ID   IL2RA_SHEEP             Reviewed;         275 AA.
AC   P26898;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 104.
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   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=T-cell;
RA   Verhagen A.A.;
RL   Submitted (DEC-1991) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1572550; DOI=10.1016/0378-1119(92)90409-i;
RA   Bujdoso R., Sargan D.R., Williamson M.L., McConnell I.;
RT   "Cloning of a cDNA encoding the ovine interleukin-2 receptor 55-kDa
RT   protein, CD25.";
RL   Gene 113:283-284(1992).
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; Z11560; CAA77652.1; -; mRNA.
DR   EMBL; X60149; CAA42723.1; -; mRNA.
DR   PIR; JC1113; JC1113.
DR   RefSeq; NP_001009415.1; NM_001009415.1.
DR   AlphaFoldDB; P26898; -.
DR   SMR; P26898; -.
DR   STRING; 9940.ENSOARP00000013772; -.
DR   Ensembl; ENSOART00020005544; ENSOARP00020004565; ENSOARG00020003621.
DR   GeneID; 443435; -.
DR   KEGG; oas:443435; -.
DR   CTD; 3559; -.
DR   eggNOG; ENOG502SUAG; Eukaryota.
DR   OrthoDB; 1236351at2759; -.
DR   Proteomes; UP000002356; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019976; F:interleukin-2 binding; IEA:InterPro.
DR   GO; GO:0004911; F:interleukin-2 receptor activity; IEA:Ensembl.
DR   GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR   GO; GO:0002664; P:regulation of T cell tolerance induction; IEA:Ensembl.
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   Pfam; PF00084; Sushi; 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..275
FT                   /note="Interleukin-2 receptor subunit alpha"
FT                   /id="PRO_0000011029"
FT   TOPO_DOM        22..243
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        244..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        263..275
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          22..81
FT                   /note="Sushi 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          121..186
FT                   /note="Sushi 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   REGION          86..130
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          188..213
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        80
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        24..64
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        49..77
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        51..79
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        123..168
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        152..184
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   CONFLICT        166
FT                   /note="S -> T (in Ref. 2; CAA42723)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   275 AA;  30904 MW;  1101A2DE5AC5A088 CRC64;
     MEPSLLMWRF FVFIVVPGCV TEACHDDPPS LRNAMFKVLR YEVGTMINCD CKAGFRRVSA
     VMRCVGDSSH SAWNNRCFCN STSPAKNPVK PVTPGSEEQR ERKPTDAQSQ TQPPEQADLP
     GHCEEPPPWE HEREPLKRVY HFTLGQTVHY QCAQGFRALH TGPAESTCTM IHGEMRWTRP
     RLKCISEGAN SQAPDEAEPP ESTEAPPGSG TFLTTRMAGT TDFQKPTDVV ATLDTFIFTT
     EYQIAVAGCI LLLSSILLLS CLTWQRRWKK NRRTI