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Q8CGK5 (INLR1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Interferon lambda receptor 1

Short name=IFN-lambda R1
Alternative name(s):
Cytokine receptor class-II member 12
Cytokine receptor family 2 member 12
Short name=CRF2-12
Interleukin-28 receptor subunit alpha
Short name=IL-28 receptor subunit alpha
Short name=IL-28R-alpha
Short name=IL-28RA
Gene names
Name:Ifnlr1
Synonyms:Il28ra
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length535 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

The IFNLR1/IL10RB dimer is a receptor for IFNL2 and IFNL3. The ligand/receptor complex seems to signal through the Jak-STAT pathway By similarity. Seems not to be essential for early virus-activated host defense in vaginal infection, but plays an important role in Toll-like receptor (TLR)-induced antiviral defense. Plays a significant role in the antiviral immune defense in the intestinal epithelium. Ref.3 Ref.4

Subunit structure

Heterodimer with IL10RB By similarity.

Subcellular location

Membrane; Single-pass type I membrane protein By similarity.

Disruption phenotype

The mice are viable and appear to be of normal size, behavior and reproductive ability. There is no effect on the ability to combat vaginal viral infection, but antiviral response evoked by Toll-like reseptor (TLR) stimulation is reduced. Mice also display enhanced rotavirus susceptibility associated with epithelial vacuolization, villus deformation and epithelial cell disruption. Ref.3 Ref.4

Sequence similarities

Belongs to the type II cytokine receptor family.

Contains 1 fibronectin type-III domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 535515Interferon lambda receptor 1
PRO_0000011020

Regions

Topological domain21 – 227207Extracellular Potential
Transmembrane228 – 24821Helical; Potential
Topological domain249 – 535287Cytoplasmic Potential
Domain26 – 12196Fibronectin type-III

Amino acid modifications

Glycosylation291N-linked (GlcNAc...) Potential
Glycosylation361N-linked (GlcNAc...) Potential
Glycosylation521N-linked (GlcNAc...) Potential
Glycosylation1411N-linked (GlcNAc...) Potential
Disulfide bond73 ↔ 81 By similarity
Disulfide bond85 ↔ 149 By similarity
Disulfide bond194 ↔ 216 By similarity

Experimental info

Sequence conflict1051H → Q in AAH57856. Ref.2
Sequence conflict2311M → L in AAH57856. Ref.2
Sequence conflict3271E → G in AAH57856. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q8CGK5 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 32D12FA52B0BA17E

FASTA53559,976
        10         20         30         40         50         60 
MWRADRWAPL LLFLLQSALG RPRLAPPRNV TLFSQNFTVY LTWLPGLGSP PNVTYFVTYQ 

        70         80         90        100        110        120 
SYIKTGWRPV EHCAGIKALV CPLMCLKKLN LYSKFKGRVQ AASAHGRSPR VESRYLEYLF 

       130        140        150        160        170        180 
DVELAPPTLV LTQMEKILRV NATYQLPPCM PSLELKYQVE FWKEGLGSKT LFPDTPYGQP 

       190        200        210        220        230        240 
VQIPLQQGAS RRHCLSARTV YTLIDIKYSQ FSEPSCIFLE APGDKRAVLA MPSLLLLLIA 

       250        260        270        280        290        300 
AVAAGVAWKI MKGNPWFQGV KTPRALDFSE YRYPVATFQP SGPEFSDDLI LCPQKELTIR 

       310        320        330        340        350        360 
NRPAPQVRNP ATLQAGPERD STEDEDEDTD YDDDGDSVQP YLERPLFISE KPRVMEHSET 

       370        380        390        400        410        420 
DESGVDSGGP WTSPVGSDGS SAWDSSDRSW SSTGDSSYKD EVGSSSCLDR KEPDQAPCGD 

       430        440        450        460        470        480 
WLQEALPCLE FSEDLGTVEE PLKDGLSGWR ISGSLSSKRD LAPVEPPVSL QTLTFCWVNN 

       490        500        510        520        530 
PEGEEEQEDE EEEEEEEEEE DWESEPKGSN AGCWGTSSVQ RTEVRGRMLG DYLVR 

« Hide

References

« Hide 'large scale' references
[1]"IFN-lambdas mediate antiviral protection through a distinct class II cytokine receptor complex."
Kotenko S.V., Gallagher G., Baurin V.V., Lewis-Antes A., Shen M., Shah N.K., Langer J.A., Sheikh F., Dickensheets H., Donnelly R.P.
Nat. Immunol. 4:69-77(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6.
[2]"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: Czech II.
Tissue: Mammary gland.
[3]"An important role for type III interferon (IFN-lambda/IL-28) in TLR-induced antiviral activity."
Ank N., Iversen M.B., Bartholdy C., Staeheli P., Hartmann R., Jensen U.B., Dagnaes-Hansen F., Thomsen A.R., Chen Z., Haugen H., Klucher K., Paludan S.R.
J. Immunol. 180:2474-2485(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[4]"IFN-lambda determines the intestinal epithelial antiviral host defense."
Pott J., Mahlakoiv T., Mordstein M., Duerr C.U., Michiels T., Stockinger S., Staeheli P., Hornef M.W.
Proc. Natl. Acad. Sci. U.S.A. 108:7944-7949(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY184376 mRNA. Translation: AAN86129.1.
BC057856 mRNA. Translation: AAH57856.1.
CCDSCCDS18788.1.
RefSeqNP_777276.3. NM_174851.3.
UniGeneMm.259623.

3D structure databases

ProteinModelPortalQ8CGK5.
SMRQ8CGK5. Positions 24-222.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000074009.

PTM databases

PhosphoSiteQ8CGK5.

Proteomic databases

PaxDbQ8CGK5.
PRIDEQ8CGK5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000074408; ENSMUSP00000074009; ENSMUSG00000062157.
GeneID242700.
KEGGmmu:242700.
UCSCuc008vgw.2. mouse.

Organism-specific databases

CTD163702.
MGIMGI:2429859. Ifnlr1.

Phylogenomic databases

eggNOGNOG46166.
GeneTreeENSGT00510000048978.
HOGENOMHOG000112989.
HOVERGENHBG052069.
InParanoidQ8CGK5.
KOK05140.
OMAPWFQRAK.
OrthoDBEOG78H3T9.
PhylomeDBQ8CGK5.
TreeFamTF336003.

Gene expression databases

BgeeQ8CGK5.
CleanExMM_IL28RA.
GenevestigatorQ8CGK5.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
InterProIPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
[Graphical view]
PfamPF01108. Tissue_fac. 1 hit.
[Graphical view]
SMARTSM00060. FN3. 1 hit.
[Graphical view]
SUPFAMSSF49265. SSF49265. 2 hits.
PROSITEPS50853. FN3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio385500.
PROQ8CGK5.
SOURCESearch...

Entry information

Entry nameINLR1_MOUSE
AccessionPrimary (citable) accession number: Q8CGK5
Secondary accession number(s): Q6PEV1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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