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Interferon alpha/beta receptor 1 (IFN-R-1) (IFN-alpha/beta receptor 1) (Type I interferon receptor 1)

 INAR1_MOUSE             Reviewed;         590 AA.
P33896; Q80UJ3;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
28-FEB-2018, entry version 153.
RecName: Full=Interferon alpha/beta receptor 1;
Short=IFN-R-1;
Short=IFN-alpha/beta receptor 1;
AltName: Full=Type I interferon receptor 1;
Flags: Precursor;
Name=Ifnar1; Synonyms=Ifar, Ifnar;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=1533935; DOI=10.1073/pnas.89.10.4774;
Uze G., Lutfalla G., Bandu M.T., Proudhon D., Mogensen K.E.;
"Behavior of a cloned murine interferon alpha/beta receptor expressed
in homospecific or heterospecific background.";
Proc. Natl. Acad. Sci. U.S.A. 89:4774-4778(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7958966; DOI=10.1016/0378-1119(94)90710-2;
Lutfalla G., Uze G.;
"Structure of the murine interferon alpha/beta receptor-encoding gene:
high-frequency rearrangements in the interferon-resistant L1210 cell
line.";
Gene 148:343-346(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Hippocampus, and Skin;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain, and Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
FUNCTION, INTERACTION WITH FBXW11, UBIQUITINATION, PHOSPHORYLATION AT
SER-526, MUTAGENESIS OF SER-526, AND SUBCELLULAR LOCATION.
PubMed=14532120; DOI=10.1093/emboj/cdg524;
Kumar K.G., Tang W., Ravindranath A.K., Clark W.A., Croze E.,
Fuchs S.Y.;
"SCF(HOS) ubiquitin ligase mediates the ligand-induced down-regulation
of the interferon-alpha receptor.";
EMBO J. 22:5480-5490(2003).
[7]
DISRUPTION PHENOTYPE.
PubMed=18724932; DOI=10.1016/j.cell.2008.06.032;
Stetson D.B., Ko J.S., Heidmann T., Medzhitov R.;
"Trex1 prevents cell-intrinsic initiation of autoimmunity.";
Cell 134:587-598(2008).
[8]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=24075985; DOI=10.1016/j.celrep.2013.08.025;
Zheng H., Gupta V., Patterson-Fortin J., Bhattacharya S.,
Katlinski K., Wu J., Varghese B., Carbone C.J., Aressy B., Fuchs S.Y.,
Greenberg R.A.;
"A BRISC-SHMT complex deubiquitinates IFNAR1 and regulates interferon
responses.";
Cell Rep. 5:180-193(2013).
[9]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 27-429 IN COMPLEX WITH IFNB1,
DISULFIDE BONDS, FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=23872679; DOI=10.1038/ni.2667;
de Weerd N.A., Vivian J.P., Nguyen T.K., Mangan N.E., Gould J.A.,
Braniff S.J., Zaker-Tabrizi L., Fung K.Y., Forster S.C., Beddoe T.,
Reid H.H., Rossjohn J., Hertzog P.J.;
"Structural basis of a unique interferon-beta signaling axis mediated
via the receptor IFNAR1.";
Nat. Immunol. 14:901-907(2013).
-!- FUNCTION: 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). {ECO:0000250|UniProtKB:P17181,
ECO:0000269|PubMed:14532120, ECO:0000269|PubMed:1533935,
ECO:0000269|PubMed:23872679, ECO:0000269|PubMed:24075985}.
-!- SUBUNIT: 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 ABRAXAS2 and the BRISC complex (By similarity). Interacts
with TYK2 (By similarity). {ECO:0000250|UniProtKB:P17181,
ECO:0000269|PubMed:14532120, ECO:0000305}.
-!- 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}.
-!- 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). Phosphorylated on tyrosine residues by TYK2
tyrosine kinase. Phosphorylated on tyrosine residues in response
to interferon (By similarity). {ECO:0000250|UniProtKB:P17181,
ECO:0000269|PubMed:14532120}.
-!- DISRUPTION PHENOTYPE: 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).
{ECO:0000269|PubMed:18724932, ECO:0000269|PubMed:23872679}.
-!- 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. {ECO:0000305}.
-!- SIMILARITY: Belongs to the type II cytokine receptor family.
{ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; M89641; AAA37890.1; -; mRNA.
EMBL; AK132431; BAE21165.1; -; mRNA.
EMBL; AK141630; BAE24775.1; -; mRNA.
EMBL; CH466602; EDL03825.1; -; Genomic_DNA.
EMBL; BC043935; AAH43935.1; -; mRNA.
EMBL; BC052429; AAH52429.1; -; mRNA.
CCDS; CCDS28326.1; -.
PIR; A45283; A45283.
RefSeq; NP_034638.2; NM_010508.2.
UniGene; Mm.502; -.
PDB; 3WCY; X-ray; 2.90 A; A=27-429.
PDBsum; 3WCY; -.
ProteinModelPortal; P33896; -.
SMR; P33896; -.
IntAct; P33896; 4.
STRING; 10090.ENSMUSP00000023689; -.
iPTMnet; P33896; -.
PhosphoSitePlus; P33896; -.
MaxQB; P33896; -.
PaxDb; P33896; -.
PRIDE; P33896; -.
Ensembl; ENSMUST00000023689; ENSMUSP00000023689; ENSMUSG00000022967.
Ensembl; ENSMUST00000117748; ENSMUSP00000112670; ENSMUSG00000022967.
Ensembl; ENSMUST00000123196; ENSMUSP00000119160; ENSMUSG00000022967.
GeneID; 15975; -.
KEGG; mmu:15975; -.
UCSC; uc007zxn.2; mouse.
CTD; 3454; -.
MGI; MGI:107658; Ifnar1.
eggNOG; ENOG410IKIP; Eukaryota.
eggNOG; ENOG4111QEU; LUCA.
GeneTree; ENSGT00530000063449; -.
HOGENOM; HOG000113067; -.
HOVERGEN; HBG052126; -.
InParanoid; P33896; -.
KO; K05130; -.
OMA; VYCVKAR; -.
OrthoDB; EOG091G04H5; -.
Reactome; R-MMU-909733; Interferon alpha/beta signaling.
Reactome; R-MMU-912694; Regulation of IFNA signaling.
ChiTaRS; Ifnar1; mouse.
PRO; PR:P33896; -.
Proteomes; UP000000589; Chromosome 16.
Bgee; ENSMUSG00000022967; -.
CleanEx; MM_IFNAR1; -.
ExpressionAtlas; P33896; baseline and differential.
Genevisible; P33896; MM.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0004904; F:interferon receptor activity; IMP:MGI.
GO; GO:0004920; F:interleukin-10 receptor activity; IBA:GO_Central.
GO; GO:0019962; F:type I interferon binding; IPI:UniProtKB.
GO; GO:0004905; F:type I interferon receptor activity; IDA:UniProtKB.
GO; GO:0035457; P:cellular response to interferon-alpha; IMP:UniProtKB.
GO; GO:0051607; P:defense response to virus; IMP:MGI.
GO; GO:0032728; P:positive regulation of interferon-beta production; IMP:CACAO.
GO; GO:0032729; P:positive regulation of interferon-gamma production; IGI:MGI.
GO; GO:0050718; P:positive regulation of interleukin-1 beta secretion; IMP:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:CACAO.
GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; IMP:MGI.
GO; GO:0032496; P:response to lipopolysaccharide; IMP:UniProtKB.
GO; GO:0042110; P:T cell activation; IGI:MGI.
GO; GO:0045351; P:type I interferon biosynthetic process; IMP:MGI.
GO; GO:0060337; P:type I interferon signaling pathway; IDA:UniProtKB.
CDD; cd00063; FN3; 1.
Gene3D; 2.60.40.10; -; 7.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR015373; Interferon/interleukin_rcp_dom.
InterPro; IPR016669; Interferon_alpha/beta_rcpt-1.
Pfam; PF09294; Interfer-bind; 2.
Pfam; PF01108; Tissue_fac; 1.
PIRSF; PIRSF016567; IFN_alpha/beta_recept-1; 1.
SMART; SM00060; FN3; 3.
SUPFAM; SSF49265; SSF49265; 4.
PROSITE; PS50853; FN3; 3.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome; Disulfide bond;
Endosome; Glycoprotein; Isopeptide bond; Lysosome; Membrane;
Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
Transmembrane; Transmembrane helix; Ubl conjugation.
SIGNAL 1 26 {ECO:0000255}.
CHAIN 27 590 Interferon alpha/beta receptor 1.
/FTId=PRO_0000011002.
TOPO_DOM 27 429 Extracellular. {ECO:0000255}.
TRANSMEM 430 449 Helical. {ECO:0000255}.
TOPO_DOM 450 590 Cytoplasmic. {ECO:0000255}.
DOMAIN 31 125 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 127 226 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 230 327 Fibronectin type-III 3.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 332 425 Fibronectin type-III 4.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
REGION 483 492 Important for interaction with TYK2.
{ECO:0000250|UniProtKB:P17181}.
MOD_RES 526 526 Phosphoserine.
{ECO:0000269|PubMed:14532120}.
CARBOHYD 43 43 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 109 109 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 181 181 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 214 214 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 314 314 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 370 370 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 409 409 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 413 413 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 78 86 {ECO:0000250|UniProtKB:P17181}.
DISULFID 199 220 {ECO:0000269|PubMed:23872679}.
DISULFID 284 292 {ECO:0000269|PubMed:23872679}.
DISULFID 397 419 {ECO:0000269|PubMed:23872679}.
CROSSLNK 517 517 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P17181}.
MUTAGEN 526 526 S->A: Abolishes interaction with FBXW11.
Prevents interalization from the cell
membrane and lysosomal degradation.
{ECO:0000269|PubMed:14532120}.
CONFLICT 274 274 R -> H (in Ref. 1; AAA37890).
{ECO:0000305}.
STRAND 38 40 {ECO:0000244|PDB:3WCY}.
STRAND 43 45 {ECO:0000244|PDB:3WCY}.
HELIX 122 125 {ECO:0000244|PDB:3WCY}.
STRAND 126 128 {ECO:0000244|PDB:3WCY}.
STRAND 132 137 {ECO:0000244|PDB:3WCY}.
STRAND 142 147 {ECO:0000244|PDB:3WCY}.
STRAND 149 152 {ECO:0000244|PDB:3WCY}.
STRAND 154 156 {ECO:0000244|PDB:3WCY}.
TURN 157 162 {ECO:0000244|PDB:3WCY}.
STRAND 164 173 {ECO:0000244|PDB:3WCY}.
STRAND 178 189 {ECO:0000244|PDB:3WCY}.
STRAND 197 205 {ECO:0000244|PDB:3WCY}.
STRAND 207 210 {ECO:0000244|PDB:3WCY}.
STRAND 219 222 {ECO:0000244|PDB:3WCY}.
STRAND 236 239 {ECO:0000244|PDB:3WCY}.
STRAND 241 247 {ECO:0000244|PDB:3WCY}.
STRAND 261 264 {ECO:0000244|PDB:3WCY}.
HELIX 265 269 {ECO:0000244|PDB:3WCY}.
STRAND 282 290 {ECO:0000244|PDB:3WCY}.
STRAND 292 295 {ECO:0000244|PDB:3WCY}.
TURN 296 298 {ECO:0000244|PDB:3WCY}.
STRAND 301 307 {ECO:0000244|PDB:3WCY}.
STRAND 323 326 {ECO:0000244|PDB:3WCY}.
STRAND 337 342 {ECO:0000244|PDB:3WCY}.
STRAND 347 352 {ECO:0000244|PDB:3WCY}.
STRAND 354 356 {ECO:0000244|PDB:3WCY}.
STRAND 362 369 {ECO:0000244|PDB:3WCY}.
STRAND 376 387 {ECO:0000244|PDB:3WCY}.
STRAND 395 403 {ECO:0000244|PDB:3WCY}.
STRAND 418 421 {ECO:0000244|PDB:3WCY}.
SEQUENCE 590 AA; 65796 MW; E887ADFA6DFEAF3C CRC64;
MLAVVGAAAL VLVAGAPWVL PSAAGGENLK PPENIDVYII DDNYTLKWSS HGESMGSVTF
SAEYRTKDEA KWLKVPECQH TTTTKCEFSL LDTNVYIKTQ FRVRAEEGNS TSSWNEVDPF
IPFYTAHMSP PEVRLEAEDK AILVHISPPG QDGNMWALEK PSFSYTIRIW QKSSSDKKTI
NSTYYVEKIP ELLPETTYCL EVKAIHPSLK KHSNYSTVQC ISTTVANKMP VPGNLQVDAQ
GKSYVLKWDY IASADVLFRA QWLPGYSKSS SGSRSDKWKP IPTCANVQTT HCVFSQDTVY
TGTFFLHVQA SEGNHTSFWS EEKFIDSQKH ILPPPPVITV TAMSDTLLVY VNCQDSTCDG
LNYEIIFWEN TSNTKISMEK DGPEFTLKNL QPLTVYCVQA RVLFRALLNK TSNFSEKLCE
KTRPGSFSTI WIITGLGVVF FSVMVLYALR SVWKYLCHVC FPPLKPPRSI DEFFSEPPSK
NLVLLTAEEH TERCFIIENT DTVAVEVKHA PEEDLRKYSS QTSQDSGNYS NEEEESVGTE
SGQAVLSKAP CGGPCSVPSP PGTLEDGTCF LGNEKYLQSP ALRTEPALLC


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