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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