Irgm
entrez
303090
canonical
uniprot
Q6AYC2
canonical
ensembl
ENSRNOG00000031138
resolver
ensembl
ENSRNOG00055018146
resolver
ensembl
ENSRNOG00060017821
resolver
ensembl
ENSRNOG00065005918
resolver
ensp
ENSRNOP00000047579
resolver
ensp
ENSRNOP00000094495
resolver
ensp
ENSRNOP00000099006
resolver
ensp
ENSRNOP00055024714
resolver
ensp
ENSRNOP00060024649
resolver
ensp
ENSRNOP00065006316
resolver
enst
ENSRNOT00000045545
resolver
enst
ENSRNOT00000106065
resolver
enst
ENSRNOT00000127882
resolver
enst
ENSRNOT00055030723
resolver
enst
ENSRNOT00060030495
resolver
enst
ENSRNOT00065008897
resolver
genesymbol
Irgm
resolver
genesymbol_syn
Ifggd3
resolver
uniprot
A0A8I6AM97
resolver
uniprot
J7NUQ1
resolver
uniprot_entry
A0A8I6AM97_RAT
resolver
uniprot_entry
IRGM_RAT
resolver
uniprot_entry
J7NUQ1_RAT
resolver
amino_acid_sequence
MKPSHKSCEAAPLLPKMPETSTHNAPLNLSFPSVPSYQIGCSSLPEISRSTERALKEGKLPELVYGVKETVATLSQIPVSIFVTGDSGNGMSSFINALRIIGHEEDASAPTGVVRTTQTRAEYSSSHFPNVVLWDLPGLGATAQTVENYIEEMKFSTCDLFIIVASEQFSSNHVKLAKIIQSMGKRFYVIWTKLDRDLSTSVLSEVRLIQNIQENIRENLQKEGVKEVPIFLVSNLDPLLHDFPELRNTLQTDLSNIRCCEPLKTLYVIYEKIIGDKVANWNQIIANGRLKSSLGVRDDDDMGECLKRYRLIFGIDDESLQQIAHGMGTVVMEYKANIKSQDFHTLRRADWKLRLMTCTTVNALFCLFKFLPCLCHCFKRMRHKRMLLLVAKDTKNILKKILMDAVSPPQI
uniprot
proteins
ec_number
3.6.5.-
uniprot
proteins
function
FUNCTION: Immunity-related GTPase that plays important roles in innate immunity and inflammatory response (By similarity). Acts as a dynamin-like protein that binds to intracellular membranes and promotes remodeling and trafficking of those membranes (By similarity). Required for clearance of acute protozoan and bacterial infections by interacting with autophagy and lysosome regulatory proteins, thereby promoting the fusion of phagosomes with lysosomes for efficient degradation of cargo including microbes (By similarity). Regulates selective autophagy, including xenophagy and mitophagy, both directly and indirectly (By similarity). Directly regulates autophagy by acting as a molecular adapter that promotes the coassembly of the core autophagy machinery to mediate antimicrobial defense: Irgm (1) activates AMPK, which in turn phosphorylates ULK1 and BECN1 to induce autophagy, (2) promotes the coassembly of ULK1 and BECN1, enhancing BECN1-interacting partners and (3) influences the composition of the BECN1 complex, by competing with the negative regulators BCL2 and RUBCN, to trigger autophagy (By similarity). Also activates autophagy by promoting recruitment of STX17 to autophagosomes (By similarity). In collaboration with ATG8 proteins, regulate lysosomal biogenesis, a fundamental process for any autophagic pathway, by promoting TFEB dephosphorylation (By similarity). Also modulates autophagy by assisting with autophagosome formation and preventing lysosomal deacidification (By similarity). Regulates autophagy by affecting mitochondrial fusion and fission (By similarity). Also involved in M1 macrophage activation for the production of proinflammatory cytokines (By similarity). While activating autophagy, acts as a key negative regulator of the inflammatory and interferon responses both by (1) promoting mitophagy and (2) mediating autophagy-dependent degradation of effectors of the inflammatory response (By similarity). Promotes degradation of damaged and IFNG/IFN-gamma-stressed mitochondria via mitophagy, preventing cytosolic release of ligands that activate inflammation (By similarity). Negatively regulates interferon-signaling in hematopoietic stem cells, preserving hematopoietic stem cell number and function (By similarity). Promotes expansion of activated CD4(+) T-cells by inhibiting IFNG/IFN-gamma signaling, thereby preventing Ifng-mediated cell death of CD4(+) T-cells (By similarity). Acts as a suppressor of inflammation by promoting recruitment of inflammation effectors, such as CGAS, RIGI/RIG-I and NLRP3, to autophagosome membranes, leading to their SQSTM1/p62-dependent autophagic degradation (By similarity). Also directly inhibits assembly of the NLRP3 inflammasome by preventing the association between NLRP3 and PYCARD (By similarity). Acts as a negative regulator of antiviral innate immune response by suppressing the RIPK2-dependent pro-inflammatory response: mediates recruitment of RIPosomes, composed of RIPK2 and NOD1 or NOD2, to autophagosome membranes, promoting their SQSTM1/p62-dependent autophagic degradation (By similarity). {ECO:0000250|UniProtKB:A1A4Y4, ECO:0000250|UniProtKB:Q60766}.
uniprot
proteins
mass_dalton
46338
uniprot
proteins
post_translational_modification
PTM: Palmitoylated on C-terminal Cys residues. Palmitoylation, together with the alpha-K amphipathic helix, which binds phosphatidylinositol, mediate binding to membranes. {ECO:0000250|UniProtKB:Q60766}.; PTM: Ubiquitinated via 'Lys-63'-linked polyubiquitination in a NOD2-dependent process. 'Lys-63'-linked polyubiquitination is required for interactions with the core autophagy factors (By similarity). Ubiquitination at Lys-272 by the DCX(WDR77) complex, also named CLR4(WDR77) complex, in intestinal cells, leading to its degradation by the proteasome (By similarity). {ECO:0000250|UniProtKB:A1A4Y4, ECO:0000250|UniProtKB:Q60766}.
uniprot
proteins
protein_family
IRG family
uniprot
proteins
protein_family
TRAFAC class dynamin-like GTPase superfamily
uniprot
proteins
pubmed
15489334
uniprot
proteins
sequence_length
411
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q60766}. Cell membrane {ECO:0000250|UniProtKB:Q60766}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:Q60766}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:Q60766}. Lysosome membrane {ECO:0000250|UniProtKB:Q60766}. Late endosome membrane {ECO:0000250|UniProtKB:Q60766}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q60766}. Cell projection, phagocytic cup {ECO:0000250|UniProtKB:Q60766}. Note=Behaves like an integral membrane protein. Recruited to the plasma membrane around forming phagocytic cups, it remains associated with maturing phagosomes. Association with phagosomes is dependent on nucleotide-binding but is IFNG-independent. Also detected in late endosomes and lysosomes: lysosomal localization is IFN-gamma-induced during bacterial infections such as S.typhimurium infection. {ECO:0000250|UniProtKB:Q60766}.
uniprot
proteins