Overview
| Uniprot ID | P00848 |
|---|
| Protein Name | ATP synthase F(0) complex subunit a |
|---|
| Gene Name | Mtatp6 |
|---|
| Organism | Mus musculus |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 55 |
WLVKLIIKQMMLIHT |
Function
Subunit a, 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. With the subunit c (ATP5MC1), forms the proton-conducting channel in the F(0) domain, that contains two crucial half-channels (inlet and outlet) that facilitate proton movement from the mitochondrial intermembrane space (IMS) into the matrix. Protons are taken up via the inlet half-channel and released through the outlet half-channel, following a Grotthuss mechanism
Protein Sequence
10
MNENLFASFI
20
TPTMMGFPIV
30
VAIIMFPSIL
40
FPSSKRLINN
50
RLHSFQHWLV
60
KLIIKQMMLI
70
HTPKGRTWTL
80
MIVSLIMFIG
90
STNLLGLLPH
100
TFTPTTQLSM
110
NLSMAIPLWA
120
GAVITGFRHK
130
LKSSLAHFLP
140
QGTPISLIPM
150
LIIIETISLF
160
IQPMALAVRL
170
TANITAGHLL
180
MHLIGGATLV
190
LMNISPPTAT
200
ITFIILLLLT
210
ILEFAVALIQ
220
AYVFTLLVSL
YLHDNT
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:0015252 |
proton channel activity |
| Molecular Function |
GO:0046933 |
proton-transporting ATP synthase activity, rotational mechanism |
| Biological Process |
GO:0015986 |
proton motive force-driven ATP synthesis |
| Biological Process |
GO:0042776 |
proton motive force-driven mitochondrial ATP synthesis |
| Biological Process |
GO:1902600 |
proton transmembrane transport |
| Biological Process |
GO:0055093 |
response to hyperoxia |
Reference
[1] Wu D, Tang Y, Li X, Xiong S, Zhang Z et al.. Characterization of protein lactylation in healthy and ischemic mouse hearts.. Front Cardiovasc Med 12:1644886. 2025. PMID: 41089239.