IL2RG_CANLF
ID IL2RG_CANLF Reviewed; 373 AA.
AC P40321;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 147.
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 Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Spleen;
RX PubMed=7829104; DOI=10.1006/geno.1994.1460;
RA Henthorn P.S., Somberg R.L., Fimiani V.M., Puck J.M., Patterson D.F.,
RA Felsburg P.J.;
RT "IL-2R gamma gene microdeletion demonstrates that canine X-linked severe
RT combined immunodeficiency is a homologue of the human disease.";
RL Genomics 23:69-74(1994).
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 (By similarity).
CC {ECO:0000250|UniProtKB:P31785}.
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). {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 -!- DISEASE: Note=Defects in IL2RG are the cause of a canine X-linked
CC severe combined immunodeficiency.
CC -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 5
CC subfamily. {ECO:0000305}.
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DR EMBL; U04361; AAC48403.1; -; mRNA.
DR PIR; A55718; A55718.
DR RefSeq; NP_001003201.1; NM_001003201.1.
DR AlphaFoldDB; P40321; -.
DR SMR; P40321; -.
DR STRING; 9612.ENSCAFP00000041465; -.
DR PaxDb; P40321; -.
DR Ensembl; ENSCAFT00040044402; ENSCAFP00040038772; ENSCAFG00040023814.
DR Ensembl; ENSCAFT00845030246; ENSCAFP00845023718; ENSCAFG00845017057.
DR GeneID; 403851; -.
DR KEGG; cfa:403851; -.
DR CTD; 3561; -.
DR VEuPathDB; HostDB:ENSCAFG00845017057; -.
DR eggNOG; ENOG502S289; Eukaryota.
DR GeneTree; ENSGT00510000048979; -.
DR HOGENOM; CLU_060544_1_0_1; -.
DR InParanoid; P40321; -.
DR OMA; NKDTSWT; -.
DR OrthoDB; 753404at2759; -.
DR TreeFam; TF333657; -.
DR Reactome; R-CFA-1266695; Interleukin-7 signaling.
DR Reactome; R-CFA-6785807; Interleukin-4 and Interleukin-13 signaling.
DR Reactome; R-CFA-8983432; Interleukin-15 signaling.
DR Reactome; R-CFA-8985947; Interleukin-9 signaling.
DR Reactome; R-CFA-9020558; Interleukin-2 signaling.
DR Reactome; R-CFA-9020958; Interleukin-21 signaling.
DR Reactome; R-CFA-912526; Interleukin receptor SHC signaling.
DR Proteomes; UP000002254; Chromosome X.
DR Bgee; ENSCAFG00000028978; Expressed in blood and 47 other tissues.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IEA:Ensembl.
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:0035723; P:interleukin-15-mediated signaling pathway; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0033089; P:positive regulation of T cell differentiation in thymus; IEA:Ensembl.
DR GO; GO:0033077; P:T cell differentiation in thymus; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; Membrane; Phosphoprotein;
KW Receptor; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..373
FT /note="Cytokine receptor common subunit gamma"
FT /id="PRO_0000010865"
FT TOPO_DOM 23..261
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..373
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 285..293
FT /note="Box 1 motif"
FT MOD_RES 291
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P31785"
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: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 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 CARBOHYD 249
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"
SQ SEQUENCE 373 AA; 42516 MW; 03A0DE1F8B089D8B CRC64;
MLKPPLPLRS LLFLQLSLLG VGLNSTVPMP NGNEDITPDF FLTATPSETL SVSSLPLPEV
QCFVFNVEYM NCTWNSSSEP RPTNLTLHYW YKNSNDDKVQ ECGHYLFSRE VTAGCWLQKE
EIHLYETFVV QLRDPREPRR QSTQKLKLQN LVIPWAPENL TLHNLSESQL ELSWSNRHLD
HCLEHVVQYR SDWDRSWTEQ SVDHRNSFSL PSVDGQKFYT FRVRSRYNPL CGSAQRWSEW
SHPIHWGSNT SKENPLFASE AVLIPLGSMG LIISLICVYY WLERSIPRIP TLKNLEDLVT
EYHGNFSAWS GVSKGLAESL QPDYSEWLCH VSEIPPKGGA PGEGPGGSPC SQHSPYWAPP
CYTLKPETGA LIP
