Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00997
Entry Name
UniProt Accession
Theoretical PI
6.49
Molecular Weight
14632.1
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Interferon-induced transmembrane protein 3
Protein Synonyms/Alias
Dispanin subfamily A member 2b; DSPA2b; Interferon-inducible protein 1-8U;
Gene Name
IFITM3
Gene Synonyms/Alias
Created Date
01-JUL-1993
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
71
Canonical
NTLFMNPCCLGFIAF
[1]
S-Palmitoylation
72
Canonical
TLFMNPCCLGFIAFA
[1]
S-Palmitoylation
105
Canonical
AYASTAKCLNIWALI
[1]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Yount JS, Moltedo B, Yang YY, Charron G, Moran TM, López CB, Hang HC.Palmitoylome profiling reveals S-palmitoylation-dependent antiviral activity ofIFITM3. Nat Chem Biol. 2010 Aug;6(8):610-4. doi: 10.1038/nchembio.405. Epub 2010 Jul 4.[PMID:20601941]
Functional Description
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.
Sequence Annotation
Topological domain: 1 57 Cytoplasmic.
Topological domain: 79 107 Cytoplasmic.
Transmembrane: 108 128 Helical.
Topological domain: 129 133 Extracellular.
Region: 60 93 Interaction with SPP1.
Region: 108 133 Interaction with VAPA.
Protein Length
133 AA.
Protein Sequence
(Canonical)
MNHTVQTFFS PVNSGQPPNY EMLKEEHEVA VLGAPHNPAP PTSTVIHIRS ETSVPDHVVW  60
SLFNTLFMNP CCLGFIAFAY SVKSRDRKMV GDVTGAQAYA STAKCLNIWA LILGILMTIL  120
LIVIPVLIFQ AYG                                                     133
FASTA
(Canonical)
>LipidDB-9606-00997|Q01628
MNHTVQTFFSPVNSGQPPNYEMLKEEHEVAVLGAPHNPAPPTSTVIHIRSETSVPDHVVW
SLFNTLFMNPCCLGFIAFAYSVKSRDRKMVGDVTGAQAYASTAKCLNIWALILGILMTIL
LIVIPVLIFQAYG
Gene Ontology
GO:0005768; C:endosome; IEA:UniProtKB-KW
GO:0070062; C:extracellular vesicular exosome; IDA:UniProt
GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW
GO:0005764; C:lysosome; IEA:UniProtKB-KW
GO:0005886; C:plasma membrane; IDA:UniProtKB
GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome
GO:0051607; P:defense response to virus; IEA:UniProtKB-KW
GO:0006955; P:immune response; TAS:ProtInc
GO:0046597; P:negative regulation of viral entry into host cell; IDA:UniProtKB
GO:0045071; P:negative regulation of viral genome replication; IDA:UniProtKB
GO:0032897; P:negative regulation of viral transcription; IDA:UniProtKB
GO:0035455; P:response to interferon-alpha; IDA:UniProtKB
GO:0035456; P:response to interferon-beta; IDA:UniProtKB
GO:0034341; P:response to interferon-gamma; IDA:UniProtKB
GO:0009615; P:response to virus; IDA:UniProtKB
GO:0060337; P:type I interferon signaling pathway; TAS:Reactome
Interpro
InterPro; IPR007593; CD225/Dispanin_fam
Pfam
Pfam; PF04505; Dispanin;
SMART
PROSITE
PRINTS