Igtp
entrez
16145
canonical
uniprot
Q9DCE9
canonical
ensembl
ENSMUSG00000078853
resolver
ensp
ENSMUSP00000047356
resolver
enst
ENSMUST00000035266
resolver
genesymbol
Igtp
resolver
genesymbol_syn
Irgm3
resolver
uniprot
J7PDL1
resolver
uniprot
Q8C2M8
resolver
uniprot_entry
IRGM3_MOUSE
resolver
uniprot_sec
J7PDL1
resolver
uniprot_sec
Q8C2M8
resolver
amino_acid_sequence
MDLVTKLPQNIWKTFTLFINMANYLKRLISPWSKSMTAGESLYSSQNSSSPEVIEDIGKAVTEGNLQKVIGIVKDEIQSKSRYRVKIAVTGDSGNGMSSFINALRFIGHEEEDSAPTGVVRTTKKPACYSSDSHFPYVELWDLPGLGATAQSVESYLEEMQISTFDLIIIVASEQFSSNHVKLAITMQRMRKRFYVVWTKLDRDLSTSTFPEPQLLQSIQRNIRENLQQAQVRDPPLFLISCFSPSFHDFPELRNTLQKDIFSIRYRDPLEIISQVCDKCISNKAFSLKEDQMLMKDLEAAVSSEDDTANLERGLQTYQKLFGVDDGSLQQVARSTGRLEMGSRALQFQDLIKMDRRLELMMCFAVNKFLRLLESSWWYGLWNVVTRYFRHQRHKLVIEIVAENTKTSLRKALKDSVLPPEIH
uniprot
proteins
ec_number
3.6.5.-
uniprot
proteins
function
FUNCTION: Immunity-related GTPase that plays important roles in host resistance to acute infection by protozoan, such as Toxoplasma gondii and Leishmania major (PubMed:10639151, PubMed:11500431, PubMed:12438372, PubMed:16940170, PubMed:18765738). Acts as a dynamin-like protein that binds to intracellular membranes and promotes remodeling and trafficking of those membranes (By similarity). Acts predominantly to restrict acute protozoan infection: expression is required in both hematopoietic and non-hematopoietic cellular compartments and is dependent on Stat1 (PubMed:12438372). Only plays a partial role in the control of latent Toxoplasma infection (PubMed:12438372). Involved in the clearance of acute protozoan infections by regulating autophagy, possibly by promoting the fusion of phagosomes with lysosomes for efficient degradation of vacuoles containing parasites (PubMed:16940170). Probably involved in membrane disruption of parasite-containing vacuoles (PubMed:18765738). In addition to its role in resistance to acute infection by protozoan, also acts as a negative regulator of the integrated stress response (ISR) following coxsackievirus B3 infection (PubMed:21981022). Promotes differentiation of activated CD8(+) T-cells (PubMed:25644000). {ECO:0000250|UniProtKB:Q60766, ECO:0000269|PubMed:10639151, ECO:0000269|PubMed:11500431, ECO:0000269|PubMed:12438372, ECO:0000269|PubMed:16940170, ECO:0000269|PubMed:18765738, ECO:0000269|PubMed:21981022, ECO:0000269|PubMed:25644000}.
uniprot
proteins
mass_dalton
48494
uniprot
proteins
mutagenesis
MUTAGEN 98; /note="S->N: Abolished GTP-binding leading tand GTPase activity without affecting localizatiom to the endoplasmic reticulum."; /evidence="ECO:0000269|PubMed:9099712
uniprot
proteins
protein_family
IRG family
uniprot
proteins
protein_family
TRAFAC class dynamin-like GTPase superfamily
uniprot
proteins
pubmed
10639151
uniprot
proteins
pubmed
11500431
uniprot
proteins
pubmed
12438372
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16940170
uniprot
proteins
pubmed
18765738
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21981022
uniprot
proteins
pubmed
22892676
uniprot
proteins
pubmed
23785284
uniprot
proteins
pubmed
25644000
uniprot
proteins
pubmed
36629440
uniprot
proteins
pubmed
8702776
uniprot
proteins
pubmed
9099712
uniprot
proteins
sequence_length
423
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:18765738, ECO:0000269|PubMed:9099712}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:18765738, ECO:0000269|PubMed:23785284}. Lipid droplet {ECO:0000269|PubMed:23785284}. Note=Delivered to the parasitophorous vacuole via the cell endoplasmic reticulum early after invasion (PubMed:18765738). It then condenses into vesicle-like structures on the vacuole just prior to parasitophorous vacuole disruption (PubMed:18765738). Mainly associates with lipid droplets and 'self' cytoplasmic vacuoles, while it only weakly coats 'non-self' pathogen-containing vacuoles (PubMed:23785284). {ECO:0000269|PubMed:18765738, ECO:0000269|PubMed:23785284}.
uniprot
proteins