I10R2_HUMAN
ID I10R2_HUMAN Reviewed; 325 AA.
AC Q08334; Q9BUU4;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 195.
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, D21S58, D21S66;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fetal brain;
RX PubMed=8314576; DOI=10.1006/geno.1993.1199;
RA Lutfalla G., Gardiner K., Uze G.;
RT "A new member of the cytokine receptor gene family maps on chromosome 21 at
RT less than 35 kb from IFNAR.";
RL Genomics 16:366-373(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7563119; DOI=10.1007/bf00186545;
RA Lutfalla G., McInnis M.G., Antonarakis S.E., Uze G.;
RT "Structure of the human CRFB4 gene: comparison with its IFNAR neighbor.";
RL J. Mol. Evol. 41:338-344(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLU-47.
RG SeattleSNPs variation discovery resource;
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [6]
RP PROTEIN SEQUENCE OF 20-34.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [7]
RP CHARACTERIZATION.
RX PubMed=9312047; DOI=10.1093/emboj/16.19.5894;
RA Kotenko S.V., Krause C.D., Izotova L.S., Pollack B.P., Wu W., Pestka S.;
RT "Identification and functional characterization of a second chain of the
RT interleukin-10 receptor complex.";
RL EMBO J. 16:5894-5903(1997).
RN [8]
RP CHARACTERIZATION.
RX PubMed=10875937; DOI=10.1074/jbc.m005304200;
RA Xie M.-H., Aggarwal S., Ho W.-H., Foster J., Zhang Z., Stinson J.,
RA Wood W.I., Goddard A.D., Gurney A.L.;
RT "Interleukin (IL)-22, a novel human cytokine that signals through the
RT interferon receptor-related proteins CRF2-4 and IL-22R.";
RL J. Biol. Chem. 275:31335-31339(2000).
RN [9]
RP FUNCTION, AND SUBUNIT.
RX PubMed=12469119; DOI=10.1038/ni873;
RA Sheppard P., Kindsvogel W., Xu W., Henderson K., Schlutsmeyer S.,
RA Whitmore T.E., Kuestner R., Garrigues U., Birks C., Roraback J.,
RA Ostrander C., Dong D., Shin J., Presnell S., Fox B., Haldeman B.,
RA Cooper E., Taft D., Gilbert T., Grant F.J., Tackett M., Krivan W.,
RA McKnight G., Clegg C., Foster D., Klucher K.M.;
RT "IL-28, IL-29 and their class II cytokine receptor IL-28R.";
RL Nat. Immunol. 4:63-68(2003).
RN [10]
RP FUNCTION.
RX PubMed=15123776; DOI=10.1189/jlb.0204117;
RA Donnelly R.P., Sheikh F., Kotenko S.V., Dickensheets H.;
RT "The expanded family of class II cytokines that share the IL-10 receptor-2
RT (IL-10R2) chain.";
RL J. Leukoc. Biol. 76:314-321(2004).
RN [11]
RP INVOLVEMENT IN SUSCEPTIBILITY TO HBV INFECTION, VARIANT GLU-47, AND
RP CHARACTERIZATION OF VARIANT GLU-47.
RX PubMed=16757563; DOI=10.1073/pnas.0602800103;
RA Frodsham A.J., Zhang L., Dumpis U., Taib N.A.M., Best S., Durham A.,
RA Hennig B.J.W., Hellier S., Knapp S., Wright M., Chiaramonte M., Bell J.I.,
RA Graves M., Whittle H.C., Thomas H.C., Thursz M.R., Hill A.V.S.;
RT "Class II cytokine receptor gene cluster is a major locus for hepatitis B
RT persistence.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:9148-9153(2006).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP INVOLVEMENT IN IBD25.
RX PubMed=19890111; DOI=10.1056/nejmoa0907206;
RA Glocker E.O., Kotlarz D., Boztug K., Gertz E.M., Schaffer A.A., Noyan F.,
RA Perro M., Diestelhorst J., Allroth A., Murugan D., Hatscher N., Pfeifer D.,
RA Sykora K.W., Sauer M., Kreipe H., Lacher M., Nustede R., Woellner C.,
RA Baumann U., Salzer U., Koletzko S., Shah N., Segal A.W., Sauerbrey A.,
RA Buderus S., Snapper S.B., Grimbacher B., Klein C.;
RT "Inflammatory bowel disease and mutations affecting the interleukin-10
RT receptor.";
RL N. Engl. J. Med. 361:2033-2045(2009).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.14 ANGSTROMS) OF 20-220, AND DISULFIDE BONDS.
RX PubMed=20462497; DOI=10.1016/j.str.2010.02.009;
RA Yoon S.I., Jones B.C., Logsdon N.J., Harris B.D., Deshpande A., Radaeva S.,
RA Halloran B.A., Gao B., Walter M.R.;
RT "Structure and mechanism of receptor sharing by the IL-10R2 common chain.";
RL Structure 18:638-648(2010).
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. {ECO:0000269|PubMed:12469119,
CC ECO:0000269|PubMed:15123776}.
CC -!- SUBUNIT: Heterodimer with IFNLR1. {ECO:0000269|PubMed:12469119}.
CC -!- INTERACTION:
CC Q08334; P22301: IL10; NbExp=2; IntAct=EBI-11175900, EBI-1031632;
CC Q08334; Q9GZX6: IL22; NbExp=2; IntAct=EBI-11175900, EBI-8040250;
CC Q08334; Q8N6P7: IL22RA1; NbExp=5; IntAct=EBI-11175900, EBI-3940749;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- POLYMORPHISM: Genetic variations in IL10RB influence susceptibility to
CC hepatitis B virus (HBV) infection [MIM:610424].
CC -!- DISEASE: Inflammatory bowel disease 25, autosomal recessive (IBD25)
CC [MIM:612567]: A chronic, relapsing inflammation of the gastrointestinal
CC tract with a complex etiology. It is subdivided into Crohn disease and
CC ulcerative colitis phenotypes. Crohn disease may affect any part of the
CC gastrointestinal tract from the mouth to the anus, but most frequently
CC it involves the terminal ileum and colon. Bowel inflammation is
CC transmural and discontinuous; it may contain granulomas or be
CC associated with intestinal or perianal fistulas. In contrast, in
CC ulcerative colitis, the inflammation is continuous and limited to
CC rectal and colonic mucosal layers; fistulas and granulomas are not
CC observed. Both diseases include extraintestinal inflammation of the
CC skin, eyes, or joints. {ECO:0000269|PubMed:19890111}. Note=The disease
CC is caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the type II cytokine receptor family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/il10rb/";
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DR EMBL; Z17227; CAA78933.1; -; mRNA.
DR EMBL; U08988; AAA86872.1; -; Genomic_DNA.
DR EMBL; BT009777; AAP88779.1; -; mRNA.
DR EMBL; AY323826; AAP72016.1; -; Genomic_DNA.
DR EMBL; BC001903; AAH01903.1; -; mRNA.
DR CCDS; CCDS13623.1; -.
DR PIR; A47003; A47003.
DR RefSeq; NP_000619.3; NM_000628.4.
DR PDB; 3LQM; X-ray; 2.14 A; A/B=20-220.
DR PDB; 5T5W; X-ray; 2.85 A; A=19-220.
DR PDB; 6X93; EM; 3.50 A; C/F=20-220.
DR PDBsum; 3LQM; -.
DR PDBsum; 5T5W; -.
DR PDBsum; 6X93; -.
DR AlphaFoldDB; Q08334; -.
DR SMR; Q08334; -.
DR BioGRID; 109802; 10.
DR ComplexPortal; CPX-6011; Interferon lambda receptor-ligand complex, IFNL1 variant.
DR ComplexPortal; CPX-6012; Interferon lambda receptor-ligand complex, IFNL2 variant.
DR ComplexPortal; CPX-6013; Interferon lambda receptor-ligand complex, IFNL3 variant.
DR ComplexPortal; CPX-6014; Interferon lambda receptor-ligand complex, IFNL4 variant.
DR CORUM; Q08334; -.
DR DIP; DIP-6016N; -.
DR IntAct; Q08334; 9.
DR STRING; 9606.ENSP00000290200; -.
DR ChEMBL; CHEMBL3831284; -.
DR GlyGen; Q08334; 5 sites.
DR iPTMnet; Q08334; -.
DR PhosphoSitePlus; Q08334; -.
DR SwissPalm; Q08334; -.
DR BioMuta; IL10RB; -.
DR DMDM; 56757647; -.
DR EPD; Q08334; -.
DR jPOST; Q08334; -.
DR MassIVE; Q08334; -.
DR MaxQB; Q08334; -.
DR PaxDb; Q08334; -.
DR PeptideAtlas; Q08334; -.
DR PRIDE; Q08334; -.
DR ProteomicsDB; 58594; -.
DR Antibodypedia; 34939; 365 antibodies from 30 providers.
DR DNASU; 3588; -.
DR Ensembl; ENST00000290200.7; ENSP00000290200.2; ENSG00000243646.10.
DR GeneID; 3588; -.
DR KEGG; hsa:3588; -.
DR MANE-Select; ENST00000290200.7; ENSP00000290200.2; NM_000628.5; NP_000619.3.
DR UCSC; uc002yrk.3; human.
DR CTD; 3588; -.
DR DisGeNET; 3588; -.
DR GeneCards; IL10RB; -.
DR HGNC; HGNC:5965; IL10RB.
DR HPA; ENSG00000243646; Low tissue specificity.
DR MalaCards; IL10RB; -.
DR MIM; 123889; gene.
DR MIM; 610424; phenotype.
DR MIM; 612567; phenotype.
DR neXtProt; NX_Q08334; -.
DR OpenTargets; ENSG00000243646; -.
DR Orphanet; 238569; Immune dysregulation-inflammatory bowel disease-arthritis-recurrent infections syndrome.
DR PharmGKB; PA29780; -.
DR VEuPathDB; HostDB:ENSG00000243646; -.
DR eggNOG; ENOG502S2QA; Eukaryota.
DR GeneTree; ENSGT00940000158231; -.
DR HOGENOM; CLU_057526_1_0_1; -.
DR InParanoid; Q08334; -.
DR OMA; NPDDSCS; -.
DR OrthoDB; 892736at2759; -.
DR PhylomeDB; Q08334; -.
DR TreeFam; TF332537; -.
DR PathwayCommons; Q08334; -.
DR Reactome; R-HSA-449836; Other interleukin signaling.
DR Reactome; R-HSA-6783783; Interleukin-10 signaling.
DR Reactome; R-HSA-8854691; Interleukin-20 family signaling.
DR SignaLink; Q08334; -.
DR SIGNOR; Q08334; -.
DR BioGRID-ORCS; 3588; 10 hits in 1077 CRISPR screens.
DR ChiTaRS; IL10RB; human.
DR EvolutionaryTrace; Q08334; -.
DR GeneWiki; Interleukin_10_receptor,_beta_subunit; -.
DR GenomeRNAi; 3588; -.
DR Pharos; Q08334; Tbio.
DR PRO; PR:Q08334; -.
DR Proteomes; UP000005640; Chromosome 21.
DR RNAct; Q08334; protein.
DR Bgee; ENSG00000243646; Expressed in placenta and 98 other tissues.
DR ExpressionAtlas; Q08334; baseline and differential.
DR Genevisible; Q08334; HS.
DR GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0032002; C:interleukin-28 receptor complex; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central.
DR GO; GO:0004920; F:interleukin-10 receptor activity; IBA:GO_Central.
DR GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
DR GO; GO:0098586; P:cellular response to virus; IC:ComplexPortal.
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:0006955; P:immune response; TAS:ProtInc.
DR GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
DR GO; GO:1901857; P:positive regulation of cellular respiration; IMP:ARUK-UCL.
DR GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; IDA:UniProtKB.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0038196; P:type III interferon signaling pathway; IC:ComplexPortal.
DR CDD; cd00063; FN3; 1.
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 SUPFAM; SSF49265; SSF49265; 2.
DR PROSITE; PS50853; FN3; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Membrane; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 20..325
FT /note="Interleukin-10 receptor subunit beta"
FT /id="PRO_0000011014"
FT TOPO_DOM 20..220
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 243..325
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 114..216
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 301..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 68
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 DISULFID 66..74
FT /evidence="ECO:0000269|PubMed:20462497"
FT DISULFID 188..209
FT /evidence="ECO:0000269|PubMed:20462497"
FT VARIANT 47
FT /note="K -> E (associated with susceptibility to HBV
FT infection; higher cell surface levels; dbSNP:rs2834167)"
FT /evidence="ECO:0000269|PubMed:16757563, ECO:0000269|Ref.4"
FT /id="VAR_020666"
FT CONFLICT 124
FT /note="A -> D (in Ref. 2; AAA86872)"
FT /evidence="ECO:0000305"
FT CONFLICT 243
FT /note="A -> S (in Ref. 1; CAA78933 and 2; AAA86872)"
FT /evidence="ECO:0000305"
FT CONFLICT 269..273
FT /note="FLGHP -> VGRME (in Ref. 2; AAA86872)"
FT /evidence="ECO:0000305"
FT CONFLICT 274..325
FT /note="Missing (in Ref. 2; AAA86872)"
FT /evidence="ECO:0000305"
FT STRAND 25..32
FT /evidence="ECO:0007829|PDB:3LQM"
FT STRAND 35..41
FT /evidence="ECO:0007829|PDB:3LQM"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:3LQM"
FT STRAND 51..58
FT /evidence="ECO:0007829|PDB:3LQM"
FT STRAND 61..75
FT /evidence="ECO:0007829|PDB:3LQM"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:3LQM"
FT STRAND 85..93
FT /evidence="ECO:0007829|PDB:3LQM"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:3LQM"
FT HELIX 107..110
FT /evidence="ECO:0007829|PDB:3LQM"
FT STRAND 117..123
FT /evidence="ECO:0007829|PDB:3LQM"
FT STRAND 126..132
FT /evidence="ECO:0007829|PDB:3LQM"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:3LQM"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:6X93"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:3LQM"
FT HELIX 145..148
FT /evidence="ECO:0007829|PDB:3LQM"
FT STRAND 153..160
FT /evidence="ECO:0007829|PDB:3LQM"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:5T5W"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:3LQM"
FT STRAND 172..178
FT /evidence="ECO:0007829|PDB:3LQM"
FT STRAND 186..194
FT /evidence="ECO:0007829|PDB:3LQM"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:3LQM"
FT STRAND 208..211
FT /evidence="ECO:0007829|PDB:3LQM"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:3LQM"
SQ SEQUENCE 325 AA; 36995 MW; E470726619AF54C2 CRC64;
MAWSLGSWLG GCLLVSALGM VPPPENVRMN SVNFKNILQW ESPAFAKGNL TFTAQYLSYR
IFQDKCMNTT LTECDFSSLS KYGDHTLRVR AEFADEHSDW VNITFCPVDD TIIGPPGMQV
EVLADSLHMR FLAPKIENEY ETWTMKNVYN SWTYNVQYWK NGTDEKFQIT PQYDFEVLRN
LEPWTTYCVQ VRGFLPDRNK AGEWSEPVCE QTTHDETVPS WMVAVILMAS VFMVCLALLG
CFALLWCVYK KTKYAFSPRN SLPQHLKEFL GHPHHNTLLF FSFPLSDEND VFDKLSVIAE
DSESGKQNPG DSCSLGTPPG QGPQS
