IFNAR1
The protein encoded by this gene is a type I membrane protein that forms one of the two chains of a receptor for interferons alpha and beta. Binding and activation of the receptor stimulates Janus protein kinases, which in turn phosphorylate several proteins, including STAT1 and STAT2. The encoded protein also functions as an antiviral factor. [provided by RefSeq, Jul 2008]
Full Name
Interferon Alpha And Beta Receptor Subunit 1
Function
Component of the receptor for type I interferons, including interferons alpha, IFNB1 and IFNW1 (PubMed:2153461, PubMed:7665574, PubMed:10049744, PubMed:14532120, PubMed:15337770, PubMed:21854986).
Functions in general as heterodimer with IFNAR2 (PubMed:7665574, PubMed:10049744, PubMed:21854986).
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 (PubMed:7665574, PubMed:21854986, PubMed:32972995).
Can form an active IFNB1 receptor by itself and activate a signaling cascade that does not involve activation of the JAK-STAT pathway (By similarity).
Biological Process
Cellular response to interferon-alpha Source: UniProtKB
Cytokine-mediated signaling pathway Source: GO_Central
Positive regulation of cellular respiration Source: ARUK-UCL
Receptor signaling pathway via JAK-STAT Source: ProtInc
Response to lipopolysaccharide Source: UniProtKB
Response to virus Source: ProtInc
Type I interferon signaling pathway Source: UniProtKB
Cellular Location
Isoform 1: Lysosome; Cell membrane; Late endosome. Interferon binding triggers internalization of the receptor from the cell membrane into endosomes and then into lysosomes.
Topology
Extracellular: 28-436
Helical: 437-457
Cytoplasmic: 458-557
PTM
Ubiquitinated, leading to its internalization and degradation (PubMed:14532120, PubMed:15337770). Polyubiquitinated via 'Lys-48'-linked and 'Lys-63'-linked ubiquitin chains, leading to receptor internalization and lysosomal degradation (PubMed:18056411). The 'Lys-63'-linked ubiquitin chains are cleaved off by the BRISC complex (PubMed:24075985).
Phosphorylated on serine residues in response to interferon binding; this promotes interaction with FBXW11 and ubiquitination (PubMed:14532120, PubMed:15337770, PubMed:24075985). Phosphorylated on tyrosine residues by TYK2 tyrosine kinase (PubMed:7526154). Phosphorylated on tyrosine residues in response to interferon (PubMed:10049744).
Palmitoylation at Cys-463 is required for the activation of STAT1 and STAT2.
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