ID   IL2RA_CANLF             Reviewed;         268 AA.
AC   O62802;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   25-MAY-2022, entry version 110.
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: Full=TAC antigen;
DE   AltName: Full=p55;
DE   AltName: CD_antigen=CD25;
DE   Flags: Precursor;
GN   Name=IL2RA;
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].
RA   Dickerson E.B., Padilla M.L., Helfand S.C.;
RT   "Cloning of the canine IL-2 receptor alpha subunit.";
RL   Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
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; AF056491; AAC13560.1; -; mRNA.
DR   AlphaFoldDB; O62802; -.
DR   SMR; O62802; -.
DR   STRING; 9615.ENSCAFP00000007785; -.
DR   eggNOG; ENOG502SUAG; Eukaryota.
DR   InParanoid; O62802; -.
DR   Proteomes; UP000002254; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019976; F:interleukin-2 binding; IBA:GO_Central.
DR   GO; GO:0004911; F:interleukin-2 receptor activity; IBA:GO_Central.
DR   GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR   GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
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..268
FT                   /note="Interleukin-2 receptor subunit alpha"
FT                   /id="PRO_0000011022"
FT   TOPO_DOM        22..237
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        238..258
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        259..268
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          22..81
FT                   /note="Sushi 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          120..183
FT                   /note="Sushi 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   REGION          83..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          186..213
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        83..101
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        199..213
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        67
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        122..165
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        149..181
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
SQ   SEQUENCE   268 AA;  30357 MW;  6622E154FDDE2F46 CRC64;
     MEPCLLMWGI LTFITVSGYT TDLCDDDPPN LKHATFKALT YKTGTVLNCD CERGFRRISS
     YMHCTGNSSH ASWENKCRCK SVSPENRKGK VTTKPEEQKG ENPTEMQSQT PPMDEVDLVG
     HCREPPPWEH ENSKRIYHFV VGQTLHYQCM QGFTALHRGP AKSICKTIFG KTRWTQPPLK
     CISESQFPDD EELQASTDAP AGRDTSSPFI TTSTPDFHKH TEVATTMESF IFTTEYQIAV
     ASCVLLLISI VLLSGLTWQR RRRKSRTI