Interleukin-15 precursor - Mus musculus (Mouse)

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P48346 (IL15_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 91. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Interleukin-15
Short name=IL-15

Gene names

Name:

Il15

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	162 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Cytokine that stimulates the proliferation of T-lymphocytes. Stimulation by IL-15 requires interaction of IL-15 with components of IL-2R, including IL-2R beta and probably IL-2R gamma but not IL-2R alpha.
Subcellular location	Secreted.
Sequence similarities	Belongs to the IL-15/IL-21 family.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Cytokine
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	NK T cell proliferation Inferred from mutant phenotype PubMed 10704459. Source: MGI aging Inferred from electronic annotation. Source: Compara cell maturation Inferred from genetic interaction PubMed 17318811. Source: MGI cellular response to vitamin D Inferred from electronic annotation. Source: Compara extrathymic T cell selection Inferred from mutant phenotype PubMed 10704459. Source: MGI hyaluronan metabolic process Inferred from electronic annotation. Source: Compara immune response Inferred from electronic annotation. Source: InterPro inflammatory response Inferred from electronic annotation. Source: Compara lymph node development Inferred from mutant phenotype PubMed 10704459. Source: MGI natural killer cell differentiation Inferred from genetic interaction PubMed 17318811. Source: MGI negative regulation of smooth muscle cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of T cell proliferation Inferred from mutant phenotype PubMed 10704459. Source: MGI positive regulation of immune response Inferred from mutant phenotype PubMed 10704459. Source: MGI positive regulation of interleukin-17 production Inferred from electronic annotation. Source: Compara positive regulation of natural killer cell differentiation Inferred from direct assay PubMed 14607906. Source: MGI positive regulation of natural killer cell proliferation Inferred from direct assay PubMed 14607906. Source: MGI positive regulation of tyrosine phosphorylation of Stat3 protein Inferred from electronic annotation. Source: Compara regulation of T cell differentiation Inferred from mutant phenotype PubMed 10704459. Source: MGI regulation of defense response to virus by host Inferred from mutant phenotype PubMed 10704459. Source: MGI skeletal muscle atrophy Inferred from electronic annotation. Source: Compara
Cellular_component	cytoplasm Inferred from direct assay PubMed 11737071. Source: MGI extracellular space Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	cytokine activity Inferred from direct assay PubMed 14607906. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 29

Potential

Propeptide

30 – 48

Potential

PRO_0000015399

Chain

49 – 162

114

Interleukin-15

PRO_0000015400

Amino acid modifications

Glycosylation

104

N-linked (GlcNAc...) Potential

Glycosylation

108

N-linked (GlcNAc...) Potential

Glycosylation

119

N-linked (GlcNAc...) Potential

Disulfide bond

Disulfide bond

Secondary structure

162

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P48346 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 68C971498CEBF296
Show »

FASTA

162

18,593

        10         20         30         40         50         60 
MKILKPYMRN TSISCYLCFL LNSHFLTEAG IHVFILGCVS VGLPKTEANW IDVRYDLEKI 

        70         80         90        100        110        120 
ESLIQSIHID TTLYTDSDFH PSCKVTAMNC FLLELQVILH EYSNMTLNET VRNVLYLANS 

       130        140        150        160 
TLSSNKNVAE SGCKECEELE EKTFTEFLQS FIRIVQMFIN TS

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Chromosomal assignment and genomic structure of IL15." Anderson D.M., Johnson L., Glaccum M.B., Copeland N.G., Gilbert D.J., Jenkins N.A., Valentine V., Kirstein M.N., Shapiro D.N., Morris S.W., Grabstein K., Cosman D. Genomics 25:701-706(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: WC/REJ X C57BL/6J. Tissue: Bone marrow.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Mammary gland.
[3]	"Crystal Structure of the interleukin-15.interleukin-15 receptor alpha complex: insights into trans and cis presentation." Olsen S.K., Ota N., Kishishita S., Kukimoto-Niino M., Murayama K., Uchiyama H., Toyama M., Terada T., Shirouzu M., Kanagawa O., Yokoyama S. J. Biol. Chem. 282:37191-37204(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS) OF 42-162 IN COMPLEX WITH IL15RA, DISULFIDE BONDS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U14332 mRNA. Translation: AAA75377.1.
BC023698 mRNA. Translation: AAH23698.1.

IPI

IPI00111090.

PIR

I49124.

RefSeq

NP_001241676.1. NM_001254747.1.
NP_032383.1. NM_008357.2.

UniGene

Mm.4392.
Mm.490053.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2PSM	X-ray	2.19	A/B	49-162	[»]

ProteinModelPortal

P48346.

SMR

P48346. Positions 46-162.

ModBase

Search...

PTM databases

PhosphoSite

P48346.

Proteomic databases

PRIDE

P48346.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000034148; ENSMUSP00000034148; ENSMUSG00000031712.

GeneID

16168.

KEGG

mmu:16168.

Organism-specific databases

CTD

3600.

MGI

MGI:103014. Il15.

Phylogenomic databases

eggNOG

NOG44071.

HOGENOM

HOG000113029.

HOVERGEN

HBG006142.

InParanoid

P48346.

K05433.

OMA

RSTSIQC.

OrthoDB

EOG40CHJ8.

Gene expression databases

ArrayExpress

P48346.

Bgee

P48346.

CleanEx

MM_IL15.

Genevestigator

P48346.

GermOnline

ENSMUSG00000031712. Mus musculus.

Family and domain databases

InterPro

IPR020439. Interleukin-15.
IPR020466. Interleukin-15_mammal.
IPR003443. Interleukin_15-like.
[Graphical view]

Pfam

PF02372. IL15. 1 hit.
[Graphical view]

PRINTS

PR01947. INTLKN15MAML.
PR01930. INTRLEUKIN15.

ProtoNet

Search...

Other

EvolutionaryTrace

P48346.

NextBio

289003.

SOURCE

Search...

Entry information

Entry name

IL15_MOUSE

Accession

Primary (citable) accession number: P48346

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	April 3, 2013
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents