ATP5L: Difference between revisions

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{{Infobox_gene}}
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{{Infobox protein family
| update_page = yes
| Symbol = ATP-synt_G
| require_manual_inspection = no
| Name = ATP-synt_G
| update_protein_box = yes
| image =  
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}}
| Pfam = PF04718
 
| Pfam_clan =   
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| InterPro = IPR006808
{{GNF_Protein_box
| SMART =  
| image = 
| PROSITE =  
| image_source = 
| MEROPS =  
| PDB =
| SCOP =  
| Name = ATP synthase, H+ transporting, mitochondrial F0 complex, subunit G
| TCDB =  
| HGNCid = 14247
| OPM family =  
| Symbol = ATP5L
| OPM protein =  
| AltSymbols =; ATP5JG
| CAZy =  
| OMIM = 
| CDD =  
| ECnumber = 
| Homologene = 86074
| MGIid = 
| GeneAtlas_image1 = PBB_GE_ATP5L_208745_at_tn.png
| GeneAtlas_image2 = PBB_GE_ATP5L_207573_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_ATP5L_208746_x_at_tn.png
| Function = {{GNF_GO|id=GO:0046872 |text = metal ion 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:0005739 |text = mitochondrion}} {{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 = 10632
    | Hs_Ensembl = ENSG00000167283
    | Hs_RefseqProtein = NP_006467
    | Hs_RefseqmRNA = NM_006476
    | Hs_GenLoc_db =   
    | Hs_GenLoc_chr = 11
    | Hs_GenLoc_start = 117777314
    | Hs_GenLoc_end = 117785769
    | Hs_Uniprot = O75964
    | Mm_EntrezGene =
    | Mm_Ensembl =
    | Mm_RefseqmRNA =
    | Mm_RefseqProtein =
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr =
    | Mm_GenLoc_start =
    | Mm_GenLoc_end = 
    | Mm_Uniprot = 
  }}
}}
}}
'''ATP synthase, H+ transporting, mitochondrial F0 complex, subunit G''', also known as '''ATP5L''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ATP5L ATP synthase, H+ transporting, mitochondrial F0 complex, subunit G| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10632| accessdate = }}</ref>
'''ATP synthase subunit g, mitochondrial''' is an [[enzyme]] that in humans is encoded by the ''ATP5L'' [[gene]].<ref name="pmid11230166">{{cite journal | vauthors = Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder 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 Res | volume = 11 | issue = 3 | pages = 422–35 |date=Mar 2001 | pmid = 11230166 | pmc = 311072 | doi = 10.1101/gr.GR1547R }}</ref><ref name="pmid11042152">{{cite journal | vauthors = Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z | title = Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells | journal = Genome Res | volume = 10 | issue = 10 | pages = 1546–60 |date=Nov 2000 | pmid = 11042152 | pmc = 310934 | doi =10.1101/gr.140200  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ATP5L ATP synthase, H+ transporting, mitochondrial F0 complex, subunit G| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10632| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. It is composed of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, F0, which comprises the proton channel. The F1 complex consists of 5 different subunits (alpha, beta, gamma, delta, and epsilon) assembled in a ratio of 3 alpha, 3 beta, and a single representative of the other 3. The F0 seems to have nine subunits (a, b, c, d, e, f, g, F6 and 8). This gene encodes the g subunit of the F0 complex.<ref name="entrez">{{cite web | title = Entrez Gene: ATP5L ATP synthase, H+ transporting, mitochondrial F0 complex, subunit G| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10632| accessdate = }}</ref>
| summary_text = Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. It is composed of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, F0, which comprises the proton channel. The F1 complex consists of 5 different subunits (alpha, beta, gamma, delta, and epsilon) assembled in a ratio of 3 alpha, 3 beta, and a single representative of the other 3. The F0 seems to have nine subunits (a, b, c, d, e, f, g, F6 and 8). This gene encodes the g subunit of the F0 complex.<ref name="entrez"/>
}}
}}
The function of subunit G is currently unknown. There is no counterpart in chloroplast or [[bacterial]] F-ATPases identified so far.<ref name="pmid8011660">{{cite journal | vauthors = Collinson IR, Runswick MJ, Buchanan SK, Fearnley IM, Skehel JM, van Raaij MJ, Griffiths DE, Walker JE | title = Fo membrane domain of ATP synthase from bovine heart mitochondria: purification, subunit composition, and reconstitution with F1-ATPase | journal = Biochemistry | volume = 33 | issue = 25 | pages = 7971–8 |date=June 1994 | pmid = 8011660 | doi = 10.1021/bi00191a026| url = }}</ref>


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==External links==
* {{UCSC gene info|ATP5L}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Kinosita K, Yasuda R, Noji H |title=F1-ATPase: a highly efficient rotary ATP machine. |journal=Essays Biochem. |volume=35 |issue=  |pages= 3-18 |year= 2003 |pmid= 12471886 |doi=  }}
*{{cite journal  | vauthors=Kinosita K, Yasuda R, Noji H |title=F1-ATPase: a highly efficient rotary ATP machine. |journal=Essays Biochem. |volume=35 |issue=  |pages= 3–18 |year= 2003 |pmid= 12471886 |doi=  }}
*{{cite journal  | author=Oster G, Wang H |title=Rotary protein motors. |journal=Trends Cell Biol. |volume=13 |issue= 3 |pages= 114-21 |year= 2003 |pmid= 12628343 |doi=  }}
*{{cite journal  | vauthors=Oster G, Wang H |title=Rotary protein motors. |journal=Trends Cell Biol. |volume=13 |issue= 3 |pages= 114–21 |year= 2003 |pmid= 12628343 |doi=10.1016/S0962-8924(03)00004-7 }}
*{{cite journal  | author=Leyva JA, Bianchet MA, Amzel LM |title=Understanding ATP synthesis: structure and mechanism of the F1-ATPase (Review). |journal=Mol. Membr. Biol. |volume=20 |issue= 1 |pages= 27-33 |year= 2003 |pmid= 12745923 |doi=  }}
*{{cite journal  | vauthors=Leyva JA, Bianchet MA, Amzel LM |title=Understanding ATP synthesis: structure and mechanism of the F1-ATPase (Review). |journal=Mol. Membr. Biol. |volume=20 |issue= 1 |pages= 27–33 |year= 2003 |pmid= 12745923 |doi=10.1080/0968768031000066532 }}
*{{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=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=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=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=Zhang QH, Ye M, Wu XY, ''et al.'' |title=Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. |journal=Genome Res. |volume=10 |issue= 10 |pages= 1546-60 |year= 2001 |pmid= 11042152 |doi=  }}
*{{cite journal  | vauthors=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=10.1101/gr.143000  | pmc=310948  }}
*{{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=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=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  | 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=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=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=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  | vauthors=Wiemann S, Arlt D, Huber W |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 | pmc=528930 |display-authors=etal}}
*{{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=Mehrle A, Rosenfelder H, Schupp I |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 | pmc=1347501 |display-authors=etal}}
*{{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  | vauthors=Ewing RM, Chu P, Elisma F |title=Large-scale mapping of human protein-protein interactions by mass spectrometry. |journal=Mol. Syst. Biol. |volume=3 |issue=  1|pages= 89 |year= 2007 |pmid= 17353931 |doi= 10.1038/msb4100134 | pmc=1847948 |display-authors=etal}}
*{{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 }}
*{{cite journal  | author=Ewing RM, Chu P, Elisma F, ''et al.'' |title=Large-scale mapping of human protein-protein interactions by mass spectrometry. |journal=Mol. Syst. Biol. |volume=3 |issue=  |pages= 89 |year= 2007 |pmid= 17353931 |doi= 10.1038/msb4100134 }}
}}
}}
{{refend}}
{{refend}}


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Revision as of 18:26, 29 August 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human
ATP-synt_G
Identifiers
SymbolATP-synt_G
PfamPF04718
InterProIPR006808

ATP synthase subunit g, mitochondrial is an enzyme that in humans is encoded by the ATP5L gene.[1][2][3]

Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. It is composed of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, F0, which comprises the proton channel. The F1 complex consists of 5 different subunits (alpha, beta, gamma, delta, and epsilon) assembled in a ratio of 3 alpha, 3 beta, and a single representative of the other 3. The F0 seems to have nine subunits (a, b, c, d, e, f, g, F6 and 8). This gene encodes the g subunit of the F0 complex.[3]

The function of subunit G is currently unknown. There is no counterpart in chloroplast or bacterial F-ATPases identified so far.[4]

References

  1. ↑ Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A (Mar 2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs". Genome Res. 11 (3): 422–35. doi:10.1101/gr.GR1547R. PMC 311072. PMID 11230166.
  2. ↑ Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z (Nov 2000). "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells". Genome Res. 10 (10): 1546–60. doi:10.1101/gr.140200. PMC 310934. PMID 11042152.
  3. ↑ 3.0 3.1 "Entrez Gene: ATP5L ATP synthase, H+ transporting, mitochondrial F0 complex, subunit G".
  4. ↑ Collinson IR, Runswick MJ, Buchanan SK, Fearnley IM, Skehel JM, van Raaij MJ, Griffiths DE, Walker JE (June 1994). "Fo membrane domain of ATP synthase from bovine heart mitochondria: purification, subunit composition, and reconstitution with F1-ATPase". Biochemistry. 33 (25): 7971–8. doi:10.1021/bi00191a026. PMID 8011660.

External links

Further reading


This article incorporates text from the public domain Pfam and InterPro: IPR006808


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