INLR1_MOUSE
ID INLR1_MOUSE Reviewed; 535 AA.
AC Q8CGK5; Q6PEV1;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Interferon lambda receptor 1;
DE Short=IFN-lambda R1;
DE AltName: Full=Cytokine receptor class-II member 12;
DE AltName: Full=Cytokine receptor family 2 member 12;
DE Short=CRF2-12;
DE AltName: Full=Interleukin-28 receptor subunit alpha;
DE Short=IL-28 receptor subunit alpha;
DE Short=IL-28R-alpha;
DE Short=IL-28RA;
DE Flags: Precursor;
GN Name=Ifnlr1; Synonyms=Il28ra;
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].
RC STRAIN=C57BL/6J;
RX PubMed=12483210; DOI=10.1038/ni875;
RA Kotenko S.V., Gallagher G., Baurin V.V., Lewis-Antes A., Shen M.,
RA Shah N.K., Langer J.A., Sheikh F., Dickensheets H., Donnelly R.P.;
RT "IFN-lambdas mediate antiviral protection through a distinct class II
RT cytokine receptor complex.";
RL Nat. Immunol. 4:69-77(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary 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 [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18250457; DOI=10.4049/jimmunol.180.4.2474;
RA Ank N., Iversen M.B., Bartholdy C., Staeheli P., Hartmann R., Jensen U.B.,
RA Dagnaes-Hansen F., Thomsen A.R., Chen Z., Haugen H., Klucher K.,
RA Paludan S.R.;
RT "An important role for type III interferon (IFN-lambda/IL-28) in TLR-
RT induced antiviral activity.";
RL J. Immunol. 180:2474-2485(2008).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21518880; DOI=10.1073/pnas.1100552108;
RA Pott J., Mahlakoiv T., Mordstein M., Duerr C.U., Michiels T.,
RA Stockinger S., Staeheli P., Hornef M.W.;
RT "IFN-lambda determines the intestinal epithelial antiviral host defense.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:7944-7949(2011).
CC -!- FUNCTION: The IFNLR1/IL10RB dimer is a receptor for the cytokine
CC ligands IFNL2 and IFNL3 and mediates their antiviral activity. The
CC ligand/receptor complex stimulate the activation of the JAK/STAT
CC signaling pathway leading to the expression of IFN-stimulated genes
CC (ISG), which contribute to the antiviral state. Determines the cell
CC type specificity of the lambda interferon action. Shows a more
CC restricted pattern of expression in the epithelial tissues thereby
CC limiting responses to lambda interferons primarily to epithelial cells
CC of the respiratory, gastrointestinal, and reproductive tracts. Seems
CC not to be essential for early virus-activated host defense in vaginal
CC infection, but plays an important role in Toll-like receptor (TLR)-
CC induced antiviral defense. Plays a significant role in the antiviral
CC immune defense in the intestinal epithelium.
CC {ECO:0000269|PubMed:18250457, ECO:0000269|PubMed:21518880}.
CC -!- SUBUNIT: Heterodimer with IL10RB. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: The mice are viable and appear to be of normal
CC size, behavior and reproductive ability. There is no effect on the
CC ability to combat vaginal viral infection, but antiviral response
CC evoked by Toll-like reseptor (TLR) stimulation is reduced. Mice also
CC display enhanced rotavirus susceptibility associated with epithelial
CC vacuolization, villus deformation and epithelial cell disruption.
CC {ECO:0000269|PubMed:18250457, ECO:0000269|PubMed:21518880}.
CC -!- SIMILARITY: Belongs to the type II cytokine receptor family.
CC {ECO:0000305}.
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DR EMBL; AY184376; AAN86129.1; -; mRNA.
DR EMBL; BC057856; AAH57856.1; -; mRNA.
DR CCDS; CCDS18788.1; -.
DR RefSeq; NP_777276.3; NM_174851.3.
DR PDB; 7T6F; EM; 3.60 A; C/D=249-298.
DR PDBsum; 7T6F; -.
DR AlphaFoldDB; Q8CGK5; -.
DR SMR; Q8CGK5; -.
DR STRING; 10090.ENSMUSP00000074009; -.
DR GlyGen; Q8CGK5; 4 sites.
DR iPTMnet; Q8CGK5; -.
DR PhosphoSitePlus; Q8CGK5; -.
DR PaxDb; Q8CGK5; -.
DR PRIDE; Q8CGK5; -.
DR Antibodypedia; 2700; 276 antibodies from 30 providers.
DR DNASU; 242700; -.
DR Ensembl; ENSMUST00000074408; ENSMUSP00000074009; ENSMUSG00000062157.
DR GeneID; 242700; -.
DR KEGG; mmu:242700; -.
DR UCSC; uc008vgw.2; mouse.
DR CTD; 163702; -.
DR MGI; MGI:2429859; Ifnlr1.
DR VEuPathDB; HostDB:ENSMUSG00000062157; -.
DR eggNOG; ENOG502S4B0; Eukaryota.
DR GeneTree; ENSGT00510000048978; -.
DR HOGENOM; CLU_043104_1_0_1; -.
DR InParanoid; Q8CGK5; -.
DR OMA; FLCPQKE; -.
DR OrthoDB; 577004at2759; -.
DR PhylomeDB; Q8CGK5; -.
DR TreeFam; TF336003; -.
DR Reactome; R-MMU-8854691; Interleukin-20 family signaling.
DR BioGRID-ORCS; 242700; 1 hit in 71 CRISPR screens.
DR PRO; PR:Q8CGK5; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8CGK5; protein.
DR Bgee; ENSMUSG00000062157; Expressed in granulocyte and 73 other tissues.
DR ExpressionAtlas; Q8CGK5; baseline and differential.
DR Genevisible; Q8CGK5; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0032002; C:interleukin-28 receptor complex; ISO:MGI.
DR GO; GO:0004896; F:cytokine receptor activity; ISO:MGI.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0051607; P:defense response to virus; IMP:UniProtKB.
DR GO; GO:0002385; P:mucosal immune response; IMP:UniProtKB.
DR GO; GO:1901857; P:positive regulation of cellular respiration; ISO:MGI.
DR GO; GO:0050691; P:regulation of defense response to virus by host; ISO:MGI.
DR GO; GO:0034342; P:response to type III interferon; ISS:UniProtKB.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR Pfam; PF01108; Tissue_fac; 1.
DR SUPFAM; SSF49265; SSF49265; 2.
DR PROSITE; PS50853; FN3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; Disulfide bond; Glycoprotein; Membrane;
KW Receptor; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..535
FT /note="Interferon lambda receptor 1"
FT /id="PRO_0000011020"
FT TOPO_DOM 21..227
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 249..535
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 26..121
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 301..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 478..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..336
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..504
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 73..81
FT /evidence="ECO:0000250"
FT DISULFID 85..149
FT /evidence="ECO:0000250"
FT DISULFID 194..216
FT /evidence="ECO:0000250"
FT CONFLICT 105
FT /note="H -> Q (in Ref. 2; AAH57856)"
FT /evidence="ECO:0000305"
FT CONFLICT 231
FT /note="M -> L (in Ref. 2; AAH57856)"
FT /evidence="ECO:0000305"
FT CONFLICT 327
FT /note="E -> G (in Ref. 2; AAH57856)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 535 AA; 59976 MW; 32D12FA52B0BA17E CRC64;
MWRADRWAPL LLFLLQSALG RPRLAPPRNV TLFSQNFTVY LTWLPGLGSP PNVTYFVTYQ
SYIKTGWRPV EHCAGIKALV CPLMCLKKLN LYSKFKGRVQ AASAHGRSPR VESRYLEYLF
DVELAPPTLV LTQMEKILRV NATYQLPPCM PSLELKYQVE FWKEGLGSKT LFPDTPYGQP
VQIPLQQGAS RRHCLSARTV YTLIDIKYSQ FSEPSCIFLE APGDKRAVLA MPSLLLLLIA
AVAAGVAWKI MKGNPWFQGV KTPRALDFSE YRYPVATFQP SGPEFSDDLI LCPQKELTIR
NRPAPQVRNP ATLQAGPERD STEDEDEDTD YDDDGDSVQP YLERPLFISE KPRVMEHSET
DESGVDSGGP WTSPVGSDGS SAWDSSDRSW SSTGDSSYKD EVGSSSCLDR KEPDQAPCGD
WLQEALPCLE FSEDLGTVEE PLKDGLSGWR ISGSLSSKRD LAPVEPPVSL QTLTFCWVNN
PEGEEEQEDE EEEEEEEEEE DWESEPKGSN AGCWGTSSVQ RTEVRGRMLG DYLVR
