ID IL31R_HUMAN Reviewed; 732 AA. AC Q8NI17; A6NIF8; Q2TBA1; Q6EBC3; Q6EBC4; Q6EBC5; Q6EBC6; Q6UWL8; Q8WYJ0; DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 09-APR-2025, entry version 176. DE RecName: Full=Interleukin-31 receptor subunit alpha; DE Short=IL-31 receptor subunit alpha; DE Short=IL-31R subunit alpha; DE Short=IL-31R-alpha; DE Short=IL-31RA; DE AltName: Full=Cytokine receptor-like 3; DE AltName: Full=GLM-R; DE Short=hGLM-R; DE AltName: Full=Gp130-like monocyte receptor; DE Short=Gp130-like receptor; DE AltName: Full=ZcytoR17; DE Flags: Precursor; GN Name=IL31RA; Synonyms=CRL3, GPL; ORFNames=UNQ6368/PRO21073/PRO21384; 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] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, RP SUBCELLULAR LOCATION, AND INDUCTION. RX PubMed=11877449; DOI=10.1074/jbc.m201140200; RA Ghilardi N., Li J., Hongo J.-A., Yi S., Gurney A., De Sauvage F.J.; RT "A novel type I cytokine receptor is expressed on monocytes, signals RT proliferation, and activates STAT-3 and STAT-5."; RL J. Biol. Chem. 277:16831-16836(2002). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4 AND 5), FUNCTION, RP OLIGOMERIZATION, TISSUE SPECIFICITY, AND INDUCTION. RX PubMed=15184896; DOI=10.1038/ni1084; RA Dillon S.R., Sprecher C., Hammond A., Bilsborough J., RA Rosenfeld-Franklin M., Presnell S.R., Haugen H.S., Maurer M., Harder B., RA Johnston J., Bort S., Mudri S., Kuijper J.L., Bukowski T., Shea P., RA Dong D.L., Dasovich M., Grant F.J., Lockwood L., Levin S.D., LeCiel C., RA Waggie K., Day H., Topouzis S., Kramer J., Kuestner R., Chen Z., Foster D., RA Parrish-Novak J., Gross J.A.; RT "Interleukin 31, a cytokine produced by activated T cells, induces RT dermatitis in mice."; RL Nat. Immunol. 5:752-760(2004). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7). RA Zhang W., Wan T., He L., Yuan Z., Cao X.; RT "A novel soluble type 1 cytokine receptor."; RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 8). RX PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A., RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale effort to RT identify novel human secreted and transmembrane proteins: a bioinformatics RT assessment."; RL Genome Res. 13:2265-2270(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15372022; DOI=10.1038/nature02919; RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S., RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.; RT "The DNA sequence and comparative analysis of human chromosome 5."; RL Nature 431:268-274(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6). 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 [7] 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 [8] RP ALTERNATIVE SPLICING (ISOFORMS 9; 10; 11 AND 12), FUNCTION, TISSUE RP SPECIFICITY, INDUCTION, SUBCELLULAR LOCATION, AND GLYCOSYLATION. RX PubMed=14504285; DOI=10.1074/jbc.m307286200; RA Diveu C., Lelievre E., Perret D., Lagrue Lak-Hal A.-H., Froger J., RA Guillet C., Chevalier S., Rousseau F., Wesa A., Preisser L., Chabbert M., RA Gauchat J.-F., Galy A., Gascan H., Morel A.; RT "GPL, a novel cytokine receptor related to GP130 and leukemia inhibitory RT factor receptor."; RL J. Biol. Chem. 278:49850-49859(2003). RN [9] RP FUNCTION, AND MUTAGENESIS OF TYR-639; TYR-670 AND TYR-708. RX PubMed=15627637; RA Diveu C., Lagrue Lak-Hal A.-H., Froger J., Ravon E., Grimaud L., RA Barbier F., Hermann J., Gascan H., Chevalier S.; RT "Predominant expression of the long isoform of GP130-like (GPL) receptor is RT required for interleukin-31 signaling."; RL Eur. Cytokine Netw. 15:291-302(2004). RN [10] RP FUNCTION, INTERACTION WITH JAK1 AND STAT3, AND MUTAGENESIS OF TYR-639; RP TYR-670 AND TYR-708. RX PubMed=15194700; DOI=10.1074/jbc.m401122200; RA Dreuw A., Radtke S., Pflanz S., Lippok B.E., Heinrich P.C., Hermanns H.M.; RT "Characterization of the signaling capacities of the novel gp130-like RT cytokine receptor."; RL J. Biol. Chem. 279:36112-36120(2004). RN [11] RP INDUCTION, AND TISSUE SPECIFICITY. RX PubMed=16461143; DOI=10.1016/j.jaci.2005.10.046; RA Bilsborough J., Leung D.Y.M., Maurer M., Howell M., Boguniewicz M., Yao L., RA Storey H., LeCiel C., Harder B., Gross J.A.; RT "IL-31 is associated with cutaneous lymphocyte antigen-positive skin homing RT T cells in patients with atopic dermatitis."; RL J. Allergy Clin. Immunol. 117:418-425(2006). RN [12] RP TISSUE SPECIFICITY, AND INDUCTION. RX PubMed=18439099; DOI=10.1089/jir.2007.0057; RA Jawa R.S., Chattopadhyay S., Tracy E., Wang Y., Huntoon K., Dayton M.T., RA Baumann H.; RT "Regulated expression of the IL-31 receptor in bronchial and alveolar RT epithelial cells, pulmonary fibroblasts, and pulmonary macrophages."; RL J. Interferon Cytokine Res. 28:207-219(2008). RN [13] RP TISSUE SPECIFICITY, AND INDUCTION. RX PubMed=21261663; DOI=10.1111/j.1398-9995.2011.02545.x; RA Kasraie S., Niebuhr M., Baumert K., Werfel T.; RT "Functional effects of interleukin 31 in human primary keratinocytes."; RL Allergy 66:845-852(2011). RN [14] RP TISSUE SPECIFICITY. RX PubMed=24373353; DOI=10.1016/j.jaci.2013.10.048; RA Cevikbas F., Wang X., Akiyama T., Kempkes C., Savinko T., Antal A., RA Kukova G., Buhl T., Ikoma A., Buddenkotte J., Soumelis V., Feld M., RA Alenius H., Dillon S.R., Carstens E., Homey B., Basbaum A., Steinhoff M.; RT "A sensory neuron-expressed IL-31 receptor mediates T helper cell-dependent RT itch: Involvement of TRPV1 and TRPA1."; RL J. Allergy Clin. Immunol. 133:448-460(2014). RN [15] RP VARIANT PLCA2 PHE-489. RX PubMed=19690585; DOI=10.1038/ejhg.2009.135; RA Lin M.W., Lee D.D., Liu T.T., Lin Y.F., Chen S.Y., Huang C.C., Weng H.Y., RA Liu Y.F., Tanaka A., Arita K., Lai-Cheong J., Palisson F., Chang Y.T., RA Wong C.K., Matsuura I., McGrath J.A., Tsai S.F.; RT "Novel IL31RA gene mutation and ancestral OSMR mutant allele in familial RT primary cutaneous amyloidosis."; RL Eur. J. Hum. Genet. 18:26-32(2010). CC -!- FUNCTION: Associates with OSMR to form the interleukin-31 receptor CC which activates STAT3 and to a lower extent STAT1 and STAT5 CC (PubMed:11877449, PubMed:14504285, PubMed:15194700, PubMed:15627637). CC May function in skin immunity (PubMed:15184896). Mediates IL31-induced CC itch, probably in a manner dependent on cation channels TRPA1 and TRPV1 CC (By similarity). Positively regulates numbers and cycling status of CC immature subsets of myeloid progenitor cells in bone marrow in vivo and CC enhances myeloid progenitor cell survival in vitro (By similarity). CC {ECO:0000250|UniProtKB:Q8K5B1, ECO:0000269|PubMed:11877449, CC ECO:0000269|PubMed:14504285, ECO:0000269|PubMed:15184896, CC ECO:0000269|PubMed:15194700, ECO:0000269|PubMed:15627637}. CC -!- SUBUNIT: Heterodimer with OSMR. Interacts with JAK1 and STAT3. CC {ECO:0000269|PubMed:15194700}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:11877449, CC ECO:0000305|PubMed:14504285}; Single-pass type I membrane protein CC {ECO:0000305|PubMed:11877449, ECO:0000305|PubMed:14504285}. Presynaptic CC cell membrane {ECO:0000250|UniProtKB:Q8K5B1}. Cell projection, axon CC {ECO:0000250|UniProtKB:Q8K5B1}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=12; CC Name=1; CC IsoId=Q8NI17-1; Sequence=Displayed; CC Name=2; Synonyms=v3; CC IsoId=Q8NI17-2; Sequence=VSP_022799; CC Name=3; Synonyms=v4; CC IsoId=Q8NI17-3; Sequence=VSP_022800, VSP_022812, VSP_022813; CC Name=4; Synonyms=v2; CC IsoId=Q8NI17-4; Sequence=VSP_022799, VSP_022801; CC Name=5; Synonyms=v1; CC IsoId=Q8NI17-5; Sequence=VSP_022799, VSP_022812, VSP_022813; CC Name=6; CC IsoId=Q8NI17-6; Sequence=VSP_022798; CC Name=7; CC IsoId=Q8NI17-7; Sequence=VSP_022800, VSP_022802, VSP_022804, CC VSP_022805; CC Name=8; CC IsoId=Q8NI17-8; Sequence=VSP_022799, VSP_022803, VSP_022807; CC Name=9; Synonyms=GPL560, short; CC IsoId=Q8NI17-9; Sequence=VSP_022800, VSP_022806; CC Name=10; Synonyms=GPL610; CC IsoId=Q8NI17-10; Sequence=VSP_022800, VSP_022809, VSP_022810; CC Name=11; Synonyms=GPL626; CC IsoId=Q8NI17-11; Sequence=VSP_022800, VSP_022808, VSP_022811; CC Name=12; Synonyms=GPL745, long; CC IsoId=Q8NI17-12; Sequence=VSP_022800; CC -!- TISSUE SPECIFICITY: Expressed in CD14- and CD56-positive blood cells CC (PubMed:11877449). Expressed in macrophages (PubMed:16461143, CC PubMed:18439099). Expressed in keratinocytes (PubMed:21261663). CC Expressed in a subset of dorsal root ganglia neurons (at protein level) CC (PubMed:24373353). Expressed at low levels in testis, ovary, brain, CC prostate, placenta, thymus, bone marrow, trachea and skin CC (PubMed:11877449, PubMed:14504285, PubMed:15184896). Expressed in CC bronchial and alveolar epithelial cells and pulmonary fibroblasts CC (PubMed:18439099). Detected in all of the myelomonocytic lineage CC (PubMed:14504285). Isoform 6: Expressed at higher levels in lesional CC skin compared to healthy skin of atopic dermatitis patients CC (PubMed:24373353). {ECO:0000269|PubMed:11877449, CC ECO:0000269|PubMed:14504285, ECO:0000269|PubMed:15184896, CC ECO:0000269|PubMed:16461143, ECO:0000269|PubMed:18439099, CC ECO:0000269|PubMed:21261663, ECO:0000269|PubMed:24373353}. CC -!- INDUCTION: Up-regulated in lesional keratinocytes of patients with CC atopic dermatitis (PubMed:16461143). Up-regulated by IFNG/IFN-gamma CC (PubMed:11877449, PubMed:14504285, PubMed:15184896, PubMed:18439099, CC PubMed:21261663). Up-regulated by bacterial lipopolysaccharides (LPS) CC (PubMed:11877449, PubMed:14504285, PubMed:15184896). Up-regulated by CC triacylated lipoprotein (Pam3Cys) (PubMed:21261663). Up-regulated by CC TGFB1/TGF-beta (PubMed:18439099). {ECO:0000269|PubMed:11877449, CC ECO:0000269|PubMed:14504285, ECO:0000269|PubMed:15184896, CC ECO:0000269|PubMed:16461143, ECO:0000269|PubMed:18439099, CC ECO:0000269|PubMed:21261663}. CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:14504285}. CC -!- DISEASE: Amyloidosis, primary localized cutaneous, 2 (PLCA2) CC [MIM:613955]: A primary amyloidosis characterized by localized CC cutaneous amyloid deposition. This condition usually presents with CC itching (especially on the lower legs) and visible changes of skin CC hyperpigmentation and thickening that may be exacerbated by chronic CC scratching and rubbing. Primary localized cutaneous amyloidosis is CC often divided into macular and lichen subtypes although many affected CC individuals often show both variants coexisting. Lichen amyloidosis CC characteristically presents as a pruritic eruption of grouped CC hyperkeratotic papules with a predilection for the shins, calves, CC ankles and dorsa of feet and thighs. Papules may coalesce to form CC hyperkeratotic plaques that can resemble lichen planus, lichen simplex CC or nodular prurigo. Macular amyloidosis is characterized by small CC pigmented macules that may merge to produce macular hyperpigmentation, CC sometimes with a reticulate or rippled pattern. In macular and lichen CC amyloidosis, amyloid is deposited in the papillary dermis in CC association with grouped colloid bodies, thought to represent CC degenerate basal keratinocytes. The amyloid deposits probably reflect a CC combination of degenerate keratin filaments, serum amyloid P component, CC and deposition of immunoglobulins. {ECO:0000269|PubMed:19690585}. CC Note=The disease is caused by variants affecting the gene represented CC in this entry. CC -!- MISCELLANEOUS: [Isoform 9]: Major isoform. Dominant negative IL31 CC receptor. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 12]: Major isoform. Functional IL31 receptor. CC {ECO:0000305}. CC -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 2 CC subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAS86444.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAS86445.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={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; AF486620; AAM27958.1; -; mRNA. DR EMBL; AY499339; AAS86444.1; ALT_INIT; mRNA. DR EMBL; AY499340; AAS86445.1; ALT_INIT; mRNA. DR EMBL; AY499341; AAS86446.1; -; mRNA. DR EMBL; AY499342; AAS86447.1; -; mRNA. DR EMBL; AF106913; AAL36452.1; -; mRNA. DR EMBL; AY358117; AAQ88484.1; -; mRNA. DR EMBL; AY358740; AAQ89100.1; -; mRNA. DR EMBL; AC008914; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC110490; AAI10491.1; -; mRNA. DR CCDS; CCDS3970.2; -. [Q8NI17-2] DR CCDS; CCDS56365.1; -. [Q8NI17-5] DR CCDS; CCDS56366.1; -. [Q8NI17-3] DR CCDS; CCDS56367.1; -. [Q8NI17-6] DR CCDS; CCDS75244.1; -. [Q8NI17-8] DR CCDS; CCDS75245.1; -. [Q8NI17-12] DR RefSeq; NP_001229565.1; NM_001242636.2. [Q8NI17-12] DR RefSeq; NP_001229566.1; NM_001242637.2. [Q8NI17-5] DR RefSeq; NP_001229567.1; NM_001242638.2. [Q8NI17-3] DR RefSeq; NP_001229568.1; NM_001242639.2. [Q8NI17-6] DR RefSeq; NP_001284499.1; NM_001297570.3. [Q8NI17-8] DR RefSeq; NP_001284501.1; NM_001297572.1. DR RefSeq; NP_620586.3; NM_139017.5. [Q8NI17-2] DR RefSeq; XP_011541444.1; XM_011543142.3. [Q8NI17-1] DR RefSeq; XP_011541445.1; XM_011543143.2. DR RefSeq; XP_011541446.1; XM_011543144.2. DR RefSeq; XP_047272656.1; XM_047416700.1. [Q8NI17-6] DR RefSeq; XP_054207547.1; XM_054351572.1. [Q8NI17-1] DR RefSeq; XP_054207548.1; XM_054351573.1. [Q8NI17-6] DR AlphaFoldDB; Q8NI17; -. DR SMR; Q8NI17; -. DR BioGRID; 126357; 29. DR IntAct; Q8NI17; 25. DR STRING; 9606.ENSP00000498630; -. DR ChEMBL; CHEMBL4630894; -. DR DrugCentral; Q8NI17; -. DR GuidetoPHARMACOLOGY; 1710; -. DR GlyCosmos; Q8NI17; 10 sites, No reported glycans. DR GlyGen; Q8NI17; 10 sites. DR iPTMnet; Q8NI17; -. DR PhosphoSitePlus; Q8NI17; -. DR BioMuta; IL31RA; -. DR DMDM; 74730327; -. DR jPOST; Q8NI17; -. DR MassIVE; Q8NI17; -. DR PaxDb; 9606-ENSP00000415900; -. DR PeptideAtlas; Q8NI17; -. DR ProteomicsDB; 73801; -. [Q8NI17-1] DR ProteomicsDB; 73802; -. [Q8NI17-10] DR ProteomicsDB; 73803; -. [Q8NI17-11] DR ProteomicsDB; 73804; -. [Q8NI17-12] DR ProteomicsDB; 73805; -. [Q8NI17-2] DR ProteomicsDB; 73806; -. [Q8NI17-3] DR ProteomicsDB; 73807; -. [Q8NI17-4] DR ProteomicsDB; 73808; -. [Q8NI17-5] DR ProteomicsDB; 73809; -. [Q8NI17-6] DR ProteomicsDB; 73810; -. [Q8NI17-7] DR ProteomicsDB; 73811; -. [Q8NI17-8] DR ProteomicsDB; 73812; -. [Q8NI17-9] DR ABCD; Q8NI17; 1 sequenced antibody. DR Antibodypedia; 23449; 346 antibodies from 27 providers. DR DNASU; 133396; -. DR Ensembl; ENST00000297015.7; ENSP00000297015.4; ENSG00000164509.17. [Q8NI17-12] DR Ensembl; ENST00000354961.8; ENSP00000347047.4; ENSG00000164509.17. [Q8NI17-3] DR Ensembl; ENST00000359040.10; ENSP00000351935.5; ENSG00000164509.17. [Q8NI17-5] DR Ensembl; ENST00000396836.6; ENSP00000380048.2; ENSG00000164509.17. [Q8NI17-8] DR Ensembl; ENST00000490985.5; ENSP00000427533.1; ENSG00000164509.17. [Q8NI17-6] DR Ensembl; ENST00000652347.2; ENSP00000498630.1; ENSG00000164509.17. [Q8NI17-2] DR GeneID; 133396; -. DR KEGG; hsa:133396; -. DR MANE-Select; ENST00000652347.2; ENSP00000498630.1; NM_139017.7; NP_620586.3. [Q8NI17-2] DR UCSC; uc003jqk.3; human. [Q8NI17-1] DR AGR; HGNC:18969; -. DR CTD; 133396; -. DR DisGeNET; 133396; -. DR GeneCards; IL31RA; -. DR HGNC; HGNC:18969; IL31RA. DR HPA; ENSG00000164509; Tissue enhanced (bone marrow, lymphoid tissue, testis). DR MalaCards; IL31RA; -. DR MIM; 609510; gene. DR MIM; 613955; phenotype. DR neXtProt; NX_Q8NI17; -. DR OpenTargets; ENSG00000164509; -. DR Orphanet; 353220; Familial primary localized cutaneous amyloidosis. DR PharmGKB; PA134952624; -. DR VEuPathDB; HostDB:ENSG00000164509; -. DR eggNOG; ENOG502QVZY; Eukaryota. DR GeneTree; ENSGT00940000155603; -. DR HOGENOM; CLU_017990_2_0_1; -. DR InParanoid; Q8NI17; -. DR OMA; NSTHWME; -. DR OrthoDB; 9828391at2759; -. DR PhylomeDB; Q8NI17; -. DR TreeFam; TF338122; -. DR PathwayCommons; Q8NI17; -. DR Reactome; R-HSA-6788467; IL-6-type cytokine receptor ligand interactions. DR SignaLink; Q8NI17; -. DR SIGNOR; Q8NI17; -. DR BioGRID-ORCS; 133396; 12 hits in 1148 CRISPR screens. DR ChiTaRS; IL31RA; human. DR GeneWiki; IL31RA; -. DR GenomeRNAi; 133396; -. DR Pharos; Q8NI17; Tbio. DR PRO; PR:Q8NI17; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; Q8NI17; protein. DR Bgee; ENSG00000164509; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 112 other cell types or tissues. DR ExpressionAtlas; Q8NI17; baseline and differential. DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell. DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central. DR GO; GO:0016020; C:membrane; NAS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell. DR GO; GO:0043235; C:receptor complex; IBA:GO_Central. DR GO; GO:0019955; F:cytokine binding; IBA:GO_Central. DR GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central. DR GO; GO:0019901; F:protein kinase binding; NAS:UniProtKB. DR GO; GO:0003713; F:transcription coactivator activity; NAS:UniProtKB. DR GO; GO:0002438; P:acute inflammatory response to antigenic stimulus; IEA:Ensembl. DR GO; GO:0007169; P:cell surface receptor protein tyrosine kinase signaling pathway; NAS:UniProtKB. DR GO; GO:0007259; P:cell surface receptor signaling pathway via JAK-STAT; IEP:UniProtKB. DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central. DR GO; GO:0006952; P:defense response; NAS:UniProtKB. DR GO; GO:0098542; P:defense response to other organism; IEA:Ensembl. DR GO; GO:0002067; P:glandular epithelial cell differentiation; IEA:Ensembl. DR GO; GO:0042592; P:homeostatic process; NAS:UniProtKB. DR GO; GO:0030225; P:macrophage differentiation; NAS:UniProtKB. DR GO; GO:0000165; P:MAPK cascade; NAS:UniProtKB. DR GO; GO:0030224; P:monocyte differentiation; IEP:UniProtKB. DR GO; GO:0043066; P:negative regulation of apoptotic process; NAS:UniProtKB. DR GO; GO:0043031; P:negative regulation of macrophage activation; NAS:UniProtKB. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:UniProtKB. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; NAS:UniProtKB. DR GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IEP:UniProtKB. DR CDD; cd00063; FN3; 2. DR FunFam; 2.60.40.10:FF:000465; Granulocyte colony-stimulating factor receptor; 1. DR FunFam; 2.60.40.10:FF:000732; Interleukin 31 receptor A; 1. DR FunFam; 2.60.40.10:FF:000908; Interleukin 31 receptor A; 1. DR FunFam; 2.60.40.10:FF:000913; Interleukin 31 receptor A; 1. DR FunFam; 2.60.40.10:FF:000414; Interleukin-6 receptor subunit beta; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 5. DR InterPro; IPR003961; FN3_dom. DR InterPro; IPR036116; FN3_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR052672; Type1_Cytokine_Rcpt_Type2. DR InterPro; IPR015321; TypeI_recpt_CBD. DR PANTHER; PTHR48423; INTERLEUKIN-27 RECEPTOR SUBUNIT ALPHA; 1. DR PANTHER; PTHR48423:SF1; INTERLEUKIN-27 RECEPTOR SUBUNIT ALPHA; 1. DR Pfam; PF00041; fn3; 1. DR Pfam; PF09240; IL6Ra-bind; 1. DR SMART; SM00060; FN3; 4. DR SUPFAM; SSF49265; Fibronectin type III; 3. DR PROSITE; PS50853; FN3; 3. PE 1: Evidence at protein level; KW Alternative splicing; Amyloidosis; Cell membrane; Cell projection; KW Direct protein sequencing; Disease variant; Glycoprotein; Immunity; KW Membrane; Proteomics identification; Receptor; Reference proteome; Repeat; KW Signal; Synapse; Transmembrane; Transmembrane helix. FT SIGNAL 1..19 FT /evidence="ECO:0000269|PubMed:15340161" FT CHAIN 20..732 FT /note="Interleukin-31 receptor subunit alpha" FT /id="PRO_0000274572" FT TOPO_DOM 20..519 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 520..540 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 541..732 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 24..122 FT /note="Fibronectin type-III 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 124..225 FT /note="Fibronectin type-III 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 223..315 FT /note="Fibronectin type-III 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 319..416 FT /note="Fibronectin type-III 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT DOMAIN 421..515 FT /note="Fibronectin type-III 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT CARBOHYD 37 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 67 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 93 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 166 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 187 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 277 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 283 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 395 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 455 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 504 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 1..110 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_022798" FT VAR_SEQ 1 FT /note="M -> MCIRQLKFFTTACVCECPQNILSPQPSCVNLGM (in isoform FT 2, isoform 4, isoform 5 and isoform 8)" FT /evidence="ECO:0000303|PubMed:12975309, FT ECO:0000303|PubMed:15184896" FT /id="VSP_022799" FT VAR_SEQ 1 FT /note="M -> MKLSPQPSCVNLGM (in isoform 3, isoform 7, FT isoform 9, isoform 10, isoform 11 and isoform 12)" FT /evidence="ECO:0000303|PubMed:15184896, ECO:0000303|Ref.3" FT /id="VSP_022800" FT VAR_SEQ 325..732 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15184896" FT /id="VSP_022801" FT VAR_SEQ 464..469 FT /note="GGKGFS -> A (in isoform 7)" FT /evidence="ECO:0000303|Ref.3" FT /id="VSP_022802" FT VAR_SEQ 469..550 FT /note="SKTVNSSILQYGLESLKRKTSYIVQVMASTSAGGTNGTSINFKTLSFSVFEI FT ILITSLIGGGLLILIILTVAYGLKKPNKLT -> CKHAHSEVEKNPKPQIDAMDRPVVG FT MAPPSHCDLQPGMNHLASLNLSENGAKSTHLLGFWGLNESEVTVPERRVLRKWKELL FT (in isoform 8)" FT /evidence="ECO:0000303|PubMed:12975309" FT /id="VSP_022803" FT VAR_SEQ 498..501 FT /note="TSAG -> YSGG (in isoform 7)" FT /evidence="ECO:0000303|Ref.3" FT /id="VSP_022804" FT VAR_SEQ 502..732 FT /note="Missing (in isoform 7)" FT /evidence="ECO:0000303|Ref.3" FT /id="VSP_022805" FT VAR_SEQ 548..732 FT /note="Missing (in isoform 9)" FT /evidence="ECO:0000305" FT /id="VSP_022806" FT VAR_SEQ 551..732 FT /note="Missing (in isoform 8)" FT /evidence="ECO:0000303|PubMed:12975309" FT /id="VSP_022807" FT VAR_SEQ 593..613 FT /note="LKPCSTPSDKLVIDKLVVNFG -> KGSELGTKLKFKPLISLDCAF (in FT isoform 11)" FT /evidence="ECO:0000305" FT /id="VSP_022808" FT VAR_SEQ 593..598 FT /note="LKPCST -> RARYQA (in isoform 10)" FT /evidence="ECO:0000305" FT /id="VSP_022809" FT VAR_SEQ 599..732 FT /note="Missing (in isoform 10)" FT /evidence="ECO:0000305" FT /id="VSP_022810" FT VAR_SEQ 614..732 FT /note="Missing (in isoform 11)" FT /evidence="ECO:0000305" FT /id="VSP_022811" FT VAR_SEQ 639..649 FT /note="YVTCPFRPDCP -> TRILSSCPTSI (in isoform 3 and isoform FT 5)" FT /evidence="ECO:0000303|PubMed:15184896" FT /id="VSP_022812" FT VAR_SEQ 650..732 FT /note="Missing (in isoform 3 and isoform 5)" FT /evidence="ECO:0000303|PubMed:15184896" FT /id="VSP_022813" FT VARIANT 155 FT /note="D -> N (in dbSNP:rs13184107)" FT /id="VAR_030328" FT VARIANT 489 FT /note="S -> F (in PLCA2)" FT /evidence="ECO:0000269|PubMed:19690585" FT /id="VAR_065809" FT VARIANT 497 FT /note="S -> N (in dbSNP:rs161704)" FT /id="VAR_030329" FT MUTAGEN 639 FT /note="Y->A: No effect on STAT1 and STAT3 activation. FT Slight decrease; when associated with A-670 and A-708." FT /evidence="ECO:0000269|PubMed:15194700, FT ECO:0000269|PubMed:15627637" FT MUTAGEN 639 FT /note="Y->F: Abrogates STAT5 activation. Mild effect on FT STAT1 activation. No effect on STAT3 activation." FT /evidence="ECO:0000269|PubMed:15194700, FT ECO:0000269|PubMed:15627637" FT MUTAGEN 670 FT /note="Y->A: No effect on STAT1 and STAT3 activation. FT Slight decrease; when associated with A-639 and A-708." FT /evidence="ECO:0000269|PubMed:15194700, FT ECO:0000269|PubMed:15627637" FT MUTAGEN 670 FT /note="Y->F: No effect on STAT3 and STAT5 activation. Mild FT effect on STAT1 activation." FT /evidence="ECO:0000269|PubMed:15194700, FT ECO:0000269|PubMed:15627637" FT MUTAGEN 708 FT /note="Y->A: No effect on STAT1 and STAT3 activation. FT Slight decrease; when associated with A-639 and A-670." FT /evidence="ECO:0000269|PubMed:15194700, FT ECO:0000269|PubMed:15627637" FT MUTAGEN 708 FT /note="Y->F: Abrogates STAT3 activation. Loss of FT interaction with STAT3. Mild effect on STAT1 activation. No FT effect on STAT5 activation." FT /evidence="ECO:0000269|PubMed:15194700, FT ECO:0000269|PubMed:15627637" SQ SEQUENCE 732 AA; 82954 MW; 30F84BD3DD99A20E CRC64; MMWTWALWML PSLCKFSLAA LPAKPENISC VYYYRKNLTC TWSPGKETSY TQYTVKRTYA FGEKHDNCTT NSSTSENRAS CSFFLPRITI PDNYTIEVEA ENGDGVIKSH MTYWRLENIA KTEPPKIFRV KPVLGIKRMI QIEWIKPELA PVSSDLKYTL RFRTVNSTSW MEVNFAKNRK DKNQTYNLTG LQPFTEYVIA LRCAVKESKF WSDWSQEKMG MTEEEAPCGL ELWRVLKPAE ADGRRPVRLL WKKARGAPVL EKTLGYNIWY YPESNTNLTE TMNTTNQQLE LHLGGESFWV SMISYNSLGK SPVATLRIPA IQEKSFQCIE VMQACVAEDQ LVVKWQSSAL DVNTWMIEWF PDVDSEPTTL SWESVSQATN WTIQQDKLKP FWCYNISVYP MLHDKVGEPY SIQAYAKEGV PSEGPETKVE NIGVKTVTIT WKEIPKSERK GIICNYTIFY QAEGGKGFSK TVNSSILQYG LESLKRKTSY IVQVMASTSA GGTNGTSINF KTLSFSVFEI ILITSLIGGG LLILIILTVA YGLKKPNKLT HLCWPTVPNP AESSIATWHG DDFKDKLNLK ESDDSVNTED RILKPCSTPS DKLVIDKLVV NFGNVLQEIF TDEARTGQEN NLGGEKNGYV TCPFRPDCPL GKSFEELPVS PEIPPRKSQY LRSRMPEGTR PEAKEQLLFS GQSLVPDHLC EEGAPNPYLK NSVTAREFLV SEKLPEHTKG EV //