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