ID   IL2RA_PANTR             Reviewed;         265 AA.
AC   Q38IC8;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 76.
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; Fragment;
GN   Name=IL2RA;
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Chen S., Yu L.;
RL   Submitted (SEP-2005) 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 {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}.
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DR   EMBL; DQ226542; ABB13530.1; -; mRNA.
DR   RefSeq; NP_001030597.1; NM_001035520.1.
DR   AlphaFoldDB; Q38IC8; -.
DR   SMR; Q38IC8; -.
DR   STRING; 9598.ENSPTRP00000003829; -.
DR   PaxDb; Q38IC8; -.
DR   GeneID; 450884; -.
DR   KEGG; ptr:450884; -.
DR   CTD; 3559; -.
DR   eggNOG; ENOG502SUAG; Eukaryota.
DR   InParanoid; Q38IC8; -.
DR   OrthoDB; 1236351at2759; -.
DR   Proteomes; UP000002277; 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..>265
FT                   /note="Interleukin-2 receptor subunit alpha"
FT                   /id="PRO_0000235185"
FT   TOPO_DOM        22..240
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        241..259
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        260..>265
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          22..84
FT                   /note="Sushi 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          123..186
FT                   /note="Sushi 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   REGION          87..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          190..210
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        70
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        89
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        125..168
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        152..184
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   NON_TER         265
SQ   SEQUENCE   265 AA;  29954 MW;  67383878E8AC5A43 CRC64;
     MDSYLLMWGL LTLIMVPGCF AELCDDDPPE ITHATFKAMA YKEGTMLNCE CKRGFRRIKS
     GSLYMLCTGN SSHSSWDNQC QCTSSATRNT TKQVTPQPEE QKERKTTEMQ SPMQPVDQAS
     LPGHCREPPP WENEATERIY HFVVGQTVYY QCVQGYRALH RGPAESVCKM THGKTRWTQP
     QLICTGEMET SQFPGEEKPQ ASPEGRPESE TSCLITTTDF QIQTEMAATM ETFIFTTEYQ
     VAVAGCVFLL ISVLLLSGLT WQRRQ