Ifnar1
entrez
15975
canonical
uniprot
P33896
canonical
ensembl
ENSMUSG00000022967
resolver
ensp
ENSMUSP00000023689
resolver
ensp
ENSMUSP00000112670
resolver
enst
ENSMUST00000023689
resolver
enst
ENSMUST00000117748
resolver
genesymbol
Ifnar1
resolver
genesymbol_syn
Ifar
resolver
genesymbol_syn
Ifnar
resolver
uniprot
Q80UJ3
resolver
uniprot_entry
INAR1_MOUSE
resolver
uniprot_sec
Q80UJ3
resolver
amino_acid_sequence
MLAVVGAAALVLVAGAPWVLPSAAGGENLKPPENIDVYIIDDNYTLKWSSHGESMGSVTFSAEYRTKDEAKWLKVPECQHTTTTKCEFSLLDTNVYIKTQFRVRAEEGNSTSSWNEVDPFIPFYTAHMSPPEVRLEAEDKAILVHISPPGQDGNMWALEKPSFSYTIRIWQKSSSDKKTINSTYYVEKIPELLPETTYCLEVKAIHPSLKKHSNYSTVQCISTTVANKMPVPGNLQVDAQGKSYVLKWDYIASADVLFRAQWLPGYSKSSSGSRSDKWKPIPTCANVQTTHCVFSQDTVYTGTFFLHVQASEGNHTSFWSEEKFIDSQKHILPPPPVITVTAMSDTLLVYVNCQDSTCDGLNYEIIFWENTSNTKISMEKDGPEFTLKNLQPLTVYCVQARVLFRALLNKTSNFSEKLCEKTRPGSFSTIWIITGLGVVFFSVMVLYALRSVWKYLCHVCFPPLKPPRSIDEFFSEPPSKNLVLLTAEEHTERCFIIENTDTVAVEVKHAPEEDLRKYSSQTSQDSGNYSNEEEESVGTESGQAVLSKAPCGGPCSVPSPPGTLEDGTCFLGNEKYLQSPALRTEPALLC
uniprot
proteins
function
FUNCTION: Together with IFNAR2, forms the heterodimeric receptor for type I interferons (including interferons alpha, beta, epsilon, omega and kappa) (PubMed:14532120, PubMed:1533935, PubMed:24075985). Type I interferon binding activates the JAK-STAT signaling cascade, and triggers tyrosine phosphorylation of a number of proteins including JAKs, TYK2, STAT proteins and the IFNR alpha- and beta-subunits themselves (By similarity). STAT proteins are then phosphorylated by the JAKs, promoting their translocation into the nucleus to regulate expression of interferon-regulated genes (By similarity). Can also act independently of IFNAR2: form an active IFNB1 receptor by itself and activate a signaling cascade that does not involve activation of the JAK-STAT pathway (PubMed:23872679). {ECO:0000250|UniProtKB:P17181, ECO:0000269|PubMed:14532120, ECO:0000269|PubMed:1533935, ECO:0000269|PubMed:23872679, ECO:0000269|PubMed:24075985}.
uniprot
proteins
mass_dalton
65796
uniprot
proteins
mutagenesis
MUTAGEN 526; /note="S->A: Abolishes interaction with FBXW11. Prevents interalization from the cell membrane and lysosomal degradation."; /evidence="ECO:0000269|PubMed:14532120
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated (PubMed:14532120). This leads to its internalization and lysosomal degradation. The 'Lys-63'-linked ubiquitin chains are cleaved off by the BRISC complex; this prevents receptor internalization and degradation. Probable ubiquitination sites have been identified in human, but are poorly conserved across species. {ECO:0000250|UniProtKB:P17181, ECO:0000269|PubMed:14532120}.; PTM: Phosphorylated on serine residues in response to interferon binding; this promotes interaction with FBXW11 and ubiquitination (PubMed:14532120). {ECO:0000269|PubMed:14532120}.
uniprot
proteins
protein_family
Type II cytokine receptor family
uniprot
proteins
pubmed
14532120
uniprot
proteins
pubmed
1533935
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
18724932
uniprot
proteins
pubmed
23872679
uniprot
proteins
pubmed
24075985
uniprot
proteins
pubmed
7958966
uniprot
proteins
sequence_length
590
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14532120, ECO:0000269|PubMed:1533935, ECO:0000269|PubMed:24075985}; Single-pass type I membrane protein {ECO:0000305}. Late endosome {ECO:0000305|PubMed:14532120}. Lysosome {ECO:0000305|PubMed:14532120}. Note=Interferon binding triggers internalization of the receptor from the cell membrane into endosomes and then into lysosomes. {ECO:0000305|PubMed:14532120, ECO:0000305|PubMed:24075985}.
uniprot
proteins
transmembrane_region
TRANSMEM 430..449; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins