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Protein

Interferon alpha/beta receptor 2

Gene

Ifnar2

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

Functioni

Associates with IFNAR1 to form the type I interferon receptor. Receptor for interferons alpha and beta. Involved in IFN-mediated STAT1, STAT2 and STAT3 activation. Isoform 1 and isoform 2 are directly involved in signal transduction due to their association with the TYR kinase, JAK1. Isoform 2 and isoform 3 may be potent inhibitors of type I IFN receptor activity.By similarity2 Publications

GO - Molecular functioni

GO - Biological processi

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 2
Short name:
IFN-R-2
Short name:
IFN-alpha/beta receptor 2
Alternative name(s):
Type I interferon receptor 2
Gene namesi
Name:Ifnar2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:1098243. Ifnar2.

Subcellular locationi

Isoform 1 :
Isoform 2 :
  • Secreted 1 Publication
Isoform 3 :

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini22 – 242221ExtracellularSequence analysisAdd
BLAST
Transmembranei243 – 26321HelicalSequence analysisAdd
BLAST
Topological domaini264 – 513250CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • extracellular space Source: MGI
  • integral component of membrane Source: MGI
  • integral component of plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence analysisAdd
BLAST
Chaini22 – 513492Interferon alpha/beta receptor 2PRO_0000011007Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi39 ↔ 123By similarity
Glycosylationi42 – 421N-linked (GlcNAc...)Sequence analysis
Glycosylationi58 – 581N-linked (GlcNAc...)Sequence analysis
Glycosylationi65 – 651N-linked (GlcNAc...)Sequence analysis
Glycosylationi78 – 781N-linked (GlcNAc...)Sequence analysis
Glycosylationi84 – 841N-linked (GlcNAc...)Sequence analysis
Disulfide bondi85 ↔ 93By similarity
Glycosylationi149 – 1491N-linked (GlcNAc...)Sequence analysis
Glycosylationi191 – 1911N-linked (GlcNAc...)Sequence analysis
Glycosylationi195 – 1951N-linked (GlcNAc...)1 Publication
Disulfide bondi210 ↔ 227By similarity
Modified residuei335 – 3351PhosphotyrosineBy similarity
Modified residuei448 – 4481PhosphoserineCombined sources
Modified residuei465 – 4651PhosphoserineCombined sources
Modified residuei510 – 5101PhosphotyrosineBy similarity

Post-translational modificationi

Phosphorylated on tyrosine residues upon interferon binding. Phosphorylation at Tyr-335 or Tyr-510 are sufficient to mediate interferon dependent activation of STAT1, STAT2 and STAT3 leading to antiproliferative effects on many different cell types (By similarity).By similarity
Glycosylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiO35664.
MaxQBiO35664.
PaxDbiO35664.
PRIDEiO35664.

PTM databases

iPTMnetiO35664.
PhosphoSiteiO35664.

Expressioni

Tissue specificityi

Widely expressed. Detected in liver, testis, kidney, salivary gland, thymus, brain, lung and placenta. Isoform 1, isoform 2 and isoform 3 are expressed in brain.2 Publications

Gene expression databases

BgeeiO35664.
CleanExiMM_IFNAR2.
ExpressionAtlasiO35664. baseline and differential.
GenevisibleiO35664. MM.

Interactioni

Subunit structurei

Heterodimer with IFNAR1. Isoform 1 interacts with the transcriptional factors STAT1 and STAT2. Interacts with JAK1.By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

BioGridi200539. 2 interactions.
IntActiO35664. 2 interactions.
STRINGi10090.ENSMUSP00000023693.

Structurei

3D structure databases

ProteinModelPortaliO35664.
SMRiO35664. Positions 34-239.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the type II cytokine receptor family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IHB9. Eukaryota.
ENOG410YTXY. LUCA.
GeneTreeiENSGT00510000049322.
HOGENOMiHOG000013219.
HOVERGENiHBG052127.
InParanoidiO35664.
KOiK05131.
OMAiPEDPDNV.
OrthoDBiEOG70W3DP.
TreeFamiTF335897.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
InterProiIPR003961. FN3_dom.
IPR013783. Ig-like_fold.
IPR015373. Interferon/interleukin_rcp_dom.
[Graphical view]
PfamiPF09294. Interfer-bind. 1 hit.
PF01108. Tissue_fac. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 2 hits.

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O35664-1) [UniParc]FASTAAdd to basket

Also known as: IFNaR2c

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MRSRCTVSAV GLLSLCLVVS ASLETITPSA FDGYPDEPCT INITIRNSRL
60 70 80 90 100
ILSWELENKS GPPANYTLWY TVMSKDENLT KVKNCSDTTK SSCDVTDKWL
110 120 130 140 150
EGMESYVVAI VIVHRGDLTV CRCSDYIVPA NAPLEPPEFE IVGFTDHINV
160 170 180 190 200
TMEFPPVTSK IIQEKMKTTP FVIKEQIGDS VRKKHEPKVN NVTGNFTFVL
210 220 230 240 250
RDLLPKTNYC VSLYFDDDPA IKSPLKCIVL QPGQESGLSE SAIVGITTSC
260 270 280 290 300
LVVMVFVSTI VMLKRIGYIC LKDNLPNVLN FRHFLTWIIP ERSPSEAIDR
310 320 330 340 350
LEIIPTNKKK RLWNYDYEDG SDSDEEVPTA SVTGYTMHGL TGKPLQQTSD
360 370 380 390 400
TSASPEDPLH EEDSGAEESD EAGAGAGAEP ELPTEAGAGP SEDPTGPYER
410 420 430 440 450
RKSVLEDSFP REDNSSMDEP GDNIIFNVNL NSVFLRVLHD EDASETLSLE
460 470 480 490 500
EDTILLDEGP QRTESDLRIA GGDRTQPPLP SLPSQDLWTE DGSSEKSDTS
510
DSDADVGDGY IMR
Length:513
Mass (Da):56,578
Last modified:July 27, 2011 - v2
Checksum:i7A645DA5F33C9EA0
GO
Isoform 2 (identifier: O35664-2) [UniParc]FASTAAdd to basket

Also known as: IFNaR2b

The sequence of this isoform differs from the canonical sequence as follows:
     237-247: GLSESAIVGIT → ELPPLFNLDNP
     248-513: Missing.

Note: Probable soluble receptor.
Show »
Length:247
Mass (Da):27,610
Checksum:i4957A16710C2D2D1
GO
Isoform 3 (identifier: O35664-3) [UniParc]FASTAAdd to basket

Also known as: IFNaR2a

The sequence of this isoform differs from the canonical sequence as follows:
     238-248: LSESAIVGITT → MARFLKFALLF
     249-513: Missing.

Note: Probable soluble receptor.
Show »
Length:248
Mass (Da):27,755
Checksum:i47D6008193F7BC3C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti160 – 1601K → Q in CAA70992 (PubMed:9322767).Curated
Sequence conflicti276 – 2761P → S in CAA70992 (PubMed:9322767).Curated
Sequence conflicti339 – 3391G → E in AAC53351 (PubMed:9295335).Curated
Sequence conflicti429 – 4291N → S in AAC53351 (PubMed:9295335).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei237 – 24711GLSESAIVGIT → ELPPLFNLDNP in isoform 2. 1 PublicationVSP_050345Add
BLAST
Alternative sequencei238 – 24811LSESAIVGITT → MARFLKFALLF in isoform 3. 2 PublicationsVSP_050346Add
BLAST
Alternative sequencei248 – 513266Missing in isoform 2. 1 PublicationVSP_050347Add
BLAST
Alternative sequencei249 – 513265Missing in isoform 3. 2 PublicationsVSP_050348Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y09813 mRNA. Translation: CAA70943.1.
Y09864 mRNA. Translation: CAA70991.1.
Y09865 mRNA. Translation: CAA70992.1.
AF013274 mRNA. Translation: AAC53351.1.
AF013486 mRNA. Translation: AAC53352.1.
AF367979 Genomic DNA. Translation: AAK73024.1.
AK139169 mRNA. Translation: BAE23909.1.
AK151474 mRNA. Translation: BAE30430.1.
AK152878 mRNA. Translation: BAE31563.1.
AK153317 mRNA. Translation: BAE31897.1.
CH466602 Genomic DNA. Translation: EDL03831.1.
BC071225 mRNA. Translation: AAH71225.1.
CCDSiCCDS28325.1. [O35664-1]
CCDS49910.1. [O35664-3]
RefSeqiNP_001103968.1. NM_001110498.1. [O35664-3]
NP_034639.2. NM_010509.2. [O35664-1]
XP_006522986.1. XM_006522923.2. [O35664-2]
UniGeneiMm.6834.

Genome annotation databases

EnsembliENSMUST00000023693; ENSMUSP00000023693; ENSMUSG00000022971. [O35664-1]
ENSMUST00000089042; ENSMUSP00000086443; ENSMUSG00000022971. [O35664-2]
ENSMUST00000117836; ENSMUSP00000113358; ENSMUSG00000022971. [O35664-3]
GeneIDi15976.
KEGGimmu:15976.
UCSCiuc007zxh.2. mouse. [O35664-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y09813 mRNA. Translation: CAA70943.1.
Y09864 mRNA. Translation: CAA70991.1.
Y09865 mRNA. Translation: CAA70992.1.
AF013274 mRNA. Translation: AAC53351.1.
AF013486 mRNA. Translation: AAC53352.1.
AF367979 Genomic DNA. Translation: AAK73024.1.
AK139169 mRNA. Translation: BAE23909.1.
AK151474 mRNA. Translation: BAE30430.1.
AK152878 mRNA. Translation: BAE31563.1.
AK153317 mRNA. Translation: BAE31897.1.
CH466602 Genomic DNA. Translation: EDL03831.1.
BC071225 mRNA. Translation: AAH71225.1.
CCDSiCCDS28325.1. [O35664-1]
CCDS49910.1. [O35664-3]
RefSeqiNP_001103968.1. NM_001110498.1. [O35664-3]
NP_034639.2. NM_010509.2. [O35664-1]
XP_006522986.1. XM_006522923.2. [O35664-2]
UniGeneiMm.6834.

3D structure databases

ProteinModelPortaliO35664.
SMRiO35664. Positions 34-239.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200539. 2 interactions.
IntActiO35664. 2 interactions.
STRINGi10090.ENSMUSP00000023693.

PTM databases

iPTMnetiO35664.
PhosphoSiteiO35664.

Proteomic databases

EPDiO35664.
MaxQBiO35664.
PaxDbiO35664.
PRIDEiO35664.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000023693; ENSMUSP00000023693; ENSMUSG00000022971. [O35664-1]
ENSMUST00000089042; ENSMUSP00000086443; ENSMUSG00000022971. [O35664-2]
ENSMUST00000117836; ENSMUSP00000113358; ENSMUSG00000022971. [O35664-3]
GeneIDi15976.
KEGGimmu:15976.
UCSCiuc007zxh.2. mouse. [O35664-1]

Organism-specific databases

CTDi3455.
MGIiMGI:1098243. Ifnar2.

Phylogenomic databases

eggNOGiENOG410IHB9. Eukaryota.
ENOG410YTXY. LUCA.
GeneTreeiENSGT00510000049322.
HOGENOMiHOG000013219.
HOVERGENiHBG052127.
InParanoidiO35664.
KOiK05131.
OMAiPEDPDNV.
OrthoDBiEOG70W3DP.
TreeFamiTF335897.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiIfnar2. mouse.
PROiO35664.
SOURCEiSearch...

Gene expression databases

BgeeiO35664.
CleanExiMM_IFNAR2.
ExpressionAtlasiO35664. baseline and differential.
GenevisibleiO35664. MM.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
InterProiIPR003961. FN3_dom.
IPR013783. Ig-like_fold.
IPR015373. Interferon/interleukin_rcp_dom.
[Graphical view]
PfamiPF09294. Interfer-bind. 1 hit.
PF01108. Tissue_fac. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mammalian type I interferon receptors consists of two subunits: IFNaR1 and IFNaR2."
    Kim S.H., Cohen B., Novick D., Rubinstein M.
    Gene 196:279-286(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), ALTERNATIVE SPLICING, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Strain: C57BL/6J.
    Tissue: Brain.
  2. "Cloning and characterization of soluble and transmembrane isoforms of a novel component of the murine type I interferon receptor, IFNAR 2."
    Owczarek C.M., Hwang S.Y., Holland K.A., Gulluyan L.M., Tavaria M., Weaver B., Reich N.C., Kola I., Hertzog P.J.
    J. Biol. Chem. 272:23865-23870(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Lung and Testis.
  3. "Multiple regions within the promoter of the murine Ifnar-2 gene confer basal and inducible expression."
    Hardy M.P., Hertzog P.J., Owczarek C.M.
    Biochem. J. 365:355-367(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: 129/SvJ.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Bone marrow and Cerebellum.
  5. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Salivary gland.
  7. "Proteome-wide characterization of N-glycosylation events by diagonal chromatography."
    Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.
    J. Proteome Res. 5:2438-2447(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-195.
    Strain: C57BL/6J.
    Tissue: Plasma.
  8. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448 AND SER-465, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Spleen.

Entry informationi

Entry nameiINAR2_MOUSE
AccessioniPrimary (citable) accession number: O35664
Secondary accession number(s): O35238
, O35663, O35983, Q923Z5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 14, 2003
Last sequence update: July 27, 2011
Last modified: June 8, 2016
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.