Overview
| Uniprot ID | P80021 |
| Protein Name | ATP synthase F(1) complex subunit alpha, mitochondrial |
| Gene Name | ATP5F1A |
| Organism | Sus scrofa |
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 126 |
FGNDKLIKEGDIVKR |
| 132 |
IKEGDIVKRTGAIVD |
| 161 |
LGNAIDGKGPIGSKT |
| 167 |
GKGPIGSKTRRRVGL |
| 175 |
TRRRVGLKAPGIIPR |
| 218 |
IGDRQTGKTSIAIDT |
| 230 |
IDTIINQKRFNDGTD |
| 239 |
FNDGTDEKKKLYCIY |
| 261 |
STVAQLVKRLTDADA |
| 305 |
EYFRDNGKHALIIYD |
| 316 |
IIYDDLSKQAVAYRQ |
| 498 |
GVRGYLDKLEPSKIT |
| 525 |
QHQALLGKIRADGKI |
| 531 |
GKIRADGKISEETDA |
| 539 |
ISEETDAKLKEIVTN |
Function
Subunit alpha, 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 (By similarity). In vivo, can only synthesize ATP although its ATP hydrolase activity can be activated artificially in vitro (By similarity). With the catalytic subunit beta (ATP5F1B), forms the catalytic core in the F(1) domain. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity)
Protein Sequence
10
MLSVRVAAAV
20
ARALPRRAGL
30
VSKNALGSSF
40
VAARNLHASN
50
TRLQKTGTAE
60
VSSILEERIL
70
GADTSVDLEE
80
TGRVLSIGDG
90
IARVHGLRNV
100
QAEEMVEFSS
110
GLKGMSLNLE
120
PDNVGVVVFG
130
NDKLIKEGDI
140
VKRTGAIVDV
150
PVGEELLGRV
160
VDALGNAIDG
170
KGPIGSKTRR
180
RVGLKAPGII
190
PRISVREPMQ
200
TGIKAVDSLV
210
PIGRGQRELI
220
IGDRQTGKTS
230
IAIDTIINQK
240
RFNDGTDEKK
250
KLYCIYVAIG
260
QKRSTVAQLV
270
KRLTDADAMK
280
YTIVVSATAS
290
DAAPLQYLAP
300
YSGCSMGEYF
310
RDNGKHALII
320
YDDLSKQAVA
330
YRQMSLLLRR
340
PPGREAYPGD
350
VFYLHSRLLE
360
RAAKMNDAFG
370
GGSLTALPVI
380
ETQAGDVSAY
390
IPTNVISITD
400
GQIFLETELF
410
YKGIRPAINV
420
GLSVSRVGSA
430
AQTRAMKQVA
440
GTMKLELAQY
450
REVAAFAQFG
460
SDLDAATQQL
470
LSRGVRLTEL
480
LKQGQYAPMA
490
IEEQVAVIYA
500
GVRGYLDKLE
510
PSKITKFENA
520
FLSHVISQHQ
530
ALLGKIRADG
540
KISEETDAKL
550
KEIVTNFLAG
FEA
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005743 |
mitochondrial inner membrane |
| Cellular Component |
GO:0005886 |
plasma 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:0046872 |
metal ion binding |
| Molecular Function |
GO:0046933 |
proton-transporting ATP synthase activity, rotational mechanism |
| Biological Process |
GO:0015986 |
proton motive force-driven ATP synthesis |
Reference
[1] Fan S, Zhou R, Wen H, Ye H, Ma S et al.. Global profiling of protein lactylome in porcine granulosa cells.. J Ovarian Res 18(1):177. 2025 Aug 8. PMID: 40781717.