Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10090-00054
Entry Name
UniProt Accession
Theoretical PI
7.68
Molecular Weight
11524.49
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Interferon-induced transmembrane protein 1
Protein Synonyms/Alias
Dispanin subfamily A member 2a; DSPA2a; Fragilis protein 2; Mouse ifitm-like protein 2; Mil-2;
Gene Name
Ifitm1
Gene Synonyms/Alias
Created Date
05-OCT-2010
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
49
Canonical
NTLFMNFCCLGFVAY
[1]
S-Palmitoylation
50
Canonical
TLFMNFCCLGFVAYA
[1]
S-Palmitoylation
83
Canonical
AFASTAKCLNISSLF
[1]
S-Palmitoylation
103
Canonical
AIVVIVVCAIR****
[1]
S-Palmitoylation
Organism
Mus musculus (Mouse)
NCBI Taxa ID
10090
Reference
[1] Hach JC, McMichael T, Chesarino NM, Yount JS. Palmitoylation on conserved and nonconserved cysteines of murine IFITM1 regulates its stability andanti-influenza A virus activity. J Virol. 2013 Sep;87(17):9923-7. doi:10.1128/JVI.00621-13. Epub 2013 Jun 26.[PMID:23804635]
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), Ebola virus (EBOV), Dengue virus (DNV) and West Nile virus (WNV). 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. Also implicated in cell adhesion and control of cell growth and migration. Plays a key role in the antiproliferative action of IFN-gamma either by inhibiting the ERK activation or by arresting cell growth in G1 phase in a p53- dependent manner. Acts as a positive regulator of osteoblast differentiation.
Sequence Annotation
Topological domain: 1 35 Cytoplasmic.
Topological domain: 57 84 Cytoplasmic.
Transmembrane: 85 105 Helical.
Topological domain: 106 106 Extracellular.
Protein Length
106 AA.
Protein Sequence
(Canonical)
MPKEQQEVVV LGSPHISTSA TATTINMPEI STPDHVVWSL FNTLFMNFCC LGFVAYAYSV  60
KSRDRKMVGD TTGAQAFAST AKCLNISSLF FTILTAIVVI VVCAIR                 106
FASTA
(Canonical)
>LipidDB-10090-00054|Q9D103
MPKEQQEVVVLGSPHISTSATATTINMPEISTPDHVVWSLFNTLFMNFCCLGFVAYAYSV
KSRDRKMVGDTTGAQAFASTAKCLNISSLFFTILTAIVVIVVCAIR
Gene Ontology
GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW
GO:0005886; C:plasma membrane; IEA:UniProtKB-KW
GO:0009952; P:anterior/posterior pattern specification; IMP:MGI
GO:0051607; P:defense response to virus; IDA:MGI
GO:0030336; P:negative regulation of cell migration; ISS:UniProtKB
GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB
GO:0046597; P:negative regulation of viral entry into host cell; IDA:UniProtKB
GO:0045071; P:negative regulation of viral genome replication; ISS:UniProtKB
GO:0001503; P:ossification; IEA:UniProtKB-KW
GO:0045669; P:positive regulation of osteoblast differentiation; ISS:UniProtKB
GO:0035455; P:response to interferon-alpha; ISS:UniProtKB
GO:0035456; P:response to interferon-beta; ISS:UniProtKB
GO:0034341; P:response to interferon-gamma; ISS:UniProtKB
GO:0009615; P:response to virus; IDA:UniProtKB
GO:0001756; P:somitogenesis; IMP:MGI
Interpro
InterPro; IPR007593; CD225/Dispanin_fam
Pfam
Pfam; PF04505; Dispanin;
SMART
PROSITE
PRINTS