Interferon-induced transmembrane protein 3

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:

  1. 108-128, 21 AA, Helical. {ECO:0000255}.

Sequence: 133 AA

10 20 30 40 50 60 MNHTVQTFFS PVNSGQPPNY EMLKEEHEVA VLGAPHNPAP PTSTVIHIRS ETSVPDHVVW 70 80 90 100 110 120 SLFNTLFMNP CCLGFIAFAY SVKSRDRKMV GDVTGAQAYA STAKCLNIWA LILGILMTIL 130 LIVIPVLIFQ AYG

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) (°)  
CLNIWALILGILMTILLIVIAVLIFQA 7.4 -50.2° 3.3 47.9 -29.6
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:


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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