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; OMA:ATP5PB - orthologs
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; ; mucosa of sigmoid colon; ; palpebral conjunctiva; ; Epithelium of choroid plexus; ; biceps brachii; ; jejunal mucosa; ; Skeletal muscle tissue of biceps brachii; ; germinal epithelium; ; oral cavity; ; kidney tubule;
	Top expressed in
	epithelium of small intestine; ; myocardium of ventricle; ; intercostal muscle; ; soleus muscle; ; atrioventricular valve; ; medial ganglionic eminence; ; vas deferens; ; atrium; ; digastric muscle; ; endocardial cushion;
	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

ATP synthase subunit b, mitochondrial is an enzyme that in humans is encoded by the ATP5F1 gene.^[5]^[6]

Template:PBB Summary

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]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000116459 – Ensembl, May 2017
^ ^a ^b ^c 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.
^ "Entrez Gene: ATP5F1 ATP synthase, H+ transporting, mitochondrial F0 complex, subunit B1".
^ 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.

References

Further reading