ATP5L

ATP synthase subunit g, mitochondrial is an enzyme that in humans is encoded by the ATP5MG gene.[5][6][7]

ATP5MG
Identifiers
AliasesATP5MG, ATP5JG, ATP synthase, H+ transporting, mitochondrial Fo complex subunit G, ATP synthase membrane subunit g, ATP5L
External IDsOMIM: 617473 MGI: 1351597 HomoloGene: 86074 GeneCards: ATP5MG
Gene location (Human)
Chr.Chromosome 11 (human)[1]
Band11q23.3Start118,401,606 bp[1]
End118,431,496 bp[1]
RNA expression pattern




More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

10632

27425

Ensembl

ENSG00000167283

ENSMUSG00000038717

UniProt

O75964

Q9CPQ8

RefSeq (mRNA)

NM_006476

NM_013795

RefSeq (protein)

NP_006467

NP_038823

Location (UCSC)Chr 11: 118.4 – 118.43 MbChr 9: 44.91 – 44.92 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse
ATP-synt_G
Identifiers
SymbolATP-synt_G
PfamPF04718
InterProIPR006808

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, Fo, 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 Fo 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.[7]

The function of subunit G is currently unknown. There is no counterpart in chloroplast or bacterial F-ATPases identified so far.[8]

References

  1. GRCh38: Ensembl release 89: ENSG00000167283 - Ensembl, May 2017
  2. GRCm38: Ensembl release 89: ENSMUSG00000038717 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. 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.
  6. 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.
  7. "Entrez Gene: ATP5MG ATP synthase membrane subunit g".
  8. 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.

Further reading


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


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