ID I10R2_MOUSE Reviewed; 349 AA. AC Q61190; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 08-NOV-2023, entry version 149. DE RecName: Full=Interleukin-10 receptor subunit beta; DE Short=IL-10 receptor subunit beta; DE Short=IL-10R subunit beta; DE Short=IL-10RB; DE AltName: Full=Cytokine receptor class-II member 4; DE AltName: Full=Cytokine receptor family 2 member 4; DE Short=CRF2-4; DE AltName: Full=Interleukin-10 receptor subunit 2; DE Short=IL-10R subunit 2; DE Short=IL-10R2; DE AltName: CD_antigen=CDw210b; DE Flags: Precursor; GN Name=Il10rb; Synonyms=Crfb4; 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]. RX PubMed=9047351; DOI=10.1016/s0378-1119(96)00690-7; RA Gibbs V.C., Pennica D.; RT "CRF2-4: isolation of cDNA clones encoding the human and mouse proteins."; RL Gene 186:97-101(1997). RN [2] RP CHARACTERIZATION. RX PubMed=9463407; DOI=10.1084/jem.187.4.571; RA Spencer S.D., Di Marco F., Hooley J., Pitts-Meek S., Bauer M., Ryan A.M., RA Sordat B., Gibbs V.C., Aguet M.; RT "The orphan receptor CRF2-4 is an essential subunit of the interleukin 10 RT receptor."; RL J. Exp. Med. 187:571-578(1998). RN [3] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299, AND IDENTIFICATION BY RP 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). CC -!- FUNCTION: Shared cell surface receptor required for the activation of CC five class 2 cytokines: IL10, IL22, IL26, IL28, and IFNL1. The CC IFNLR1/IL10RB dimer is a receptor for the cytokine ligands IFNL2 and CC IFNL3 and mediates their antiviral activity. The ligand/receptor CC complex stimulate the activation of the JAK/STAT signaling pathway CC leading to the expression of IFN-stimulated genes (ISG), which CC contribute to the antiviral state (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Heterodimer with IFNLR1. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. CC -!- SIMILARITY: Belongs to the type II cytokine receptor family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U53696; AAC53062.1; -; mRNA. DR PDB; 6WEO; X-ray; 2.60 A; 0/3/6/9/C/E/H/K/O/R/U/X=20-220. DR PDBsum; 6WEO; -. DR AlphaFoldDB; Q61190; -. DR SMR; Q61190; -. DR STRING; 10090.ENSMUSP00000023691; -. DR GlyCosmos; Q61190; 4 sites, No reported glycans. DR GlyGen; Q61190; 4 sites. DR iPTMnet; Q61190; -. DR PhosphoSitePlus; Q61190; -. DR MaxQB; Q61190; -. DR PaxDb; 10090-ENSMUSP00000023691; -. DR ProteomicsDB; 273243; -. DR AGR; MGI:109380; -. DR MGI; MGI:109380; Il10rb. DR eggNOG; ENOG502S2QA; Eukaryota. DR InParanoid; Q61190; -. DR Reactome; R-MMU-6783783; Interleukin-10 signaling. DR Reactome; R-MMU-8854691; Interleukin-20 family signaling. DR ChiTaRS; Il10rb; mouse. DR PRO; PR:Q61190; -. DR Proteomes; UP000000589; Unplaced. DR RNAct; Q61190; Protein. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004920; F:interleukin-10 receptor activity; IMP:MGI. DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central. DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW. DR GO; GO:1901857; P:positive regulation of cellular respiration; ISO:MGI. DR GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; ISO:MGI. DR CDD; cd00063; FN3; 2. DR Gene3D; 2.60.40.10; Immunoglobulins; 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 PANTHER; PTHR20859; INTERFERON/INTERLEUKIN RECEPTOR; 1. DR PANTHER; PTHR20859:SF50; INTERLEUKIN-10 RECEPTOR SUBUNIT BETA; 1. DR Pfam; PF09294; Interfer-bind; 1. DR Pfam; PF01108; Tissue_fac; 1. DR SMART; SM00060; FN3; 2. DR SUPFAM; SSF49265; Fibronectin type III; 2. DR PROSITE; PS50853; FN3; 2. PE 1: Evidence at protein level; KW 3D-structure; Antiviral defense; Disulfide bond; Glycoprotein; Membrane; KW Phosphoprotein; Receptor; Reference proteome; Repeat; Signal; KW Transmembrane; Transmembrane helix. FT SIGNAL 1..19 FT /evidence="ECO:0000255" FT CHAIN 20..349 FT /note="Interleukin-10 receptor subunit beta" FT /id="PRO_0000011015" FT TOPO_DOM 20..220 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 221..241 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 242..349 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 23..111 FT /note="Fibronectin type-III 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 112..215 FT /note="Fibronectin type-III 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT REGION 300..349 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 322..337 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 299 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19144319" FT CARBOHYD 49 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 102 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 161 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 199 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 66..74 FT /evidence="ECO:0000250" FT DISULFID 188..209 FT /evidence="ECO:0000250" FT STRAND 25..32 FT /evidence="ECO:0007829|PDB:6WEO" FT STRAND 35..41 FT /evidence="ECO:0007829|PDB:6WEO" FT STRAND 51..58 FT /evidence="ECO:0007829|PDB:6WEO" FT STRAND 61..75 FT /evidence="ECO:0007829|PDB:6WEO" FT STRAND 85..93 FT /evidence="ECO:0007829|PDB:6WEO" FT STRAND 101..105 FT /evidence="ECO:0007829|PDB:6WEO" FT HELIX 107..110 FT /evidence="ECO:0007829|PDB:6WEO" FT STRAND 117..121 FT /evidence="ECO:0007829|PDB:6WEO" FT STRAND 124..132 FT /evidence="ECO:0007829|PDB:6WEO" FT STRAND 137..141 FT /evidence="ECO:0007829|PDB:6WEO" FT HELIX 145..147 FT /evidence="ECO:0007829|PDB:6WEO" FT STRAND 152..159 FT /evidence="ECO:0007829|PDB:6WEO" FT STRAND 167..180 FT /evidence="ECO:0007829|PDB:6WEO" FT STRAND 187..195 FT /evidence="ECO:0007829|PDB:6WEO" FT STRAND 201..204 FT /evidence="ECO:0007829|PDB:6WEO" FT STRAND 208..210 FT /evidence="ECO:0007829|PDB:6WEO" SQ SEQUENCE 349 AA; 39774 MW; 58BA4F6B86330A39 CRC64; MAPCVAGWLG GFLLVPALGM IPPPEKVRMN SVNFKNILQW EVPAFPKTNL TFTAQYESYR SFQDHCKRTA STQCDFSHLS KYGDYTVRVR AELADEHSEW VNVTFCPVED TIIGPPEMQI ESLAESLHLR FSAPQIENEP ETWTLKNIYD SWAYRVQYWK NGTNEKFQVV SPYDSEVLRN LEPWTTYCIQ VQGFLLDQNR TGEWSEPICE RTGNDEITPS WIVAIILIVS VLVVFLFLLG CFVVLWLIYK KTKHTFRSGT SLPQHLKEFL GHPHHSTFLL FSFPPPEEAE VFDKLSIISE ESEGSKQSPE DNCASEPPSD PGPRELESKD EAPSPPHDDP KLLTSTSEV //