IL2RA_RAT
ID IL2RA_RAT Reviewed; 267 AA.
AC P26897;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Interleukin-2 receptor subunit alpha;
DE Short=IL-2 receptor subunit alpha;
DE Short=IL-2-RA;
DE Short=IL-2R subunit alpha;
DE Short=IL2-RA;
DE AltName: CD_antigen=CD25;
DE Flags: Precursor;
GN Name=Il2ra;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1889461; DOI=10.1002/eji.1830210922;
RA Page T.H., Dallman M.J.;
RT "Molecular cloning of cDNAs for the rat interleukin 2 receptor alpha and
RT beta chain genes: differentially regulated gene activity in response to
RT mitogenic stimulation.";
RL Eur. J. Immunol. 21:2133-2138(1991).
CC -!- FUNCTION: Receptor for interleukin-2. The receptor is involved in the
CC regulation of immune tolerance by controlling regulatory T cells
CC (TREGs) activity. TREGs suppress the activation and expansion of
CC autoreactive T-cells. {ECO:0000250|UniProtKB:P01589}.
CC -!- SUBUNIT: Non-covalent dimer of an alpha and a beta subunit. IL2R exists
CC in 3 different forms: a high affinity dimer, an intermediate affinity
CC monomer (beta subunit), and a low affinity monomer (alpha subunit). The
CC high and intermediate affinity forms also associate with a gamma
CC subunit (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
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DR EMBL; M55049; AAA41428.1; -; mRNA.
DR PIR; A46535; A46535.
DR RefSeq; NP_037295.1; NM_013163.1.
DR AlphaFoldDB; P26897; -.
DR SMR; P26897; -.
DR STRING; 10116.ENSRNOP00000066383; -.
DR GlyGen; P26897; 2 sites.
DR PaxDb; P26897; -.
DR Ensembl; ENSRNOT00000073144; ENSRNOP00000066383; ENSRNOG00000047647.
DR GeneID; 25704; -.
DR KEGG; rno:25704; -.
DR UCSC; RGD:2895; rat.
DR CTD; 3559; -.
DR RGD; 2895; Il2ra.
DR eggNOG; ENOG502SUAG; Eukaryota.
DR GeneTree; ENSGT00390000018872; -.
DR HOGENOM; CLU_089677_1_0_1; -.
DR InParanoid; P26897; -.
DR OMA; HYQCIQG; -.
DR OrthoDB; 1236351at2759; -.
DR PhylomeDB; P26897; -.
DR Reactome; R-RNO-5673001; RAF/MAP kinase cascade.
DR Reactome; R-RNO-9020558; Interleukin-2 signaling.
DR Reactome; R-RNO-912526; Interleukin receptor SHC signaling.
DR PRO; PR:P26897; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Bgee; ENSRNOG00000047647; Expressed in thymus and 11 other tissues.
DR Genevisible; P26897; RN.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019976; F:interleukin-2 binding; ISO:RGD.
DR GO; GO:0004911; F:interleukin-2 receptor activity; IPI:RGD.
DR GO; GO:0050798; P:activated T cell proliferation; IEA:Ensembl.
DR GO; GO:0006924; P:activation-induced cell death of T cells; ISO:RGD.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0002437; P:inflammatory response to antigenic stimulus; IMP:RGD.
DR GO; GO:0050728; P:negative regulation of inflammatory response; ISO:RGD.
DR GO; GO:0050672; P:negative regulation of lymphocyte proliferation; ISO:RGD.
DR GO; GO:0042130; P:negative regulation of T cell proliferation; ISO:RGD.
DR GO; GO:0007219; P:Notch signaling pathway; ISO:RGD.
DR GO; GO:0042104; P:positive regulation of activated T cell proliferation; ISO:RGD.
DR GO; GO:0045582; P:positive regulation of T cell differentiation; IMP:RGD.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; IMP:RGD.
DR GO; GO:2000561; P:regulation of CD4-positive, alpha-beta T cell proliferation; IEA:Ensembl.
DR GO; GO:0046013; P:regulation of T cell homeostatic proliferation; ISO:RGD.
DR GO; GO:0002664; P:regulation of T cell tolerance induction; ISO:RGD.
DR GO; GO:0043029; P:T cell homeostasis; ISO:RGD.
DR CDD; cd00033; CCP; 1.
DR InterPro; IPR015486; IL-2_rcpt_alpha.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR PANTHER; PTHR10573; PTHR10573; 1.
DR SMART; SM00032; CCP; 2.
DR SUPFAM; SSF57535; SSF57535; 2.
DR PROSITE; PS50923; SUSHI; 2.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Immunity; Membrane; Receptor;
KW Reference proteome; Repeat; Signal; Sushi; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000250"
FT CHAIN 22..267
FT /note="Interleukin-2 receptor subunit alpha"
FT /id="PRO_0000011028"
FT TOPO_DOM 22..235
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 257..267
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 22..79
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 118..181
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT REGION 82..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 24..66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 49..75
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 51..77
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 120..163
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 147..179
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 267 AA; 30557 MW; 647B92D2E274302C CRC64;
MEPHLLMLGF LSFTIVPGCW AELCLYDPPE VPNATFKALS YKNGTILNCE CKRGFRRLNE
LVYMACLGNS WSNNCQCTSN SHDNSREQVT PQPEGQKEQQ TTDTQKSTQS VYQENLAGHC
REPPPWRHED TKRIYHFVEG QIVLYTCIQG YKALQRGPAI SICKTVCGEI RWTHPQLTCV
DEKEHHQFLA SEESQGSRNS FPESEASCPT PNTDFSQLTE ATTTMETFVF TKEYQVAVAS
CIFLLLSILL LSGFTWQHRW RKSRRTI
