ID   IL5_SIGHI               Reviewed;         132 AA.
AC   Q9ESI9;
DT   05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 73.
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   Sigmodon hispidus (Hispid cotton rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Sigmodontinae; Sigmodon.
OX   NCBI_TaxID=42415;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Spleen;
RX   PubMed=11054577; DOI=10.1016/s0378-1119(00)00366-8;
RA   Houard S., Jacquet A., Haumont M., Daminet V., Milican F., Glineur F.,
RA   Bollen A.;
RT   "Cloning, expression and purification of recombinant cotton rat
RT   interleukin-5.";
RL   Gene 257:149-155(2000).
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}.
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DR   EMBL; AF148211; AAG16722.1; -; mRNA.
DR   AlphaFoldDB; Q9ESI9; -.
DR   SMR; Q9ESI9; -.
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   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..19
FT                   /evidence="ECO:0000250"
FT   CHAIN           20..132
FT                   /note="Interleukin-5"
FT                   /id="PRO_0000015567"
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;  15434 MW;  B328B81B2371FEB9 CRC64;
     MRMLLHLSIL TLACVWTFAV EIPMHTVVKE TLIQLSTHRA LLTSNETVRL PVPTHKNHQL
     CIGEIFRGLD ILKNQTVRGG TVETLFQNLS LIKKYIDRQK EKCGEERRRT RQFLDYLQEF
     LGVMGTEWTM EH