ID   IL15_MARMO              Reviewed;         162 AA.
AC   Q5WQV8; Q5EEK6;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=Interleukin-15;
DE            Short=IL-15;
DE   Flags: Precursor;
GN   Name=IL15;
OS   Marmota monax (Woodchuck).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC   Xerinae; Marmotini; Marmota.
OX   NCBI_TaxID=9995;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=16406557; DOI=10.1016/j.cyto.2005.11.007;
RA   Wang B., Lohrengel B., Lu Y., Meng Z., Xu Y., Yang D., Roggendorf M.,
RA   Lu M.;
RT   "Molecular characterization of woodchuck interleukin 15 (wIL-15) and
RT   detection of its expression in liver samples of woodchucks infected with
RT   woodchuck hepatitis virus (WHV).";
RL   Cytokine 32:296-303(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Berraondo P., Ochoa L., Crettaz J., Prieto J., Gonzalez-Aseguinolaza G.;
RT   "Molecular and functional characterization of woodchuck IL-15.";
RL   Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cytokine that stimulates the proliferation of T-lymphocytes.
CC       Stimulation by IL15 requires interaction of IL15 with components of the
CC       IL2 receptor, including IL2RB and probably IL2RG but not IL2RA (By
CC       similarity). In neutrophils, stimulates phagocytosis probably by
CC       signaling through the IL15 receptor, composed of the subunits IL15RA,
CC       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; AY426605; AAR83922.1; -; mRNA.
DR   EMBL; AY900230; AAW82751.1; -; mRNA.
DR   AlphaFoldDB; Q5WQV8; -.
DR   SMR; Q5WQV8; -.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR   GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR   GO; GO:0005126; F:cytokine receptor binding; IEA:InterPro.
DR   GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR   GO; GO:0006955; P:immune response; IEA:InterPro.
DR   GO; GO:0035723; P:interleukin-15-mediated signaling pathway; ISS:UniProtKB.
DR   GO; GO:0042119; P:neutrophil activation; ISS:UniProtKB.
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   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   2: Evidence at transcript level;
KW   Cytokine; Disulfide bond; Glycoprotein; Secreted; Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   PROPEP          30..48
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000358330"
FT   CHAIN           49..162
FT                   /note="Interleukin-15"
FT                   /id="PRO_5000092329"
FT   CARBOHYD        119
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        127
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        143
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        83..133
FT                   /evidence="ECO:0000250"
FT   DISULFID        90..136
FT                   /evidence="ECO:0000250"
FT   CONFLICT        42
FT                   /note="G -> S (in Ref. 2; AAW82751)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        55
FT                   /note="K -> R (in Ref. 2; AAW82751)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   162 AA;  18363 MW;  58CC3CB7A1325E0A CRC64;
     MRISKPHLRI TSIQCYVCLL LNTHFLTEAG IRVFILGCIS AGIPKTEANW EDVRKDLQKI
     ENLIQSLHMD ATLYTESDVH PRCKVTAMNC FLLELEVISH ESRDGDIEET VKNLILLANS
     SLSSNGNITE SGCKVCEELE EKNITEFLES FKHIVQMFIN PP