IL4RA_HUMAN
ID IL4RA_HUMAN Reviewed; 825 AA.
AC P24394; B4E076; B9EKU8; H3BSY5; Q96P01; Q9H181; Q9H182; Q9H183; Q9H184;
AC Q9H185; Q9H186; Q9H187; Q9H188;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 232.
DE RecName: Full=Interleukin-4 receptor subunit alpha;
DE Short=IL-4 receptor subunit alpha;
DE Short=IL-4R subunit alpha;
DE Short=IL-4R-alpha;
DE Short=IL-4RA;
DE AltName: CD_antigen=CD124;
DE Contains:
DE RecName: Full=Soluble interleukin-4 receptor subunit alpha;
DE Short=Soluble IL-4 receptor subunit alpha;
DE Short=Soluble IL-4R-alpha;
DE Short=sIL4Ralpha/prot;
DE AltName: Full=IL-4-binding protein;
DE Short=IL4-BP;
DE Flags: Precursor;
GN Name=IL4R; Synonyms=IL4RA; ORFNames=582J2.1;
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).
RC TISSUE=Peripheral blood;
RX PubMed=2307934; DOI=10.1084/jem.171.3.861;
RA Idzerda R.L., March C.J., Mosley B., Lyman S.D., Bos T.V., Gimpel S.D.,
RA Din W.S., Grabstein K.H., Widmer M.B., Park L.S., Cosman D., Beckmann M.P.;
RT "Human interleukin 4 receptor confers biological responsiveness and defines
RT a novel receptor superfamily.";
RL J. Exp. Med. 171:861-873(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Myeloid leukemia cell;
RX PubMed=2278997; DOI=10.1093/intimm/2.7.669;
RA Galizzi J.-P., Zuber C.E., Harada N., Gorman D.M., Djossou O.,
RA Kastelein R., Banchereau J., Howard M., Miyajima A.;
RT "Molecular cloning of a cDNA encoding the human interleukin 4 receptor.";
RL Int. Immunol. 2:669-675(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC TISSUE=Blood;
RX PubMed=10590262; DOI=10.1093/intimm/11.12.1965;
RA Kruse S., Forster J., Kuehr J., Deichmann K.A.;
RT "Characterization of the membrane-bound and a soluble form of human IL-4
RT receptor alpha produced by alternative splicing.";
RL Int. Immunol. 11:1965-1970(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 1).
RX PubMed=10493829; DOI=10.1006/geno.1999.5927;
RA Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R., Fuhrmann J.,
RA Mason T., Crosby M.L., Barnstead M., Cronin L., Mays A.D., Cao Y., Xu R.X.,
RA Kang H.-L., Mitchell S., Eichler E.E., Harris P.C., Venter J.C.,
RA Adams M.D.;
RT "Genome duplications and other features in 12 Mb of DNA sequence from human
RT chromosome 16p and 16q.";
RL Genomics 60:295-308(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-75; ALA-400; ARG-431;
RP LEU-436; PRO-503; ARG-576; ILE-579; SER-675 AND ALA-752.
RG SeattleSNPs variation discovery resource;
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 301-825 (ISOFORM 1), AND VARIANTS
RP ALA-400; ARG-431; LEU-436; PRO-503; ARG-576 AND ILE-579.
RX PubMed=11285129; DOI=10.1034/j.1399-0039.2001.057003216.x;
RA Lozano F., Places L., Vila J.-M., Padilla O., Arman M., Gimferrer I.,
RA Suarez B., Lopez de la Iglesia A., Miserachs N., Vives J.;
RT "Identification of a novel single-nucleotide polymorphism (Val554Ile) and
RT definition of eight common alleles for human IL4RA exon 11.";
RL Tissue Antigens 57:216-220(2001).
RN [10]
RP FUNCTION IN IRS1 ACTIVATION, PHOSPHORYLATION AT TYR-497, AND MUTAGENESIS OF
RP TYR-497.
RX PubMed=8124718; DOI=10.1016/0092-8674(94)90356-5;
RA Keegan A.D., Nelms K., White M., Wang L.-M., Pierce J.H., Paul W.E.;
RT "An IL-4 receptor region containing an insulin receptor motif is important
RT for IL-4-mediated IRS-1 phosphorylation and cell growth.";
RL Cell 76:811-820(1994).
RN [11]
RP DOMAIN JAK3 ACTIVATION.
RX PubMed=7721895; DOI=10.1074/jbc.270.16.9630;
RA Malabarba M.G., Kirken R.A., Rui H., Koettnitz K., Kawamura M.,
RA O'Shea J.J., Kalthoff F.S., Farrar W.L.;
RT "Activation of JAK3, but not JAK1, is critical to interleukin-4 (IL4)
RT stimulated proliferation and requires a membrane-proximal region of IL4
RT receptor alpha.";
RL J. Biol. Chem. 270:9630-9637(1995).
RN [12]
RP INTERACTION WITH IL13RA1.
RX PubMed=7775445; DOI=10.1074/jbc.270.23.13869;
RA Zurawski S.M., Chomarat P., Djossou O., Bidaud C., McKenzie A.N.,
RA Miossec P., Banchereau J., Zurawski G.;
RT "The primary binding subunit of the human interleukin-4 receptor is also a
RT component of the interleukin-13 receptor.";
RL J. Biol. Chem. 270:13869-13878(1995).
RN [13]
RP INTERACTION WITH JAK3.
RX PubMed=7538655;
RA Rolling C., Treton D., Beckmann P., Galanaud P., Richard Y.;
RT "JAK3 associates with the human interleukin 4 receptor and is tyrosine
RT phosphorylated following receptor triggering.";
RL Oncogene 10:1757-1761(1995).
RN [14]
RP INTERACTION WITH IL13RA1, AND PHOSPHORYLATION.
RX PubMed=8804422; DOI=10.1016/0014-5793(96)00835-6;
RA Rolling C., Treton D., Pellegrini S., Galanaud P., Richard Y.;
RT "IL4 and IL13 receptors share the gamma c chain and activate STAT6, STAT3
RT and STAT5 proteins in normal human B cells.";
RL FEBS Lett. 393:53-56(1996).
RN [15]
RP DOMAIN STAT6 ACTIVATION, MUTAGENESIS OF TYR-575; TYR-603 AND TYR-631, AND
RP PHOSPHORYLATION AT TYR-575; TYR-603 AND TYR-631.
RX PubMed=8624803; DOI=10.1016/s1074-7613(00)80677-9;
RA Ryan J.J., McReynolds L.J., Keegan A., Wang L.-H., Garfein E., Rothman P.,
RA Nelms K., Paul W.E.;
RT "Growth and gene expression are predominantly controlled by distinct
RT regions of the human IL-4 receptor.";
RL Immunity 4:123-132(1996).
RN [16]
RP PROTEOLYTIC PROCESSING.
RX PubMed=10341317; DOI=10.1159/000024171;
RA Jung T., Schrader N., Hellwig M., Enssle K.H., Neumann C.;
RT "Soluble human interleukin-4 receptor is produced by activated T cells
RT under the control of metalloproteinases.";
RL Int. Arch. Allergy Immunol. 119:23-30(1999).
RN [17]
RP INTERACTION WITH PTPN6; PTPN11 AND INPP5D, STAT6 ACTIVATION, AND
RP MUTAGENESIS OF TYR-713.
RX PubMed=11714803; DOI=10.4049/jimmunol.167.11.6382;
RA Kashiwada M., Giallourakis C.C., Pan P.-Y., Rothman P.B.;
RT "Immunoreceptor tyrosine-based inhibitory motif of the IL-4 receptor
RT associates with SH2-containing phosphatases and regulates IL-4-induced
RT proliferation.";
RL J. Immunol. 167:6382-6387(2001).
RN [18]
RP LIGAND-BINDING SITES, AND MUTAGENESIS OF TYR-38; MET-39; SER-40; LEU-64;
RP PHE-66; LEU-67; LEU-68; ASP-91; ASP-92; VAL-93; VAL-94; SER-95; ASP-97;
RP ASN-98; TYR-99; LYS-116; PRO-117; SER-118; GLU-119; ASP-150; ASN-151;
RP TYR-152; LEU-153; TYR-154 AND TYR-208.
RX PubMed=11786020; DOI=10.1006/jmbi.2001.5243;
RA Zhang J.-L., Simeonowa I., Wang Y., Sebald W.;
RT "The high-affinity interaction of human IL-4 and the receptor alpha chain
RT is constituted by two independent binding clusters.";
RL J. Mol. Biol. 315:399-407(2002).
RN [19]
RP STAT6 ACTIVATION, AND INHIBITION BY TYROSINE PHOSPHATASE SHP1.
RX PubMed=12459556; DOI=10.1074/jbc.m211747200;
RA Hanson E.M., Dickensheets H., Qu C.K., Donnelly R.P., Keegan A.D.;
RT "Regulation of the dephosphorylation of Stat6. Participation of Tyr-713 in
RT the interleukin-4 receptor alpha, the tyrosine phosphatase SHP-1, and the
RT proteasome.";
RL J. Biol. Chem. 278:3903-3911(2003).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 26-232 IN COMPLEX WITH IL4.
RX PubMed=10219247; DOI=10.1016/S0092-8674(00)80736-9;
RA Hage T., Sebald W., Reinemer P.;
RT "Crystal structure of the interleukin-4/receptor alpha chain complex
RT reveals a mosaic binding interface.";
RL Cell 97:271-281(1999).
RN [21]
RP VARIANTS VAL-75; ALA-400; ARG-431; LEU-436 AND PRO-786.
RX PubMed=9070874; DOI=10.1006/bbrc.1997.6115;
RA Deichmann K., Bardutzky J., Forster J., Heinzmann A., Kuehr J.;
RT "Common polymorphisms in the coding part of the IL4-receptor gene.";
RL Biochem. Biophys. Res. Commun. 231:696-697(1997).
RN [22]
RP VARIANT ARG-576.
RX PubMed=9392697; DOI=10.1056/nejm199712113372403;
RA Hershey G.K.K., Friedrich M.F., Esswein L.A., Thomas M.L., Chatila T.A.;
RT "The association of atopy with a gain-of-function mutation in the alpha
RT subunit of the interleukin-4 receptor.";
RL N. Engl. J. Med. 337:1720-1725(1997).
RN [23]
RP VARIANT VAL-75.
RX PubMed=9620765; DOI=10.1038/472;
RA Mitsuyasu H., Izuhara K., Mao X.-Q., Gao P.S., Arinobu Y., Enomoto T.,
RA Kawai M., Sasaki S., Dake Y., Hamasaki N., Shirakawa T., Hopkin J.M.;
RT "Ile50Val variant of IL4R alpha upregulates IgE synthesis and associates
RT with atopic asthma.";
RL Nat. Genet. 19:119-120(1998).
RN [24]
RP VARIANT VAL-75.
RX PubMed=10390422; DOI=10.1164/ajrccm.160.1.9807130;
RA Noguchi E., Shibasaki M., Arinami T., Takeda K., Yokouchi Y., Kobayashi K.,
RA Imoto N., Nakahara S., Matsui A., Hamaguchi H.;
RT "No association between atopy/asthma and the Ile50Val polymorphism of IL-4
RT receptor.";
RL Am. J. Respir. Crit. Care Med. 160:342-345(1999).
RN [25]
RP VARIANTS PRO-503 AND ARG-576.
RX PubMed=10233717; DOI=10.1046/j.1365-2567.1999.00705.x;
RA Kruse S., Japha T., Tedner M., Sparholt S.H., Forster J., Kuehr J.,
RA Deichmann K.A.;
RT "The polymorphisms S503P and Q576R in the interleukin-4 receptor alpha gene
RT are associated with atopy and influence the signal transduction.";
RL Immunology 96:365-371(1999).
RN [26]
RP CHARACTERIZATION OF VARIANT ARG-576, AND MUTAGENESIS OF TYR-575.
RX PubMed=10201973;
RA Wang H.Y., Shelburne C.P., Zamorano J., Kelly A.E., Ryan J.J., Keegan A.D.;
RT "Effects of an allergy-associated mutation in the human IL-4R alpha (Q576R)
RT on human IL-4-induced signal transduction.";
RL J. Immunol. 162:4385-4389(1999).
RN [27]
RP VARIANT ALA-752.
RX PubMed=10677312; DOI=10.1086/302781;
RA Ober C., Leavitt S.A., Tsalenko A., Howard T.D., Hoki D.M., Daniel R.,
RA Newman D.L., Wu X., Parry R., Lester L.A., Solway J., Blumenthal M.,
RA King R.A., Xu J., Meyers D.A., Bleecker E.R., Cox N.J.;
RT "Variation in the interleukin 4-receptor alpha gene confers susceptibility
RT to asthma and atopy in ethnically diverse populations.";
RL Am. J. Hum. Genet. 66:517-526(2000).
RN [28]
RP VARIANT ARG-576.
RX PubMed=10809862; DOI=10.1046/j.1365-2133.2000.03485.x;
RA Oiso N., Fukai K., Ishii M.;
RT "Interleukin 4 receptor alpha chain polymorphism Gln551Arg is associated
RT with adult atopic dermatitis in Japan.";
RL Br. J. Dermatol. 142:1003-1006(2000).
RN [29]
RP VARIANT PRO-786.
RX PubMed=11513543; DOI=10.1006/clim.2001.5082;
RA Andrews R.P., Burrell L., Rosa-Rosa L., Cunningham C.M., Brzezinski J.L.,
RA Bernstein J.A., Khurana Hershey G.K.;
RT "Analysis of the Ser786Pro interleukin-4 receptor alpha allelic variant in
RT allergic and nonallergic asthma and its functional consequences.";
RL Clin. Immunol. 100:298-304(2001).
RN [30]
RP VARIANTS VAL-75 AND ALA-400, AND POLYMORPHISM.
RX PubMed=14657871; DOI=10.1016/j.jaci.2003.08.051;
RA Nakamura H., Miyagawa K., Ogino K., Endo T., Imai T., Ozasa K.,
RA Motohashi Y., Matsuzaki I., Sasahara S., Hatta K., Eboshida A.;
RT "High contribution contrast between the genes of eosinophil peroxidase and
RT IL-4 receptor alpha-chain in Japanese cedar pollinosis.";
RL J. Allergy Clin. Immunol. 112:1127-1131(2003).
CC -!- FUNCTION: Receptor for both interleukin 4 and interleukin 13. Couples
CC to the JAK1/2/3-STAT6 pathway. The IL4 response is involved in
CC promoting Th2 differentiation. The IL4/IL13 responses are involved in
CC regulating IgE production and, chemokine and mucus production at sites
CC of allergic inflammation. In certain cell types, can signal through
CC activation of insulin receptor substrates, IRS1/IRS2.
CC {ECO:0000269|PubMed:8124718}.
CC -!- FUNCTION: Soluble IL4R (sIL4R) inhibits IL4-mediated cell proliferation
CC and IL5 up-regulation by T-cells. {ECO:0000269|PubMed:8124718}.
CC -!- SUBUNIT: The functional IL4 receptor is formed by initial binding of
CC IL4 to IL4R. Subsequent recruitment to the complex of the common gamma
CC chain, in immune cells, creates a type I receptor and, in non-immune
CC cells, of IL13RA1 forms a type II receptor. IL4R can also interact with
CC the IL13/IL13RA1 complex to form a similar type II receptor
CC (PubMed:7775445, PubMed:8804422). Interacts with PIK3C3 (By
CC similarity). Interacts with the SH2-containing phosphatases,
CC PTPN6/SHIP1, PTPN11/SHIP2 and INPP5D/SHIP (PubMed:11714803). Interacts
CC with JAK1 through a Box 1-containing region; inhibited by SOCS5.
CC Interacts with SOCS5; inhibits IL4 signaling (By similarity). Interacts
CC with JAK3 (PubMed:7538655). Interacts with CLM1 (By similarity).
CC {ECO:0000250|UniProtKB:P16382, ECO:0000269|PubMed:11714803,
CC ECO:0000269|PubMed:7538655, ECO:0000269|PubMed:7775445,
CC ECO:0000269|PubMed:8804422}.
CC -!- INTERACTION:
CC P24394; P05112: IL4; NbExp=7; IntAct=EBI-367009, EBI-367025;
CC P24394; P42226: STAT6; NbExp=4; IntAct=EBI-367009, EBI-1186478;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Membrane-bound form;
CC IsoId=P24394-1; Sequence=Displayed;
CC Name=2; Synonyms=Soluble form, sIL4Ralpha/splice;
CC IsoId=P24394-2; Sequence=VSP_011116, VSP_011117;
CC Name=3;
CC IsoId=P24394-3; Sequence=VSP_053738;
CC -!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are highly expressed in
CC activated T-cells.
CC -!- DOMAIN: The extracellular domain represents the IL4 binding protein
CC (IL4BP).
CC -!- DOMAIN: The WSXWS motif appears to be necessary for proper protein
CC folding and thereby efficient intracellular transport and cell-surface
CC receptor binding.
CC -!- DOMAIN: The box 1 motif is required for JAK interaction and/or
CC activation.
CC -!- DOMAIN: Contains 1 copy of a cytoplasmic motif that is referred to as
CC the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is
CC involved in modulation of cellular responses. The phosphorylated ITIM
CC motif can bind the SH2 domain of several SH2-containing phosphatases.
CC -!- PTM: On IL4 binding, phosphorylated on C-terminal tyrosine residues.
CC Phosphorylation on any one of tyrosine residues, Tyr-575, Tyr-603 or
CC Tyr-631, is required for STAT6-induced gene induction.
CC {ECO:0000269|PubMed:8624803}.
CC -!- PTM: The soluble form (sIL4R/IL4BP) can also be produced by proteolytic
CC cleavage at the cell surface (shedding) by a metalloproteinase.
CC {ECO:0000269|PubMed:10341317}.
CC -!- POLYMORPHISM: Allelic variants in IL4RA are associated with a
CC susceptibility to atopy, an immunological condition that can lead to
CC clinical symptoms such as allergic rhinitis, sinusitis, asthma and
CC eczema.
CC -!- POLYMORPHISM: Allelic variants in IL4RA are associated with cedar
CC pollen sensitization. Individuals develop Japanese cedar pollinosis
CC with increased exposure to cedar pollen. Japanese cedar pollinosis is a
CC type I allergic disease with ocular and nasal symptoms that develop
CC paroxysmally on contact with Japanese cedar pollen. These symptoms,
CC which occur seasonally each year, are typical features of allergic
CC rhinitis, such as sneezing, excessive nasal secretion, nasal
CC congestion, and conjunctival itching.
CC -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 4
CC subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/il4r/";
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DR EMBL; X52425; CAA36672.1; -; mRNA.
DR EMBL; AC004525; AAC23495.1; -; Genomic_DNA.
DR EMBL; AF421855; AAL12163.1; -; Genomic_DNA.
DR EMBL; AJ293647; CAC20445.1; -; Genomic_DNA.
DR EMBL; AJ293648; CAC20446.1; -; Genomic_DNA.
DR EMBL; AJ293649; CAC20447.1; -; Genomic_DNA.
DR EMBL; AJ293650; CAC20448.1; -; Genomic_DNA.
DR EMBL; AJ293651; CAC20449.1; -; Genomic_DNA.
DR EMBL; AJ293652; CAC20450.1; -; Genomic_DNA.
DR EMBL; AJ293653; CAC20451.1; -; Genomic_DNA.
DR EMBL; AK303255; BAG64338.1; -; mRNA.
DR EMBL; AC106739; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC151131; AAI51132.1; -; mRNA.
DR EMBL; AJ293654; CAC20452.1; -; Genomic_DNA.
DR CCDS; CCDS10629.1; -. [P24394-1]
DR CCDS; CCDS58441.1; -. [P24394-3]
DR PIR; A60386; A60386.
DR RefSeq; NP_000409.1; NM_000418.3. [P24394-1]
DR RefSeq; NP_001244335.1; NM_001257406.1. [P24394-1]
DR RefSeq; NP_001244336.1; NM_001257407.1. [P24394-3]
DR RefSeq; XP_011544127.1; XM_011545825.1. [P24394-1]
DR RefSeq; XP_011544128.1; XM_011545826.2. [P24394-1]
DR RefSeq; XP_011544129.1; XM_011545827.2. [P24394-1]
DR PDB; 1IAR; X-ray; 2.30 A; B=26-232.
DR PDB; 1IRS; NMR; -; B=489-499.
DR PDB; 3BPL; X-ray; 2.93 A; B=27-227.
DR PDB; 3BPN; X-ray; 3.02 A; B=27-227.
DR PDB; 3BPO; X-ray; 3.00 A; B=27-227.
DR PDB; 5E4E; X-ray; 3.00 A; B=26-228.
DR PDB; 6OEL; X-ray; 3.10 A; B=27-224.
DR PDB; 6WGL; X-ray; 2.82 A; C=26-232.
DR PDBsum; 1IAR; -.
DR PDBsum; 1IRS; -.
DR PDBsum; 3BPL; -.
DR PDBsum; 3BPN; -.
DR PDBsum; 3BPO; -.
DR PDBsum; 5E4E; -.
DR PDBsum; 6OEL; -.
DR PDBsum; 6WGL; -.
DR AlphaFoldDB; P24394; -.
DR SMR; P24394; -.
DR BioGRID; 109780; 54.
DR CORUM; P24394; -.
DR DIP; DIP-3223N; -.
DR ELM; P24394; -.
DR IntAct; P24394; 34.
DR MINT; P24394; -.
DR STRING; 9606.ENSP00000379111; -.
DR ChEMBL; CHEMBL3580490; -.
DR DrugBank; DB05078; AER001.
DR DrugBank; DB12159; Dupilumab.
DR DrugCentral; P24394; -.
DR GuidetoPHARMACOLOGY; 1697; -.
DR TCDB; 8.A.152.1.9; the interleukin receptor (ilr) family.
DR GlyConnect; 2053; 1 N-Linked glycan (1 site).
DR GlyGen; P24394; 6 sites, 2 N-linked glycans (1 site).
DR iPTMnet; P24394; -.
DR PhosphoSitePlus; P24394; -.
DR BioMuta; IL4R; -.
DR DMDM; 124335; -.
DR EPD; P24394; -.
DR jPOST; P24394; -.
DR MassIVE; P24394; -.
DR PaxDb; P24394; -.
DR PeptideAtlas; P24394; -.
DR PRIDE; P24394; -.
DR ProteomicsDB; 54203; -. [P24394-1]
DR ProteomicsDB; 54204; -. [P24394-2]
DR ProteomicsDB; 5656; -.
DR ABCD; P24394; 48 sequenced antibodies.
DR Antibodypedia; 3843; 654 antibodies from 40 providers.
DR DNASU; 3566; -.
DR Ensembl; ENST00000170630.6; ENSP00000170630.3; ENSG00000077238.14. [P24394-3]
DR Ensembl; ENST00000395762.7; ENSP00000379111.2; ENSG00000077238.14. [P24394-1]
DR Ensembl; ENST00000543915.6; ENSP00000441667.2; ENSG00000077238.14. [P24394-1]
DR GeneID; 3566; -.
DR KEGG; hsa:3566; -.
DR MANE-Select; ENST00000395762.7; ENSP00000379111.2; NM_000418.4; NP_000409.1.
DR UCSC; uc002don.5; human. [P24394-1]
DR CTD; 3566; -.
DR DisGeNET; 3566; -.
DR GeneCards; IL4R; -.
DR HGNC; HGNC:6015; IL4R.
DR HPA; ENSG00000077238; Low tissue specificity.
DR MalaCards; IL4R; -.
DR MIM; 147781; gene.
DR neXtProt; NX_P24394; -.
DR OpenTargets; ENSG00000077238; -.
DR PharmGKB; PA29832; -.
DR VEuPathDB; HostDB:ENSG00000077238; -.
DR eggNOG; ENOG502S3Y8; Eukaryota.
DR GeneTree; ENSGT00510000049182; -.
DR HOGENOM; CLU_020561_0_0_1; -.
DR InParanoid; P24394; -.
DR OMA; GYKPFQN; -.
DR PhylomeDB; P24394; -.
DR TreeFam; TF337996; -.
DR PathwayCommons; P24394; -.
DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
DR SignaLink; P24394; -.
DR SIGNOR; P24394; -.
DR BioGRID-ORCS; 3566; 6 hits in 1072 CRISPR screens.
DR ChiTaRS; IL4R; human.
DR EvolutionaryTrace; P24394; -.
DR GeneWiki; Interleukin-4_receptor; -.
DR GenomeRNAi; 3566; -.
DR Pharos; P24394; Tclin.
DR PRO; PR:P24394; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P24394; protein.
DR Bgee; ENSG00000077238; Expressed in granulocyte and 157 other tissues.
DR ExpressionAtlas; P24394; baseline and differential.
DR Genevisible; P24394; HS.
DR GO; GO:0034451; C:centriolar satellite; IDA:HPA.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0043235; C:receptor complex; IDA:MGI.
DR GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central.
DR GO; GO:0004913; F:interleukin-4 receptor activity; TAS:ProtInc.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0042832; P:defense response to protozoan; IEA:Ensembl.
DR GO; GO:0006955; P:immune response; TAS:ProtInc.
DR GO; GO:0016064; P:immunoglobulin mediated immune response; IBA:GO_Central.
DR GO; GO:0045626; P:negative regulation of T-helper 1 cell differentiation; IEA:Ensembl.
DR GO; GO:0030728; P:ovulation; IEA:Ensembl.
DR GO; GO:0032722; P:positive regulation of chemokine production; IEA:Ensembl.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0002639; P:positive regulation of immunoglobulin production; IEA:Ensembl.
DR GO; GO:0043032; P:positive regulation of macrophage activation; IEA:Ensembl.
DR GO; GO:0043306; P:positive regulation of mast cell degranulation; IEA:Ensembl.
DR GO; GO:1901741; P:positive regulation of myoblast fusion; IEA:Ensembl.
DR GO; GO:0045630; P:positive regulation of T-helper 2 cell differentiation; IEA:Ensembl.
DR GO; GO:0002532; P:production of molecular mediator involved in inflammatory response; IEA:InterPro.
DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
DR GO; GO:1990834; P:response to odorant; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0045063; P:T-helper 1 cell differentiation; IEA:Ensembl.
DR GO; GO:0045064; P:T-helper 2 cell differentiation; IEA:Ensembl.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR IDEAL; IID00653; -.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR003531; Hempt_rcpt_S_F1_CS.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR015319; IL-4_rcpt-alpha_N.
DR Pfam; PF09238; IL4Ra_N; 1.
DR SUPFAM; SSF49265; SSF49265; 2.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS01355; HEMATOPO_REC_S_F1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Disulfide bond;
KW Glycoprotein; Immunity; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000250"
FT CHAIN 26..825
FT /note="Interleukin-4 receptor subunit alpha"
FT /id="PRO_0000010887"
FT CHAIN 26..?
FT /note="Soluble interleukin-4 receptor subunit alpha"
FT /id="PRO_0000010888"
FT TOPO_DOM 26..232
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 233..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 257..825
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 125..224
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 373..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..557
FT /note="Required for IRS1 activation and IL4-induced cell
FT growth"
FT REGION 558..657
FT /note="Required for IL4-induced gene expression"
FT REGION 651..703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 782..809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 212..216
FT /note="WSXWS motif"
FT MOTIF 262..270
FT /note="Box 1 motif"
FT MOTIF 711..716
FT /note="ITIM motif"
FT COMPBIAS 381..397
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..809
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 38
FT /note="Major IL4 binding determinant"
FT SITE 64
FT /note="Minor IL4 binding determinant"
FT SITE 66
FT /note="Minor IL4 binding determinant"
FT SITE 92
FT /note="Minor IL4 binding determinant"
FT SITE 94
FT /note="Minor IL4 binding determinant"
FT SITE 97
FT /note="Major IL4 binding determinant"
FT SITE 152
FT /note="Minor IL4 binding determinant"
FT SITE 208
FT /note="Major IL4 binding determinant"
FT MOD_RES 497
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:8124718"
FT MOD_RES 575
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000305|PubMed:8624803"
FT MOD_RES 603
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000305|PubMed:8624803"
FT MOD_RES 631
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000305|PubMed:8624803"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 34..44
FT /evidence="ECO:0000250"
FT DISULFID 74..86
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..23
FT /note="MGWLCSGLLFPVSCLVLLQVASS -> MQKDARRE (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_053738"
FT VAR_SEQ 225..227
FT /note="YRE -> NIC (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_011116"
FT VAR_SEQ 228..825
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_011117"
FT VARIANT 75
FT /note="I -> F (in dbSNP:rs1805010)"
FT /id="VAR_059302"
FT VARIANT 75
FT /note="I -> L (in dbSNP:rs1805010)"
FT /id="VAR_059303"
FT VARIANT 75
FT /note="I -> V (associated with atopic asthma and cedar
FT pollen sensitization; dbSNP:rs1805010)"
FT /evidence="ECO:0000269|PubMed:10390422,
FT ECO:0000269|PubMed:14657871, ECO:0000269|PubMed:9070874,
FT ECO:0000269|PubMed:9620765, ECO:0000269|Ref.5"
FT /id="VAR_008034"
FT VARIANT 387
FT /note="S -> L (in dbSNP:rs6413500)"
FT /id="VAR_019999"
FT VARIANT 400
FT /note="E -> A (associated with cedar pollen sensitization;
FT dbSNP:rs1805011)"
FT /evidence="ECO:0000269|PubMed:11285129,
FT ECO:0000269|PubMed:14657871, ECO:0000269|PubMed:9070874,
FT ECO:0000269|Ref.5"
FT /id="VAR_011657"
FT VARIANT 431
FT /note="C -> R (in dbSNP:rs1805012)"
FT /evidence="ECO:0000269|PubMed:11285129,
FT ECO:0000269|PubMed:9070874, ECO:0000269|Ref.5"
FT /id="VAR_011658"
FT VARIANT 436
FT /note="S -> L (in dbSNP:rs1805013)"
FT /evidence="ECO:0000269|PubMed:11285129,
FT ECO:0000269|PubMed:9070874, ECO:0000269|Ref.5"
FT /id="VAR_011659"
FT VARIANT 492
FT /note="A -> T (in dbSNP:rs35606110)"
FT /id="VAR_049164"
FT VARIANT 492
FT /note="A -> V (in dbSNP:rs34727572)"
FT /id="VAR_049165"
FT VARIANT 503
FT /note="S -> P (lowered total IgE concentration;
FT dbSNP:rs1805015)"
FT /evidence="ECO:0000269|PubMed:10233717,
FT ECO:0000269|PubMed:11285129, ECO:0000269|Ref.5"
FT /id="VAR_011660"
FT VARIANT 576
FT /note="Q -> R (associated with atopic dermatitis; lowered
FT total IgE concentration; no effect on IL4-induced signal
FT transduction; dbSNP:rs1801275)"
FT /evidence="ECO:0000269|PubMed:10201973,
FT ECO:0000269|PubMed:10233717, ECO:0000269|PubMed:10809862,
FT ECO:0000269|PubMed:11285129, ECO:0000269|PubMed:9392697,
FT ECO:0000269|Ref.5"
FT /id="VAR_008035"
FT VARIANT 579
FT /note="V -> I (in dbSNP:rs3024677)"
FT /evidence="ECO:0000269|PubMed:11285129, ECO:0000269|Ref.5"
FT /id="VAR_011661"
FT VARIANT 675
FT /note="P -> S (in dbSNP:rs3024678)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_020000"
FT VARIANT 752
FT /note="S -> A (in dbSNP:rs1805016)"
FT /evidence="ECO:0000269|PubMed:10677312, ECO:0000269|Ref.5"
FT /id="VAR_011662"
FT VARIANT 786
FT /note="S -> P (in 1.8% of the population; dbSNP:rs1805014)"
FT /evidence="ECO:0000269|PubMed:11513543,
FT ECO:0000269|PubMed:9070874"
FT /id="VAR_011663"
FT MUTAGEN 38
FT /note="Y->A: 700-fold reduction in IL4 binding."
FT /evidence="ECO:0000269|PubMed:11786020"
FT MUTAGEN 38
FT /note="Y->F: 25-fold reduction in IL4 binding."
FT /evidence="ECO:0000269|PubMed:11786020"
FT MUTAGEN 39
FT /note="M->A: No effect on IL4 binding."
FT /evidence="ECO:0000269|PubMed:11786020"
FT MUTAGEN 40
FT /note="S->A: No effect on IL4 binding."
FT /evidence="ECO:0000269|PubMed:11786020"
FT MUTAGEN 64
FT /note="L->A: 100-fold reduction in IL4 binding."
FT /evidence="ECO:0000269|PubMed:11786020"
FT MUTAGEN 66
FT /note="F->A: 45-fold reduction in IL4 binding."
FT /evidence="ECO:0000269|PubMed:11786020"
FT MUTAGEN 67
FT /note="L->A: No effect on IL4 binding."
FT /evidence="ECO:0000269|PubMed:11786020"
FT MUTAGEN 68
FT /note="L->A: No effect on IL4 binding."
FT /evidence="ECO:0000269|PubMed:11786020"
FT MUTAGEN 91
FT /note="D->A: Little effect on IL4 binding."
FT /evidence="ECO:0000269|PubMed:11786020"
FT MUTAGEN 92
FT /note="D->A: 50-fold reduction in IL4 binding."
FT /evidence="ECO:0000269|PubMed:11786020"
FT MUTAGEN 93
FT /note="V->A: Little effect on IL4 binding."
FT /evidence="ECO:0000269|PubMed:11786020"
FT MUTAGEN 94
FT /note="V->A: 35-fold reduction in IL4 binding."
FT /evidence="ECO:0000269|PubMed:11786020"
FT MUTAGEN 95
FT /note="S->A: No effect on IL4 binding."
FT /evidence="ECO:0000269|PubMed:11786020"
FT MUTAGEN 97
FT /note="D->A,N: >150-fold reduction in IL4 binding."
FT /evidence="ECO:0000269|PubMed:11786020"
FT MUTAGEN 98
FT /note="N->A: No effect on IL4 binding."
FT /evidence="ECO:0000269|PubMed:11786020"
FT MUTAGEN 99
FT /note="Y->A: 10-fold reduction in IL4 binding."
FT /evidence="ECO:0000269|PubMed:11786020"
FT MUTAGEN 116
FT /note="K->A: Little effect on IL4 binding."
FT /evidence="ECO:0000269|PubMed:11786020"
FT MUTAGEN 117
FT /note="P->A: Little effect on IL4 binding."
FT /evidence="ECO:0000269|PubMed:11786020"
FT MUTAGEN 118
FT /note="S->A: No effect on IL4 binding."
FT /evidence="ECO:0000269|PubMed:11786020"
FT MUTAGEN 119
FT /note="E->A: No effect on IL4 binding."
FT /evidence="ECO:0000269|PubMed:11786020"
FT MUTAGEN 150
FT /note="D->A: Little effect on IL4 binding."
FT /evidence="ECO:0000269|PubMed:11786020"
FT MUTAGEN 151
FT /note="N->A: Little effect on IL4 binding."
FT /evidence="ECO:0000269|PubMed:11786020"
FT MUTAGEN 152
FT /note="Y->A: 40-fold reduction in IL4 binding."
FT /evidence="ECO:0000269|PubMed:11786020"
FT MUTAGEN 152
FT /note="Y->F: No effect on IL4 binding."
FT /evidence="ECO:0000269|PubMed:11786020"
FT MUTAGEN 153
FT /note="L->A: Little effect on IL4 binding."
FT /evidence="ECO:0000269|PubMed:11786020"
FT MUTAGEN 154
FT /note="Y->A: Little effect on IL4 binding."
FT /evidence="ECO:0000269|PubMed:11786020"
FT MUTAGEN 208
FT /note="Y->A: 500-fold reduction in IL4 binding."
FT /evidence="ECO:0000269|PubMed:11786020"
FT MUTAGEN 208
FT /note="Y->F: 200-fold reduction in IL4 binding."
FT /evidence="ECO:0000269|PubMed:11786020"
FT MUTAGEN 497
FT /note="Y->F: Abolishes IRS1 tyrosine phosphorylation. No
FT cell proliferation."
FT /evidence="ECO:0000269|PubMed:8124718"
FT MUTAGEN 575
FT /note="Y->F: Loss of CD23 gene induction; when associated
FT with F-603 and F-631."
FT /evidence="ECO:0000269|PubMed:10201973,
FT ECO:0000269|PubMed:8624803"
FT MUTAGEN 603
FT /note="Y->F: Loss of CD23 gene induction; when associated
FT with F-575 and F-631."
FT /evidence="ECO:0000269|PubMed:8624803"
FT MUTAGEN 631
FT /note="Y->F: Loss of CD23 gene induction; when associated
FT with F-575 and F-603."
FT /evidence="ECO:0000269|PubMed:8624803"
FT MUTAGEN 713
FT /note="Y->F: Increased IL4-induced cell proliferation and
FT STAT6 activation."
FT /evidence="ECO:0000269|PubMed:11714803"
FT STRAND 28..36
FT /evidence="ECO:0007829|PDB:1IAR"
FT STRAND 38..50
FT /evidence="ECO:0007829|PDB:1IAR"
FT HELIX 54..57
FT /evidence="ECO:0007829|PDB:1IAR"
FT STRAND 58..68
FT /evidence="ECO:0007829|PDB:1IAR"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:1IAR"
FT STRAND 77..89
FT /evidence="ECO:0007829|PDB:1IAR"
FT STRAND 99..105
FT /evidence="ECO:0007829|PDB:1IAR"
FT STRAND 108..115
FT /evidence="ECO:0007829|PDB:1IAR"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:1IAR"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:1IAR"
FT TURN 135..137
FT /evidence="ECO:0007829|PDB:3BPO"
FT STRAND 139..144
FT /evidence="ECO:0007829|PDB:1IAR"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:1IAR"
FT STRAND 158..168
FT /evidence="ECO:0007829|PDB:1IAR"
FT STRAND 172..177
FT /evidence="ECO:0007829|PDB:1IAR"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:6WGL"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:1IAR"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:3BPL"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:3BPO"
FT STRAND 197..204
FT /evidence="ECO:0007829|PDB:1IAR"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:1IAR"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:1IAR"
FT HELIX 495..497
FT /evidence="ECO:0007829|PDB:1IRS"
SQ 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
