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'''ATP synthase lipid-binding protein, mitochondrial''' is an [[enzyme]] that in humans is encoded by the ''ATP5G2'' [[gene]].<ref name="pmid8328972">{{cite journal | vauthors = Dyer MR, Walker JE | title = Sequences of members of the human gene family for the c subunit of mitochondrial ATP synthase | journal = Biochem J | volume = 293 | issue =  1| pages = 51–64 |date=Aug 1993 | pmid = 8328972 | pmc = 1134319 | doi =  10.1042/bj2930051}}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ATP5G2 ATP synthase, H+ transporting, mitochondrial F0 complex, subunit C2 (subunit 9)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=517| accessdate = }}</ref>
 
 
'''ATP synthase, H+ transporting, mitochondrial F0 complex, subunit C2 (subunit 9)''', also known as '''ATP5G2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ATP5G2 ATP synthase, H+ transporting, mitochondrial F0 complex, subunit C2 (subunit 9)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=517| accessdate = }}</ref>


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| summary_text = This gene encodes a subunit of mitochondrial ATP synthase. Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. ATP synthase is composed of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, F0, comprising the proton channel. The catalytic portion of mitochondrial ATP synthase consists of 5 different subunits (alpha, beta, gamma, delta, and epsilon) assembled with a stoichiometry of 3 alpha, 3 beta, and single representatives of the gamma, delta, and epsilon subunits. The proton channel likely has nine subunits (a, b, c, d, e, f, g, F6 and 8). There are three separate genes which encode subunit c of the proton channel and they specify precursors with different import sequences but identical mature proteins. The protein encoded by this gene is one of three precursors of subunit c. Alternatively spliced transcript variants encoding different isoforms have been identified. This gene has multiple pseudogenes.<ref name="entrez">{{cite web | title = Entrez Gene: ATP5G2 ATP synthase, H+ transporting, mitochondrial F0 complex, subunit C2 (subunit 9)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=517| accessdate = }}</ref>
| summary_text = This gene encodes a subunit of mitochondrial ATP synthase. Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. ATP synthase is composed of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, F0, comprising the proton channel. The catalytic portion of mitochondrial ATP synthase consists of 5 different subunits (alpha, beta, gamma, delta, and epsilon) assembled with a stoichiometry of 3 alpha, 3 beta, and single representatives of the gamma, delta, and epsilon subunits. The proton channel likely has nine subunits (a, b, c, d, e, f, g, F6 and 8). There are three separate genes which encode subunit c of the proton channel and they specify precursors with different import sequences but identical mature proteins. The protein encoded by this gene is one of three precursors of subunit c. Alternatively spliced transcript variants encoding different isoforms have been identified. This gene has multiple pseudogenes.<ref name="entrez"/>
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==References==
==References==
{{reflist|2}}
{{reflist}}
 
==External links==
* {{UCSC gene info|ATP5G2}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
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| citations =  
| citations =  
*{{cite journal  | author=Farrell LB, Nagley P |title=Human liver cDNA clones encoding proteolipid subunit 9 of the mitochondrial ATPase complex. |journal=Biochem. Biophys. Res. Commun. |volume=144 |issue= 3 |pages= 1257–64 |year= 1987 |pmid= 2883974 |doi=  }}
*{{cite journal  | vauthors=Farrell LB, Nagley P |title=Human liver cDNA clones encoding proteolipid subunit 9 of the mitochondrial ATPase complex. |journal=Biochem. Biophys. Res. Commun. |volume=144 |issue= 3 |pages= 1257–64 |year= 1987 |pmid= 2883974 |doi=10.1016/0006-291X(87)91446-X }}
*{{cite journal  | author=Yan WL, Lerner TJ, Haines JL, Gusella JF |title=Sequence analysis and mapping of a novel human mitochondrial ATP synthase subunit 9 cDNA (ATP5G3). |journal=Genomics |volume=24 |issue= 2 |pages= 375–7 |year= 1995 |pmid= 7698763 |doi= 10.1006/geno.1994.1631 }}
*{{cite journal  | vauthors=Yan WL, Lerner TJ, Haines JL, Gusella JF |title=Sequence analysis and mapping of a novel human mitochondrial ATP synthase subunit 9 cDNA (ATP5G3). |journal=Genomics |volume=24 |issue= 2 |pages= 375–7 |year= 1995 |pmid= 7698763 |doi= 10.1006/geno.1994.1631 }}
*{{cite journal  | author=Houstĕk J, Andersson U, Tvrdík P, ''et al.'' |title=The expression of subunit c correlates with and thus may limit the biosynthesis of the mitochondrial F0F1-ATPase in brown adipose tissue. |journal=J. Biol. Chem. |volume=270 |issue= 13 |pages= 7689–94 |year= 1995 |pmid= 7706317 |doi= }}
*{{cite journal  | vauthors=Houstĕk J, Andersson U, Tvrdík P |title=The expression of subunit c correlates with and thus may limit the biosynthesis of the mitochondrial F0F1-ATPase in brown adipose tissue. |journal=J. Biol. Chem. |volume=270 |issue= 13 |pages= 7689–94 |year= 1995 |pmid= 7706317 |doi=10.1074/jbc.270.13.7689 |display-authors=etal}}
*{{cite journal  | author=Dyer MR, Walker JE |title=Sequences of members of the human gene family for the c subunit of mitochondrial ATP synthase. |journal=Biochem. J. |volume=293 ( Pt 1) |issue= |pages= 51–64 |year= 1993 |pmid= 8328972 |doi= }}
*{{cite journal  | vauthors=Higuti T, Kawamura Y, Kuroiwa K |title=Molecular cloning and sequence of two cDNAs for human subunit c of H(+)-ATP synthase in mitochondria. |journal=Biochim. Biophys. Acta |volume=1173 |issue= 1 |pages= 87–90 |year= 1993 |pmid= 8485160 |doi=  10.1016/0167-4781(93)90249-D|display-authors=etal}}
*{{cite journal  | author=Higuti T, Kawamura Y, Kuroiwa K, ''et al.'' |title=Molecular cloning and sequence of two cDNAs for human subunit c of H(+)-ATP synthase in mitochondria. |journal=Biochim. Biophys. Acta |volume=1173 |issue= 1 |pages= 87–90 |year= 1993 |pmid= 8485160 |doi=  }}
*{{cite journal  | vauthors=Elston T, Wang H, Oster G |title=Energy transduction in ATP synthase. |journal=Nature |volume=391 |issue= 6666 |pages= 510–3 |year= 1998 |pmid= 9461222 |doi= 10.1038/35185 }}
*{{cite journal  | author=Elston T, Wang H, Oster G |title=Energy transduction in ATP synthase. |journal=Nature |volume=391 |issue= 6666 |pages= 510–3 |year= 1998 |pmid= 9461222 |doi= 10.1038/35185 }}
*{{cite journal  | vauthors=Wang H, Oster G |title=Energy transduction in the F1 motor of ATP synthase. |journal=Nature |volume=396 |issue= 6708 |pages= 279–82 |year= 1998 |pmid= 9834036 |doi= 10.1038/24409 }}
*{{cite journal  | author=Wang H, Oster G |title=Energy transduction in the F1 motor of ATP synthase. |journal=Nature |volume=396 |issue= 6708 |pages= 279–82 |year= 1998 |pmid= 9834036 |doi= 10.1038/24409 }}
*{{cite journal  | vauthors=Harrington JJ, Sherf B, Rundlett S |title=Creation of genome-wide protein expression libraries using random activation of gene expression. |journal=Nat. Biotechnol. |volume=19 |issue= 5 |pages= 440–5 |year= 2001 |pmid= 11329013 |doi= 10.1038/88107 |display-authors=etal}}
*{{cite journal  | author=Harrington JJ, Sherf B, Rundlett S, ''et al.'' |title=Creation of genome-wide protein expression libraries using random activation of gene expression. |journal=Nat. Biotechnol. |volume=19 |issue= 5 |pages= 440–5 |year= 2001 |pmid= 11329013 |doi= 10.1038/88107 }}
*{{cite journal  | vauthors=Strausberg RL, Feingold EA, Grouse LH |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 |display-authors=etal}}
*{{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=Cross RL |title=Molecular motors: turning the ATP motor. |journal=Nature |volume=427 |issue= 6973 |pages= 407–8 |year= 2004 |pmid= 14749816 |doi= 10.1038/427407b }}
*{{cite journal  | author=Cross RL |title=Molecular motors: turning the ATP motor. |journal=Nature |volume=427 |issue= 6973 |pages= 407–8 |year= 2004 |pmid= 14749816 |doi= 10.1038/427407b }}
*{{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  | vauthors=Gerhard DS, Wagner L, Feingold EA |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 |display-authors=etal}}
*{{cite journal  | author=Otsuki T, Ota T, Nishikawa T, ''et al.'' |title=Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries. |journal=DNA Res. |volume=12 |issue= 2 |pages= 117–26 |year= 2007 |pmid= 16303743 |doi= 10.1093/dnares/12.2.117 }}
*{{cite journal  | vauthors=Otsuki T, Ota T, Nishikawa T |title=Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries. |journal=DNA Res. |volume=12 |issue= 2 |pages= 117–26 |year= 2007 |pmid= 16303743 |doi= 10.1093/dnares/12.2.117 |display-authors=etal}}
}}
}}
{{refend}}
{{refend}}


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Revision as of 18:25, 29 August 2017

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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

ATP synthase lipid-binding protein, mitochondrial is an enzyme that in humans is encoded by the ATP5G2 gene.[1][2]

This gene encodes a subunit of mitochondrial ATP synthase. Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. ATP synthase is composed of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, F0, comprising the proton channel. The catalytic portion of mitochondrial ATP synthase consists of 5 different subunits (alpha, beta, gamma, delta, and epsilon) assembled with a stoichiometry of 3 alpha, 3 beta, and single representatives of the gamma, delta, and epsilon subunits. The proton channel likely has nine subunits (a, b, c, d, e, f, g, F6 and 8). There are three separate genes which encode subunit c of the proton channel and they specify precursors with different import sequences but identical mature proteins. The protein encoded by this gene is one of three precursors of subunit c. Alternatively spliced transcript variants encoding different isoforms have been identified. This gene has multiple pseudogenes.[2]

References

  1. ↑ Dyer MR, Walker JE (Aug 1993). "Sequences of members of the human gene family for the c subunit of mitochondrial ATP synthase". Biochem J. 293 (1): 51–64. doi:10.1042/bj2930051. PMC 1134319. PMID 8328972.
  2. ↑ 2.0 2.1 "Entrez Gene: ATP5G2 ATP synthase, H+ transporting, mitochondrial F0 complex, subunit C2 (subunit 9)".

External links

Further reading



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