USMG5

From Wikipedia, the free encyclopedia

AliasesATP5MK, 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
End103,396,492 bp[1]
ATP5MK
Identifiers
AliasesATP5MK, 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 IDsOMIM: 615204; MGI: 1891435; HomoloGene: 11331; GeneCards: ATP5MK; OMA:ATP5MK - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_032747
NM_001206426
NM_001206427

NM_023211

RefSeq (protein)

NP_001193355
NP_001193356
NP_116136

NP_075700

Location (UCSC)Chr 10: 103.39 – 103.4 MbChr 19: 47.07 – 47.08 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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]

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

Interactions

References

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