IL4RA_HORSE
ID IL4RA_HORSE Reviewed; 809 AA.
AC Q6WG24; Q8MIR9;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 25-MAY-2022, entry version 113.
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 Flags: Precursor;
GN Name=IL4R;
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANTS VAL-464;
RP SER-554; THR-559 AND ALA-572.
RC TISSUE=Monocyte;
RX PubMed=14741137; DOI=10.1016/j.vetimm.2003.09.004;
RA Solberg O.D., Jackson K.A., Millon L.V., Stott J.L., Vandenplas M.L.,
RA Moore J.N., Watson J.L.;
RT "Genomic characterization of equine interleukin-4 receptor alpha-chain
RT (IL4R).";
RL Vet. Immunol. Immunopathol. 97:187-194(2004).
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 (By similarity).
CC {ECO:0000250}.
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 PIK3C3. Interacts with the SH2-containing phosphatases,
CC PTPN6/SHIP1, PTPN11/SHIP2 and INPP5D/SHIP. Interacts with JAK1 through
CC a Box 1-containing region; inhibited by SOCS5. Interacts with SOCS5;
CC inhibits IL4 signaling. Interacts with JAK3. Interacts with CLM1.
CC {ECO:0000250|UniProtKB:P16382, ECO:0000250|UniProtKB:P24394}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Membrane form;
CC IsoId=Q6WG24-1; Sequence=Displayed;
CC Name=2; Synonyms=Soluble form;
CC IsoId=Q6WG24-2; Sequence=VSP_011114, VSP_011115;
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 tyrosine residues in the
CC cytoplasmic domain. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 4
CC subfamily. {ECO:0000305}.
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DR EMBL; AY081138; AAL87462.1; -; mRNA.
DR EMBL; AY289616; AAQ56236.1; -; mRNA.
DR RefSeq; NP_001075243.1; NM_001081774.2. [Q6WG24-1]
DR AlphaFoldDB; Q6WG24; -.
DR SMR; Q6WG24; -.
DR STRING; 9796.ENSECAP00000050346; -.
DR PaxDb; Q6WG24; -.
DR GeneID; 791252; -.
DR KEGG; ecb:791252; -.
DR CTD; 3566; -.
DR InParanoid; Q6WG24; -.
DR OrthoDB; 476828at2759; -.
DR Proteomes; UP000002281; Unplaced.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0016064; P:immunoglobulin mediated immune response; IBA:GO_Central.
DR GO; GO:0002532; P:production of molecular mediator involved in inflammatory response; IEA:InterPro.
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 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Membrane; Phosphoprotein; Receptor; Reference proteome; Secreted; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000250"
FT CHAIN 26..809
FT /note="Interleukin-4 receptor subunit alpha"
FT /id="PRO_0000010886"
FT TOPO_DOM 26..231
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 256..809
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 125..222
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 369..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 441..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 606..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 211..215
FT /note="WSXWS motif"
FT MOTIF 261..269
FT /note="Box 1 motif"
FT MOTIF 695..700
FT /note="ITIM motif"
FT COMPBIAS 443..469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16382"
FT MOD_RES 488
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P24394"
FT MOD_RES 566
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P24394"
FT MOD_RES 590
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P24394"
FT MOD_RES 618
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P24394"
FT CARBOHYD 53
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 112
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 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 208
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 223..224
FT /note="YY -> SP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14741137"
FT /id="VSP_011114"
FT VAR_SEQ 225..809
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14741137"
FT /id="VSP_011115"
FT VARIANT 464
FT /note="A -> V"
FT /evidence="ECO:0000269|PubMed:14741137"
FT VARIANT 554
FT /note="A -> S"
FT /evidence="ECO:0000269|PubMed:14741137"
FT VARIANT 559
FT /note="A -> T"
FT /evidence="ECO:0000269|PubMed:14741137"
FT VARIANT 572
FT /note="V -> A"
FT /evidence="ECO:0000269|PubMed:14741137"
SQ SEQUENCE 809 AA; 86735 MW; 55CFBA1358375DA0 CRC64;
MGCLCPGLTL PVSCLILVWA AGSGSVKVLR LTACFSDYIS ASTCEWKMDR PTNCSAQLRL
SYQLNDEFSD NLTCIPENRE DEVCVCRMLM DNIVSEDVYE LDLWAGNQLL WNSSFKPSRH
VKPRAPQNLT VHAISHTWLL TWSNPYPLKN HLWSELTYLV NISKEDDPTD FKIYNVTYMD
PTLRVTASTL KSRATYSARV KARAQNYNST WSEWSPSTTW HNYYEQPLEQ RLPLGVSISC
VVILAICLSC YFSIIKIKKE WWDQIPNPAH SPLVAIVLQD SQVSLWGKQS RGQEPAKCPR
WKTCLTKLLP CLLEHGLQKE EDSSKTVRNG PFQSPGKSAW HTVEVNHTIL RPEIISVVPC
VELCEAQVES EEEEVEEDRG SFCPSPESSG SGFQEGREGV AARLTESLFL GLLGAENGAL
GESCLLPPLG SAHMPWARIS SAGPQEAASQ GEEQPLNPES NPLATLTQSP GSLAFTEAPA
VVADNPAYRS FSNSLSQPRG PGELDSDPQL AEHLGQVDPS IPSAPQPSEP PTALQPEPET
WEQMLRQSVL QQGAAPAPAS APTGGYREFA QVVKQGGGAA GSGPSGEAGY KAFSSLLAGS
AVCPGQSGVE ASSGEGGYRP YESPDPGAPA PVPVPLFTFG LDVEPPHSPQ NSLLPGGSPE
LPGPEPTVKG EDPRKPLLSA QQATDSLRDD LGSGIVYSAL TCHLCGHLKQ CHGQEEHGEA
HTVASPCCGC CCGDRSSPPV SPVRALDPPP GGVPLEAGLS LASLGSLGLS EERKPSLFFQ
PAPGNAQSSS QTPLTVAMLS TGPTCTSAS
