ID IL5_HUMAN Reviewed; 134 AA. AC P05113; Q13840; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 13-AUG-1987, sequence version 1. DT 11-NOV-2015, entry version 172. DE RecName: Full=Interleukin-5; DE Short=IL-5; DE AltName: Full=B-cell differentiation factor I; DE AltName: Full=Eosinophil differentiation factor; DE AltName: Full=T-cell replacing factor; DE Short=TRF; DE Flags: Precursor; GN Name=IL5; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3024129; DOI=10.1093/nar/14.22.9149; RA Azuma C., Tanabe T., Konishi M., Kinashi T., Noma T., Matsuda F., RA Yaoita Y., Takatsu K., Hammarstroem L., Smith C.I.E., Severinson E., RA Honjo T.; RT "Cloning of cDNA for human T-cell replacing factor (interleukin-5) and RT comparison with the murine homologue."; RL Nucleic Acids Res. 14:9149-9158(1986). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2824500; RA Tanabe T., Konishi M., Mizuta T., Noma T., Honjo T.; RT "Molecular cloning and structure of the human interleukin-5 gene."; RL J. Biol. Chem. 262:16580-16584(1987). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3498940; DOI=10.1073/pnas.84.19.6629; RA Campbell H.D., Tucker W.Q.J., Hort Y., Martinson M.E., Mayo G., RA Clutterbuck E.J., Sanderson C.J., Young I.G.; RT "Molecular cloning, nucleotide sequence, and expression of the gene RT encoding human eosinophil differentiation factor (interleukin 5)."; RL Proc. Natl. Acad. Sci. U.S.A. 84:6629-6633(1987). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2823259; DOI=10.1073/pnas.84.21.7388; RA Yokota T., Coffman R.L., Hagiwara H., Rennick D.M., Takebe Y., RA Yokota K., Gemmell L., Shrader B., Yang G., Meyerson P., Luh J., RA Hoy P., Pene J., Briere F., Spits H., Banchereau J., de Vries J., RA Lee F.D., Arai N., Arai K.; RT "Isolation and characterization of lymphokine cDNA clones encoding RT mouse and human IgA-enhancing factor and eosinophil colony-stimulating RT factor activities: relationship to interleukin 5."; RL Proc. Natl. Acad. Sci. U.S.A. 84:7388-7392(1987). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RA Honjo T., Takatsu K., Severinson E.; RL Submitted (FEB-1992) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RG SeattleSNPs variation discovery resource; RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP PROTEIN SEQUENCE OF 20-134, DISULFIDE BONDS, GLYCOSYLATION AT THR-22 RP AND ASN-47, AND LACK OF GLYCOSYLATION AT ASN-90. RX PubMed=2361960; RA Minamitake Y., Kodama S., Katayama T., Adachi H., Tanaka S., RA Tsujimoto M.; RT "Structure of recombinant human interleukin 5 produced by Chinese RT hamster ovary cells."; RL J. Biochem. 107:292-297(1990). RN [9] RP DISULFIDE BONDS. RX PubMed=2037074; DOI=10.1016/0014-5793(91)80553-F; RA Proudfoot A.E.I., Davies J.G., Turcatti G., Wingfield P.T.; RT "Human interleukin-5 expressed in Escherichia coli: assignment of the RT disulfide bridges of the purified unglycosylated protein."; RL FEBS Lett. 283:61-64(1991). RN [10] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), AND DISULFIDE BONDS. RX PubMed=8483502; DOI=10.1038/363172a0; RA Milburn M.V., Hassell A.M., Lambert M.H., Jordan S.R., RA Proudfoot A.E.I., Graber P., Wells T.N.C.; RT "A novel dimer configuration revealed by the crystal structure at 2.4- RT A resolution of human interleukin-5."; RL Nature 363:172-176(1993). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 19-134 IN COMPLEX WITH RP IL5RA, AND DISULFIDE BONDS. RX PubMed=22153509; DOI=10.1016/j.str.2011.08.015; RA Patino E., Kotzsch A., Saremba S., Nickel J., Schmitz W., Sebald W., RA Mueller T.D.; RT "Structure analysis of the IL-5 ligand-receptor complex reveals a RT wrench-like architecture for IL-5Ralpha."; RL Structure 19:1864-1875(2011). CC -!- FUNCTION: Factor that induces terminal differentiation of late- CC developing B-cells to immunoglobulin secreting cells. CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:2037074, CC ECO:0000269|PubMed:22153509, ECO:0000269|PubMed:2361960, CC ECO:0000269|PubMed:8483502}. CC -!- INTERACTION: CC P32927:CSF2RB; NbExp=2; IntAct=EBI-2435811, EBI-1809771; CC Q01344:IL5RA; NbExp=2; IntAct=EBI-2435811, EBI-1759442; CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- SIMILARITY: Belongs to the IL-5 family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=R&D Systems' cytokine mini-reviews: IL-5; CC URL="http://www.rndsystems.com/molecule_detail.aspx?m=1646"; CC -!- WEB RESOURCE: Name=Wikipedia; Note=Interleukin-5 entry; CC URL="https://en.wikipedia.org/wiki/Interleukin_5"; CC -!- WEB RESOURCE: Name=SeattleSNPs; CC URL="http://pga.gs.washington.edu/data/il5/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X04688; CAA28390.1; -; mRNA. DR EMBL; J03478; AAA74469.1; -; Genomic_DNA. DR EMBL; J02971; AAA98620.1; -; Genomic_DNA. DR EMBL; X12705; CAA31210.1; -; mRNA. DR EMBL; X12706; CAA31211.1; -; Genomic_DNA. DR EMBL; AF353265; AAK19759.1; -; Genomic_DNA. DR EMBL; BC066282; AAH66282.1; -; mRNA. DR CCDS; CCDS4156.1; -. DR PIR; A28477; A28477. DR RefSeq; NP_000870.1; NM_000879.2. DR RefSeq; XP_011541675.1; XM_011543373.1. DR RefSeq; XP_011541676.1; XM_011543374.1. DR UniGene; Hs.2247; -. DR PDB; 1HUL; X-ray; 2.40 A; A/B=24-131. DR PDB; 3QT2; X-ray; 2.55 A; C/D/E/F=19-134. DR PDB; 3VA2; X-ray; 2.70 A; A/B=23-134. DR PDBsum; 1HUL; -. DR PDBsum; 3QT2; -. DR PDBsum; 3VA2; -. DR ProteinModelPortal; P05113; -. DR SMR; P05113; 24-131. DR BioGrid; 109781; 3. DR DIP; DIP-28N; -. DR IntAct; P05113; 2. DR STRING; 9606.ENSP00000231454; -. DR BindingDB; P05113; -. DR ChEMBL; CHEMBL1169600; -. DR DrugBank; DB01411; Pranlukast. DR BioMuta; IL5; -. DR DMDM; 124341; -. DR PaxDb; P05113; -. DR PeptideAtlas; P05113; -. DR PRIDE; P05113; -. DR Ensembl; ENST00000231454; ENSP00000231454; ENSG00000113525. DR GeneID; 3567; -. DR KEGG; hsa:3567; -. DR UCSC; uc003kxe.1; human. DR CTD; 3567; -. DR GeneCards; IL5; -. DR HGNC; HGNC:6016; IL5. DR HPA; CAB010304; -. DR MIM; 147850; gene. DR neXtProt; NX_P05113; -. DR PharmGKB; PA29833; -. DR eggNOG; ENOG410IYJN; Eukaryota. DR eggNOG; ENOG41117ER; LUCA. DR GeneTree; ENSGT00390000016991; -. DR HOGENOM; HOG000074049; -. DR HOVERGEN; HBG003865; -. DR InParanoid; P05113; -. DR KO; K05428; -. DR OMA; GVINTEW; -. DR OrthoDB; EOG70PC0S; -. DR PhylomeDB; P05113; -. DR TreeFam; TF338422; -. DR Reactome; R-HSA-114604; GPVI-mediated activation cascade. DR Reactome; R-HSA-392451; G beta:gamma signalling through PI3Kgamma. DR Reactome; R-HSA-512988; Interleukin-3, 5 and GM-CSF signaling. DR Reactome; R-HSA-5673001; RAF/MAP kinase cascade. DR Reactome; R-HSA-912526; Interleukin receptor SHC signaling. DR SignaLink; P05113; -. DR ChiTaRS; IL5; human. DR EvolutionaryTrace; P05113; -. DR GeneWiki; Interleukin_5; -. DR GenomeRNAi; 3567; -. DR NextBio; 13932; -. DR PRO; PR:P05113; -. DR Proteomes; UP000005640; Chromosome 5. DR Bgee; P05113; -. DR CleanEx; HS_IL5; -. DR ExpressionAtlas; P05113; baseline and differential. DR Genevisible; P05113; HS. DR GO; GO:0005576; C:extracellular region; IDA:BHF-UCL. DR GO; GO:0005615; C:extracellular space; TAS:UniProtKB. DR GO; GO:0005622; C:intracellular; TAS:GOC. DR GO; GO:0005125; F:cytokine activity; IBA:GO_Central. DR GO; GO:0005137; F:interleukin-5 receptor binding; TAS:ProtInc. DR GO; GO:0000186; P:activation of MAPKK activity; TAS:Reactome. DR GO; GO:0007411; P:axon guidance; TAS:Reactome. DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central. DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:Reactome. DR GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome. DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; TAS:Reactome. DR GO; GO:0006954; P:inflammatory response; TAS:ProtInc. DR GO; GO:0045087; P:innate immune response; TAS:Reactome. DR GO; GO:0008286; P:insulin receptor signaling pathway; TAS:Reactome. DR GO; GO:0000165; P:MAPK cascade; TAS:Reactome. DR GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome. DR GO; GO:0030890; P:positive regulation of B cell proliferation; IBA:GO_Central. DR GO; GO:0045645; P:positive regulation of eosinophil differentiation; IEA:Ensembl. DR GO; GO:0051024; P:positive regulation of immunoglobulin secretion; IBA:GO_Central. DR GO; GO:0046427; P:positive regulation of JAK-STAT cascade; IEA:Ensembl. DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISS:UniProtKB. DR GO; GO:0071803; P:positive regulation of podosome assembly; IDA:BHF-UCL. DR GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IEA:Ensembl. DR GO; GO:0007265; P:Ras protein signal transduction; TAS:Reactome. DR GO; GO:0007264; P:small GTPase mediated signal transduction; TAS:Reactome. DR GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; TAS:Reactome. DR Gene3D; 1.20.1250.10; -; 1. DR InterPro; IPR009079; 4_helix_cytokine-like_core. DR InterPro; IPR012351; 4_helix_cytokine_core. DR InterPro; IPR000186; IL-5. DR PANTHER; PTHR10525; PTHR10525; 1. DR Pfam; PF02025; IL5; 1. DR PRINTS; PR00432; INTERLEUKIN5. DR ProDom; PD006721; Interleukin_5; 1. DR SUPFAM; SSF47266; SSF47266; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytokine; Direct protein sequencing; KW Disulfide bond; Glycoprotein; Growth factor; Reference proteome; KW Secreted; Signal. FT SIGNAL 1 19 {ECO:0000269|PubMed:2361960}. FT CHAIN 20 134 Interleukin-5. FT /FTId=PRO_0000015560. FT SITE 90 90 Not glycosylated. FT CARBOHYD 22 22 O-linked (GalNAc...). FT {ECO:0000269|PubMed:2361960}. FT CARBOHYD 47 47 N-linked (GlcNAc...). FT {ECO:0000305|PubMed:2361960}. FT DISULFID 63 63 Interchain (with C-105). FT {ECO:0000269|PubMed:2037074}. FT DISULFID 105 105 Interchain (with C-63). FT {ECO:0000269|PubMed:2037074}. FT CONFLICT 88 88 F -> L (in Ref. 5; CAA31210). FT {ECO:0000305}. FT HELIX 26 39 {ECO:0000244|PDB:1HUL}. FT HELIX 41 45 {ECO:0000244|PDB:1HUL}. FT STRAND 51 54 {ECO:0000244|PDB:1HUL}. FT STRAND 56 58 {ECO:0000244|PDB:1HUL}. FT HELIX 60 62 {ECO:0000244|PDB:1HUL}. FT HELIX 64 75 {ECO:0000244|PDB:1HUL}. FT HELIX 84 103 {ECO:0000244|PDB:1HUL}. FT STRAND 106 111 {ECO:0000244|PDB:1HUL}. FT HELIX 112 128 {ECO:0000244|PDB:1HUL}. SQ SEQUENCE 134 AA; 15238 MW; DC984467179556A3 CRC64; MRMLLHLSLL ALGAAYVYAI PTEIPTSALV KETLALLSTH RTLLIANETL RIPVPVHKNH QLCTEEIFQG IGTLESQTVQ GGTVERLFKN LSLIKKYIDG QKKKCGEERR RVNQFLDYLQ EFLGVMNTEW IIES //