ID   IL2RA_PIG               Reviewed;         270 AA.
AC   O02733;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   25-MAY-2022, entry version 108.
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   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9429903; DOI=10.1038/icb.1997.81;
RA   Kokuho T., Uchimura A., Inumaru S.;
RT   "cDNA cloning of porcine interleukin-2 receptor-alpha gene.";
RL   Immunol. Cell Biol. 75:515-517(1997).
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; U78317; AAC48781.1; -; mRNA.
DR   EMBL; AF052037; AAC27994.1; -; Genomic_DNA.
DR   RefSeq; NP_999000.1; NM_213835.1.
DR   AlphaFoldDB; O02733; -.
DR   SMR; O02733; -.
DR   STRING; 9823.ENSSSCP00000023036; -.
DR   PaxDb; O02733; -.
DR   GeneID; 396814; -.
DR   KEGG; ssc:396814; -.
DR   CTD; 3559; -.
DR   eggNOG; ENOG502SUAG; Eukaryota.
DR   HOGENOM; CLU_3427951_0_0_1; -.
DR   InParanoid; O02733; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; 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..270
FT                   /note="Interleukin-2 receptor subunit alpha"
FT                   /id="PRO_0000011027"
FT   TOPO_DOM        22..245
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        246..264
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        265..270
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          22..84
FT                   /note="Sushi 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          124..191
FT                   /note="Sushi 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   REGION          87..124
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          190..225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        197..225
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        70
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        195
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        227
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        24..67
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        49..80
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        51..82
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        126..171
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        153..189
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
SQ   SEQUENCE   270 AA;  30437 MW;  25446EC7DDF4FCC2 CRC64;
     MEPSLLMWGF FTFTMIPGCM AGACVQQPPS LRNATFKILG YKVGTTLNCD CQRGFRRDPS
     SGPYMICRGN SSHSFWENKC QCMPTSSPRI PVKQVTPRPE EQKERKTTET QGQMQPPNQA
     NLPGHCKEPP PWEHESLKRV YHFMEGQTVR YQCLPGFRDG SAQNNSAQSV CKKQEDQEVM
     RWTQPKLKCK SEKENGSFPE PQMSTAAPPT TKTSLPTRTK GTTDSQNLTE VPATMQPIIF
     TTQYQLAVAG CVLLLLSILL LSGLTWQRRR