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 27-MAR-2024, entry version 198. 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}. 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; 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 PDB; 8DDC; NMR; -; A=253-286. DR PDB; 8DDD; NMR; -; A=253-286. DR PDBsum; 6DG5; -. DR PDBsum; 8DDC; -. DR PDBsum; 8DDD; -. DR AlphaFoldDB; P34902; -. DR SMR; P34902; -. DR IntAct; P34902; 3. DR STRING; 10090.ENSMUSP00000033664; -. DR GlyCosmos; P34902; 6 sites, No reported glycans. DR GlyGen; P34902; 6 sites. DR iPTMnet; P34902; -. DR PhosphoSitePlus; P34902; -. DR SwissPalm; P34902; -. DR EPD; P34902; -. DR PaxDb; 10090-ENSMUSP00000033664; -. DR ProteomicsDB; 267323; -. DR DNASU; 16186; -. DR Ensembl; ENSMUST00000033664.14; ENSMUSP00000033664.8; ENSMUSG00000031304.19. DR GeneID; 16186; -. DR KEGG; mmu:16186; -. DR UCSC; uc009txc.1; mouse. DR AGR; MGI:96551; -. 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; TAGCWLQ; -. DR OrthoDB; 5174285at2759; -. 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 78 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 117 other cell types or tissues. DR ExpressionAtlas; P34902; baseline and differential. DR GO; GO:0009986; C:cell surface; ISS:UniProtKB. DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI. DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005886; C:plasma membrane; ISO:MGI. DR GO; GO:0043235; C:receptor complex; IBA:GO_Central. DR GO; GO:0015026; F:coreceptor activity; ISO:MGI. 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:0038110; P:interleukin-2-mediated signaling pathway; ISO:MGI. DR GO; GO:0038113; P:interleukin-9-mediated signaling pathway; ISO:MGI. 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; Immunoglobulins; 2. DR InterPro; IPR048648; CRLF2-like_D2. DR InterPro; IPR048651; CRLF2_D1. 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 PANTHER; PTHR23037; CYTOKINE RECEPTOR; 1. DR PANTHER; PTHR23037:SF41; CYTOKINE RECEPTOR-LIKE FACTOR 2-RELATED; 1. DR Pfam; PF21605; CRLF2-like_D2; 1. DR Pfam; PF21604; CRLF2_D1; 1. DR SMART; SM00060; FN3; 1. DR SUPFAM; SSF49265; Fibronectin type III; 2. DR PROSITE; PS50853; FN3; 1. DR PROSITE; PS01355; HEMATOPO_REC_S_F1; 1. DR Genevisible; P34902; MM. 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" FT TURN 257..260 FT /evidence="ECO:0007829|PDB:8DDC" FT HELIX 262..265 FT /evidence="ECO:0007829|PDB:8DDC" FT HELIX 267..284 FT /evidence="ECO:0007829|PDB:8DDC" 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 //