I10R1_MOUSE
ID I10R1_MOUSE Reviewed; 575 AA.
AC Q61727;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Interleukin-10 receptor subunit alpha;
DE Short=IL-10 receptor subunit alpha;
DE Short=IL-10R subunit alpha;
DE Short=IL-10RA;
DE AltName: Full=CDw210a;
DE AltName: Full=Interleukin-10 receptor subunit 1;
DE Short=IL-10R subunit 1;
DE Short=IL-10R1;
DE AltName: CD_antigen=CD210;
DE Flags: Precursor;
GN Name=Il10ra; Synonyms=Il10r;
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/6 X AJ F1; TISSUE=Hematopoietic;
RX PubMed=8248239; DOI=10.1073/pnas.90.23.11267;
RA Ho A.S.-Y., Liu Y., Khan T.A., Hsu D.-H., Bazan J.F., Moore K.W.;
RT "A receptor for interleukin 10 is related to interferon receptors.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:11267-11271(1993).
RN [2]
RP FUNCTION, INTERACTION WITH STAT3, PHOSPHORYLATION AT TYR-443 AND TYR-493,
RP AND MUTAGENESIS OF TYR-443 AND TYR-493.
RX PubMed=8910398; DOI=10.1074/jbc.271.44.27954;
RA Weber-Nordt R.M., Riley J.K., Greenlund A.C., Moore K.W., Darnell J.E.,
RA Schreiber R.D.;
RT "Stat3 recruitment by two distinct ligand-induced, tyrosine-phosphorylated
RT docking sites in the interleukin-10 receptor intracellular domain.";
RL J. Biol. Chem. 271:27954-27961(1996).
CC -!- FUNCTION: Cell surface receptor for the cytokine IL10 that participates
CC in IL10-mediated anti-inflammatory functions, limiting excessive tissue
CC disruption caused by inflammation. Upon binding to IL10, induces a
CC conformational change in IL10RB, allowing IL10RB to bind IL10 as well.
CC In turn, the heterotetrameric assembly complex, composed of two
CC subunits of IL10RA and IL10RB, activates the kinases JAK1 and TYK2 that
CC are constitutively associated with IL10RA and IL10RB respectively.
CC These kinases then phosphorylate specific tyrosine residues in the
CC intracellular domain in IL10RA leading to the recruitment and
CC subsequent phosphorylation of STAT3 (PubMed:8910398). Once
CC phosphorylated, STAT3 homodimerizes, translocates to the nucleus and
CC activates the expression of anti-inflammatory genes. In addition,
CC IL10RA-mediated activation of STAT3 inhibits starvation-induced
CC autophagy (By similarity). {ECO:0000250|UniProtKB:Q13651,
CC ECO:0000269|PubMed:8910398}.
CC -!- SUBUNIT: Interacts with IL10. Interacts with IL10RB. Interacts (via its
CC cytoplasmic domain) with JAK1 (via N-terminus). Interacts with BTRC;
CC this interaction leads to IL10RA ubiquitination and subsequent
CC degradation (By similarity). Interacts with STAT3 (PubMed:8910398).
CC {ECO:0000250|UniProtKB:Q13651, ECO:0000269|PubMed:8910398}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q13651};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q13651}.
CC Cytoplasm {ECO:0000250|UniProtKB:Q13651}.
CC -!- PTM: Phosphorylated. Phosphorylation of the cytoplasmic tail induced
CC STAT3 activation. {ECO:0000269|PubMed:8910398}.
CC -!- PTM: Ubiquitinated by BTRC; ubiquitination leads to endocytosis and
CC subsequent degradation of IL10RA. {ECO:0000250|UniProtKB:Q13651}.
CC -!- SIMILARITY: Belongs to the type II cytokine receptor family.
CC {ECO:0000305}.
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DR EMBL; L12120; AAA16156.1; -; mRNA.
DR CCDS; CCDS23131.1; -.
DR PIR; A49667; A49667.
DR RefSeq; NP_032374.1; NM_008348.3.
DR AlphaFoldDB; Q61727; -.
DR SMR; Q61727; -.
DR DIP; DIP-247N; -.
DR IntAct; Q61727; 1.
DR STRING; 10090.ENSMUSP00000034594; -.
DR GlyGen; Q61727; 5 sites.
DR iPTMnet; Q61727; -.
DR PhosphoSitePlus; Q61727; -.
DR PaxDb; Q61727; -.
DR PRIDE; Q61727; -.
DR ProteomicsDB; 273067; -.
DR Antibodypedia; 18560; 858 antibodies from 40 providers.
DR DNASU; 16154; -.
DR Ensembl; ENSMUST00000034594; ENSMUSP00000034594; ENSMUSG00000032089.
DR GeneID; 16154; -.
DR KEGG; mmu:16154; -.
DR UCSC; uc009pfn.1; mouse.
DR CTD; 3587; -.
DR MGI; MGI:96538; Il10ra.
DR VEuPathDB; HostDB:ENSMUSG00000032089; -.
DR eggNOG; ENOG502S2PS; Eukaryota.
DR GeneTree; ENSGT00510000048847; -.
DR HOGENOM; CLU_033904_0_0_1; -.
DR InParanoid; Q61727; -.
DR OMA; SHFREYE; -.
DR OrthoDB; 1456451at2759; -.
DR PhylomeDB; Q61727; -.
DR TreeFam; TF334107; -.
DR Reactome; R-MMU-6783783; Interleukin-10 signaling.
DR BioGRID-ORCS; 16154; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Il10ra; mouse.
DR PRO; PR:Q61727; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q61727; protein.
DR Bgee; ENSMUSG00000032089; Expressed in granulocyte and 62 other tissues.
DR ExpressionAtlas; Q61727; baseline and differential.
DR Genevisible; Q61727; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central.
DR GO; GO:0019969; F:interleukin-10 binding; ISO:MGI.
DR GO; GO:0004920; F:interleukin-10 receptor activity; ISO:MGI.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0010507; P:negative regulation of autophagy; ISO:MGI.
DR GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; ISO:MGI.
DR GO; GO:0050807; P:regulation of synapse organization; ISO:MGI.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0070086; P:ubiquitin-dependent endocytosis; ISO:MGI.
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.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Disulfide bond; Glycoprotein; Membrane;
KW Phosphoprotein; Receptor; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Ubl conjugation.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..575
FT /note="Interleukin-10 receptor subunit alpha"
FT /id="PRO_0000011013"
FT TOPO_DOM 17..241
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 263..575
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 443
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:8910398"
FT MOD_RES 493
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:8910398"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 238
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 204..225
FT /evidence="ECO:0000255"
FT MUTAGEN 443
FT /note="Y->F: Complete loss of STAT3 activation; in
FT association with F-493."
FT /evidence="ECO:0000269|PubMed:8910398"
FT MUTAGEN 493
FT /note="Y->F: Complete loss of STAT3 activation; in
FT association with F-443."
FT /evidence="ECO:0000269|PubMed:8910398"
SQ SEQUENCE 575 AA; 64248 MW; 820B9CD576F686B7 CRC64;
MLSRLLPFLV TISSLSLEFI AYGTELPSPS YVWFEARFFQ HILHWKPIPN QSESTYYEVA
LKQYGNSTWN DIHICRKAQA LSCDLTTFTL DLYHRSYGYR ARVRAVDNSQ YSNWTTTETR
FTVDEVILTV DSVTLKAMDG IIYGTIHPPR PTITPAGDEY EQVFKDLRVY KISIRKFSEL
KNATKRVKQE TFTLTVPIGV RKFCVKVLPR LESRINKAEW SEEQCLLITT EQYFTVTNLS
ILVISMLLFC GILVCLVLQW YIRHPGKLPT VLVFKKPHDF FPANPLCPET PDAIHIVDLE
VFPKVSLELR DSVLHGSTDS GFGSGKPSLQ TEESQFLLPG SHPQIQGTLG KEESPGLQAT
CGDNTDSGIC LQEPGLHSSM GPAWKQQLGY THQDQDDSDV NLVQNSPGQP KYTQDASALG
HVCLLEPKAP EEKDQVMVTF QGYQKQTRWK AEAAGPAECL DEEIPLTDAF DPELGVHLQD
DLAWPPPALA AGYLKQESQG MASAPPGTPS RQWNQLTEEW SLLGVVSCED LSIESWRFAH
KLDPLDCGAA PGGLLDSLGS NLVTLPLISS LQVEE
