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IL2_BOSTR
ID   IL2_BOSTR               Reviewed;         155 AA.
AC   Q4U313;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Interleukin-2;
DE            Short=IL-2;
DE   AltName: Full=T-cell growth factor;
DE            Short=TCGF;
DE   Flags: Precursor;
GN   Name=IL2;
OS   Boselaphus tragocamelus (Nilgai).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Boselaphus.
OX   NCBI_TaxID=9917;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Saini M., Das D.K., Swarup D., Yadav M.P., Gupta P.K.;
RT   "Nucleotide and amino acid sequence comparison of Boselaphus tragocamelus
RT   IL-2 with other ruminants.";
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cytokine produced by activated CD4-positive helper T-cells
CC       and to a lesser extend activated CD8-positive T-cells and natural
CC       killer (NK) cells that plays pivotal roles in the immune response and
CC       tolerance. Binds to a receptor complex composed of either the high-
CC       affinity trimeric IL-2R (IL2RA/CD25, IL2RB/CD122 and IL2RG/CD132) or
CC       the low-affinity dimeric IL-2R (IL2RB and IL2RG). Interaction with the
CC       receptor leads to oligomerization and conformation changes in the IL-2R
CC       subunits resulting in downstream signaling starting with
CC       phosphorylation of JAK1 and JAK3. In turn, JAK1 and JAK3 phosphorylate
CC       the receptor to form a docking site leading to the phosphorylation of
CC       several substrates including STAT5. This process leads to activation of
CC       several pathways including STAT, phosphoinositide-3-kinase/PI3K and
CC       mitogen-activated protein kinase/MAPK pathways. Functions as a T-cell
CC       growth factor and can increase NK-cell cytolytic activity as well.
CC       Promotes strong proliferation of activated B-cells and subsequently
CC       immunoglobulin production. Plays a pivotal role in regulating the
CC       adaptive immune system by controlling the survival and proliferation of
CC       regulatory T-cells, which are required for the maintenance of immune
CC       tolerance. Moreover, participates in the differentiation and
CC       homeostasis of effector T-cell subsets, including Th1, Th2, Th17 as
CC       well as memory CD8-positive T-cells. {ECO:0000250|UniProtKB:P60568}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the IL-2 family. {ECO:0000305}.
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DR   EMBL; DQ017831; AAY41281.1; -; mRNA.
DR   AlphaFoldDB; Q4U313; -.
DR   SMR; Q4U313; -.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR   GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0005134; F:interleukin-2 receptor binding; IEA:InterPro.
DR   GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR   GO; GO:0009893; P:positive regulation of metabolic process; IEA:UniProt.
DR   Gene3D; 1.20.1250.10; -; 1.
DR   InterPro; IPR009079; 4_helix_cytokine-like_core.
DR   InterPro; IPR000779; IL-2.
DR   InterPro; IPR030477; IL-2_CS.
DR   Pfam; PF00715; IL2; 1.
DR   PRINTS; PR00265; INTERLEUKIN2.
DR   SMART; SM00189; IL2; 1.
DR   SUPFAM; SSF47266; SSF47266; 1.
DR   PROSITE; PS00424; INTERLEUKIN_2; 1.
PE   2: Evidence at transcript level;
KW   Adaptive immunity; Cytokine; Disulfide bond; Glycoprotein; Growth factor;
KW   Immunity; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000250"
FT   CHAIN           21..155
FT                   /note="Interleukin-2"
FT                   /id="PRO_0000253501"
FT   CARBOHYD        23
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250"
FT   DISULFID        79..127
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   155 AA;  17693 MW;  21AF33394CDF380D CRC64;
     MYKIQLLSCI ALTLALVANG APTSSSTGNT MKEVKSLLLD LQLLLEKVKN PENLKHSRMH
     TFNFYVPKVN ATELKHLKCL LEELKLLEEV LNLAPSKNLN PREIKDSMDN IKRIVLELQG
     SETRFTCEYD DVTVKAVEFL NKWITFCQSI YSTMT
 
 
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