IL2RA_BOVIN
ID IL2RA_BOVIN Reviewed; 275 AA.
AC P12342;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 25-MAY-2022, entry version 125.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2835311;
RA Weinberg A.D., Shaw J., Paetkau V., Bleackley R.C., Magnuson N.S.,
RA Reeves R., Magnuson J.A.;
RT "Cloning of cDNA for the bovine IL-2 receptor (bovine Tac antigen).";
RL Immunology 63:603-610(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
RX PubMed=8563178; DOI=10.1007/bf00354302;
RA Yoo J., de Leon F.A., Stone R.T., Beattie C.W.;
RT "Cloning and chromosomal assignment of the bovine interleukin-2 receptor
RT alpha (IL-2R alpha) gene.";
RL Mamm. Genome 6:751-753(1995).
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.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M20818; AAA51414.1; -; mRNA.
DR EMBL; U24226; AAC48487.1; -; Genomic_DNA.
DR PIR; S07442; S07442.
DR RefSeq; NP_776783.1; NM_174358.2.
DR AlphaFoldDB; P12342; -.
DR SMR; P12342; -.
DR STRING; 9913.ENSBTAP00000027834; -.
DR PaxDb; P12342; -.
DR PRIDE; P12342; -.
DR GeneID; 281861; -.
DR KEGG; bta:281861; -.
DR CTD; 3559; -.
DR eggNOG; ENOG502SUAG; Eukaryota.
DR InParanoid; P12342; -.
DR OrthoDB; 1236351at2759; -.
DR Proteomes; UP000009136; 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 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 CHAIN 22..275
FT /note="Interleukin-2 receptor subunit alpha"
FT /id="PRO_0000011021"
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 88..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 109
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"
SQ SEQUENCE 275 AA; 31239 MW; 4901BBF9A4862390 CRC64;
MEPSLLMWRF FVFIVVPGCV TEACHDDPPS LRNAMFKVFR YEVGTMINCD CKTGFRRVSA
VMRCVGDSSH SAWENRCFCN STSPAKNQVK QVTPAPEEHR EKKHTDAQNQ TQPPEEADLP
GHCEEPPPWE HEREPLKRVY HFTLGQTVHY QCAQGFRALQ TSPAESTCMM INGELRWTRP
RLKCIREGEH GQASDDAEPQ ESTEAPPGSG TFLPTRMAGT TNFQKPTDEI ATLDTFIFTT
EYQIAVAGCT LLLASILLLS CLTWQRKWKK NRRTI
