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IL15_CHLAE
ID   IL15_CHLAE              Reviewed;         162 AA.
AC   P40221;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Interleukin-15;
DE            Short=IL-15;
DE   Flags: Precursor;
GN   Name=IL15;
OS   Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Chlorocebus.
OX   NCBI_TaxID=9534;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 49-81.
RC   TISSUE=Kidney;
RX   PubMed=8178155; DOI=10.1126/science.8178155;
RA   Grabstein K.H., Eisenman J., Shanebeck K., Rauch C., Srinivasan S.,
RA   Fung V., Beers C., Richardson J., Schoenborn M.A., Ahdieh M., Johnson L.,
RA   Alderson M.R., Watson J.D., Anderson D.M., Giri J.G.;
RT   "Cloning of a T cell growth factor that interacts with the beta chain of
RT   the interleukin-2 receptor.";
RL   Science 264:965-968(1994).
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; U03099; AAA18416.1; -; mRNA.
DR   PIR; A53484; A53484.
DR   AlphaFoldDB; P40221; -.
DR   SMR; P40221; -.
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   1: Evidence at protein level;
KW   Cytokine; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Secreted; Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   PROPEP          30..48
FT                   /evidence="ECO:0000269|PubMed:8178155"
FT                   /id="PRO_0000015391"
FT   CHAIN           49..162
FT                   /note="Interleukin-15"
FT                   /id="PRO_0000015392"
FT   CARBOHYD        127
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"
SQ   SEQUENCE   162 AA;  18222 MW;  1BF9A82644E1C9B7 CRC64;
     MRISKPHLRS ISIQCYLCLL LKSHFLTEAG IHVFILGCFS AGLPKTEANW VNVISDLKKI
     EDLIQSMHID ATLYTESDVH PSCKVTAMKC FLLELQVISH ESGDTDIHDT VENLIILANN
     ILSSNGNITE SGCKECEELE EKNIKEFLQS FVHIVQMFIN TS
 
 
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