Overview
| Uniprot ID | A0A5G2RAC9 |
| Protein Name | ATP synthase subunit b |
| Gene Name | ATP5PB |
| Organism | Sus scrofa |
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 113 |
ADKLNEQKIAQLEEV |
| 121 |
IAQLEEVKQASIKQI |
| 126 |
EVKQASIKQIQDAID |
| 144 |
SQQALVQKRHYLFDV |
| 203 |
HMIRWVEKHVVQSIS |
| 215 |
SISAQQEKETIAKCI |
| 220 |
QEKETIAKCIADLKL |
| 226 |
AKCIADLKLLAKKAQ |
Function
Subunit b, 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
ICIIATYRVL
20
QATRIFHTGQ
30
PSLAPVPPLP
40
EHGGKVRLGL
50
IPEEFFQFLY
60
PKTGVTGPYV
70
LGTGLILYLL
80
SKEIYVITAE
90
TFSAISTIGV
100
LVYIVKKYGA
110
SIGAFADKLN
120
EQKIAQLEEV
130
KQASIKQIQD
140
AIDLEKSQQA
150
LVQKRHYLFD
160
VQRNNIAMAL
170
EVTYRERLHR
180
VYKEIKNRLD
190
YHISVQNMMR
200
QKEQEHMIRW
210
VEKHVVQSIS
220
AQQEKETIAK
230
CIADLKLLAK
KAQAQPVL
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:0015078 |
proton transmembrane transporter activity |
| 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.