Cytokine receptor common subunit gamma (Interleukin-2 receptor subunit gamma) (IL-2 receptor subunit gamma) (IL-2R subunit gamma) (IL-2RG) (gammaC) (p64) (CD antigen CD132)

 IL2RG_MOUSE             Reviewed;         369 AA.
 P34902;
 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
 01-FEB-1994, sequence version 1.
 02-DEC-2020, entry version 184.
 RecName: Full=Cytokine receptor common subunit gamma;
 AltName: Full=Interleukin-2 receptor subunit gamma;
          Short=IL-2 receptor subunit gamma;
          Short=IL-2R subunit gamma;
          Short=IL-2RG;
 AltName: Full=gammaC;
 AltName: Full=p64;
 AltName: CD_antigen=CD132;
 Flags: Precursor;
 Name=Il2rg;
 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=8503926; DOI=10.1006/bbrc.1993.1631;
 Kumaki S., Kondo M., Takeshita T., Asao H., Nakamura M., Sugamura K.;
 "Cloning of the mouse interleukin 2 receptor gamma chain: demonstration of
 functional differences between the mouse and human receptors.";
 Biochem. Biophys. Res. Commun. 193:356-363(1993).
 [2]
 NUCLEOTIDE SEQUENCE [MRNA].
 STRAIN=CBA/CaJ;
 PubMed=8378320; DOI=10.1073/pnas.90.18.8464;
 Cao X., Kozak C.A., Liu Y.J., Noguchi M., O'Connell E., Leonard W.J.;
 "Characterization of cDNAs encoding the murine interleukin 2 receptor (IL-
 2R) gamma chain: chromosomal mapping and tissue specificity of IL-2R gamma
 chain expression.";
 Proc. Natl. Acad. Sci. U.S.A. 90:8464-8468(1993).
 [3]
 NUCLEOTIDE SEQUENCE [MRNA].
 PubMed=8359699; DOI=10.1016/0378-1119(93)90436-7;
 Kobayashi N., Nakagawa S., Minami Y., Taniguchi T., Kono T.;
 "Cloning and sequencing of the cDNA encoding a mouse IL-2 receptor gamma.";
 Gene 130:303-304(1993).
 [4]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
 PubMed=7805729; DOI=10.1002/eji.1830241214;
 Disanto J.P., Certain S., Wilson A., Macdonald H.R., Avner P., Fischer A.,
 de Saint Basile G.;
 "The murine interleukin-2 receptor gamma chain gene: organization,
 chromosomal localization and expression in the adult thymus.";
 Eur. J. Immunol. 24:3014-3018(1994).
 [5]
 NUCLEOTIDE SEQUENCE.
 STRAIN=B6.S;
 PubMed=8750189; DOI=10.1007/bf01052626;
 Chiu R.K., Droll A., Cooper D.L., Dougherty S.T., Dirks J.F.,
 Dougherty G.J.;
 "Molecular mechanisms regulating the hyaluronan binding activity of the
 adhesion protein CD44.";
 J. Neurooncol. 26:231-239(1995).
 [6]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
 STRAIN=FVB/N; TISSUE=Salivary gland;
 PubMed=15489334; DOI=10.1101/gr.2596504;
 The MGC Project Team;
 "The status, quality, and expansion of the NIH full-length cDNA project:
 the Mammalian Gene Collection (MGC).";
 Genome Res. 14:2121-2127(2004).
 -!- FUNCTION: Common subunit for the receptors for a variety of
     interleukins. Probably in association with IL15RA, involved in the
     stimulation of neutrophil phagocytosis by IL15 (By similarity).
     {ECO:0000250|UniProtKB:P31785}.
 -!- SUBUNIT: The gamma subunit is common to the IL2, IL4, IL7, IL15, IL21
     and probably also the IL13 receptors. Interacts with SHB upon
     interleukin stimulation (By similarity). {ECO:0000250}.
 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P31785};
     Single-pass type I membrane protein {ECO:0000255}. Cell surface
     {ECO:0000250|UniProtKB:P31785}.
 -!- 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.
 -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 5
     subfamily. {ECO:0000305}.
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 EMBL; D13821; BAA02974.1; -; mRNA.
 EMBL; U21795; AAA64279.1; -; Genomic_DNA.
 EMBL; D13565; BAA02760.1; -; mRNA.
 EMBL; L20048; AAA39286.1; -; mRNA.
 EMBL; S75852; AAB32904.1; -; Genomic_DNA.
 EMBL; S75844; AAB32904.1; JOINED; Genomic_DNA.
 EMBL; S75845; AAB32904.1; JOINED; Genomic_DNA.
 EMBL; S75847; AAB32904.1; JOINED; Genomic_DNA.
 EMBL; S75848; AAB32904.1; JOINED; Genomic_DNA.
 EMBL; S75849; AAB32904.1; JOINED; Genomic_DNA.
 EMBL; S75850; AAB32904.1; JOINED; Genomic_DNA.
 EMBL; S75851; AAB32904.1; JOINED; Genomic_DNA.
 EMBL; X75337; CAA53085.1; -; mRNA.
 EMBL; BC014720; AAH14720.1; -; mRNA.
 CCDS; CCDS30312.1; -.
 PIR; I49280; I49280.
 RefSeq; NP_038591.1; NM_013563.4.
 PDB; 6DG5; X-ray; 2.52 A; C=56-254.
 PDBsum; 6DG5; -.
 SMR; P34902; -.
 IntAct; P34902; 3.
 STRING; 10090.ENSMUSP00000033664; -.
 GlyGen; P34902; 6 sites.
 iPTMnet; P34902; -.
 PhosphoSitePlus; P34902; -.
 SwissPalm; P34902; -.
 EPD; P34902; -.
 PaxDb; P34902; -.
 PRIDE; P34902; -.
 Ensembl; ENSMUST00000033664; ENSMUSP00000033664; ENSMUSG00000031304.
 GeneID; 16186; -.
 KEGG; mmu:16186; -.
 UCSC; uc009txc.1; mouse.
 CTD; 3561; -.
 MGI; MGI:96551; Il2rg.
 eggNOG; ENOG502S289; Eukaryota.
 GeneTree; ENSGT00510000048979; -.
 HOGENOM; CLU_060544_1_0_1; -.
 InParanoid; P34902; -.
 OMA; MPRIPNP; -.
 OrthoDB; 753404at2759; -.
 PhylomeDB; P34902; -.
 TreeFam; TF333657; -.
 BioGRID-ORCS; 16186; 0 hits in 17 CRISPR screens.
 ChiTaRS; Il2rg; mouse.
 PRO; PR:P34902; -.
 Proteomes; UP000000589; Chromosome X.
 RNAct; P34902; protein.
 Bgee; ENSMUSG00000031304; Expressed in lymph node and 211 other tissues.
 ExpressionAtlas; P34902; baseline and differential.
 Genevisible; P34902; MM.
 GO; GO:0009986; C:cell surface; ISS:UniProtKB.
 GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
 GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
 GO; GO:0005886; C:plasma membrane; TAS:Reactome.
 GO; GO:0043235; C:receptor complex; IBA:GO_Central.
 GO; GO:0019955; F:cytokine binding; IBA:GO_Central.
 GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central.
 GO; GO:0042010; F:interleukin-15 receptor activity; ISS:UniProtKB.
 GO; GO:0019976; F:interleukin-2 binding; IPI:MGI.
 GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
 GO; GO:0035723; P:interleukin-15-mediated signaling pathway; ISS:UniProtKB.
 GO; GO:0045579; P:positive regulation of B cell differentiation; IMP:MGI.
 GO; GO:0032831; P:positive regulation of CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation; IMP:MGI.
 GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI.
 GO; GO:0045621; P:positive regulation of lymphocyte differentiation; IMP:MGI.
 GO; GO:0050766; P:positive regulation of phagocytosis; ISS:UniProtKB.
 GO; GO:0033089; P:positive regulation of T cell differentiation in thymus; IMP:MGI.
 GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
 CDD; cd00063; FN3; 1.
 Gene3D; 2.60.40.10; -; 2.
 InterPro; IPR003961; FN3_dom.
 InterPro; IPR036116; FN3_sf.
 InterPro; IPR003531; Hempt_rcpt_S_F1_CS.
 InterPro; IPR013783; Ig-like_fold.
 InterPro; IPR015321; TypeI_recpt_CBD.
 Pfam; PF00041; fn3; 1.
 Pfam; PF09240; IL6Ra-bind; 1.
 SMART; SM00060; FN3; 1.
 SUPFAM; SSF49265; SSF49265; 2.
 PROSITE; PS50853; FN3; 1.
 PROSITE; PS01355; HEMATOPO_REC_S_F1; 1.
 1: Evidence at protein level;
 3D-structure; Cell membrane; Disulfide bond; Glycoprotein; Membrane;
 Receptor; Reference proteome; Signal; Transmembrane; Transmembrane helix.
 SIGNAL          1..22
                 /evidence="ECO:0000250"
 CHAIN           23..369
                 /note="Cytokine receptor common subunit gamma"
                 /id="PRO_0000010867"
 TOPO_DOM        23..263
                 /note="Extracellular"
                 /evidence="ECO:0000255"
 TRANSMEM        264..284
                 /note="Helical"
                 /evidence="ECO:0000255"
 TOPO_DOM        285..369
                 /note="Cytoplasmic"
                 /evidence="ECO:0000255"
 DOMAIN          156..254
                 /note="Fibronectin type-III"
                 /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
 MOTIF           238..242
                 /note="WSXWS motif"
 MOTIF           286..294
                 /note="Box 1 motif"
 CARBOHYD        71
                 /note="N-linked (GlcNAc...) asparagine"
                 /evidence="ECO:0000255"
 CARBOHYD        75
                 /note="N-linked (GlcNAc...) asparagine"
                 /evidence="ECO:0000255"
 CARBOHYD        84
                 /note="N-linked (GlcNAc...) asparagine"
                 /evidence="ECO:0000255"
 CARBOHYD        96
                 /note="N-linked (GlcNAc...) asparagine"
                 /evidence="ECO:0000255"
 CARBOHYD        159
                 /note="N-linked (GlcNAc...) asparagine"
                 /evidence="ECO:0000255"
 CARBOHYD        164
                 /note="N-linked (GlcNAc...) asparagine"
                 /evidence="ECO:0000255"
 DISULFID        62..72
                 /evidence="ECO:0000255"
 DISULFID        102..115
                 /evidence="ECO:0000255"
 STRAND          61..65
                 /evidence="ECO:0000244|PDB:6DG5"
 TURN            66..68
                 /evidence="ECO:0000244|PDB:6DG5"
 STRAND          69..73
                 /evidence="ECO:0000244|PDB:6DG5"
 HELIX           76..78
                 /evidence="ECO:0000244|PDB:6DG5"
 STRAND          79..81
                 /evidence="ECO:0000244|PDB:6DG5"
 STRAND          86..92
                 /evidence="ECO:0000244|PDB:6DG5"
 STRAND          103..108
                 /evidence="ECO:0000244|PDB:6DG5"
 STRAND          111..118
                 /evidence="ECO:0000244|PDB:6DG5"
 HELIX           119..121
                 /evidence="ECO:0000244|PDB:6DG5"
 STRAND          128..133
                 /evidence="ECO:0000244|PDB:6DG5"
 STRAND          141..146
                 /evidence="ECO:0000244|PDB:6DG5"
 HELIX           148..150
                 /evidence="ECO:0000244|PDB:6DG5"
 STRAND          151..153
                 /evidence="ECO:0000244|PDB:6DG5"
 STRAND          158..163
                 /evidence="ECO:0000244|PDB:6DG5"
 STRAND          165..168
                 /evidence="ECO:0000244|PDB:6DG5"
 STRAND          170..175
                 /evidence="ECO:0000244|PDB:6DG5"
 STRAND          177..179
                 /evidence="ECO:0000244|PDB:6DG5"
 TURN            181..183
                 /evidence="ECO:0000244|PDB:6DG5"
 STRAND          185..191
                 /evidence="ECO:0000244|PDB:6DG5"
 STRAND          199..206
                 /evidence="ECO:0000244|PDB:6DG5"
 STRAND          208..211
                 /evidence="ECO:0000244|PDB:6DG5"
 STRAND          216..218
                 /evidence="ECO:0000244|PDB:6DG5"
 STRAND          220..227
                 /evidence="ECO:0000244|PDB:6DG5"
 STRAND          230..232
                 /evidence="ECO:0000244|PDB:6DG5"
 STRAND          245..247
                 /evidence="ECO:0000244|PDB:6DG5"
 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

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