INAR2_MOUSE
ID INAR2_MOUSE Reviewed; 513 AA.
AC O35664; O35238; O35663; O35983; Q923Z5;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Interferon alpha/beta receptor 2;
DE Short=IFN-R-2;
DE Short=IFN-alpha/beta receptor 2;
DE AltName: Full=Type I interferon receptor 2;
DE Flags: Precursor;
GN Name=Ifnar2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), ALTERNATIVE SPLICING,
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=9322767; DOI=10.1016/s0378-1119(97)00240-0;
RA Kim S.H., Cohen B., Novick D., Rubinstein M.;
RT "Mammalian type I interferon receptors consists of two subunits: IFNaR1 and
RT IFNaR2.";
RL Gene 196:279-286(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), FUNCTION, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Lung, and Testis;
RX PubMed=9295335; DOI=10.1074/jbc.272.38.23865;
RA Owczarek C.M., Hwang S.Y., Holland K.A., Gulluyan L.M., Tavaria M.,
RA Weaver B., Reich N.C., Kola I., Hertzog P.J.;
RT "Cloning and characterization of soluble and transmembrane isoforms of a
RT novel component of the murine type I interferon receptor, IFNAR 2.";
RL J. Biol. Chem. 272:23865-23870(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=129/SvJ;
RX PubMed=11939908; DOI=10.1042/bj20020105;
RA Hardy M.P., Hertzog P.J., Owczarek C.M.;
RT "Multiple regions within the promoter of the murine Ifnar-2 gene confer
RT basal and inducible expression.";
RL Biochem. J. 365:355-367(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Cerebellum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Salivary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-195.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=16944957; DOI=10.1021/pr060186m;
RA Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.;
RT "Proteome-wide characterization of N-glycosylation events by diagonal
RT chromatography.";
RL J. Proteome Res. 5:2438-2447(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448 AND SER-465, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Associates with IFNAR1 to form the plasma membrane receptor
CC in the type I interferon signaling pathway. Directly involved in signal
CC transduction through its association with the TYR kinase JAK1. Involved
CC in interferon-mediated STAT1, STAT2 and STAT3 activation.
CC {ECO:0000250|UniProtKB:P48551}.
CC -!- FUNCTION: [Isoform 2]: May be potent inhibitors of type I IFN receptor
CC activity. {ECO:0000305|PubMed:9295335, ECO:0000305|PubMed:9322767}.
CC -!- FUNCTION: [Isoform 3]: May be potent inhibitors of type I IFN receptor
CC activity. {ECO:0000305|PubMed:9295335, ECO:0000305|PubMed:9322767}.
CC -!- SUBUNIT: Heterodimer with IFNAR1. Interacts with the transcriptional
CC factors STAT1 and STAT2. Interacts with JAK1. Interacts with USP18;
CC indirectly via STAT2, it negatively regulates the assembly of the
CC ternary interferon-IFNAR1-IFNAR2 complex and therefore type I
CC interferon signaling. {ECO:0000250|UniProtKB:P48551}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane
CC {ECO:0000305|PubMed:9295335, ECO:0000305|PubMed:9322767}; Single-pass
CC type I membrane protein {ECO:0000305|PubMed:9322767}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted
CC {ECO:0000305|PubMed:9322767}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Secreted
CC {ECO:0000305|PubMed:9295335, ECO:0000305|PubMed:9322767}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=IFNaR2c;
CC IsoId=O35664-1; Sequence=Displayed;
CC Name=2; Synonyms=IFNaR2b;
CC IsoId=O35664-2; Sequence=VSP_050345, VSP_050347;
CC Name=3; Synonyms=IFNaR2a;
CC IsoId=O35664-3; Sequence=VSP_050346, VSP_050348;
CC -!- TISSUE SPECIFICITY: Widely expressed. Detected in liver, testis,
CC kidney, salivary gland, thymus, brain, lung and placenta. Isoform 1,
CC isoform 2 and isoform 3 are expressed in brain.
CC {ECO:0000269|PubMed:9295335, ECO:0000269|PubMed:9322767}.
CC -!- PTM: Phosphorylated on tyrosine residues upon interferon binding.
CC Phosphorylation at Tyr-335 or Tyr-510 are sufficient to mediate
CC interferon dependent activation of STAT1, STAT2 and STAT3 leading to
CC antiproliferative effects on many different cell types (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Glycosylated. {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 2]: Probable soluble receptor. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Probable soluble receptor. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the type II cytokine receptor family.
CC {ECO:0000305}.
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DR EMBL; Y09813; CAA70943.1; -; mRNA.
DR EMBL; Y09864; CAA70991.1; -; mRNA.
DR EMBL; Y09865; CAA70992.1; -; mRNA.
DR EMBL; AF013274; AAC53351.1; -; mRNA.
DR EMBL; AF013486; AAC53352.1; -; mRNA.
DR EMBL; AF367979; AAK73024.1; -; Genomic_DNA.
DR EMBL; AK139169; BAE23909.1; -; mRNA.
DR EMBL; AK151474; BAE30430.1; -; mRNA.
DR EMBL; AK152878; BAE31563.1; -; mRNA.
DR EMBL; AK153317; BAE31897.1; -; mRNA.
DR EMBL; CH466602; EDL03831.1; -; Genomic_DNA.
DR EMBL; BC071225; AAH71225.1; -; mRNA.
DR CCDS; CCDS28325.1; -. [O35664-1]
DR CCDS; CCDS49910.1; -. [O35664-3]
DR CCDS; CCDS84262.1; -. [O35664-2]
DR RefSeq; NP_001103968.1; NM_001110498.1. [O35664-3]
DR RefSeq; NP_001334187.1; NM_001347258.1. [O35664-2]
DR RefSeq; NP_034639.2; NM_010509.2. [O35664-1]
DR AlphaFoldDB; O35664; -.
DR SMR; O35664; -.
DR BioGRID; 200539; 2.
DR IntAct; O35664; 2.
DR STRING; 10090.ENSMUSP00000023693; -.
DR GlyGen; O35664; 8 sites.
DR iPTMnet; O35664; -.
DR PhosphoSitePlus; O35664; -.
DR jPOST; O35664; -.
DR MaxQB; O35664; -.
DR PaxDb; O35664; -.
DR PeptideAtlas; O35664; -.
DR PRIDE; O35664; -.
DR ProteomicsDB; 266986; -. [O35664-1]
DR ProteomicsDB; 266987; -. [O35664-2]
DR ProteomicsDB; 266988; -. [O35664-3]
DR Antibodypedia; 34938; 441 antibodies from 35 providers.
DR DNASU; 15976; -.
DR Ensembl; ENSMUST00000023693; ENSMUSP00000023693; ENSMUSG00000022971. [O35664-1]
DR Ensembl; ENSMUST00000089042; ENSMUSP00000086443; ENSMUSG00000022971. [O35664-2]
DR Ensembl; ENSMUST00000117836; ENSMUSP00000113358; ENSMUSG00000022971. [O35664-3]
DR GeneID; 15976; -.
DR KEGG; mmu:15976; -.
DR UCSC; uc007zxh.2; mouse. [O35664-1]
DR CTD; 3455; -.
DR MGI; MGI:1098243; Ifnar2.
DR VEuPathDB; HostDB:ENSMUSG00000022971; -.
DR eggNOG; ENOG502S60E; Eukaryota.
DR GeneTree; ENSGT00510000049322; -.
DR HOGENOM; CLU_040302_0_0_1; -.
DR InParanoid; O35664; -.
DR OMA; PSAECPW; -.
DR OrthoDB; 680035at2759; -.
DR TreeFam; TF335897; -.
DR Reactome; R-MMU-909733; Interferon alpha/beta signaling.
DR Reactome; R-MMU-912694; Regulation of IFNA/IFNB signaling.
DR BioGRID-ORCS; 15976; 12 hits in 79 CRISPR screens.
DR ChiTaRS; Ifnar2; mouse.
DR PRO; PR:O35664; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; O35664; protein.
DR Bgee; ENSMUSG00000022971; Expressed in granulocyte and 245 other tissues.
DR ExpressionAtlas; O35664; baseline and differential.
DR Genevisible; O35664; MM.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; TAS:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0019962; F:type I interferon binding; ISO:MGI.
DR GO; GO:0004905; F:type I interferon receptor activity; IDA:MGI.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
DR GO; GO:0033080; P:immature T cell proliferation in thymus; IDA:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0035455; P:response to interferon-alpha; ISS:UniProtKB.
DR GO; GO:0035456; P:response to interferon-beta; ISS:UniProtKB.
DR GO; GO:0060337; P:type I interferon signaling pathway; ISO:MGI.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR015373; Interferon/interleukin_rcp_dom.
DR Pfam; PF09294; Interfer-bind; 1.
DR Pfam; PF01108; Tissue_fac; 1.
DR SUPFAM; SSF49265; SSF49265; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Membrane; Phosphoprotein; Receptor; Reference proteome; Secreted; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..513
FT /note="Interferon alpha/beta receptor 2"
FT /id="PRO_0000011007"
FT TOPO_DOM 22..242
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 264..513
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 334..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..444
FT /note="Mediates interaction with STAT2 (and required for
FT the recruitment of USP18)"
FT /evidence="ECO:0000250|UniProtKB:P48551"
FT REGION 458..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..354
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 335
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P48551"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48551"
FT MOD_RES 448
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 510
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P48551"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 58
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957"
FT DISULFID 39..123
FT /evidence="ECO:0000250|UniProtKB:P48551"
FT DISULFID 85..93
FT /evidence="ECO:0000250|UniProtKB:P48551"
FT DISULFID 210..227
FT /evidence="ECO:0000250|UniProtKB:P48551"
FT VAR_SEQ 237..247
FT /note="GLSESAIVGIT -> ELPPLFNLDNP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9322767"
FT /id="VSP_050345"
FT VAR_SEQ 238..248
FT /note="LSESAIVGITT -> MARFLKFALLF (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9295335,
FT ECO:0000303|PubMed:9322767"
FT /id="VSP_050346"
FT VAR_SEQ 248..513
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9322767"
FT /id="VSP_050347"
FT VAR_SEQ 249..513
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9295335,
FT ECO:0000303|PubMed:9322767"
FT /id="VSP_050348"
FT CONFLICT 160
FT /note="K -> Q (in Ref. 1; CAA70992)"
FT /evidence="ECO:0000305"
FT CONFLICT 276
FT /note="P -> S (in Ref. 1; CAA70992)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="G -> E (in Ref. 2; AAC53351)"
FT /evidence="ECO:0000305"
FT CONFLICT 429
FT /note="N -> S (in Ref. 2; AAC53351)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 513 AA; 56578 MW; 7A645DA5F33C9EA0 CRC64;
MRSRCTVSAV GLLSLCLVVS ASLETITPSA FDGYPDEPCT INITIRNSRL ILSWELENKS
GPPANYTLWY TVMSKDENLT KVKNCSDTTK SSCDVTDKWL EGMESYVVAI VIVHRGDLTV
CRCSDYIVPA NAPLEPPEFE IVGFTDHINV TMEFPPVTSK IIQEKMKTTP FVIKEQIGDS
VRKKHEPKVN NVTGNFTFVL RDLLPKTNYC VSLYFDDDPA IKSPLKCIVL QPGQESGLSE
SAIVGITTSC LVVMVFVSTI VMLKRIGYIC LKDNLPNVLN FRHFLTWIIP ERSPSEAIDR
LEIIPTNKKK RLWNYDYEDG SDSDEEVPTA SVTGYTMHGL TGKPLQQTSD TSASPEDPLH
EEDSGAEESD EAGAGAGAEP ELPTEAGAGP SEDPTGPYER RKSVLEDSFP REDNSSMDEP
GDNIIFNVNL NSVFLRVLHD EDASETLSLE EDTILLDEGP QRTESDLRIA GGDRTQPPLP
SLPSQDLWTE DGSSEKSDTS DSDADVGDGY IMR
