From Wikipedia, the free encyclopedia
Protein-coding gene in the species Homo sapiens
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 kExternal IDs
OMIM :
615204 ;
MGI :
1891435 ;
HomoloGene :
11331 ;
GeneCards :
ATP5MK ;
OMA :
ATP5MK - orthologs
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
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
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
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
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
^
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 .