Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10090-00143
Entry Name
UniProt Accession
Theoretical PI
6.89
Molecular Weight
14954.34
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Interferon-induced transmembrane protein 3
Protein Synonyms/Alias
Dispanin subfamily A member 2b; DSPA2b; Fragilis protein; Interferon-inducible protein 15; Mouse ifitm-like protein 1; Mil-1;
Gene Name
Ifitm3
Gene Synonyms/Alias
Created Date
05-OCT-2010
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
71
Canonical
NTLFMNFCCLGFIAY
[1]
S-Palmitoylation
72
Canonical
TLFMNFCCLGFIAYA
[1]
S-Palmitoylation
105
Canonical
AYASTAKCLNISTLV
[1]
S-Palmitoylation
Organism
Mus musculus (Mouse)
NCBI Taxa ID
10090
Reference
[1] Predicted from GPS-Lipid
Functional Description
IFN-induced antiviral protein which inhibits the entry of viruses to the host cell cytoplasm, permitting endocytosis, but preventing subsequent viral fusion and release of viral contents into the cytosol. 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) and human immunodeficiency virus type 1 (HIV-1). Can inhibit: influenza virus hemagglutinin protein-mediated viral entry, MARV and EBOV GP1,2-mediated viral entry and SARS-CoV S 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. Involved in initiating germ cell competence and specification, and in the demarcation of PGCs from their somatic neighbors.
Sequence Annotation
Topological domain: 1 57 Cytoplasmic.
Topological domain: 79 109 Cytoplasmic.
Transmembrane: 110 130 Helical.
Topological domain: 131 137 Extracellular.
Region: 60 93 Interaction with SPP1.
Modified residue: 27 27 Phosphotyrosine.
Protein Length
137 AA.
Protein Sequence
(Canonical)
MNHTSQAFIT AASGGQPPNY ERIKEEYEVA EMGAPHGSAS VRTTVINMPR EVSVPDHVVW  60
SLFNTLFMNF CCLGFIAYAY SVKSRDRKMV GDVTGAQAYA STAKCLNIST LVLSILMVVI  120
TIVSVIIIVL NAQNLHT                                                 137
FASTA
(Canonical)
>LipidDB-10090-00143|Q9CQW9
MNHTSQAFITAASGGQPPNYERIKEEYEVAEMGAPHGSASVRTTVINMPREVSVPDHVVW
SLFNTLFMNFCCLGFIAYAYSVKSRDRKMVGDVTGAQAYASTAKCLNISTLVLSILMVVI
TIVSVIIIVLNAQNLHT
Gene Ontology
GO:0045177; C:apical part of cell; IDA:MGI
GO:0009986; C:cell surface; IDA:MGI
GO:0005737; C:cytoplasm; IDA:MGI
GO:0016023; C:cytoplasmic membrane-bounded vesicle; IDA:MGI
GO:0005783; C:endoplasmic reticulum; IDA:MGI
GO:0005768; C:endosome; IEA:UniProtKB-KW
GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW
GO:0005764; C:lysosome; IEA:UniProtKB-KW
GO:0005634; C:nucleus; IDA:MGI
GO:0005886; C:plasma membrane; IEA:UniProtKB-KW
GO:0051607; P:defense response to virus; IDA:MGI
GO:0008285; P:negative regulation of cell proliferation; IDA:MGI
GO:0046597; P:negative regulation of viral entry into host cell; IDA:UniProtKB
GO:0009615; P:response to virus; IDA:UniProtKB
GO:0060337; P:type I interferon signaling pathway; IDA:MGI
Interpro
InterPro; IPR007593; CD225/Dispanin_fam
Pfam
Pfam; PF04505; Dispanin;
SMART
PROSITE
PRINTS