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Interleukin-15 receptor subunit alpha (IL-15 receptor subunit alpha) (IL-15R-alpha) (IL-15RA) (CD antigen CD215) [Cleaved into: Soluble interleukin-15 receptor subunit alpha (sIL-15 receptor subunit alpha) (sIL-15R-alpha) (sIL-15RA)]

 I15RA_MOUSE             Reviewed;         263 AA.
Q60819; A2AP35; A2AP36; A2AP37; Q80Z90; Q80Z91; Q80Z92; Q8R5E4;
01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
12-SEP-2018, entry version 138.
RecName: Full=Interleukin-15 receptor subunit alpha;
Short=IL-15 receptor subunit alpha;
Short=IL-15R-alpha;
Short=IL-15RA;
AltName: CD_antigen=CD215;
Contains:
RecName: Full=Soluble interleukin-15 receptor subunit alpha;
Short=sIL-15 receptor subunit alpha;
Short=sIL-15R-alpha;
Short=sIL-15RA;
Flags: Precursor;
Name=Il15ra;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), LIGAND-BINDING, SUBUNIT, AND
TISSUE SPECIFICITY.
PubMed=7641685;
Giri J.G., Kumaki S., Ahdieh M., Friend D.J., Loomis A., Shanebeck K.,
DuBose R., Cosman D., Park L.S., Anderson D.M.;
"Identification and cloning of a novel IL-15 binding protein that is
structurally related to the alpha chain of the IL-2 receptor.";
EMBO J. 14:3654-3663(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4 AND 5), AND TISSUE
SPECIFICITY.
STRAIN=C57BL/6J;
PubMed=12885940; DOI=10.1189/jlb.0303097;
Toomey J.A., Gays F., Foster D., Brooks C.G.;
"Cytokine requirements for the growth and development of mouse NK
cells in vitro.";
J. Leukoc. Biol. 74:233-242(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
STRAIN=FVB/N; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
ALTERNATIVE SPLICING (ISOFORMS 3; 4 AND 6), FUNCTION, SUBCELLULAR
LOCATION, GLYCOSYLATION, AND INTERACTION WITH SYK.
PubMed=12734349; DOI=10.4049/jimmunol.170.10.5045;
Bulanova E., Budagian V., Orinska Z., Krause H., Paus R.,
Bulfone-Paus S.;
"Mast cells express novel functional IL-15 receptor alpha isoforms.";
J. Immunol. 170:5045-5055(2003).
[6]
ERRATUM, AND RETRACTION.
PubMed=21289316; DOI=10.4049/jimmunol.1090143;
Krause H., Paus R., Orinska Z., Bulfone-Paus S.;
J. Immunol. 186:2682-2682(2011).
[7]
PROTEOLYTIC PROCESSING BY ADAM17.
PubMed=15215246; DOI=10.1074/jbc.M404125200;
Budagian V., Bulanova E., Orinska Z., Ludwig A., Rose-John S.,
Saftig P., Borden E.C., Bulfone-Paus S.;
"Natural soluble interleukin-15Ralpha is generated by cleavage that
involves the tumor necrosis factor-alpha-converting enzyme
(TACE/ADAM17).";
J. Biol. Chem. 279:40368-40375(2004).
[8]
X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS) OF 33-103 IN COMPLEX WITH IL15,
FUNCTION, AND DISULFIDE BONDS.
PubMed=17947230; DOI=10.1074/jbc.M706150200;
Olsen S.K., Ota N., Kishishita S., Kukimoto-Niino M., Murayama K.,
Uchiyama H., Toyama M., Terada T., Shirouzu M., Kanagawa O.,
Yokoyama S.;
"Crystal Structure of the interleukin-15.interleukin-15 receptor alpha
complex: insights into trans and cis presentation.";
J. Biol. Chem. 282:37191-37204(2007).
-!- FUNCTION: High-affinity receptor for interleukin-15. Can signal
both in cis and trans where IL15R from one subset of cells
presents IL15 to neighboring IL2RG-expressing cells. Signal
transduction involves SYK (By similarity). {ECO:0000250,
ECO:0000269|PubMed:12734349, ECO:0000269|PubMed:17947230}.
-!- SUBUNIT: The interleukin-15 receptor IL15R is a heterotrimer of
IL15RA, IL2RB and IL2RG. IL15RA also self-associates. Interacts
with SYK (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
membrane protein {ECO:0000250}. Nucleus membrane {ECO:0000250};
Single-pass type I membrane protein {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Soluble interleukin-15 receptor subunit
alpha: Secreted, extracellular space {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1;
IsoId=Q60819-1; Sequence=Displayed;
Name=2; Synonyms=1A;
IsoId=Q60819-2; Sequence=VSP_012629, VSP_012630;
Name=3; Synonyms=1B, IL-15R-alphadelta4;
IsoId=Q60819-3; Sequence=VSP_012629, VSP_012630, VSP_012631;
Name=4; Synonyms=1C, IL-15R-alphadelta34;
IsoId=Q60819-4; Sequence=VSP_012628, VSP_012629, VSP_012630,
VSP_012631, VSP_012632;
Name=5; Synonyms=2, 2A;
IsoId=Q60819-5; Sequence=VSP_012627, VSP_012628, VSP_012629;
Name=6; Synonyms=IL-15R-alphadelta345;
IsoId=Q60819-6; Sequence=VSP_012628, VSP_012629, VSP_012630,
VSP_012631, VSP_012633;
-!- TISSUE SPECIFICITY: Widely expressed.
{ECO:0000269|PubMed:12885940, ECO:0000269|PubMed:7641685}.
-!- PTM: Phosphorylated by activated SYK. {ECO:0000250}.
-!- PTM: N-glycosylated and O-glycosylated. {ECO:0000250}.
-!- PTM: A soluble form (sIL-15RA) arises from proteolytic shedding of
the membrane-anchored receptor. The cleavage involves ADAM17/TACE.
It also binds IL15 and thus interferes with IL15 binding to the
membrane receptor (By similarity). {ECO:0000250}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; U22339; AAC52240.1; -; Genomic_DNA.
EMBL; AY219715; AAO62310.1; -; mRNA.
EMBL; AY219716; AAO62311.1; -; mRNA.
EMBL; AY219717; AAO62312.1; -; mRNA.
EMBL; AY221616; AAO74882.1; -; mRNA.
EMBL; AL831794; CAM13743.1; -; Genomic_DNA.
EMBL; AL831794; CAM13744.1; -; Genomic_DNA.
EMBL; AL831794; CAM13745.1; -; Genomic_DNA.
EMBL; BC022705; AAH22705.1; -; mRNA.
CCDS; CCDS15686.1; -. [Q60819-1]
CCDS; CCDS15687.1; -. [Q60819-5]
CCDS; CCDS70977.1; -. [Q60819-2]
CCDS; CCDS70978.1; -. [Q60819-3]
CCDS; CCDS70979.1; -. [Q60819-4]
PIR; S57346; S57346.
RefSeq; NP_001258426.1; NM_001271497.1. [Q60819-5]
RefSeq; NP_001258428.1; NM_001271499.1. [Q60819-2]
RefSeq; NP_001258429.1; NM_001271500.1. [Q60819-3]
RefSeq; NP_001258430.1; NM_001271501.1. [Q60819-4]
RefSeq; NP_032384.1; NM_008358.2. [Q60819-1]
RefSeq; NP_598597.1; NM_133836.2. [Q60819-5]
RefSeq; XP_006497427.1; XM_006497364.1. [Q60819-5]
RefSeq; XP_017171184.1; XM_017315695.1. [Q60819-6]
UniGene; Mm.200196; -.
PDB; 2PSM; X-ray; 2.19 A; C/F=33-103.
PDBsum; 2PSM; -.
ProteinModelPortal; Q60819; -.
SMR; Q60819; -.
STRING; 10090.ENSMUSP00000077878; -.
PaxDb; Q60819; -.
PRIDE; Q60819; -.
Ensembl; ENSMUST00000078834; ENSMUSP00000077878; ENSMUSG00000023206. [Q60819-1]
Ensembl; ENSMUST00000114831; ENSMUSP00000110480; ENSMUSG00000023206. [Q60819-2]
Ensembl; ENSMUST00000114832; ENSMUSP00000110481; ENSMUSG00000023206. [Q60819-6]
Ensembl; ENSMUST00000114833; ENSMUSP00000110482; ENSMUSG00000023206. [Q60819-4]
Ensembl; ENSMUST00000114834; ENSMUSP00000110483; ENSMUSG00000023206. [Q60819-3]
Ensembl; ENSMUST00000128156; ENSMUSP00000126364; ENSMUSG00000023206. [Q60819-5]
Ensembl; ENSMUST00000135341; ENSMUSP00000132731; ENSMUSG00000023206. [Q60819-5]
Ensembl; ENSMUST00000138349; ENSMUSP00000131473; ENSMUSG00000023206. [Q60819-5]
GeneID; 16169; -.
KEGG; mmu:16169; -.
UCSC; uc008iiw.2; mouse. [Q60819-6]
UCSC; uc008iix.2; mouse. [Q60819-1]
UCSC; uc008iiy.2; mouse. [Q60819-2]
UCSC; uc008iiz.2; mouse. [Q60819-3]
UCSC; uc008ija.2; mouse. [Q60819-4]
CTD; 3601; -.
MGI; MGI:104644; Il15ra.
eggNOG; ENOG410IWP4; Eukaryota.
eggNOG; ENOG410Z8MM; LUCA.
GeneTree; ENSGT00390000000121; -.
HOVERGEN; HBG052061; -.
InParanoid; Q60819; -.
KO; K05074; -.
OMA; LLACYIK; -.
OrthoDB; EOG091G0OD7; -.
PhylomeDB; Q60819; -.
TreeFam; TF338443; -.
Reactome; R-MMU-8983432; Interleukin-15 signaling.
ChiTaRS; Il15ra; mouse.
EvolutionaryTrace; Q60819; -.
PMAP-CutDB; Q60819; -.
PRO; PR:Q60819; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000023206; Expressed in 184 organ(s), highest expression level in brown adipose tissue.
CleanEx; MM_IL15RA; -.
ExpressionAtlas; Q60819; baseline and differential.
Genevisible; Q60819; MM.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0007259; P:JAK-STAT cascade; ISO:MGI.
GO; GO:0010977; P:negative regulation of neuron projection development; ISO:MGI.
GO; GO:0032825; P:positive regulation of natural killer cell differentiation; IMP:MGI.
CDD; cd00033; CCP; 1.
InterPro; IPR035976; Sushi/SCR/CCP_sf.
InterPro; IPR000436; Sushi_SCR_CCP_dom.
Pfam; PF00084; Sushi; 1.
SMART; SM00032; CCP; 1.
SUPFAM; SSF57535; SSF57535; 1.
PROSITE; PS50923; SUSHI; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Disulfide bond;
Glycoprotein; Membrane; Nucleus; Phosphoprotein; Receptor;
Reference proteome; Secreted; Signal; Sushi; Transmembrane;
Transmembrane helix.
SIGNAL 1 32 {ECO:0000255}.
CHAIN 33 263 Interleukin-15 receptor subunit alpha.
/FTId=PRO_0000011045.
CHAIN 33 ? Soluble interleukin-15 receptor subunit
alpha.
/FTId=PRO_0000333856.
TOPO_DOM 33 205 Extracellular. {ECO:0000255}.
TRANSMEM 206 226 Helical. {ECO:0000255}.
TOPO_DOM 227 263 Cytoplasmic. {ECO:0000255}.
DOMAIN 34 98 Sushi. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
CARBOHYD 51 51 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 36 78 {ECO:0000255|PROSITE-ProRule:PRU00302,
ECO:0000269|PubMed:17947230}.
DISULFID 62 96 {ECO:0000255|PROSITE-ProRule:PRU00302,
ECO:0000269|PubMed:17947230}.
VAR_SEQ 1 97 Missing (in isoform 5).
{ECO:0000303|PubMed:12885940,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_012627.
VAR_SEQ 98 128 Missing (in isoform 4, isoform 5 and
isoform 6). {ECO:0000303|PubMed:12885940,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_012628.
VAR_SEQ 129 140 Missing (in isoform 2, isoform 3, isoform
4, isoform 5 and isoform 6).
{ECO:0000303|PubMed:12885940,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_012629.
VAR_SEQ 141 161 Missing (in isoform 2, isoform 3, isoform
4 and isoform 6).
{ECO:0000303|PubMed:12885940}.
/FTId=VSP_012630.
VAR_SEQ 162 194 Missing (in isoform 3, isoform 4 and
isoform 6).
{ECO:0000303|PubMed:12885940}.
/FTId=VSP_012631.
VAR_SEQ 195 206 EISPHSSKMTKV -> M (in isoform 6).
{ECO:0000305}.
/FTId=VSP_012633.
VAR_SEQ 195 195 E -> K (in isoform 4).
{ECO:0000303|PubMed:12885940}.
/FTId=VSP_012632.
STRAND 57 59 {ECO:0000244|PDB:2PSM}.
STRAND 66 68 {ECO:0000244|PDB:2PSM}.
STRAND 75 80 {ECO:0000244|PDB:2PSM}.
TURN 82 84 {ECO:0000244|PDB:2PSM}.
STRAND 87 89 {ECO:0000244|PDB:2PSM}.
STRAND 96 98 {ECO:0000244|PDB:2PSM}.
SEQUENCE 263 AA; 28061 MW; BFCC2CE4BA58B504 CRC64;
MASPQLRGYG VQAIPVLLLL LLLLLLPLRV TPGTTCPPPV SIEHADIRVK NYSVNSRERY
VCNSGFKRKA GTSTLIECVI NKNTNVAHWT TPSLKCIRDP SLAHYSPVPT VVTPKVTSQP
ESPSPSAKEP EAFSPKSDTA MTTETAIMPG SRLTPSQTTS AGTTGTGSHK SSRAPSLAAT
MTLEPTASTS LRITEISPHS SKMTKVAIST SVLLVGAGVV MAFLAWYIKS RQPSQPCRVE
VETMETVPMT VRASSKEDED TGA


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