USMG5
| ATP5MK | |||||||||||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Aliases | ATP5MK, DAPIT, HCVFTP2, bA792D24.4, up-regulated during skeletal muscle growth 5 homolog (mouse), USMG5, ATP synthase membrane subunit DAPIT, MC5DN6, AGP, ATP5MD, ATP synthase membrane subunit k | ||||||||||||||||||||||||||||||||||||||||||||||||||
| External IDs | OMIM: 615204 MGI: 1891435 HomoloGene: 11331 GeneCards: ATP5MK | ||||||||||||||||||||||||||||||||||||||||||||||||||
| |||||||||||||||||||||||||||||||||||||||||||||||||||
| |||||||||||||||||||||||||||||||||||||||||||||||||||
| |||||||||||||||||||||||||||||||||||||||||||||||||||
| |||||||||||||||||||||||||||||||||||||||||||||||||||
| Wikidata | |||||||||||||||||||||||||||||||||||||||||||||||||||
| |||||||||||||||||||||||||||||||||||||||||||||||||||
Up-regulated during skeletal muscle growth protein 5 (USMG5), also known as ATP synthase membrane subunit DAPIT (ATP5MD), Diabetes-associated protein in insulin-sensitive tissues, or HCV F-transactivated protein 2 is a protein that in humans is encoded by the USMG5 gene. [5][6][7]
Structure[edit]
The USMG5 gene is located on the q arm of chromosome 10 at position 24.33 and it spans 7,463 base pairs.[5] The USMG5 gene produces a 6.46 kDa protein composed of 58 amino acids.[8][9] USMG5 is a small subunit of the mitochondrial ATP synthase (complex V), as well as the lysosomal V-ATPase.[10] The protein is associated with the ATP synthase in a stoichiometric manner.[11] The structure of the protein contains a putative transmembrane segment and a single presumed α-helix that spans from amino acid 23 to 45. The structure has been found to be similar to its putative yeast ortholog.[12]
Function[edit]
The human USMG5 gene codes for a protein with a role in maintaining and regulating the ATP synthase population in the mitochondria.[6][7][12] The protein is responsible for several minor roles that are expendable for the core function of complex V.[11] A knockdown of the protein has been shown to lead to reduced ATP synthesis rate and CV dimer expression, while the wild type has been shown to boost the dimerization of complex V as well as enhance the ATP synthesis rate.[13]
Clinical Significance[edit]
Mutations in USMG5 has been found to result in mitochondrial deficiencies and associated disorders of the mitochondrial ATP synthase (complex V). Homozygous splice-site mutations (c.87 + 1G>C) in the Ashkenazi Jewish population have been associated with cases of leigh syndrome caused by the decrease of Complex V dimerization and ATP synthesis. Leigh syndrome is a heterogeneous mitochondrial oxidative phosphorylation (OXPHOS) disease that is characterized by psychomotor retardation and necrotizing lesions in the brain.[13]
Interactions[edit]
USMG5 is a component of the ATP synthase complex, and has co-complex interactions with ATP5F1, ATP5MC1, TP5F1E, ATP5H, ATP5ME, ATP5J, ATP5J2, and others.[6][7]
References[edit]
- ^ a b c GRCh38: Ensembl release 89: ENSG00000173915 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000071528 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ a b
"Entrez Gene: ATP synthase membrane subunit DAPIT". Retrieved 2018-08-14.
This article incorporates text from this source, which is in the public domain.
- ^ a b c
"USMG5 - Up-regulated during skeletal muscle growth protein 5 - Homo sapiens (Human) - USMG5 gene & protein". Retrieved 2018-08-07.
This article incorporates text available under the CC BY 4.0 license.
- ^ a b c "UniProt: the universal protein knowledgebase". Nucleic Acids Research. 45 (D1): D158–D169. January 2017. doi:10.1093/nar/gkw1099. PMC 5210571. PMID 27899622.
- ^ Zong NC, Li H, Li H, Lam MP, Jimenez RC, Kim CS, Deng N, Kim AK, Choi JH, Zelaya I, Liem D, Meyer D, Odeberg J, Fang C, Lu HJ, Xu T, Weiss J, Duan H, Uhlen M, Yates JR, Apweiler R, Ge J, Hermjakob H, Ping P (Oct 2013). "Integration of cardiac proteome biology and medicine by a specialized knowledgebase". Circulation Research. 113 (9): 1043–53. doi:10.1161/CIRCRESAHA.113.301151. PMC 4076475. PMID 23965338.
- ^ "Up-regulated during skeletal muscle growth protein 5". Cardiac Organellar Protein Atlas Knowledgebase (COPaKB). Archived from the original on 2018-08-15. Retrieved 2018-08-14.
- ^ Kontro, H; Hulmi, JJ; Rahkila, P; Kainulainen, H (22 May 2012). "Cellular and tissue expression of DAPIT, a phylogenetically conserved peptide". European Journal of Histochemistry. 56 (2): e18. doi:10.4081/ejh.2012.18. PMC 3428967. PMID 22688299.
- ^ a b Ohsakaya S, Fujikawa M, Hisabori T, Yoshida M (June 2011). "Knockdown of DAPIT (diabetes-associated protein in insulin-sensitive tissue) results in loss of ATP synthase in mitochondria". J. Biol. Chem. 286 (23): 20292–6. doi:10.1074/jbc.M110.198523. PMC 3121504. PMID 21345788.
- ^ a b Kontro H, Hulmi JJ, Rahkila P, Kainulainen H (May 2012). "Cellular and tissue expression of DAPIT, a phylogenetically conserved peptide". Eur J Histochem. 56 (2): e18. doi:10.4081/ejh.2012.18. PMC 3428967. PMID 22688299.
- ^ a b Barca, E; Ganetzky, RD; Potluri, P; Juanola-Falgarona, M; Gai, X; Li, D; Jalas, C; Hirsch, Y; Emmanuele, V; Tadesse, S; Ziosi, M; Akman, HO; Chung, WK; Tanji, K; McCormick, E; Place, E; Consugar, M; Pierce, EA; Hakonarson, H; Wallace, DC; Hirano, M; Falk, MJ (18 June 2018). "USMG5 Ashkenazi Jewish founder mutation impairs mitochondrial complex V dimerization and ATP synthesis". Human Molecular Genetics. 27 (19): 3305–3312. doi:10.1093/hmg/ddy231. PMC 6140788. PMID 29917077.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.