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Protein

Interferon alpha/beta receptor 1

Gene

Ifnar1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the receptor for type I interferons, including interferons alpha, IFNB1 and IFNW1 (PubMed:1533935, PubMed:14532120, PubMed:23872679). Functions in general as heterodimer with IFNAR2 (By similarity). 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:14532120). Can form an active IFNB1 receptor by itself and activate a signaling cascade that does not involve activation of the JAK-STAT pathway (PubMed:23872679). Contributes to modulate the innate immune response to bacterial lipopolysaccharide (PubMed:23872679).By similarity4 Publications

GO - Molecular functioni

  • interferon receptor activity Source: MGI
  • type I interferon binding Source: UniProtKB
  • type I interferon receptor activity Source: UniProtKB

GO - Biological processi

  • cellular response to interferon-alpha Source: UniProtKB
  • defense response to virus Source: MGI
  • positive regulation of interferon-beta production Source: CACAO
  • positive regulation of interferon-gamma production Source: MGI
  • positive regulation of interleukin-1 beta secretion Source: MGI
  • positive regulation of transcription, DNA-templated Source: CACAO
  • regulation of peptidyl-tyrosine phosphorylation Source: MGI
  • regulation of type I interferon-mediated signaling pathway Source: Reactome
  • response to lipopolysaccharide Source: UniProtKB
  • T cell activation Source: MGI
  • type I interferon biosynthetic process Source: MGI
  • type I interferon signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Enzyme and pathway databases

ReactomeiR-MMU-909733. Interferon alpha/beta signaling.
R-MMU-912694. Regulation of IFNA signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Interferon alpha/beta receptor 1
Short name:
IFN-R-1
Short name:
IFN-alpha/beta receptor 1
Alternative name(s):
Type I interferon receptor 1
Gene namesi
Name:Ifnar1
Synonyms:Ifar, Ifnar
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:107658. Ifnar1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini27 – 429403ExtracellularSequence analysisAdd
BLAST
Transmembranei430 – 44920HelicalSequence analysisAdd
BLAST
Topological domaini450 – 590141CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of plasma membrane Source: UniProtKB
  • late endosome Source: UniProtKB-SubCell
  • lysosome Source: UniProtKB-SubCell
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endosome, Lysosome, Membrane

Pathology & Biotechi

Disruption phenotypei

Mice are protected from the lethal septic effects of intraperitoneal LPS administration observed in wild-type mice (PubMed:23872679). Double knockout with TREX1 does not show a visible phenotype (PubMed:18724932).2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi526 – 5261S → A: Abolishes interaction with FBXW11. Prevents interalization from the cell membrane and lysosomal degradation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Sequence analysisAdd
BLAST
Chaini27 – 590564Interferon alpha/beta receptor 1PRO_0000011002Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi43 – 431N-linked (GlcNAc...)Sequence analysis
Disulfide bondi78 ↔ 86By similarity
Glycosylationi109 – 1091N-linked (GlcNAc...)Sequence analysis
Glycosylationi181 – 1811N-linked (GlcNAc...)Sequence analysis
Disulfide bondi199 ↔ 2201 Publication
Glycosylationi214 – 2141N-linked (GlcNAc...)Sequence analysis
Disulfide bondi284 ↔ 2921 Publication
Glycosylationi314 – 3141N-linked (GlcNAc...)Sequence analysis
Glycosylationi370 – 3701N-linked (GlcNAc...)Sequence analysis
Disulfide bondi397 ↔ 4191 Publication
Glycosylationi409 – 4091N-linked (GlcNAc...)Sequence analysis
Glycosylationi413 – 4131N-linked (GlcNAc...)Sequence analysis
Modified residuei526 – 5261Phosphoserine1 Publication

Post-translational modificationi

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.By similarity1 Publication
Phosphorylated on serine residues in response to interferon binding; this promotes interaction with FBXW11 and ubiquitination (PubMed:14532120). Phosphorylated on tyrosine residues by TYK2 tyrosine kinase. Phosphorylated on tyrosine residues in response to interferon (By similarity).By similarity1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP33896.
PaxDbiP33896.
PRIDEiP33896.

PTM databases

iPTMnetiP33896.
PhosphoSiteiP33896.

Expressioni

Gene expression databases

BgeeiENSMUSG00000022967.
CleanExiMM_IFNAR1.
ExpressionAtlasiP33896. baseline and differential.
GenevisibleiP33896. MM.

Interactioni

Subunit structurei

Heterodimer with IFNAR2. Interacts (serine-phosphorylated form) with FBXW11, the substrate recognition component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex (PubMed:14532120). Interacts with SHMT2; this promotes interaction with FAM175B and the BRISC complex (By similarity). Interacts with TYK2 (By similarity).By similarityCurated1 Publication

GO - Molecular functioni

  • type I interferon binding Source: UniProtKB

Protein-protein interaction databases

IntActiP33896. 4 interactions.
MINTiMINT-1513172.
STRINGi10090.ENSMUSP00000023689.

Structurei

Secondary structure

1
590
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi38 – 403Combined sources
Beta strandi43 – 453Combined sources
Helixi122 – 1254Combined sources
Beta strandi126 – 1283Combined sources
Beta strandi132 – 1376Combined sources
Beta strandi142 – 1476Combined sources
Beta strandi149 – 1524Combined sources
Beta strandi154 – 1563Combined sources
Turni157 – 1626Combined sources
Beta strandi164 – 17310Combined sources
Beta strandi178 – 18912Combined sources
Beta strandi197 – 2059Combined sources
Beta strandi207 – 2104Combined sources
Beta strandi219 – 2224Combined sources
Beta strandi236 – 2394Combined sources
Beta strandi241 – 2477Combined sources
Beta strandi261 – 2644Combined sources
Helixi265 – 2695Combined sources
Beta strandi282 – 2909Combined sources
Beta strandi292 – 2954Combined sources
Turni296 – 2983Combined sources
Beta strandi301 – 3077Combined sources
Beta strandi323 – 3264Combined sources
Beta strandi337 – 3426Combined sources
Beta strandi347 – 3526Combined sources
Beta strandi354 – 3563Combined sources
Beta strandi362 – 3698Combined sources
Beta strandi376 – 38712Combined sources
Beta strandi395 – 4039Combined sources
Beta strandi418 – 4214Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3WCYX-ray2.90A27-429[»]
ProteinModelPortaliP33896.
SMRiP33896. Positions 35-426.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini31 – 12595Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini127 – 226100Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini230 – 32798Fibronectin type-III 3PROSITE-ProRule annotationAdd
BLAST
Domaini332 – 42594Fibronectin type-III 4PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni483 – 49210Important for interaction with TYK2By similarity

Sequence similaritiesi

Belongs to the type II cytokine receptor family.Curated
Contains 4 fibronectin type-III domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IKIP. Eukaryota.
ENOG4111QEU. LUCA.
GeneTreeiENSGT00530000063449.
HOGENOMiHOG000113067.
HOVERGENiHBG052126.
InParanoidiP33896.
KOiK05130.
OMAiVYCVKAR.
OrthoDBiEOG091G04H5.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
InterProiIPR003961. FN3_dom.
IPR013783. Ig-like_fold.
IPR015373. Interferon/interleukin_rcp_dom.
IPR016669. Interferon_alpha/beta_rcpt-1.
[Graphical view]
PfamiPF09294. Interfer-bind. 2 hits.
PF01108. Tissue_fac. 1 hit.
[Graphical view]
PIRSFiPIRSF016567. IFN_alpha/beta_recept-1. 1 hit.
SMARTiSM00060. FN3. 3 hits.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 4 hits.
PROSITEiPS50853. FN3. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P33896-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLAVVGAAAL VLVAGAPWVL PSAAGGENLK PPENIDVYII DDNYTLKWSS
60 70 80 90 100
HGESMGSVTF SAEYRTKDEA KWLKVPECQH TTTTKCEFSL LDTNVYIKTQ
110 120 130 140 150
FRVRAEEGNS TSSWNEVDPF IPFYTAHMSP PEVRLEAEDK AILVHISPPG
160 170 180 190 200
QDGNMWALEK PSFSYTIRIW QKSSSDKKTI NSTYYVEKIP ELLPETTYCL
210 220 230 240 250
EVKAIHPSLK KHSNYSTVQC ISTTVANKMP VPGNLQVDAQ GKSYVLKWDY
260 270 280 290 300
IASADVLFRA QWLPGYSKSS SGSRSDKWKP IPTCANVQTT HCVFSQDTVY
310 320 330 340 350
TGTFFLHVQA SEGNHTSFWS EEKFIDSQKH ILPPPPVITV TAMSDTLLVY
360 370 380 390 400
VNCQDSTCDG LNYEIIFWEN TSNTKISMEK DGPEFTLKNL QPLTVYCVQA
410 420 430 440 450
RVLFRALLNK TSNFSEKLCE KTRPGSFSTI WIITGLGVVF FSVMVLYALR
460 470 480 490 500
SVWKYLCHVC FPPLKPPRSI DEFFSEPPSK NLVLLTAEEH TERCFIIENT
510 520 530 540 550
DTVAVEVKHA PEEDLRKYSS QTSQDSGNYS NEEEESVGTE SGQAVLSKAP
560 570 580 590
CGGPCSVPSP PGTLEDGTCF LGNEKYLQSP ALRTEPALLC
Length:590
Mass (Da):65,796
Last modified:July 27, 2011 - v2
Checksum:iE887ADFA6DFEAF3C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti274 – 2741R → H in AAA37890 (PubMed:1533935).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M89641 mRNA. Translation: AAA37890.1.
AK132431 mRNA. Translation: BAE21165.1.
AK141630 mRNA. Translation: BAE24775.1.
CH466602 Genomic DNA. Translation: EDL03825.1.
BC043935 mRNA. Translation: AAH43935.1.
BC052429 mRNA. Translation: AAH52429.1.
CCDSiCCDS28326.1.
PIRiA45283.
RefSeqiNP_034638.2. NM_010508.2.
UniGeneiMm.502.

Genome annotation databases

EnsembliENSMUST00000023689; ENSMUSP00000023689; ENSMUSG00000022967.
ENSMUST00000117748; ENSMUSP00000112670; ENSMUSG00000022967.
ENSMUST00000123196; ENSMUSP00000119160; ENSMUSG00000022967.
GeneIDi15975.
KEGGimmu:15975.
UCSCiuc007zxn.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M89641 mRNA. Translation: AAA37890.1.
AK132431 mRNA. Translation: BAE21165.1.
AK141630 mRNA. Translation: BAE24775.1.
CH466602 Genomic DNA. Translation: EDL03825.1.
BC043935 mRNA. Translation: AAH43935.1.
BC052429 mRNA. Translation: AAH52429.1.
CCDSiCCDS28326.1.
PIRiA45283.
RefSeqiNP_034638.2. NM_010508.2.
UniGeneiMm.502.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3WCYX-ray2.90A27-429[»]
ProteinModelPortaliP33896.
SMRiP33896. Positions 35-426.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP33896. 4 interactions.
MINTiMINT-1513172.
STRINGi10090.ENSMUSP00000023689.

PTM databases

iPTMnetiP33896.
PhosphoSiteiP33896.

Proteomic databases

MaxQBiP33896.
PaxDbiP33896.
PRIDEiP33896.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000023689; ENSMUSP00000023689; ENSMUSG00000022967.
ENSMUST00000117748; ENSMUSP00000112670; ENSMUSG00000022967.
ENSMUST00000123196; ENSMUSP00000119160; ENSMUSG00000022967.
GeneIDi15975.
KEGGimmu:15975.
UCSCiuc007zxn.2. mouse.

Organism-specific databases

CTDi3454.
MGIiMGI:107658. Ifnar1.

Phylogenomic databases

eggNOGiENOG410IKIP. Eukaryota.
ENOG4111QEU. LUCA.
GeneTreeiENSGT00530000063449.
HOGENOMiHOG000113067.
HOVERGENiHBG052126.
InParanoidiP33896.
KOiK05130.
OMAiVYCVKAR.
OrthoDBiEOG091G04H5.

Enzyme and pathway databases

ReactomeiR-MMU-909733. Interferon alpha/beta signaling.
R-MMU-912694. Regulation of IFNA signaling.

Miscellaneous databases

ChiTaRSiIfnar1. mouse.
PROiP33896.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000022967.
CleanExiMM_IFNAR1.
ExpressionAtlasiP33896. baseline and differential.
GenevisibleiP33896. MM.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
InterProiIPR003961. FN3_dom.
IPR013783. Ig-like_fold.
IPR015373. Interferon/interleukin_rcp_dom.
IPR016669. Interferon_alpha/beta_rcpt-1.
[Graphical view]
PfamiPF09294. Interfer-bind. 2 hits.
PF01108. Tissue_fac. 1 hit.
[Graphical view]
PIRSFiPIRSF016567. IFN_alpha/beta_recept-1. 1 hit.
SMARTiSM00060. FN3. 3 hits.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 4 hits.
PROSITEiPS50853. FN3. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiINAR1_MOUSE
AccessioniPrimary (citable) accession number: P33896
Secondary accession number(s): Q80UJ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: July 27, 2011
Last modified: September 7, 2016
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

The interferon signaling pathway is not identical between species. Thus, the interaction with STAT1 and STAT2 may not be conserved in mouse; in human it requires phosphorylation at 'Tyr-466', but the mouse protein has a Phe at the equivalent position. Likewise, cysteine palmitoylation is required for the activation of STAT1 and STAT2 in human, but the Cys is not conserved in mouse.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.