I10R2_MOUSE
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 25-MAY-2022, entry version 144.
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}.
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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 GlyGen; Q61190; 4 sites.
DR iPTMnet; Q61190; -.
DR PhosphoSitePlus; Q61190; -.
DR MaxQB; Q61190; -.
DR PaxDb; Q61190; -.
DR PRIDE; Q61190; -.
DR ProteomicsDB; 273243; -.
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:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central.
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; -; 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 SMART; SM00060; FN3; 2.
DR SUPFAM; SSF49265; SSF49265; 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
