IL4RA_MOUSE
ID IL4RA_MOUSE Reviewed; 810 AA.
AC P16382; O54690; Q60583; Q8CBW5;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 201.
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;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), AND PROTEIN SEQUENCE OF
RP 26-39; 162-179 AND 194-210.
RC STRAIN=C57BL/6J; TISSUE=T-cell;
RX PubMed=2805066; DOI=10.1016/0092-8674(89)90295-x;
RA Mosley B., Beckmann M.P., March C.J., Idzerda R.L., Gimpel S.D.,
RA VandenBos T., Friend D., Alpert A., Anderson D., Jackson J., Wignall J.M.,
RA Smith C., Gallis B., Sims J.E., Urdal D., Widmer M.B., Cosman D.,
RA Park L.S.;
RT "The murine interleukin-4 receptor: molecular cloning and characterization
RT of secreted and membrane bound forms.";
RL Cell 59:335-348(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Mast cell;
RX PubMed=2405398; DOI=10.1073/pnas.87.3.857;
RA Harada N., Castle B.E., Gorman D.M., Itoh N., Schreurs J., Barrett R.L.,
RA Howard M., Miyajima A.;
RT "Expression cloning of a cDNA encoding the murine interleukin 4 receptor
RT based on ligand binding.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:857-861(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RC STRAIN=BALB/cJ; TISSUE=Sperm;
RX PubMed=1534014; DOI=10.3109/08977199209011014;
RA Wrighton N., Campbell L.A., Harada N., Miyajima A., Lee F.;
RT "The murine interleukin-4 receptor gene: genomic structure, expression and
RT potential for alternative splicing.";
RL Growth Factors 6:103-118(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND CHARACTERIZATION OF VARIANT
RP ILE-74.
RC STRAIN=AKR/J, BALB/cJ, C3H/HeN, C57BL/6J, CB-17/SCID, CBA/J, DBA/2J, FVB/N,
RC and SJL/J;
RX PubMed=9348299; DOI=10.1084/jem.186.9.1419;
RA Schulte T., Kurrle R., Roellinghoff M., Gessner A.;
RT "Molecular characterization and functional analysis of murine interleukin 4
RT receptor allotypes.";
RL J. Exp. Med. 186:1419-1429(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Diencephalon, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP INTERACTION WITH JAK1 AND SOCS5.
RX PubMed=12242343; DOI=10.1073/pnas.202477099;
RA Seki Y., Hayashi K., Matsumoto A., Seki N., Tsukada J., Ransom J., Naka T.,
RA Kishimoto T., Yoshimura A., Kubo M.;
RT "Expression of the suppressor of cytokine signaling-5 (SOCS5) negatively
RT regulates IL-4-dependent STAT6 activation and Th2 differentiation.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13003-13008(2002).
RN [7]
RP PHOSPHORYLATION, AND INTERACTION WITH PIK3C3.
RX PubMed=8390454; DOI=10.1016/s0021-9258(19)38624-7;
RA Izuhara K., Harada N.;
RT "Interleukin-4 (IL-4) induces protein tyrosine phosphorylation of the IL-4
RT receptor and association of phosphatidylinositol 3-kinase to the IL-4
RT receptor in a mouse T cell line, HT2.";
RL J. Biol. Chem. 268:13097-13102(1993).
RN [8]
RP PROTEOLYTIC PROCESSING.
RX PubMed=8757301;
RA Blum H., Wolf M., Enssle K., Roellinghoff M., Gessner A.;
RT "Two distinct stimulus-dependent pathways lead to production of soluble
RT murine interleukin-4 receptor.";
RL J. Immunol. 157:1846-1853(1996).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [10]
RP TISSUE SPECIFICITY, AND INTERACTION WITH CLM1.
RX PubMed=26124135; DOI=10.1073/pnas.1507625112;
RA Moshkovits I., Karo-Atar D., Itan M., Reichman H., Rozenberg P.,
RA Morgenstern-Ben-Baruch N., Shik D., Ejarque-Ortiz A., Hershko A.Y.,
RA Tian L., Coligan J.E., Sayos J., Munitz A.;
RT "CD300f associates with IL-4 receptor alpha and amplifies IL-4-induced
RT immune cell responses.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:8708-8713(2015).
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 -!- 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. Interacts
CC with the SH2-containing phosphatases, PTPN6/SHIP1, PTPN11/SHIP2 and
CC INPP5D/SHIP. Interacts with JAK3 (By similarity). Interacts with PIK3C3
CC (PubMed:8390454). Interacts with JAK1 through a Box 1-containing
CC region; inhibited by SOCS5 (PubMed:12242343). Interacts with SOCS5;
CC inhibits IL4 signaling (PubMed:12242343). Interacts with CLM1
CC (PubMed:26124135). {ECO:0000250|UniProtKB:P24394,
CC ECO:0000269|PubMed:12242343, ECO:0000269|PubMed:26124135,
CC ECO:0000269|PubMed:8390454}.
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;
CC IsoId=P16382-1; Sequence=Displayed;
CC Name=2; Synonyms=Secreted;
CC IsoId=P16382-2; Sequence=VSP_001675, VSP_001676;
CC Name=3;
CC IsoId=P16382-3; Sequence=VSP_001677;
CC -!- TISSUE SPECIFICITY: Expressed in both Th1 and Th2 cells.
CC -!- DOMAIN: The extracellular domain represents the IL4 binding protein
CC (IL4BP). {ECO:0000250}.
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 {ECO:0000250|UniProtKB:P24394}.
CC -!- PTM: Soluble IL4R can also be produced by proteolytic cleavage at the
CC cell surface (shedding). {ECO:0000269|PubMed:8757301}.
CC -!- MISCELLANEOUS: The sequences from strains C3H, CBA, DBA/2 and FVB/N are
CC all identical to the one displayed.
CC -!- MISCELLANEOUS: [Isoform 1]: Binds IL-4.
CC -!- MISCELLANEOUS: [Isoform 2]: Binds IL-4. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Lacks the cytoplasmic domain. Binds IL4.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 4
CC subfamily. {ECO:0000305}.
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DR EMBL; M27959; AAA39299.1; -; mRNA.
DR EMBL; M27960; AAA39300.1; -; mRNA.
DR EMBL; M29854; AAA39297.1; -; mRNA.
DR EMBL; M64879; AAB59727.1; -; Genomic_DNA.
DR EMBL; M64870; AAB59727.1; JOINED; Genomic_DNA.
DR EMBL; M64871; AAB59727.1; JOINED; Genomic_DNA.
DR EMBL; M64872; AAB59727.1; JOINED; Genomic_DNA.
DR EMBL; M64873; AAB59727.1; JOINED; Genomic_DNA.
DR EMBL; M64874; AAB59727.1; JOINED; Genomic_DNA.
DR EMBL; M64876; AAB59727.1; JOINED; Genomic_DNA.
DR EMBL; M64877; AAB59727.1; JOINED; Genomic_DNA.
DR EMBL; M64878; AAB59727.1; JOINED; Genomic_DNA.
DR EMBL; AF000304; AAB87750.1; -; mRNA.
DR EMBL; AK034466; BAC28718.1; -; mRNA.
DR EMBL; AK088086; BAC40137.1; -; mRNA.
DR CCDS; CCDS40121.1; -. [P16382-1]
DR PIR; A33380; A33380.
DR RefSeq; NP_001008700.1; NM_001008700.3. [P16382-1]
DR AlphaFoldDB; P16382; -.
DR SMR; P16382; -.
DR BioGRID; 200638; 3.
DR DIP; DIP-1168N; -.
DR STRING; 10090.ENSMUSP00000033004; -.
DR GlyGen; P16382; 4 sites.
DR iPTMnet; P16382; -.
DR PhosphoSitePlus; P16382; -.
DR EPD; P16382; -.
DR jPOST; P16382; -.
DR MaxQB; P16382; -.
DR PaxDb; P16382; -.
DR PRIDE; P16382; -.
DR ProteomicsDB; 267324; -. [P16382-1]
DR ProteomicsDB; 267325; -. [P16382-2]
DR ProteomicsDB; 267326; -. [P16382-3]
DR Antibodypedia; 3843; 654 antibodies from 40 providers.
DR DNASU; 16190; -.
DR Ensembl; ENSMUST00000033004; ENSMUSP00000033004; ENSMUSG00000030748. [P16382-1]
DR Ensembl; ENSMUST00000206846; ENSMUSP00000145824; ENSMUSG00000030748. [P16382-2]
DR GeneID; 16190; -.
DR KEGG; mmu:16190; -.
DR UCSC; uc009jqc.1; mouse. [P16382-1]
DR CTD; 16190; -.
DR MGI; MGI:105367; Il4ra.
DR VEuPathDB; HostDB:ENSMUSG00000030748; -.
DR eggNOG; ENOG502S3Y8; Eukaryota.
DR GeneTree; ENSGT00510000049182; -.
DR HOGENOM; CLU_020561_0_0_1; -.
DR InParanoid; P16382; -.
DR OMA; GYKPFQN; -.
DR PhylomeDB; P16382; -.
DR TreeFam; TF337996; -.
DR Reactome; R-MMU-6785807; Interleukin-4 and Interleukin-13 signaling.
DR BioGRID-ORCS; 16190; 4 hits in 76 CRISPR screens.
DR PRO; PR:P16382; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P16382; protein.
DR Bgee; ENSMUSG00000030748; Expressed in lumbar dorsal root ganglion and 165 other tissues.
DR ExpressionAtlas; P16382; baseline and differential.
DR Genevisible; P16382; MM.
DR GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0042832; P:defense response to protozoan; IMP:MGI.
DR GO; GO:0016064; P:immunoglobulin mediated immune response; IMP:MGI.
DR GO; GO:0045626; P:negative regulation of T-helper 1 cell differentiation; IGI:MGI.
DR GO; GO:0032722; P:positive regulation of chemokine production; IMP:BHF-UCL.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0002639; P:positive regulation of immunoglobulin production; IMP:MGI.
DR GO; GO:0043032; P:positive regulation of macrophage activation; IMP:BHF-UCL.
DR GO; GO:0043306; P:positive regulation of mast cell degranulation; IMP:MGI.
DR GO; GO:1901741; P:positive regulation of myoblast fusion; IMP:MGI.
DR GO; GO:0045630; P:positive regulation of T-helper 2 cell differentiation; IGI:MGI.
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; ISO:MGI.
DR GO; GO:0045063; P:T-helper 1 cell differentiation; IGI:MGI.
DR GO; GO:0045064; P:T-helper 2 cell differentiation; IGI:MGI.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.10; -; 2.
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 Alternative splicing; Cell membrane; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Immunity; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:2805066"
FT CHAIN 26..810
FT /note="Interleukin-4 receptor subunit alpha"
FT /id="PRO_0000010889"
FT CHAIN 26..?
FT /note="Soluble interleukin-4 receptor subunit alpha"
FT /id="PRO_0000010890"
FT TOPO_DOM 26..233
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 258..810
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 126..224
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 441..557
FT /note="Required for IRS1 activation and IL4-induced cell
FT growth"
FT /evidence="ECO:0000250"
FT REGION 460..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..653
FT /note="Required for IL4-induced gene expression"
FT /evidence="ECO:0000250"
FT REGION 586..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 766..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 213..217
FT /note="WSXWS motif"
FT MOTIF 263..271
FT /note="Box 1 motif"
FT MOTIF 707..712
FT /note="ITIM motif"
FT COMPBIAS 635..662
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 500
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P24394"
FT MOD_RES 575
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P24394"
FT MOD_RES 603
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P24394"
FT MOD_RES 631
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P24394"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 34..44
FT /evidence="ECO:0000250"
FT DISULFID 75..87
FT /evidence="ECO:0000250"
FT VAR_SEQ 225..230
FT /note="HFQLPL -> PSNENL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:2805066"
FT /id="VSP_001675"
FT VAR_SEQ 231..810
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:2805066"
FT /id="VSP_001676"
FT VAR_SEQ 258..810
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:2805066"
FT /id="VSP_001677"
FT VARIANT 59
FT /note="C -> R (in strain: BALB/c, AKR/J and SJL/J)"
FT VARIANT 74
FT /note="T -> I (in strain: BALB/c, AKR/J and SJL/J; reduced
FT IL4-neutralizing capacity of soluble form)"
FT /evidence="ECO:0000269|PubMed:9348299"
FT VARIANT 193
FT /note="M -> T (in strain: BALB/c, AKR/J and SJL/J)"
FT VARIANT 334
FT /note="L -> P (in strain: BALB/c, AKR/J and SJL/J)"
FT VARIANT 374
FT /note="N -> S (in strain: BALB/c, AKR/J and SJL/J)"
FT VARIANT 382
FT /note="I -> M (in strain: BALB/c, AKR/J and SJL/J)"
FT VARIANT 472
FT /note="G -> D (in strain: BALB/c, AKR/J and SJL/J)"
FT VARIANT 626
FT /note="D -> G (in strain: BALB/c, AKR/J and SJL/J)"
FT CONFLICT 436
FT /note="S -> C (in Ref. 5; BAC28718)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 810 AA; 87627 MW; 536B9E01E938FF6D CRC64;
MGRLCTKFLT SVGCLILLLV TGSGSIKVLG EPTCFSDYIR TSTCEWFLDS AVDCSSQLCL
HYRLMFFEFS ENLTCIPRNS ASTVCVCHME MNRPVQSDRY QMELWAEHRQ LWQGSFSPSG
NVKPLAPDNL TLHTNVSDEW LLTWNNLYPS NNLLYKDLIS MVNISREDNP AEFIVYNVTY
KEPRLSFPIN ILMSGVYYTA RVRVRSQILT GTWSEWSPSI TWYNHFQLPL IQRLPLGVTI
SCLCIPLFCL FCYFSITKIK KIWWDQIPTP ARSPLVAIII QDAQVPLWDK QTRSQESTKY
PHWKTCLDKL LPCLLKHRVK KKTDFPKAAP TKSLQSPGKA GWCPMEVSRT VLWPENVSVS
VVRCMELFEA PVQNVEEEED EIVKEDLSMS PENSGGCGFQ ESQADIMARL TENLFSDLLE
AENGGLGQSA LAESCSPLPS GSGQASVSWA CLPMGPSEEA TCQVTEQPSH PGPLSGSPAQ
SAPTLACTQV PLVLADNPAY RSFSDCCSPA PNPGELAPEQ QQADHLEEEE PPSPADPHSS
GPPMQPVESW EQILHMSVLQ HGAAAGSTPA PAGGYQEFVQ AVKQGAAQDP GVPGVRPSGD
PGYKAFSSLL SSNGIRGDTA AAGTDDGHGG YKPFQNPVPN QSPSSVPLFT FGLDTELSPS
PLNSDPPKSP PECLGLELGL KGGDWVKAPP PADQVPKPFG DDLGFGIVYS SLTCHLCGHL
KQHHSQEEGG QSPIVASPGC GCCYDDRSPS LGSLSGALES CPEGIPPEAN LMSAPKTPSN
LSGEGKGPGH SPVPSQTTEV PVGALGIAVS
