |year= 2000 |pmid= 11054125 |doi=10.1046/j.1432-1327.2000.01771.x |name-list-format=vanc| author2=Tsumori K  | author3=Ohmasa Y  | display-authors=3  | last4=Takahashi  | first4=Yoshinori  | last5=Munekata  | first5=Eisuke }}
*{{cite journal  | author=Kako K, Tsumori K, Ohmasa Y, ''et al.'' |title=The expression of Cox17p in rodent tissues and cells. |journal=Eur. J. Biochem. |volume=267 |issue= 22 |pages= 6699-707 |year= 2000 |pmid= 11054125 |doi= }}
*{{cite journal  | vauthors=Heaton DN, George GN, Garrison G, Winge DR |title=The mitochondrial copper metallochaperone Cox17 exists as an oligomeric, polycopper complex |journal=Biochemistry |volume=40 |issue= 3 |pages= 743–51 |year= 2001 |pmid= 11170391 |doi=10.1021/bi002315x  }}
*{{cite journal | author=Heaton DN, George GN, Garrison G, Winge DR |title=The mitochondrial copper metallochaperone Cox17 exists as an oligomeric, polycopper complex. |journal=Biochemistry |volume=40 |issue= 3 |pages= 743-51 |year= 2001 |pmid= 11170391 |doi=  }}
*{{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=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=Suzuki C |title=Identification of COX17 as a therapeutic target for non-small cell lung cancer |journal=Cancer Res. |volume=63 |issue= 21 |pages= 7038–41 |year= 2004 |pmid= 14612491 |doi=  |name-list-format=vanc| author2=Daigo Y  | author3=Kikuchi T  | display-authors=3  | last4=Katagiri  | first4=T  | last5=Nakamura  | first5=Y  }}
*{{cite journal  | author=Suzuki C, Daigo Y, Kikuchi T, ''et al.'' |title=Identification of COX17 as a therapeutic target for non-small cell lung cancer. |journal=Cancer Res. |volume=63 |issue= 21 |pages= 7038-41 |year= 2004 |pmid= 14612491 |doi= }}
*{{cite journal  | author=Ota T |title=Complete sequencing and characterization of 21,243 full-length human cDNAs |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 |name-list-format=vanc| author2=Suzuki Y  | author3=Nishikawa T  | display-authors=3  | last4=Otsuki  | first4=Tetsuji  | last5=Sugiyama  | first5=Tomoyasu  | last6=Irie  | first6=Ryotaro  | last7=Wakamatsu | first7=Ai  | last8=Hayashi  | first8=Koji  | last9=Sato  | first9=Hiroyuki }}
*{{cite journal | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{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=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=Kako K |title=A selective requirement for copper-dependent activation of cytochrome c oxidase by Cox17p |journal=Biochem. Biophys. Res. Commun. |volume=324 |issue= 4 |pages= 1379–85 |year= 2005 |pmid= 15504366 |doi= 10.1016/j.bbrc.2004.09.211 |name-list-format=vanc| author2=Takehara A | author3=Arai H  | display-authors=3  | last4=Onodera  | first4=T  | last5=Takahashi  | first5=Y  | last6=Hanagata  | first6=H  | last7=Ogra  | first7=Y  | last8=Takagi  | first8=H  | last9=Kodama  | first9=H }}
*{{cite journal | author=Kako K, Takehara A, Arai H, ''et al.'' |title=A selective requirement for copper-dependent activation of cytochrome c oxidase by Cox17p. |journal=Biochem. Biophys. Res. Commun. |volume=324 |issue= 4 |pages= 1379-85 |year= 2005 |pmid= 15504366 |doi= 10.1016/j.bbrc.2004.09.211 }}
*{{cite journal  | author=Arnesano F |title=Folding studies of Cox17 reveal an important interplay of cysteine oxidation and copper binding |journal=Structure |volume=13 |issue= 5 |pages= 713–22 |year= 2005 |pmid= 15893662 |doi= 10.1016/j.str.2005.02.015  |name-list-format=vanc| author2=Balatri E  | author3=Banci L  | display-authors=3  | last4=Bertini  | first4=Ivano  | last5=Winge  | first5=Dennis R. }}
*{{cite journal  | author=Arnesano F, Balatri E, Banci L, ''et al.'' |title=Folding studies of Cox17 reveal an important interplay of cysteine oxidation and copper binding. |journal=Structure |volume=13 |issue= 5 |pages= 713-22 |year= 2005 |pmid= 15893662 |doi= 10.1016/j.str.2005.02.015 }}
*{{cite journal  | author=Stelzl U |title=A human protein-protein interaction network: a resource for annotating the proteome |journal=Cell |volume=122 |issue= 6 |pages= 957–68 |year= 2005 |pmid= 16169070 |doi= 10.1016/j.cell.2005.08.029  |name-list-format=vanc| author2=Worm U  | author3=Lalowski M  | display-authors=3  | last4=Haenig  | first4=Christian  | last5=Brembeck  | first5=Felix H.  | last6=Goehler  | first6=Heike  | last7=Stroedicke  | first7=Martin  | last8=Zenkner  | first8=Martina  | last9=Schoenherr  | first9=Anke }}
*{{cite journal | author=Stelzl U, Worm U, Lalowski M, ''et al.'' |title=A human protein-protein interaction network: a resource for annotating the proteome. |journal=Cell |volume=122 |issue= 6 |pages= 957-68 |year= 2005 |pmid= 16169070 |doi= 10.1016/j.cell.2005.08.029 }}
*{{cite journal  | author=Rual JF |title=Towards a proteome-scale map of the human protein-protein interaction network |journal=Nature |volume=437 |issue= 7062 |pages= 1173–8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209  |name-list-format=vanc| author2=Venkatesan K  | author3=Hao T  | display-authors=3  | last4=Hirozane-Kishikawa  | first4=Tomoko  | last5=Dricot  | first5=Amélie  | last6=Li  | first6=Ning  | last7=Berriz  | first7=Gabriel F.  | last8=Gibbons  | first8=Francis D.  | last9=Dreze  | first9=Matija }}
*{{cite journal | author=Rual JF, Venkatesan K, Hao T, ''et al.'' |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173-8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 }}
*{{cite journal  | author=Cobine PA |title=The P174L mutation in human Sco1 severely compromises Cox17-dependent metallation but does not impair copper binding |journal=J. Biol. Chem. |volume=281 |issue= 18 |pages= 12270–6 |year= 2006 |pmid= 16520371 |doi= 10.1074/jbc.M600496200  |name-list-format=vanc| author2=Pierrel F  | author3=Leary SC  | display-authors=3  | last4=Sasarman  | first4=F  | last5=Horng  | first5=YC  | last6=Shoubridge  | first6=EA  | last7=Winge  | first7=DR }}
*{{cite journal | author=Cobine PA, Pierrel F, Leary SC, ''et al.'' |title=The P174L mutation in human Sco1 severely compromises Cox17-dependent metallation but does not impair copper binding. |journal=J. Biol. Chem. |volume=281 |issue= 18 |pages= 12270-6 |year= 2006 |pmid= 16520371 |doi= 10.1074/jbc.M600496200 }}
*{{cite journal  | author=Ma J |title=Identifying leukocyte gene expression patterns associated with plasma lipid levels in human subjects |journal=Atherosclerosis |volume=191 |issue= 1 |pages= 63–72 |year= 2007 |pmid= 16806233 |doi= 10.1016/j.atherosclerosis.2006.05.032  |name-list-format=vanc| author2=Dempsey AA  | author3=Stamatiou D  | display-authors=3  | last4=Marshall  | first4=K  | last5=Liew  | first5=C }}
*{{cite journal  | author=Ma J, Dempsey AA, Stamatiou D, ''et al.'' |title=Identifying leukocyte gene expression patterns associated with plasma lipid levels in human subjects. |journal=Atherosclerosis |volume=191 |issue= 1 |pages= 63-72 |year= 2007 |pmid= 16806233 |doi= 10.1016/j.atherosclerosis.2006.05.032 }}
*{{cite journal  | author=Voronova A |title=Cox17, a copper chaperone for cytochrome c oxidase: expression, purification, and formation of mixed disulphide adducts with thiol reagents |journal=Protein Expr. Purif. |volume=53 |issue= 1 |pages= 138–44 |year= 2007 |pmid= 17208454 |doi= 10.1016/j.pep.2006.11.014  |name-list-format=vanc| author2=Kazantseva J  | author3=Tuuling M  | display-authors=3  | last4=Sokolova  | first4=Niina  | last5=Sillard  | first5=Rannar  | last6=Palumaa  | first6=Peep }}
*{{cite journal | author=Voronova A, Kazantseva J, Tuuling M, ''et al.'' |title=Cox17, a copper chaperone for cytochrome c oxidase: expression, purification, and formation of mixed disulphide adducts with thiol reagents. |journal=Protein Expr. Purif. |volume=53 |issue= 1 |pages= 138-44 |year= 2007 |pmid= 17208454 |doi= 10.1016/j.pep.2006.11.014 }}
*{{cite journal  | author=Voronova A |title=Oxidative switches in functioning of mammalian copper chaperone Cox17 |journal=Biochem. J. |volume=408 |issue= 1 |pages= 139–48 |year= 2007 |pmid= 17672825 |doi= 10.1042/BJ20070804 | pmc=2049083  |name-list-format=vanc| author2=Meyer-Klaucke W  | author3=Meyer T  | display-authors=3  | last4=Rompel  | first4=Annette  | last5=Krebs  | first5=Bernt  | last6=Kazantseva  | first6=Jekaterina  | last7=Sillard  | first7=Rannar  | last8=Palumaa  | first8=Peep }}
*{{cite journal  | author=Voronova A, Meyer-Klaucke W, Meyer T, ''et al.'' |title=Oxidative switches in functioning of mammalian copper chaperone Cox17. |journal=Biochem. J. |volume=408 |issue= 1 |pages= 139-48 |year= 2007 |pmid= 17672825 |doi= 10.1042/BJ20070804 }}
}}
}}
{{refend}}
{{refend}}


{{protein-stub}}
==External links==
{{WikiDoc Sources}}
* {{UCSC genome browser|COX17}}
* {{UCSC gene details|COX17}}
 
 
{{gene-3-stub}}

Latest revision as of 09:57, 30 August 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 copper chaperone is a protein that in humans is encoded by the COX17 gene.[1][2]

Function

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 a protein which is not a structural subunit, but may be involved in the recruitment of copper to mitochondria for incorporation into the COX apoenzyme. This protein shares 92% amino acid sequence identity with mouse and rat Cox17 proteins. This gene is no longer considered to be a candidate gene for COX deficiency. A pseudogene COX17P has been found on chromosome 13.[2]

References

  1. ↑ Amaravadi R, Glerum DM, Tzagoloff A (Mar 1997). "Isolation of a cDNA encoding the human homolog of COX17, a yeast gene essential for mitochondrial copper recruitment". Hum Genet. 99 (3): 329–33. doi:10.1007/s004390050367. PMID 9050918.
  2. ↑ 2.0 2.1 "Entrez Gene: COX17 COX17 cytochrome c oxidase assembly homolog (S. cerevisiae)".

Further reading

External links


Retrieved from "https://www.wikidoc.org/index.php?title=COX17&oldid=1413515"