ID   IL5_MOUSE               Reviewed;         133 AA.
AC   P04401;
DT   20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1988, sequence version 1.
DT   27-MAR-2024, entry version 183.
DE   RecName: Full=Interleukin-5;
DE            Short=IL-5;
DE   AltName: Full=B-cell growth factor II;
DE            Short=BCGF-II;
DE   AltName: Full=Cytotoxic T-lymphocyte inducer;
DE   AltName: Full=Eosinophil differentiation factor;
DE   AltName: Full=T-cell replacing factor;
DE            Short=TRF;
DE   Flags: Precursor;
GN   Name=Il5; Synonyms=Il-5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3133208; DOI=10.1111/j.1432-1033.1988.tb14104.x;
RA   Campbell H.D., Sanderson C.J., Wang Y., Hort Y., Martinson M.E.,
RA   Tucker W.Q.J., Stellwagen A., Strath M., Young I.G.;
RT   "Isolation, structure and expression of cDNA and genomic clones for murine
RT   eosinophil differentiation factor. Comparison with other eosinophilopoietic
RT   lymphokines and identity with interleukin-5.";
RL   Eur. J. Biochem. 174:345-352(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/cJ;
RX   PubMed=3024009; DOI=10.1038/324070a0;
RA   Kinashi T., Harada N., Severinson E., Tanabe T., Sideras P., Konishi M.,
RA   Azuma C., Tominaga A., Bergstedt-Lindqvist S., Takahashi M., Matsuda F.,
RA   Yaoita Y., Takatsu K., Honjo T.;
RT   "Cloning of complementary DNA encoding T-cell replacing factor and identity
RT   with B-cell growth factor II.";
RL   Nature 324:70-73(1986).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=3078564; DOI=10.3109/08977198809000246;
RA   Mizuta T.R., Tanabe T., Nakakubo H., Noma T., Honjo T.;
RT   "Molecular cloning and structure of the mouse interleukin-5 gene.";
RL   Growth Factors 1:51-57(1988).
RN   [4]
RP   FUNCTION.
RX   PubMed=3128631; DOI=10.1084/jem.167.4.1377;
RA   Karasuyama H., Rolink A., Melchers F.;
RT   "Recombinant interleukin 2 or 5, but not 3 or 4, induces maturation of
RT   resting mouse B lymphocytes and propagates proliferation of activated B
RT   cell blasts.";
RL   J. Exp. Med. 167:1377-1390(1988).
RN   [5]
RP   GLYCOSYLATION AT ASN-46.
RX   PubMed=2215480; DOI=10.1016/0161-5890(90)90158-v;
RA   Takahashi T., Yamaguchi N., Mita S., Yamaguchi Y., Suda T., Tominaga A.,
RA   Kikuchi Y., Miura Y., Takatsu K.;
RT   "Structural comparison of murine T-cell (B151K12)-derived T-cell-replacing
RT   factor (IL-5) with rIL-5: dimer formation is essential for the expression
RT   of biological activity.";
RL   Mol. Immunol. 27:911-920(1990).
RN   [6]
RP   FUNCTION, AND INTERACTION WITH IL5RA.
RX   PubMed=1873482; DOI=10.1016/1043-4666(91)90503-6;
RA   Barry S.C., McKenzie A.N., Strath M., Sanderson C.J.;
RT   "Analysis of interleukin 5 receptors on murine eosinophils: a comparison
RT   with receptors on B13 cells.";
RL   Cytokine 3:339-344(1991).
RN   [7]
RP   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=10444455; DOI=10.1152/ajpgi.1999.277.2.g400;
RA   Vallance B.A., Blennerhassett P.A., Deng Y., Matthaei K.I., Young I.G.,
RA   Collins S.M.;
RT   "IL-5 contributes to worm expulsion and muscle hypercontractility in a
RT   primary T. spiralis infection.";
RL   Am. J. Physiol. 277:G400-G408(1999).
RN   [8] {ECO:0007744|PDB:3B5K}
RP   X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 21-133, AND DISULFIDE BONDS.
RA   Patino E., Kraich M., Kotzsch A., Saremba S., Paschke A., Sebald W.,
RA   Mueller T.D.;
RT   "Crystal structure of murine interleukin-5.";
RL   Submitted (OCT-2007) to the PDB data bank.
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 (PubMed:10444455,
CC       PubMed:1873482). Acts also on activated and resting B-cells to induce
CC       immunoglobulin production, growth, and differentiation
CC       (PubMed:3128631). Mechanistically, exerts its biological effects
CC       through a receptor composed of IL5RA subunit and the cytokine receptor
CC       common subunit beta/CSF2RB. Binding to the receptor leads to activation
CC       of various kinases including LYN, SYK and JAK2 and thereby propagates
CC       signals through the RAS-MAPK and JAK-STAT5 pathways respectively (By
CC       similarity). {ECO:0000250|UniProtKB:P05113,
CC       ECO:0000269|PubMed:10444455, ECO:0000269|PubMed:1873482,
CC       ECO:0000269|PubMed:3128631}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with IL5RA
CC       (PubMed:1873482). Interacts with CSF2RB. {ECO:0000250|UniProtKB:P05113,
CC       ECO:0000269|PubMed:1873482}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- DISRUPTION PHENOTYPE: In IL-5 deletion mice, the intestinal
CC       eosinophilia that developed in WT mice during T. spiralis infection was
CC       completely abolished, revealing the importance of IL5 for the increased
CC       production and recruitment of eosinophils to the gut during infection.
CC       {ECO:0000269|PubMed:10444455}.
CC   -!- SIMILARITY: Belongs to the IL-5 family. {ECO:0000305}.
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DR   EMBL; X06270; CAA29606.1; -; mRNA.
DR   EMBL; X06271; CAA29607.1; -; Genomic_DNA.
DR   EMBL; X04601; CAA28266.1; -; mRNA.
DR   CCDS; CCDS24685.1; -.
DR   PIR; S00807; ICMS5.
DR   RefSeq; NP_034688.1; NM_010558.1.
DR   PDB; 3B5K; X-ray; 2.50 A; A/B=21-133.
DR   PDBsum; 3B5K; -.
DR   AlphaFoldDB; P04401; -.
DR   SMR; P04401; -.
DR   STRING; 10090.ENSMUSP00000043369; -.
DR   BindingDB; P04401; -.
DR   ChEMBL; CHEMBL1163111; -.
DR   DrugCentral; P04401; -.
DR   GlyCosmos; P04401; 3 sites, No reported glycans.
DR   GlyGen; P04401; 3 sites.
DR   iPTMnet; P04401; -.
DR   PhosphoSitePlus; P04401; -.
DR   PaxDb; 10090-ENSMUSP00000043369; -.
DR   Antibodypedia; 4146; 935 antibodies from 42 providers.
DR   DNASU; 16191; -.
DR   Ensembl; ENSMUST00000048605.3; ENSMUSP00000043369.3; ENSMUSG00000036117.3.
DR   GeneID; 16191; -.
DR   KEGG; mmu:16191; -.
DR   UCSC; uc007iwv.1; mouse.
DR   AGR; MGI:96557; -.
DR   CTD; 3567; -.
DR   MGI; MGI:96557; Il5.
DR   VEuPathDB; HostDB:ENSMUSG00000036117; -.
DR   eggNOG; ENOG502RWD8; Eukaryota.
DR   GeneTree; ENSGT00390000016991; -.
DR   HOGENOM; CLU_156269_0_0_1; -.
DR   InParanoid; P04401; -.
DR   OMA; VPTHKNH; -.
DR   OrthoDB; 4626282at2759; -.
DR   PhylomeDB; P04401; -.
DR   TreeFam; TF338422; -.
DR   BioGRID-ORCS; 16191; 2 hits in 77 CRISPR screens.
DR   EvolutionaryTrace; P04401; -.
DR   PRO; PR:P04401; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; P04401; Protein.
DR   Bgee; ENSMUSG00000036117; Expressed in mesodermal cell in embryo and 7 other cell types or tissues.
DR   ExpressionAtlas; P04401; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; ISO:MGI.
DR   GO; GO:0005615; C:extracellular space; IDA:MGI.
DR   GO; GO:0005125; F:cytokine activity; IDA:MGI.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0005137; F:interleukin-5 receptor binding; ISO:MGI.
DR   GO; GO:0019221; P:cytokine-mediated signaling pathway; ISO:MGI.
DR   GO; GO:0006955; P:immune response; IEA:InterPro.
DR   GO; GO:0038043; P:interleukin-5-mediated signaling pathway; ISO:MGI.
DR   GO; GO:0030890; P:positive regulation of B cell proliferation; ISO:MGI.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR   GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:BHF-UCL.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:BHF-UCL.
DR   GO; GO:0045645; P:positive regulation of eosinophil differentiation; ISO:MGI.
DR   GO; GO:0002639; P:positive regulation of immunoglobulin production; IGI:BHF-UCL.
DR   GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:MGI.
DR   GO; GO:0071803; P:positive regulation of podosome assembly; ISO:MGI.
DR   GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; ISO:MGI.
DR   Gene3D; 1.20.1250.10; -; 1.
DR   InterPro; IPR009079; 4_helix_cytokine-like_core.
DR   InterPro; IPR000186; IL-5.
DR   PANTHER; PTHR48403; INTERLEUKIN-5; 1.
DR   PANTHER; PTHR48403:SF1; INTERLEUKIN-5; 1.
DR   Pfam; PF02025; IL5; 1.
DR   PRINTS; PR00432; INTERLEUKIN5.
DR   SUPFAM; SSF47266; 4-helical cytokines; 1.
DR   Genevisible; P04401; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Cytokine; Disulfide bond; Glycoprotein; Growth factor;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..20
FT   CHAIN           21..133
FT                   /note="Interleukin-5"
FT                   /id="PRO_0000015564"
FT   CARBOHYD        46
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:2215480"
FT   CARBOHYD        75
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        89
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        62
FT                   /note="Interchain (with C-104)"
FT                   /evidence="ECO:0000269|Ref.8, ECO:0007744|PDB:3B5K"
FT   DISULFID        104
FT                   /note="Interchain (with C-62)"
FT                   /evidence="ECO:0000269|Ref.8, ECO:0007744|PDB:3B5K"
FT   HELIX           28..38
FT                   /evidence="ECO:0007829|PDB:3B5K"
FT   HELIX           40..43
FT                   /evidence="ECO:0007829|PDB:3B5K"
FT   STRAND          50..52
FT                   /evidence="ECO:0007829|PDB:3B5K"
FT   STRAND          55..57
FT                   /evidence="ECO:0007829|PDB:3B5K"
FT   HELIX           59..62
FT                   /evidence="ECO:0007829|PDB:3B5K"
FT   HELIX           63..74
FT                   /evidence="ECO:0007829|PDB:3B5K"
FT   HELIX           83..102
FT                   /evidence="ECO:0007829|PDB:3B5K"
FT   TURN            103..105
FT                   /evidence="ECO:0007829|PDB:3B5K"
FT   STRAND          108..110
FT                   /evidence="ECO:0007829|PDB:3B5K"
FT   HELIX           111..125
FT                   /evidence="ECO:0007829|PDB:3B5K"
SQ   SEQUENCE   133 AA;  15410 MW;  C6DC091682452AF4 CRC64;
     MRRMLLHLSV LTLSCVWATA MEIPMSTVVK ETLTQLSAHR ALLTSNETMR LPVPTHKNHQ
     LCIGEIFQGL DILKNQTVRG GTVEMLFQNL SLIKKYIDRQ KEKCGEERRR TRQFLDYLQE
     FLGVMSTEWA MEG
//