Overview
| Uniprot ID | B3SP85 |
|---|
| Protein Name | Gamma-interferon-inducible-lysosomal thiol reductase |
|---|
| Gene Name | IFI30 |
|---|
| Organism | Sus scrofa |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 132 |
VEACLLDKLEKNMAF |
Function
Lysosomal thiol reductase that catalyzes protein disulfide bonds reduction. Plays an important role in antigen processing and presentation, of namely both major histocompatibility complex (MHC) class I- and class II-restricted antigen by reducing the disulfide bonds of endocytosed proteins and facilitating their unfolding and optimal degradation. Shares with thioredoxin a reduction mechanism in which the N-terminal cysteine thiol group in the CXXC active site motif initiates a nucleophilic attack on the substrate disulfide bond,resulting in the formation of a mixed disulfide-linked enzyme-substrate intermediate. Subsequent intramolecular attack by the second cysteine thiol group enables the release of the reduced substrate and oxidized enzyme. Lysosomal cysteine is a physiological reducing agent that is capable of reducing IFI30, so that it can catalyzes the next reaction. Dithiothreitol, cysteine, and cysteinyl glycine, but not glutathione, are capable of regenerating active precursor and mature IFI30 in vitro
Protein Sequence
10
MASSPLLPFL
20
PLLLLLLLEV
30
PAAAPASPLQ
40
SLLQGAAPCK
50
AGEPCLQRPV
60
GKSDPPPVNV
70
NLYYESLCNG
80
CRYFLVRELF
90
PTWLMVWEIL
100
NVTLVPYGNA
110
QERNVSGRWE
120
FTCQHGEQEC
130
KMNKVEACLL
140
DKLEKNMAFL
150
TIVCIEELDD
160
MEKNLEPCLQ
170
IYAPKVSPDS
180
IMECAMGDRG
190
MQLLHINAQL
200
TDALKPPHEY
210
VPWVVVNGKP
220
MTEKDQLLRL
230
VCQLYEGEKP
240
DVCQILASSH
KEVCFK
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005576 |
extracellular region |
| Cellular Component |
GO:0005764 |
lysosome |
| Molecular Function |
GO:0016671 |
oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor |
| Biological Process |
GO:0042590 |
antigen processing and presentation of exogenous peptide antigen via MHC class I |
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.