Overview
| Uniprot ID | A0A8D0MI69 |
|---|
| Protein Name | ATP synthase subunit b |
|---|
| Gene Name | ATP5PB |
|---|
| Organism | Sus scrofa |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 131 |
ADKLNEQKIAQLEEV |
| 139 |
IAQLEEVKQASIKQI |
| 144 |
EVKQASIKQIQDAID |
| 162 |
SQQALVQKRHYLFDV |
| 221 |
HMIRWVEKHVVQSIS |
| 233 |
SISAQQEKETIAKCI |
| 238 |
QEKETIAKCIADLKL |
| 244 |
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
MLSRVVLSAA
20
AAAAPSLKNA
30
ALLGPGVLQA
40
TRIFHTGQPS
50
LAPVPPLPEH
60
GGKVRLGLIP
70
EEFFQFLYPK
80
TGVTGPYVLG
90
TGLILYLLSK
100
EIYVITAETF
110
SAISTIGVLV
120
YIVKKYGASI
130
GAFADKLNEQ
140
KIAQLEEVKQ
150
ASIKQIQDAI
160
DLEKSQQALV
170
QKRHYLFDVQ
180
RNNIAMALEV
190
TYRERLHRVY
200
KEIKNRLDYH
210
ISVQNMMRQK
220
EQEHMIRWVE
230
KHVVQSISAQ
240
QEKETIAKCI
250
ADLKLLAKKA
QAQPVL
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:0015986 |
proton motive force-driven ATP synthesis |
| Biological Process |
GO:0042776 |
proton motive force-driven mitochondrial 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.