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Interleukin-5 (IL-5) (B-cell differentiation factor I) (Eosinophil differentiation factor) (T-cell replacing factor) (TRF)

 IL5_HUMAN               Reviewed;         134 AA.
P05113; Q13840;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
13-AUG-1987, sequence version 1.
02-JUN-2021, entry version 208.
RecName: Full=Interleukin-5;
Short=IL-5;
AltName: Full=B-cell differentiation factor I;
AltName: Full=Eosinophil differentiation factor;
AltName: Full=T-cell replacing factor;
Short=TRF;
Flags: Precursor;
Name=IL5;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3024129; DOI=10.1093/nar/14.22.9149;
Azuma C., Tanabe T., Konishi M., Kinashi T., Noma T., Matsuda F.,
Yaoita Y., Takatsu K., Hammarstroem L., Smith C.I.E., Severinson E.,
Honjo T.;
"Cloning of cDNA for human T-cell replacing factor (interleukin-5) and
comparison with the murine homologue.";
Nucleic Acids Res. 14:9149-9158(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2824500;
Tanabe T., Konishi M., Mizuta T., Noma T., Honjo T.;
"Molecular cloning and structure of the human interleukin-5 gene.";
J. Biol. Chem. 262:16580-16584(1987).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3498940; DOI=10.1073/pnas.84.19.6629;
Campbell H.D., Tucker W.Q.J., Hort Y., Martinson M.E., Mayo G.,
Clutterbuck E.J., Sanderson C.J., Young I.G.;
"Molecular cloning, nucleotide sequence, and expression of the gene
encoding human eosinophil differentiation factor (interleukin 5).";
Proc. Natl. Acad. Sci. U.S.A. 84:6629-6633(1987).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2823259; DOI=10.1073/pnas.84.21.7388;
Yokota T., Coffman R.L., Hagiwara H., Rennick D.M., Takebe Y., Yokota K.,
Gemmell L., Shrader B., Yang G., Meyerson P., Luh J., Hoy P., Pene J.,
Briere F., Spits H., Banchereau J., de Vries J., Lee F.D., Arai N.,
Arai K.;
"Isolation and characterization of lymphokine cDNA clones encoding mouse
and human IgA-enhancing factor and eosinophil colony-stimulating factor
activities: relationship to interleukin 5.";
Proc. Natl. Acad. Sci. U.S.A. 84:7388-7392(1987).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Honjo T., Takatsu K., Severinson E.;
Submitted (FEB-1992) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
SeattleSNPs variation discovery resource;
Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PROTEIN SEQUENCE OF 20-134, DISULFIDE BONDS, GLYCOSYLATION AT THR-22 AND
ASN-47, AND LACK OF GLYCOSYLATION AT ASN-90.
PubMed=2361960; DOI=10.1093/oxfordjournals.jbchem.a123041;
Minamitake Y., Kodama S., Katayama T., Adachi H., Tanaka S., Tsujimoto M.;
"Structure of recombinant human interleukin 5 produced by Chinese hamster
ovary cells.";
J. Biochem. 107:292-297(1990).
[9]
DISULFIDE BONDS.
PubMed=2037074; DOI=10.1016/0014-5793(91)80553-f;
Proudfoot A.E.I., Davies J.G., Turcatti G., Wingfield P.T.;
"Human interleukin-5 expressed in Escherichia coli: assignment of the
disulfide bridges of the purified unglycosylated protein.";
FEBS Lett. 283:61-64(1991).
[10]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), AND DISULFIDE BONDS.
PubMed=8483502; DOI=10.1038/363172a0;
Milburn M.V., Hassell A.M., Lambert M.H., Jordan S.R., Proudfoot A.E.I.,
Graber P., Wells T.N.C.;
"A novel dimer configuration revealed by the crystal structure at 2.4-A
resolution of human interleukin-5.";
Nature 363:172-176(1993).
[11]
X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 19-134 IN COMPLEX WITH IL5RA, AND
DISULFIDE BONDS.
PubMed=22153509; DOI=10.1016/j.str.2011.08.015;
Patino E., Kotzsch A., Saremba S., Nickel J., Schmitz W., Sebald W.,
Mueller T.D.;
"Structure analysis of the IL-5 ligand-receptor complex reveals a wrench-
like architecture for IL-5Ralpha.";
Structure 19:1864-1875(2011).
-!- FUNCTION: Factor that induces terminal differentiation of late-
developing B-cells to immunoglobulin secreting cells.
-!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:2037074,
ECO:0000269|PubMed:22153509, ECO:0000269|PubMed:2361960,
ECO:0000269|PubMed:8483502}.
-!- INTERACTION:
P05113; P32927: CSF2RB; NbExp=2; IntAct=EBI-2435811, EBI-1809771;
P05113; Q01344: IL5RA; NbExp=2; IntAct=EBI-2435811, EBI-1759442;
P05113; Q01344-2: IL5RA; NbExp=4; IntAct=EBI-2435811, EBI-15957545;
-!- SUBCELLULAR LOCATION: Secreted.
-!- SIMILARITY: Belongs to the IL-5 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Interleukin-5 entry;
URL="https://en.wikipedia.org/wiki/Interleukin_5";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/il5/";
---------------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
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EMBL; X04688; CAA28390.1; -; mRNA.
EMBL; J03478; AAA74469.1; -; Genomic_DNA.
EMBL; J02971; AAA98620.1; -; Genomic_DNA.
EMBL; X12705; CAA31210.1; -; mRNA.
EMBL; X12706; CAA31211.1; -; Genomic_DNA.
EMBL; AF353265; AAK19759.1; -; Genomic_DNA.
EMBL; BC066282; AAH66282.1; -; mRNA.
CCDS; CCDS4156.1; -.
PIR; A28477; A28477.
RefSeq; NP_000870.1; NM_000879.2.
RefSeq; XP_011541675.1; XM_011543373.2.
RefSeq; XP_011541676.1; XM_011543374.2.
PDB; 1HUL; X-ray; 2.40 A; A/B=24-131.
PDB; 3QT2; X-ray; 2.55 A; C/D/E/F=19-134.
PDB; 3VA2; X-ray; 2.70 A; A/B=23-134.
PDBsum; 1HUL; -.
PDBsum; 3QT2; -.
PDBsum; 3VA2; -.
SMR; P05113; -.
BioGRID; 109781; 2.
DIP; DIP-28N; -.
IntAct; P05113; 2.
STRING; 9606.ENSP00000231454; -.
BindingDB; P05113; -.
ChEMBL; CHEMBL1169600; -.
DrugBank; DB06612; Mepolizumab.
DrugBank; DB01411; Pranlukast.
DrugBank; DB06602; Reslizumab.
DrugCentral; P05113; -.
GlyGen; P05113; 2 sites.
iPTMnet; P05113; -.
PhosphoSitePlus; P05113; -.
BioMuta; IL5; -.
DMDM; 124341; -.
MassIVE; P05113; -.
PaxDb; P05113; -.
PeptideAtlas; P05113; -.
PRIDE; P05113; -.
ProteomicsDB; 51799; -.
ABCD; P05113; 12 sequenced antibodies.
Antibodypedia; 4146; 806 antibodies.
DNASU; 3567; -.
Ensembl; ENST00000231454; ENSP00000231454; ENSG00000113525.
GeneID; 3567; -.
KEGG; hsa:3567; -.
UCSC; uc003kxe.1; human.
CTD; 3567; -.
DisGeNET; 3567; -.
GeneCards; IL5; -.
HGNC; HGNC:6016; IL5.
HPA; ENSG00000113525; Tissue enhanced (blood, testis).
MIM; 147850; gene.
neXtProt; NX_P05113; -.
OpenTargets; ENSG00000113525; -.
PharmGKB; PA29833; -.
VEuPathDB; HostDB:ENSG00000113525.9; -.
eggNOG; ENOG502RWD8; Eukaryota.
GeneTree; ENSGT00390000016991; -.
HOGENOM; CLU_156269_0_0_1; -.
InParanoid; P05113; -.
OMA; NTEWTME; -.
OrthoDB; 1469027at2759; -.
PhylomeDB; P05113; -.
TreeFam; TF338422; -.
PathwayCommons; P05113; -.
Reactome; R-HSA-512988; Interleukin-3, Interleukin-5 and GM-CSF signaling.
Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
Reactome; R-HSA-912526; Interleukin receptor SHC signaling.
SignaLink; P05113; -.
SIGNOR; P05113; -.
BioGRID-ORCS; 3567; 6 hits in 981 CRISPR screens.
ChiTaRS; IL5; human.
EvolutionaryTrace; P05113; -.
GeneWiki; Interleukin_5; -.
GenomeRNAi; 3567; -.
Pharos; P05113; Tclin.
PRO; PR:P05113; -.
Proteomes; UP000005640; Chromosome 5.
RNAct; P05113; protein.
Bgee; ENSG00000113525; Expressed in testis and 105 other tissues.
ExpressionAtlas; P05113; baseline and differential.
Genevisible; P05113; HS.
GO; GO:0005576; C:extracellular region; IDA:BHF-UCL.
GO; GO:0005615; C:extracellular space; TAS:UniProtKB.
GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
GO; GO:0005137; F:interleukin-5 receptor binding; TAS:ProtInc.
GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
GO; GO:0006955; P:immune response; IEA:InterPro.
GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0030890; P:positive regulation of B cell proliferation; IEA:Ensembl.
GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IEA:Ensembl.
GO; GO:0045645; P:positive regulation of eosinophil differentiation; IEA:Ensembl.
GO; GO:0002639; P:positive regulation of immunoglobulin production; IEA:Ensembl.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
GO; GO:0071803; P:positive regulation of podosome assembly; IDA:BHF-UCL.
GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; IEA:Ensembl.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
InterPro; IPR009079; 4_helix_cytokine-like_core.
InterPro; IPR000186; IL-5.
Pfam; PF02025; IL5; 1.
PRINTS; PR00432; INTERLEUKIN5.
SUPFAM; SSF47266; SSF47266; 1.
1: Evidence at protein level;
3D-structure; Cytokine; Direct protein sequencing; Disulfide bond;
Glycoprotein; Growth factor; Reference proteome; Secreted; Signal.
SIGNAL 1..19
/evidence="ECO:0000269|PubMed:2361960"
CHAIN 20..134
/note="Interleukin-5"
/id="PRO_0000015560"
SITE 90
/note="Not glycosylated"
/evidence="ECO:0000269|PubMed:2361960"
CARBOHYD 22
/note="O-linked (GalNAc...) threonine"
/evidence="ECO:0000269|PubMed:2361960"
CARBOHYD 47
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000305|PubMed:2361960"
DISULFID 63
/note="Interchain (with C-105)"
/evidence="ECO:0000269|PubMed:2037074"
DISULFID 105
/note="Interchain (with C-63)"
/evidence="ECO:0000269|PubMed:2037074"
CONFLICT 88
/note="F -> L (in Ref. 5; CAA31210)"
/evidence="ECO:0000305"
HELIX 26..39
/evidence="ECO:0007829|PDB:1HUL"
HELIX 41..45
/evidence="ECO:0007829|PDB:1HUL"
STRAND 51..54
/evidence="ECO:0007829|PDB:1HUL"
STRAND 56..58
/evidence="ECO:0007829|PDB:1HUL"
HELIX 60..62
/evidence="ECO:0007829|PDB:1HUL"
HELIX 64..75
/evidence="ECO:0007829|PDB:1HUL"
HELIX 84..103
/evidence="ECO:0007829|PDB:1HUL"
STRAND 106..111
/evidence="ECO:0007829|PDB:1HUL"
HELIX 112..128
/evidence="ECO:0007829|PDB:1HUL"
SEQUENCE 134 AA; 15238 MW; DC984467179556A3 CRC64;
MRMLLHLSLL ALGAAYVYAI PTEIPTSALV KETLALLSTH RTLLIANETL RIPVPVHKNH
QLCTEEIFQG IGTLESQTVQ GGTVERLFKN LSLIKKYIDG QKKKCGEERR RVNQFLDYLQ
EFLGVMNTEW IIES


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[IL4] Interleukin-4 (IL-4) (B-cell stimulatory factor 1) (BSF-1) (Binetrakin) (Lymphocyte stimulatory factor 1) (Pitrakinra)
[Il6 Il-6] Interleukin-6 (IL-6) (B-cell hybridoma growth factor) (Interleukin HP-1)
[Il2 Il-2] Interleukin-2 (IL-2) (T-cell growth factor) (TCGF)
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[IL2] Interleukin-2 (IL-2) (T-cell growth factor) (TCGF) (Aldesleukin)
[Il2 Il-2] Interleukin-2 (IL-2) (T-cell growth factor) (TCGF)
[NRG1 GGF HGL HRGA NDF SMDF] Pro-neuregulin-1, membrane-bound isoform (Pro-NRG1) [Cleaved into: Neuregulin-1 (Acetylcholine receptor-inducing activity) (ARIA) (Breast cancer cell differentiation factor p45) (Glial growth factor) (Heregulin) (HRG) (Neu differentiation factor) (Sensory and motor neuron-derived factor)]
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[Cd4] T-cell surface glycoprotein CD4 (T-cell differentiation antigen L3T4) (T-cell surface antigen T4/Leu-3) (CD antigen CD4)
[Il18 Igif] Interleukin-18 (IL-18) (Interferon gamma-inducing factor) (IFN-gamma-inducing factor) (Interleukin-1 gamma) (IL-1 gamma)
[Cebpb Crp2 Nf-il6 Sfb] CCAAT/enhancer-binding protein beta (C/EBP beta) (C/EBP-related protein 2) (Interleukin-6-dependent-binding protein) (IL-6DBP) (Liver-enriched inhibitory protein) (LIP) (Liver-enriched transcriptional activator) (LAP) (Silencer factor B) (SF-B)
[Il18 Igif] Interleukin-18 (IL-18) (Interferon gamma-inducing factor) (IFN-gamma-inducing factor) (Interleukin-1 gamma) (IL-1 gamma)
[IL18 IGIF] Interleukin-18 (IL-18) (Interferon gamma-inducing factor) (IFN-gamma-inducing factor) (Interleukin-1 gamma) (IL-1 gamma)
[IL18 IGIF] Interleukin-18 (IL-18) (Interferon gamma-inducing factor) (IFN-gamma-inducing factor) (Interleukin-1 gamma) (IL-1 gamma)
[Cd40lg Cd40l Tnfsf5] CD40 ligand (CD40-L) (T-cell antigen Gp39) (TNF-related activation protein) (TRAP) (Tumor necrosis factor ligand superfamily member 5) (CD antigen CD154) [Cleaved into: CD40 ligand, membrane form; CD40 ligand, soluble form (sCD40L)]
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[NEUROD1 NEUROD] Neurogenic differentiation factor 1 (NeuroD1) (Beta-cell E-box transcriptional activator 2) (Beta2)
[NFIL3 E4BP4 IL3BP1] Nuclear factor interleukin-3-regulated protein (E4 promoter-binding protein 4) (Interleukin-3 promoter transcriptional activator) (Interleukin-3-binding protein 1) (Transcriptional activator NF-IL3A)
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[Asap1 Ddef1 Kiaa1249 Shag1] Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1 (130 kDa phosphatidylinositol 4,5-bisphosphate-dependent ARF1 GTPase-activating protein) (ADP-ribosylation factor-directed GTPase-activating protein 1) (ARF GTPase-activating protein 1) (Development and differentiation-enhancing factor 1) (DEF-1) (Differentiation-enhancing factor 1) (PIP2-dependent ARF1 GAP)
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[LEF1] Lymphoid enhancer-binding factor 1 (LEF-1) (T cell-specific transcription factor 1-alpha) (TCF1-alpha)
[Tbx21 Tbet Tblym] T-box transcription factor TBX21 (T-box protein 21) (T-cell-specific T-box transcription factor T-bet) (Transcription factor TBLYM)
[CXCL12 SDF1 SDF1A SDF1B] Stromal cell-derived factor 1 (SDF-1) (hSDF-1) (C-X-C motif chemokine 12) (Intercrine reduced in hepatomas) (IRH) (hIRH) (Pre-B cell growth-stimulating factor) (PBSF) [Cleaved into: SDF-1-beta(3-72); SDF-1-alpha(3-67)]
[GDF5 BMP14 CDMP1] Growth/differentiation factor 5 (GDF-5) (Bone morphogenetic protein 14) (BMP-14) (Cartilage-derived morphogenetic protein 1) (CDMP-1) (Lipopolysaccharide-associated protein 4) (LAP-4) (LPS-associated protein 4) (Radotermin)
[Nfatc2 Nfat1 Nfatp] Nuclear factor of activated T-cells, cytoplasmic 2 (NF-ATc2) (NFATc2) (NFAT pre-existing subunit) (NF-ATp) (T-cell transcription factor NFAT1)

Bibliography :
[25566252] Revisiting the identification and cDNA cloning of T cell-replacing factor/interleukin-5.
[3260684] Biological characterization of T cell-replacing factor in the synovial fluid of rheumatoid arthritis patients.
[3495803] Interleukin 5, a T-cell-derived B-cell differentiation factor also induces cytotoxic T lymphocytes.
[3024009] Cloning of complementary DNA encoding T-cell replacing factor and identity with B-cell growth factor II.