ID IL15_HUMAN Reviewed; 162 AA. AC P40933; D3DNZ2; O00440; O43512; Q495Z8; Q6FGX7; Q93058; Q9UBA3; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 27-MAR-2024, entry version 197. DE RecName: Full=Interleukin-15; DE Short=IL-15; DE Flags: Precursor; GN Name=IL15; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM IL15-S48AA), AND FUNCTION. RC TISSUE=Bone marrow; RX PubMed=8178155; DOI=10.1126/science.8178155; RA Grabstein K.H., Eisenman J., Shanebeck K., Rauch C., Srinivasan S., RA Fung V., Beers C., Richardson J., Schoenborn M.A., Ahdieh M., Johnson L., RA Alderson M.R., Watson J.D., Anderson D.M., Giri J.G.; RT "Cloning of a T cell growth factor that interacts with the beta chain of RT the interleukin-2 receptor."; RL Science 264:965-968(1994). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8932977; DOI=10.1006/cyto.1996.0089; RA Krause H., Jandrig B., Wernicke C., Bulfone-Paus S., Pohl T., RA Diamantstein T.; RT "Genomic sequence and chromosomal location of the human interleukin-15 gene RT (IL15)."; RL Cytokine 8:667-674(1996). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM IL15-S21AA). RC TISSUE=Lung cancer; RX PubMed=8668345; RA Meazza R., Verdiani S., Biassoni R., Coppolecchia M., Gaggero A., RA Orengo A.M., Colombo M.P., Azzarone B., Ferrini S.; RT "Identification of a novel interleukin-15 (IL-15) transcript isoform RT generated by alternative splicing in human small cell lung cancer cell RT lines."; RL Oncogene 12:2187-2192(1996). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM IL15-S21AA). RC TISSUE=Testis; RX PubMed=9405632; DOI=10.1073/pnas.94.26.14444; RA Tagaya Y., Kurys G., Thies T.A., Losi J.M., Azimi N., Hanover J.A., RA Bamford R.N., Waldmann T.A.; RT "Generation of secretable and nonsecretable interleukin 15 isoforms through RT alternate usage of signal peptides."; RL Proc. Natl. Acad. Sci. U.S.A. 94:14444-14449(1997). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Meazza R., Ferrini S.; RT "Expression of two IL-15 mRNA isoforms in human tumors does not correlate RT with secretion: role of different signal peptides."; RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM IL15-S21AA). RA Li C.; RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM IL15-S21AA). RC TISSUE=Cerebellum, and Heart; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM IL15-S21AA). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS IL15-S48AA AND RP IL15-S21AA). RC TISSUE=Colon; 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 project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [11] RP NUCLEOTIDE SEQUENCE [MRNA] OF 49-162. RC TISSUE=Epidermis; RA Sorel M.A., Jacques Y.; RT "IL15 expression in human keratinocytes."; RL Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases. RN [12] RP FUNCTION. RX PubMed=8026467; DOI=10.1002/j.1460-2075.1994.tb06576.x; RA Giri J.G., Ahdieh M., Eisenman J., Shanebeck K., Grabstein K., Kumaki S., RA Namen A., Park L.S., Cosman D., Anderson D.; RT "Utilization of the beta and gamma chains of the IL-2 receptor by the novel RT cytokine IL-15."; RL EMBO J. 13:2822-2830(1994). RN [13] RP FUNCTION. RX PubMed=7568001; DOI=10.1073/pnas.92.19.8705; RA Johnston J.A., Bacon C.M., Finbloom D.S., Rees R.C., Kaplan D., Shibuya K., RA Ortaldo J.R., Gupta S., Chen Y.Q., Giri J.D.; RT "Tyrosine phosphorylation and activation of STAT5, STAT3, and Janus kinases RT by interleukins 2 and 15."; RL Proc. Natl. Acad. Sci. U.S.A. 92:8705-8709(1995). RN [14] RP FUNCTION. RX PubMed=9326248; RA Badolato R., Ponzi A.N., Millesimo M., Notarangelo L.D., Musso T.; RT "Interleukin-15 (IL-15) induces IL-8 and monocyte chemotactic protein 1 RT production in human monocytes."; RL Blood 90:2804-2809(1997). RN [15] RP FUNCTION, AND INDUCTION BY INTERFERON-GAMMA. RX PubMed=10233906; RA Musso T., Calosso L., Zucca M., Millesimo M., Ravarino D., Giovarelli M., RA Malavasi F., Ponzi A.N., Paus R., Bulfone-Paus S.; RT "Human monocytes constitutively express membrane-bound, biologically RT active, and interferon-gamma-upregulated interleukin-15."; RL Blood 93:3531-3539(1999). RN [16] RP FUNCTION. RX PubMed=15123770; DOI=10.1189/jlb.0605298; RA Ratthe C., Girard D.; RT "Interleukin-15 enhances human neutrophil phagocytosis by a Syk-dependent RT mechanism: importance of the IL-15Ralpha chain."; RL J. Leukoc. Biol. 76:162-168(2004). RN [17] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 49-162 IN COMPLEX WITH ANTIBODY, RP AND DISULFIDE BONDS. RX PubMed=21167836; DOI=10.1016/j.jmb.2010.12.017; RA Lowe D.C., Gerhardt S., Ward A., Hargreaves D., Anderson M., Ferraro F., RA Pauptit R.A., Pattison D.V., Buchanan C., Popovic B., Finch D.K., RA Wilkinson T., Sleeman M., Vaughan T.J., Mallinder P.R.; RT "Engineering a high-affinity anti-IL-15 antibody: crystal structure reveals RT an alpha-helix in VH CDR3 as key component of paratope."; RL J. Mol. Biol. 406:160-175(2011). RN [18] {ECO:0007744|PDB:4GS7} RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 49-162, DISULFIDE BONDS, AND RP FUNCTION. RX PubMed=23104097; DOI=10.1038/ni.2449; RA Ring A.M., Lin J.X., Feng D., Mitra S., Rickert M., Bowman G.R., RA Pande V.S., Li P., Moraga I., Spolski R., Ozkan E., Leonard W.J., RA Garcia K.C.; RT "Mechanistic and structural insight into the functional dichotomy between RT IL-2 and IL-15."; RL J. Immunol. 13:1187-1195(2012). CC -!- FUNCTION: Cytokine that plays a major role in the development of CC inflammatory and protective immune responses to microbial invaders and CC parasites by modulating immune cells of both the innate and adaptive CC immune systems (PubMed:15123770). Stimulates the proliferation of CC natural killer cells, T-cells and B-cells and promotes the secretion of CC several cytokines (PubMed:8178155, PubMed:9326248). In monocytes, CC induces the production of IL8 and monocyte chemotactic protein 1/CCL2, CC two chemokines that attract neutrophils and monocytes respectively to CC sites of infection (PubMed:9326248). Unlike most cytokines, which are CC secreted in soluble form, IL15 is expressed in association with its CC high affinity IL15RA on the surface of IL15-producing cells and CC delivers signals to target cells that express IL2RB and IL2RG receptor CC subunits (PubMed:8026467, PubMed:23104097, PubMed:10233906). Binding to CC its receptor triggers the phosphorylation of JAK1 and JAK3 and the CC recruitment and subsequent phosphorylation of signal transducer and CC activator of transcription-3/STAT3 and STAT5 (PubMed:7568001). In mast CC cells, induces the rapid tyrosine phosphorylation of STAT6 and thereby CC controls mast cell survival and release of cytokines such as IL4 (By CC similarity). {ECO:0000250|UniProtKB:P48346, CC ECO:0000269|PubMed:10233906, ECO:0000269|PubMed:15123770, CC ECO:0000269|PubMed:23104097, ECO:0000269|PubMed:7568001, CC ECO:0000269|PubMed:8026467, ECO:0000269|PubMed:8178155, CC ECO:0000269|PubMed:9326248}. CC -!- INTERACTION: CC P40933; Q13261: IL15RA; NbExp=5; IntAct=EBI-980274, EBI-980354; CC P40933; P14784: IL2RB; NbExp=3; IntAct=EBI-980274, EBI-2866779; CC -!- SUBCELLULAR LOCATION: [Isoform IL15-S48AA]: Secreted. CC -!- SUBCELLULAR LOCATION: [Isoform IL15-S21AA]: Cytoplasm. Nucleus. CC Note=IL15-S21AA is not secreted, but rather is stored intracellularly, CC appearing in the nucleus and cytoplasmic components. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=IL15-S48AA; CC IsoId=P40933-1; Sequence=Displayed; CC Name=IL15-S21AA; CC IsoId=P40933-2; Sequence=VSP_002660; CC -!- TISSUE SPECIFICITY: Most abundant in placenta and skeletal muscle. It CC is also detected in the heart, lung, liver and kidney. IL15-S21AA is CC preferentially expressed in tissues such as testis and thymus. CC -!- INDUCTION: By interferon-gamma. {ECO:0000269|PubMed:10233906}. CC -!- SIMILARITY: Belongs to the IL-15/IL-21 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAA71044.1; Type=Miscellaneous discrepancy; Note=Man-made cDNA with a signal peptide sequence to increase protein secretion (substitution with a signal peptide derived from the mouse IgV kappa chain).; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Wikipedia; Note=Interleukin-15 entry; CC URL="https://en.wikipedia.org/wiki/Interleukin_15"; 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; U14407; AAA21551.1; -; mRNA. DR EMBL; X91233; CAA62616.1; -; Genomic_DNA. DR EMBL; X94223; CAA63914.1; -; mRNA. DR EMBL; X94222; CAA63913.1; -; mRNA. DR EMBL; AF031167; AAB97518.1; -; mRNA. DR EMBL; Y09908; CAA71044.1; ALT_SEQ; mRNA. DR EMBL; AY720442; AAU21241.1; -; mRNA. DR EMBL; AK122993; BAG53839.1; -; mRNA. DR EMBL; AK290619; BAF83308.1; -; mRNA. DR EMBL; CR541980; CAG46777.1; -; mRNA. DR EMBL; CR542007; CAG46804.1; -; mRNA. DR EMBL; CH471056; EAX05083.1; -; Genomic_DNA. DR EMBL; CH471056; EAX05084.1; -; Genomic_DNA. DR EMBL; CH471056; EAX05085.1; -; Genomic_DNA. DR EMBL; CH471056; EAX05086.1; -; Genomic_DNA. DR EMBL; CH471056; EAX05087.1; -; Genomic_DNA. DR EMBL; BC018149; AAH18149.1; -; mRNA. DR EMBL; BC100961; AAI00962.1; -; mRNA. DR EMBL; BC100962; AAI00963.1; -; mRNA. DR EMBL; BC100963; AAI00964.1; -; mRNA. DR EMBL; Z38000; CAA86100.1; -; mRNA. DR CCDS; CCDS3755.1; -. [P40933-1] DR CCDS; CCDS3756.1; -. [P40933-2] DR RefSeq; NP_000576.1; NM_000585.4. [P40933-1] DR RefSeq; NP_751915.1; NM_172175.2. [P40933-2] DR PDB; 2XQB; X-ray; 2.60 A; A=49-162. DR PDB; 2Z3Q; X-ray; 1.85 A; A/C=49-162. DR PDB; 2Z3R; X-ray; 2.00 A; A/C/E/G/I/K/M/O=49-162. DR PDB; 4GS7; X-ray; 2.35 A; A=49-162. DR PDBsum; 2XQB; -. DR PDBsum; 2Z3Q; -. DR PDBsum; 2Z3R; -. DR PDBsum; 4GS7; -. DR AlphaFoldDB; P40933; -. DR SMR; P40933; -. DR BioGRID; 109813; 10. DR CORUM; P40933; -. DR DIP; DIP-3046N; -. DR IntAct; P40933; 5. DR STRING; 9606.ENSP00000296545; -. DR BindingDB; P40933; -. DR ChEMBL; CHEMBL3712954; -. DR DrugBank; DB01327; Cefazolin. DR GlyCosmos; P40933; 1 site, No reported glycans. DR GlyGen; P40933; 1 site. DR iPTMnet; P40933; -. DR PhosphoSitePlus; P40933; -. DR BioMuta; IL15; -. DR PaxDb; 9606-ENSP00000296545; -. DR ProteomicsDB; 55387; -. [P40933-1] DR ProteomicsDB; 55388; -. [P40933-2] DR ABCD; P40933; 1 sequenced antibody. DR Antibodypedia; 3844; 1235 antibodies from 43 providers. DR DNASU; 3600; -. DR Ensembl; ENST00000296545.11; ENSP00000296545.7; ENSG00000164136.17. [P40933-1] DR Ensembl; ENST00000320650.9; ENSP00000323505.4; ENSG00000164136.17. [P40933-1] DR Ensembl; ENST00000394159.2; ENSP00000377714.1; ENSG00000164136.17. [P40933-2] DR Ensembl; ENST00000477265.5; ENSP00000436914.1; ENSG00000164136.17. [P40933-2] DR Ensembl; ENST00000514653.5; ENSP00000422271.1; ENSG00000164136.17. [P40933-2] DR Ensembl; ENST00000529613.5; ENSP00000435462.1; ENSG00000164136.17. [P40933-1] DR GeneID; 3600; -. DR KEGG; hsa:3600; -. DR MANE-Select; ENST00000320650.9; ENSP00000323505.4; NM_000585.5; NP_000576.1. DR UCSC; uc003iis.4; human. [P40933-1] DR AGR; HGNC:5977; -. DR CTD; 3600; -. DR DisGeNET; 3600; -. DR GeneCards; IL15; -. DR HGNC; HGNC:5977; IL15. DR HPA; ENSG00000164136; Low tissue specificity. DR MIM; 600554; gene. DR neXtProt; NX_P40933; -. DR OpenTargets; ENSG00000164136; -. DR PharmGKB; PA29790; -. DR VEuPathDB; HostDB:ENSG00000164136; -. DR eggNOG; ENOG502SCMF; Eukaryota. DR GeneTree; ENSGT00390000016264; -. DR HOGENOM; CLU_135111_0_0_1; -. DR InParanoid; P40933; -. DR OMA; FVWGCIS; -. DR OrthoDB; 5354716at2759; -. DR PhylomeDB; P40933; -. DR TreeFam; TF336199; -. DR PathwayCommons; P40933; -. DR Reactome; R-HSA-8983432; Interleukin-15 signaling. DR SignaLink; P40933; -. DR SIGNOR; P40933; -. DR BioGRID-ORCS; 3600; 6 hits in 1115 CRISPR screens. DR ChiTaRS; IL15; human. DR EvolutionaryTrace; P40933; -. DR GeneWiki; Interleukin_15; -. DR GenomeRNAi; 3600; -. DR Pharos; P40933; Tchem. DR PRO; PR:P40933; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; P40933; Protein. DR Bgee; ENSG00000164136; Expressed in decidua and 152 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005768; C:endosome; TAS:Reactome. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IDA:UniProt. DR GO; GO:0005794; C:Golgi apparatus; TAS:ProtInc. DR GO; GO:0016607; C:nuclear speck; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005125; F:cytokine activity; IDA:UniProt. DR GO; GO:0005126; F:cytokine receptor binding; IEA:InterPro. DR GO; GO:0048469; P:cell maturation; IEA:Ensembl. DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc. DR GO; GO:0045062; P:extrathymic T cell selection; IEA:Ensembl. DR GO; GO:0006955; P:immune response; TAS:ProtInc. DR GO; GO:0035723; P:interleukin-15-mediated signaling pathway; IDA:UniProtKB. DR GO; GO:0048535; P:lymph node development; IEA:Ensembl. DR GO; GO:0030225; P:macrophage differentiation; IDA:ARUK-UCL. DR GO; GO:0001779; P:natural killer cell differentiation; IEA:Ensembl. DR GO; GO:0001787; P:natural killer cell proliferation; IEA:Ensembl. DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; ISS:YuBioLab. DR GO; GO:0042119; P:neutrophil activation; IDA:UniProtKB. DR GO; GO:0001866; P:NK T cell proliferation; IEA:Ensembl. DR GO; GO:0008284; P:positive regulation of cell population proliferation; TAS:ProtInc. DR GO; GO:0001819; P:positive regulation of cytokine production; IBA:GO_Central. DR GO; GO:0050778; P:positive regulation of immune response; IBA:GO_Central. DR GO; GO:0050729; P:positive regulation of inflammatory response; IC:BHF-UCL. DR GO; GO:0032740; P:positive regulation of interleukin-17 production; IDA:BHF-UCL. DR GO; GO:0032825; P:positive regulation of natural killer cell differentiation; IEA:Ensembl. DR GO; GO:0032819; P:positive regulation of natural killer cell proliferation; IEA:Ensembl. DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:UniProtKB. DR GO; GO:0050766; P:positive regulation of phagocytosis; IDA:UniProtKB. DR GO; GO:1904100; P:positive regulation of protein O-linked glycosylation; IEA:Ensembl. DR GO; GO:0042102; P:positive regulation of T cell proliferation; IBA:GO_Central. DR GO; GO:0034105; P:positive regulation of tissue remodeling; IC:BHF-UCL. DR GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IBA:GO_Central. DR GO; GO:0050691; P:regulation of defense response to virus by host; IEA:Ensembl. DR GO; GO:0045580; P:regulation of T cell differentiation; IEA:Ensembl. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR GO; GO:0007260; P:tyrosine phosphorylation of STAT protein; IDA:CACAO. DR Gene3D; 1.20.1250.70; Interleukin-15/Interleukin-21; 1. DR InterPro; IPR009079; 4_helix_cytokine-like_core. DR InterPro; IPR020439; IL-15. DR InterPro; IPR003443; IL-15/IL-21_fam. DR InterPro; IPR020466; IL-15_mml. DR PANTHER; PTHR14356:SF3; INTERLEUKIN-15; 1. DR PANTHER; PTHR14356; INTERLEUKIN-15-RELATED; 1. DR Pfam; PF02372; IL15; 1. DR PRINTS; PR01947; INTLKN15MAML. DR PRINTS; PR01930; INTRLEUKIN15. DR SUPFAM; SSF47266; 4-helical cytokines; 1. DR Genevisible; P40933; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cytokine; Cytoplasm; Disulfide bond; KW Glycoprotein; Nucleus; Reference proteome; Secreted; Signal. FT SIGNAL 1..29 FT /evidence="ECO:0000255" FT PROPEP 30..48 FT /evidence="ECO:0000255" FT /id="PRO_0000015393" FT CHAIN 49..162 FT /note="Interleukin-15" FT /id="PRO_0000015394" FT CARBOHYD 127 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 83..133 FT /evidence="ECO:0000269|PubMed:21167836, FT ECO:0000269|PubMed:23104097" FT DISULFID 90..136 FT /evidence="ECO:0000269|PubMed:21167836, FT ECO:0000269|PubMed:23104097" FT VAR_SEQ 1..37 FT /note="MRISKPHLRSISIQCYLCLLLNSHFLTEAGIHVFILG -> MVLGTIDLCS FT (in isoform IL15-S21AA)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:8668345, FT ECO:0000303|PubMed:9405632, ECO:0000303|Ref.6, FT ECO:0000303|Ref.8" FT /id="VSP_002660" FT CONFLICT 141 FT /note="E -> K (in Ref. 4; AAB97518)" FT /evidence="ECO:0000305" FT HELIX 49..64 FT /evidence="ECO:0007829|PDB:2Z3Q" FT STRAND 73..75 FT /evidence="ECO:0007829|PDB:2Z3Q" FT HELIX 81..83 FT /evidence="ECO:0007829|PDB:2Z3Q" FT HELIX 84..102 FT /evidence="ECO:0007829|PDB:2Z3Q" FT HELIX 105..119 FT /evidence="ECO:0007829|PDB:2Z3Q" FT HELIX 136..138 FT /evidence="ECO:0007829|PDB:2Z3Q" FT STRAND 139..142 FT /evidence="ECO:0007829|PDB:2Z3Q" FT HELIX 144..158 FT /evidence="ECO:0007829|PDB:2Z3Q" SQ SEQUENCE 162 AA; 18086 MW; 0CE0520C1D8379E2 CRC64; MRISKPHLRS ISIQCYLCLL LNSHFLTEAG IHVFILGCFS AGLPKTEANW VNVISDLKKI EDLIQSMHID ATLYTESDVH PSCKVTAMKC FLLELQVISL ESGDASIHDT VENLIILANN SLSSNGNVTE SGCKECEELE EKNIKEFLQS FVHIVQMFIN TS //