I10R1_HUMAN
ID I10R1_HUMAN Reviewed; 578 AA.
AC Q13651; A8K6I0; B0YJ27;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 2.
DT 03-AUG-2022, entry version 184.
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 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], AND VARIANT GLY-351.
RC TISSUE=Lymphoma;
RX PubMed=8120391;
RA Liu Y., Wei S.H.-Y., Ho A.S.-Y., de Waal Malefyt R., Moore K.W.;
RT "Expression cloning and characterization of a human IL-10 receptor.";
RL J. Immunol. 152:1821-1829(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-61; ILE-113; GLY-159;
RP GLN-212; GLY-351 AND LEU-420.
RG SeattleSNPs variation discovery resource;
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLY-351.
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLY-351.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLY-351.
RC TISSUE=Blood;
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 [8]
RP PROTEIN SEQUENCE OF 22-36.
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 [9]
RP FUNCTION, AND INTERACTION WITH JAK1.
RX PubMed=12133952; DOI=10.4049/jimmunol.169.3.1302;
RA Usacheva A., Kotenko S., Witte M.M., Colamonici O.R.;
RT "Two distinct domains within the N-terminal region of Janus kinase 1
RT interact with cytokine receptors.";
RL J. Immunol. 169:1302-1308(2002).
RN [10]
RP FUNCTION, AND INTERACTION WITH IL10 AND IL10RB.
RX PubMed=16982608; DOI=10.1074/jbc.m606791200;
RA Yoon S.I., Logsdon N.J., Sheikh F., Donnelly R.P., Walter M.R.;
RT "Conformational changes mediate interleukin-10 receptor 2 (IL-10R2) binding
RT to IL-10 and assembly of the signaling complex.";
RL J. Biol. Chem. 281:35088-35096(2006).
RN [11]
RP INTERACTION WITH BTRC, SUBCELLULAR LOCATION, AND UBIQUITINATION.
RX PubMed=22087322; DOI=10.1371/journal.pone.0027464;
RA Jiang H., Lu Y., Yuan L., Liu J.;
RT "Regulation of interleukin-10 receptor ubiquitination and stability by
RT beta-TrCP-containing ubiquitin E3 ligase.";
RL PLoS ONE 6:E27464-E27464(2011).
RN [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=26962683; DOI=10.1038/cddis.2016.44;
RA Shi J., Wang H., Guan H., Shi S., Li Y., Wu X., Li N., Yang C., Bai X.,
RA Cai W., Yang F., Wang X., Su L., Zheng Z., Hu D.;
RT "IL10 inhibits starvation-induced autophagy in hypertrophic scar
RT fibroblasts via cross talk between the IL10-IL10R-STAT3 and IL10-AKT-mTOR
RT pathways.";
RL Cell Death Dis. 7:E2133-E2133(2016).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 22-235 IN COMPLEX WITH IL10, AND
RP DISULFIDE BONDS.
RX PubMed=11485736; DOI=10.1016/s1074-7613(01)00169-8;
RA Josephson K., Logsdon N.J., Walter M.R.;
RT "Crystal structure of the IL-10/IL-10R1 complex reveals a shared receptor
RT binding site.";
RL Immunity 15:35-46(2001).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 22-235 IN COMPLEX WITH
RP CYTOMEGALOVIRUS IL10 (MICROBIAL INFECTION).
RX PubMed=12093920; DOI=10.1073/pnas.152147499;
RA Jones B.C., Logsdon N.J., Josephson K., Cook J., Barry P.A., Walter M.R.;
RT "Crystal structure of human cytomegalovirus IL-10 bound to soluble human
RT IL-10R1.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:9404-9409(2002).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 22-335 IN COMPLEX WITH IL10 AND
RP EPSTEIN-BARR VIRUS IL10 (MICROBIAL INFECTION).
RX PubMed=15837194; DOI=10.1016/j.str.2005.01.016;
RA Yoon S.I., Jones B.C., Logsdon N.J., Walter M.R.;
RT "Same structure, different function crystal structure of the Epstein-Barr
RT virus IL-10 bound to the soluble IL-10R1 chain.";
RL Structure 13:551-564(2005).
RN [16]
RP VARIANTS IBD28 ILE-84 AND ARG-141.
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 [17]
RP VARIANTS IBD28 CYS-91; TRP-101; HIS-117 AND CYS-262.
RX PubMed=23839161; DOI=10.1097/meg.0b013e328361a4f9;
RA Shim J.O., Hwang S., Yang H.R., Moon J.S., Chang J.Y., Ko J.S., Park S.S.,
RA Kang G.H., Kim W.S., Seo J.K.;
RT "Interleukin-10 receptor mutations in children with neonatal-onset Crohn's
RT disease and intractable ulcerating enterocolitis.";
RL Eur. J. Gastroenterol. Hepatol. 25:1235-1240(2013).
RN [18]
RP VARIANTS IBD28 ARG-69; CYS-91; TRP-101; HIS-117 AND CYS-262.
RX PubMed=24785691; DOI=10.1038/jhg.2014.32;
RA Shim J.O., Seo J.K.;
RT "Very early-onset inflammatory bowel disease (IBD) in infancy is a
RT different disease entity from adult-onset IBD; one form of interleukin-10
RT receptor mutations.";
RL J. Hum. Genet. 59:337-341(2014).
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 (PubMed:16982608). In turn, the heterotetrameric assembly complex,
CC composed of two subunits of IL10RA and IL10RB, activates the kinases
CC JAK1 and TYK2 that are constitutively associated with IL10RA and IL10RB
CC respectively (PubMed:12133952). These kinases then phosphorylate
CC specific tyrosine residues in the intracellular domain in IL10RA
CC leading to the recruitment and subsequent phosphorylation of STAT3.
CC Once phosphorylated, STAT3 homodimerizes, translocates to the nucleus
CC and activates the expression of anti-inflammatory genes. In addition,
CC IL10RA-mediated activation of STAT3 inhibits starvation-induced
CC autophagy (PubMed:26962683). {ECO:0000269|PubMed:12133952,
CC ECO:0000269|PubMed:16982608, ECO:0000269|PubMed:26962683}.
CC -!- SUBUNIT: Interacts with IL10 (PubMed:16982608, PubMed:15837194).
CC Interacts with IL10RB (PubMed:16982608). Interacts (via its cytoplasmic
CC domain) with JAK1 (via N-terminus) (PubMed:12133952). Interacts with
CC BTRC; this interaction leads to IL10RA ubiquitination and subsequent
CC degradation (PubMed:22087322). Interacts with STAT3 (By similarity).
CC {ECO:0000250|UniProtKB:Q61727, ECO:0000269|PubMed:12133952,
CC ECO:0000269|PubMed:15837194, ECO:0000269|PubMed:16982608,
CC ECO:0000269|PubMed:22087322}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human cytomegalovirus
CC protein IL10. {ECO:0000269|PubMed:12093920}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Epstein-Barr virus
CC protein IL10. {ECO:0000269|PubMed:15837194}.
CC -!- INTERACTION:
CC Q13651; P27449: ATP6V0C; NbExp=3; IntAct=EBI-1031656, EBI-721179;
CC Q13651; Q9Y297: BTRC; NbExp=6; IntAct=EBI-1031656, EBI-307461;
CC Q13651; Q86Z23: C1QL4; NbExp=3; IntAct=EBI-1031656, EBI-12062109;
CC Q13651; Q8IX05: CD302; NbExp=3; IntAct=EBI-1031656, EBI-14259393;
CC Q13651; O95674: CDS2; NbExp=3; IntAct=EBI-1031656, EBI-3913685;
CC Q13651; Q96MX0: CMTM3; NbExp=3; IntAct=EBI-1031656, EBI-7247651;
CC Q13651; P02724: GYPA; NbExp=3; IntAct=EBI-1031656, EBI-702665;
CC Q13651; B0YJ81: HACD1; NbExp=3; IntAct=EBI-1031656, EBI-12051643;
CC Q13651; Q6Y1H2: HACD2; NbExp=3; IntAct=EBI-1031656, EBI-530257;
CC Q13651; P22301: IL10; NbExp=9; IntAct=EBI-1031656, EBI-1031632;
CC Q13651; P21145: MAL; NbExp=3; IntAct=EBI-1031656, EBI-3932027;
CC Q13651; Q0D2K0: NIPAL4; NbExp=3; IntAct=EBI-1031656, EBI-9550165;
CC Q13651; Q8IY26: PLPP6; NbExp=3; IntAct=EBI-1031656, EBI-11721828;
CC Q13651; Q96GQ5: RUSF1; NbExp=3; IntAct=EBI-1031656, EBI-8636004;
CC Q13651; Q9Y6D0: SELENOK; NbExp=3; IntAct=EBI-1031656, EBI-9679163;
CC Q13651; Q9BRI3: SLC30A2; NbExp=3; IntAct=EBI-1031656, EBI-8644112;
CC Q13651; Q9NVC3: SLC38A7; NbExp=3; IntAct=EBI-1031656, EBI-10314552;
CC Q13651; Q8N2U9: SLC66A2; NbExp=3; IntAct=EBI-1031656, EBI-3907610;
CC Q13651; Q8TBB6: SLC7A14; NbExp=3; IntAct=EBI-1031656, EBI-5235586;
CC Q13651; Q9NRQ5: SMCO4; NbExp=3; IntAct=EBI-1031656, EBI-8640191;
CC Q13651; Q9NWH2: TMEM242; NbExp=3; IntAct=EBI-1031656, EBI-10315004;
CC Q13651; Q9H2L4: TMEM60; NbExp=3; IntAct=EBI-1031656, EBI-2852148;
CC Q13651; Q71RG4: TMUB2; NbExp=3; IntAct=EBI-1031656, EBI-2820477;
CC Q13651; O95183: VAMP5; NbExp=3; IntAct=EBI-1031656, EBI-10191195;
CC Q13651; Q96EC8: YIPF6; NbExp=3; IntAct=EBI-1031656, EBI-751210;
CC Q13651; P03180: BCRF1; Xeno; NbExp=4; IntAct=EBI-1031656, EBI-1042167;
CC Q13651; P03495: NS; Xeno; NbExp=2; IntAct=EBI-1031656, EBI-2548993;
CC Q13651; P17150: UL111A; Xeno; NbExp=2; IntAct=EBI-1031656, EBI-1033736;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22087322,
CC ECO:0000269|PubMed:26962683}; Single-pass type I membrane protein.
CC Cytoplasm {ECO:0000269|PubMed:26962683}.
CC -!- TISSUE SPECIFICITY: Primarily expressed in hematopoetic cells including
CC B-cells, T-cells, NK cells, monocytes and macrophages. Not expressed in
CC non-hematopoetic cells such as fibroblasts or endothelial cells.
CC -!- PTM: Phosphorylated. Phosphorylation of the cytoplasmic tail induced
CC STAT3 activation. {ECO:0000250|UniProtKB:Q61727}.
CC -!- PTM: Ubiquitinated by BTRC; ubiquitination leads to endocytosis and
CC subsequent degradation of IL10RA. {ECO:0000269|PubMed:22087322}.
CC -!- DISEASE: Inflammatory bowel disease 28, autosomal recessive (IBD28)
CC [MIM:613148]: 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,
CC ECO:0000269|PubMed:23839161, ECO:0000269|PubMed:24785691}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC 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/il10ra/";
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DR EMBL; U00672; AAA17896.1; -; mRNA.
DR EMBL; AY195619; AAN86349.1; -; Genomic_DNA.
DR EMBL; EF444988; ACA06005.1; -; Genomic_DNA.
DR EMBL; AK291645; BAF84334.1; -; mRNA.
DR EMBL; AP002962; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471065; EAW67343.1; -; Genomic_DNA.
DR EMBL; BC028082; AAH28082.1; -; mRNA.
DR CCDS; CCDS8388.1; -.
DR PIR; I56215; I56215.
DR RefSeq; NP_001549.2; NM_001558.3.
DR PDB; 1J7V; X-ray; 2.90 A; R=22-235.
DR PDB; 1LQS; X-ray; 2.70 A; R/S=22-235.
DR PDB; 1Y6K; X-ray; 2.52 A; R=22-235.
DR PDB; 1Y6M; X-ray; 2.80 A; R=22-235.
DR PDB; 1Y6N; X-ray; 2.70 A; R=22-235.
DR PDB; 5IXI; X-ray; 2.57 A; B=263-303.
DR PDB; 6X93; EM; 3.50 A; B/E=22-235.
DR PDBsum; 1J7V; -.
DR PDBsum; 1LQS; -.
DR PDBsum; 1Y6K; -.
DR PDBsum; 1Y6M; -.
DR PDBsum; 1Y6N; -.
DR PDBsum; 5IXI; -.
DR PDBsum; 6X93; -.
DR AlphaFoldDB; Q13651; -.
DR SMR; Q13651; -.
DR BioGRID; 109801; 23.
DR CORUM; Q13651; -.
DR DIP; DIP-3512N; -.
DR IntAct; Q13651; 32.
DR MINT; Q13651; -.
DR STRING; 9606.ENSP00000227752; -.
DR GuidetoPHARMACOLOGY; 1727; -.
DR GlyGen; Q13651; 6 sites.
DR iPTMnet; Q13651; -.
DR PhosphoSitePlus; Q13651; -.
DR BioMuta; IL10RA; -.
DR DMDM; 322510034; -.
DR PaxDb; Q13651; -.
DR PeptideAtlas; Q13651; -.
DR PRIDE; Q13651; -.
DR Antibodypedia; 18560; 858 antibodies from 40 providers.
DR DNASU; 3587; -.
DR Ensembl; ENST00000227752.8; ENSP00000227752.4; ENSG00000110324.11.
DR GeneID; 3587; -.
DR KEGG; hsa:3587; -.
DR MANE-Select; ENST00000227752.8; ENSP00000227752.4; NM_001558.4; NP_001549.2.
DR UCSC; uc001prv.5; human.
DR CTD; 3587; -.
DR DisGeNET; 3587; -.
DR GeneCards; IL10RA; -.
DR HGNC; HGNC:5964; IL10RA.
DR HPA; ENSG00000110324; Tissue enhanced (bone marrow, lymphoid tissue).
DR MalaCards; IL10RA; -.
DR MIM; 146933; gene.
DR MIM; 613148; phenotype.
DR neXtProt; NX_Q13651; -.
DR OpenTargets; ENSG00000110324; -.
DR Orphanet; 238569; Immune dysregulation-inflammatory bowel disease-arthritis-recurrent infections syndrome.
DR PharmGKB; PA29779; -.
DR VEuPathDB; HostDB:ENSG00000110324; -.
DR eggNOG; ENOG502S2PS; Eukaryota.
DR GeneTree; ENSGT00510000048847; -.
DR HOGENOM; CLU_033904_0_0_1; -.
DR InParanoid; Q13651; -.
DR OMA; SHFREYE; -.
DR OrthoDB; 1456451at2759; -.
DR PhylomeDB; Q13651; -.
DR TreeFam; TF334107; -.
DR PathwayCommons; Q13651; -.
DR Reactome; R-HSA-6783783; Interleukin-10 signaling.
DR SignaLink; Q13651; -.
DR SIGNOR; Q13651; -.
DR BioGRID-ORCS; 3587; 12 hits in 1076 CRISPR screens.
DR ChiTaRS; IL10RA; human.
DR EvolutionaryTrace; Q13651; -.
DR GeneWiki; Interleukin_10_receptor,_alpha_subunit; -.
DR GenomeRNAi; 3587; -.
DR Pharos; Q13651; Tbio.
DR PRO; PR:Q13651; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q13651; protein.
DR Bgee; ENSG00000110324; Expressed in granulocyte and 155 other tissues.
DR ExpressionAtlas; Q13651; baseline and differential.
DR Genevisible; Q13651; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central.
DR GO; GO:0019969; F:interleukin-10 binding; IEA:Ensembl.
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:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0010507; P:negative regulation of autophagy; IDA:UniProtKB.
DR GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; IDA:UniProtKB.
DR GO; GO:0050807; P:regulation of synapse organization; IEA:Ensembl.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0070086; P:ubiquitin-dependent endocytosis; IDA:UniProtKB.
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 3D-structure; Cell membrane; Cytoplasm; Direct protein sequencing;
KW Disease variant; Disulfide bond; Glycoprotein; Membrane; Phosphoprotein;
KW Receptor; Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 22..578
FT /note="Interleukin-10 receptor subunit alpha"
FT /id="PRO_0000011012"
FT TOPO_DOM 22..235
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 257..578
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 313..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 318..323
FT /note="BTRC recognition motif"
FT /evidence="ECO:0000269|PubMed:22087322"
FT COMPBIAS 316..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 56..75
FT /evidence="ECO:0000269|PubMed:11485736"
FT DISULFID 202..223
FT /evidence="ECO:0000269|PubMed:11485736"
FT VARIANT 61
FT /note="L -> V (in dbSNP:rs4252250)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_016294"
FT VARIANT 69
FT /note="W -> R (in IBD28; dbSNP:rs1343534194)"
FT /evidence="ECO:0000269|PubMed:24785691"
FT /id="VAR_071663"
FT VARIANT 84
FT /note="T -> I (in IBD28; dbSNP:rs137853580)"
FT /evidence="ECO:0000269|PubMed:19890111"
FT /id="VAR_063542"
FT VARIANT 91
FT /note="Y -> C (in IBD28; dbSNP:rs1591261607)"
FT /evidence="ECO:0000269|PubMed:23839161,
FT ECO:0000269|PubMed:24785691"
FT /id="VAR_071664"
FT VARIANT 101
FT /note="R -> W (in IBD28; dbSNP:rs368287711)"
FT /evidence="ECO:0000269|PubMed:23839161,
FT ECO:0000269|PubMed:24785691"
FT /id="VAR_071665"
FT VARIANT 113
FT /note="V -> I (in dbSNP:rs4252303)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_016295"
FT VARIANT 117
FT /note="R -> H (in IBD28; dbSNP:rs199989396)"
FT /evidence="ECO:0000269|PubMed:23839161,
FT ECO:0000269|PubMed:24785691"
FT /id="VAR_071666"
FT VARIANT 141
FT /note="G -> R (in IBD28; dbSNP:rs137853579)"
FT /evidence="ECO:0000269|PubMed:19890111"
FT /id="VAR_063543"
FT VARIANT 159
FT /note="S -> G (in dbSNP:rs3135932)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_016296"
FT VARIANT 212
FT /note="R -> Q (in dbSNP:rs4252273)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_016297"
FT VARIANT 224
FT /note="I -> V (in dbSNP:rs2228055)"
FT /id="VAR_020004"
FT VARIANT 262
FT /note="R -> C (in IBD28; dbSNP:rs149491038)"
FT /evidence="ECO:0000269|PubMed:23839161,
FT ECO:0000269|PubMed:24785691"
FT /id="VAR_071667"
FT VARIANT 351
FT /note="R -> G (in dbSNP:rs2229113)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:8120391,
FT ECO:0000269|Ref.2, ECO:0000269|Ref.6"
FT /id="VAR_016298"
FT VARIANT 353
FT /note="P -> S (in dbSNP:rs35235073)"
FT /id="VAR_049175"
FT VARIANT 420
FT /note="S -> L (in dbSNP:rs2229114)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_016299"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:1Y6K"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:1Y6K"
FT STRAND 56..63
FT /evidence="ECO:0007829|PDB:1Y6K"
FT STRAND 70..82
FT /evidence="ECO:0007829|PDB:1Y6K"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:1Y6K"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:1Y6K"
FT STRAND 96..104
FT /evidence="ECO:0007829|PDB:1Y6K"
FT STRAND 107..113
FT /evidence="ECO:0007829|PDB:6X93"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:1Y6K"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:1Y6K"
FT STRAND 128..134
FT /evidence="ECO:0007829|PDB:1Y6K"
FT STRAND 136..144
FT /evidence="ECO:0007829|PDB:1Y6K"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:1Y6K"
FT HELIX 157..160
FT /evidence="ECO:0007829|PDB:1Y6K"
FT STRAND 165..176
FT /evidence="ECO:0007829|PDB:1Y6K"
FT STRAND 181..193
FT /evidence="ECO:0007829|PDB:1Y6K"
FT STRAND 199..209
FT /evidence="ECO:0007829|PDB:1Y6K"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:1Y6K"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:5IXI"
SQ SEQUENCE 578 AA; 63003 MW; 54B183ABE84808DB CRC64;
MLPCLVVLLA ALLSLRLGSD AHGTELPSPP SVWFEAEFFH HILHWTPIPN QSESTCYEVA
LLRYGIESWN SISNCSQTLS YDLTAVTLDL YHSNGYRARV RAVDGSRHSN WTVTNTRFSV
DEVTLTVGSV NLEIHNGFIL GKIQLPRPKM APANDTYESI FSHFREYEIA IRKVPGNFTF
THKKVKHENF SLLTSGEVGE FCVQVKPSVA SRSNKGMWSK EECISLTRQY FTVTNVIIFF
AFVLLLSGAL AYCLALQLYV RRRKKLPSVL LFKKPSPFIF ISQRPSPETQ DTIHPLDEEA
FLKVSPELKN LDLHGSTDSG FGSTKPSLQT EEPQFLLPDP HPQADRTLGN REPPVLGDSC
SSGSSNSTDS GICLQEPSLS PSTGPTWEQQ VGSNSRGQDD SGIDLVQNSE GRAGDTQGGS
ALGHHSPPEP EVPGEEDPAA VAFQGYLRQT RCAEEKATKT GCLEEESPLT DGLGPKFGRC
LVDEAGLHPP ALAKGYLKQD PLEMTLASSG APTGQWNQPT EEWSLLALSS CSDLGISDWS
FAHDLAPLGC VAAPGGLLGS FNSDLVTLPL ISSLQSSE
