ATP5F1

Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

ATP-synt_B
ATP-synt_B
	atp synthase b subunit dimerization domain
Identifiers
Symbol	ATP-synt_B
Pfam	PF00430
Pfam clan	CL0255
InterPro	IPR002146
SCOP2	1b9u / SCOPe / SUPFAM
Pfam
Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

ATP5PB
Identifiers
Aliases	ATP5PB , PIG47, ATP synthase, H+ transporting, mitochondrial Fo complex subunit B1, ATP synthase peripheral stalk-membrane subunit b, ATP5F1
External IDs	OMIM: 603270 MGI: 1100495 HomoloGene: 1275 GeneCards: ATP5PB
Gene location (Human)
Chr.	Chromosome 1 (human)
End	111,462,773 bp
Gene location (Mouse)
Chr.	Chromosome 3 (mouse)
End	105,867,415 bp
RNA expression pattern
	Top expressed in
	right ventricle; ; palpebral conjunctiva; ; biceps brachii; ; jejunal mucosa; ; germinal epithelium; ; cavity of mouth; ; kidney tubule; ; tibia; ; parietal pleura; ; body of tongue;
	Top expressed in
	myocardium of ventricle; ; intercostal muscle; ; soleus muscle; ; atrioventricular valve; ; medial ganglionic eminence; ; vas deferens; ; atrium; ; digastric muscle; ; endocardial cushion; ; quadriceps femoris muscle;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	protein binding ; ATPase activity ; proton transmembrane transporter activity ; proton-transporting ATP synthase activity, rotational mechanism ; transmembrane transporter activity ;
Cellular component	nucleoplasm ; mitochondrion ; mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) ; mitochondrial matrix ; proton-transporting ATP synthase complex, coupling factor F(o) ; nucleus ; membrane ; myelin sheath ; mitochondrial proton-transporting ATP synthase complex ; mitochondrial inner membrane ; extracellular exosome ;
Biological process	substantia nigra development ; ion transport ; ATP synthesis coupled proton transport ; mitochondrial ATP synthesis coupled proton transport ; ATP biosynthetic process ; cristae formation ; transport ;
	Sources:Amigo / QuickGO
Orthologs
	515
	11950
	ENSG00000116459
	ENSMUSG00000000563
	P24539
	Q9CQQ7
	NM_001688 ; NM_001002014 ; NM_001002015
	NM_009725 ; NM_001304719
	NP_001679
	NP_001291648 ; NP_033855
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated October 20, 2022

ATP synthase subunit b, mitochondrial is an enzyme that in humans is encoded by the ATP5PB gene.^[5]^[6]

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. The catalytic portion of mitochondrial ATP synthase consists of 5 different subunits (alpha, beta, gamma, delta, and epsilon) assembled with a stoichiometry of 3 alpha, 3 beta, and a single representative of the other 3. The proton channel seems to have nine subunits (a, b, c, d, e, f, g, F6 and 8). This gene encodes the b subunit of the proton channel.^[6]

The b subunits are part of the peripheral stalk that links the F1 and FO complexes together, and which acts as a stator to prevent certain subunits from rotating with the central rotary element. The peripheral stalk differs in subunit composition between mitochondrial, chloroplast and bacterial F-ATPases. In bacterial and chloroplast F-ATPases, the peripheral stalk is composed of one copy of the delta subunit (homologous to OSCP in mitochondria), and two copies of subunit b in bacteria, or one copy each of subunits b and b' in chloroplasts and photosynthetic bacteria.^[7]

Related Research Articles

ATP synthase is a protein that catalyzes the formation of the energy storage molecule adenosine triphosphate (ATP) using adenosine diphosphate (ADP) and inorganic phosphate (P_i). It is classified under ligases as it changes ADP by the formation of P-O bond (phosphodiester bond). ATP synthase is a molecular machine. The overall reaction catalyzed by ATP synthase is:

MT-ATP8 is a mitochondrial gene with the full name 'mitochondrially encoded ATP synthase membrane subunit 8' that encodes a subunit of mitochondrial ATP synthase, ATP synthase F_o subunit 8. This subunit belongs to the F_o complex of the large, transmembrane F-type ATP synthase. This enzyme, which is also known as complex V, is responsible for the final step of oxidative phosphorylation in the electron transport chain. Specifically, one segment of ATP synthase allows positively charged ions, called protons, to flow across a specialized membrane inside mitochondria. Another segment of the enzyme uses the energy created by this proton flow to convert a molecule called adenosine diphosphate (ADP) to ATP. Subunit 8 differs in sequence between Metazoa, plants and Fungi.

MT-ATP6 is a mitochondrial gene with the full name 'mitochondrially encoded ATP synthase membrane subunit 6' that encodes the ATP synthase F_o subunit 6. This subunit belongs to the F_o complex of the large, transmembrane F-type ATP synthase. This enzyme, which is also known as complex V, is responsible for the final step of oxidative phosphorylation in the electron transport chain. Specifically, one segment of ATP synthase allows positively charged ions, called protons, to flow across a specialized membrane inside mitochondria. Another segment of the enzyme uses the energy created by this proton flow to convert a molecule called adenosine diphosphate (ADP) to ATP. Mutations in the MT-ATP6 gene have been found in approximately 10 to 20 percent of people with Leigh syndrome.

ATP synthase F1 subunit beta, mitochondrial is an enzyme that in humans is encoded by the ATP5F1B gene.

ATP synthase F1 subunit alpha, mitochondrial is an enzyme that in humans is encoded by the ATP5F1A gene.

ATP synthase-coupling factor 6, mitochondrial is an enzyme subunit that in humans is encoded by the ATP5PF gene.

The ATP5MC1 gene is one of three human paralogs that encode membrane subunit c of the mitochondrial ATP synthase.

The ATP5MF gene encodes the ATP synthase subunit f, mitochondrial enzyme in humans.

ATP synthase delta subunit is a subunit of bacterial and chloroplast F-ATPase/synthase. It is known as OSCP in mitochondrial ATPase.

ATP synthase subunit g, mitochondrial is an enzyme that in humans is encoded by the ATP5MG gene.

The human ATP5F1C gene encodes the gamma subunit of an enzyme called mitochondrial ATP synthase.

ATP synthase subunit s, mitochondrial is an enzyme that in humans is encoded by the ATP5S gene.

The ATP5MC2 gene is one of three human paralogs that encode membrane subunit c of the mitochondrial ATP synthase.

ATP synthase subunit e, mitochondrial is an enzyme that in humans is encoded by the ATP5ME gene.

The human gene ATP5PD encodes subunit d of the peripheral stalk part of the enzyme mitochondrial ATP synthase.

ATP synthase subunit delta, mitochondrial, also known as ATP synthase F1 subunit delta or F-ATPase delta subunit is an enzyme that in humans is encoded by the ATP5F1D 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 F1 subunit epsilon, mitochondrial is an enzyme that in humans is encoded by the ATP5F1E gene. The protein encoded by ATP5F1E is a subunit of ATP synthase, also known as Complex V. Variations of this gene have been associated with mitochondrial complex V deficiency, nuclear 3 (MC5DN3) and Papillary Thyroid Cancer.

The ATP5MC3 gene is one of three human paralogs that encode membrane subunit c of the mitochondrial ATP synthase.

ATP synthase subunit O, mitochondrial is an enzyme that in humans is encoded by the ATP5PO gene.

V-type proton ATPase subunit E 2 is an enzyme that in humans is encoded by the ATP6V1E2 gene.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000116459 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000000563 - 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.
↑ Higuti T, Tsurumi C, Osaka F, Kawamura Y, Tsujita H, Yoshihara Y, Tani I, Tanaka K, Ichihara A (Sep 1991). "Molecular cloning of cDNA for the import precursor of human subunit B of H(+)-ATP synthase in mitochondria". Biochem Biophys Res Commun. 178 (3): 1014–20. doi:10.1016/0006-291X(91)90993-H. PMID 1831354.
1 2 "Entrez Gene: ATP5PB ATP synthase peripheral stalk-membrane subunit b".
↑ Carbajo RJ, Kellas FA, Runswick MJ, Montgomery MG, Walker JE, Neuhaus D (August 2005). "Structure of the F1-binding domain of the stator of bovine F1Fo-ATPase and how it binds an alpha-subunit". J. Mol. Biol. 351 (4): 824–38. doi:10.1016/j.jmb.2005.06.012. PMID 16045926.

External links

Human ATP5PB genome location and ATP5PB gene details page in the UCSC Genome Browser .

Gay NJ, Walker JE (1986). "Two genes encoding the bovine mitochondrial ATP synthase proteolipid specify precursors with different import sequences and are expressed in a tissue-specific manner". EMBO J. 4 (13A): 3519–24. doi:10.1002/j.1460-2075.1985.tb04111.x. PMC 554691 . PMID 2868890.
Farrell LB, Nagley P (1987). "Human liver cDNA clones encoding proteolipid subunit 9 of the mitochondrial ATPase complex". Biochem. Biophys. Res. Commun. 144 (3): 1257–64. doi:10.1016/0006-291X(87)91446-X. PMID 2883974.
Houstĕk J, Andersson U, Tvrdík P, et al. (1995). "The expression of subunit c correlates with and thus may limit the biosynthesis of the mitochondrial F0F1-ATPase in brown adipose tissue". J. Biol. Chem. 270 (13): 7689–94. doi: 10.1074/jbc.270.13.7689 . PMID 7706317.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
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.
Jia L, Young MF, Powell J, et al. (2002). "Gene expression profile of human bone marrow stromal cells: high-throughput expressed sequence tag sequencing analysis". Genomics. 79 (1): 7–17. doi:10.1006/geno.2001.6683. PMID 11827452.
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. S2CID 52819856.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928 . PMID 15489334.
Gregory SG, Barlow KF, McLay KE, et al. (2006). "The DNA sequence and biological annotation of human chromosome 1". Nature. 441 (7091): 315–21. Bibcode:2006Natur.441..315G. doi: 10.1038/nature04727 . PMID 16710414.
Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein–protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948 . PMID 17353931.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000116459 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000000563 - 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.

[pmid1831354-5] Higuti T, Tsurumi C, Osaka F, Kawamura Y, Tsujita H, Yoshihara Y, Tani I, Tanaka K, Ichihara A (Sep 1991). "Molecular cloning of cDNA for the import precursor of human subunit B of H(+)-ATP synthase in mitochondria". Biochem Biophys Res Commun. 178 (3): 1014–20. doi:10.1016/0006-291X(91)90993-H. PMID 1831354.

[entrez-6] 1 2 "Entrez Gene: ATP5PB ATP synthase peripheral stalk-membrane subunit b".

[pmid16045926-7] Carbajo RJ, Kellas FA, Runswick MJ, Montgomery MG, Walker JE, Neuhaus D (August 2005). "Structure of the F1-binding domain of the stator of bovine F1Fo-ATPase and how it binds an alpha-subunit". J. Mol. Biol. 351 (4): 824–38. doi:10.1016/j.jmb.2005.06.012. PMID 16045926.

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ATP5F1

Contents

Related Research Articles

References

External links

Further reading