IL15_MOUSE
ID IL15_MOUSE Reviewed; 162 AA.
AC P48346;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Interleukin-15;
DE Short=IL-15;
DE Flags: Precursor;
GN Name=Il15;
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].
RC STRAIN=WC/REJ X C57BL/6J; TISSUE=Bone marrow;
RX PubMed=7759105; DOI=10.1016/0888-7543(95)80013-c;
RA Anderson D.M., Johnson L., Glaccum M.B., Copeland N.G., Gilbert D.J.,
RA Jenkins N.A., Valentine V., Kirstein M.N., Shapiro D.N., Morris S.W.,
RA Grabstein K., Cosman D.;
RT "Chromosomal assignment and genomic structure of IL15.";
RL Genomics 25:701-706(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 [3]
RP X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS) OF 42-162 IN COMPLEX WITH IL15RA,
RP 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: Cytokine that stimulates the proliferation of T-lymphocytes.
CC Stimulation by IL-15 requires interaction of IL-15 with components of
CC IL-2R, including IL-2R beta and probably IL-2R gamma but not IL-2R
CC alpha (By similarity). In neutrophils, stimulates phagocytosis probably
CC by signaling through the IL15 receptor, composed of the subunits
CC IL15RA, IL2RB and IL2RG, which results in kinase SYK activation (By
CC similarity). {ECO:0000250|UniProtKB:P40933}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the IL-15/IL-21 family. {ECO:0000305}.
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DR EMBL; U14332; AAA75377.1; -; mRNA.
DR EMBL; BC023698; AAH23698.1; -; mRNA.
DR CCDS; CCDS40401.1; -.
DR PIR; I49124; I49124.
DR RefSeq; NP_001241676.1; NM_001254747.1.
DR RefSeq; NP_032383.1; NM_008357.2.
DR RefSeq; XP_006530768.1; XM_006530705.3.
DR RefSeq; XP_006530769.1; XM_006530706.3.
DR RefSeq; XP_006530770.1; XM_006530707.3.
DR RefSeq; XP_006530771.1; XM_006530708.3.
DR RefSeq; XP_006530772.1; XM_006530709.2.
DR RefSeq; XP_006530773.1; XM_006530710.2.
DR RefSeq; XP_006530774.1; XM_006530711.3.
DR RefSeq; XP_006530775.1; XM_006530712.3.
DR RefSeq; XP_006530776.1; XM_006530713.3.
DR RefSeq; XP_011246614.1; XM_011248312.2.
DR RefSeq; XP_011246615.1; XM_011248313.2.
DR RefSeq; XP_011246616.1; XM_011248314.2.
DR PDB; 2PSM; X-ray; 2.19 A; A/B=49-162.
DR PDBsum; 2PSM; -.
DR AlphaFoldDB; P48346; -.
DR SMR; P48346; -.
DR STRING; 10090.ENSMUSP00000034148; -.
DR GlyGen; P48346; 3 sites.
DR PhosphoSitePlus; P48346; -.
DR PaxDb; P48346; -.
DR PRIDE; P48346; -.
DR ProteomicsDB; 267121; -.
DR Antibodypedia; 3844; 1019 antibodies from 43 providers.
DR DNASU; 16168; -.
DR Ensembl; ENSMUST00000034148; ENSMUSP00000034148; ENSMUSG00000031712.
DR Ensembl; ENSMUST00000209363; ENSMUSP00000147848; ENSMUSG00000031712.
DR Ensembl; ENSMUST00000209573; ENSMUSP00000148256; ENSMUSG00000031712.
DR GeneID; 16168; -.
DR KEGG; mmu:16168; -.
DR UCSC; uc009mjk.2; mouse.
DR CTD; 3600; -.
DR MGI; MGI:103014; Il15.
DR VEuPathDB; HostDB:ENSMUSG00000031712; -.
DR eggNOG; ENOG502SCMF; Eukaryota.
DR GeneTree; ENSGT00390000016264; -.
DR HOGENOM; CLU_135111_0_0_1; -.
DR InParanoid; P48346; -.
DR OMA; ANWQDVI; -.
DR OrthoDB; 1521691at2759; -.
DR PhylomeDB; P48346; -.
DR TreeFam; TF336199; -.
DR Reactome; R-MMU-8983432; Interleukin-15 signaling.
DR BioGRID-ORCS; 16168; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Il15; mouse.
DR EvolutionaryTrace; P48346; -.
DR PRO; PR:P48346; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P48346; protein.
DR Bgee; ENSMUSG00000031712; Expressed in granulocyte and 139 other tissues.
DR ExpressionAtlas; P48346; baseline and differential.
DR Genevisible; P48346; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005125; F:cytokine activity; IDA:MGI.
DR GO; GO:0005126; F:cytokine receptor binding; IEA:InterPro.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0048469; P:cell maturation; IGI:MGI.
DR GO; GO:0071305; P:cellular response to vitamin D; IEA:Ensembl.
DR GO; GO:0045062; P:extrathymic T cell selection; IMP:MGI.
DR GO; GO:0030212; P:hyaluronan metabolic process; ISO:MGI.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
DR GO; GO:0035723; P:interleukin-15-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0048535; P:lymph node development; IMP:MGI.
DR GO; GO:0030225; P:macrophage differentiation; ISO:MGI.
DR GO; GO:0001779; P:natural killer cell differentiation; IDA:MGI.
DR GO; GO:0001787; P:natural killer cell proliferation; IDA:MGI.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:0042119; P:neutrophil activation; ISS:UniProtKB.
DR GO; GO:0001866; P:NK T cell proliferation; IMP:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0001819; P:positive regulation of cytokine production; IBA:GO_Central.
DR GO; GO:0050778; P:positive regulation of immune response; IMP:MGI.
DR GO; GO:0032740; P:positive regulation of interleukin-17 production; ISO:MGI.
DR GO; GO:0032825; P:positive regulation of natural killer cell differentiation; IDA:MGI.
DR GO; GO:0032819; P:positive regulation of natural killer cell proliferation; IDA:MGI.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
DR GO; GO:0050766; P:positive regulation of phagocytosis; ISS:UniProtKB.
DR GO; GO:1904100; P:positive regulation of protein O-linked glycosylation; IMP:MGI.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; IMP:MGI.
DR GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; ISO:MGI.
DR GO; GO:0050691; P:regulation of defense response to virus by host; IMP:MGI.
DR GO; GO:0045580; P:regulation of T cell differentiation; IMP:MGI.
DR GO; GO:0014732; P:skeletal muscle atrophy; IEA:Ensembl.
DR GO; GO:0007260; P:tyrosine phosphorylation of STAT protein; ISO:MGI.
DR Gene3D; 1.20.1250.70; -; 1.
DR InterPro; IPR009079; 4_helix_cytokine-like_core.
DR InterPro; IPR020439; IL-15.
DR InterPro; IPR003443; IL-15/IL-21_fam.
DR InterPro; IPR020466; IL-15_mml.
DR PANTHER; PTHR14356; PTHR14356; 1.
DR Pfam; PF02372; IL15; 1.
DR PRINTS; PR01947; INTLKN15MAML.
DR PRINTS; PR01930; INTRLEUKIN15.
DR SUPFAM; SSF47266; SSF47266; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytokine; Disulfide bond; Glycoprotein; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT PROPEP 30..48
FT /evidence="ECO:0000255"
FT /id="PRO_0000015399"
FT CHAIN 49..162
FT /note="Interleukin-15"
FT /id="PRO_0000015400"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 83..133
FT /evidence="ECO:0000269|PubMed:17947230"
FT DISULFID 90..136
FT /evidence="ECO:0000269|PubMed:17947230"
FT HELIX 49..63
FT /evidence="ECO:0007829|PDB:2PSM"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:2PSM"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:2PSM"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:2PSM"
FT HELIX 84..101
FT /evidence="ECO:0007829|PDB:2PSM"
FT HELIX 105..124
FT /evidence="ECO:0007829|PDB:2PSM"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:2PSM"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:2PSM"
FT HELIX 144..160
FT /evidence="ECO:0007829|PDB:2PSM"
SQ SEQUENCE 162 AA; 18593 MW; 68C971498CEBF296 CRC64;
MKILKPYMRN TSISCYLCFL LNSHFLTEAG IHVFILGCVS VGLPKTEANW IDVRYDLEKI
ESLIQSIHID TTLYTDSDFH PSCKVTAMNC FLLELQVILH EYSNMTLNET VRNVLYLANS
TLSSNKNVAE SGCKECEELE EKTFTEFLQS FIRIVQMFIN TS
