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Cytokine receptor common subunit beta (GM-CSF/IL-3/IL-5 receptor common beta subunit) (CD antigen CD131)

 IL3RB_MOUSE             Reviewed;         896 AA.
P26955; Q3U7L5;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
25-OCT-2017, entry version 157.
RecName: Full=Cytokine receptor common subunit beta;
AltName: Full=GM-CSF/IL-3/IL-5 receptor common beta subunit;
AltName: CD_antigen=CD131;
Flags: Precursor;
Name=Csf2rb; Synonyms=Aic2b, Csf2rb1, Il3rb1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1695379; DOI=10.1073/pnas.87.14.5459;
Gorman D.M., Itoh N., Kitamura T., Schreurs J., Yonehara S.,
Yahara I., Arai K., Miyajima A.;
"Cloning and expression of a gene encoding an interleukin 3 receptor-
like protein: identification of another member of the cytokine
receptor gene family.";
Proc. Natl. Acad. Sci. U.S.A. 87:5459-5463(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Bone marrow;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
PHOSPHORYLATION, AND INTERACTION WITH LYN.
PubMed=10672044; DOI=10.1046/j.1365-2443.2000.00312.x;
Dahl M.E., Arai K.I., Watanabe S.;
"Association of Lyn tyrosine kinase to the GM-CSF and IL-3 receptor
common betac subunit and role of Src tyrosine kinases in DNA synthesis
and anti-apoptosis.";
Genes Cells 5:143-153(2000).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-752; SER-754 AND
TYR-765, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Mast cell;
PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
Kawakami T., Salomon A.R.;
"Quantitative time-resolved phosphoproteomic analysis of mast cell
signaling.";
J. Immunol. 179:5864-5876(2007).
-!- FUNCTION: High affinity receptor for interleukin-3, interleukin-5
and granulocyte-macrophage colony-stimulating factor.
-!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The beta
subunit is common to the IL3, IL5 and GM-CSF receptors. The
signaling GM-CSF receptor complex is a dodecamer of two head-to-
head hexamers of two alpha, two beta, and two ligand subunits.
Interacts with TMEM102; this interaction occurs preferentially in
the absence of CSF2 (By similarity). Interacts with LYN.
{ECO:0000250, ECO:0000269|PubMed:10672044}.
-!- INTERACTION:
P09055:Itgb1; NbExp=2; IntAct=EBI-1810026, EBI-644224;
P05532:Kit; NbExp=4; IntAct=EBI-1810026, EBI-8559255;
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- DOMAIN: The WSXWS motif appears to be necessary for proper protein
folding and thereby efficient intracellular transport and cell-
surface receptor binding.
-!- DOMAIN: The box 1 motif is required for JAK interaction and/or
activation.
-!- PTM: May be phosphorylated by LYN. {ECO:0000269|PubMed:10672044}.
-!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 4
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M34397; AAA37204.1; -; mRNA.
EMBL; AK152608; BAE31354.1; -; mRNA.
CCDS; CCDS27612.1; -.
PIR; A35782; A35782.
RefSeq; NP_031806.3; NM_007780.4.
RefSeq; XP_006520450.1; XM_006520387.3.
UniGene; Mm.235324; -.
ProteinModelPortal; P26955; -.
BioGrid; 198932; 2.
CORUM; P26955; -.
DIP; DIP-46527N; -.
IntAct; P26955; 3.
STRING; 10090.ENSMUSP00000094082; -.
iPTMnet; P26955; -.
PhosphoSitePlus; P26955; -.
MaxQB; P26955; -.
PaxDb; P26955; -.
PRIDE; P26955; -.
Ensembl; ENSMUST00000096355; ENSMUSP00000094082; ENSMUSG00000071713.
GeneID; 12983; -.
KEGG; mmu:12983; -.
UCSC; uc007woz.2; mouse.
CTD; 1439; -.
MGI; MGI:1339759; Csf2rb.
eggNOG; ENOG410IGEX; Eukaryota.
eggNOG; ENOG4112BQP; LUCA.
GeneTree; ENSGT00510000048963; -.
HOGENOM; HOG000113049; -.
HOVERGEN; HBG052113; -.
InParanoid; P26955; -.
KO; K04738; -.
OMA; CRWADTQ; -.
OrthoDB; EOG091G05K0; -.
TreeFam; TF337996; -.
Reactome; R-MMU-114604; GPVI-mediated activation cascade.
Reactome; R-MMU-392451; G beta:gamma signalling through PI3Kgamma.
Reactome; R-MMU-512988; Interleukin-3, 5 and GM-CSF signaling.
Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
Reactome; R-MMU-5683826; Surfactant metabolism.
Reactome; R-MMU-912526; Interleukin receptor SHC signaling.
PRO; PR:P26955; -.
Proteomes; UP000000589; Chromosome 15.
Bgee; ENSMUSG00000071713; -.
Genevisible; P26955; MM.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0004896; F:cytokine receptor activity; IEA:InterPro.
GO; GO:0019221; P:cytokine-mediated signaling pathway; IDA:MGI.
GO; GO:0001558; P:regulation of cell growth; IGI:MGI.
CDD; cd00063; FN3; 1.
Gene3D; 2.60.40.10; -; 4.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR003531; Hempt_rcpt_S_F1_CS.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR011365; IL3_rcpt_beta.
InterPro; IPR015373; Interferon/interleukin_rcp_dom.
InterPro; IPR015321; TypeI_recpt_CBD.
Pfam; PF09240; IL6Ra-bind; 1.
Pfam; PF09294; Interfer-bind; 1.
PIRSF; PIRSF001956; IL3R_beta_c; 1.
SMART; SM00060; FN3; 2.
SUPFAM; SSF49265; SSF49265; 4.
PROSITE; PS50853; FN3; 2.
PROSITE; PS01355; HEMATOPO_REC_S_F1; 1.
1: Evidence at protein level;
Complete proteome; Disulfide bond; Glycoprotein; Membrane;
Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 22 {ECO:0000255}.
CHAIN 23 896 Cytokine receptor common subunit beta.
/FTId=PRO_0000010863.
TOPO_DOM 23 441 Extracellular. {ECO:0000255}.
TRANSMEM 442 463 Helical. {ECO:0000255}.
TOPO_DOM 464 896 Cytoplasmic. {ECO:0000255}.
DOMAIN 136 243 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 343 439 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
MOTIF 428 432 WSXWS motif.
MOTIF 477 485 Box 1 motif.
MOD_RES 752 752 Phosphoserine.
{ECO:0000244|PubMed:17947660}.
MOD_RES 754 754 Phosphoserine.
{ECO:0000244|PubMed:17947660}.
MOD_RES 765 765 Phosphotyrosine.
{ECO:0000244|PubMed:17947660}.
CARBOHYD 62 62 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 141 141 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 350 350 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 39 49 {ECO:0000250}.
DISULFID 77 99 {ECO:0000250}.
DISULFID 88 94 {ECO:0000250}.
DISULFID 253 263 {ECO:0000250}.
DISULFID 292 310 {ECO:0000250}.
CONFLICT 82 82 E -> K (in Ref. 1; AAA37204).
{ECO:0000305}.
CONFLICT 213 213 A -> P (in Ref. 1; AAA37204).
{ECO:0000305}.
CONFLICT 220 220 S -> Y (in Ref. 1; AAA37204).
{ECO:0000305}.
CONFLICT 236 236 V -> A (in Ref. 1; AAA37204).
{ECO:0000305}.
CONFLICT 634 634 P -> A (in Ref. 1; AAA37204).
{ECO:0000305}.
CONFLICT 639 639 A -> V (in Ref. 1; AAA37204).
{ECO:0000305}.
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


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