ID   IL5_MERUN               Reviewed;         132 AA.
AC   Q62575;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Interleukin-5;
DE            Short=IL-5;
DE   AltName: Full=Eosinophil differentiation factor;
DE   AltName: Full=T-cell replacing factor;
DE            Short=TRF;
DE   Flags: Precursor;
GN   Name=IL5;
OS   Meriones unguiculatus (Mongolian jird) (Gerbillus unguiculatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Gerbillinae; Meriones.
OX   NCBI_TaxID=10047;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Spleen;
RA   Mai Z., Klei T.R.;
RL   Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Homodimeric cytokine expressed predominantly by T-lymphocytes
CC       and NK cells that plays an important role in the survival,
CC       differentiation, and chemotaxis of eosinophils. Acts also on activated
CC       and resting B-cells to induce immunoglobulin production, growth, and
CC       differentiation (By similarity). Mechanistically, exerts its biological
CC       effects through a receptor composed of IL5RA subunit and the cytokine
CC       receptor common subunit beta/CSF2RB. Binding to the receptor leads to
CC       activation of various kinases including LYN, SYK and JAK2 and thereby
CC       propagates signals through the RAS-MAPK and JAK-STAT5 pathways
CC       respectively (By similarity). {ECO:0000250|UniProtKB:P04401,
CC       ECO:0000250|UniProtKB:P05113}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with IL5RA. Interacts
CC       with CSF2RB. {ECO:0000250|UniProtKB:P04401,
CC       ECO:0000250|UniProtKB:P05113}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P04401}.
CC   -!- SIMILARITY: Belongs to the IL-5 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; L37780; AAA65675.1; -; mRNA.
DR   AlphaFoldDB; Q62575; -.
DR   SMR; Q62575; -.
DR   Ensembl; ENSMUGT00000025203; ENSMUGP00000021958; ENSMUGG00000018446.
DR   OrthoDB; 1469027at2759; -.
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:0005137; F:interleukin-5 receptor binding; IEA:InterPro.
DR   GO; GO:0006955; P:immune response; IEA:InterPro.
DR   GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR   GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IEA:Ensembl.
DR   GO; GO:0002639; P:positive regulation of immunoglobulin production; IEA:Ensembl.
DR   GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR   GO; GO:0071803; P:positive regulation of podosome assembly; IEA:Ensembl.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
DR   Gene3D; 1.20.1250.10; -; 1.
DR   InterPro; IPR009079; 4_helix_cytokine-like_core.
DR   InterPro; IPR000186; IL-5.
DR   Pfam; PF02025; IL5; 1.
DR   PRINTS; PR00432; INTERLEUKIN5.
DR   SUPFAM; SSF47266; SSF47266; 1.
PE   2: Evidence at transcript level;
KW   Cytokine; Disulfide bond; Glycoprotein; Growth factor; Secreted; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..132
FT                   /note="Interleukin-5"
FT                   /id="PRO_0000015563"
FT   CARBOHYD        45
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        74
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        88
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        61
FT                   /note="Interchain (with C-103)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        103
FT                   /note="Interchain (with C-61)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   132 AA;  15164 MW;  60CE3852F9F84261 CRC64;
     MRLPLQLSIL TLAWVWAVAL EIPMSAVVKE TLIQLSTHRA LLTSNETVRL PVPTHKNHQL
     CIGEIFQGLD ILKNQTARGG AVETLFQNLS LIKKYIDRQK EKCGEERRRA RQFLDYLQEF
     LGVMSTEWTM EG