Ifngr1
entrez
15979
canonical
uniprot
P15261
canonical
ensembl
ENSMUSG00000020009
resolver
ensp
ENSMUSP00000020188
resolver
enst
ENSMUST00000020188
resolver
genesymbol
Ifngr1
resolver
genesymbol_syn
Ifngr
resolver
uniprot
Q91Y85
resolver
uniprot_entry
INGR1_MOUSE
resolver
uniprot_sec
Q91Y85
resolver
amino_acid_sequence
MGPQAAAGRMILLVVLMLSAKVGSGALTSTEDPEPPSVPVPTNVLIKSYNLNPVVCWEYQNMSQTPIFTVQVKVYSGSWTDSCTNISDHCCNIYEQIMYPDVSAWARVKAKVGQKESDYARSKEFLMCLKGKVGPPGLEIRRKKEEQLSVLVFHPEVVVNGESQGTMFGDGSTCYTFDYTVYVEHNRSGEILHTKHTVEKEECNETLCELNISVSTLDSRYCISVDGISSFWQVRTEKSKDVCIPPFHDDRKDSIWILVVAPLTVFTVVILVFAYWYTKKNSFKRKSIMLPKSLLSVVKSATLETKPESKYSLVTPHQPAVLESETVICEEPLSTVTAPDSPEAAEQEELSKETKALEAGGSTSAMTPDSPPTPTQRRSFSLLSSNQSGPCSLTAYHSRNGSDSGLVGSGSSISDLESLPNNNSETKMAEHDPPPVRKAPMASGYDKPHMLVDVLVDVGGKESLMGYRLTGEAQELS
uniprot
proteins
function
FUNCTION: Receptor subunit for interferon gamma/INFG that plays crucial roles in antimicrobial, antiviral, and antitumor responses by activating effector immune cells and enhancing antigen presentation (, PubMed:20926559, PubMed:27286456). Associates with transmembrane accessory factor IFNGR2 to form a functional receptor (PubMed:2137461, PubMed:2530216, PubMed:2530582, PubMed:2531896, PubMed:2532365). Upon ligand binding, the intracellular domain of IFNGR1 opens out to allow association of downstream signaling components JAK1 and JAK2. In turn, activated JAK1 phosphorylates IFNGR1 to form a docking site for STAT1. Subsequent phosphorylation of STAT1 leads to its dimerization, translocation to the nucleus, and stimulation of target gene transcription (PubMed:19889125). STAT3 can also be activated in a similar manner although activation seems weaker (PubMed:15284232). IFNGR1 intracellular domain phosphorylation also provides a docking site for SOCS1 that regulates the JAK-STAT pathway by competing with STAT1 binding to IFNGR1 (PubMed:15522878). {ECO:0000269|PubMed:15284232, ECO:0000269|PubMed:19889125, ECO:0000269|PubMed:20926559, ECO:0000269|PubMed:2137461, ECO:0000269|PubMed:2530216, ECO:0000269|PubMed:2530582, ECO:0000269|PubMed:2531896, ECO:0000269|PubMed:2532365, ECO:0000269|PubMed:27286456}.
uniprot
proteins
mass_dalton
52343
uniprot
proteins
mutagenesis
MUTAGEN 445; /note="Y->F: Complete loss of STAT1 and STAT3 activation."; /evidence="ECO:0000269|PubMed:15284232"; MUTAGEN 467; /note="Y->F: Complete loss of interaction with SOCS1."; /evidence="ECO:0000269|PubMed:15522878
uniprot
proteins
post_translational_modification
PTM: Phosphorylated at Ser/Thr residues. Phosphorylation of Tyr-445 is required for IFNG receptor signal transduction. Influenza virus infection leads to phosphorylation in a CSNK1A1-dependent manner. {ECO:0000250|UniProtKB:P15260}.; PTM: Ubiquitinated after phosphorylation in a CSNK1A1-dependent manner, leading to the lysosome-dependent degradation. Proteasomally degraded through 'Lys-48'-mediated ubiquitination. Ubiquitination is necessary for efficient IFNGR1 signaling. {ECO:0000250|UniProtKB:P15260}.
uniprot
proteins
protein_family
Type II cytokine receptor family
uniprot
proteins
pubmed
15284232
uniprot
proteins
pubmed
15522878
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
19889125
uniprot
proteins
pubmed
20926559
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
2137461
uniprot
proteins
pubmed
2530216
uniprot
proteins
pubmed
2530582
uniprot
proteins
pubmed
2531896
uniprot
proteins
pubmed
2532365
uniprot
proteins
pubmed
27286456
uniprot
proteins
pubmed
7890167
uniprot
proteins
sequence_length
477
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2137461, ECO:0000269|PubMed:2530216, ECO:0000269|PubMed:2530582, ECO:0000269|PubMed:2531896, ECO:0000269|PubMed:2532365}; Single-pass type I membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 255..275; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins