IL2_CAPHI
ID IL2_CAPHI Reviewed; 155 AA.
AC P36835; P79156;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 91.
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 Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Blood;
RA Rimstad E.;
RT "The molecular cloning and expression of caprine interleukin 2.";
RL Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Beyer J.C., Cheevers W.P.;
RT "Nucleotide sequence of caprine interferon-gamma, interleukin-2 and
RT interleukin-4 cDNAs.";
RL Submitted (DEC-1996) 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.
CC -!- SIMILARITY: Belongs to the IL-2 family. {ECO:0000305}.
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DR EMBL; X76063; CAA53664.1; -; mRNA.
DR EMBL; U34274; AAB38527.1; -; mRNA.
DR PIR; S38662; S38662.
DR AlphaFoldDB; P36835; -.
DR SMR; P36835; -.
DR STRING; 9925.ENSCHIP00000029633; -.
DR Proteomes; UP000291000; Unassembled WGS sequence.
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 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; Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000250"
FT CHAIN 21..155
FT /note="Interleukin-2"
FT /id="PRO_0000015477"
FT CARBOHYD 23
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT DISULFID 79..127
FT /evidence="ECO:0000250"
FT CONFLICT 3..5
FT /note="RMQ -> QIP (in Ref. 2; AAB38527)"
FT /evidence="ECO:0000305"
FT CONFLICT 22
FT /note="P -> T (in Ref. 2; AAB38527)"
FT /evidence="ECO:0000305"
FT CONFLICT 30
FT /note="T -> P (in Ref. 2; AAB38527)"
FT /evidence="ECO:0000305"
FT CONFLICT 51
FT /note="L -> P (in Ref. 2; AAB38527)"
FT /evidence="ECO:0000305"
FT CONFLICT 71
FT /note="D -> A (in Ref. 2; AAB38527)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="D -> E (in Ref. 2; AAB38527)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="R -> L (in Ref. 2; AAB38527)"
FT /evidence="ECO:0000305"
FT CONFLICT 107..113
FT /note="YMASLKG -> SMDNIKR (in Ref. 2; AAB38527)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="Q -> L (in Ref. 2; AAB38527)"
FT /evidence="ECO:0000305"
FT CONFLICT 144
FT /note="T -> I (in Ref. 2; AAB38527)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="L -> M (in Ref. 2; AAB38527)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 155 AA; 17704 MW; 90022DFBB6AF78DE CRC64;
MYRMQLLSCI ALTLALVANG APTSSSTGNT MKEVKSLLLD LQLLLEKVKN LENLKLSRMH
TFNFYMPKVN DTELKHLKCL LEELKLLEDV LDLAPSKNRN TREIKDYMAS LKGIVLELQG
SETRFTCEYD DATVKAVEFQ NKWTTFCQSI YSTLT
