ID   IL15_BUBBU              Reviewed;         162 AA.
AC   Q4GZL1;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 44.
DE   RecName: Full=Interleukin-15;
DE            Short=IL-15;
DE   Flags: Precursor;
GN   Name=IL15;
OS   Bubalus bubalis (Domestic water buffalo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bubalus.
OX   NCBI_TaxID=89462;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Spleen;
RA   Tiwari M., Ahsan Z., Srivastava J., Pathak D., Ali S., Garg L.C.;
RT   "Cloning and sequencing of interleukin-15 gene of Bubalus bubalis.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Tiwari M., Ahsan Z., Pathak D., Srivastava J., Ali S., Garg L.C.;
RL   Submitted (JUN-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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the IL-15/IL-21 family. {ECO:0000305}.
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DR   EMBL; AJ891036; CAI94538.1; -; mRNA.
DR   EMBL; DQ083522; AAY83832.1; -; mRNA.
DR   AlphaFoldDB; Q4GZL1; -.
DR   SMR; Q4GZL1; -.
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_0000233183"
FT   CHAIN           49..162
FT                   /note="Interleukin-15"
FT                   /id="PRO_0000233184"
FT   CARBOHYD        113
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        121
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
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;  18465 MW;  D7E2CBE23CF142F8 CRC64;
     MRILKPYLRS TSIQCYLCLL LNSHFLTEAG IHVFILGCIS AGLPKTEANW QYVINDLKTI
     EHLIQSIHMD ATLYTEGDAH PNCKVTAMQC FLLELRVILH ESKNAAIYEI IENLTMLANS
     NLSSIENKTE LGCKECEELE EKSIKEFLKS FVHIVKMFIN TS