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Interleukin-31 receptor subunit alpha (IL-31 receptor subunit alpha) (IL-31R subunit alpha) (IL-31R-alpha) (IL-31RA) (Cytokine receptor-like 3) (GLM-R) (hGLM-R) (Gp130-like monocyte receptor) (Gp130-like receptor) (ZcytoR17)

 IL31R_HUMAN             Reviewed;         732 AA.
Q8NI17; A6NIF8; Q2TBA1; Q6EBC3; Q6EBC4; Q6EBC5; Q6EBC6; Q6UWL8;
Q8WYJ0;
06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 1.
30-AUG-2017, entry version 132.
RecName: Full=Interleukin-31 receptor subunit alpha;
Short=IL-31 receptor subunit alpha;
Short=IL-31R subunit alpha;
Short=IL-31R-alpha;
Short=IL-31RA;
AltName: Full=Cytokine receptor-like 3;
AltName: Full=GLM-R;
Short=hGLM-R;
AltName: Full=Gp130-like monocyte receptor;
Short=Gp130-like receptor;
AltName: Full=ZcytoR17;
Flags: Precursor;
Name=IL31RA; Synonyms=CRL3, GPL; ORFNames=UNQ6368/PRO21073/PRO21384;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
SUBCELLULAR LOCATION, AND INDUCTION.
PubMed=11877449; DOI=10.1074/jbc.M201140200;
Ghilardi N., Li J., Hongo J.-A., Yi S., Gurney A., De Sauvage F.J.;
"A novel type I cytokine receptor is expressed on monocytes, signals
proliferation, and activates STAT-3 and STAT-5.";
J. Biol. Chem. 277:16831-16836(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4 AND 5), FUNCTION,
OLIGOMERIZATION, TISSUE SPECIFICITY, AND INDUCTION.
PubMed=15184896; DOI=10.1038/ni1084;
Dillon S.R., Sprecher C., Hammond A., Bilsborough J.,
Rosenfeld-Franklin M., Presnell S.R., Haugen H.S., Maurer M.,
Harder B., Johnston J., Bort S., Mudri S., Kuijper J.L., Bukowski T.,
Shea P., Dong D.L., Dasovich M., Grant F.J., Lockwood L., Levin S.D.,
LeCiel C., Waggie K., Day H., Topouzis S., Kramer J., Kuestner R.,
Chen Z., Foster D., Parrish-Novak J., Gross J.A.;
"Interleukin 31, a cytokine produced by activated T cells, induces
dermatitis in mice.";
Nat. Immunol. 5:752-760(2004).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7).
Zhang W., Wan T., He L., Yuan Z., Cao X.;
"A novel soluble type 1 cytokine receptor.";
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 8).
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 20-34.
PubMed=15340161; DOI=10.1110/ps.04682504;
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally
verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[8]
ALTERNATIVE SPLICING (ISOFORMS 9; 10; 11 AND 12), FUNCTION, TISSUE
SPECIFICITY, INDUCTION, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
PubMed=14504285; DOI=10.1074/jbc.M307286200;
Diveu C., Lelievre E., Perret D., Lagrue Lak-Hal A.-H., Froger J.,
Guillet C., Chevalier S., Rousseau F., Wesa A., Preisser L.,
Chabbert M., Gauchat J.-F., Galy A., Gascan H., Morel A.;
"GPL, a novel cytokine receptor related to GP130 and leukemia
inhibitory factor receptor.";
J. Biol. Chem. 278:49850-49859(2003).
[9]
FUNCTION, AND MUTAGENESIS OF TYR-639; TYR-670 AND TYR-708.
PubMed=15627637;
Diveu C., Lagrue Lak-Hal A.-H., Froger J., Ravon E., Grimaud L.,
Barbier F., Hermann J., Gascan H., Chevalier S.;
"Predominant expression of the long isoform of GP130-like (GPL)
receptor is required for interleukin-31 signaling.";
Eur. Cytokine Netw. 15:291-302(2004).
[10]
FUNCTION, INTERACTION WITH JAK1 AND STAT3, AND MUTAGENESIS OF TYR-639;
TYR-670 AND TYR-708.
PubMed=15194700; DOI=10.1074/jbc.M401122200;
Dreuw A., Radtke S., Pflanz S., Lippok B.E., Heinrich P.C.,
Hermanns H.M.;
"Characterization of the signaling capacities of the novel gp130-like
cytokine receptor.";
J. Biol. Chem. 279:36112-36120(2004).
[11]
INDUCTION, AND TISSUE SPECIFICITY.
PubMed=16461143; DOI=10.1016/j.jaci.2005.10.046;
Bilsborough J., Leung D.Y.M., Maurer M., Howell M., Boguniewicz M.,
Yao L., Storey H., LeCiel C., Harder B., Gross J.A.;
"IL-31 is associated with cutaneous lymphocyte antigen-positive skin
homing T cells in patients with atopic dermatitis.";
J. Allergy Clin. Immunol. 117:418-425(2006).
[12]
TISSUE SPECIFICITY, AND INDUCTION.
PubMed=18439099; DOI=10.1089/jir.2007.0057;
Jawa R.S., Chattopadhyay S., Tracy E., Wang Y., Huntoon K.,
Dayton M.T., Baumann H.;
"Regulated expression of the IL-31 receptor in bronchial and alveolar
epithelial cells, pulmonary fibroblasts, and pulmonary macrophages.";
J. Interferon Cytokine Res. 28:207-219(2008).
[13]
TISSUE SPECIFICITY, AND INDUCTION.
PubMed=21261663; DOI=10.1111/j.1398-9995.2011.02545.x;
Kasraie S., Niebuhr M., Baumert K., Werfel T.;
"Functional effects of interleukin 31 in human primary
keratinocytes.";
Allergy 66:845-852(2011).
[14]
TISSUE SPECIFICITY.
PubMed=24373353; DOI=10.1016/j.jaci.2013.10.048;
Cevikbas F., Wang X., Akiyama T., Kempkes C., Savinko T., Antal A.,
Kukova G., Buhl T., Ikoma A., Buddenkotte J., Soumelis V., Feld M.,
Alenius H., Dillon S.R., Carstens E., Homey B., Basbaum A.,
Steinhoff M.;
"A sensory neuron-expressed IL-31 receptor mediates T helper cell-
dependent itch: Involvement of TRPV1 and TRPA1.";
J. Allergy Clin. Immunol. 133:448-460(2014).
[15]
VARIANT PLCA2 PHE-489.
PubMed=19690585; DOI=10.1038/ejhg.2009.135;
Lin M.W., Lee D.D., Liu T.T., Lin Y.F., Chen S.Y., Huang C.C.,
Weng H.Y., Liu Y.F., Tanaka A., Arita K., Lai-Cheong J., Palisson F.,
Chang Y.T., Wong C.K., Matsuura I., McGrath J.A., Tsai S.F.;
"Novel IL31RA gene mutation and ancestral OSMR mutant allele in
familial primary cutaneous amyloidosis.";
Eur. J. Hum. Genet. 18:26-32(2010).
-!- FUNCTION: Associates with OSMR to form the interleukin-31 receptor
which activates STAT3 and to a lower extent STAT1 and STAT5
(PubMed:11877449, PubMed:14504285, PubMed:15627637,
PubMed:15194700). May function in skin immunity (PubMed:15184896).
Mediates IL31-induced itch, probably in a manner dependent on
cation channels TRPA1 and TRPV1 (By similarity). Positively
regulates numbers and cycling status of immature subsets of
myeloid progenitor cells in bone marrow in vivo and enhances
myeloid progenitor cell survival in vitro (By similarity).
{ECO:0000250|UniProtKB:Q8K5B1, ECO:0000269|PubMed:11877449,
ECO:0000269|PubMed:14504285, ECO:0000269|PubMed:15184896,
ECO:0000269|PubMed:15194700, ECO:0000269|PubMed:15627637}.
-!- SUBUNIT: Heterodimer with OSMR. Interacts with JAK1 and STAT3.
{ECO:0000269|PubMed:15194700}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:11877449,
ECO:0000305|PubMed:14504285}; Single-pass type I membrane protein
{ECO:0000305|PubMed:11877449, ECO:0000305|PubMed:14504285}. Cell
junction, synapse, presynaptic cell membrane
{ECO:0000250|UniProtKB:Q8K5B1}. Cell projection, axon
{ECO:0000250|UniProtKB:Q8K5B1}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=12;
Name=1;
IsoId=Q8NI17-1; Sequence=Displayed;
Name=2; Synonyms=v3;
IsoId=Q8NI17-2; Sequence=VSP_022799;
Name=3; Synonyms=v4;
IsoId=Q8NI17-3; Sequence=VSP_022800, VSP_022812, VSP_022813;
Name=4; Synonyms=v2;
IsoId=Q8NI17-4; Sequence=VSP_022799, VSP_022801;
Name=5; Synonyms=v1;
IsoId=Q8NI17-5; Sequence=VSP_022799, VSP_022812, VSP_022813;
Name=6;
IsoId=Q8NI17-6; Sequence=VSP_022798;
Note=No experimental confirmation available.;
Name=7;
IsoId=Q8NI17-7; Sequence=VSP_022800, VSP_022802, VSP_022804,
VSP_022805;
Note=No experimental confirmation available.;
Name=8;
IsoId=Q8NI17-8; Sequence=VSP_022799, VSP_022803, VSP_022807;
Note=No experimental confirmation available.;
Name=9; Synonyms=GPL560, short;
IsoId=Q8NI17-9; Sequence=VSP_022800, VSP_022806;
Note=Major isoform. Dominant negative IL31 receptor.;
Name=10; Synonyms=GPL610;
IsoId=Q8NI17-10; Sequence=VSP_022800, VSP_022809, VSP_022810;
Name=11; Synonyms=GPL626;
IsoId=Q8NI17-11; Sequence=VSP_022800, VSP_022808, VSP_022811;
Name=12; Synonyms=GPL745, long;
IsoId=Q8NI17-12; Sequence=VSP_022800;
Note=Major isoform. Functional IL31 receptor.;
-!- TISSUE SPECIFICITY: Expressed in CD14- and CD56-positive blood
cells (PubMed:11877449). Expressed in macrophages
(PubMed:16461143, PubMed:18439099). Expressed in keratinocytes
(PubMed:21261663). Expressed in a subset of dorsal root ganglia
neurons (at protein level) (PubMed:24373353). Expressed at low
levels in testis, ovary, brain, prostate, placenta, thymus, bone
marrow, trachea and skin (PubMed:15184896, PubMed:11877449,
PubMed:14504285). Expressed in bronchial and alveolar epithelial
cells and pulmonary fibroblasts (PubMed:18439099). Detected in all
of the myelomonocytic lineage (PubMed:14504285). Isoform 6:
Expressed at higher levels in lesional skin compared to healthy
skin of atopic dermatitis patients (PubMed:24373353).
{ECO:0000269|PubMed:11877449, ECO:0000269|PubMed:14504285,
ECO:0000269|PubMed:15184896, ECO:0000269|PubMed:16461143,
ECO:0000269|PubMed:18439099, ECO:0000269|PubMed:21261663,
ECO:0000269|PubMed:24373353}.
-!- INDUCTION: Up-regulated in lesional keratinocytes of patients with
atopic dermatitis (PubMed:16461143). Up-regulated by IFNG/IFN-
gamma (PubMed:11877449, PubMed:14504285, PubMed:15184896,
PubMed:21261663, PubMed:18439099). Up-regulated by bacterial
lipopolysaccharides (LPS) (PubMed:11877449, PubMed:15184896,
PubMed:14504285). Up-regulated by triacylated lipoprotein
(Pam3Cys) (PubMed:21261663). Up-regulated by TGFB1/TGF-beta
(PubMed:18439099). {ECO:0000269|PubMed:11877449,
ECO:0000269|PubMed:14504285, ECO:0000269|PubMed:15184896,
ECO:0000269|PubMed:16461143, ECO:0000269|PubMed:18439099,
ECO:0000269|PubMed:21261663}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:14504285}.
-!- DISEASE: Amyloidosis, primary localized cutaneous, 2 (PLCA2)
[MIM:613955]: A primary amyloidosis characterized by localized
cutaneous amyloid deposition. This condition usually presents with
itching (especially on the lower legs) and visible changes of skin
hyperpigmentation and thickening that may be exacerbated by
chronic scratching and rubbing. Primary localized cutaneous
amyloidosis is often divided into macular and lichen subtypes
although many affected individuals often show both variants
coexisting. Lichen amyloidosis characteristically presents as a
pruritic eruption of grouped hyperkeratotic papules with a
predilection for the shins, calves, ankles and dorsa of feet and
thighs. Papules may coalesce to form hyperkeratotic plaques that
can resemble lichen planus, lichen simplex or nodular prurigo.
Macular amyloidosis is characterized by small pigmented macules
that may merge to produce macular hyperpigmentation, sometimes
with a reticulate or rippled pattern. In macular and lichen
amyloidosis, amyloid is deposited in the papillary dermis in
association with grouped colloid bodies, thought to represent
degenerate basal keratinocytes. The amyloid deposits probably
reflect a combination of degenerate keratin filaments, serum
amyloid P component, and deposition of immunoglobulins.
{ECO:0000269|PubMed:19690585}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 2
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAS86444.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAS86445.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AF486620; AAM27958.1; -; mRNA.
EMBL; AY499339; AAS86444.1; ALT_INIT; mRNA.
EMBL; AY499340; AAS86445.1; ALT_INIT; mRNA.
EMBL; AY499341; AAS86446.1; -; mRNA.
EMBL; AY499342; AAS86447.1; -; mRNA.
EMBL; AF106913; AAL36452.1; -; mRNA.
EMBL; AY358117; AAQ88484.1; -; mRNA.
EMBL; AY358740; AAQ89100.1; -; mRNA.
EMBL; AC008914; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC110490; AAI10491.1; -; mRNA.
CCDS; CCDS3970.2; -. [Q8NI17-2]
CCDS; CCDS56365.1; -. [Q8NI17-5]
CCDS; CCDS56366.1; -. [Q8NI17-3]
CCDS; CCDS56367.1; -. [Q8NI17-6]
CCDS; CCDS75244.1; -. [Q8NI17-8]
CCDS; CCDS75245.1; -. [Q8NI17-12]
RefSeq; NP_001229565.1; NM_001242636.1. [Q8NI17-12]
RefSeq; NP_001229566.1; NM_001242637.1. [Q8NI17-5]
RefSeq; NP_001229567.1; NM_001242638.1. [Q8NI17-3]
RefSeq; NP_001229568.1; NM_001242639.1. [Q8NI17-6]
RefSeq; NP_001284499.1; NM_001297570.1. [Q8NI17-8]
RefSeq; NP_001284501.1; NM_001297572.1.
RefSeq; NP_620586.3; NM_139017.5. [Q8NI17-2]
RefSeq; XP_011541444.1; XM_011543142.2. [Q8NI17-1]
RefSeq; XP_011541445.1; XM_011543143.2. [Q8NI17-3]
RefSeq; XP_011541446.1; XM_011543144.2. [Q8NI17-6]
UniGene; Hs.55378; -.
ProteinModelPortal; Q8NI17; -.
SMR; Q8NI17; -.
BioGrid; 126357; 26.
IntAct; Q8NI17; 1.
STRING; 9606.ENSP00000415900; -.
GuidetoPHARMACOLOGY; 1710; -.
iPTMnet; Q8NI17; -.
PhosphoSitePlus; Q8NI17; -.
BioMuta; IL31RA; -.
DMDM; 74730327; -.
MaxQB; Q8NI17; -.
PaxDb; Q8NI17; -.
PeptideAtlas; Q8NI17; -.
PRIDE; Q8NI17; -.
Ensembl; ENST00000297015; ENSP00000297015; ENSG00000164509. [Q8NI17-12]
Ensembl; ENST00000354961; ENSP00000347047; ENSG00000164509. [Q8NI17-3]
Ensembl; ENST00000359040; ENSP00000351935; ENSG00000164509. [Q8NI17-5]
Ensembl; ENST00000396834; ENSP00000380046; ENSG00000164509. [Q8NI17-3]
Ensembl; ENST00000396836; ENSP00000380048; ENSG00000164509. [Q8NI17-8]
Ensembl; ENST00000447346; ENSP00000415900; ENSG00000164509. [Q8NI17-2]
Ensembl; ENST00000490985; ENSP00000427533; ENSG00000164509. [Q8NI17-6]
GeneID; 133396; -.
KEGG; hsa:133396; -.
UCSC; uc003jqk.3; human. [Q8NI17-1]
CTD; 133396; -.
DisGeNET; 133396; -.
GeneCards; IL31RA; -.
HGNC; HGNC:18969; IL31RA.
HPA; HPA051532; -.
MalaCards; IL31RA; -.
MIM; 609510; gene.
MIM; 613955; phenotype.
neXtProt; NX_Q8NI17; -.
OpenTargets; ENSG00000164509; -.
Orphanet; 353220; Familial primary localized cutaneous amyloidosis.
PharmGKB; PA134952624; -.
eggNOG; ENOG410IJG6; Eukaryota.
eggNOG; ENOG410YAI2; LUCA.
GeneTree; ENSGT00550000074436; -.
HOVERGEN; HBG081788; -.
InParanoid; Q8NI17; -.
OMA; IWYFPEN; -.
OrthoDB; EOG091G01XM; -.
PhylomeDB; Q8NI17; -.
TreeFam; TF338122; -.
Reactome; R-HSA-449836; Other interleukin signaling.
SignaLink; Q8NI17; -.
SIGNOR; Q8NI17; -.
ChiTaRS; IL31RA; human.
GeneWiki; IL31RA; -.
GenomeRNAi; 133396; -.
PRO; PR:Q8NI17; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000164509; -.
ExpressionAtlas; Q8NI17; baseline and differential.
Genevisible; Q8NI17; HS.
GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:0019955; F:cytokine binding; NAS:UniProtKB.
GO; GO:0004896; F:cytokine receptor activity; TAS:UniProtKB.
GO; GO:0019901; F:protein kinase binding; NAS:UniProtKB.
GO; GO:0003713; F:transcription coactivator activity; NAS:UniProtKB.
GO; GO:0002438; P:acute inflammatory response to antigenic stimulus; IEA:Ensembl.
GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:UniProtKB.
GO; GO:0006952; P:defense response; NAS:UniProtKB.
GO; GO:0098542; P:defense response to other organism; IEA:Ensembl.
GO; GO:0002067; P:glandular epithelial cell differentiation; IEA:Ensembl.
GO; GO:0042592; P:homeostatic process; NAS:UniProtKB.
GO; GO:0007259; P:JAK-STAT cascade; IEP:UniProtKB.
GO; GO:0030225; P:macrophage differentiation; NAS:UniProtKB.
GO; GO:0000165; P:MAPK cascade; NAS:UniProtKB.
GO; GO:0030224; P:monocyte differentiation; IEP:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; NAS:UniProtKB.
GO; GO:0043031; P:negative regulation of macrophage activation; NAS:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; NAS:UniProtKB.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IEP:UniProtKB.
GO; GO:0035745; P:T-helper 2 cell cytokine production; IEA:Ensembl.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; NAS:UniProtKB.
CDD; cd00063; FN3; 2.
Gene3D; 2.60.40.10; -; 5.
InterPro; IPR003961; FN3_dom.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR015321; TypeI_recpt_CBD.
Pfam; PF00041; fn3; 2.
Pfam; PF09240; IL6Ra-bind; 1.
SMART; SM00060; FN3; 4.
SUPFAM; SSF49265; SSF49265; 3.
PROSITE; PS50853; FN3; 3.
1: Evidence at protein level;
Alternative splicing; Amyloidosis; Cell junction; Cell membrane;
Cell projection; Complete proteome; Direct protein sequencing;
Disease mutation; Glycoprotein; Immunity; Membrane; Polymorphism;
Receptor; Reference proteome; Repeat; Signal; Synapse; Transmembrane;
Transmembrane helix.
SIGNAL 1 19 {ECO:0000269|PubMed:15340161}.
CHAIN 20 732 Interleukin-31 receptor subunit alpha.
/FTId=PRO_0000274572.
TOPO_DOM 20 519 Extracellular. {ECO:0000255}.
TRANSMEM 520 540 Helical. {ECO:0000255}.
TOPO_DOM 541 732 Cytoplasmic. {ECO:0000255}.
DOMAIN 24 122 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 124 225 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 223 315 Fibronectin type-III 3.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 319 416 Fibronectin type-III 4.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 421 515 Fibronectin type-III 5.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
CARBOHYD 37 37 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 67 67 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 93 93 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 166 166 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 187 187 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 277 277 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 283 283 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 395 395 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 455 455 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 504 504 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 1 110 Missing (in isoform 6).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_022798.
VAR_SEQ 1 1 M -> MCIRQLKFFTTACVCECPQNILSPQPSCVNLGM
(in isoform 2, isoform 4, isoform 5 and
isoform 8). {ECO:0000303|PubMed:12975309,
ECO:0000303|PubMed:15184896}.
/FTId=VSP_022799.
VAR_SEQ 1 1 M -> MKLSPQPSCVNLGM (in isoform 3,
isoform 7, isoform 9, isoform 10, isoform
11 and isoform 12).
{ECO:0000303|PubMed:15184896,
ECO:0000303|Ref.3}.
/FTId=VSP_022800.
VAR_SEQ 325 732 Missing (in isoform 4).
{ECO:0000303|PubMed:15184896}.
/FTId=VSP_022801.
VAR_SEQ 464 469 GGKGFS -> A (in isoform 7).
{ECO:0000303|Ref.3}.
/FTId=VSP_022802.
VAR_SEQ 469 550 SKTVNSSILQYGLESLKRKTSYIVQVMASTSAGGTNGTSIN
FKTLSFSVFEIILITSLIGGGLLILIILTVAYGLKKPNKLT
-> CKHAHSEVEKNPKPQIDAMDRPVVGMAPPSHCDLQPGM
NHLASLNLSENGAKSTHLLGFWGLNESEVTVPERRVLRKWK
ELL (in isoform 8).
{ECO:0000303|PubMed:12975309}.
/FTId=VSP_022803.
VAR_SEQ 498 501 TSAG -> YSGG (in isoform 7).
{ECO:0000303|Ref.3}.
/FTId=VSP_022804.
VAR_SEQ 502 732 Missing (in isoform 7).
{ECO:0000303|Ref.3}.
/FTId=VSP_022805.
VAR_SEQ 548 732 Missing (in isoform 9). {ECO:0000305}.
/FTId=VSP_022806.
VAR_SEQ 551 732 Missing (in isoform 8).
{ECO:0000303|PubMed:12975309}.
/FTId=VSP_022807.
VAR_SEQ 593 613 LKPCSTPSDKLVIDKLVVNFG -> KGSELGTKLKFKPLIS
LDCAF (in isoform 11). {ECO:0000305}.
/FTId=VSP_022808.
VAR_SEQ 593 598 LKPCST -> RARYQA (in isoform 10).
{ECO:0000305}.
/FTId=VSP_022809.
VAR_SEQ 599 732 Missing (in isoform 10). {ECO:0000305}.
/FTId=VSP_022810.
VAR_SEQ 614 732 Missing (in isoform 11). {ECO:0000305}.
/FTId=VSP_022811.
VAR_SEQ 639 649 YVTCPFRPDCP -> TRILSSCPTSI (in isoform 3
and isoform 5).
{ECO:0000303|PubMed:15184896}.
/FTId=VSP_022812.
VAR_SEQ 650 732 Missing (in isoform 3 and isoform 5).
{ECO:0000303|PubMed:15184896}.
/FTId=VSP_022813.
VARIANT 155 155 D -> N (in dbSNP:rs13184107).
/FTId=VAR_030328.
VARIANT 489 489 S -> F (in PLCA2).
{ECO:0000269|PubMed:19690585}.
/FTId=VAR_065809.
VARIANT 497 497 S -> N (in dbSNP:rs161704).
/FTId=VAR_030329.
MUTAGEN 639 639 Y->A: No effect on STAT1 and STAT3
activation. Slight decrease; when
associated with A-670 and A-708.
{ECO:0000269|PubMed:15194700,
ECO:0000269|PubMed:15627637}.
MUTAGEN 639 639 Y->F: Abrogates STAT5 activation. Mild
effect on STAT1 activation. No effect on
STAT3 activation.
{ECO:0000269|PubMed:15194700,
ECO:0000269|PubMed:15627637}.
MUTAGEN 670 670 Y->A: No effect on STAT1 and STAT3
activation. Slight decrease; when
associated with A-639 and A-708.
{ECO:0000269|PubMed:15194700,
ECO:0000269|PubMed:15627637}.
MUTAGEN 670 670 Y->F: No effect on STAT3 and STAT5
activation. Mild effect on STAT1
activation. {ECO:0000269|PubMed:15194700,
ECO:0000269|PubMed:15627637}.
MUTAGEN 708 708 Y->A: No effect on STAT1 and STAT3
activation. Slight decrease; when
associated with A-639 and A-670.
{ECO:0000269|PubMed:15194700,
ECO:0000269|PubMed:15627637}.
MUTAGEN 708 708 Y->F: Abrogates STAT3 activation. Loss of
interaction with STAT3. Mild effect on
STAT1 activation. No effect on STAT5
activation. {ECO:0000269|PubMed:15194700,
ECO:0000269|PubMed:15627637}.
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


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