IL5_MOUSE
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 03-AUG-2022, entry version 174.
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
CC (PubMed:10444455,PubMed:1873482). Acts also on activated and resting B-
CC cells to induce 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 GlyGen; P04401; 3 sites.
DR iPTMnet; P04401; -.
DR PhosphoSitePlus; P04401; -.
DR PaxDb; P04401; -.
DR PRIDE; P04401; -.
DR Antibodypedia; 4146; 800 antibodies from 40 providers.
DR DNASU; 16191; -.
DR Ensembl; ENSMUST00000048605; ENSMUSP00000043369; ENSMUSG00000036117.
DR GeneID; 16191; -.
DR KEGG; mmu:16191; -.
DR UCSC; uc007iwv.1; mouse.
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; RWRVKKF; -.
DR OrthoDB; 1469027at2759; -.
DR PhylomeDB; P04401; -.
DR TreeFam; TF338422; -.
DR BioGRID-ORCS; 16191; 2 hits in 72 CRISPR screens.
DR EvolutionaryTrace; P04401; -.
DR PRO; PR:P04401; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P04401; protein.
DR Bgee; ENSMUSG00000036117; Expressed in perirhinal cortex and 6 other tissues.
DR ExpressionAtlas; P04401; baseline and differential.
DR Genevisible; P04401; MM.
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:0006954; P:inflammatory response; IEA:Ensembl.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA: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: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 GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:BHF-UCL.
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 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
