IL31R_HUMAN
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 03-AUG-2022, entry version 161.
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:15627637, PubMed:15194700).
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:15184896, PubMed:11877449, PubMed:14504285). 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:21261663,
CC PubMed:18439099). Up-regulated by bacterial lipopolysaccharides (LPS)
CC (PubMed:11877449, PubMed:15184896, PubMed:14504285). 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};
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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_001242636.1. [Q8NI17-12]
DR RefSeq; NP_001229566.1; NM_001242637.1. [Q8NI17-5]
DR RefSeq; NP_001229567.1; NM_001242638.1. [Q8NI17-3]
DR RefSeq; NP_001229568.1; NM_001242639.1. [Q8NI17-6]
DR RefSeq; NP_001284499.1; NM_001297570.1. [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_011543142.2. [Q8NI17-1]
DR RefSeq; XP_011541445.1; XM_011543143.2. [Q8NI17-3]
DR RefSeq; XP_011541446.1; XM_011543144.2. [Q8NI17-6]
DR AlphaFoldDB; Q8NI17; -.
DR SMR; Q8NI17; -.
DR BioGRID; 126357; 28.
DR IntAct; Q8NI17; 25.
DR STRING; 9606.ENSP00000415900; -.
DR ChEMBL; CHEMBL4630894; -.
DR GuidetoPHARMACOLOGY; 1710; -.
DR GlyGen; Q8NI17; 10 sites.
DR iPTMnet; Q8NI17; -.
DR PhosphoSitePlus; Q8NI17; -.
DR BioMuta; IL31RA; -.
DR DMDM; 74730327; -.
DR MassIVE; Q8NI17; -.
DR MaxQB; Q8NI17; -.
DR PaxDb; Q8NI17; -.
DR PeptideAtlas; Q8NI17; -.
DR PRIDE; 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; 278 antibodies from 26 providers.
DR DNASU; 133396; -.
DR Ensembl; ENST00000297015.7; ENSP00000297015.4; ENSG00000164509.16. [Q8NI17-12]
DR Ensembl; ENST00000354961.8; ENSP00000347047.4; ENSG00000164509.16. [Q8NI17-3]
DR Ensembl; ENST00000359040.10; ENSP00000351935.5; ENSG00000164509.16. [Q8NI17-5]
DR Ensembl; ENST00000396836.6; ENSP00000380048.2; ENSG00000164509.16. [Q8NI17-8]
DR Ensembl; ENST00000490985.5; ENSP00000427533.1; ENSG00000164509.16. [Q8NI17-6]
DR Ensembl; ENST00000652347.2; ENSP00000498630.1; ENSG00000164509.16. [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 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; ILQYDLE; -.
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 1070 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 monocyte and 111 other tissues.
DR ExpressionAtlas; Q8NI17; baseline and differential.
DR Genevisible; Q8NI17; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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:0016021; C:integral component of 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:0051916; F:granulocyte colony-stimulating factor binding; 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: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 transcription, DNA-templated; NAS:UniProtKB.
DR GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IEP:UniProtKB.
DR GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; IEP:UniProtKB.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; NAS:UniProtKB.
DR CDD; cd00063; FN3; 2.
DR Gene3D; 2.60.40.10; -; 5.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR015321; TypeI_recpt_CBD.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF09240; IL6Ra-bind; 1.
DR SMART; SM00060; FN3; 4.
DR SUPFAM; SSF49265; SSF49265; 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; Receptor; Reference proteome; Repeat; Signal; Synapse;
KW 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
