ATP5F1A Protein, Human (His-SUMO)

ATP5F1A is an important component of mitochondrial ATP synthase (complex V) that coordinates ATP production from ADP by utilizing the transmembrane proton gradient. As part of the F-type ATPase, the α and β subunits of ATP5F1A form the catalytic core to achieve ATP hydrolysis. ATP5F1A Protein, Human (His-SUMO) is the recombinant human-derived ATP5F1A protein, expressed by E. coli , with N-6*His, N-SUMO labeled tag. The total length of ATP5F1A Protein, Human (His-SUMO) is 510 a.a., with molecular weight of ~71.2 kDa.

ATP5F1A, a crucial component of the mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V), plays a pivotal role in ATP production from ADP by harnessing the proton gradient across the membrane generated by the respiratory chain's electron transport complexes. Comprising the catalytic core (F(1)) and the membrane proton channel (F(0)), F-type ATPases, like ATP5F1A, consist of multiple subunits with distinct functions. The alpha and beta subunits form the catalytic core in F(1), where rotation of the central stalk against surrounding alpha(3)beta(3) subunits facilitates ATP hydrolysis. Intriguingly, ATP5F1A binds the bacterial siderophore enterobactin, promoting the accumulation of enterobactin-derived iron ions within mitochondria. Additionally, ATP5F1A interacts with various proteins, such as ATPAF2, HRG, PLG, BLOC1S1, BCL2L1 isoform BCL-X(L), CLN5, PPT1, S100A1, and ABCB7, influencing diverse cellular processes ranging from metabolic efficiency and iron homeostasis to apoptotic regulation. Furthermore, ATP5F1A is a crucial component of the ATP synthase complex, highlighting its central role in cellular energy production. Understanding these intricate interactions sheds light on the multifaceted functions of ATP5F1A in cellular physiology.

Human

E. coli

N-6*His;N-SUMO

P25705 (Q44-A553)

498  [NCBI]

QKTGTAEMSSILEERILGADTSVDLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLKGMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGEELLGRVVDALGNAIDGKGPIGSKTRRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDTIINQKRFNDGSDEKKKLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDAFGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSRGVRLTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITKFENAFLSHVVSQHQALLGTIRADGKISEQSDAKLKEIVTNFLAGFEA

Approximately 71.2 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.