IL3B2_MOUSE
ID IL3B2_MOUSE Reviewed; 878 AA.
AC P26954;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Interleukin-3 receptor class 2 subunit beta;
DE Short=IL-3 receptor class 2 subunit beta;
DE Short=IL-3R class 2 subunit beta;
DE AltName: Full=Colony-stimulating factor 2 receptor subunit beta-2;
DE AltName: Full=Interleukin-3 receptor class II beta chain;
DE Flags: Precursor;
GN Name=Csf2rb2; Synonyms=Ai2ca, Il3r, Il3rb2;
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=2404337; DOI=10.1126/science.2404337;
RA Itoh N., Yonehara S., Schreurs J., Gorman D.M., Maruyama K., Ishii A.,
RA Yahara I., Arai K., Miyajima A.;
RT "Cloning of an interleukin-3 receptor gene: a member of a distinct receptor
RT gene family.";
RL Science 247:324-327(1990).
CC -!- FUNCTION: In mouse, there are two classes of high-affinity IL3
CC receptors. One contains this IL3-specific beta subunit and the other
CC contains the beta subunit also shared by high-affinity IL5 and GM-CSF
CC receptors.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit.
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 -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 4
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M29855; AAA39295.1; -; mRNA.
DR CCDS; CCDS27611.1; -.
DR PIR; A40091; A40091.
DR RefSeq; NP_031807.1; NM_007781.3.
DR PDB; 4QQV; X-ray; 3.45 A; A/B/C/D=23-438.
DR PDBsum; 4QQV; -.
DR AlphaFoldDB; P26954; -.
DR SMR; P26954; -.
DR BioGRID; 198933; 2.
DR DIP; DIP-143N; -.
DR MINT; P26954; -.
DR STRING; 10090.ENSMUSP00000094083; -.
DR GlyGen; P26954; 2 sites.
DR iPTMnet; P26954; -.
DR MaxQB; P26954; -.
DR PaxDb; P26954; -.
DR PRIDE; P26954; -.
DR ProteomicsDB; 267046; -.
DR DNASU; 12984; -.
DR Ensembl; ENSMUST00000096356; ENSMUSP00000094083; ENSMUSG00000071714.
DR GeneID; 12984; -.
DR KEGG; mmu:12984; -.
DR UCSC; uc007woy.2; mouse.
DR CTD; 12984; -.
DR MGI; MGI:1339760; Csf2rb2.
DR VEuPathDB; HostDB:ENSMUSG00000071714; -.
DR eggNOG; ENOG502RP2T; Eukaryota.
DR GeneTree; ENSGT00510000048963; -.
DR HOGENOM; CLU_015884_0_0_1; -.
DR InParanoid; P26954; -.
DR OMA; KMEQASF; -.
DR OrthoDB; 263501at2759; -.
DR PhylomeDB; P26954; -.
DR TreeFam; TF337996; -.
DR Reactome; R-MMU-512988; Interleukin-3, Interleukin-5 and GM-CSF signaling.
DR Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
DR Reactome; R-MMU-5683826; Surfactant metabolism.
DR Reactome; R-MMU-912526; Interleukin receptor SHC signaling.
DR BioGRID-ORCS; 12984; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Csf2rb2; mouse.
DR PRO; PR:P26954; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P26954; protein.
DR Bgee; ENSMUSG00000071714; Expressed in peripheral lymph node and 83 other tissues.
DR ExpressionAtlas; P26954; baseline and differential.
DR Genevisible; P26954; 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; IDA:MGI.
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: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 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 3D-structure; Disulfide bond; Glycoprotein; Membrane; Phosphoprotein;
KW Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..878
FT /note="Interleukin-3 receptor class 2 subunit beta"
FT /id="PRO_0000010885"
FT TOPO_DOM 23..440
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 441..462
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 463..878
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 139..244
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 343..438
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 223..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..709
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 REGION 829..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 427..431
FT /note="WSXWS motif"
FT MOTIF 476..484
FT /note="Box 1 motif"
FT COMPBIAS 555..574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 752
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26955"
FT MOD_RES 754
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26955"
FT MOD_RES 765
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P26955"
FT CARBOHYD 62
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 78..95
FT /evidence="ECO:0000250"
FT DISULFID 254..264
FT /evidence="ECO:0000250"
FT DISULFID 293..310
FT /evidence="ECO:0000250"
FT HELIX 32..35
FT /evidence="ECO:0007829|PDB:4QQV"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:4QQV"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:4QQV"
FT STRAND 47..54
FT /evidence="ECO:0007829|PDB:4QQV"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:4QQV"
FT STRAND 63..69
FT /evidence="ECO:0007829|PDB:4QQV"
FT STRAND 95..102
FT /evidence="ECO:0007829|PDB:4QQV"
FT STRAND 114..121
FT /evidence="ECO:0007829|PDB:4QQV"
FT STRAND 125..130
FT /evidence="ECO:0007829|PDB:4QQV"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:4QQV"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:4QQV"
FT STRAND 149..157
FT /evidence="ECO:0007829|PDB:4QQV"
FT STRAND 164..167
FT /evidence="ECO:0007829|PDB:4QQV"
FT STRAND 172..181
FT /evidence="ECO:0007829|PDB:4QQV"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:4QQV"
FT STRAND 190..201
FT /evidence="ECO:0007829|PDB:4QQV"
FT STRAND 210..220
FT /evidence="ECO:0007829|PDB:4QQV"
FT STRAND 237..240
FT /evidence="ECO:0007829|PDB:4QQV"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:4QQV"
FT STRAND 250..256
FT /evidence="ECO:0007829|PDB:4QQV"
FT STRAND 258..269
FT /evidence="ECO:0007829|PDB:4QQV"
FT HELIX 270..274
FT /evidence="ECO:0007829|PDB:4QQV"
FT STRAND 278..284
FT /evidence="ECO:0007829|PDB:4QQV"
FT TURN 285..287
FT /evidence="ECO:0007829|PDB:4QQV"
FT STRAND 303..313
FT /evidence="ECO:0007829|PDB:4QQV"
FT STRAND 322..329
FT /evidence="ECO:0007829|PDB:4QQV"
FT STRAND 332..335
FT /evidence="ECO:0007829|PDB:4QQV"
FT STRAND 353..355
FT /evidence="ECO:0007829|PDB:4QQV"
FT STRAND 360..362
FT /evidence="ECO:0007829|PDB:4QQV"
FT STRAND 375..379
FT /evidence="ECO:0007829|PDB:4QQV"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:4QQV"
FT STRAND 398..400
FT /evidence="ECO:0007829|PDB:4QQV"
FT STRAND 413..417
FT /evidence="ECO:0007829|PDB:4QQV"
SQ SEQUENCE 878 AA; 97195 MW; 8EBC9092ADC24D56 CRC64;
MDQQMALTWG LCYMALVALC WGHEVTEEEE TVPLKTLECY NDYTNRIICS WADTEDAQGL
INMTLLYHQL DKIQSVSCEL SEKLMWSECP SSHRCVPRRC VIPYTRFSNG DNDYYSFQPD
RDLGIQLMVP LAQHVQPPPP KDIHISPSGD HFLLEWSVSL GDSQVSWLSS KDIEFEVAYK
RLQDSWEDAS SLHTSNFQVN LEPKLFLPNS IYAARVRTRL SAGSSLSGRP SRWSPEVHWD
SQPGDKAQPQ NLQCFFDGIQ SLHCSWEVWT QTTGSVSFGL FYRPSPAAPE EKCSPVVKEP
QASVYTRYRC SLPVPEPSAH SQYTVSVKHL EQGKFIMSYY HIQMEPPILN QTKNRDSYSL
HWETQKIPKY IDHTFQVQYK KKSESWKDSK TENLGRVNSM DLPQLEPDTS YCARVRVKPI
SDYDGIWSEW SNEYTWTTDW VMPTLWIVLI LVFLIFTLLL ALHFGRVYGY RTYRKWKEKI
PNPSKSLLFQ DGGKGLWPPG SMAAFATKNP ALQGPQSRLL AEQQGVSYEH LEDNNVSPLT
IEDPNIIRDP PSRPDTTPAA SSESTEQLPN VQVEGPIPSS RPRKQLPSFD FNGPYLGPPQ
SHSLPDLPGQ LGSPQVGGSL KPALPGSLEY MCLPPGGQVQ LVPLSQVMGQ GQAMDVQCGS
SLETTGSPSV EPKENPPVEL SVEKQEARDN PMTLPISSGG PEGSMMASDY VTPGDPVLTL
PTGPLSTSLG PSLGLPSAQS PSLCLKLPRV PSGSPALGPP GFEDYVELPP SVSQAATSPP
GHPAPPVASS PTVIPGEPRE EVGPASPHPE GLLVLQQVGD YCFLPGLGPG SLSPHSKPPS
PSLCSETEDL DQDLSVKKFP YQPLPQAPAI QFFKSLKY
