Overview
| Uniprot ID | A0A5G2QT83 |
|---|
| Protein Name | Prohibitin |
|---|
| Gene Name | PHB2 |
|---|
| Organism | Sus scrofa |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 147 |
VLKSVVAKFNASQLI |
| 216 |
RAQFLVEKAKQEQRQ |
| 224 |
AKQEQRQKIVQAEGE |
| 250 |
SKNPGYIKLRKIRAA |
| 262 |
RAAQNISKTIATSQN |
| 6 |
**MAQNLKDLAGRLP |
Function
In the mitochondria, together with PHB, forms large ring complexes (prohibitin complexes) in the inner mitochondrial membrane (IMM) and functions as a chaperone protein that stabilizes mitochondrial respiratory enzymes and maintains mitochondrial integrity in the IMM, which is required for mitochondrial morphogenesis, neuronal survival, and normal lifespan. The prohibitin complex, with DNAJC19, regulates cardiolipin remodeling and the protein turnover of OMA1 in a cardiolipin-binding manner. Also regulates cytochrome-c oxidase assembly (COX) and mitochondrial respiration. Binding to sphingoid 1-phosphate (SPP) modulates its regulator activity. Has a key role of mitophagy receptor involved in targeting mitochondria for autophagic degradation. Involved in mitochondrial-mediated antiviral innate immunity, activates RIG-I-mediated signal transduction and production of IFNB1 and pro-inflammatory cytokine IL6
Protein Sequence
10
MAQNLKDLAG
20
RLPSGPRGMG
30
TALKLLLGAG
40
AVAYGIRESV
50
FTVEGGHRAI
60
FFNRIGGVQQ
70
DTILAEGLHF
80
RIPWFQYPII
90
YDIRARPRKI
100
SSPTGSKDLQ
110
MVNISLRVLS
120
RPNAMELPSM
130
YQRLGLDYEE
140
RVLPSIVNEV
150
LKSVVAKFNA
160
SQLITQRAQV
170
SLLIRRELTE
180
RAKDFSLILD
190
DVAITELSFS
200
REYTAAVEAK
210
QVAQQEAQRA
220
QFLVEKAKQE
230
QRQKIVQAEG
240
EAEAARMLGE
250
ALSKNPGYIK
260
LRKIRAAQNI
270
SKTIATSQNR
280
IYLTADNLVL
290
NLQDESFTRG
SDSLIKSKK
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0009986 |
cell surface |
| Cellular Component |
GO:0005741 |
mitochondrial outer membrane |
| Cellular Component |
GO:0035632 |
mitochondrial prohibitin complex |
| Cellular Component |
GO:0005739 |
mitochondrion |
| Cellular Component |
GO:0016363 |
nuclear matrix |
| Cellular Component |
GO:0005886 |
plasma membrane |
| Molecular Function |
GO:0033218 |
amide binding |
| Molecular Function |
GO:0046982 |
protein heterodimerization activity |
| Molecular Function |
GO:0042803 |
protein homodimerization activity |
| Molecular Function |
GO:0046625 |
sphingolipid binding |
| Biological Process |
GO:0140374 |
antiviral innate immune response |
| Biological Process |
GO:0042113 |
B cell activation |
| Biological Process |
GO:0016477 |
cell migration |
| Biological Process |
GO:0007005 |
mitochondrion organization |
| Biological Process |
GO:0000423 |
mitophagy |
| Biological Process |
GO:0043066 |
negative regulation of apoptotic process |
| Biological Process |
GO:0045892 |
negative regulation of DNA-templated transcription |
| Biological Process |
GO:0070374 |
positive regulation of ERK1 and ERK2 cascade |
| Biological Process |
GO:0002639 |
positive regulation of immunoglobulin production |
| Biological Process |
GO:1901224 |
positive regulation of non-canonical NF-kappaB signal transduction |
| Biological Process |
GO:0006606 |
protein import into nucleus |
| Biological Process |
GO:0050821 |
protein stabilization |
| Biological Process |
GO:1900208 |
regulation of cardiolipin metabolic process |
| Biological Process |
GO:0006357 |
regulation of transcription by RNA polymerase II |
| Biological Process |
GO:0039529 |
RIG-I signaling pathway |
| Biological Process |
GO:0007062 |
sister chromatid cohesion |
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.