ATP5G1: Difference between revisions

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{{Infobox_gene}}
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'''ATP synthase lipid-binding protein, mitochondrial''' is an [[enzyme]] that in humans is encoded by the ''ATP5G1'' [[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 = The Biochemical Journal | volume = 293 | issue = Pt 1 | pages = 51–64 | date = Jul 1993 | pmid = 8328972 | pmc = 1134319 | doi =  10.1042/bj2930051}}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ATP5G1 ATP synthase, H+ transporting, mitochondrial F0 complex, subunit C1 (subunit 9)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=516| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = 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 = ATP synthase, H+ transporting, mitochondrial F0 complex, subunit C1 (subunit 9)
| HGNCid = 841
| Symbol = ATP5G1
| AltSymbols =; ATP5A; ATP5G
| OMIM = 603192
| ECnumber = 
| Homologene = 38017
| MGIid = 107653
| GeneAtlas_image1 = PBB_GE_ATP5G1_208972_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005215 |text = transporter activity}} {{GNF_GO|id=GO:0008289 |text = lipid binding}} {{GNF_GO|id=GO:0046933 |text = hydrogen ion transporting ATP synthase activity, rotational mechanism}} {{GNF_GO|id=GO:0046961 |text = hydrogen ion transporting ATPase activity, rotational mechanism}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005753 |text = mitochondrial proton-transporting ATP synthase complex}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016469 |text = proton-transporting two-sector ATPase complex}} {{GNF_GO|id=GO:0045263 |text = proton-transporting ATP synthase complex, coupling factor F(o)}}
| Process = {{GNF_GO|id=GO:0006811 |text = ion transport}} {{GNF_GO|id=GO:0015986 |text = ATP synthesis coupled proton transport}} {{GNF_GO|id=GO:0015992 |text = proton transport}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 516
    | Hs_Ensembl = ENSG00000159199
    | Hs_RefseqProtein = NP_001002027
    | Hs_RefseqmRNA = NM_001002027
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 17
    | Hs_GenLoc_start = 44325779
    | Hs_GenLoc_end = 44328229
    | Hs_Uniprot = P05496
    | Mm_EntrezGene = 11951
    | Mm_Ensembl = ENSMUSG00000006057
    | Mm_RefseqmRNA = NM_007506
    | Mm_RefseqProtein = NP_031532
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 11
    | Mm_GenLoc_start = 95884940
    | Mm_GenLoc_end = 95891127
    | Mm_Uniprot = 
  }}
}}
'''ATP synthase, H+ transporting, mitochondrial F0 complex, subunit C1 (subunit 9)''', also known as '''ATP5G1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ATP5G1 ATP synthase, H+ transporting, mitochondrial F0 complex, subunit C1 (subunit 9)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=516| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
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, Fo, 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 a single representative of the other 3. The proton channel seems to have nine subunits (a, b, c, d, e, f, g, F6 and 8). This gene is one of three genes that encode subunit c of the proton channel. Each of the three genes have distinct mitochondrial import sequences but encode the identical mature protein. Alternatively spliced transcript variants encoding the same protein have been identified.<ref name="entrez" />
{{PBB_Summary
| section_title =
| 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, Fo, 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 a single representative of the other 3. The proton channel seems to have nine subunits (a, b, c, d, e, f, g, F6 and 8). This gene is one of three genes that encode subunit c of the proton channel. Each of the three genes have distinct mitochondrial import sequences but encode the identical mature protein. Alternatively spliced transcript variants encoding the same protein have been identified.<ref name="entrez">{{cite web | title = Entrez Gene: ATP5G1 ATP synthase, H+ transporting, mitochondrial F0 complex, subunit C1 (subunit 9)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=516| accessdate = }}</ref>
}}


==References==
== References ==
{{reflist|2}}
{{reflist}}
==Further reading==
 
==External links==
* {{UCSC gene info|ATP5G1}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Farrell LB, Nagley P | title = Human liver cDNA clones encoding proteolipid subunit 9 of the mitochondrial ATPase complex | journal = Biochemical and Biophysical Research Communications | volume = 144 | issue = 3 | pages = 1257–64 | date = May 1987 | pmid = 2883974 | doi = 10.1016/0006-291X(87)91446-X }}
| citations =
* {{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 | date = Nov 1994 | pmid = 7698763 | doi = 10.1006/geno.1994.1631 }}
*{{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 = Higuti T, Kawamura Y, Kuroiwa K, Miyazaki S, Tsujita H | title = Molecular cloning and sequence of two cDNAs for human subunit c of H(+)-ATP synthase in mitochondria | journal = Biochimica et Biophysica Acta | volume = 1173 | issue = 1 | pages = 87–90 | date = Apr 1993 | pmid = 8485160 | doi = 10.1016/0167-4781(93)90249-D }}
*{{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 = Bonaldo MF, Lennon G, Soares MB | title = Normalization and subtraction: two approaches to facilitate gene discovery | journal = Genome Research | volume = 6 | issue = 9 | pages = 791–806 | date = Sep 1996 | pmid = 8889548 | doi = 10.1101/gr.6.9.791 }}
*{{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 = Elston T, Wang H, Oster G | title = Energy transduction in ATP synthase | journal = Nature | volume = 391 | issue = 6666 | pages = 510–3 | date = Jan 1998 | pmid = 9461222 | doi = 10.1038/35185 }}
*{{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 = Wang H, Oster G | title = Energy transduction in the F1 motor of ATP synthase | journal = Nature | volume = 396 | issue = 6708 | pages = 279–82 | date = Nov 1998 | pmid = 9834036 | doi = 10.1038/24409 }}
*{{cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi= }}
* {{cite journal | vauthors = Hartley JL, Temple GF, Brasch MA | title = DNA cloning using in vitro site-specific recombination | journal = Genome Research | volume = 10 | issue = 11 | pages = 1788–95 | date = Nov 2000 | pmid = 11076863 | pmc = 310948 | doi = 10.1101/gr.143000 }}
*{{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 = Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Böcher M, Blöcker H, Bauersachs S, Blum H, Lauber J, Düsterhöft A, Beyer A, Köhrer K, Strack N, Mewes HW, Ottenwälder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A | title = Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs | journal = Genome Research | volume = 11 | issue = 3 | pages = 422–35 | date = Mar 2001 | pmid = 11230166 | pmc = 311072 | doi = 10.1101/gr.GR1547R }}
*{{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 = Cross RL | title = Molecular motors: turning the ATP motor | journal = Nature | volume = 427 | issue = 6973 | pages = 407–8 | date = Jan 2004 | pmid = 14749816 | doi = 10.1038/427407b }}
*{{cite journal | author=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788-95 |year= 2001 |pmid= 11076863 |doi= }}
* {{cite journal | vauthors = Wiemann S, Arlt D, Huber W, Wellenreuther R, Schleeger S, Mehrle A, Bechtel S, Sauermann M, Korf U, Pepperkok R, Sültmann H, Poustka A | title = From ORFeome to biology: a functional genomics pipeline | journal = Genome Research | volume = 14 | issue = 10B | pages = 2136–44 | date = Oct 2004 | pmid = 15489336 | pmc = 528930 | doi = 10.1101/gr.2576704 }}
*{{cite journal | author=Wiemann S, Weil B, Wellenreuther R, ''et al.'' |title=Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. |journal=Genome Res. |volume=11 |issue= 3 |pages= 422-35 |year= 2001 |pmid= 11230166 |doi= 10.1101/gr.154701 }}
* {{cite journal | vauthors = Wang HL, Zhu ZM, Yerle M, Wu X, Wang H, Yang SL, Li K | title = Full-length coding sequences and mapping of porcine ATP6VOE and ATP5G1 genes | journal = Cytogenetic and Genome Research | volume = 109 | issue = 4 | pages = 533 | year = 2005 | pmid = 15906478 | doi = 10.1159/000084223 }}
*{{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 | vauthors = Mehrle A, Rosenfelder H, Schupp I, del Val C, Arlt D, Hahne F, Bechtel S, Simpson J, Hofmann O, Hide W, Glatting KH, Huber W, Pepperkok R, Poustka A, Wiemann S | title = The LIFEdb database in 2006 | journal = Nucleic Acids Research | volume = 34 | issue = Database issue | pages = D415–8 | date = Jan 2006 | pmid = 16381901 | pmc = 1347501 | doi = 10.1093/nar/gkj139 }}
*{{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=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  | author=Wiemann S, Arlt D, Huber W, ''et al.'' |title=From ORFeome to biology: a functional genomics pipeline. |journal=Genome Res. |volume=14 |issue= 10B |pages= 2136-44 |year= 2004 |pmid= 15489336 |doi= 10.1101/gr.2576704 }}
*{{cite journal | author=Wang HL, Zhu ZM, Yerle M, ''et al.'' |title=Full-length coding sequences and mapping of porcine ATP6VOE and ATP5G1 genes. |journal=Cytogenet. Genome Res. |volume=109 |issue= 4 |pages= 533 |year= 2005 |pmid= 15906478 |doi= }}
*{{cite journal | author=Mehrle A, Rosenfelder H, Schupp I, ''et al.'' |title=The LIFEdb database in 2006. |journal=Nucleic Acids Res. |volume=34 |issue= Database issue |pages= D415-8 |year= 2006 |pmid= 16381901 |doi= 10.1093/nar/gkj139 }}
}}
{{refend}}
{{refend}}


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Revision as of 18:25, 29 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

ATP synthase lipid-binding protein, mitochondrial is an enzyme that in humans is encoded by the ATP5G1 gene.[1][2]

Function

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, Fo, 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 a single representative of the other 3. The proton channel seems to have nine subunits (a, b, c, d, e, f, g, F6 and 8). This gene is one of three genes that encode subunit c of the proton channel. Each of the three genes have distinct mitochondrial import sequences but encode the identical mature protein. Alternatively spliced transcript variants encoding the same protein have been identified.[2]

References

  1. ↑ Dyer MR, Walker JE (Jul 1993). "Sequences of members of the human gene family for the c subunit of mitochondrial ATP synthase". The Biochemical Journal. 293 (Pt 1): 51–64. doi:10.1042/bj2930051. PMC 1134319. PMID 8328972.
  2. ↑ 2.0 2.1 "Entrez Gene: ATP5G1 ATP synthase, H+ transporting, mitochondrial F0 complex, subunit C1 (subunit 9)".

External links

Further reading


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