ID IL2RG_HUMAN Reviewed; 369 AA. AC P31785; Q5FC12; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 1. DT 27-MAR-2024, entry version 242. 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 Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE. RX PubMed=1631559; DOI=10.1126/science.1631559; RA Takeshita T., Asao H., Ohtani K., Ishii N., Kumaki S., Tanaka N., RA Munakata H., Nakamura M., Sugamura K.; RT "Cloning of the gamma chain of the human IL-2 receptor."; RL Science 257:379-382(1992). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Liver; RX PubMed=8514792; DOI=10.1016/s0021-9258(19)38691-0; RA Noguchi M., Adelstein S., Cao X., Leonard W.J.; RT "Characterization of the human interleukin-2 receptor gamma chain gene."; RL J. Biol. Chem. 268:13601-13608(1993). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS XSCID ASP-114 AND ASN-153. RX PubMed=8401490; DOI=10.1093/hmg/2.8.1099; RA Puck J.M., Deschenes S.M., Porter J.C., Dutra A.S., Brown C.J., Willard H., RA Henthorn P.S.; RT "The interleukin-2 receptor gamma chain maps to Xq13.1 and is mutated in X- RT linked severe combined immunodeficiency, SCIDX1."; RL Hum. Mol. Genet. 2:1099-1104(1993). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RA Hayashi A., Sameshima E., Tabata Y., Iida K., Mitsuyama M., Kanai S., RA Furuya T., Saito T.; RT "IL2RG mRNA, nirs splice variant 2."; RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LYS-109. RG SeattleSNPs variation discovery resource; RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=B-cell; 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 [8] RP IDENTIFICATION AS A IL4R SUBUNIT. RX PubMed=8266076; DOI=10.1126/science.8266076; RA Kondo M., Takeshita T., Ishii N., Nakamura M., Watanabe S., Arai K., RA Sugamura K.; RT "Sharing of the interleukin-2 (IL-2) receptor gamma chain between receptors RT for IL-2 and IL-4."; RL Science 262:1874-1877(1993). RN [9] RP IDENTIFICATION AS A IL4R SUBUNIT. RX PubMed=8266078; DOI=10.1126/science.8266078; RA Russell S.M., Kkegan A.D., Harada N., Nakamura Y., Noguchi M., Leland P., RA Friedmann M.C., Miyajima A., Puri R.K., Paul W.E., Leonard W.J.; RT "Interleukin-2 receptor gamma chain: a functional component of the RT interleukin-4 receptor."; RL Science 262:1880-1883(1993). RN [10] RP IDENTIFICATION AS A IL7R SUBUNIT. RX PubMed=8266077; DOI=10.1126/science.8266077; RA Noguchi M., Nakamura Y., Russell S.M., Ziegler S.F., Tsang M., Cao X., RA Leonard W.J.; RT "Interleukin-2 receptor gamma chain: a functional component of the RT interleukin-7 receptor."; RL Science 262:1877-1880(1993). RN [11] RP INTERACTION WITH HTLV-1 ACCESSORY PROTEIN P12I (MICROBIAL INFECTION). RX PubMed=8648694; DOI=10.1128/jvi.70.6.3599-3605.1996; RA Mulloy J.C., Crownley R.W., Fullen J., Leonard W.J., Franchini G.; RT "The human T-cell leukemia/lymphotropic virus type 1 p12I proteins bind the RT interleukin-2 receptor beta and gammac chains and affects their expression RT on the cell surface."; RL J. Virol. 70:3599-3605(1996). RN [12] RP INTERACTION WITH SHB. RX PubMed=12200137; DOI=10.1016/s0006-291x(02)02016-8; RA Lindholm C.K.; RT "IL-2 receptor signaling through the Shb adapter protein in T and NK RT cells."; RL Biochem. Biophys. Res. Commun. 296:929-936(2002). RN [13] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=15123770; DOI=10.1189/jlb.0605298; RA Ratthe C., Girard D.; RT "Interleukin-15 enhances human neutrophil phagocytosis by a Syk-dependent RT mechanism: importance of the IL-15Ralpha chain."; RL J. Leukoc. Biol. 76:162-168(2004). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-292, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [15] RP 3D-STRUCTURE MODELING OF 57-248. RX PubMed=7529123; DOI=10.1016/s0969-2126(94)00085-9; RA Bamborough P., Hedgecock C.J., Richards W.G.; RT "The interleukin-2 and interleukin-4 receptors studied by molecular RT modelling."; RL Structure 2:839-851(1994). RN [16] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 56-254 IN COMPLEX WITH IL2; IL2RA RP AND IL2RB, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-71; ASN-84 AND RP ASN-159. RX PubMed=16293754; DOI=10.1126/science.1117893; RA Wang X., Rickert M., Garcia K.C.; RT "Structure of the quaternary complex of interleukin-2 with its alpha, beta, RT and gammac receptors."; RL Science 310:1159-1163(2005). RN [17] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 23-255 IN COMPLEX WITH IL2; IL2RA RP AND IL2RB, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-71; ASN-84 AND RP ASN-159. RX PubMed=16477002; DOI=10.1073/pnas.0511161103; RA Stauber D.J., Debler E.W., Horton P.A., Smith K.A., Wilson I.A.; RT "Crystal structure of the IL-2 signaling complex: paradigm for a RT heterotrimeric cytokine receptor."; RL Proc. Natl. Acad. Sci. U.S.A. 103:2788-2793(2006). RN [18] RP VARIANTS XSCID PHE-115; CYS-240 AND ILE-241. RX PubMed=8299698; DOI=10.1002/eji.1830240232; RA Disanto J.P., Dautry-Varsat A., Certain S., Fischer A., de Saint Basile G.; RT "Interleukin-2 (IL-2) receptor gamma chain mutations in X-linked severe RT combined immunodeficiency disease result in the loss of high-affinity IL-2 RT receptor binding."; RL Eur. J. Immunol. 24:475-479(1994). RN [19] RP VARIANT XSCID LYS-68. RX PubMed=8088810; DOI=10.1006/geno.1994.1265; RA Markiewicz S., Subtil A., Dautry-Varsat A., Fischer A., de Saint Basile G.; RT "Detection of three nonsense mutations and one missense mutation in the RT interleukin-2 receptor gamma chain gene in SCIDX1 that differently affect RT the mRNA processing."; RL Genomics 21:291-293(1994). RN [20] RP VARIANT XSCID HIS-162. RX PubMed=8027558; RA Ishii N., Asao H., Kimura Y., Takeshita T., Nakamura M., Tsuchiya S., RA Konno T., Maeda M., Uchiyama T., Sugamura K.; RT "Impairment of ligand binding and growth signaling of mutant IL-2 receptor RT gamma-chains in patients with X-linked severe combined immunodeficiency."; RL J. Immunol. 153:1310-1317(1994). RN [21] RP VARIANT XSCID ASN-39. RX PubMed=7937790; DOI=10.1073/pnas.91.20.9466; RA Disanto J.P., Rieux-Laucat F., Dautry-Varsat A., Fischer A., RA de Saint Basile G.; RT "Defective human interleukin 2 receptor gamma chain in an atypical X RT chromosome-linked severe combined immunodeficiency with peripheral T RT cells."; RL Proc. Natl. Acad. Sci. U.S.A. 91:9466-9470(1994). RN [22] RP VARIANTS XSCID CYS-226 AND HIS-226. RX PubMed=7668284; RA Pepper A.E., Buckley R.H., Small T.N., Puck J.M.; RT "Two mutational hotspots in the interleukin-2 receptor gamma chain gene RT causing human X-linked severe combined immunodeficiency."; RL Am. J. Hum. Genet. 57:564-571(1995). RN [23] RP VARIANT XSCID SER-183. RX PubMed=7557965; DOI=10.1007/bf00191801; RA Clark P.A., Lester T., Genet S., Jones A.M., Hendriks R., Levinsky R.L., RA Kinnon C.; RT "Screening for mutations causing X-linked severe combined immunodeficiency RT in the IL-2R gamma chain gene by single-strand conformation polymorphism RT analysis."; RL Hum. Genet. 96:427-432(1995). RN [24] RP VARIANT XSCID GLN-HIS-TRP-237 INS. RX PubMed=7860773; DOI=10.1172/jci117740; RA Puck J.M., Pepper A.E., Bedard P.-M., Laframboise R.; RT "Female germ line mosaicism as the origin of a unique IL-2 receptor gamma- RT chain mutation causing X-linked severe combined immunodeficiency."; RL J. Clin. Invest. 95:895-899(1995). RN [25] RP VARIANT XCID GLN-293. RX PubMed=7883965; DOI=10.1172/jci117765; RA Schmalstieg F.C., Leonard W.J., Noguchi M., Berg M., Rudloff H.E., RA Denney R.M., Dave S.K., Brooks E.G., Goldman A.S.; RT "Missense mutation in exon 7 of the common gamma chain gene causes a RT moderate form of X-linked combined immunodeficiency."; RL J. Clin. Invest. 95:1169-1173(1995). RN [26] RP VARIANT XSCID ARG-115. RX PubMed=8900089; DOI=10.1056/nejm199611213352104; RA Stephan V., Wahn V., Le Deist F., Dirksen U., Broeker B., RA Mueller-Fleckenstein I., Horneff G., Schroten H., Fischer A., RA de Saint Basile G.; RT "Atypical X-linked severe combined immunodeficiency due to possible RT spontaneous reversion of the genetic defect in T cells."; RL N. Engl. J. Med. 335:1563-1567(1996). RN [27] RP VARIANT XSCID GLN-285. RX PubMed=9150740; DOI=10.1007/s004390050428; RA Jones A.M., Clark P.A., Katz F., Genet S., McMahon C., Alterman L., RA Cant A., Kinnon C.; RT "B-cell-negative severe combined immunodeficiency associated with a common RT gamma chain mutation."; RL Hum. Genet. 99:677-680(1997). RN [28] RP VARIANT XSCID TRP-224. RX PubMed=9049783; DOI=10.1023/a:1027332327827; RA O'Marcaigh A.S., Puck J.M., Pepper A.E., De Santes K., Cowan M.J.; RT "Maternal mosaicism for a novel interleukin-2 receptor gamma-chain mutation RT causing X-linked severe combined immunodeficiency in a Navajo kindred."; RL J. Clin. Immunol. 17:29-33(1997). RN [29] RP VARIANT XCID CYS-222. RX PubMed=9399950; DOI=10.1172/jci119858; RA Sharfe N., Shahar M., Roifman C.M.; RT "An interleukin-2 receptor gamma chain mutation with normal thymus RT morphology."; RL J. Clin. Invest. 100:3036-3043(1997). CC -!- FUNCTION: Common subunit for the receptors for a variety of CC interleukins. Probably in association with IL15RA, involved in the CC stimulation of neutrophil phagocytosis by IL15 (PubMed:15123770). CC {ECO:0000269|PubMed:15123770}. 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. Interacts with IL9 (By similarity). CC {ECO:0000250|UniProtKB:P34902, ECO:0000269|PubMed:12200137, CC ECO:0000269|PubMed:16293754, ECO:0000269|PubMed:16477002}. CC -!- SUBUNIT: (Microbial infection) Interacts with HTLV-1 accessory protein CC p12I. {ECO:0000269|PubMed:8648694}. CC -!- INTERACTION: CC P31785; P13232: IL7; NbExp=2; IntAct=EBI-80475, EBI-80516; CC P31785; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-80475, EBI-10171774; CC P31785; Q6L8G8: KRTAP5-7; NbExp=3; IntAct=EBI-80475, EBI-11987425; CC P31785; Q7Z3S9: NOTCH2NLA; NbExp=4; IntAct=EBI-80475, EBI-945833; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15123770}; CC Single-pass type I membrane protein {ECO:0000255}. Cell surface CC {ECO:0000269|PubMed:15123770}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P31785-1; Sequence=Displayed; CC Name=2; CC IsoId=P31785-2; Sequence=VSP_047581, VSP_047582; 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 -!- DISEASE: Severe combined immunodeficiency X-linked T-cell-negative/B- CC cell-positive/NK-cell-negative (XSCID) [MIM:300400]: A form of severe CC combined immunodeficiency (SCID), a genetically and clinically CC heterogeneous group of rare congenital disorders characterized by CC impairment of both humoral and cell-mediated immunity, leukopenia, and CC low or absent antibody levels. Patients present in infancy recurrent, CC persistent infections by opportunistic organisms. The common CC characteristic of all types of SCID is absence of T-cell-mediated CC cellular immunity due to a defect in T-cell development. CC {ECO:0000269|PubMed:7557965, ECO:0000269|PubMed:7668284, CC ECO:0000269|PubMed:7860773, ECO:0000269|PubMed:7937790, CC ECO:0000269|PubMed:8027558, ECO:0000269|PubMed:8088810, CC ECO:0000269|PubMed:8299698, ECO:0000269|PubMed:8401490, CC ECO:0000269|PubMed:8900089, ECO:0000269|PubMed:9049783, CC ECO:0000269|PubMed:9150740}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: X-linked combined immunodeficiency (XCID) [MIM:312863]: Less CC severe form of X-linked immunodeficiency with a less severe degree of CC deficiency in cellular and humoral immunity than that seen in XSCID. CC {ECO:0000269|PubMed:7883965, ECO:0000269|PubMed:9399950}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 5 CC subfamily. {ECO:0000305}. CC -!- WEB RESOURCE: Name=IL2RGbase; Note=X-linked SCID mutation database; CC URL="http://research.nhgri.nih.gov/scid/"; CC -!- WEB RESOURCE: Name=SeattleSNPs; CC URL="http://pga.gs.washington.edu/data/il2rg/"; 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; D11086; BAA01857.1; -; mRNA. DR EMBL; L12183; AAA59145.1; -; Genomic_DNA. DR EMBL; L12178; AAA59145.1; JOINED; Genomic_DNA. DR EMBL; L12176; AAA59145.1; JOINED; Genomic_DNA. DR EMBL; L12177; AAA59145.1; JOINED; Genomic_DNA. DR EMBL; L12179; AAA59145.1; JOINED; Genomic_DNA. DR EMBL; L12180; AAA59145.1; JOINED; Genomic_DNA. DR EMBL; L12181; AAA59145.1; JOINED; Genomic_DNA. DR EMBL; L12182; AAA59145.1; JOINED; Genomic_DNA. DR EMBL; L19546; AAC37524.1; -; Genomic_DNA. DR EMBL; AB102794; BAD89385.1; -; mRNA. DR EMBL; AY692262; AAT85803.1; -; Genomic_DNA. DR EMBL; AL590764; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC014972; AAH14972.1; -; mRNA. DR CCDS; CCDS14406.1; -. [P31785-1] DR PIR; A42565; A42565. DR RefSeq; NP_000197.1; NM_000206.2. [P31785-1] DR PDB; 2B5I; X-ray; 2.30 A; C=56-254. DR PDB; 2ERJ; X-ray; 3.00 A; C/G=23-255. DR PDB; 3BPL; X-ray; 2.93 A; C=56-254. DR PDB; 3QAZ; X-ray; 3.80 A; C/F/I/L/O/R/U/X/a/d/g/j=56-254. DR PDB; 3QB7; X-ray; 3.24 A; C/D=55-254. DR PDB; 4GS7; X-ray; 2.35 A; C=55-254. DR PDB; 5M5E; X-ray; 2.30 A; C=23-262. DR PDB; 6OEL; X-ray; 3.10 A; C=61-249. DR PDB; 7S2R; X-ray; 2.49 A; A=54-254. DR PDB; 8ENT; X-ray; 2.83 A; C/F/I=55-254. DR PDB; 8EPA; EM; 3.40 A; I=23-262. DR PDBsum; 2B5I; -. DR PDBsum; 2ERJ; -. DR PDBsum; 3BPL; -. DR PDBsum; 3QAZ; -. DR PDBsum; 3QB7; -. DR PDBsum; 4GS7; -. DR PDBsum; 5M5E; -. DR PDBsum; 6OEL; -. DR PDBsum; 7S2R; -. DR PDBsum; 8ENT; -. DR PDBsum; 8EPA; -. DR AlphaFoldDB; P31785; -. DR EMDB; EMD-28278; -. DR EMDB; EMD-28523; -. DR SMR; P31785; -. DR BioGRID; 109776; 26. DR CORUM; P31785; -. DR DIP; DIP-173N; -. DR IntAct; P31785; 18. DR STRING; 9606.ENSP00000363318; -. DR ChEMBL; CHEMBL2364167; -. DR ChEMBL; CHEMBL4665588; -. DR ChEMBL; CHEMBL4665592; -. DR DrugBank; DB00041; Aldesleukin. DR DrugBank; DB00004; Denileukin diftitox. DR DrugBank; DB05943; Resatorvid. DR DrugCentral; P31785; -. DR GuidetoPHARMACOLOGY; 2303; -. DR GlyCosmos; P31785; 6 sites, No reported glycans. DR GlyGen; P31785; 8 sites. DR iPTMnet; P31785; -. DR PhosphoSitePlus; P31785; -. DR BioMuta; IL2RG; -. DR DMDM; 400048; -. DR EPD; P31785; -. DR MassIVE; P31785; -. DR MaxQB; P31785; -. DR PaxDb; 9606-ENSP00000363318; -. DR PeptideAtlas; P31785; -. DR ProteomicsDB; 54802; -. [P31785-1] DR ProteomicsDB; 62802; -. DR ABCD; P31785; 1 sequenced antibody. DR Antibodypedia; 27479; 696 antibodies from 36 providers. DR CPTC; P31785; 1 antibody. DR DNASU; 3561; -. DR Ensembl; ENST00000374202.7; ENSP00000363318.3; ENSG00000147168.14. [P31785-1] DR GeneID; 3561; -. DR KEGG; hsa:3561; -. DR MANE-Select; ENST00000374202.7; ENSP00000363318.3; NM_000206.3; NP_000197.1. DR UCSC; uc004dyw.4; human. [P31785-1] DR AGR; HGNC:6010; -. DR CTD; 3561; -. DR DisGeNET; 3561; -. DR GeneCards; IL2RG; -. DR GeneReviews; IL2RG; -. DR HGNC; HGNC:6010; IL2RG. DR HPA; ENSG00000147168; Tissue enhanced (intestine, lymphoid tissue). DR MalaCards; IL2RG; -. DR MIM; 300400; phenotype. DR MIM; 308380; gene. DR MIM; 312863; phenotype. DR neXtProt; NX_P31785; -. DR OpenTargets; ENSG00000147168; -. DR Orphanet; 39041; Omenn syndrome. DR Orphanet; 276; T-B+ severe combined immunodeficiency due to gamma chain deficiency. DR PharmGKB; PA196; -. DR VEuPathDB; HostDB:ENSG00000147168; -. DR eggNOG; ENOG502S289; Eukaryota. DR GeneTree; ENSGT00510000048979; -. DR HOGENOM; CLU_060544_1_0_1; -. DR InParanoid; P31785; -. DR OMA; TAGCWLQ; -. DR OrthoDB; 5174285at2759; -. DR PhylomeDB; P31785; -. DR TreeFam; TF333657; -. DR PathwayCommons; P31785; -. DR Reactome; R-HSA-1266695; Interleukin-7 signaling. DR Reactome; R-HSA-5673001; RAF/MAP kinase cascade. DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling. DR Reactome; R-HSA-8983432; Interleukin-15 signaling. DR Reactome; R-HSA-8985947; Interleukin-9 signaling. DR Reactome; R-HSA-9020558; Interleukin-2 signaling. DR Reactome; R-HSA-9020958; Interleukin-21 signaling. DR Reactome; R-HSA-912526; Interleukin receptor SHC signaling. DR Reactome; R-HSA-9701898; STAT3 nuclear events downstream of ALK signaling. DR SignaLink; P31785; -. DR SIGNOR; P31785; -. DR BioGRID-ORCS; 3561; 14 hits in 788 CRISPR screens. DR ChiTaRS; IL2RG; human. DR EvolutionaryTrace; P31785; -. DR GeneWiki; Common_gamma_chain; -. DR GenomeRNAi; 3561; -. DR Pharos; P31785; Tclin. DR PRO; PR:P31785; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; P31785; Protein. DR Bgee; ENSG00000147168; Expressed in granulocyte and 149 other cell types or tissues. DR ExpressionAtlas; P31785; baseline and differential. DR GO; GO:0009986; C:cell surface; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA. DR GO; GO:0005768; C:endosome; TAS:Reactome. DR GO; GO:0009897; C:external side of plasma membrane; ISS:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0043235; C:receptor complex; IBA:GO_Central. DR GO; GO:0015026; F:coreceptor activity; IDA:UniProt. 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; IDA:UniProtKB. DR GO; GO:0019976; F:interleukin-2 binding; ISS:UniProtKB. DR GO; GO:0002361; P:CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation; IEA:Ensembl. DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central. DR GO; GO:0010467; P:gene expression; IEA:Ensembl. DR GO; GO:0006955; P:immune response; TAS:ProtInc. DR GO; GO:0035723; P:interleukin-15-mediated signaling pathway; IMP:UniProtKB. DR GO; GO:0038110; P:interleukin-2-mediated signaling pathway; IDA:UniProt. DR GO; GO:0035771; P:interleukin-4-mediated signaling pathway; IEA:GOC. DR GO; GO:0038111; P:interleukin-7-mediated signaling pathway; IEA:GOC. DR GO; GO:0038113; P:interleukin-9-mediated signaling pathway; IDA:UniProt. DR GO; GO:0002335; P:mature B cell differentiation; IEA:Ensembl. DR GO; GO:0045579; P:positive regulation of B cell differentiation; IEA:Ensembl. DR GO; GO:0032831; P:positive regulation of CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation; IEA:Ensembl. DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl. DR GO; GO:0050766; P:positive regulation of phagocytosis; IMP:UniProtKB. DR GO; GO:0033089; P:positive regulation of T cell differentiation in thymus; IEA:Ensembl. DR GO; GO:0007165; P:signal transduction; NAS:ProtInc. DR GO; GO:0033077; P:T cell differentiation in thymus; IEA:Ensembl. 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 SUPFAM; SSF49265; Fibronectin type III; 2. DR PROSITE; PS50853; FN3; 1. DR PROSITE; PS01355; HEMATOPO_REC_S_F1; 1. DR Genevisible; P31785; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; KW Direct protein sequencing; Disease variant; Disulfide bond; Glycoprotein; KW Host-virus interaction; Membrane; Phosphoprotein; Receptor; KW Reference proteome; SCID; Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1..22 FT CHAIN 23..369 FT /note="Cytokine receptor common subunit gamma" FT /id="PRO_0000010866" FT TOPO_DOM 23..262 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 263..283 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 284..369 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 156..253 FT /note="Fibronectin type-III" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316" FT MOTIF 237..241 FT /note="WSXWS motif" FT MOTIF 286..294 FT /note="Box 1 motif" FT MOD_RES 292 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19690332" FT CARBOHYD 24 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 71 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16293754, FT ECO:0000269|PubMed:16477002" 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:0000269|PubMed:16293754, FT ECO:0000269|PubMed:16477002" FT CARBOHYD 159 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16293754, FT ECO:0000269|PubMed:16477002" FT CARBOHYD 249 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 62..72 FT DISULFID 102..115 FT DISULFID 182..231 FT VAR_SEQ 1..8 FT /note="MLKPSLPF -> MGMKTPQL (in isoform 2)" FT /evidence="ECO:0000303|Ref.4" FT /id="VSP_047581" FT VAR_SEQ 9..198 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|Ref.4" FT /id="VSP_047582" FT VARIANT 39 FT /note="D -> N (in XSCID)" FT /evidence="ECO:0000269|PubMed:7937790" FT /id="VAR_002668" FT VARIANT 44 FT /note="T -> S (in dbSNP:rs7885041)" FT /id="VAR_059301" FT VARIANT 62 FT /note="C -> G (in XSCID)" FT /id="VAR_002669" FT VARIANT 68 FT /note="E -> G (in XSCID)" FT /id="VAR_002670" FT VARIANT 68 FT /note="E -> K (in XSCID; dbSNP:rs1057520644)" FT /evidence="ECO:0000269|PubMed:8088810" FT /id="VAR_002671" FT VARIANT 84 FT /note="N -> K (in XSCID)" FT /id="VAR_002672" FT VARIANT 89 FT /note="Y -> C (in XSCID)" FT /id="VAR_002673" FT VARIANT 105 FT /note="Y -> C (in XSCID; dbSNP:rs193922347)" FT /id="VAR_002674" FT VARIANT 109 FT /note="E -> K (in dbSNP:rs17875899)" FT /evidence="ECO:0000269|Ref.5" FT /id="VAR_020611" FT VARIANT 114 FT /note="G -> D (in XSCID; dbSNP:rs111033620)" FT /evidence="ECO:0000269|PubMed:8401490" FT /id="VAR_002675" FT VARIANT 115 FT /note="C -> F (in XSCID)" FT /evidence="ECO:0000269|PubMed:8299698" FT /id="VAR_002676" FT VARIANT 115 FT /note="C -> R (in XSCID; atypical; dbSNP:rs111033622)" FT /evidence="ECO:0000269|PubMed:8900089" FT /id="VAR_002677" FT VARIANT 123 FT /note="H -> P (in XSCID)" FT /id="VAR_002678" FT VARIANT 125 FT /note="Y -> N (in XSCID)" FT /id="VAR_002679" FT VARIANT 144 FT /note="Q -> P (in XSCID)" FT /id="VAR_002680" FT VARIANT 153 FT /note="I -> N (in XSCID; dbSNP:rs111033621)" FT /evidence="ECO:0000269|PubMed:8401490" FT /id="VAR_002681" FT VARIANT 156 FT /note="A -> V (in XSCID; dbSNP:rs1057521062)" FT /id="VAR_002682" FT VARIANT 162 FT /note="L -> H (in XSCID)" FT /evidence="ECO:0000269|PubMed:8027558" FT /id="VAR_002683" FT VARIANT 172 FT /note="L -> P (in XSCID)" FT /id="VAR_002684" FT VARIANT 172 FT /note="L -> Q (in XSCID)" FT /id="VAR_002685" FT VARIANT 182 FT /note="C -> R (in XSCID)" FT /id="VAR_002686" FT VARIANT 183 FT /note="L -> S (in XSCID)" FT /evidence="ECO:0000269|PubMed:7557965" FT /id="VAR_002687" FT VARIANT 222 FT /note="R -> C (in XCID; dbSNP:rs111033618)" FT /evidence="ECO:0000269|PubMed:9399950" FT /id="VAR_002688" FT VARIANT 224 FT /note="R -> W (in XSCID; dbSNP:rs869320658)" FT /evidence="ECO:0000269|PubMed:9049783" FT /id="VAR_002689" FT VARIANT 226 FT /note="R -> C (in XSCID; dbSNP:rs869320659)" FT /evidence="ECO:0000269|PubMed:7668284" FT /id="VAR_002690" FT VARIANT 226 FT /note="R -> H (in XSCID; dbSNP:rs869320660)" FT /evidence="ECO:0000269|PubMed:7668284" FT /id="VAR_002691" FT VARIANT 227 FT /note="F -> C (in XSCID)" FT /id="VAR_002692" FT VARIANT 230 FT /note="L -> P (in XSCID)" FT /id="VAR_002693" FT VARIANT 231 FT /note="C -> Y (in XSCID)" FT /id="VAR_002694" FT VARIANT 232 FT /note="G -> R (in XSCID; dbSNP:rs1569479909)" FT /id="VAR_002695" FT VARIANT 237 FT /note="W -> WQHW (in XSCID)" FT /evidence="ECO:0000269|PubMed:7860773" FT /id="VAR_002696" FT VARIANT 240 FT /note="W -> C (in XSCID)" FT /evidence="ECO:0000269|PubMed:8299698" FT /id="VAR_002697" FT VARIANT 241 FT /note="S -> I (in XSCID)" FT /evidence="ECO:0000269|PubMed:8299698" FT /id="VAR_002698" FT VARIANT 270 FT /note="M -> R (in XSCID)" FT /id="VAR_002699" FT VARIANT 285 FT /note="R -> Q (in XSCID; dbSNP:rs111033617)" FT /evidence="ECO:0000269|PubMed:9150740" FT /id="VAR_002701" FT VARIANT 293 FT /note="L -> Q (in XCID; dbSNP:rs137852510)" FT /evidence="ECO:0000269|PubMed:7883965" FT /id="VAR_002702" FT STRAND 61..65 FT /evidence="ECO:0007829|PDB:2B5I" FT TURN 66..68 FT /evidence="ECO:0007829|PDB:2B5I" FT STRAND 69..73 FT /evidence="ECO:0007829|PDB:2B5I" FT STRAND 78..81 FT /evidence="ECO:0007829|PDB:2B5I" FT STRAND 86..91 FT /evidence="ECO:0007829|PDB:2B5I" FT STRAND 94..96 FT /evidence="ECO:0007829|PDB:2B5I" FT STRAND 99..101 FT /evidence="ECO:0007829|PDB:4GS7" FT STRAND 103..108 FT /evidence="ECO:0007829|PDB:2B5I" FT STRAND 111..118 FT /evidence="ECO:0007829|PDB:2B5I" FT HELIX 119..121 FT /evidence="ECO:0007829|PDB:2B5I" FT STRAND 124..126 FT /evidence="ECO:0007829|PDB:3BPL" FT STRAND 128..133 FT /evidence="ECO:0007829|PDB:2B5I" FT STRAND 135..137 FT /evidence="ECO:0007829|PDB:4GS7" FT STRAND 141..146 FT /evidence="ECO:0007829|PDB:2B5I" FT HELIX 148..150 FT /evidence="ECO:0007829|PDB:2B5I" FT STRAND 151..153 FT /evidence="ECO:0007829|PDB:2B5I" FT STRAND 158..166 FT /evidence="ECO:0007829|PDB:2B5I" FT STRAND 169..175 FT /evidence="ECO:0007829|PDB:2B5I" FT HELIX 180..182 FT /evidence="ECO:0007829|PDB:5M5E" FT STRAND 184..191 FT /evidence="ECO:0007829|PDB:2B5I" FT STRAND 198..202 FT /evidence="ECO:0007829|PDB:2B5I" FT STRAND 207..210 FT /evidence="ECO:0007829|PDB:2B5I" FT STRAND 215..217 FT /evidence="ECO:0007829|PDB:3QB7" FT STRAND 219..226 FT /evidence="ECO:0007829|PDB:2B5I" FT STRAND 229..231 FT /evidence="ECO:0007829|PDB:2B5I" FT STRAND 244..246 FT /evidence="ECO:0007829|PDB:2B5I" SQ SEQUENCE 369 AA; 42287 MW; 3B6215246D610215 CRC64; MLKPSLPFTS LLFLQLPLLG VGLNTTILTP NGNEDTTADF FLTTMPTDSL SVSTLPLPEV QCFVFNVEYM NCTWNSSSEP QPTNLTLHYW YKNSDNDKVQ KCSHYLFSEE ITSGCQLQKK EIHLYQTFVV QLQDPREPRR QATQMLKLQN LVIPWAPENL TLHKLSESQL ELNWNNRFLN HCLEHLVQYR TDWDHSWTEQ SVDYRHKFSL PSVDGQKRYT FRVRSRFNPL CGSAQHWSEW SHPIHWGSNT SKENPFLFAL EAVVISVGSM GLIISLLCVY FWLERTMPRI PTLKNLEDLV TEYHGNFSAW SGVSKGLAES LQPDYSERLC LVSEIPPKGG ALGEGPGASP CNQHSPYWAP PCYTLKPET //