Full text data of IL3RA
IL3RA
(IL3R)
[Confidence: high (a blood group or CD marker)]
Interleukin-3 receptor subunit alpha; IL-3 receptor subunit alpha; IL-3R subunit alpha; IL-3R-alpha; IL-3RA (CD123; Flags: Precursor)
Interleukin-3 receptor subunit alpha; IL-3 receptor subunit alpha; IL-3R subunit alpha; IL-3R-alpha; IL-3RA (CD123; Flags: Precursor)
UniProt
P26951
ID IL3RA_HUMAN Reviewed; 378 AA.
AC P26951; A8K3F3; B9VI81; Q5HYQ7;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-1993, sequence version 1.
DT 22-JAN-2014, entry version 130.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT beta subunit for the human IL-3 and GM-CSF receptors.";
RL Cell 66:1165-1174(1991).
RN [2]
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.,
RA Young I.G.;
RT "A new isoform of IL-3 receptor alpha with novel differentiation
RT activity and high affinity binding mode.";
RL J. Biol. Chem. 284:5763-5773(2009).
RN [3]
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-12; GLY-77;
RP THR-123 AND LEU-323.
RG SeattleSNPs variation discovery resource;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
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.,
RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA 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.,
RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA 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.,
RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA 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.,
RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA 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.,
RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [6]
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: This is a receptor for interleukin-3.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The beta
CC subunit is common to the IL3, IL5 and GM-CSF receptors.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC 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-
CC surface 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.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/IL3RAID40959chXp22Yp13.html";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/il3ra/";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; M74782; AAA59148.1; -; mRNA.
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; BX901885; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC035407; AAH35407.1; -; mRNA.
DR PIR; A40266; A40266.
DR RefSeq; NP_001254642.1; NM_001267713.1.
DR RefSeq; NP_002174.1; NM_002183.3.
DR RefSeq; XP_005274488.1; XM_005274431.1.
DR RefSeq; XP_005274837.1; XM_005274780.1.
DR UniGene; Hs.632790; -.
DR ProteinModelPortal; P26951; -.
DR SMR; P26951; 23-293.
DR DIP; DIP-3293N; -.
DR IntAct; P26951; 12.
DR MINT; MINT-7241956; -.
DR STRING; 9606.ENSP00000327890; -.
DR DrugBank; DB00020; Sargramostim.
DR GuidetoPHARMACOLOGY; 1705; -.
DR PhosphoSite; P26951; -.
DR DMDM; 417184; -.
DR PaxDb; P26951; -.
DR PRIDE; P26951; -.
DR DNASU; 3563; -.
DR Ensembl; ENST00000331035; ENSP00000327890; ENSG00000185291.
DR Ensembl; ENST00000381469; ENSP00000370878; ENSG00000185291.
DR GeneID; 3563; -.
DR KEGG; hsa:3563; -.
DR UCSC; uc004cps.3; human.
DR CTD; 3563; -.
DR GeneCards; GC0XP001455; -.
DR HGNC; HGNC:6012; IL3RA.
DR HPA; CAB018374; -.
DR HPA; HPA003539; -.
DR MIM; 308385; gene.
DR MIM; 430000; gene.
DR neXtProt; NX_P26951; -.
DR PharmGKB; PA29831; -.
DR eggNOG; NOG44788; -.
DR HOVERGEN; HBG107484; -.
DR InParanoid; P26951; -.
DR KO; K04737; -.
DR OMA; KNLRMEP; -.
DR OrthoDB; EOG7TJ3J7; -.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; P26951; -.
DR GeneWiki; IL3RA; -.
DR GenomeRNAi; 3563; -.
DR NextBio; 13916; -.
DR PRO; PR:P26951; -.
DR ArrayExpress; P26951; -.
DR Bgee; P26951; -.
DR CleanEx; HS_IL3RA; -.
DR Genevestigator; P26951; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0004912; F:interleukin-3 receptor activity; TAS:ProtInc.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR003961; Fibronectin_type3.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR015321; IL-6_rcpt_alpha-bd.
DR InterPro; IPR003532; Short_hematopoietin_rcpt_2_CS.
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 Alternative splicing; Complete proteome; Glycoprotein; Membrane;
KW Polymorphism; Receptor; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1 18 Potential.
FT CHAIN 19 378 Interleukin-3 receptor subunit alpha.
FT /FTId=PRO_0000010883.
FT TOPO_DOM 19 305 Extracellular (Potential).
FT TRANSMEM 306 325 Helical; (Potential).
FT TOPO_DOM 326 378 Cytoplasmic (Potential).
FT MOTIF 282 286 WSXWS motif.
FT MOTIF 334 342 Box 1 motif.
FT CARBOHYD 46 46 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 64 64 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 80 80 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 109 109 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 212 212 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 218 218 N-linked (GlcNAc...) (Potential).
FT VAR_SEQ 22 100 Missing (in isoform 2).
FT /FTId=VSP_040622.
FT VARIANT 12 12 A -> T (in dbSNP:rs6647004).
FT /FTId=VAR_021113.
FT VARIANT 77 77 E -> G (in dbSNP:rs17886756).
FT /FTId=VAR_021114.
FT VARIANT 123 123 S -> T (in dbSNP:rs17883572).
FT /FTId=VAR_021115.
FT VARIANT 323 323 V -> L (in dbSNP:rs17883366).
FT /FTId=VAR_021116.
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
//
ID IL3RA_HUMAN Reviewed; 378 AA.
AC P26951; A8K3F3; B9VI81; Q5HYQ7;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-1993, sequence version 1.
DT 22-JAN-2014, entry version 130.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT beta subunit for the human IL-3 and GM-CSF receptors.";
RL Cell 66:1165-1174(1991).
RN [2]
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.,
RA Young I.G.;
RT "A new isoform of IL-3 receptor alpha with novel differentiation
RT activity and high affinity binding mode.";
RL J. Biol. Chem. 284:5763-5773(2009).
RN [3]
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-12; GLY-77;
RP THR-123 AND LEU-323.
RG SeattleSNPs variation discovery resource;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
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.,
RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA 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.,
RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA 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.,
RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA 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.,
RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA 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.,
RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [6]
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: This is a receptor for interleukin-3.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The beta
CC subunit is common to the IL3, IL5 and GM-CSF receptors.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC 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-
CC surface 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.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/IL3RAID40959chXp22Yp13.html";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/il3ra/";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; M74782; AAA59148.1; -; mRNA.
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; BX901885; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC035407; AAH35407.1; -; mRNA.
DR PIR; A40266; A40266.
DR RefSeq; NP_001254642.1; NM_001267713.1.
DR RefSeq; NP_002174.1; NM_002183.3.
DR RefSeq; XP_005274488.1; XM_005274431.1.
DR RefSeq; XP_005274837.1; XM_005274780.1.
DR UniGene; Hs.632790; -.
DR ProteinModelPortal; P26951; -.
DR SMR; P26951; 23-293.
DR DIP; DIP-3293N; -.
DR IntAct; P26951; 12.
DR MINT; MINT-7241956; -.
DR STRING; 9606.ENSP00000327890; -.
DR DrugBank; DB00020; Sargramostim.
DR GuidetoPHARMACOLOGY; 1705; -.
DR PhosphoSite; P26951; -.
DR DMDM; 417184; -.
DR PaxDb; P26951; -.
DR PRIDE; P26951; -.
DR DNASU; 3563; -.
DR Ensembl; ENST00000331035; ENSP00000327890; ENSG00000185291.
DR Ensembl; ENST00000381469; ENSP00000370878; ENSG00000185291.
DR GeneID; 3563; -.
DR KEGG; hsa:3563; -.
DR UCSC; uc004cps.3; human.
DR CTD; 3563; -.
DR GeneCards; GC0XP001455; -.
DR HGNC; HGNC:6012; IL3RA.
DR HPA; CAB018374; -.
DR HPA; HPA003539; -.
DR MIM; 308385; gene.
DR MIM; 430000; gene.
DR neXtProt; NX_P26951; -.
DR PharmGKB; PA29831; -.
DR eggNOG; NOG44788; -.
DR HOVERGEN; HBG107484; -.
DR InParanoid; P26951; -.
DR KO; K04737; -.
DR OMA; KNLRMEP; -.
DR OrthoDB; EOG7TJ3J7; -.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; P26951; -.
DR GeneWiki; IL3RA; -.
DR GenomeRNAi; 3563; -.
DR NextBio; 13916; -.
DR PRO; PR:P26951; -.
DR ArrayExpress; P26951; -.
DR Bgee; P26951; -.
DR CleanEx; HS_IL3RA; -.
DR Genevestigator; P26951; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0004912; F:interleukin-3 receptor activity; TAS:ProtInc.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR003961; Fibronectin_type3.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR015321; IL-6_rcpt_alpha-bd.
DR InterPro; IPR003532; Short_hematopoietin_rcpt_2_CS.
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 Alternative splicing; Complete proteome; Glycoprotein; Membrane;
KW Polymorphism; Receptor; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1 18 Potential.
FT CHAIN 19 378 Interleukin-3 receptor subunit alpha.
FT /FTId=PRO_0000010883.
FT TOPO_DOM 19 305 Extracellular (Potential).
FT TRANSMEM 306 325 Helical; (Potential).
FT TOPO_DOM 326 378 Cytoplasmic (Potential).
FT MOTIF 282 286 WSXWS motif.
FT MOTIF 334 342 Box 1 motif.
FT CARBOHYD 46 46 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 64 64 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 80 80 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 109 109 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 212 212 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 218 218 N-linked (GlcNAc...) (Potential).
FT VAR_SEQ 22 100 Missing (in isoform 2).
FT /FTId=VSP_040622.
FT VARIANT 12 12 A -> T (in dbSNP:rs6647004).
FT /FTId=VAR_021113.
FT VARIANT 77 77 E -> G (in dbSNP:rs17886756).
FT /FTId=VAR_021114.
FT VARIANT 123 123 S -> T (in dbSNP:rs17883572).
FT /FTId=VAR_021115.
FT VARIANT 323 323 V -> L (in dbSNP:rs17883366).
FT /FTId=VAR_021116.
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
//
MIM
308385
*RECORD*
*FIELD* NO
308385
*FIELD* TI
*308385 INTERLEUKIN 3 RECEPTOR, ALPHA; IL3RA
;;CD123 ANTIGEN; CD123
*FIELD* TX
DESCRIPTION
read more
The receptor for interleukin-3 (IL3; 147740) is a heterodimer that
shares a beta chain (CSF2RB; 138981) in common with the receptors for
IL5 (IL5RA; 147851) and GMCSF (CSF2RA; 306250), and, like these other
cytokine receptors, has a ligand-specific alpha chain (IL3RA) (Kremer et
al., 1993).
CLONING
Itoh et al. (1990) cloned IL3RA, a binding component of the IL3
receptor. Sequence comparison of the IL3 receptor with other cytokine
receptors showed a common motif of a distinct receptor gene family.
Kitamura et al. (1991) showed that the alpha chain for the IL3 receptor
is a 360-amino acid glycoprotein of approximately 70 kD.
GENE FUNCTION
Kitamura et al. (1991) found that IL3RA alone bound human IL3 with
extremely low affinity. A high affinity IL3-binding site was
reconstituted by coexpressing IL3RA and CSF2RB, indicating that IL3R and
CSF2RA share the same beta subunit. As in human hematopoietic cells, IL3
and GMCSF competed for binding in fibroblasts expressing the cDNAs for
IL3RA, CSF2RA, and the common beta subunit, indicating that different
alpha subunits compete for a common beta subunit.
Siracusa et al. (2011) demonstrated that TSLP (607003) promotes systemic
basophilia, that disruption of TSLP-TSLPR (300357) interactions results
in defective basophil responses, and that TSLPR-sufficient basophils can
restore TH2-cell-dependent immunity in vivo. TSLP acted directly on bone
marrow-resident progenitors to promote basophil responses selectively.
Critically, TSLP could elicit basophil responses in both
IL3-IL3R-sufficient and -deficient environments, and genomewide
transcriptional profiling and functional analyses identified
heterogeneity between TSLP-elicited versus IL3-elicited basophils.
Furthermore, activated human basophils expressed TSLPR, and basophils
isolated from eosinophilic esophagitis (see 610247) patients were
distinct from classical basophils. Siracusa et al. (2011) concluded that
collectively, their studies identified previously unrecognized
heterogeneity within the basophil cell lineage and indicated that
expression of TSLP may influence susceptibility to multiple allergic
diseases by regulating basophil hematopoiesis and eliciting a population
of functionally distinct basophils that promote TH2 cytokine-mediated
inflammation.
GENE STRUCTURE
Kosugi et al. (1995) cloned the IL3RA gene which spans about 40 kb and
has 12 exons. The genomic structures of IL3RA and CSF2RA are very
similar and share an additional exon encoding part of the C-terminal
domain not found in other members of this gene family. This suggested
that the 2 loci may share a common evolutionary pathway.
MAPPING
Kremer et al. (1993) found that the gene for the IL3 receptor, like the
CSF2RA gene, maps within the X-Y pseudoautosomal region (PAR) (see
430000 for Y-chromosomal IL3RA). Kremer et al. (1993) mapped the gene to
the X and Y chromosomes by PCR analysis of human/rodent somatic cell
hybrids and to chromosomes Yp13.3 and Xp22.3 by fluorescence in situ
hybridization. The pseudoautosomal location of IL3R was confirmed by
screening of 2 informative CEPH families showing male meiotic
recombination with respect to RFLPs. Using long-range restriction
mapping, they found, furthermore, that IL3RA maps to the same 190-kb
restriction fragment as CSF2RA, suggesting that a cytokine receptor gene
cluster may reside in the PAR.
Milatovich et al. (1993) independently mapped the IL3RA gene to the X-Y
pseudoautosomal region near the CSF2RA gene. Their methods were Southern
analysis of somatic cell hybrid panels, pulsed field gel
electrophoresis, and fluorescence chromosomal in situ hybridization. The
CSF2RA and IL3RA genes were so close that their order could not be
determined by two-color interphase in situ hybridization.
Pseudoautosomal inheritance was demonstrated by an EcoRI RFLP detected
with the IL3RA cDNA probe; 16 of 17 unrelated individuals of both sexes
were heterozygous. They cited unpublished data indicating that the
murine Il3ra locus maps to chromosome 14. Milatovich et al. (1993) found
that the CSF2RA and IL3RA genes shared PFGE fragments generated by
different restriction enzymes down to the 50- to 100-kb size range.
*FIELD* RF
1. Itoh, N.; Yonehara, S.; Schreurs, J.; Gorman, D. M.; Maruyama,
K.; Ishii, A.; Yahara, I.; Arai, K.; Miyajima, A.: Cloning of an
interleukin-3 receptor gene: a member of a distinct receptor gene
family. Science 247: 324-327, 1990.
2. Kitamura, T.; Sato, N.; Arai, K.; Miyajima, A.: Expression cloning
of the human IL-3 receptor cDNA reveals a shared beta-subunit for
the human IL-3 and GM-CSF receptors. Cell 66: 1165-1174, 1991.
3. Kosugi, H.; Nakagawa, Y.; Hotta, T.; Saito, H.; Miyajima, A.; Arai,
K.; Yokota, T.: Structure of the gene encoding the alpha subunit
of the human interleukin 3 receptor. Biochem. Biophys. Res. Commun. 208:
360-367, 1995.
4. Kremer, E.; Baker, E.; D'Andrea, R. J.; Slim, R.; Phillips, H.;
Moretti, P. A. B.; Lopez, A. F.; Petit, C.; Vadas, M. A.; Sutherland,
G. R.; Goodall, G. J.: A cytokine receptor gene cluster in the X-Y
pseudoautosomal region? Blood 82: 22-28, 1993.
5. Milatovich, A.; Kitamura, T.; Miyajima, A.; Francke, U.: Gene
for the alpha-subunit of the human interleukin-3 receptor (IL3RA)
localized to the X-Y pseudoautosomal region. Am. J. Hum. Genet. 53:
1146-1153, 1993.
6. Siracusa, M. C.; Saenz, S. A.; Hill, D. A.; Kim, B. S.; Headley,
M. B.; Doering, T. A.; Wherry, E. J.; Jessup, H. K.; Siegel, L. A.;
Kambayashi, T.; Dudek, E. C.; Kubo, M.; Cianferoni, A.; Spergel, J.
M.; Ziegler, S. F.; Comeau, M. R.; Artis, D.: TSLP promotes interleukin-3-independent
basophil haematopoiesis and type 2 inflammation. Nature 477: 229-233,
2011.
*FIELD* CN
Ada Hamosh - updated: 9/21/2011
Matthew B. Gross - updated: 2/19/2009
Alan F. Scott - updated: 6/26/1995
*FIELD* CD
Victor A. McKusick: 10/1/1993
*FIELD* ED
alopez: 09/22/2011
terry: 9/21/2011
mgross: 2/19/2009
terry: 8/26/2008
mgross: 9/19/2002
dkim: 7/2/1998
joanna: 5/8/1998
mark: 6/26/1995
carol: 4/27/1994
terry: 4/21/1994
carol: 11/8/1993
carol: 10/21/1993
carol: 10/18/1993
*RECORD*
*FIELD* NO
308385
*FIELD* TI
*308385 INTERLEUKIN 3 RECEPTOR, ALPHA; IL3RA
;;CD123 ANTIGEN; CD123
*FIELD* TX
DESCRIPTION
read more
The receptor for interleukin-3 (IL3; 147740) is a heterodimer that
shares a beta chain (CSF2RB; 138981) in common with the receptors for
IL5 (IL5RA; 147851) and GMCSF (CSF2RA; 306250), and, like these other
cytokine receptors, has a ligand-specific alpha chain (IL3RA) (Kremer et
al., 1993).
CLONING
Itoh et al. (1990) cloned IL3RA, a binding component of the IL3
receptor. Sequence comparison of the IL3 receptor with other cytokine
receptors showed a common motif of a distinct receptor gene family.
Kitamura et al. (1991) showed that the alpha chain for the IL3 receptor
is a 360-amino acid glycoprotein of approximately 70 kD.
GENE FUNCTION
Kitamura et al. (1991) found that IL3RA alone bound human IL3 with
extremely low affinity. A high affinity IL3-binding site was
reconstituted by coexpressing IL3RA and CSF2RB, indicating that IL3R and
CSF2RA share the same beta subunit. As in human hematopoietic cells, IL3
and GMCSF competed for binding in fibroblasts expressing the cDNAs for
IL3RA, CSF2RA, and the common beta subunit, indicating that different
alpha subunits compete for a common beta subunit.
Siracusa et al. (2011) demonstrated that TSLP (607003) promotes systemic
basophilia, that disruption of TSLP-TSLPR (300357) interactions results
in defective basophil responses, and that TSLPR-sufficient basophils can
restore TH2-cell-dependent immunity in vivo. TSLP acted directly on bone
marrow-resident progenitors to promote basophil responses selectively.
Critically, TSLP could elicit basophil responses in both
IL3-IL3R-sufficient and -deficient environments, and genomewide
transcriptional profiling and functional analyses identified
heterogeneity between TSLP-elicited versus IL3-elicited basophils.
Furthermore, activated human basophils expressed TSLPR, and basophils
isolated from eosinophilic esophagitis (see 610247) patients were
distinct from classical basophils. Siracusa et al. (2011) concluded that
collectively, their studies identified previously unrecognized
heterogeneity within the basophil cell lineage and indicated that
expression of TSLP may influence susceptibility to multiple allergic
diseases by regulating basophil hematopoiesis and eliciting a population
of functionally distinct basophils that promote TH2 cytokine-mediated
inflammation.
GENE STRUCTURE
Kosugi et al. (1995) cloned the IL3RA gene which spans about 40 kb and
has 12 exons. The genomic structures of IL3RA and CSF2RA are very
similar and share an additional exon encoding part of the C-terminal
domain not found in other members of this gene family. This suggested
that the 2 loci may share a common evolutionary pathway.
MAPPING
Kremer et al. (1993) found that the gene for the IL3 receptor, like the
CSF2RA gene, maps within the X-Y pseudoautosomal region (PAR) (see
430000 for Y-chromosomal IL3RA). Kremer et al. (1993) mapped the gene to
the X and Y chromosomes by PCR analysis of human/rodent somatic cell
hybrids and to chromosomes Yp13.3 and Xp22.3 by fluorescence in situ
hybridization. The pseudoautosomal location of IL3R was confirmed by
screening of 2 informative CEPH families showing male meiotic
recombination with respect to RFLPs. Using long-range restriction
mapping, they found, furthermore, that IL3RA maps to the same 190-kb
restriction fragment as CSF2RA, suggesting that a cytokine receptor gene
cluster may reside in the PAR.
Milatovich et al. (1993) independently mapped the IL3RA gene to the X-Y
pseudoautosomal region near the CSF2RA gene. Their methods were Southern
analysis of somatic cell hybrid panels, pulsed field gel
electrophoresis, and fluorescence chromosomal in situ hybridization. The
CSF2RA and IL3RA genes were so close that their order could not be
determined by two-color interphase in situ hybridization.
Pseudoautosomal inheritance was demonstrated by an EcoRI RFLP detected
with the IL3RA cDNA probe; 16 of 17 unrelated individuals of both sexes
were heterozygous. They cited unpublished data indicating that the
murine Il3ra locus maps to chromosome 14. Milatovich et al. (1993) found
that the CSF2RA and IL3RA genes shared PFGE fragments generated by
different restriction enzymes down to the 50- to 100-kb size range.
*FIELD* RF
1. Itoh, N.; Yonehara, S.; Schreurs, J.; Gorman, D. M.; Maruyama,
K.; Ishii, A.; Yahara, I.; Arai, K.; Miyajima, A.: Cloning of an
interleukin-3 receptor gene: a member of a distinct receptor gene
family. Science 247: 324-327, 1990.
2. Kitamura, T.; Sato, N.; Arai, K.; Miyajima, A.: Expression cloning
of the human IL-3 receptor cDNA reveals a shared beta-subunit for
the human IL-3 and GM-CSF receptors. Cell 66: 1165-1174, 1991.
3. Kosugi, H.; Nakagawa, Y.; Hotta, T.; Saito, H.; Miyajima, A.; Arai,
K.; Yokota, T.: Structure of the gene encoding the alpha subunit
of the human interleukin 3 receptor. Biochem. Biophys. Res. Commun. 208:
360-367, 1995.
4. Kremer, E.; Baker, E.; D'Andrea, R. J.; Slim, R.; Phillips, H.;
Moretti, P. A. B.; Lopez, A. F.; Petit, C.; Vadas, M. A.; Sutherland,
G. R.; Goodall, G. J.: A cytokine receptor gene cluster in the X-Y
pseudoautosomal region? Blood 82: 22-28, 1993.
5. Milatovich, A.; Kitamura, T.; Miyajima, A.; Francke, U.: Gene
for the alpha-subunit of the human interleukin-3 receptor (IL3RA)
localized to the X-Y pseudoautosomal region. Am. J. Hum. Genet. 53:
1146-1153, 1993.
6. Siracusa, M. C.; Saenz, S. A.; Hill, D. A.; Kim, B. S.; Headley,
M. B.; Doering, T. A.; Wherry, E. J.; Jessup, H. K.; Siegel, L. A.;
Kambayashi, T.; Dudek, E. C.; Kubo, M.; Cianferoni, A.; Spergel, J.
M.; Ziegler, S. F.; Comeau, M. R.; Artis, D.: TSLP promotes interleukin-3-independent
basophil haematopoiesis and type 2 inflammation. Nature 477: 229-233,
2011.
*FIELD* CN
Ada Hamosh - updated: 9/21/2011
Matthew B. Gross - updated: 2/19/2009
Alan F. Scott - updated: 6/26/1995
*FIELD* CD
Victor A. McKusick: 10/1/1993
*FIELD* ED
alopez: 09/22/2011
terry: 9/21/2011
mgross: 2/19/2009
terry: 8/26/2008
mgross: 9/19/2002
dkim: 7/2/1998
joanna: 5/8/1998
mark: 6/26/1995
carol: 4/27/1994
terry: 4/21/1994
carol: 11/8/1993
carol: 10/21/1993
carol: 10/18/1993
MIM
430000
*RECORD*
*FIELD* NO
430000
*FIELD* TI
*430000 INTERLEUKIN 3 RECEPTOR, Y-CHROMOSOMAL; IL3RA
;;IL3RY;;
IL3RAY
*FIELD* TX
DESCRIPTION
read more
The receptor for interleukin-3 (IL3; 147740) is a heterodimer that
shares a beta chain (CSF2RB; 138981) in common with the receptors for
IL5 (IL5R; 147851) and GMCSF (CSF2R; 306250), and, like these other
cytokine receptors, has a ligand-specific alpha chain (IL3RA).
MAPPING
By fluorescence in situ hybridization, Kremer et al. (1993) demonstrated
that the IL3RY gene is located in the pseudoautosomal region of the X
and Y chromosomes. See 308385.
*FIELD* RF
1. Kremer, E.; Baker, E.; D'Andrea, R. J.; Slim, R.; Phillips, H.;
Moretti, P. A. B.; Lopez, A. F.; Petit, C.; Vadas, M. A.; Sutherland,
G. R.; Goodall, G. J.: A cytokine receptor gene cluster in the X-Y
pseudoautosomal region? Blood 82: 22-28, 1993.
*FIELD* CD
Victor A. McKusick: 10/1/1993
*FIELD* ED
terry: 08/26/2008
mgross: 9/6/2006
dkim: 7/2/1998
mark: 7/26/1995
mimadm: 3/11/1994
carol: 10/1/1993
*RECORD*
*FIELD* NO
430000
*FIELD* TI
*430000 INTERLEUKIN 3 RECEPTOR, Y-CHROMOSOMAL; IL3RA
;;IL3RY;;
IL3RAY
*FIELD* TX
DESCRIPTION
read more
The receptor for interleukin-3 (IL3; 147740) is a heterodimer that
shares a beta chain (CSF2RB; 138981) in common with the receptors for
IL5 (IL5R; 147851) and GMCSF (CSF2R; 306250), and, like these other
cytokine receptors, has a ligand-specific alpha chain (IL3RA).
MAPPING
By fluorescence in situ hybridization, Kremer et al. (1993) demonstrated
that the IL3RY gene is located in the pseudoautosomal region of the X
and Y chromosomes. See 308385.
*FIELD* RF
1. Kremer, E.; Baker, E.; D'Andrea, R. J.; Slim, R.; Phillips, H.;
Moretti, P. A. B.; Lopez, A. F.; Petit, C.; Vadas, M. A.; Sutherland,
G. R.; Goodall, G. J.: A cytokine receptor gene cluster in the X-Y
pseudoautosomal region? Blood 82: 22-28, 1993.
*FIELD* CD
Victor A. McKusick: 10/1/1993
*FIELD* ED
terry: 08/26/2008
mgross: 9/6/2006
dkim: 7/2/1998
mark: 7/26/1995
mimadm: 3/11/1994
carol: 10/1/1993