Overview
| Uniprot ID | A0A286XZ92 |
|---|
| Protein Name | ATP synthase peripheral stalk subunit d, mitochondrial |
|---|
| Gene Name | ATP5PD |
|---|
| Organism | Cavia porcellus |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 117 |
ARIVEYEKQLEKMNN |
| 63 |
YYKANVAKAGLVDEF |
| 95 |
ALVDAEEKEDVKSCA |
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. ATP synthase complex consist of a soluble F(1) head domain - the catalytic core - and a membrane F(1) domain - the membrane proton channel. These two domains are linked by a central stalk rotating inside the F(1) region and a stationary peripheral stalk. 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. In vivo, can only synthesize ATP although its ATP hydrolase activity can be activated artificially in vitro. Part of the complex F(0) domain. 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
Protein Sequence
10
MAGRKLTLKA
20
IDWVAFGQII
30
PANQKAVANS
40
LKSWNESLSS
50
RLAALSEKPP
60
AIDWAYYKAN
70
VAKAGLVDEF
80
EKKFNALKVP
90
VPEDKYTALV
100
DAEEKEDVKS
110
CAEFVSLSKA
120
RIVEYEKQLE
130
KMNNIIPFDQ
140
MTIEDLNEVF
150
PETKLDKKKY
160
PYWPHQPIEN
L
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005743 |
mitochondrial inner membrane |
| Cellular Component |
GO:0045259 |
proton-transporting ATP synthase complex |
| Molecular Function |
GO:0046933 |
proton-transporting ATP synthase activity, rotational mechanism |
| Biological Process |
GO:0042776 |
proton motive force-driven mitochondrial ATP synthesis |
Reference
[1] Feng J, Chen X, Li R, Xie Y, Zhang X et al.. Lactylome analysis reveals potential target modified proteins in the retina of form-deprivation myopia.. iScience 27(9):110606. 2024 Sep 20. PMID: 39246443.