IL2RG_MOUSE
ID IL2RG_MOUSE Reviewed; 369 AA.
AC P34902;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Cytokine receptor common subunit gamma;
DE AltName: Full=Interleukin-2 receptor subunit gamma;
DE Short=IL-2 receptor subunit gamma;
DE Short=IL-2R subunit gamma;
DE Short=IL-2RG;
DE AltName: Full=gammaC;
DE AltName: Full=p64;
DE AltName: CD_antigen=CD132;
DE Flags: Precursor;
GN Name=Il2rg;
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=8503926; DOI=10.1006/bbrc.1993.1631;
RA Kumaki S., Kondo M., Takeshita T., Asao H., Nakamura M., Sugamura K.;
RT "Cloning of the mouse interleukin 2 receptor gamma chain: demonstration of
RT functional differences between the mouse and human receptors.";
RL Biochem. Biophys. Res. Commun. 193:356-363(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=CBA/CaJ;
RX PubMed=8378320; DOI=10.1073/pnas.90.18.8464;
RA Cao X., Kozak C.A., Liu Y.J., Noguchi M., O'Connell E., Leonard W.J.;
RT "Characterization of cDNAs encoding the murine interleukin 2 receptor (IL-
RT 2R) gamma chain: chromosomal mapping and tissue specificity of IL-2R gamma
RT chain expression.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:8464-8468(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8359699; DOI=10.1016/0378-1119(93)90436-7;
RA Kobayashi N., Nakagawa S., Minami Y., Taniguchi T., Kono T.;
RT "Cloning and sequencing of the cDNA encoding a mouse IL-2 receptor gamma.";
RL Gene 130:303-304(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7805729; DOI=10.1002/eji.1830241214;
RA Disanto J.P., Certain S., Wilson A., Macdonald H.R., Avner P., Fischer A.,
RA de Saint Basile G.;
RT "The murine interleukin-2 receptor gamma chain gene: organization,
RT chromosomal localization and expression in the adult thymus.";
RL Eur. J. Immunol. 24:3014-3018(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=B6.S;
RX PubMed=8750189; DOI=10.1007/bf01052626;
RA Chiu R.K., Droll A., Cooper D.L., Dougherty S.T., Dirks J.F.,
RA Dougherty G.J.;
RT "Molecular mechanisms regulating the hyaluronan binding activity of the
RT adhesion protein CD44.";
RL J. Neurooncol. 26:231-239(1995).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Salivary gland;
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 [7]
RP FUNCTION, AND INTERACTION WITH IL9.
RX PubMed=7718508; DOI=10.1093/intimm/7.1.115;
RA Kimura Y., Takeshita T., Kondo M., Ishii N., Nakamura M., Van Snick J.,
RA Sugamura K.;
RT "Sharing of the IL-2 receptor gamma chain with the functional IL-9 receptor
RT complex.";
RL Int. Immunol. 7:115-120(1995).
CC -!- FUNCTION: Common subunit for the receptors for a variety of
CC interleukins (PubMed:7718508). Probably in association with IL15RA,
CC involved in the stimulation of neutrophil phagocytosis by IL15 (By
CC similarity). {ECO:0000250|UniProtKB:P31785,
CC ECO:0000269|PubMed:7718508}.
CC -!- SUBUNIT: The gamma subunit is common to the IL2, IL4, IL7, IL15, IL21
CC and probably also the IL13 receptors. Interacts with SHB upon
CC interleukin stimulation (By similarity). Interacts with IL9
CC (PubMed:7718508). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P31785};
CC Single-pass type I membrane protein {ECO:0000255}. Cell surface
CC {ECO:0000250|UniProtKB:P31785}.
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 5
CC subfamily. {ECO:0000305}.
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DR EMBL; D13821; BAA02974.1; -; mRNA.
DR EMBL; U21795; AAA64279.1; -; Genomic_DNA.
DR EMBL; D13565; BAA02760.1; -; mRNA.
DR EMBL; L20048; AAA39286.1; -; mRNA.
DR EMBL; S75852; AAB32904.1; -; Genomic_DNA.
DR EMBL; S75844; AAB32904.1; JOINED; Genomic_DNA.
DR EMBL; S75845; AAB32904.1; JOINED; Genomic_DNA.
DR EMBL; S75847; AAB32904.1; JOINED; Genomic_DNA.
DR EMBL; S75848; AAB32904.1; JOINED; Genomic_DNA.
DR EMBL; S75849; AAB32904.1; JOINED; Genomic_DNA.
DR EMBL; S75850; AAB32904.1; JOINED; Genomic_DNA.
DR EMBL; S75851; AAB32904.1; JOINED; Genomic_DNA.
DR EMBL; X75337; CAA53085.1; -; mRNA.
DR EMBL; BC014720; AAH14720.1; -; mRNA.
DR CCDS; CCDS30312.1; -.
DR PIR; I49280; I49280.
DR RefSeq; NP_038591.1; NM_013563.4.
DR PDB; 6DG5; X-ray; 2.52 A; C=56-254.
DR PDBsum; 6DG5; -.
DR AlphaFoldDB; P34902; -.
DR SMR; P34902; -.
DR IntAct; P34902; 3.
DR STRING; 10090.ENSMUSP00000033664; -.
DR GlyGen; P34902; 6 sites.
DR iPTMnet; P34902; -.
DR PhosphoSitePlus; P34902; -.
DR SwissPalm; P34902; -.
DR EPD; P34902; -.
DR PaxDb; P34902; -.
DR PRIDE; P34902; -.
DR ProteomicsDB; 267323; -.
DR DNASU; 16186; -.
DR Ensembl; ENSMUST00000033664; ENSMUSP00000033664; ENSMUSG00000031304.
DR GeneID; 16186; -.
DR KEGG; mmu:16186; -.
DR UCSC; uc009txc.1; mouse.
DR CTD; 3561; -.
DR MGI; MGI:96551; Il2rg.
DR VEuPathDB; HostDB:ENSMUSG00000031304; -.
DR eggNOG; ENOG502S289; Eukaryota.
DR GeneTree; ENSGT00510000048979; -.
DR HOGENOM; CLU_060544_1_0_1; -.
DR InParanoid; P34902; -.
DR OMA; NKDTSWT; -.
DR OrthoDB; 753404at2759; -.
DR PhylomeDB; P34902; -.
DR TreeFam; TF333657; -.
DR Reactome; R-MMU-1266695; Interleukin-7 signaling.
DR Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
DR Reactome; R-MMU-6785807; Interleukin-4 and Interleukin-13 signaling.
DR Reactome; R-MMU-8983432; Interleukin-15 signaling.
DR Reactome; R-MMU-8985947; Interleukin-9 signaling.
DR Reactome; R-MMU-9020558; Interleukin-2 signaling.
DR Reactome; R-MMU-9020958; Interleukin-21 signaling.
DR Reactome; R-MMU-912526; Interleukin receptor SHC signaling.
DR BioGRID-ORCS; 16186; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Il2rg; mouse.
DR PRO; PR:P34902; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; P34902; protein.
DR Bgee; ENSMUSG00000031304; Expressed in mesenteric lymph node and 114 other tissues.
DR ExpressionAtlas; P34902; baseline and differential.
DR Genevisible; P34902; MM.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
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:0042010; F:interleukin-15 receptor activity; ISS:UniProtKB.
DR GO; GO:0019976; F:interleukin-2 binding; IPI:MGI.
DR GO; GO:0030183; P:B cell differentiation; IMP:MGI.
DR GO; GO:0002361; P:CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation; IMP:MGI.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR GO; GO:0035723; P:interleukin-15-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0030098; P:lymphocyte differentiation; IMP:MGI.
DR GO; GO:0002335; P:mature B cell differentiation; IMP:MGI.
DR GO; GO:0045579; P:positive regulation of B cell differentiation; IMP:MGI.
DR GO; GO:0032831; P:positive regulation of CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation; IMP:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI.
DR GO; GO:0050766; P:positive regulation of phagocytosis; ISS:UniProtKB.
DR GO; GO:0033089; P:positive regulation of T cell differentiation in thymus; IMP:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR GO; GO:0033077; P:T cell differentiation in thymus; IMP:MGI.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR003531; Hempt_rcpt_S_F1_CS.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR015321; TypeI_recpt_CBD.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF09240; IL6Ra-bind; 1.
DR SMART; SM00060; FN3; 1.
DR SUPFAM; SSF49265; SSF49265; 2.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS01355; HEMATOPO_REC_S_F1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Disulfide bond; Glycoprotein; Membrane;
KW Receptor; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000250"
FT CHAIN 23..369
FT /note="Cytokine receptor common subunit gamma"
FT /id="PRO_0000010867"
FT TOPO_DOM 23..263
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 285..369
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 156..254
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT MOTIF 238..242
FT /note="WSXWS motif"
FT MOTIF 286..294
FT /note="Box 1 motif"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 62..72
FT /evidence="ECO:0000255"
FT DISULFID 102..115
FT /evidence="ECO:0000255"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:6DG5"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:6DG5"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:6DG5"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:6DG5"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:6DG5"
FT STRAND 86..92
FT /evidence="ECO:0007829|PDB:6DG5"
FT STRAND 103..108
FT /evidence="ECO:0007829|PDB:6DG5"
FT STRAND 111..118
FT /evidence="ECO:0007829|PDB:6DG5"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:6DG5"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:6DG5"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:6DG5"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:6DG5"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:6DG5"
FT STRAND 158..163
FT /evidence="ECO:0007829|PDB:6DG5"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:6DG5"
FT STRAND 170..175
FT /evidence="ECO:0007829|PDB:6DG5"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:6DG5"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:6DG5"
FT STRAND 185..191
FT /evidence="ECO:0007829|PDB:6DG5"
FT STRAND 199..206
FT /evidence="ECO:0007829|PDB:6DG5"
FT STRAND 208..211
FT /evidence="ECO:0007829|PDB:6DG5"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:6DG5"
FT STRAND 220..227
FT /evidence="ECO:0007829|PDB:6DG5"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:6DG5"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:6DG5"
SQ SEQUENCE 369 AA; 42241 MW; CB2D5AB459077AC7 CRC64;
MLKLLLSPRS FLVLQLLLLR AGWSSKVLMS SANEDIKADL ILTSTAPEHL SAPTLPLPEV
QCFVFNIEYM NCTWNSSSEP QATNLTLHYR YKVSDNNTFQ ECSHYLFSKE ITSGCQIQKE
DIQLYQTFVV QLQDPQKPQR RAVQKLNLQN LVIPRAPENL TLSNLSESQL ELRWKSRHIK
ERCLQYLVQY RSNRDRSWTE LIVNHEPRFS LPSVDELKRY TFRVRSRYNP ICGSSQQWSK
WSQPVHWGSH TVEENPSLFA LEAVLIPVGT MGLIITLIFV YCWLERMPPI PPIKNLEDLV
TEYQGNFSAW SGVSKGLTES LQPDYSERFC HVSEIPPKGG ALGEGPGGSP CSLHSPYWPP
PCYSLKPEA
