UniProt data
UniProt name: IFM3_HUMAN (Q01628)
Gene name: IFITM3
Organism: Homo sapiens (Human).
Function: IFN-induced antiviral protein which disrupts intracellular cholesterol homeostasis. Inhibits the entry of viruses to the host cell cytoplasm by preventing viral fusion with cholesterol depleted endosomes. May inactivate new enveloped viruses which buds out of the infected cell, by letting them go out with a cholesterol depleted membrane. Active against multiple viruses, including influenza A virus, SARS coronavirus (SARS-CoV), Marburg virus (MARV) and Ebola virus (EBOV), Dengue virus (DNV), West Nile virus (WNV), human immunodeficiency virus type 1 (HIV-1) and vesicular stomatitis virus (VSV). Can inhibit: influenza virus hemagglutinin protein-mediated viral entry, MARV and EBOV GP1,2- mediated viral entry, SARS-CoV S protein-mediated viral entry and VSV G protein-mediated viral entry. Plays a critical role in the structural stability and function of vacuolar ATPase (v-ATPase). Establishes physical contact with the v-ATPase of endosomes which is critical for proper clathrin localization and is also required for the function of the v-ATPase to lower the pH in phagocytic endosomes thus establishing an antiviral state. {ECO:0000269|PubMed:20064371, ECO:0000269|PubMed:20534863, ECO:0000269|PubMed:20943977, ECO:0000269|PubMed:21177806, ECO:0000269|PubMed:21253575, ECO:0000269|PubMed:22046135, ECO:0000269|PubMed:22479637, ECO:0000269|PubMed:23601107}.
Subcellular location: Cell membrane; Single-pass type II membrane protein. Late endosome membrane; Single-pass type II membrane protein. Lysosome membrane; Single-pass type II membrane protein.
Transmembrane domains:
- 108-128, 21 AA, Helical. {ECO:0000255}.
Sequence: 133 AA
CATM prediction
The sequence of IFM3_HUMAN returned 1 potential models
The positions at the dimer's interface are highlighted in yellow. The position at the crossing point is highlighted in orange.
| # | Sequence and interface | d | θ | Z' | ω' | Score |
|---|---|---|---|---|---|---|
| 110 120 13 + | + | + | |
(Å) | (°) | (Å) | (°) | ||
| Model 1 | CLNIWALILGILMTILLIVIAVLIFQA | 7.4 | -50.2° | 3.3 | 47.9 | -29.6 |
| Prolines* | CLNIWALILGILMTILLIVIPVLIFQA |
* Note: this sequence contains Pro residues. CATM substituted them with Ala during the modeling. The positions are marked.
Click on the model number to visualize its details below.
MODEL 1 DETAILS
Precited structure:
Download model 1 structure: PDB, PyMOL session
List of hydrogen bonds:
| Donor | Acceptor | Distance |
|---|---|---|
| B, 111, LEU, HA | A, 110, ALA, O | 3.30Å |
| B, 114, GLY, HA1 | A, 111, LEU, O | 3.32Å |
| B, 115, ILE, HA | A, 118, THR, OG1 | 2.77Å |
| A, 111, LEU, HA | B, 110, ALA, O | 3.30Å |
| A, 114, GLY, HA1 | B, 111, LEU, O | 3.32Å |
| A, 115, ILE, HA | B, 118, THR, OG1 | 2.77Å |

