IL3RB_MOUSE
ID IL3RB_MOUSE Reviewed; 896 AA.
AC P26955; Q3U7L5;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Cytokine receptor common subunit beta;
DE AltName: Full=GM-CSF/IL-3/IL-5 receptor common beta subunit;
DE AltName: CD_antigen=CD131;
DE Flags: Precursor;
GN Name=Csf2rb; Synonyms=Aic2b, Csf2rb1, Il3rb1;
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=1695379; DOI=10.1073/pnas.87.14.5459;
RA Gorman D.M., Itoh N., Kitamura T., Schreurs J., Yonehara S., Yahara I.,
RA Arai K., Miyajima A.;
RT "Cloning and expression of a gene encoding an interleukin 3 receptor-like
RT protein: identification of another member of the cytokine receptor gene
RT family.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:5459-5463(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP FUNCTION, AND INTERACTION WITH IL3RA.
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 [4]
RP PHOSPHORYLATION, AND INTERACTION WITH LYN.
RX PubMed=10672044; DOI=10.1046/j.1365-2443.2000.00312.x;
RA Dahl M.E., Arai K.I., Watanabe S.;
RT "Association of Lyn tyrosine kinase to the GM-CSF and IL-3 receptor common
RT betac subunit and role of Src tyrosine kinases in DNA synthesis and anti-
RT apoptosis.";
RL Genes Cells 5:143-153(2000).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-752; SER-754 AND TYR-765, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [6]
RP INTERACTION WITH FCER1G.
RX PubMed=19098920; DOI=10.1038/ni.1686;
RA Hida S., Yamasaki S., Sakamoto Y., Takamoto M., Obata K., Takai T.,
RA Karasuyama H., Sugane K., Saito T., Taki S.;
RT "Fc receptor gamma-chain, a constitutive component of the IL-3 receptor, is
RT required for IL-3-induced IL-4 production in basophils.";
RL Nat. Immunol. 10:214-222(2009).
CC -!- FUNCTION: High affinity receptor for interleukin-3, interleukin-5 and
CC granulocyte-macrophage colony-stimulating factor.
CC {ECO:0000269|PubMed:10477686}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit (PubMed:10477686).
CC The beta subunit is common to the IL3, IL5 and GM-CSF receptors. The
CC signaling GM-CSF receptor complex is a dodecamer of two head-to-head
CC hexamers of two alpha, two beta, and two ligand subunits. Interacts
CC with TMEM102; this interaction occurs preferentially in the absence of
CC CSF2 (By similarity). Interacts with FCER1G; this interaction is direct
CC (PubMed:19098920). Interacts with LYN. {ECO:0000250,
CC ECO:0000269|PubMed:10477686, ECO:0000269|PubMed:10672044,
CC ECO:0000269|PubMed:19098920}.
CC -!- INTERACTION:
CC P26955; P09055: Itgb1; NbExp=2; IntAct=EBI-1810026, EBI-644224;
CC P26955; P05532: Kit; NbExp=4; IntAct=EBI-1810026, EBI-8559255;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
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 -!- PTM: May be phosphorylated by LYN. {ECO:0000269|PubMed:10672044}.
CC -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 4
CC subfamily. {ECO:0000305}.
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DR EMBL; M34397; AAA37204.1; -; mRNA.
DR EMBL; AK152608; BAE31354.1; -; mRNA.
DR CCDS; CCDS27612.1; -.
DR PIR; A35782; A35782.
DR RefSeq; NP_031806.3; NM_007780.4.
DR RefSeq; XP_006520450.1; XM_006520387.3.
DR AlphaFoldDB; P26955; -.
DR SMR; P26955; -.
DR BioGRID; 198932; 2.
DR CORUM; P26955; -.
DR DIP; DIP-46527N; -.
DR IntAct; P26955; 3.
DR STRING; 10090.ENSMUSP00000094082; -.
DR GlyGen; P26955; 3 sites.
DR iPTMnet; P26955; -.
DR PhosphoSitePlus; P26955; -.
DR MaxQB; P26955; -.
DR PaxDb; P26955; -.
DR PRIDE; P26955; -.
DR ProteomicsDB; 301650; -.
DR DNASU; 12983; -.
DR Ensembl; ENSMUST00000096355; ENSMUSP00000094082; ENSMUSG00000071713.
DR Ensembl; ENSMUST00000230264; ENSMUSP00000154836; ENSMUSG00000071713.
DR GeneID; 12983; -.
DR KEGG; mmu:12983; -.
DR UCSC; uc007woz.2; mouse.
DR CTD; 1439; -.
DR MGI; MGI:1339759; Csf2rb.
DR VEuPathDB; HostDB:ENSMUSG00000071713; -.
DR eggNOG; ENOG502RP2T; Eukaryota.
DR GeneTree; ENSGT00510000048963; -.
DR HOGENOM; CLU_015884_0_0_1; -.
DR InParanoid; P26955; -.
DR OMA; LRFCGMY; -.
DR OrthoDB; 263501at2759; -.
DR PhylomeDB; P26955; -.
DR TreeFam; TF337996; -.
DR BioGRID-ORCS; 12983; 3 hits in 73 CRISPR screens.
DR PRO; PR:P26955; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P26955; protein.
DR Bgee; ENSMUSG00000071713; Expressed in mesenteric lymph node and 133 other tissues.
DR ExpressionAtlas; P26955; baseline and differential.
DR Genevisible; P26955; MM.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0030526; C:granulocyte macrophage colony-stimulating factor receptor complex; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IDA:MGI.
DR GO; GO:0038157; P:granulocyte-macrophage colony-stimulating factor signaling pathway; ISO:MGI.
DR GO; GO:0016064; P:immunoglobulin mediated immune response; IBA:GO_Central.
DR GO; GO:0070665; P:positive regulation of leukocyte proliferation; ISO:MGI.
DR GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
DR GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; ISO:MGI.
DR GO; GO:0001558; P:regulation of cell growth; IGI:MGI.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.10; -; 4.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR015152; Growth/epo_recpt_lig-bind.
DR InterPro; IPR003531; Hempt_rcpt_S_F1_CS.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR011365; IL3_rcpt_beta.
DR InterPro; IPR015373; Interferon/interleukin_rcp_dom.
DR Pfam; PF09067; EpoR_lig-bind; 1.
DR Pfam; PF09294; Interfer-bind; 1.
DR PIRSF; PIRSF001956; IL3R_beta_c; 1.
DR SMART; SM00060; FN3; 2.
DR SUPFAM; SSF49265; SSF49265; 4.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS01355; HEMATOPO_REC_S_F1; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..896
FT /note="Cytokine receptor common subunit beta"
FT /id="PRO_0000010863"
FT TOPO_DOM 23..441
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 442..463
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 464..896
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 136..243
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 343..439
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 220..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 543..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 771..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 428..432
FT /note="WSXWS motif"
FT MOTIF 477..485
FT /note="Box 1 motif"
FT COMPBIAS 556..575
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 752
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT MOD_RES 754
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT MOD_RES 765
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 350
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 39..49
FT /evidence="ECO:0000250"
FT DISULFID 77..99
FT /evidence="ECO:0000250"
FT DISULFID 88..94
FT /evidence="ECO:0000250"
FT DISULFID 253..263
FT /evidence="ECO:0000250"
FT DISULFID 292..310
FT /evidence="ECO:0000250"
FT CONFLICT 82
FT /note="E -> K (in Ref. 1; AAA37204)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="A -> P (in Ref. 1; AAA37204)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="S -> Y (in Ref. 1; AAA37204)"
FT /evidence="ECO:0000305"
FT CONFLICT 236
FT /note="V -> A (in Ref. 1; AAA37204)"
FT /evidence="ECO:0000305"
FT CONFLICT 634
FT /note="P -> A (in Ref. 1; AAA37204)"
FT /evidence="ECO:0000305"
FT CONFLICT 639
FT /note="A -> V (in Ref. 1; AAA37204)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 896 AA; 99036 MW; 8E30ECB42C67F89A CRC64;
MDQQMALTWG LCYMALVALC WGHGVTEAEE TVPLKTLQCY NDYTNHIICS WADTEDAQGL
INMTLYHQLE KKQPVSCELS EELMWSECPS SHRCVPRRCV IPYTRFSITN EDYYSFRPDS
DLGIQLMVPL AQNVQPPLPK NVSISSSEDR FLLEWSVSLG DAQVSWLSSK DIEFEVAYKR
LQDSWEDAYS LHTSKFQVNF EPKLFLPNSI YAARVRTRLS PGSSLSGRPS RWSPEVHWDS
QPGDKAQPQN LQCFFDGIQS LHCSWEVWTQ TTGSVSFGLF YRPSPVAPEE KCSPVVKEPP
GASVYTRYHC SLPVPEPSAH SQYTVSVKHL EQGKFIMSYN HIQMEPPTLN LTKNRDSYSL
HWETQKMAYS FIEHTFQVQY KKKSDSWEDS KTENLDRAHS MDLSQLEPDT SYCARVRVKP
ISNYDGIWSK WSEEYTWKTD WVMPTLWIVL ILVFLILTLL LILRFGCVSV YRTYRKWKEK
IPNPSKSLLF QDGGKGLWPP GSMAAFATKN PALQGPQSRL LAEQQGESYA HLEDNNVSPL
TIEDPNIIRV PPSGPDTTPA ASSESTEQLP NVQVEGPTPN RPRKQLPSFD FNGPYLGPPQ
SHSLPDLPDQ LGSPQVGGSL KPALPGSLEY MCLPPGGQAQ LVPLSQVMGQ GQAMDVQCGS
SLETSGSPSV EPKENPPVEL SMEEQEARDN PVTLPISSGG PEGSMMASDY VTPGDPVLTL
PTGPLSTSLG PSLGLPSAQS PSLCLKLPRV PSGSPALGPP GFEDYVELPP SVSQAAKSPP
GHPAPPVASS PTVIPGEPRE EVGPASPHPE GLLVLQQVGD YCFLPGLGPG SLSPHSKPPS
PSLCSETEDL VQDLSVKKFP YQPMPQAPAI QFFKSLKHQD YLSLPPWDNS QSGKVC
