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IL5RA_MOUSE
ID   IL5RA_MOUSE             Reviewed;         415 AA.
AC   P21183;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 1.
DT   03-AUG-2022, entry version 169.
DE   RecName: Full=Interleukin-5 receptor subunit alpha;
DE            Short=IL-5 receptor subunit alpha;
DE            Short=IL-5R subunit alpha;
DE            Short=IL-5R-alpha;
DE            Short=IL-5RA;
DE   AltName: CD_antigen=CD125;
DE   Flags: Precursor;
GN   Name=Il5ra; Synonyms=Il5r;
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].
RX   PubMed=2265612; DOI=10.1002/j.1460-2075.1990.tb07886.x;
RA   Takaki S., Tominaga A., Mita S., Sonoda E., Yamaguchi N., Takatsu K.;
RT   "Molecular cloning and expression of the murine interleukin-5 receptor.";
RL   EMBO J. 9:4367-4374(1990).
RN   [2]
RP   FUNCTION, AND INTERACTION WITH IL5.
RX   PubMed=1873482; DOI=10.1016/1043-4666(91)90503-6;
RA   Barry S.C., McKenzie A.N., Strath M., Sanderson C.J.;
RT   "Analysis of interleukin 5 receptors on murine eosinophils: a comparison
RT   with receptors on B13 cells.";
RL   Cytokine 3:339-344(1991).
CC   -!- FUNCTION: Cell surface receptor that plays an important role in the
CC       survival, differentiation, and chemotaxis of eosinophils
CC       (PubMed:1873482). Acts by forming an heterodimeric receptor with CSF2RB
CC       subunit and subsequently binding to interleukin-5. In unstimulated
CC       conditions, interacts constitutively with JAK2. Heterodimeric receptor
CC       activation leads to JAK2 stimulation and subsequent activation of the
CC       JAK-STAT pathway. {ECO:0000250|UniProtKB:Q01344,
CC       ECO:0000269|PubMed:1873482}.
CC   -!- SUBUNIT: Interacts with IL5 (PubMed:1873482). Interacts with CSF2RB.
CC       Interacts with JAK2. Interacts with SDCBP.
CC       {ECO:0000250|UniProtKB:Q01344, ECO:0000269|PubMed:1873482}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC   -!- TISSUE SPECIFICITY: Expressed on eosinophils and basophils. Also on B-
CC       cells.
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.
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DR   EMBL; D90205; BAA14231.1; -; mRNA.
DR   CCDS; CCDS20396.1; -.
DR   PIR; S12357; S12357.
DR   RefSeq; NP_032396.1; NM_008370.2.
DR   RefSeq; XP_017176895.1; XM_017321406.1.
DR   AlphaFoldDB; P21183; -.
DR   SMR; P21183; -.
DR   STRING; 10090.ENSMUSP00000129781; -.
DR   BindingDB; P21183; -.
DR   ChEMBL; CHEMBL4523198; -.
DR   GlyGen; P21183; 4 sites.
DR   PhosphoSitePlus; P21183; -.
DR   PaxDb; P21183; -.
DR   PRIDE; P21183; -.
DR   ProteomicsDB; 267048; -.
DR   Antibodypedia; 2274; 413 antibodies from 34 providers.
DR   DNASU; 16192; -.
DR   Ensembl; ENSMUST00000167925; ENSMUSP00000129781; ENSMUSG00000005364.
DR   Ensembl; ENSMUST00000204659; ENSMUSP00000144718; ENSMUSG00000005364.
DR   GeneID; 16192; -.
DR   KEGG; mmu:16192; -.
DR   UCSC; uc009dcx.1; mouse.
DR   CTD; 3568; -.
DR   MGI; MGI:96558; Il5ra.
DR   VEuPathDB; HostDB:ENSMUSG00000005364; -.
DR   eggNOG; ENOG502QZNV; Eukaryota.
DR   GeneTree; ENSGT00940000160890; -.
DR   HOGENOM; CLU_039945_0_0_1; -.
DR   InParanoid; P21183; -.
DR   OMA; HAIDQVN; -.
DR   OrthoDB; 1151666at2759; -.
DR   PhylomeDB; P21183; -.
DR   TreeFam; TF331549; -.
DR   Reactome; R-MMU-512988; Interleukin-3, Interleukin-5 and GM-CSF signaling.
DR   Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
DR   Reactome; R-MMU-912526; Interleukin receptor SHC signaling.
DR   BioGRID-ORCS; 16192; 3 hits in 72 CRISPR screens.
DR   PRO; PR:P21183; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; P21183; protein.
DR   Bgee; ENSMUSG00000005364; Expressed in right kidney and 12 other tissues.
DR   ExpressionAtlas; P21183; baseline and differential.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR   GO; GO:0019955; F:cytokine binding; IBA:GO_Central.
DR   GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central.
DR   GO; GO:0071310; P:cellular response to organic substance; IMP:MGI.
DR   GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0002437; P:inflammatory response to antigenic stimulus; IMP:MGI.
DR   GO; GO:0032674; P:regulation of interleukin-5 production; IMP:MGI.
DR   CDD; cd00063; FN3; 1.
DR   Gene3D; 2.60.40.10; -; 3.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003532; Short_hematopoietin_rcpt_2_CS.
DR   InterPro; IPR015321; TypeI_recpt_CBD.
DR   Pfam; PF09240; IL6Ra-bind; 1.
DR   SUPFAM; SSF49265; SSF49265; 2.
DR   PROSITE; PS50853; FN3; 2.
DR   PROSITE; PS01356; HEMATOPO_REC_S_F2; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Glycoprotein; Membrane; Receptor; Reference proteome;
KW   Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..17
FT   CHAIN           18..415
FT                   /note="Interleukin-5 receptor subunit alpha"
FT                   /id="PRO_0000010894"
FT   TOPO_DOM        18..339
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        340..361
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        362..415
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          29..120
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          238..331
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   MOTIF           319..323
FT                   /note="WSXWS motif"
FT   MOTIF           367..375
FT                   /note="Box 1 motif"
FT   CARBOHYD        32
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        213
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        241
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        131..152
FT                   /evidence="ECO:0000250"
FT   DISULFID        179..193
FT                   /evidence="ECO:0000250"
FT   DISULFID        266..313
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   415 AA;  46989 MW;  A4326D2922571C08 CRC64;
     MVPVLLILVG ALATLQADLL NHKKFLLLPP VNFTIKATGL AQVLLHWDPN PDQEQRHVDL
     EYHVKINAPQ EDEYDTRKTE SKCVTPLHEG FAASVRTILK SSHTTLASSW VSAELKAPPG
     SPGTSVTNLT CTTHTVVSSH THLRPYQVSL RCTWLVGKDA PEDTQYFLYY RFGVLTEKCQ
     EYSRDALNRN TACWFPRTFI NSKGFEQLAV HINGSSKRAA IKPFDQLFSP LAIDQVNPPR
     NVTVEIESNS LYIQWEKPLS AFPDHCFNYE LKIYNTKNGH IQKEKLIANK FISKIDDVST
     YSIQVRAAVS SPCRMPGRWG EWSQPIYVGK ERKSLVEWHL IVLPTAACFV LLIFSLICRV
     CHLWTRLFPP VPAPKSNIKD LPVVTEYEKP SNETKIEVVH CVEEVGFEVM GNSTF
 
 
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