Gene Ontology annotation through association of InterPro records with GO terms.
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt.
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods.
Assembly of human mitochondrial ATP synthase through two separate intermediates, F1-c-ring and b-e-g complex.
-
Human ATP synthase is assembled via two separate intermediates, one containing the central rotor shaft with the c-ring and catalytic F1 subunits, and the other containing peripheral stator stalk components.
"[human cells] accumulated two subcomplexes, one...containing a central rotor shaft plus catalytic subunits (F1-c-ring) and the...other containing stator stalk components ("b-e-g" complex)."
-
The c-ring (which includes the c-subunit encoded by ATP5MC3) assembles with the F1 catalytic domain into a discrete F1-c-ring intermediate, with the central rotor shaft and stator stalk forming separately before assembling together.
"F1-c-ring was also...formed when expression of mitochondrial DNA-coded a-subunit and A6L was...suppressed. Thus, the central rotor shaft and the stator stalk are formed...separately and they assemble later."
TMEM70 and TMEM242 help to assemble the rotor ring of human ATP synthase and interact with assembly factors for complex I.
-
Assembly of the ATP synthase c8-ring (composed of subunit c proteins including ATP5MC3) requires the transmembrane assembly factors TMEM70 and TMEM242, which physically interact with subunit c.
"Here, we show that the assembly of the c8-ring requires not only TMEM70 but also a previously unidentified transmembrane protein, TMEM242. Moreover, both TMEM70 and TMEM242 interact with subunit c, and also with the mitochondrial complex I assembly complex, or MCIA complex."
-
An F1-catalytic-domain intermediate associated with the membrane c8-ring rotor and peripheral stalk is a central node in ATP synthase assembly, and the c8-ring can be added to this complex as a pre-built module.
"This intermediate consists of the F1-catalytic domain attached to the membrane associated c8-ring component of the enzyme’s rotor plus an elongated peripheral stalk (PS) complex bound to the F1-domain and extending into the membrane domain of the enzyme."
-
Transcripts from ATP5MC1-3 remained at normal or higher levels in cells lacking TMEM70 and/or TMEM242, indicating subunit c protein loss arises from post-translational degradation when assembly factors are missing.
"As transcripts for subunit c from ATP5MC1-3 were present in normal or higher amounts in both HEK293-∆δ.∆TMEM242 and HEK293-∆δ.∆TMEM70.∆TMEM242 cells (SI Appendix, Fig. S12), it is probable that the lower level of subunit c in these cells arises from the degradation of the protein."
Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context.
-
A high-confidence human mitochondrial proteome (MitoCoP) of >1,100 proteins was defined, with identified interactors of translocases, respiratory chain, and ATP synthase assembly factors.
"mitochondrial high-confidence proteome of >1,100 proteins (MitoCoP). We...identified interactors of translocases, respiratory chain, and ATP synthase...assembly factors."
-
OXPHOS subunits, including those of ATP synthase (complex V), are among the highly abundant mitochondrial proteins quantified in the MitoCoP dataset.
"Our data show a high abundance of OXPHOS subunits and factors involved in protein maturation and folding with the molecular chaperones HSP60/10...as the two most abundant mitochondrial proteins"
Enzyme-bound ATP is released
ADP and Pi bind to ATPase
F1Fo ATP synthase dimerizes
Deep research on ATP5MC3 function
Cyberian deep research on ATP5MC3 function