Overview
| Uniprot ID | Q01915 |
|---|
| Protein Name | ATP synthase subunit alpha, mitochondrial |
|---|
| Gene Name | ATPA |
|---|
| Organism | Glycine max |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 387 |
AAQLKAMKQVCGSLK |
Function
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) 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. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a 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. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity)
Protein Sequence
10
MEFSVRAAEL
20
TTLLESRITN
30
FYTNFQVDEI
40
GRVVSVGDGI
50
ARVYGLNEIQ
60
AGEMVEFASG
70
VKGIALNLEN
80
ENVGIVVFGS
90
DTAIKEGDLV
100
KRTGSIVDVP
110
AGKAMLGRVV
120
DALGVPIDGR
130
GALSDHERRR
140
VEVKAPGIIE
150
RKSVHEPMQT
160
GLKAVDSLVP
170
IGRGQRELII
180
GDRQTGKTAI
190
AIDTILNQKQ
200
MNSRATSESE
210
TLYCVYVAIG
220
QKRSTVAQLV
230
QILSEANALE
240
YSILVAATAS
250
DPAPLQFLAP
260
YSGCAMGEYF
270
RDNGMHALII
280
YDDLSKQAVA
290
YRQMSLLLRR
300
PPGREAFPGD
310
VFYLHSRLLE
320
RAAKRSDQTG
330
AGSLTALPVI
340
ETQAGDVSAY
350
IPTNVISITD
360
GQICLETELF
370
YRGIRPAINV
380
GLSVSRVGSA
390
AQLKAMKQVC
400
GSLKLELAQY
410
REVAAFAQFG
420
SDLDAATQAL
430
LNRGARLTEV
440
LKQPQYAPLP
450
IEKQILVIYA
460
AVNGFCDRMP
470
LDKIPQYERD
480
ILTTIKPELL
490
QSLKGGLTSE
500
RKIELEKFLK
EKGGTYYI
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:0043531 |
ADP binding |
| Molecular Function |
GO:0005524 |
ATP binding |
| Molecular Function |
GO:0046933 |
proton-transporting ATP synthase activity, rotational mechanism |
| Biological Process |
GO:0015986 |
proton motive force-driven ATP synthesis |
Reference
[1] Xu C, Li J, Dong C, Zhang Y, Li H et al.. Lactylome Profiling Reveals the Potential Role of Lysine Lactylation in Regulating Soybean Seed Quality.. J Agric Food Chem 73(23):14666-14676. 2025 Jun 11. PMID: 40440508.