ID   IL5_CERAT               Reviewed;         134 AA.
AC   P46685;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 87.
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   Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Cercocebus.
OX   NCBI_TaxID=9531;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=FUj;
RX   PubMed=7561102;
RA   Villinger F.J., Brar S.S., Mayne A.E., Chikkala N., Ansari A.A.;
RT   "Comparative sequence analysis of cytokine genes from human and nonhuman
RT   primates.";
RL   J. Immunol. 155:3946-3954(1995).
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; L26033; AAA99971.1; -; mRNA.
DR   AlphaFoldDB; P46685; -.
DR   SMR; P46685; -.
DR   STRING; 9531.ENSCATP00000016781; -.
DR   Proteomes; UP000233060; Whole Genome Shotgun Assembly.
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; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000250"
FT   CHAIN           20..134
FT                   /note="Interleukin-5"
FT                   /id="PRO_0000015557"
FT   CARBOHYD        22
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        47
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        90
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        63
FT                   /note="Interchain (with C-105)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        105
FT                   /note="Interchain (with C-63)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   134 AA;  15339 MW;  7BDD491C437981ED CRC64;
     MRMLLHLSLL ALGASYMYAI PTEIPTSALV KETLTLLSTH RTLLIGNETL RIPVPVHKHH
     QLCTEEIFQG IGTLESQTLQ GGTVERLFKN LSLIKKYIDG QKKKCGEERR RVNQFLDYLQ
     EFLGVMNTEW IIES