IL3RA_MOUSE
ID IL3RA_MOUSE Reviewed; 396 AA.
AC P26952; B9VI80;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Interleukin-3 receptor subunit alpha;
DE Short=IL-3 receptor subunit alpha;
DE Short=IL-3R subunit alpha;
DE Short=IL-3R-alpha;
DE Short=IL-3RA;
DE AltName: Full=Interleukin-3 receptor class II alpha chain;
DE AltName: CD_antigen=CD123;
DE Flags: Precursor;
GN Name=Il3ra; Synonyms=Sut-1;
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] (ISOFORM 1).
RC STRAIN=B6.S;
RX PubMed=1582416; DOI=10.1002/j.1460-2075.1992.tb05239.x;
RA Hara T., Miyajima A.;
RT "Two distinct functional high affinity receptors for mouse interleukin-3
RT (IL-3).";
RL EMBO J. 11:1875-1884(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), AND SUBCELLULAR LOCATION.
RC STRAIN=A/J, and C57BL/6J;
RX PubMed=7889941; DOI=10.1002/j.1460-2075.1995.tb07075.x;
RA Ichihara M., Hara T., Takagi M., Cho L.C., Gorman D.M., Miyajima A.;
RT "Impaired interleukin-3 (IL-3) response of the A/J mouse is caused by a
RT branch point deletion in the IL-3 receptor alpha subunit gene.";
RL EMBO J. 14:939-950(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING.
RX PubMed=19109256; DOI=10.1074/jbc.m808197200;
RA Chen J., Olsen J., Ford S., Mirza S., Walker A., Murphy J.M., Young I.G.;
RT "A new isoform of IL-3 receptor alpha with novel differentiation activity
RT and high affinity binding mode.";
RL J. Biol. Chem. 284:5763-5773(2009).
RN [4]
RP FUNCTION, AND INTERACTION WITH IL3RB.
RX PubMed=10477686;
RA Orban P.C., Levings M.K., Schrader J.W.;
RT "Heterodimerization of the alpha and beta chains of the interleukin-3 (IL-
RT 3) receptor is necessary and sufficient for IL-3-induced mitogenesis.";
RL Blood 94:1614-1622(1999).
RN [5]
RP FUNCTION IN STAT5 ACTIVATION.
RX PubMed=10376805; DOI=10.1016/s0898-6568(98)00049-7;
RA Jaster R., Tschirch E., Bittorf T., Brock J.;
RT "Role of STAT5 in interferon-alpha signal transduction in Ba/F3 cells.";
RL Cell. Signal. 11:331-335(1999).
CC -!- FUNCTION: Cell surface receptor for IL3 expressed on hematopoietic
CC progenitor cells, monocytes and B-lymphocytes that controls the
CC production and differentiation of hematopoietic progenitor cells into
CC lineage-restricted cells (By similarity). Ligand stimulation rapidly
CC induces hetrodimerization with IL3RB, phosphorylation and enzyme
CC activity of effector proteins such as JAK2 and PI3K that play a role in
CC signaling cell proliferation and differentiation (PubMed:10477686).
CC Activation of JAK2 leads to STAT5-mediated transcriptional program
CC (PubMed:10376805). {ECO:0000250|UniProtKB:P26951,
CC ECO:0000269|PubMed:10376805, ECO:0000269|PubMed:10477686}.
CC -!- SUBUNIT: Interacts with IL3. Heterodimer of an alpha and a beta subunit
CC (PubMed:10477686). The beta subunit is common to the IL3, IL5 and GM-
CC CSF receptors. {ECO:0000250|UniProtKB:P26951,
CC ECO:0000269|PubMed:10477686}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass type I
CC membrane protein. Note=Expressed on the cell surface.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Endomembrane system; Single-pass
CC type I membrane protein. Note=Mostly distributed inside the cells,
CC except in the nuclei and is not transported to the cell surface.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=B, SP1;
CC IsoId=P26952-1; Sequence=Displayed;
CC Name=2; Synonyms=SP2;
CC IsoId=P26952-3; Sequence=VSP_040623;
CC Name=3; Synonyms=A;
CC IsoId=P26952-2; Sequence=VSP_011265;
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 -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 5
CC subfamily. {ECO:0000305}.
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DR EMBL; X64534; CAA45833.1; -; mRNA.
DR EMBL; FJ550346; ACM24115.1; -; mRNA.
DR CCDS; CCDS26827.1; -. [P26952-1]
DR PIR; S22909; S22909.
DR RefSeq; NP_032395.1; NM_008369.1. [P26952-1]
DR AlphaFoldDB; P26952; -.
DR SMR; P26952; -.
DR BioGRID; 200636; 3.
DR DIP; DIP-59621N; -.
DR IntAct; P26952; 1.
DR STRING; 10090.ENSMUSP00000088079; -.
DR GlyGen; P26952; 5 sites.
DR PhosphoSitePlus; P26952; -.
DR EPD; P26952; -.
DR MaxQB; P26952; -.
DR PaxDb; P26952; -.
DR PRIDE; P26952; -.
DR ProteomicsDB; 301647; -. [P26952-1]
DR ProteomicsDB; 301648; -. [P26952-3]
DR ProteomicsDB; 301649; -. [P26952-2]
DR DNASU; 16188; -.
DR Ensembl; ENSMUST00000090591; ENSMUSP00000088079; ENSMUSG00000068758. [P26952-1]
DR Ensembl; ENSMUST00000224163; ENSMUSP00000153358; ENSMUSG00000068758. [P26952-1]
DR Ensembl; ENSMUST00000224877; ENSMUSP00000153086; ENSMUSG00000068758. [P26952-3]
DR GeneID; 16188; -.
DR KEGG; mmu:16188; -.
DR UCSC; uc007sgm.1; mouse. [P26952-1]
DR UCSC; uc011zgb.1; mouse. [P26952-3]
DR CTD; 3563; -.
DR MGI; MGI:96553; Il3ra.
DR VEuPathDB; HostDB:ENSMUSG00000068758; -.
DR eggNOG; ENOG502RZVR; Eukaryota.
DR GeneTree; ENSGT00940000171119; -.
DR HOGENOM; CLU_039627_1_0_1; -.
DR InParanoid; P26952; -.
DR OMA; RVASPPF; -.
DR OrthoDB; 1201451at2759; -.
DR PhylomeDB; P26952; -.
DR TreeFam; TF331549; -.
DR BioGRID-ORCS; 16188; 5 hits in 75 CRISPR screens.
DR ChiTaRS; Slc13a4; mouse.
DR PRO; PR:P26952; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; P26952; protein.
DR Bgee; ENSMUSG00000068758; Expressed in granulocyte and 86 other tissues.
DR ExpressionAtlas; P26952; baseline and differential.
DR Genevisible; P26952; MM.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
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:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0038156; P:interleukin-3-mediated signaling pathway; IDA:MGI.
DR Gene3D; 2.60.40.10; -; 2.
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; 1.
DR PROSITE; PS01356; HEMATOPO_REC_S_F2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..396
FT /note="Interleukin-3 receptor subunit alpha"
FT /id="PRO_0000010884"
FT TOPO_DOM 17..331
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 332..355
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 356..396
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOTIF 312..316
FT /note="WSXWS motif"
FT MOTIF 363..371
FT /note="Box 1 motif"
FT CARBOHYD 91
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 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 62..79
FT /evidence="ECO:0000250|UniProtKB:P26951"
FT DISULFID 87..223
FT /evidence="ECO:0000250|UniProtKB:P26951"
FT DISULFID 125..134
FT /evidence="ECO:0000250|UniProtKB:P26951"
FT DISULFID 165..187
FT /evidence="ECO:0000250|UniProtKB:P26951"
FT DISULFID 245..323
FT /evidence="ECO:0000250|UniProtKB:P26951"
FT VAR_SEQ 20..112
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19109256"
FT /id="VSP_040623"
FT VAR_SEQ 274..283
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:7889941"
FT /id="VSP_011265"
FT CONFLICT 113
FT /note="D -> G (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 396 AA; 43195 MW; F1A5BF11743AB8A3 CRC64;
MAANLWLILG LLASHSSDLA AVREAPPTAV TTPIQNLHID PAHYTLSWDP APGADITTGA
FCRKGRDIFV WADPGLARCS FQSLSLCHVT NFTVFLGKDR AVAGSIQFPP DDDGDHEAAA
QDLRCWVHEG QLSCQWERGP KATGDVHYRM FWRDVRLGPA HNRECPHYHS LDVNTAGPAP
HGGHEGCTLD LDTVLGSTPN SPDLVPQVTI TVNGSGRAGP VPCMDNTVDL QRAEVLAPPT
LTVECNGSEA HARWVARNRF HHGLLGYTLQ VNQSSRSEPQ EYNVSIPHFW VPNAGAISFR
VKSRSEVYPR KLSSWSEAWG LVCPPEVMPV KTALVTSVAT VLGAGLVAAG LLLWWRKSLL
YRLCPPIPRL RLPLAGEMVV WEPALEDCEV TPVTDA
