Interleukin-1 beta precursor - Mus musculus (Mouse)

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P10749 (IL1B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 128. 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-1 beta
Short name=IL-1 beta

Gene names

Name:

Il1b

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	269 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	Produced by activated macrophages, IL-1 stimulates thymocyte proliferation by inducing IL-2 release, B-cell maturation and proliferation, and fibroblast growth factor activity. IL-1 proteins are involved in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the release of prostaglandin and collagenase from synovial cells.
Subunit structure	Monomer.
Subcellular location	Secreted. Note: The lack of a specific hydrophobic segment in the precursor sequence suggests that IL-1 is released by damaged cells or is secreted by a mechanism differing from that used for other secretory proteins.
Domain	The similarity among the IL-1 precursors suggests that the amino ends of these proteins serve some as yet undefined function.
Sequence similarities	Belongs to the IL-1 family.

Ontologies

Keywords
Biological process	Inflammatory response
Cellular component	Secreted
Molecular function	Cytokine Mitogen Pyrogen
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	MAPK cascade Inferred from electronic annotation. Source: Compara activation of MAPK activity Inferred from electronic annotation. Source: Compara cellular response to drug Inferred from sequence orthology PubMed 19158679. Source: MGI cellular response to mechanical stimulus Inferred from electronic annotation. Source: Compara cellular response to organic cyclic compound Inferred from electronic annotation. Source: Compara cellular response to organic substance Inferred from sequence orthology PubMed 19158679. Source: MGI fever generation Inferred from electronic annotation. Source: UniProtKB-KW hyaluronan biosynthetic process Inferred from electronic annotation. Source: Compara immune response Inferred from electronic annotation. Source: InterPro interleukin-1 beta production Inferred from genetic interaction PubMed 19158679. Source: MGI lipopolysaccharide-mediated signaling pathway Inferred from electronic annotation. Source: Compara monocyte aggregation Inferred from electronic annotation. Source: Compara negative regulation of MAP kinase activity Inferred from direct assay PubMed 16865359. Source: BHF-UCL negative regulation of adiponectin secretion Inferred from direct assay PubMed 16865359. Source: BHF-UCL negative regulation of apoptotic process Inferred from electronic annotation. Source: Compara negative regulation of cell proliferation Inferred from electronic annotation. Source: Compara negative regulation of glucose transport Inferred from direct assay PubMed 16865359. Source: BHF-UCL negative regulation of insulin receptor signaling pathway Inferred from direct assay PubMed 16865359. Source: BHF-UCL negative regulation of lipid catabolic process Inferred from electronic annotation. Source: Compara negative regulation of lipid metabolic process Inferred from direct assay PubMed 16865359. Source: BHF-UCL neutrophil chemotaxis Inferred from direct assay PubMed 12925700. Source: MGI positive regulation of I-kappaB kinase/NF-kappaB cascade Inferred from direct assay PubMed 16260493. Source: MGI positive regulation of JNK cascade Inferred from direct assay PubMed 16260493. Source: MGI positive regulation of NF-kappaB import into nucleus Inferred from electronic annotation. Source: Compara positive regulation of NF-kappaB transcription factor activity Inferred from electronic annotation. Source: Compara positive regulation of T cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of angiogenesis Inferred from mutant phenotype PubMed 12598651. Source: BHF-UCL positive regulation of calcidiol 1-monooxygenase activity Inferred from electronic annotation. Source: Compara positive regulation of cell division Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of chemokine biosynthetic process Inferred from direct assay PubMed 12925700. Source: MGI positive regulation of fever generation Inferred from direct assay PubMed 19940926. Source: BHF-UCL positive regulation of granulocyte macrophage colony-stimulating factor production Inferred from electronic annotation. Source: Compara positive regulation of heterotypic cell-cell adhesion Inferred from electronic annotation. Source: Compara positive regulation of interferon-gamma production Inferred from electronic annotation. Source: Compara positive regulation of interleukin-2 biosynthetic process Inferred from electronic annotation. Source: Compara positive regulation of interleukin-6 biosynthetic process Inferred from direct assay PubMed 12925700. Source: MGI positive regulation of interleukin-6 production Inferred from direct assay PubMed 15292196 PubMed 19734906. Source: MGI positive regulation of interleukin-8 production Inferred from electronic annotation. Source: Compara positive regulation of lipid catabolic process Inferred from direct assay PubMed 16865359. Source: BHF-UCL positive regulation of membrane protein ectodomain proteolysis Inferred from electronic annotation. Source: Compara positive regulation of mitosis Inferred from electronic annotation. Source: Compara positive regulation of monocyte chemotactic protein-1 production Inferred from electronic annotation. Source: Compara positive regulation of myosin light chain kinase activity Inferred from electronic annotation. Source: Compara positive regulation of nitric oxide biosynthetic process Inferred from electronic annotation. Source: Compara positive regulation of prostaglandin secretion Inferred from direct assay PubMed 19940926. Source: BHF-UCL positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay PubMed 19734906. Source: MGI positive regulation vascular endothelial growth factor production Inferred from mutant phenotype PubMed 12598651. Source: BHF-UCL protein kinase B signaling cascade Inferred from electronic annotation. Source: Compara regulation of insulin secretion Inferred from electronic annotation. Source: Compara response to ATP Inferred from direct assay PubMed 15905573 PubMed 16301672 PubMed 18490713. Source: MGI response to lipopolysaccharide Inferred from direct assay PubMed 16423834 PubMed 18490713. Source: MGI sequestering of triglyceride Inferred from electronic annotation. Source: Compara
Cellular_component	extracellular space Inferred from direct assay PubMed 11016935 PubMed 11168643 PubMed 15905573 PubMed 16423834. Source: MGI secretory granule Inferred from direct assay PubMed 16423834. Source: MGI
Molecular_function	cytokine activity Inferred from direct assay PubMed 12925700 PubMed 15292196. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Propeptide

1 – 117

117

PRO_0000015311

Chain

118 – 269

152

Interleukin-1 beta

PRO_0000015312

Secondary structure

269

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P10749 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 734FA17B02ED87EE
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FASTA

269

30,931

        10         20         30         40         50         60 
MATVPELNCE MPPFDSDEND LFFEVDGPQK MKGCFQTFDL GCPDESIQLQ ISQQHINKSF 

        70         80         90        100        110        120 
RQAVSLIVAV EKLWQLPVSF PWTFQDEDMS TFFSFIFEEE PILCDSWDDD DNLLVCDVPI 

       130        140        150        160        170        180 
RQLHYRLRDE QQKSLVLSDP YELKALHLNG QNINQQVIFS MSFVQGEPSN DKIPVALGLK 

       190        200        210        220        230        240 
GKNLYLSCVM KDGTPTLQLE SVDPKQYPKK KMEKRFVFNK IEVKSKVEFE SAEFPNWYIS 

       250        260 
TSQAEHKPVF LGNNSGQDII DFTMESVSS

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Two interleukin 1 genes in the mouse: cloning and expression of the cDNA for murine interleukin 1 beta." Gray P.W., Glaister D., Chen E., Goeddel D.V., Pennica D. J. Immunol. 137:3644-3648(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The murine interleukin 1 beta gene: structure and evolution." Telford J.L., Macchia G., Massone A., Carinci V., Palla E., Melli M. Nucleic Acids Res. 14:9955-9963(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"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: Czech II. Tissue: Mammary gland.
[4]	"Characterization of murine IL-1 beta. Isolation, expression, and purification." Huang J.J., Newton R.C., Rutledge S.J., Horuk R., Matthew J.B., Covington M., Lin Y. J. Immunol. 140:3838-3843(1988) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 118-139.
[5]	"The structure of murine interleukin-1 beta at 2.8-A resolution." van Oostrum J., Priestle J.P., Gruetter M.G., Schmitz A. J. Struct. Biol. 107:189-195(1991) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M15131 mRNA. Translation: AAA39276.1.
X04964 Genomic DNA. Translation: CAA28637.1.
BC011437 mRNA. Translation: AAH11437.1.

IPI

IPI00114067.

PIR

I55969.

RefSeq

NP_032387.1. NM_008361.3.

UniGene

Mm.222830.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2MIB	X-ray	2.84	A	118-269	[»]
8I1B	X-ray	2.40	A	118-269	[»]

ProteinModelPortal

P10749.

SMR

P10749. Positions 122-267.

ModBase

Search...

Protein-protein interaction databases

IntAct

P10749. 1 interaction.

STRING

10090.ENSMUSP00000028881.

Proteomic databases

PRIDE

P10749.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000028881; ENSMUSP00000028881; ENSMUSG00000027398.

GeneID

16176.

KEGG

mmu:16176.

Organism-specific databases

CTD

3553.

MGI

MGI:96543. Il1b.

Phylogenomic databases

eggNOG

NOG40099.

HOGENOM

HOG000246399.

HOVERGEN

HBG007328.

InParanoid

P10749.

K04519.

OMA

SNDKIPV.

OrthoDB

EOG4N30Q1.

Gene expression databases

ArrayExpress

P10749.

Bgee

P10749.

CleanEx

MM_IL1B.

Genevestigator

P10749.

GermOnline

ENSMUSG00000027398. Mus musculus.

Family and domain databases

InterPro

IPR008996. Cytokine_IL1-like.
IPR002348. IL1_HBGF.
IPR003502. IL1_propep.
IPR020877. Interleukin-1_CS.
IPR000975. Interleukin_1.
IPR003294. InterleukinIL1AB.
IPR003296. InterleukinIL1B.
[Graphical view]

Pfam

PF00340. IL1. 1 hit.
PF02394. IL1_propep. 1 hit.
[Graphical view]

PRINTS

PR00262. IL1HBGF.
PR00264. INTERLEUKIN1.
PR01359. INTRLEUKIN1B.
PR01357. INTRLEUKN1AB.

SMART

SM00125. IL1. 1 hit.
[Graphical view]

SUPFAM

SSF50353. Cytok_IL1_like. 1 hit.

PROSITE

PS00253. INTERLEUKIN_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P10749.

NextBio

289037.

PMAP-CutDB

P10749.

SOURCE

Search...

Entry information

Entry name

IL1B_MOUSE

Accession

Primary (citable) accession number: P10749

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 1, 1989
Last modified:	April 3, 2013
This is version 128 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

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction 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