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IL2RA_MOUSE
ID   IL2RA_MOUSE             Reviewed;         268 AA.
AC   P01590; Q61731;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 181.
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=p55;
DE   AltName: CD_antigen=CD25;
DE   Flags: Precursor;
GN   Name=Il2ra; Synonyms=Il2r;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3921620;
RA   Miller J., Malek T.R., Leonard W.J., Greene W.C., Shevach E.M.,
RA   Germain R.N.;
RT   "Nucleotide sequence and expression of a mouse interleukin 2 receptor
RT   cDNA.";
RL   J. Immunol. 134:4212-4217(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2987826; DOI=10.1093/nar/13.5.1505;
RA   Shimuzu A., Kondo S., Takeda S., Yodoi J., Ishida N., Sabe H., Osawa H.,
RA   Diamantstein T., Nikaido T., Honjo T.;
RT   "Nucleotide sequence of mouse IL-2 receptor cDNA and its comparison with
RT   the human IL-2 receptor sequence.";
RL   Nucleic Acids Res. 13:1505-1516(1985).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   McKereghan K.N., Alpert A.R., Grabstein K.H., Cosman D., Cerretti D.P.;
RT   "Recombinant lymphokines and their receptors: molecular analysis for the
RT   murine interleukin-2 receptor.";
RL   Immunol. Ser. 35:109-123(1987).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-21.
RX   PubMed=3135330;
RA   Froussard P., Chastagner P., Somme G., Abadie A., Greene W., Theze J.,
RA   Longacre S.;
RT   "p55 IL-2 receptor mRNA precursors in murine T lymphocyte nuclei.";
RL   J. Immunol. 141:1358-1364(1988).
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.
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DR   EMBL; K02891; AAA39285.1; -; mRNA.
DR   EMBL; M30856; AAA39282.1; -; mRNA.
DR   EMBL; M54934; AAA39290.1; -; mRNA.
DR   EMBL; M21977; AAA39288.1; -; mRNA.
DR   EMBL; M21978; AAA39287.1; -; mRNA.
DR   CCDS; CCDS15685.1; -.
DR   PIR; A01857; UHMS2.
DR   RefSeq; NP_032393.3; NM_008367.3.
DR   AlphaFoldDB; P01590; -.
DR   SMR; P01590; -.
DR   STRING; 10090.ENSMUSP00000028111; -.
DR   BindingDB; P01590; -.
DR   ChEMBL; CHEMBL3287; -.
DR   GlyGen; P01590; 3 sites.
DR   PhosphoSitePlus; P01590; -.
DR   EPD; P01590; -.
DR   PaxDb; P01590; -.
DR   PRIDE; P01590; -.
DR   ProteomicsDB; 301644; -.
DR   Antibodypedia; 3715; 3086 antibodies from 52 providers.
DR   DNASU; 16184; -.
DR   Ensembl; ENSMUST00000028111; ENSMUSP00000028111; ENSMUSG00000026770.
DR   GeneID; 16184; -.
DR   KEGG; mmu:16184; -.
DR   UCSC; uc008iiq.2; mouse.
DR   CTD; 3559; -.
DR   MGI; MGI:96549; Il2ra.
DR   VEuPathDB; HostDB:ENSMUSG00000026770; -.
DR   eggNOG; ENOG502SUAG; Eukaryota.
DR   GeneTree; ENSGT00390000018872; -.
DR   HOGENOM; CLU_089677_1_0_1; -.
DR   InParanoid; P01590; -.
DR   OMA; HYQCIQG; -.
DR   OrthoDB; 1236351at2759; -.
DR   PhylomeDB; P01590; -.
DR   TreeFam; TF337408; -.
DR   Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
DR   Reactome; R-MMU-9020558; Interleukin-2 signaling.
DR   Reactome; R-MMU-912526; Interleukin receptor SHC signaling.
DR   BioGRID-ORCS; 16184; 3 hits in 73 CRISPR screens.
DR   ChiTaRS; Il2ra; mouse.
DR   PRO; PR:P01590; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; P01590; protein.
DR   Bgee; ENSMUSG00000026770; Expressed in thymus and 34 other tissues.
DR   ExpressionAtlas; P01590; baseline and differential.
DR   Genevisible; P01590; MM.
DR   GO; GO:0009986; C:cell surface; ISO:MGI.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019976; F:interleukin-2 binding; IPI:MGI.
DR   GO; GO:0004911; F:interleukin-2 receptor activity; IMP:MGI.
DR   GO; GO:0050798; P:activated T cell proliferation; IMP:MGI.
DR   GO; GO:0006924; P:activation-induced cell death of T cells; IMP:MGI.
DR   GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR   GO; GO:0002437; P:inflammatory response to antigenic stimulus; ISO:MGI.
DR   GO; GO:0046651; P:lymphocyte proliferation; IMP:MGI.
DR   GO; GO:0050728; P:negative regulation of inflammatory response; IMP:MGI.
DR   GO; GO:0050672; P:negative regulation of lymphocyte proliferation; IMP:MGI.
DR   GO; GO:0042130; P:negative regulation of T cell proliferation; IMP:MGI.
DR   GO; GO:0007219; P:Notch signaling pathway; IGI:MGI.
DR   GO; GO:0042104; P:positive regulation of activated T cell proliferation; IMP:MGI.
DR   GO; GO:0045582; P:positive regulation of T cell differentiation; ISO:MGI.
DR   GO; GO:0042102; P:positive regulation of T cell proliferation; ISO:MGI.
DR   GO; GO:2000561; P:regulation of CD4-positive, alpha-beta T cell proliferation; IMP:MGI.
DR   GO; GO:0046013; P:regulation of T cell homeostatic proliferation; IMP:MGI.
DR   GO; GO:0002664; P:regulation of T cell tolerance induction; ISO:MGI.
DR   GO; GO:0043029; P:T cell homeostasis; IMP:MGI.
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..268
FT                   /note="Interleukin-2 receptor subunit alpha"
FT                   /id="PRO_0000011026"
FT   TOPO_DOM        22..236
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        237..257
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        258..268
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          22..79
FT                   /note="Sushi 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          119..182
FT                   /note="Sushi 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   REGION          86..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          189..219
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        94..109
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        194..219
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        43
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        116
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        24..66
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        49..75
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        51..77
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        121..164
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        148..180
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   CONFLICT        1..4
FT                   /note="MEPR -> MCQEDGAT (in Ref. 3; AAA39290)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        7
FT                   /note="M -> T (in Ref. 2; AAA39282)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        118
FT                   /note="T -> A (in Ref. 2; AAA39282)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        140
FT                   /note="E -> V (in Ref. 2; AAA39282)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        216
FT                   /note="F -> L (in Ref. 2; AAA39282)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        227
FT                   /note="E -> V (in Ref. 2; AAA39282)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   268 AA;  30723 MW;  20C8F712B719192D CRC64;
     MEPRLLMLGF LSLTIVPSCR AELCLYDPPE VPNATFKALS YKNGTILNCE CKRGFRRLKE
     LVYMRCLGNS WSSNCQCTSN SHDKSRKQVT AQLEHQKEQQ TTTDMQKPTQ SMHQENLTGH
     CREPPPWKHE DSKRIYHFVE GQSVHYECIP GYKALQRGPA ISICKMKCGK TGWTQPQLTC
     VDEREHHRFL ASEESQGSRN SSPESETSCP ITTTDFPQPT ETTAMTETFV LTMEYKVAVA
     SCLFLLISIL LLSGLTWQHR WRKSRRTI
 
 
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