I15RA_MOUSE
ID I15RA_MOUSE Reviewed; 263 AA.
AC Q60819; A2AP35; A2AP36; A2AP37; Q80Z90; Q80Z91; Q80Z92; Q8R5E4;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Interleukin-15 receptor subunit alpha;
DE Short=IL-15 receptor subunit alpha;
DE Short=IL-15R-alpha;
DE Short=IL-15RA;
DE AltName: CD_antigen=CD215;
DE Contains:
DE RecName: Full=Soluble interleukin-15 receptor subunit alpha;
DE Short=sIL-15 receptor subunit alpha;
DE Short=sIL-15R-alpha;
DE Short=sIL-15RA;
DE Flags: Precursor;
GN Name=Il15ra;
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] (ISOFORM 1), LIGAND-BINDING, SUBUNIT, AND TISSUE
RP SPECIFICITY.
RX PubMed=7641685; DOI=10.1002/j.1460-2075.1995.tb00035.x;
RA Giri J.G., Kumaki S., Ahdieh M., Friend D.J., Loomis A., Shanebeck K.,
RA DuBose R., Cosman D., Park L.S., Anderson D.M.;
RT "Identification and cloning of a novel IL-15 binding protein that is
RT structurally related to the alpha chain of the IL-2 receptor.";
RL EMBO J. 14:3654-3663(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4 AND 5), AND TISSUE
RP SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=12885940; DOI=10.1189/jlb.0303097;
RA Toomey J.A., Gays F., Foster D., Brooks C.G.;
RT "Cytokine requirements for the growth and development of mouse NK cells in
RT vitro.";
RL J. Leukoc. Biol. 74:233-242(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP RETRACTED PAPER.
RX PubMed=12734349; DOI=10.4049/jimmunol.170.10.5045;
RA Bulanova E., Budagian V., Orinska Z., Krause H., Paus R., Bulfone-Paus S.;
RT "Mast cells express novel functional IL-15 receptor alpha isoforms.";
RL J. Immunol. 170:5045-5055(2003).
RN [6]
RP RETRACTION NOTICE OF PUBMED:12734349.
RX PubMed=21289316; DOI=10.4049/jimmunol.1090143;
RA Krause H., Paus R., Orinska Z., Bulfone-Paus S.;
RT "Mast cells express novel functional IL-15 receptor alpha isoforms.";
RL J. Immunol. 186:2682-2682(2011).
RN [7]
RP RETRACTED PAPER.
RX PubMed=15215246; DOI=10.1074/jbc.m404125200;
RA Budagian V., Bulanova E., Orinska Z., Ludwig A., Rose-John S., Saftig P.,
RA Borden E.C., Bulfone-Paus S.;
RT "Natural soluble interleukin-15Ralpha is generated by cleavage that
RT involves the tumor necrosis factor-alpha-converting enzyme (TACE/ADAM17).";
RL J. Biol. Chem. 279:40368-40375(2004).
RN [8]
RP RETRACTION NOTICE OF PUBMED:15215246.
RX PubMed=21516612; DOI=10.1074/jbc.a110.404125;
RA Budagian V., Bulanova E., Orinska Z., Ludwig A., Rose-John S., Saftig P.,
RA Borden E.C., Bulfone-Paus S.;
RT "Natural soluble interleukin-15Ralpha is generated by cleavage that
RT involves the tumor necrosis factor-alpha-converting enzyme (TACE/ADAM17).";
RL J. Biol. Chem. 286:9894-9894(2011).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS) OF 33-103 IN COMPLEX WITH IL15,
RP FUNCTION, AND DISULFIDE BONDS.
RX PubMed=17947230; DOI=10.1074/jbc.m706150200;
RA Olsen S.K., Ota N., Kishishita S., Kukimoto-Niino M., Murayama K.,
RA Uchiyama H., Toyama M., Terada T., Shirouzu M., Kanagawa O., Yokoyama S.;
RT "Crystal Structure of the interleukin-15.interleukin-15 receptor alpha
RT complex: insights into trans and cis presentation.";
RL J. Biol. Chem. 282:37191-37204(2007).
CC -!- FUNCTION: High-affinity receptor for interleukin-15 (PubMed:17947230).
CC Can signal both in cis and trans where IL15R from one subset of cells
CC presents IL15 to neighboring IL2RG-expressing cells (PubMed:17947230).
CC In neutrophils, binds and activates kinase SYK in response to IL15
CC stimulation (By similarity). In neutrophils, required for IL15-induced
CC phagocytosis in a SYK-dependent manner (By similarity).
CC {ECO:0000250|UniProtKB:Q13261, ECO:0000269|PubMed:17947230}.
CC -!- SUBUNIT: The interleukin-15 receptor IL15R is a heterotrimer of IL15RA,
CC IL2RB and IL2RG. IL15RA also self-associates (By similarity). Interacts
CC with SYK (By similarity). {ECO:0000250|UniProtKB:Q13261}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q13261}; Single-
CC pass type I membrane protein {ECO:0000250|UniProtKB:Q13261}. Nucleus
CC membrane {ECO:0000250|UniProtKB:Q13261}; Single-pass type I membrane
CC protein {ECO:0000250|UniProtKB:Q13261}. Cell surface
CC {ECO:0000250|UniProtKB:Q13261}.
CC -!- SUBCELLULAR LOCATION: [Soluble interleukin-15 receptor subunit alpha]:
CC Secreted, extracellular space {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q60819-1; Sequence=Displayed;
CC Name=2; Synonyms=1A;
CC IsoId=Q60819-2; Sequence=VSP_012629, VSP_012630;
CC Name=3; Synonyms=1B, IL-15R-alphadelta4;
CC IsoId=Q60819-3; Sequence=VSP_012629, VSP_012630, VSP_012631;
CC Name=4; Synonyms=1C, IL-15R-alphadelta34;
CC IsoId=Q60819-4; Sequence=VSP_012628, VSP_012629, VSP_012630,
CC VSP_012631, VSP_012632;
CC Name=5; Synonyms=2, 2A;
CC IsoId=Q60819-5; Sequence=VSP_012627, VSP_012628, VSP_012629;
CC Name=6; Synonyms=IL-15R-alphadelta345;
CC IsoId=Q60819-6; Sequence=VSP_012628, VSP_012629, VSP_012630,
CC VSP_012631, VSP_012633;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12885940,
CC ECO:0000269|PubMed:7641685}.
CC -!- PTM: N-glycosylated and O-glycosylated. {ECO:0000250|UniProtKB:Q13261}.
CC -!- PTM: A soluble form (sIL-15RA) arises from proteolytic shedding of the
CC membrane-anchored receptor (By similarity). It also binds IL15 and thus
CC interferes with IL15 binding to the membrane receptor (By similarity).
CC {ECO:0000250|UniProtKB:Q13261}.
CC -!- CAUTION: It was shown that proteolytic cleavage of Il15ra involves
CC ADAM17/TACE; this publication has later been retracted.
CC {ECO:0000269|PubMed:15215246, ECO:0000305|PubMed:21516612}.
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DR EMBL; U22339; AAC52240.1; -; Genomic_DNA.
DR EMBL; AY219715; AAO62310.1; -; mRNA.
DR EMBL; AY219716; AAO62311.1; -; mRNA.
DR EMBL; AY219717; AAO62312.1; -; mRNA.
DR EMBL; AY221616; AAO74882.1; -; mRNA.
DR EMBL; AL831794; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC022705; AAH22705.1; -; mRNA.
DR CCDS; CCDS15686.1; -. [Q60819-1]
DR CCDS; CCDS15687.1; -. [Q60819-5]
DR CCDS; CCDS70977.1; -. [Q60819-2]
DR CCDS; CCDS70978.1; -. [Q60819-3]
DR CCDS; CCDS70979.1; -. [Q60819-4]
DR PIR; S57346; S57346.
DR RefSeq; NP_001258426.1; NM_001271497.1. [Q60819-5]
DR RefSeq; NP_001258428.1; NM_001271499.1. [Q60819-2]
DR RefSeq; NP_001258429.1; NM_001271500.1. [Q60819-3]
DR RefSeq; NP_001258430.1; NM_001271501.1. [Q60819-4]
DR RefSeq; NP_032384.1; NM_008358.2. [Q60819-1]
DR RefSeq; NP_598597.1; NM_133836.2. [Q60819-5]
DR RefSeq; XP_006497427.1; XM_006497364.1. [Q60819-5]
DR RefSeq; XP_017171184.1; XM_017315695.1. [Q60819-6]
DR PDB; 2PSM; X-ray; 2.19 A; C/F=33-103.
DR PDBsum; 2PSM; -.
DR AlphaFoldDB; Q60819; -.
DR SMR; Q60819; -.
DR STRING; 10090.ENSMUSP00000077878; -.
DR GlyGen; Q60819; 1 site.
DR EPD; Q60819; -.
DR PaxDb; Q60819; -.
DR PRIDE; Q60819; -.
DR ProteomicsDB; 273244; -. [Q60819-1]
DR ProteomicsDB; 273245; -. [Q60819-2]
DR ProteomicsDB; 273246; -. [Q60819-3]
DR ProteomicsDB; 273247; -. [Q60819-4]
DR ProteomicsDB; 273248; -. [Q60819-5]
DR ProteomicsDB; 273249; -. [Q60819-6]
DR Antibodypedia; 24259; 484 antibodies from 35 providers.
DR DNASU; 16169; -.
DR Ensembl; ENSMUST00000078834; ENSMUSP00000077878; ENSMUSG00000023206. [Q60819-1]
DR Ensembl; ENSMUST00000114831; ENSMUSP00000110480; ENSMUSG00000023206. [Q60819-2]
DR Ensembl; ENSMUST00000114832; ENSMUSP00000110481; ENSMUSG00000023206. [Q60819-6]
DR Ensembl; ENSMUST00000114833; ENSMUSP00000110482; ENSMUSG00000023206. [Q60819-4]
DR Ensembl; ENSMUST00000114834; ENSMUSP00000110483; ENSMUSG00000023206. [Q60819-3]
DR Ensembl; ENSMUST00000128156; ENSMUSP00000126364; ENSMUSG00000023206. [Q60819-5]
DR Ensembl; ENSMUST00000135341; ENSMUSP00000132731; ENSMUSG00000023206. [Q60819-5]
DR Ensembl; ENSMUST00000138349; ENSMUSP00000131473; ENSMUSG00000023206. [Q60819-5]
DR GeneID; 16169; -.
DR KEGG; mmu:16169; -.
DR UCSC; uc008iiw.2; mouse. [Q60819-6]
DR UCSC; uc008iix.2; mouse. [Q60819-1]
DR UCSC; uc008iiy.2; mouse. [Q60819-2]
DR UCSC; uc008iiz.2; mouse. [Q60819-3]
DR UCSC; uc008ija.2; mouse. [Q60819-4]
DR CTD; 3601; -.
DR MGI; MGI:104644; Il15ra.
DR VEuPathDB; HostDB:ENSMUSG00000023206; -.
DR eggNOG; ENOG502SG86; Eukaryota.
DR GeneTree; ENSGT00390000000121; -.
DR HOGENOM; CLU_2014496_0_0_1; -.
DR InParanoid; Q60819; -.
DR OMA; QVEMESM; -.
DR OrthoDB; 1326471at2759; -.
DR PhylomeDB; Q60819; -.
DR TreeFam; TF338443; -.
DR Reactome; R-MMU-8983432; Interleukin-15 signaling.
DR BioGRID-ORCS; 16169; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Il15ra; mouse.
DR EvolutionaryTrace; Q60819; -.
DR PRO; PR:Q60819; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q60819; protein.
DR Bgee; ENSMUSG00000023206; Expressed in hindlimb stylopod muscle and 154 other tissues.
DR ExpressionAtlas; Q60819; baseline and differential.
DR Genevisible; Q60819; MM.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0042010; F:interleukin-15 receptor activity; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0035723; P:interleukin-15-mediated signaling pathway; ISO:MGI.
DR GO; GO:0001779; P:natural killer cell differentiation; IMP:MGI.
DR GO; GO:0010977; P:negative regulation of neuron projection development; ISO:MGI.
DR GO; GO:0032825; P:positive regulation of natural killer cell differentiation; IMP:MGI.
DR GO; GO:0050766; P:positive regulation of phagocytosis; ISS:UniProtKB.
DR GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; ISO:MGI.
DR CDD; cd00033; CCP; 1.
DR InterPro; IPR042372; IL15RA.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR PANTHER; PTHR15060; PTHR15060; 1.
DR Pfam; PF00084; Sushi; 1.
DR SMART; SM00032; CCP; 1.
DR SUPFAM; SSF57535; SSF57535; 1.
DR PROSITE; PS50923; SUSHI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Disulfide bond; Glycoprotein; Membrane;
KW Nucleus; Phosphoprotein; Receptor; Reference proteome; Secreted; Signal;
KW Sushi; Transmembrane; Transmembrane helix.
FT SIGNAL 1..32
FT /evidence="ECO:0000255"
FT CHAIN 33..263
FT /note="Interleukin-15 receptor subunit alpha"
FT /id="PRO_0000011045"
FT CHAIN 33..?
FT /note="Soluble interleukin-15 receptor subunit alpha"
FT /id="PRO_0000333856"
FT TOPO_DOM 33..205
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 227..263
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 34..98
FT /note="Sushi"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT REGION 113..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 36..78
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:17947230"
FT DISULFID 62..96
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:17947230"
FT VAR_SEQ 1..97
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:12885940,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_012627"
FT VAR_SEQ 98..128
FT /note="Missing (in isoform 4, isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:12885940,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_012628"
FT VAR_SEQ 129..140
FT /note="Missing (in isoform 2, isoform 3, isoform 4, isoform
FT 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:12885940,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_012629"
FT VAR_SEQ 141..161
FT /note="Missing (in isoform 2, isoform 3, isoform 4 and
FT isoform 6)"
FT /evidence="ECO:0000303|PubMed:12885940"
FT /id="VSP_012630"
FT VAR_SEQ 162..194
FT /note="Missing (in isoform 3, isoform 4 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:12885940"
FT /id="VSP_012631"
FT VAR_SEQ 195..206
FT /note="EISPHSSKMTKV -> M (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_012633"
FT VAR_SEQ 195
FT /note="E -> K (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:12885940"
FT /id="VSP_012632"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:2PSM"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:2PSM"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:2PSM"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:2PSM"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:2PSM"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:2PSM"
SQ 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