IL4RA_PIG
ID IL4RA_PIG Reviewed; 830 AA.
AC Q863Z5;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 107.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zarlenga D.S. Jr., Dawson H., Solano-Aguilar G., Urban J.F. Jr.;
RT "Molecular cloning of the swine IL-4 receptor alpha and IL-13 receptor
RT alpha 1 chains: effects of experimental Toxoplasma gondii and Ascaris suum
RT infections on tissue mRNA levels.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
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: Membrane {ECO:0000250}; Single-pass type I
CC membrane protein {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}.
CC -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 4
CC subfamily. {ECO:0000305}.
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DR EMBL; AY266143; AAP23302.1; -; mRNA.
DR RefSeq; NP_999505.1; NM_214340.1.
DR AlphaFoldDB; Q863Z5; -.
DR SMR; Q863Z5; -.
DR STRING; 9823.ENSSSCP00000008346; -.
DR PaxDb; Q863Z5; -.
DR PRIDE; Q863Z5; -.
DR GeneID; 397614; -.
DR KEGG; ssc:397614; -.
DR CTD; 3566; -.
DR eggNOG; ENOG502S3Y8; Eukaryota.
DR HOGENOM; CLU_020561_0_0_1; -.
DR InParanoid; Q863Z5; -.
DR OrthoDB; 476828at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; Q863Z5; SS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004896; F:cytokine receptor activity; IEA:InterPro.
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 Disulfide bond; Glycoprotein; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..830
FT /note="Interleukin-4 receptor subunit alpha"
FT /id="PRO_0000010891"
FT TOPO_DOM 33..240
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 265..830
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 133..232
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 378..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..564
FT /note="Required for IRS1 activation and IL4-induced cell
FT growth"
FT /evidence="ECO:0000250"
FT REGION 450..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..662
FT /note="Required for IL4-induced gene expression"
FT /evidence="ECO:0000250"
FT REGION 623..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 811..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 220..224
FT /note="WSXWS motif"
FT MOTIF 270..278
FT /note="Box 1 motif"
FT MOTIF 716..721
FT /note="ITIM motif"
FT COMPBIAS 463..488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..553
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..677
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16382"
FT MOD_RES 504
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P24394"
FT MOD_RES 583
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P24394"
FT MOD_RES 610
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P24394"
FT MOD_RES 638
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P24394"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 41..51
FT /evidence="ECO:0000250"
FT DISULFID 82..94
FT /evidence="ECO:0000250"
SQ SEQUENCE 830 AA; 89441 MW; 22EB899AE87B1683 CRC64;
MGWLCPGLTF SVSCLILVWA AGSGVTCVSP GGVRVLEWPI CLSDYVSTST CEWRMAGPVN
CSAEFRLSYQ LKFFNTENHT TCVPENRAGS VCVCHMLMES IVIVDTYQLD LWAGEQLLWN
SSFKPSQNVK PLAPRNLMVH ANISHTWLLT WSNPYPSESY LYSELTYLVN ISNENDPTDF
RIYNVTYLGP TLRFPANTLK SGAAYSARVK AWAQRYNSTW SEWSPSVKWL NYYEEPLEQR
LPLGVSISCV VILIICLSCY FGIIRIKKEW WDQIPNPAHS PLVAIVIQDS QVSLWGKRSR
GQEPAKCPRW KTCLTKLLPC FLEHGVDRDE DSSKAARNGP SQGPAKAAWR PVEVSKTILW
PESISVVRCV ELFEAQVENE EEEEEEDKGS FCPSPENSGG SFQEGREGIA ARLTESLFLD
LLGDESGAFS PQGMGQSCLL PPLENASAPM PWAEFPRVGS PEASSQGKEQ PLNPEPSPQA
TPTQSLASLA FPELPAVIAD NPAYRSFSTF LSQSSDPGEL DSDPELAEAL EEVEPSLPAA
PQPSEPPPTL QPEPETWEQI LRQSVLQRRA APAPASGPSS SGYREFVHAV EQGTQDRRAA
GSGPCGEAGY KAFSSLLAGS ASCPGTSGLE PSSGESGYKP FQSLPPGCPE TPVPTPLFTF
GLDMEPPPSP QNPPFPGSSA ECPGLEPAVK GEDGQKPPLA LEQAADPLRD DLGSGIVYSA
LTCHLCGHLK QCHGQEDGGK VHVVASPCCS CCCEDGSPPM VTPLRAPDAP SSGVPLEASL
SPASLALLGV SREGKIPPCL QITPSNVQSS SQTPTAVAML SPGPACMDTS
