IL13_HUMAN
ID IL13_HUMAN Reviewed; 146 AA.
AC P35225; O43644; Q4VB52; Q9UDC7;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=Interleukin-13;
DE Short=IL-13;
DE Flags: Precursor;
GN Name=IL13; Synonyms=NC30;
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], AND FUNCTION.
RX PubMed=8096327; DOI=10.1038/362248a0;
RA Minty A.J., Chalon P., Derocq J.-M., Dumont X., Guillemot J.-C., Kaghad M.,
RA Labit C., Leplatois P., Liauzun P., Miloux B., Minty C., Casellas P.,
RA Loison G., Lupker J., Shire D., Ferrara P., Caput D.;
RT "Interleukin-13 is a new human lymphokine regulating inflammatory and
RT immune responses.";
RL Nature 362:248-250(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8097324; DOI=10.1073/pnas.90.8.3735;
RA McKenzie A.N., Culpepper J.A., Waal Malefyt R., Briere F., Punnonen J.,
RA Aversa G., Sato A., Dang W., Cocks B.G., Menon S., de Vries J.E.,
RA Banchereau J., Zurawski G.R.;
RT "Interleukin 13, a T-cell-derived cytokine that regulates human monocyte
RT and B-cell function.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:3735-3739(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Blood;
RX PubMed=7721105; DOI=10.1016/0378-1119(94)00720-d;
RA Smirnov D.V., Smirnova M.G., Korobko V.G., Frolova E.I.;
RT "Tandem arrangement of human genes for interleukin-4 and interleukin-13:
RT resemblance in their organization.";
RL Gene 155:277-281(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8605348;
RA Dolganov G., Bort S., Lovett M., Burr J., Schubert L., Short D., McGurn M.,
RA Gibson C., Lewis D.B.;
RT "Coexpression of the interleukin-13 and interleukin-4 genes correlates with
RT their physical linkage in the cytokine gene cluster on human chromosome
RT 5q23-31.";
RL Blood 87:3316-3326(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLN-144.
RG SeattleSNPs variation discovery resource;
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLN-144.
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-144.
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 14-146.
RA Jang J.S., Kim B.E.;
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 15-63.
RC TISSUE=Peripheral blood lymphocyte;
RX PubMed=1408833; DOI=10.1093/nar/20.19.5173;
RA Morgan J.G., Dolganov G.M., Robbins S.E., Hinton L.M., Lovett M.;
RT "The selective isolation of novel cDNAs encoded by the regions surrounding
RT the human interleukin 4 and 5 genes.";
RL Nucleic Acids Res. 20:5173-5179(1992).
RN [10]
RP FUNCTION.
RX PubMed=7903680; DOI=10.1084/jem.179.1.135;
RA Defrance T., Carayon P., Billian G., Guillemot J.C., Minty A., Caput D.,
RA Ferrara P.;
RT "Interleukin 13 is a B cell stimulating factor.";
RL J. Exp. Med. 179:135-143(1994).
RN [11]
RP FUNCTION.
RX PubMed=8759755;
RA Luttmann W., Knoechel B., Foerster M., Matthys H., Virchow J.C. Jr.,
RA Kroegel C.;
RT "Activation of human eosinophils by IL-13. Induction of CD69 surface
RT antigen, its relationship to messenger RNA expression, and promotion of
RT cellular viability.";
RL J. Immunol. 157:1678-1683(1996).
RN [12]
RP FUNCTION.
RX PubMed=9013879; DOI=10.1016/s0014-5793(96)01462-7;
RA Miloux B., Laurent P., Bonnin O., Lupker J., Caput D., Vita N., Ferrara P.;
RT "Cloning of the human IL-13R alpha1 chain and reconstitution with the IL4R
RT alpha of a functional IL-4/IL-13 receptor complex.";
RL FEBS Lett. 401:163-166(1997).
RN [13]
RP FUNCTION.
RX PubMed=8639787;
RA Schnyder B., Lugli S., Feng N., Etter H., Lutz R.A., Ryffel B.,
RA Sugamura K., Wunderli-Allenspach H., Moser R.;
RT "Interleukin-4 (IL-4) and IL-13 bind to a shared heterodimeric complex on
RT endothelial cells mediating vascular cell adhesion molecule-1 induction in
RT the absence of the common gamma chain.";
RL Blood 87:4286-4295(1996).
RN [14]
RP FUNCTION.
RX PubMed=21622864; DOI=10.4049/jimmunol.1100467;
RA Kasaian M.T., Raible D., Marquette K., Cook T.A., Zhou S., Tan X.Y.,
RA Tchistiakova L.;
RT "IL-13 antibodies influence IL-13 clearance in humans by modulating
RT scavenger activity of IL-13Ralpha2.";
RL J. Immunol. 187:561-569(2011).
RN [15]
RP STRUCTURE BY NMR OF 35-146, AND DISULFIDE BONDS.
RX PubMed=11419948; DOI=10.1006/jmbi.2001.4764;
RA Moy F.J., Diblasio E., Wilhelm J., Powers R.;
RT "Solution structure of human IL-13 and implication for receptor binding.";
RL J. Mol. Biol. 310:219-230(2001).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF 15-146 IN COMPLEX WITH IL13RA2,
RP AND DISULFIDE BONDS.
RX PubMed=20223216; DOI=10.1016/j.str.2010.01.003;
RA Lupardus P.J., Birnbaum M.E., Garcia K.C.;
RT "Molecular basis for shared cytokine recognition revealed in the structure
RT of an unusually high affinity complex between IL-13 and IL-13Ralpha2.";
RL Structure 18:332-342(2010).
RN [17]
RP VARIANT GLN-144.
RX PubMed=10699178; DOI=10.1093/hmg/9.4.549;
RA Heinzmann A., Mao X.-Q., Akaiwa M., Kreomer R.T., Gao P.-S., Ohshima K.,
RA Umeshita R., Abe Y., Braun S., Yamashita T., Roberts M.H., Sugimoto R.,
RA Arima K., Arinobu Y., Yu B., Kruse S., Enomoto T., Dake Y., Kawai M.,
RA Shimazu S., Sasaki S., Adra C.N., Kitaichi M., Inoue H., Yamauchi K.,
RA Tomichi N., Kurimoto F., Hamasaki N., Hopkin J.M., Izuhara K.,
RA Shirakawa T., Deichmann K.A.;
RT "Genetic variants of IL-13 signalling and human asthma and atopy.";
RL Hum. Mol. Genet. 9:549-559(2000).
RN [18]
RP VARIANT GLN-144.
RX PubMed=11588017; DOI=10.1165/ajrcmb.25.3.4483;
RA Howard T.D., Whittaker P.A., Zaiman A.L., Koppelman G.H., Xu J.,
RA Hanley M.T., Meyers D.A., Postma D.S., Bleecker E.R.;
RT "Identification and association of polymorphisms in the interleukin-13 gene
RT with asthma and atopy in a Dutch population.";
RL Am. J. Respir. Cell Mol. Biol. 25:377-384(2001).
RN [19]
RP VARIANT GLN-144.
RX PubMed=12928861; DOI=10.1007/s00439-003-1001-x;
RA Wang M., Xing Z.-M., Lu C., Ma Y.-X., Yu D.-L., Yan Z., Wang S.-W.,
RA Yu L.-S.;
RT "A common IL-13 Arg130Gln single nucleotide polymorphism among Chinese
RT atopy patients with allergic rhinitis.";
RL Hum. Genet. 113:387-390(2003).
CC -!- FUNCTION: Cytokine that plays important roles in allergic inflammation
CC and immune response to parasite infection (PubMed:8096327,
CC PubMed:8097324). Synergizes with IL2 in regulating interferon-gamma
CC synthesis (PubMed:8096327). Stimulates B-cell proliferation, and
CC activation of eosinophils, basophils, and mast cells (PubMed:7903680,
CC PubMed:8759755). Plays an important role in controlling IL33 activity
CC by modulating the production of transmembrane and soluble forms of
CC interleukin-1 receptor-like 1/IL1RL1 (By similarity). Displays the
CC capacity to antagonize Th1-driven proinflammatory immune response and
CC downregulates synthesis of many proinflammatory cytokines including
CC IL1, IL6, IL10, IL12 and TNF-alpha through a mechanism that partially
CC involves suppression of NF-kappa-B (By similarity). Functions also on
CC nonhematopoietic cells, including endothelial cells where it induces
CC vascular cell adhesion protein 1/VCAM1, which is important in the
CC recruitment of eosinophils (PubMed:8639787). Exerts its biological
CC effects through its receptors which comprises the IL4R chain and the
CC IL13RA1 chain, to activate JAK1 and TYK2, leading to the activation of
CC STAT6 (PubMed:9013879). Aside from IL13RA1, another receptor IL13RA2
CC acts as a high affinity decoy for IL13 and mediates internalization and
CC depletion of extracellular IL13 (PubMed:21622864).
CC {ECO:0000250|UniProtKB:P20109, ECO:0000250|UniProtKB:P42203,
CC ECO:0000269|PubMed:21622864, ECO:0000269|PubMed:7903680,
CC ECO:0000269|PubMed:8096327, ECO:0000269|PubMed:8097324,
CC ECO:0000269|PubMed:8639787, ECO:0000269|PubMed:8759755,
CC ECO:0000269|PubMed:9013879}.
CC -!- SUBUNIT: Interacts with IL13RA2. {ECO:0000269|PubMed:20223216}.
CC -!- INTERACTION:
CC P35225; P78552: IL13RA1; NbExp=6; IntAct=EBI-1647828, EBI-1391535;
CC P35225; Q14627: IL13RA2; NbExp=9; IntAct=EBI-1647828, EBI-4320063;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- DISEASE: Allergic rhinitis (ALRH) [MIM:607154]: A common disease with
CC complex inheritance characterized by mucosal inflammation caused by
CC allergen exposure. Note=Disease susceptibility is associated with
CC variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the IL-4/IL-13 family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-15 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA36107.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAA83738.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAB01681.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAC03535.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAK53823.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA48824.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Interleukin-13 entry;
CC URL="https://en.wikipedia.org/wiki/Interleukin_13";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/il13/";
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DR EMBL; X69079; CAA48823.1; -; mRNA.
DR EMBL; X69079; CAA48824.1; ALT_INIT; mRNA.
DR EMBL; L06801; AAA36107.1; ALT_INIT; mRNA.
DR EMBL; U10307; AAA83738.1; ALT_INIT; Genomic_DNA.
DR EMBL; U31120; AAB01681.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF377331; AAK53823.1; ALT_INIT; Genomic_DNA.
DR EMBL; AC004039; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC096139; AAH96139.1; -; mRNA.
DR EMBL; AF043334; AAC03535.1; ALT_INIT; mRNA.
DR CCDS; CCDS4157.1; -.
DR PIR; I38060; A47481.
DR RefSeq; NP_002179.2; NM_002188.2.
DR PDB; 1GA3; NMR; -; A=35-146.
DR PDB; 1IJZ; NMR; -; A=35-146.
DR PDB; 1IK0; NMR; -; A=35-146.
DR PDB; 3BPO; X-ray; 3.00 A; A=34-146.
DR PDB; 3G6D; X-ray; 3.20 A; A=35-146.
DR PDB; 3L5W; X-ray; 2.00 A; I/J=35-146.
DR PDB; 3L5X; X-ray; 1.90 A; A=35-146.
DR PDB; 3LB6; X-ray; 3.05 A; A/B=15-146.
DR PDB; 4I77; X-ray; 1.90 A; Z=35-146.
DR PDB; 4PS4; X-ray; 2.80 A; A=35-146.
DR PDB; 5E4E; X-ray; 3.00 A; A=34-146.
DR PDB; 5L6Y; X-ray; 1.99 A; C=35-146.
DR PDBsum; 1GA3; -.
DR PDBsum; 1IJZ; -.
DR PDBsum; 1IK0; -.
DR PDBsum; 3BPO; -.
DR PDBsum; 3G6D; -.
DR PDBsum; 3L5W; -.
DR PDBsum; 3L5X; -.
DR PDBsum; 3LB6; -.
DR PDBsum; 4I77; -.
DR PDBsum; 4PS4; -.
DR PDBsum; 5E4E; -.
DR PDBsum; 5L6Y; -.
DR AlphaFoldDB; P35225; -.
DR BMRB; P35225; -.
DR SMR; P35225; -.
DR BioGRID; 109810; 14.
DR DIP; DIP-3224N; -.
DR IntAct; P35225; 4.
DR STRING; 9606.ENSP00000304915; -.
DR ChEMBL; CHEMBL3580486; -.
DR DrugBank; DB05305; Cintredekin besudotox.
DR DrugBank; DB11914; Lebrikizumab.
DR DrugBank; DB12169; Tralokinumab.
DR GlyGen; P35225; 4 sites.
DR BioMuta; IL13; -.
DR DMDM; 239938644; -.
DR MassIVE; P35225; -.
DR PaxDb; P35225; -.
DR PeptideAtlas; P35225; -.
DR PRIDE; P35225; -.
DR ABCD; P35225; 77 sequenced antibodies.
DR Antibodypedia; 14499; 1206 antibodies from 43 providers.
DR DNASU; 3596; -.
DR Ensembl; ENST00000304506.7; ENSP00000304915.3; ENSG00000169194.10.
DR GeneID; 3596; -.
DR KEGG; hsa:3596; -.
DR UCSC; uc003kxj.2; human.
DR CTD; 3596; -.
DR DisGeNET; 3596; -.
DR GeneCards; IL13; -.
DR HGNC; HGNC:5973; IL13.
DR HPA; ENSG00000169194; Tissue enriched (testis).
DR MalaCards; IL13; -.
DR MIM; 147683; gene.
DR MIM; 607154; phenotype.
DR neXtProt; NX_P35225; -.
DR PharmGKB; PA199; -.
DR VEuPathDB; HostDB:ENSG00000169194; -.
DR eggNOG; ENOG502SZKX; Eukaryota.
DR InParanoid; P35225; -.
DR OrthoDB; 1578920at2759; -.
DR PhylomeDB; P35225; -.
DR TreeFam; TF336383; -.
DR PathwayCommons; P35225; -.
DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
DR Reactome; R-HSA-9012546; Interleukin-18 signaling.
DR SignaLink; P35225; -.
DR SIGNOR; P35225; -.
DR BioGRID-ORCS; 3596; 7 hits in 1066 CRISPR screens.
DR ChiTaRS; IL13; human.
DR EvolutionaryTrace; P35225; -.
DR GeneWiki; Interleukin_13; -.
DR GenomeRNAi; 3596; -.
DR Pharos; P35225; Tbio.
DR PRO; PR:P35225; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P35225; protein.
DR Bgee; ENSG00000169194; Expressed in left testis and 114 other tissues.
DR ExpressionAtlas; P35225; baseline and differential.
DR Genevisible; P35225; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; IDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR GO; GO:0005144; F:interleukin-13 receptor binding; IEA:Ensembl.
DR GO; GO:0071345; P:cellular response to cytokine stimulus; IEA:Ensembl.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
DR GO; GO:0042116; P:macrophage activation; IGI:ARUK-UCL.
DR GO; GO:0001774; P:microglial cell activation; IEA:Ensembl.
DR GO; GO:1903660; P:negative regulation of complement-dependent cytotoxicity; IMP:AgBase.
DR GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; IMP:AgBase.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IGI:ARUK-UCL.
DR GO; GO:1901247; P:negative regulation of lung ciliated cell differentiation; NAS:BHF-UCL.
DR GO; GO:0033861; P:negative regulation of NAD(P)H oxidase activity; IEA:Ensembl.
DR GO; GO:1901215; P:negative regulation of neuron death; IEA:Ensembl.
DR GO; GO:0071635; P:negative regulation of transforming growth factor beta production; IEA:Ensembl.
DR GO; GO:0030890; P:positive regulation of B cell proliferation; IEA:Ensembl.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0032723; P:positive regulation of connective tissue growth factor production; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IGI:ARUK-UCL.
DR GO; GO:0002639; P:positive regulation of immunoglobulin production; IEA:Ensembl.
DR GO; GO:0032733; P:positive regulation of interleukin-10 production; IGI:ARUK-UCL.
DR GO; GO:1901251; P:positive regulation of lung goblet cell differentiation; NAS:BHF-UCL.
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:2000231; P:positive regulation of pancreatic stellate cell proliferation; IEA:Ensembl.
DR GO; GO:0050714; P:positive regulation of protein secretion; IEA:Ensembl.
DR GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; IEA:Ensembl.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IEA:Ensembl.
DR GO; GO:0010155; P:regulation of proton transport; IEA:Ensembl.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0035094; P:response to nicotine; IEA:Ensembl.
DR Gene3D; 1.20.1250.10; -; 1.
DR InterPro; IPR009079; 4_helix_cytokine-like_core.
DR InterPro; IPR020470; IL-13.
DR InterPro; IPR001325; IL-4/IL-13.
DR InterPro; IPR018096; IL-4/IL-13_CS.
DR Pfam; PF03487; IL13; 1.
DR PRINTS; PR01929; INTRLEUKIN13.
DR SMART; SM00190; IL4_13; 1.
DR SUPFAM; SSF47266; SSF47266; 1.
DR PROSITE; PS00838; INTERLEUKIN_4_13; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytokine; Disulfide bond; Glycoprotein; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..146
FT /note="Interleukin-13"
FT /id="PRO_0000015547"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 62..90
FT /evidence="ECO:0000269|PubMed:11419948,
FT ECO:0000269|PubMed:20223216"
FT DISULFID 78..104
FT /evidence="ECO:0000269|PubMed:11419948,
FT ECO:0000269|PubMed:20223216"
FT VARIANT 144
FT /note="R -> Q (associated with increased risk for asthma
FT development; at homozygosity associated with higher levels
FT of serum total IgE in some allergic rhinitis patients;
FT dbSNP:rs20541)"
FT /evidence="ECO:0000269|PubMed:10699178,
FT ECO:0000269|PubMed:11588017, ECO:0000269|PubMed:12928861,
FT ECO:0000269|PubMed:15372022, ECO:0000269|PubMed:15489334,
FT ECO:0000269|Ref.5"
FT /id="VAR_010037"
FT CONFLICT 1
FT /note="M -> R (in Ref. 2; CAA48824)"
FT /evidence="ECO:0000305"
FT CONFLICT 26
FT /note="T -> A (in Ref. 9; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 32
FT /note="A -> D (in Ref. 9; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 51
FT /note="V -> S (in Ref. 9; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="N -> T (in Ref. 9; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="A -> R (in Ref. 3; AAA83738)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="S -> G (in Ref. 8; AAC03535)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="Missing (in Ref. 3; AAA83738)"
FT /evidence="ECO:0000305"
FT HELIX 41..54
FT /evidence="ECO:0007829|PDB:3L5X"
FT TURN 61..64
FT /evidence="ECO:0007829|PDB:3L5X"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:3L5X"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:3L5X"
FT HELIX 77..84
FT /evidence="ECO:0007829|PDB:3L5X"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:3L5X"
FT HELIX 94..103
FT /evidence="ECO:0007829|PDB:3L5X"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:3LB6"
FT HELIX 113..116
FT /evidence="ECO:0007829|PDB:5E4E"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:3L5X"
FT HELIX 125..142
FT /evidence="ECO:0007829|PDB:3L5X"
SQ SEQUENCE 146 AA; 15816 MW; BE2D46CCF913D129 CRC64;
MHPLLNPLLL ALGLMALLLT TVIALTCLGG FASPGPVPPS TALRELIEEL VNITQNQKAP
LCNGSMVWSI NLTAGMYCAA LESLINVSGC SAIEKTQRML SGFCPHKVSA GQFSSLHVRD
TKIEVAQFVK DLLLHLKKLF REGRFN
