protein
ATP synthase peripheral stalk subunit d, mitochondrial
aka ATPase subunit d
Gene
ATP5PD
Organism
Homo sapiens(9606)
Length
161 aa
Mass
18,491 Da
ATP5PD encodes ATP synthase peripheral stalk subunit d, a component of the mitochondrial F₁F₀-ATP synthase complex (Complex V) (UniProt: O75947). This subunit is part of the peripheral stalk, which functions as a stator to stabilize the catalytic core relative to the rotating central stalk during ATP synthesis driven by the proton gradient across the inner mitochondrial membrane.
ATP5PD is expressed in mitochondria-rich tissues where oxidative phosphorylation is active. No baseline diseases are annotated in UniProt for this gene. The protein's role in cellular energy production positions it within core metabolic pathways essential for neuronal function.
This protein has been curated for Alzheimer's Disease relevance based on Chaparral AD proteomics data. Analysis of post-mortem AD brain tissue versus age-matched controls showed ambiguous direction of change across subcellular fractions (mean log2FC +0.68, two fractions measured). The inconsistent regulation across fractions suggests compartment-specific changes in ATP5PD abundance in AD pathology, though no uniform up- or down-regulation pattern emerged (Chaparral AD proteomics).
Generated from the curated entity record below. May contain errors — verify against source links.
Proteomics Evidence · AD
⚠ Ambiguous — detected in AD samples, direction unclear across fractionsP3
-0.711
P2
not detected
S2
+2.073
S3
not detected
Mean log₂FC across detected fractions: +0.6814 (2 of 4 fractions detected)
Human post-mortem AD brain vs age-matched controls, TMT-labeled, 4 subcellular fractions (P2, P3, S2, S3), DDA proteomics.
Related Publications
Browse all →Tau molecular diversity contributes to clinical heterogeneity in Alzheimer's disease.
Dujardin Simon et al.Nature medicine2020PMID 32572268Deep Multilayer Brain Proteomics Identifies Molecular Networks in Alzheimer's Disease Progression.
Bai Bing et al.Neuron2020PMID 31926610A Multi-network Approach Identifies Protein-Specific Co-expression in Asymptomatic and Symptomatic Alzheimer's Disease.
Seyfried Nicholas T et al.Cell systems2017PMID 27989508Large-scale deep multi-layer analysis of Alzheimer's disease brain reveals strong proteomic disease-related changes not observed at the RNA level.
Johnson Erik C B et al.Nature neuroscience2022PMID 35115731Organization and regulation of gene transcription.
Cramer PatrickNature2019PMID 31462772
Function
Subunit d, of the mitochondrial membrane ATP synthase complex (F(1)F(0) ATP synthase or Complex V) that produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain (PubMed:37244256). ATP synthase complex consist of a soluble F(1) head domain - the catalytic core - and a membrane F(1) domain - the membrane proton channel (PubMed:37244256). These two domains are linked by a central stalk rotating inside the F(1) region and a stationary peripheral stalk (PubMed:37244256). During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (Probable). In vivo, can only synthesize ATP although its ATP hydrolase activity can be activated artificially in vitro (By similarity). Part of the complex F(0) domain (PubMed:37244256). Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements (By similarity)
Sources
Last updated 5/8/2026, 6:27:15 AM