ID   IL4_CEREL               Reviewed;         135 AA.
AC   P51744;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Interleukin-4;
DE            Short=IL-4;
DE   AltName: Full=B-cell stimulatory factor 1;
DE            Short=BSF-1;
DE   AltName: Full=Lymphocyte stimulatory factor 1;
DE   Flags: Precursor;
GN   Name=IL4;
OS   Cervus elaphus (Red deer).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Cervidae;
OC   Cervinae; Cervus.
OX   NCBI_TaxID=9860;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8029646; DOI=10.1111/j.1365-3083.1994.tb03435.x;
RA   Hook S.M., Crawford A.M., Chinn D.N., Griffin J.F.T., Buchan G.S.;
RT   "Cloning and expression of the cervine interleukin 4 gene.";
RL   Scand. J. Immunol. 40:71-76(1994).
CC   -!- FUNCTION: Participates in at least several B-cell activation processes
CC       as well as of other cell types. It is a costimulator of DNA-synthesis.
CC       It induces the expression of class II MHC molecules on resting B-cells.
CC       It enhances both secretion and cell surface expression of IgE and IgG1.
CC       It also regulates the expression of the low affinity Fc receptor for
CC       IgE (CD23) on both lymphocytes and monocytes. Positively regulates
CC       IL31RA expression in macrophages. Stimulates autophagy in dendritic
CC       cells by interfering with mTORC1 signaling and through the induction of
CC       RUFY4. {ECO:0000250|UniProtKB:P07750}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the IL-4/IL-13 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; L07081; AAC37322.1; -; mRNA.
DR   PIR; I46142; I46142.
DR   AlphaFoldDB; P51744; -.
DR   SMR; P51744; -.
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:0005136; F:interleukin-4 receptor binding; IEA:InterPro.
DR   GO; GO:0042113; P:B cell activation; IEA:UniProtKB-KW.
DR   GO; GO:0006955; P:immune response; IEA:InterPro.
DR   GO; GO:0016239; P:positive regulation of macroautophagy; ISS:UniProtKB.
DR   Gene3D; 1.20.1250.10; -; 1.
DR   InterPro; IPR009079; 4_helix_cytokine-like_core.
DR   InterPro; IPR002354; IL-4.
DR   InterPro; IPR001325; IL-4/IL-13.
DR   InterPro; IPR018096; IL-4/IL-13_CS.
DR   PANTHER; PTHR47401; PTHR47401; 1.
DR   Pfam; PF00727; IL4; 1.
DR   PIRSF; PIRSF001941; Interleukin_4; 1.
DR   PRINTS; PR00431; INTERLEUKIN4.
DR   SMART; SM00190; IL4_13; 1.
DR   SUPFAM; SSF47266; SSF47266; 1.
DR   PROSITE; PS00838; INTERLEUKIN_4_13; 1.
PE   2: Evidence at transcript level;
KW   B-cell activation; Cytokine; Disulfide bond; Glycoprotein; Growth factor;
KW   Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..135
FT                   /note="Interleukin-4"
FT                   /id="PRO_0000015528"
FT   CARBOHYD        62
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        96
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        27..135
FT                   /evidence="ECO:0000250"
FT   DISULFID        48..85
FT                   /evidence="ECO:0000250"
FT   DISULFID        70..105
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   135 AA;  15156 MW;  6110E6EF31F4F266 CRC64;
     MGLTSQLIPV LVCLLACTSH FVHGHKCDIT LEEIIKTLNI LTARKNSCME LPVADVFAAP
     KNTTEKETLC RAGIELRRIY RSHTCLNRFL SRLDRNLSGL ASKTCSVNEA KTSTSTLKNL
     LERLKTIMKE KYSKC