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DMAC2L
Identifiers
Aliases	DMAC2L, ATPW, FB, HSU79253, ATP synthase, H+ transporting, mitochondrial Fo complex subunit s (factor B), ATP5S, distal membrane arm assembly complex 2 like, distal membrane arm assembly component 2 like
External IDs	MGI: 1915305; HomoloGene: 12232; GeneCards: DMAC2L; OMA:DMAC2L - orthologs
Gene location (Human) Chr. Chromosome 14 (human) Band 14q21.3 Start 50,312,324 bp End 50,335,558 bp
Gene location (Mouse) Chr. Chromosome 12 (mouse) Band 12|12 C2 Start 69,771,724 bp End 69,791,434 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in sperm right uterine tube Skeletal muscle tissue of biceps brachii endothelial cell triceps brachii muscle glutes oocyte thoracic diaphragm skin of thigh right ventricle Top expressed in interventricular septum spermatid right ventricle right kidney spermatocyte sternocleidomastoid muscle digastric muscle myocardium of ventricle triceps brachii muscle temporal muscle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function proton transmembrane transporter activity metal ion binding Cellular component mitochondrion membrane proton-transporting ATP synthase complex, coupling factor F(o) mitochondrial inner membrane Biological process ion transport ATP biosynthetic process cristae formation proton transmembrane transport mitochondrial ATP synthesis coupled proton transport Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 27109 68055 Ensembl ENSG00000125375 ENSMUSG00000054894 UniProt Q99766 Q9CRA7 RefSeq (mRNA) NM_001003803 NM_001003805 NM_015684 NM_001370605 NM_001382507 NM_001382509 NM_001382510 NM_026536 NM_001361690 NM_001361691 RefSeq (protein) NP_001003803 NP_001003805 NP_056499 NP_001357534 NP_001369436 NP_001369438 NP_001369439 NP_080812 NP_001348619 NP_001348620 Location (UCSC) Chr 14: 50.31 – 50.34 Mb Chr 12: 69.77 – 69.79 Mb PubMed search
Wikidata
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ATP synthase subunit s, mitochondrial is an enzyme that in humans is encoded by the ATP5S gene.

This gene encodes a subunit of mitochondrial ATP synthase. Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. ATP synthase is composed of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, Fo, comprising the proton channel. This gene encodes the subunit s, also known as factor B, of the proton channel. This subunit is necessary for the energy transduction activity of the ATP synthase complexes. Alternatively spliced transcript variants encoding different isoforms have been identified.

References

1. ^ GRCh38: Ensembl release 89: ENSG00000125375 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000054894 – 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. Belogrudov GI, Hatefi Y (Feb 2002). "Factor B and the mitochondrial ATP synthase complex". J Biol Chem. 277 (8): 6097–103. doi:10.1074/jbc.M111256200. PMID 11744738.
6. Andersson B, Wentland MA, Ricafrente JY, Liu W, Gibbs RA (Jun 1996). "A "double adaptor" method for improved shotgun library construction". Anal Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
7. ^ "Entrez Gene: ATP5S ATP synthase, H+ transporting, mitochondrial F0 complex, subunit s (factor B)".

External links

• Human ATP5S genome location and ATP5S gene details page in the UCSC Genome Browser.
• ATP5S: ATP synthase, H+ transporting, mitochondrial Fo complex subunit s (factor B)

Further reading

• Kinosita K, Yasuda R, Noji H (2003). "F1-ATPase: a highly efficient rotary ATP machine". Essays Biochem. 35: 3–18. doi:10.1042/bse0350003. PMID 12471886.
• Oster G, Wang H (2003). "Rotary protein motors". Trends Cell Biol. 13 (3): 114–21. doi:10.1016/S0962-8924(03)00004-7. PMID 12628343.
• Leyva JA, Bianchet MA, Amzel LM (2003). "Understanding ATP synthesis: structure and mechanism of the F1-ATPase (Review)". Mol. Membr. Biol. 20 (1): 27–33. doi:10.1080/0968768031000066532. PMID 12745923. S2CID 218895820.
• Sanadi DR, Pringle M, Kantham L, et al. (1984). "Evidence for the involvement of coupling factor B in the H+ channel of the mitochondrial H+-ATPase". Proc. Natl. Acad. Sci. U.S.A. 81 (5): 1371–4. Bibcode:1984PNAS...81.1371S. doi:10.1073/pnas.81.5.1371. PMC 344835. PMID 6143319.
• Yu W, Andersson B, Worley KC, et al. (1997). "Large-Scale Concatenation cDNA Sequencing". Genome Res. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174.
• Elston T, Wang H, Oster G (1998). "Energy transduction in ATP synthase". Nature. 391 (6666): 510–3. Bibcode:1998Natur.391..510E. doi:10.1038/35185. PMID 9461222. S2CID 4406161.
• Wang H, Oster G (1998). "Energy transduction in the F1 motor of ATP synthase". Nature. 396 (6708): 279–82. Bibcode:1998Natur.396..279W. doi:10.1038/24409. PMID 9834036. S2CID 4424498.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Cross RL (2004). "Molecular motors: turning the ATP motor". Nature. 427 (6973): 407–8. Bibcode:2004Natur.427..407C. doi:10.1038/427407b. PMID 14749816.
• Ma J, Dempsey AA, Stamatiou D, et al. (2007). "Identifying leukocyte gene expression patterns associated with plasma lipid levels in human subjects". Atherosclerosis. 191 (1): 63–72. doi:10.1016/j.atherosclerosis.2006.05.032. PMID 16806233.

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