IL3RA_HUMAN
ID IL3RA_HUMAN Reviewed; 378 AA.
AC P26951; A8K3F3; B9VI81; Q5HYQ7; Q5HYQ8; Q9UEH7;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 193.
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: CD_antigen=CD123;
DE Flags: Precursor;
GN Name=IL3RA; Synonyms=IL3R;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=1833064; DOI=10.1016/0092-8674(91)90039-2;
RA Kitamura T., Sato N., Arai K., Miyajima A.;
RT "Expression cloning of the human IL-3 receptor cDNA reveals a shared beta
RT subunit for the human IL-3 and GM-CSF receptors.";
RL Cell 66:1165-1174(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=7887951; DOI=10.1006/bbrc.1995.1346;
RA Kosugi H., Nakagawa Y., Hotta T., Saito H., Miyajima A., Arai K.,
RA Yokota T.;
RT "Structure of the gene encoding the alpha subunit of the human interleukin
RT 3 receptor.";
RL Biochem. Biophys. Res. Commun. 208:360-367(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-12; GLY-77; THR-123 AND
RP LEU-323.
RG SeattleSNPs variation discovery resource;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT THR-12.
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=10527461; DOI=10.1002/stem.170265;
RA Huang S., Chen Z., Yu J.F., Young D., Bashey A., Ho A.D., Law P.;
RT "Correlation between IL-3 receptor expression and growth potential of human
RT CD34+ hematopoietic cells from different tissues.";
RL Stem Cells 17:265-272(1999).
RN [9] {ECO:0007744|PDB:4JZJ}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 20-307, GLYCOSYLATION AT ASN-46
RP AND ASN-80, AND DISULFIDE BONDS.
RX PubMed=25043189; DOI=10.1016/j.celrep.2014.06.038;
RA Broughton S.E., Hercus T.R., Hardy M.P., McClure B.J., Nero T.L.,
RA Dottore M., Huynh H., Braley H., Barry E.F., Kan W.L., Dhagat U.,
RA Scotney P., Hartman D., Busfield S.J., Owczarek C.M., Nash A.D.,
RA Wilson N.J., Parker M.W., Lopez A.F.;
RT "Dual mechanism of interleukin-3 receptor blockade by an anti-cancer
RT antibody.";
RL Cell Rep. 8:410-419(2014).
RN [10] {ECO:0007744|PDB:5UV8, ECO:0007744|PDB:5UWC}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 20-307, DISULFIDE BONDS,
RP FUNCTION, AND INTERACTION WITH IL3.
RX PubMed=29374162; DOI=10.1038/s41467-017-02633-7;
RA Broughton S.E., Hercus T.R., Nero T.L., Kan W.L., Barry E.F., Dottore M.,
RA Cheung Tung Shing K.S., Morton C.J., Dhagat U., Hardy M.P., Wilson N.J.,
RA Downton M.T., Schieber C., Hughes T.P., Lopez A.F., Parker M.W.;
RT "A dual role for the N-terminal domain of the IL-3 receptor in cell
RT signalling.";
RL Nat. Commun. 9:386-386(2018).
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 (PubMed:10527461). 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. Activation of JAK2
CC leads to STAT5-mediated transcriptional program (By similarity).
CC {ECO:0000250|UniProtKB:P26952, ECO:0000269|PubMed:10527461,
CC ECO:0000269|PubMed:29374162}.
CC -!- SUBUNIT: Interacts with IL3 (PubMed:29374162). Heterodimer of an alpha
CC and a beta subunit. The beta subunit is common to the IL3, IL5 and GM-
CC CSF receptors.
CC -!- INTERACTION:
CC P26951; O95393: BMP10; NbExp=3; IntAct=EBI-1757512, EBI-3922513;
CC P26951; O14523: C2CD2L; NbExp=3; IntAct=EBI-1757512, EBI-12822627;
CC P26951; Q8N6F1-2: CLDN19; NbExp=3; IntAct=EBI-1757512, EBI-12256978;
CC P26951; P54852: EMP3; NbExp=3; IntAct=EBI-1757512, EBI-3907816;
CC P26951; Q8WWP7: GIMAP1; NbExp=3; IntAct=EBI-1757512, EBI-11991950;
CC P26951; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-1757512, EBI-10266796;
CC P26951; Q92993: KAT5; NbExp=3; IntAct=EBI-1757512, EBI-399080;
CC P26951; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-1757512, EBI-11742507;
CC P26951; Q9NZG7: NINJ2; NbExp=3; IntAct=EBI-1757512, EBI-10317425;
CC P26951; Q9NXK6: PAQR5; NbExp=3; IntAct=EBI-1757512, EBI-10316423;
CC P26951; P17252: PRKCA; NbExp=3; IntAct=EBI-1757512, EBI-1383528;
CC P26951; Q9Y6X1: SERP1; NbExp=3; IntAct=EBI-1757512, EBI-10329948;
CC P26951; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-1757512, EBI-9090795;
CC P26951; Q0VAQ4: SMAGP; NbExp=3; IntAct=EBI-1757512, EBI-10226799;
CC P26951; Q8N2H4: SYS1; NbExp=3; IntAct=EBI-1757512, EBI-13075176;
CC P26951; Q5BJH2-2: TMEM128; NbExp=3; IntAct=EBI-1757512, EBI-10694905;
CC P26951; Q9BVK8: TMEM147; NbExp=3; IntAct=EBI-1757512, EBI-348587;
CC P26951; Q8TBM7: TMEM254; NbExp=3; IntAct=EBI-1757512, EBI-11956809;
CC P26951; Q6PI78: TMEM65; NbExp=3; IntAct=EBI-1757512, EBI-6656213;
CC P26951; A5PKU2: TUSC5; NbExp=3; IntAct=EBI-1757512, EBI-11988865;
CC P26951; O95183: VAMP5; NbExp=3; IntAct=EBI-1757512, EBI-10191195;
CC P26951; P61981: YWHAG; NbExp=3; IntAct=EBI-1757512, EBI-359832;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=SP1;
CC IsoId=P26951-1; Sequence=Displayed;
CC Name=2; Synonyms=SP2;
CC IsoId=P26951-2; Sequence=VSP_040622;
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 -!- MISCELLANEOUS: The gene coding for this protein is located in the
CC pseudoautosomal region 1 (PAR1) of X and Y chromosomes.
CC -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 5
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA08393.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/IL3RAID40959chXp22Yp13.html";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/il3ra/";
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DR EMBL; M74782; AAA59148.1; -; mRNA.
DR EMBL; D49410; BAA08393.1; ALT_SEQ; Genomic_DNA.
DR EMBL; FJ550347; ACM24116.1; -; mRNA.
DR EMBL; AK290568; BAF83257.1; -; mRNA.
DR EMBL; AY789109; AAV40832.1; -; Genomic_DNA.
DR EMBL; BX296563; CAI39694.1; -; Genomic_DNA.
DR EMBL; AL683870; CAI39694.1; JOINED; Genomic_DNA.
DR EMBL; BX119906; CAI39694.1; JOINED; Genomic_DNA.
DR EMBL; BX296563; CAI39695.1; -; Genomic_DNA.
DR EMBL; BX119906; CAI39695.1; JOINED; Genomic_DNA.
DR EMBL; BX901885; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC035407; AAH35407.1; -; mRNA.
DR CCDS; CCDS14113.1; -. [P26951-1]
DR CCDS; CCDS59158.1; -. [P26951-2]
DR PIR; A40266; A40266.
DR RefSeq; NP_001254642.1; NM_001267713.1. [P26951-2]
DR RefSeq; NP_002174.1; NM_002183.3. [P26951-1]
DR RefSeq; XP_005274488.1; XM_005274431.4. [P26951-1]
DR RefSeq; XP_005274837.1; XM_005274780.4. [P26951-1]
DR PDB; 4JZJ; X-ray; 2.80 A; C/D=20-307.
DR PDB; 5UV8; X-ray; 2.70 A; A/G=20-307.
DR PDB; 5UWC; X-ray; 2.40 A; G=20-307.
DR PDB; 6NMY; X-ray; 3.30 A; F/M=20-307.
DR PDBsum; 4JZJ; -.
DR PDBsum; 5UV8; -.
DR PDBsum; 5UWC; -.
DR PDBsum; 6NMY; -.
DR AlphaFoldDB; P26951; -.
DR SMR; P26951; -.
DR BioGRID; 109778; 89.
DR DIP; DIP-3293N; -.
DR IntAct; P26951; 34.
DR STRING; 9606.ENSP00000327890; -.
DR ChEMBL; CHEMBL3712987; -.
DR DrugBank; DB00020; Sargramostim.
DR DrugBank; DB14731; Tagraxofusp.
DR DrugCentral; P26951; -.
DR GlyGen; P26951; 9 sites.
DR iPTMnet; P26951; -.
DR PhosphoSitePlus; P26951; -.
DR BioMuta; IL3RA; -.
DR DMDM; 417184; -.
DR jPOST; P26951; -.
DR MassIVE; P26951; -.
DR PaxDb; P26951; -.
DR PeptideAtlas; P26951; -.
DR PRIDE; P26951; -.
DR ProteomicsDB; 54369; -. [P26951-1]
DR ProteomicsDB; 54370; -. [P26951-2]
DR ABCD; P26951; 62 sequenced antibodies.
DR Antibodypedia; 565; 1182 antibodies from 42 providers.
DR DNASU; 3563; -.
DR Ensembl; ENST00000331035.10; ENSP00000327890.4; ENSG00000185291.12. [P26951-1]
DR Ensembl; ENST00000381469.7; ENSP00000370878.2; ENSG00000185291.12. [P26951-2]
DR GeneID; 3563; -.
DR KEGG; hsa:3563; -.
DR MANE-Select; ENST00000331035.10; ENSP00000327890.4; NM_002183.4; NP_002174.1.
DR UCSC; uc004cps.4; human. [P26951-1]
DR CTD; 3563; -.
DR DisGeNET; 3563; -.
DR GeneCards; IL3RA; -.
DR HGNC; HGNC:6012; IL3RA.
DR HPA; ENSG00000185291; Low tissue specificity.
DR MIM; 308385; gene.
DR MIM; 430000; gene.
DR neXtProt; NX_P26951; -.
DR OpenTargets; ENSG00000185291; -.
DR PharmGKB; PA29831; -.
DR VEuPathDB; HostDB:ENSG00000185291; -.
DR eggNOG; ENOG502RZVR; Eukaryota.
DR GeneTree; ENSGT00940000163802; -.
DR HOGENOM; CLU_039627_2_0_1; -.
DR InParanoid; P26951; -.
DR OMA; RVASPPF; -.
DR OrthoDB; 1201451at2759; -.
DR PhylomeDB; P26951; -.
DR TreeFam; TF331549; -.
DR PathwayCommons; P26951; -.
DR Reactome; R-HSA-512988; Interleukin-3, Interleukin-5 and GM-CSF signaling.
DR Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
DR Reactome; R-HSA-912526; Interleukin receptor SHC signaling.
DR SignaLink; P26951; -.
DR SIGNOR; P26951; -.
DR BioGRID-ORCS; 3563; 14 hits in 576 CRISPR screens.
DR ChiTaRS; IL3RA; human.
DR GeneWiki; IL3RA; -.
DR GenomeRNAi; 3563; -.
DR Pharos; P26951; Tclin.
DR PRO; PR:P26951; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P26951; protein.
DR Bgee; ENSG00000185291; Expressed in right uterine tube and 116 other tissues.
DR ExpressionAtlas; P26951; baseline and differential.
DR Genevisible; P26951; HS.
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:0005886; C:plasma membrane; TAS:Reactome.
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:0004912; F:interleukin-3 receptor activity; TAS:ProtInc.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR040907; IL3Ra_N.
DR InterPro; IPR003532; Short_hematopoietin_rcpt_2_CS.
DR InterPro; IPR015321; TypeI_recpt_CBD.
DR Pfam; PF18611; IL3Ra_N; 1.
DR Pfam; PF09240; IL6Ra-bind; 1.
DR SUPFAM; SSF49265; SSF49265; 2.
DR PROSITE; PS01356; HEMATOPO_REC_S_F2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Disulfide bond; Glycoprotein; Membrane;
KW Receptor; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..378
FT /note="Interleukin-3 receptor subunit alpha"
FT /id="PRO_0000010883"
FT TOPO_DOM 19..305
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 326..378
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOTIF 282..286
FT /note="WSXWS motif"
FT MOTIF 334..342
FT /note="Box 1 motif"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:25043189,
FT ECO:0007744|PDB:4JZJ"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:25043189,
FT ECO:0007744|PDB:4JZJ"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 52..68
FT /evidence="ECO:0000269|PubMed:25043189,
FT ECO:0000269|PubMed:29374162"
FT DISULFID 76..195
FT /evidence="ECO:0000269|PubMed:25043189,
FT ECO:0000269|PubMed:29374162"
FT DISULFID 112..122
FT /evidence="ECO:0000269|PubMed:25043189,
FT ECO:0000269|PubMed:29374162"
FT DISULFID 151..165
FT /evidence="ECO:0000269|PubMed:25043189,
FT ECO:0000269|PubMed:29374162"
FT DISULFID 217..293
FT /evidence="ECO:0000269|PubMed:29374162"
FT VAR_SEQ 22..100
FT /note="DPNPPITNLRMKAKAQQLTWDLNRNVTDIECVKDADYSMPAVNNSYCQFGAI
FT SLCEVTNYTVRVANPPFSTWILFPENS -> G (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19109256"
FT /id="VSP_040622"
FT VARIANT 12
FT /note="A -> T (in dbSNP:rs6647004)"
FT /evidence="ECO:0000269|PubMed:15772651, ECO:0000269|Ref.5"
FT /id="VAR_021113"
FT VARIANT 77
FT /note="E -> G (in dbSNP:rs17886756)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_021114"
FT VARIANT 123
FT /note="S -> T (in dbSNP:rs17883572)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_021115"
FT VARIANT 323
FT /note="V -> L (in dbSNP:rs17883366)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_021116"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:5UV8"
FT TURN 34..37
FT /evidence="ECO:0007829|PDB:5UWC"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:5UV8"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:5UWC"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:5UWC"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:5UWC"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:5UWC"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:5UWC"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:5UWC"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:5UWC"
FT TURN 86..89
FT /evidence="ECO:0007829|PDB:4JZJ"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:5UWC"
FT STRAND 108..115
FT /evidence="ECO:0007829|PDB:5UWC"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:5UWC"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:5UWC"
FT STRAND 135..142
FT /evidence="ECO:0007829|PDB:5UWC"
FT TURN 143..146
FT /evidence="ECO:0007829|PDB:6NMY"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:5UWC"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:5UWC"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:6NMY"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:5UWC"
FT HELIX 170..174
FT /evidence="ECO:0007829|PDB:5UWC"
FT STRAND 179..187
FT /evidence="ECO:0007829|PDB:5UWC"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:5UWC"
FT STRAND 196..201
FT /evidence="ECO:0007829|PDB:5UWC"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:5UWC"
FT STRAND 212..216
FT /evidence="ECO:0007829|PDB:5UWC"
FT STRAND 219..227
FT /evidence="ECO:0007829|PDB:5UWC"
FT STRAND 236..243
FT /evidence="ECO:0007829|PDB:5UWC"
FT STRAND 250..256
FT /evidence="ECO:0007829|PDB:5UWC"
FT STRAND 258..264
FT /evidence="ECO:0007829|PDB:5UWC"
FT STRAND 266..276
FT /evidence="ECO:0007829|PDB:5UWC"
FT TURN 277..279
FT /evidence="ECO:0007829|PDB:5UWC"
FT STRAND 289..292
FT /evidence="ECO:0007829|PDB:5UWC"
SQ SEQUENCE 378 AA; 43330 MW; 716CE1803F2E5FC0 CRC64;
MVLLWLTLLL IALPCLLQTK EDPNPPITNL RMKAKAQQLT WDLNRNVTDI ECVKDADYSM
PAVNNSYCQF GAISLCEVTN YTVRVANPPF STWILFPENS GKPWAGAENL TCWIHDVDFL
SCSWAVGPGA PADVQYDLYL NVANRRQQYE CLHYKTDAQG TRIGCRFDDI SRLSSGSQSS
HILVRGRSAA FGIPCTDKFV VFSQIEILTP PNMTAKCNKT HSFMHWKMRS HFNRKFRYEL
QIQKRMQPVI TEQVRDRTSF QLLNPGTYTV QIRARERVYE FLSAWSTPQR FECDQEEGAN
TRAWRTSLLI ALGTLLALVC VFVICRRYLV MQRLFPRIPH MKDPIGDSFQ NDKLVVWEAG
KAGLEECLVT EVQVVQKT
