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Interleukin-4 receptor subunit alpha (IL-4 receptor subunit alpha) (IL-4R subunit alpha) (IL-4R-alpha) (IL-4RA) (CD antigen CD124) [Cleaved into: Soluble interleukin-4 receptor subunit alpha (Soluble IL-4 receptor subunit alpha) (Soluble IL-4R-alpha) (sIL4Ralpha/prot) (IL-4-binding protein) (IL4-BP)]

 IL4RA_HUMAN             Reviewed;         825 AA.
P24394; B4E076; B9EKU8; H3BSY5; Q96P01; Q9H181; Q9H182; Q9H183;
Q9H184; Q9H185; Q9H186; Q9H187; Q9H188;
01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
01-MAR-1992, sequence version 1.
25-OCT-2017, entry version 202.
RecName: Full=Interleukin-4 receptor subunit alpha;
Short=IL-4 receptor subunit alpha;
Short=IL-4R subunit alpha;
Short=IL-4R-alpha;
Short=IL-4RA;
AltName: CD_antigen=CD124;
Contains:
RecName: Full=Soluble interleukin-4 receptor subunit alpha;
Short=Soluble IL-4 receptor subunit alpha;
Short=Soluble IL-4R-alpha;
Short=sIL4Ralpha/prot;
AltName: Full=IL-4-binding protein;
Short=IL4-BP;
Flags: Precursor;
Name=IL4R; Synonyms=IL4RA; ORFNames=582J2.1;
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).
TISSUE=Peripheral blood;
PubMed=2307934; DOI=10.1084/jem.171.3.861;
Idzerda R.L., March C.J., Mosley B., Lyman S.D., Bos T.V.,
Gimpel S.D., Din W.S., Grabstein K.H., Widmer M.B., Park L.S.,
Cosman D., Beckmann M.P.;
"Human interleukin 4 receptor confers biological responsiveness and
defines a novel receptor superfamily.";
J. Exp. Med. 171:861-873(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Myeloid leukemia cell;
PubMed=2278997; DOI=10.1093/intimm/2.7.669;
Galizzi J.-P., Zuber C.E., Harada N., Gorman D.M., Djossou O.,
Kastelein R., Banchereau J., Howard M., Miyajima A.;
"Molecular cloning of a cDNA encoding the human interleukin 4
receptor.";
Int. Immunol. 2:669-675(1990).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
TISSUE=Blood;
PubMed=10590262; DOI=10.1093/intimm/11.12.1965;
Kruse S., Forster J., Kuehr J., Deichmann K.A.;
"Characterization of the membrane-bound and a soluble form of human
IL-4 receptor alpha produced by alternative splicing.";
Int. Immunol. 11:1965-1970(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 1).
PubMed=10493829; DOI=10.1006/geno.1999.5927;
Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R.,
Fuhrmann J., Mason T., Crosby M.L., Barnstead M., Cronin L.,
Mays A.D., Cao Y., Xu R.X., Kang H.-L., Mitchell S., Eichler E.E.,
Harris P.C., Venter J.C., Adams M.D.;
"Genome duplications and other features in 12 Mb of DNA sequence from
human chromosome 16p and 16q.";
Genomics 60:295-308(1999).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-75; ALA-400;
ARG-431; LEU-436; PRO-503; ARG-576; ILE-579; SER-675 AND ALA-752.
SeattleSNPs variation discovery resource;
Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Thymus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Testis;
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).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 301-825 (ISOFORM 1), AND VARIANTS
ALA-400; ARG-431; LEU-436; PRO-503; ARG-576 AND ILE-579.
PubMed=11285129; DOI=10.1034/j.1399-0039.2001.057003216.x;
Lozano F., Places L., Vila J.-M., Padilla O., Arman M., Gimferrer I.,
Suarez B., Lopez de la Iglesia A., Miserachs N., Vives J.;
"Identification of a novel single-nucleotide polymorphism (Val554Ile)
and definition of eight common alleles for human IL4RA exon 11.";
Tissue Antigens 57:216-220(2001).
[10]
FUNCTION IN IRS1 ACTIVATION, PHOSPHORYLATION AT TYR-497, AND
MUTAGENESIS OF TYR-497.
PubMed=8124718; DOI=10.1016/0092-8674(94)90356-5;
Keegan A.D., Nelms K., White M., Wang L.-M., Pierce J.H., Paul W.E.;
"An IL-4 receptor region containing an insulin receptor motif is
important for IL-4-mediated IRS-1 phosphorylation and cell growth.";
Cell 76:811-820(1994).
[11]
DOMAIN JAK3 ACTIVATION.
PubMed=7721895; DOI=10.1074/jbc.270.16.9630;
Malabarba M.G., Kirken R.A., Rui H., Koettnitz K., Kawamura M.,
O'Shea J.J., Kalthoff F.S., Farrar W.L.;
"Activation of JAK3, but not JAK1, is critical to interleukin-4 (IL4)
stimulated proliferation and requires a membrane-proximal region of
IL4 receptor alpha.";
J. Biol. Chem. 270:9630-9637(1995).
[12]
INTERACTION WITH IL13RA1.
PubMed=7775445; DOI=10.1074/jbc.270.23.13869;
Zurawski S.M., Chomarat P., Djossou O., Bidaud C., McKenzie A.N.,
Miossec P., Banchereau J., Zurawski G.;
"The primary binding subunit of the human interleukin-4 receptor is
also a component of the interleukin-13 receptor.";
J. Biol. Chem. 270:13869-13878(1995).
[13]
INTERACTION WITH JAK3.
PubMed=7538655;
Rolling C., Treton D., Beckmann P., Galanaud P., Richard Y.;
"JAK3 associates with the human interleukin 4 receptor and is tyrosine
phosphorylated following receptor triggering.";
Oncogene 10:1757-1761(1995).
[14]
INTERACTION WITH IL13RA1, AND PHOSPHORYLATION.
PubMed=8804422; DOI=10.1016/0014-5793(96)00835-6;
Rolling C., Treton D., Pellegrini S., Galanaud P., Richard Y.;
"IL4 and IL13 receptors share the gamma c chain and activate STAT6,
STAT3 and STAT5 proteins in normal human B cells.";
FEBS Lett. 393:53-56(1996).
[15]
DOMAIN STAT6 ACTIVATION, AND MUTAGENESIS OF TYR-575; TYR-603 AND
TYR-631.
PubMed=8624803; DOI=10.1016/S1074-7613(00)80677-9;
Ryan J.J., McReynolds L.J., Keegan A., Wang L.-H., Garfein E.,
Rothman P., Nelms K., Paul W.E.;
"Growth and gene expression are predominantly controlled by distinct
regions of the human IL-4 receptor.";
Immunity 4:123-132(1996).
[16]
PROTEOLYTIC PROCESSING.
PubMed=10341317; DOI=10.1159/000024171;
Jung T., Schrader N., Hellwig M., Enssle K.H., Neumann C.;
"Soluble human interleukin-4 receptor is produced by activated T cells
under the control of metalloproteinases.";
Int. Arch. Allergy Immunol. 119:23-30(1999).
[17]
INTERACTION WITH PTPN6; PTPN11 AND INPP5D, STAT6 ACTIVATION, AND
MUTAGENESIS OF TYR-713.
PubMed=11714803; DOI=10.4049/jimmunol.167.11.6382;
Kashiwada M., Giallourakis C.C., Pan P.-Y., Rothman P.B.;
"Immunoreceptor tyrosine-based inhibitory motif of the IL-4 receptor
associates with SH2-containing phosphatases and regulates IL-4-induced
proliferation.";
J. Immunol. 167:6382-6387(2001).
[18]
LIGAND-BINDING SITES, AND MUTAGENESIS OF TYR-38; MET-39; SER-40;
LEU-64; PHE-66; LEU-67; LEU-68; ASP-91; ASP-92; VAL-93; VAL-94;
SER-95; ASP-97; ASN-98; TYR-99; LYS-116; PRO-117; SER-118; GLU-119;
ASP-150; ASN-151; TYR-152; LEU-153; TYR-154 AND TYR-208.
PubMed=11786020; DOI=10.1006/jmbi.2001.5243;
Zhang J.-L., Simeonowa I., Wang Y., Sebald W.;
"The high-affinity interaction of human IL-4 and the receptor alpha
chain is constituted by two independent binding clusters.";
J. Mol. Biol. 315:399-407(2002).
[19]
STAT6 ACTIVATION, AND INHIBITION BY TYROSINE PHOSPHATASE SHP1.
PubMed=12459556; DOI=10.1074/jbc.M211747200;
Hanson E.M., Dickensheets H., Qu C.K., Donnelly R.P., Keegan A.D.;
"Regulation of the dephosphorylation of Stat6. Participation of Tyr-
713 in the interleukin-4 receptor alpha, the tyrosine phosphatase SHP-
1, and the proteasome.";
J. Biol. Chem. 278:3903-3911(2003).
[20]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 26-232 IN COMPLEX WITH IL4.
PubMed=10219247; DOI=10.1016/S0092-8674(00)80736-9;
Hage T., Sebald W., Reinemer P.;
"Crystal structure of the interleukin-4/receptor alpha chain complex
reveals a mosaic binding interface.";
Cell 97:271-281(1999).
[21]
VARIANTS VAL-75; ALA-400; ARG-431; LEU-436 AND PRO-786.
PubMed=9070874; DOI=10.1006/bbrc.1997.6115;
Deichmann K., Bardutzky J., Forster J., Heinzmann A., Kuehr J.;
"Common polymorphisms in the coding part of the IL4-receptor gene.";
Biochem. Biophys. Res. Commun. 231:696-697(1997).
[22]
VARIANT ARG-576.
PubMed=9392697; DOI=10.1056/NEJM199712113372403;
Hershey G.K.K., Friedrich M.F., Esswein L.A., Thomas M.L.,
Chatila T.A.;
"The association of atopy with a gain-of-function mutation in the
alpha subunit of the interleukin-4 receptor.";
N. Engl. J. Med. 337:1720-1725(1997).
[23]
VARIANT VAL-75.
PubMed=9620765; DOI=10.1038/472;
Mitsuyasu H., Izuhara K., Mao X.-Q., Gao P.S., Arinobu Y., Enomoto T.,
Kawai M., Sasaki S., Dake Y., Hamasaki N., Shirakawa T., Hopkin J.M.;
"Ile50Val variant of IL4R alpha upregulates IgE synthesis and
associates with atopic asthma.";
Nat. Genet. 19:119-120(1998).
[24]
VARIANT VAL-75.
PubMed=10390422; DOI=10.1164/ajrccm.160.1.9807130;
Noguchi E., Shibasaki M., Arinami T., Takeda K., Yokouchi Y.,
Kobayashi K., Imoto N., Nakahara S., Matsui A., Hamaguchi H.;
"No association between atopy/asthma and the Ile50Val polymorphism of
IL-4 receptor.";
Am. J. Respir. Crit. Care Med. 160:342-345(1999).
[25]
VARIANTS PRO-503 AND ARG-576.
PubMed=10233717; DOI=10.1046/j.1365-2567.1999.00705.x;
Kruse S., Japha T., Tedner M., Sparholt S.H., Forster J., Kuehr J.,
Deichmann K.A.;
"The polymorphisms S503P and Q576R in the interleukin-4 receptor alpha
gene are associated with atopy and influence the signal
transduction.";
Immunology 96:365-371(1999).
[26]
CHARACTERIZATION OF VARIANT ARG-576, AND MUTAGENESIS OF TYR-575.
PubMed=10201973;
Wang H.Y., Shelburne C.P., Zamorano J., Kelly A.E., Ryan J.J.,
Keegan A.D.;
"Effects of an allergy-associated mutation in the human IL-4R alpha
(Q576R) on human IL-4-induced signal transduction.";
J. Immunol. 162:4385-4389(1999).
[27]
VARIANT ALA-752.
PubMed=10677312; DOI=10.1086/302781;
Ober C., Leavitt S.A., Tsalenko A., Howard T.D., Hoki D.M., Daniel R.,
Newman D.L., Wu X., Parry R., Lester L.A., Solway J., Blumenthal M.,
King R.A., Xu J., Meyers D.A., Bleecker E.R., Cox N.J.;
"Variation in the interleukin 4-receptor alpha gene confers
susceptibility to asthma and atopy in ethnically diverse
populations.";
Am. J. Hum. Genet. 66:517-526(2000).
[28]
VARIANT ARG-576.
PubMed=10809862; DOI=10.1046/j.1365-2133.2000.03485.x;
Oiso N., Fukai K., Ishii M.;
"Interleukin 4 receptor alpha chain polymorphism Gln551Arg is
associated with adult atopic dermatitis in Japan.";
Br. J. Dermatol. 142:1003-1006(2000).
[29]
VARIANT PRO-786.
PubMed=11513543; DOI=10.1006/clim.2001.5082;
Andrews R.P., Burrell L., Rosa-Rosa L., Cunningham C.M.,
Brzezinski J.L., Bernstein J.A., Khurana Hershey G.K.;
"Analysis of the Ser786Pro interleukin-4 receptor alpha allelic
variant in allergic and nonallergic asthma and its functional
consequences.";
Clin. Immunol. 100:298-304(2001).
[30]
VARIANTS VAL-75 AND ALA-400, AND POLYMORPHISM.
PubMed=14657871; DOI=10.1016/j.jaci.2003.08.051;
Nakamura H., Miyagawa K., Ogino K., Endo T., Imai T., Ozasa K.,
Motohashi Y., Matsuzaki I., Sasahara S., Hatta K., Eboshida A.;
"High contribution contrast between the genes of eosinophil peroxidase
and IL-4 receptor alpha-chain in Japanese cedar pollinosis.";
J. Allergy Clin. Immunol. 112:1127-1131(2003).
-!- FUNCTION: Receptor for both interleukin 4 and interleukin 13.
Couples to the JAK1/2/3-STAT6 pathway. The IL4 response is
involved in promoting Th2 differentiation. The IL4/IL13 responses
are involved in regulating IgE production and, chemokine and mucus
production at sites of allergic inflammation. In certain cell
types, can signal through activation of insulin receptor
substrates, IRS1/IRS2. {ECO:0000269|PubMed:8124718}.
-!- FUNCTION: Soluble IL4R (sIL4R) inhibits IL4-mediated cell
proliferation and IL5 up-regulation by T-cells.
{ECO:0000269|PubMed:8124718}.
-!- SUBUNIT: The functional IL4 receptor is formed by initial binding
of IL4 to IL4R. Subsequent recruitment to the complex of the
common gamma chain, in immune cells, creates a type I receptor
and, in non-immune cells, of IL13RA1 forms a type II receptor.
IL4R can also interact with the IL13/IL13RA1 complex to form a
similar type II receptor (PubMed:7775445, PubMed:8804422).
Interacts with PIK3C3 (By similarity). Interacts with the SH2-
containing phosphatases, PTPN6/SHIP1, PTPN11/SHIP2 and INPP5D/SHIP
(PubMed:11714803). Interacts with JAK1 through a Box 1-containing
region; inhibited by SOCS5. Interacts with SOCS5; inhibits IL4
signaling (By similarity). Interacts with JAK3 (PubMed:7538655).
Interacts with CLM1 (By similarity).
{ECO:0000250|UniProtKB:P16382, ECO:0000269|PubMed:11714803,
ECO:0000269|PubMed:7538655, ECO:0000269|PubMed:7775445,
ECO:0000269|PubMed:8804422}.
-!- INTERACTION:
P05112:IL4; NbExp=7; IntAct=EBI-367009, EBI-367025;
P42226:STAT6; NbExp=4; IntAct=EBI-367009, EBI-1186478;
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
protein.
-!- SUBCELLULAR LOCATION: Isoform 2: Secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=Membrane-bound form;
IsoId=P24394-1; Sequence=Displayed;
Name=2; Synonyms=Soluble form, sIL4Ralpha/splice;
IsoId=P24394-2; Sequence=VSP_011116, VSP_011117;
Name=3;
IsoId=P24394-3; Sequence=VSP_053738;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are highly expressed
in activated T-cells.
-!- DOMAIN: The extracellular domain represents the IL4 binding
protein (IL4BP).
-!- DOMAIN: The WSXWS motif appears to be necessary for proper protein
folding and thereby efficient intracellular transport and cell-
surface receptor binding.
-!- DOMAIN: The box 1 motif is required for JAK interaction and/or
activation.
-!- DOMAIN: Contains 1 copy of a cytoplasmic motif that is referred to
as the immunoreceptor tyrosine-based inhibitor motif (ITIM). This
motif is involved in modulation of cellular responses. The
phosphorylated ITIM motif can bind the SH2 domain of several SH2-
containing phosphatases.
-!- PTM: On IL4 binding, phosphorylated on C-terminal tyrosine
residues. Phosphorylation on any one of tyrosine residues, Tyr-
575, Tyr-603 or Tyr-631, is required for STAT6-induced gene
induction. {ECO:0000269|PubMed:8804422}.
-!- PTM: The soluble form (sIL4R/IL4BP) can also be produced by
proteolytic cleavage at the cell surface (shedding) by a
metalloproteinase. {ECO:0000269|PubMed:10341317}.
-!- POLYMORPHISM: Allelic variants in IL4RA are associated with a
susceptibility to atopy, an immunological condition that can lead
to clinical symptoms such as allergic rhinitis, sinusitis, asthma
and eczema.
-!- POLYMORPHISM: Allelic variants in IL4RA are associated with cedar
pollen sensitization. Individuals develop Japanese cedar
pollinosis with increased exposure to cedar pollen. Japanese cedar
pollinosis is a type I allergic disease with ocular and nasal
symptoms that develop paroxysmally on contact with Japanese cedar
pollen. These symptoms, which occur seasonally each year, are
typical features of allergic rhinitis, such as sneezing, excessive
nasal secretion, nasal congestion, and conjunctival itching.
-!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 4
subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/il4r/";
-!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
polymorphism database;
URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=IL4R";
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EMBL; X52425; CAA36672.1; -; mRNA.
EMBL; AC004525; AAC23495.1; -; Genomic_DNA.
EMBL; AF421855; AAL12163.1; -; Genomic_DNA.
EMBL; AJ293647; CAC20445.1; -; Genomic_DNA.
EMBL; AJ293648; CAC20446.1; -; Genomic_DNA.
EMBL; AJ293649; CAC20447.1; -; Genomic_DNA.
EMBL; AJ293650; CAC20448.1; -; Genomic_DNA.
EMBL; AJ293651; CAC20449.1; -; Genomic_DNA.
EMBL; AJ293652; CAC20450.1; -; Genomic_DNA.
EMBL; AJ293653; CAC20451.1; -; Genomic_DNA.
EMBL; AK303255; BAG64338.1; -; mRNA.
EMBL; AC106739; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC151131; AAI51132.1; -; mRNA.
EMBL; AJ293654; CAC20452.1; -; Genomic_DNA.
CCDS; CCDS10629.1; -. [P24394-1]
CCDS; CCDS58441.1; -. [P24394-3]
PIR; A60386; A60386.
RefSeq; NP_000409.1; NM_000418.3. [P24394-1]
RefSeq; NP_001244335.1; NM_001257406.1. [P24394-1]
RefSeq; NP_001244336.1; NM_001257407.1. [P24394-3]
RefSeq; XP_011544127.1; XM_011545825.1. [P24394-1]
RefSeq; XP_011544128.1; XM_011545826.2. [P24394-1]
RefSeq; XP_011544129.1; XM_011545827.2. [P24394-1]
UniGene; Hs.513457; -.
UniGene; Hs.742121; -.
PDB; 1IAR; X-ray; 2.30 A; B=26-232.
PDB; 1IRS; NMR; -; B=489-499.
PDB; 1ITE; Model; -; C=26-232.
PDB; 3BPL; X-ray; 2.93 A; B=27-227.
PDB; 3BPN; X-ray; 3.02 A; B=27-227.
PDB; 3BPO; X-ray; 3.00 A; B=27-227.
PDB; 5E4E; X-ray; 3.00 A; B=26-228.
PDBsum; 1IAR; -.
PDBsum; 1IRS; -.
PDBsum; 1ITE; -.
PDBsum; 3BPL; -.
PDBsum; 3BPN; -.
PDBsum; 3BPO; -.
PDBsum; 5E4E; -.
ProteinModelPortal; P24394; -.
SMR; P24394; -.
BioGrid; 109780; 39.
CORUM; P24394; -.
DIP; DIP-3223N; -.
ELM; P24394; -.
IntAct; P24394; 11.
MINT; MINT-90363; -.
STRING; 9606.ENSP00000170630; -.
ChEMBL; CHEMBL3580490; -.
DrugBank; DB05078; AER001.
GuidetoPHARMACOLOGY; 1697; -.
iPTMnet; P24394; -.
PhosphoSitePlus; P24394; -.
BioMuta; IL4R; -.
DMDM; 124335; -.
PaxDb; P24394; -.
PeptideAtlas; P24394; -.
PRIDE; P24394; -.
Ensembl; ENST00000170630; ENSP00000170630; ENSG00000077238. [P24394-3]
Ensembl; ENST00000395762; ENSP00000379111; ENSG00000077238. [P24394-1]
Ensembl; ENST00000543915; ENSP00000441667; ENSG00000077238. [P24394-1]
GeneID; 3566; -.
KEGG; hsa:3566; -.
UCSC; uc002don.5; human. [P24394-1]
CTD; 3566; -.
DisGeNET; 3566; -.
EuPathDB; HostDB:ENSG00000077238.13; -.
GeneCards; IL4R; -.
HGNC; HGNC:6015; IL4R.
HPA; CAB004451; -.
HPA; HPA050124; -.
MalaCards; IL4R; -.
MIM; 147781; gene.
neXtProt; NX_P24394; -.
OpenTargets; ENSG00000077238; -.
PharmGKB; PA29832; -.
eggNOG; ENOG410IGBQ; Eukaryota.
eggNOG; ENOG41124QC; LUCA.
GeneTree; ENSGT00510000049182; -.
HOVERGEN; HBG052116; -.
InParanoid; P24394; -.
KO; K05071; -.
OMA; ASPCCGC; -.
OrthoDB; EOG091G010H; -.
PhylomeDB; P24394; -.
TreeFam; TF337996; -.
Reactome; R-HSA-6785807; Interleukin-4 and 13 signaling.
SignaLink; P24394; -.
SIGNOR; P24394; -.
ChiTaRS; IL4R; human.
EvolutionaryTrace; P24394; -.
GeneWiki; Interleukin-4_receptor; -.
GenomeRNAi; 3566; -.
PRO; PR:P24394; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000077238; -.
ExpressionAtlas; P24394; baseline and differential.
Genevisible; P24394; HS.
GO; GO:0005615; C:extracellular space; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0043235; C:receptor complex; IDA:MGI.
GO; GO:0004913; F:interleukin-4 receptor activity; TAS:ProtInc.
GO; GO:0005057; F:signal transducer activity, downstream of receptor; TAS:ProtInc.
GO; GO:0042832; P:defense response to protozoan; IEA:Ensembl.
GO; GO:0006955; P:immune response; TAS:ProtInc.
GO; GO:0016064; P:immunoglobulin mediated immune response; IEA:Ensembl.
GO; GO:0045626; P:negative regulation of T-helper 1 cell differentiation; IEA:Ensembl.
GO; GO:0030728; P:ovulation; IEA:Ensembl.
GO; GO:0090197; P:positive regulation of chemokine secretion; IEA:Ensembl.
GO; GO:0002639; P:positive regulation of immunoglobulin production; IEA:Ensembl.
GO; GO:0043032; P:positive regulation of macrophage activation; IEA:Ensembl.
GO; GO:0043306; P:positive regulation of mast cell degranulation; IEA:Ensembl.
GO; GO:1901741; P:positive regulation of myoblast fusion; IEA:Ensembl.
GO; GO:0045630; P:positive regulation of T-helper 2 cell differentiation; IEA:Ensembl.
GO; GO:0002532; P:production of molecular mediator involved in inflammatory response; IEA:InterPro.
GO; GO:0042127; P:regulation of cell proliferation; IEA:Ensembl.
GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
GO; GO:1990834; P:response to odorant; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
CDD; cd00063; FN3; 1.
Gene3D; 2.60.40.10; -; 2.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR003531; Hempt_rcpt_S_F1_CS.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR015319; IL-4_rcpt-alpha_N.
Pfam; PF09238; IL4Ra_N; 1.
SUPFAM; SSF49265; SSF49265; 2.
PROSITE; PS50853; FN3; 1.
PROSITE; PS01355; HEMATOPO_REC_S_F1; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Complete proteome;
Disulfide bond; Glycoprotein; Immunity; Membrane; Phosphoprotein;
Polymorphism; Receptor; Reference proteome; Secreted; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 25 {ECO:0000250}.
CHAIN 26 825 Interleukin-4 receptor subunit alpha.
/FTId=PRO_0000010887.
CHAIN 26 ? Soluble interleukin-4 receptor subunit
alpha.
/FTId=PRO_0000010888.
TOPO_DOM 26 232 Extracellular. {ECO:0000255}.
TRANSMEM 233 256 Helical. {ECO:0000255}.
TOPO_DOM 257 825 Cytoplasmic. {ECO:0000255}.
DOMAIN 125 224 Fibronectin type-III.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
REGION 437 557 Required for IRS1 activation and IL4-
induced cell growth.
REGION 558 657 Required for IL4-induced gene expression.
MOTIF 212 216 WSXWS motif.
MOTIF 262 270 Box 1 motif.
MOTIF 711 716 ITIM motif.
COMPBIAS 370 380 Poly-Glu.
COMPBIAS 563 566 Poly-Ala.
COMPBIAS 789 794 Poly-Ser.
SITE 38 38 Major IL4 binding determinant.
SITE 64 64 Minor IL4 binding determinant.
SITE 66 66 Minor IL4 binding determinant.
SITE 92 92 Minor IL4 binding determinant.
SITE 94 94 Minor IL4 binding determinant.
SITE 97 97 Major IL4 binding determinant.
SITE 152 152 Minor IL4 binding determinant.
SITE 208 208 Major IL4 binding determinant.
MOD_RES 497 497 Phosphotyrosine.
{ECO:0000269|PubMed:8124718}.
MOD_RES 575 575 Phosphotyrosine.
{ECO:0000305|PubMed:8804422}.
MOD_RES 603 603 Phosphotyrosine.
{ECO:0000305|PubMed:8804422}.
MOD_RES 631 631 Phosphotyrosine.
{ECO:0000305|PubMed:8804422}.
CARBOHYD 53 53 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 98 98 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 128 128 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 134 134 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 176 176 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 209 209 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 34 44 {ECO:0000250}.
DISULFID 74 86 {ECO:0000250}.
VAR_SEQ 1 23 MGWLCSGLLFPVSCLVLLQVASS -> MQKDARRE (in
isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_053738.
VAR_SEQ 225 227 YRE -> NIC (in isoform 2). {ECO:0000305}.
/FTId=VSP_011116.
VAR_SEQ 228 825 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_011117.
VARIANT 75 75 I -> F (in dbSNP:rs1805010).
/FTId=VAR_059302.
VARIANT 75 75 I -> L (in dbSNP:rs1805010).
/FTId=VAR_059303.
VARIANT 75 75 I -> V (associated with atopic asthma and
cedar pollen sensitization;
dbSNP:rs1805010).
{ECO:0000269|PubMed:10390422,
ECO:0000269|PubMed:14657871,
ECO:0000269|PubMed:9070874,
ECO:0000269|PubMed:9620765,
ECO:0000269|Ref.5}.
/FTId=VAR_008034.
VARIANT 387 387 S -> L (in dbSNP:rs6413500).
/FTId=VAR_019999.
VARIANT 400 400 E -> A (associated with cedar pollen
sensitization; dbSNP:rs1805011).
{ECO:0000269|PubMed:11285129,
ECO:0000269|PubMed:14657871,
ECO:0000269|PubMed:9070874,
ECO:0000269|Ref.5}.
/FTId=VAR_011657.
VARIANT 431 431 C -> R (in dbSNP:rs1805012).
{ECO:0000269|PubMed:11285129,
ECO:0000269|PubMed:9070874,
ECO:0000269|Ref.5}.
/FTId=VAR_011658.
VARIANT 436 436 S -> L (in dbSNP:rs1805013).
{ECO:0000269|PubMed:11285129,
ECO:0000269|PubMed:9070874,
ECO:0000269|Ref.5}.
/FTId=VAR_011659.
VARIANT 492 492 A -> T (in dbSNP:rs35606110).
/FTId=VAR_049164.
VARIANT 492 492 A -> V (in dbSNP:rs34727572).
/FTId=VAR_049165.
VARIANT 503 503 S -> P (lowered total IgE concentration;
dbSNP:rs1805015).
{ECO:0000269|PubMed:10233717,
ECO:0000269|PubMed:11285129,
ECO:0000269|Ref.5}.
/FTId=VAR_011660.
VARIANT 576 576 Q -> R (associated with atopic
dermatitis; lowered total IgE
concentration; no effect on IL4-induced
signal transduction; dbSNP:rs1801275).
{ECO:0000269|PubMed:10201973,
ECO:0000269|PubMed:10233717,
ECO:0000269|PubMed:10809862,
ECO:0000269|PubMed:11285129,
ECO:0000269|PubMed:9392697,
ECO:0000269|Ref.5}.
/FTId=VAR_008035.
VARIANT 579 579 V -> I (in dbSNP:rs3024677).
{ECO:0000269|PubMed:11285129,
ECO:0000269|Ref.5}.
/FTId=VAR_011661.
VARIANT 675 675 P -> S (in dbSNP:rs3024678).
{ECO:0000269|Ref.5}.
/FTId=VAR_020000.
VARIANT 752 752 S -> A (in dbSNP:rs1805016).
{ECO:0000269|PubMed:10677312,
ECO:0000269|Ref.5}.
/FTId=VAR_011662.
VARIANT 786 786 S -> P (in 1.8% of the population;
dbSNP:rs1805014).
{ECO:0000269|PubMed:11513543,
ECO:0000269|PubMed:9070874}.
/FTId=VAR_011663.
MUTAGEN 38 38 Y->A: 700-fold reduction in IL4 binding.
{ECO:0000269|PubMed:11786020}.
MUTAGEN 38 38 Y->F: 25-fold reduction in IL4 binding.
{ECO:0000269|PubMed:11786020}.
MUTAGEN 39 39 M->A: No effect on IL4 binding.
{ECO:0000269|PubMed:11786020}.
MUTAGEN 40 40 S->A: No effect on IL4 binding.
{ECO:0000269|PubMed:11786020}.
MUTAGEN 64 64 L->A: 100-fold reduction in IL4 binding.
{ECO:0000269|PubMed:11786020}.
MUTAGEN 66 66 F->A: 45-fold reduction in IL4 binding.
{ECO:0000269|PubMed:11786020}.
MUTAGEN 67 67 L->A: No effect on IL4 binding.
{ECO:0000269|PubMed:11786020}.
MUTAGEN 68 68 L->A: No effect on IL4 binding.
{ECO:0000269|PubMed:11786020}.
MUTAGEN 91 91 D->A: Little effect on IL4 binding.
{ECO:0000269|PubMed:11786020}.
MUTAGEN 92 92 D->A: 50-fold reduction in IL4 binding.
{ECO:0000269|PubMed:11786020}.
MUTAGEN 93 93 V->A: Little effect on IL4 binding.
{ECO:0000269|PubMed:11786020}.
MUTAGEN 94 94 V->A: 35-fold reduction in IL4 binding.
{ECO:0000269|PubMed:11786020}.
MUTAGEN 95 95 S->A: No effect on IL4 binding.
{ECO:0000269|PubMed:11786020}.
MUTAGEN 97 97 D->A,N: >150-fold reduction in IL4
binding. {ECO:0000269|PubMed:11786020}.
MUTAGEN 98 98 N->A: No effect on IL4 binding.
{ECO:0000269|PubMed:11786020}.
MUTAGEN 99 99 Y->A: 10-fold reduction in IL4 binding.
{ECO:0000269|PubMed:11786020}.
MUTAGEN 116 116 K->A: Little effect on IL4 binding.
{ECO:0000269|PubMed:11786020}.
MUTAGEN 117 117 P->A: Little effect on IL4 binding.
{ECO:0000269|PubMed:11786020}.
MUTAGEN 118 118 S->A: No effect on IL4 binding.
{ECO:0000269|PubMed:11786020}.
MUTAGEN 119 119 E->A: No effect on IL4 binding.
{ECO:0000269|PubMed:11786020}.
MUTAGEN 150 150 D->A: Little effect on IL4 binding.
{ECO:0000269|PubMed:11786020}.
MUTAGEN 151 151 N->A: Little effect on IL4 binding.
{ECO:0000269|PubMed:11786020}.
MUTAGEN 152 152 Y->A: 40-fold reduction in IL4 binding.
{ECO:0000269|PubMed:11786020}.
MUTAGEN 152 152 Y->F: No effect on IL4 binding.
{ECO:0000269|PubMed:11786020}.
MUTAGEN 153 153 L->A: Little effect on IL4 binding.
{ECO:0000269|PubMed:11786020}.
MUTAGEN 154 154 Y->A: Little effect on IL4 binding.
{ECO:0000269|PubMed:11786020}.
MUTAGEN 208 208 Y->A: 500-fold reduction in IL4 binding.
{ECO:0000269|PubMed:11786020}.
MUTAGEN 208 208 Y->F: 200-fold reduction in IL4 binding.
{ECO:0000269|PubMed:11786020}.
MUTAGEN 497 497 Y->F: Abolishes IRS1 tyrosine
phosphorylation. No cell proliferation.
{ECO:0000269|PubMed:8124718}.
MUTAGEN 575 575 Y->F: Loss of CD23 gene induction; when
associated with F-603 and F-631.
{ECO:0000269|PubMed:10201973,
ECO:0000269|PubMed:8624803}.
MUTAGEN 603 603 Y->F: Loss of CD23 gene induction; when
associated with F-575 and F-631.
{ECO:0000269|PubMed:8624803}.
MUTAGEN 631 631 Y->F: Loss of CD23 gene induction; when
associated with F-575 and F-603.
{ECO:0000269|PubMed:8624803}.
MUTAGEN 713 713 Y->F: Increased IL4-induced cell
proliferation and STAT6 activation.
{ECO:0000269|PubMed:11714803}.
STRAND 28 36 {ECO:0000244|PDB:1IAR}.
STRAND 38 50 {ECO:0000244|PDB:1IAR}.
HELIX 54 57 {ECO:0000244|PDB:1IAR}.
STRAND 58 68 {ECO:0000244|PDB:1IAR}.
STRAND 72 74 {ECO:0000244|PDB:1IAR}.
STRAND 77 89 {ECO:0000244|PDB:1IAR}.
STRAND 99 105 {ECO:0000244|PDB:1IAR}.
STRAND 108 115 {ECO:0000244|PDB:1IAR}.
HELIX 117 119 {ECO:0000244|PDB:1IAR}.
STRAND 127 132 {ECO:0000244|PDB:1IAR}.
TURN 135 137 {ECO:0000244|PDB:3BPO}.
STRAND 139 144 {ECO:0000244|PDB:1IAR}.
HELIX 154 156 {ECO:0000244|PDB:1IAR}.
STRAND 158 168 {ECO:0000244|PDB:1IAR}.
STRAND 172 177 {ECO:0000244|PDB:1IAR}.
STRAND 179 181 {ECO:0000244|PDB:5E4E}.
STRAND 183 186 {ECO:0000244|PDB:1IAR}.
HELIX 188 190 {ECO:0000244|PDB:3BPL}.
STRAND 193 195 {ECO:0000244|PDB:3BPO}.
STRAND 197 204 {ECO:0000244|PDB:1IAR}.
HELIX 206 208 {ECO:0000244|PDB:1IAR}.
STRAND 219 221 {ECO:0000244|PDB:1IAR}.
HELIX 495 497 {ECO:0000244|PDB:1IRS}.
SEQUENCE 825 AA; 89658 MW; 9F886DF5612297F8 CRC64;
MGWLCSGLLF PVSCLVLLQV ASSGNMKVLQ EPTCVSDYMS ISTCEWKMNG PTNCSTELRL
LYQLVFLLSE AHTCIPENNG GAGCVCHLLM DDVVSADNYT LDLWAGQQLL WKGSFKPSEH
VKPRAPGNLT VHTNVSDTLL LTWSNPYPPD NYLYNHLTYA VNIWSENDPA DFRIYNVTYL
EPSLRIAAST LKSGISYRAR VRAWAQCYNT TWSEWSPSTK WHNSYREPFE QHLLLGVSVS
CIVILAVCLL CYVSITKIKK EWWDQIPNPA RSRLVAIIIQ DAQGSQWEKR SRGQEPAKCP
HWKNCLTKLL PCFLEHNMKR DEDPHKAAKE MPFQGSGKSA WCPVEISKTV LWPESISVVR
CVELFEAPVE CEEEEEVEEE KGSFCASPES SRDDFQEGRE GIVARLTESL FLDLLGEENG
GFCQQDMGES CLLPPSGSTS AHMPWDEFPS AGPKEAPPWG KEQPLHLEPS PPASPTQSPD
NLTCTETPLV IAGNPAYRSF SNSLSQSPCP RELGPDPLLA RHLEEVEPEM PCVPQLSEPT
TVPQPEPETW EQILRRNVLQ HGAAAAPVSA PTSGYQEFVH AVEQGGTQAS AVVGLGPPGE
AGYKAFSSLL ASSAVSPEKC GFGASSGEEG YKPFQDLIPG CPGDPAPVPV PLFTFGLDRE
PPRSPQSSHL PSSSPEHLGL EPGEKVEDMP KPPLPQEQAT DPLVDSLGSG IVYSALTCHL
CGHLKQCHGQ EDGGQTPVMA SPCCGCCCGD RSSPPTTPLR APDPSPGGVP LEASLCPASL
APSGISEKSK SSSSFHPAPG NAQSSSQTPK IVNFVSVGPT YMRVS


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