Interleukin-5 precursor - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot P05113 (IL5_HUMAN)

Last modified January 19, 2010. Version 118. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Interleukin-5
      Short name=IL-5
Alternative name(s):
    T-cell replacing factor
      Short name=TRF
    Eosinophil differentiation factor
    B-cell differentiation factor I

Gene names

Name:

IL5

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	134 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Factor that induces terminal differentiation of late-developing B-cells to immunoglobulin secreting cells.
Subunit structure	Homodimer; disulfide-linked. Ref.8 Ref.9 Ref.10
Subcellular location	Secreted.
Sequence similarities	Belongs to the IL-5 family.

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Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Cytokine Growth factor
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	immune response Inferred from electronic annotation. Source: InterPro inflammatory response Ref.3 Traceable author statement. Source: ProtInc positive regulation of peptidyl-tyrosine phosphorylation Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	extracellular space Ref.1 Traceable author statement. Source: UniProtKB
Molecular function	cytokine activity Inferred from electronic annotation. Source: UniProtKB-KW growth factor activity Inferred from electronic annotation. Source: UniProtKB-KW interleukin-5 receptor binding Ref.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

Ref.8

Chain

20 – 134

115

Interleukin-5

PRO_0000015560

Sites

Site

Not glycosylated

Amino acid modifications

Glycosylation

O-linked (GalNAc...) Probable Ref.8

Glycosylation

N-linked (GlcNAc...) Probable

Disulfide bond

Interchain (with C-105) Ref.8 Ref.9 Ref.10

Disulfide bond

105

Interchain (with C-63) Ref.8 Ref.9 Ref.10

Experimental info

Sequence conflict

F → L in CAA31210. Ref.5

Secondary structure

134

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P05113-1 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: DC984467179556A3
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FASTA

134

15,238

        10         20         30         40         50         60 
MRMLLHLSLL ALGAAYVYAI PTEIPTSALV KETLALLSTH RTLLIANETL RIPVPVHKNH 

        70         80         90        100        110        120 
QLCTEEIFQG IGTLESQTVQ GGTVERLFKN LSLIKKYIDG QKKKCGEERR RVNQFLDYLQ 

       130 
EFLGVMNTEW IIES

« Hide

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of cDNA for human T-cell replacing factor (interleukin-5) and comparison with the murine homologue." 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. Nucleic Acids Res. 14:9149-9158(1986) [PubMed: 3024129] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Molecular cloning and structure of the human interleukin-5 gene." Tanabe T., Konishi M., Mizuta T., Noma T., Honjo T. J. Biol. Chem. 262:16580-16584(1987) [PubMed: 2824500] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Molecular cloning, nucleotide sequence, and expression of the gene encoding human eosinophil differentiation factor (interleukin 5)." Campbell H.D., Tucker W.Q.J., Hort Y., Martinson M.E., Mayo G., Clutterbuck E.J., Sanderson C.J., Young I.G. Proc. Natl. Acad. Sci. U.S.A. 84:6629-6633(1987) [PubMed: 3498940] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Isolation and characterization of lymphokine cDNA clones encoding mouse and human IgA-enhancing factor and eosinophil colony-stimulating factor activities: relationship to interleukin 5." 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. Proc. Natl. Acad. Sci. U.S.A. 84:7388-7392(1987) [PubMed: 2823259] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]	Honjo T., Takatsu K., Severinson E. Submitted (FEB-1992) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[6]	SeattleSNPs variation discovery resource Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[8]	"Structure of recombinant human interleukin 5 produced by Chinese hamster ovary cells." Minamitake Y., Kodama S., Katayama T., Adachi H., Tanaka S., Tsujimoto M. J. Biochem. 107:292-297(1990) [PubMed: 2361960] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-134, DISULFIDE BONDS, GLYCOSYLATION AT THR-22 AND ASN-47, LACK OF GLYCOSYLATION AT ASN-90.
[9]	"Human interleukin-5 expressed in Escherichia coli: assignment of the disulfide bridges of the purified unglycosylated protein." Proudfoot A.E.I., Davies J.G., Turcatti G., Wingfield P.T. FEBS Lett. 283:61-64(1991) [PubMed: 2037074] [Abstract] Cited for: DISULFIDE BONDS.
[10]	"A novel dimer configuration revealed by the crystal structure at 2.4-A resolution of human interleukin-5." Milburn M.V., Hassell A.M., Lambert M.H., Jordan S.R., Proudfoot A.E.I., Graber P., Wells T.N.C. Nature 363:172-176(1993) [PubMed: 8483502] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), DISULFIDE BONDS.
+	Additional computationally mapped references.

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Web resources

R&D Systems' cytokine mini-reviews: IL-5

Wikipedia

Interleukin-5 entry

SeattleSNPs

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X04688 mRNA. Translation: CAA28390.1.
J03478 Genomic DNA. Translation: AAA74469.1.
J02971 Genomic DNA. Translation: AAA98620.1.
X12705 mRNA. Translation: CAA31210.1.
X12706 Genomic DNA. Translation: CAA31211.1.
AF353265 Genomic DNA. Translation: AAK19759.1.
BC066282 mRNA. Translation: AAH66282.1.

IPI

IPI00007082.

PIR

A28477.

RefSeq

NP_000870.1.

UniGene

Hs.2247

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1HUL	X-ray	2.40	A/B	24-131	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-28N.

STRING

P05113.

Proteomic databases

PeptideAtlas

P05113.

PRIDE

P05113.

Genome annotation databases

Ensembl

ENST00000231454; ENSP00000231454; ENSG00000113525; Homo sapiens. [Genome view]

GeneID

3567.

KEGG

hsa:3567.

UCSC

uc003kxe.1. human.

Organism-specific databases

CTD

3567.

GeneCards

GC05M131905.

H-InvDB

HIX0032076.

HGNC

HGNC:6016. IL5.

HPA

CAB010304.

MIM

147850. gene.

PharmGKB

PA29833.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG20251.

HOGENOM

HBG125107.

HOVERGEN

P05113.

InParanoid

P05113.

OMA

EVFQGID.

OrthoDB

EOG9WHC60.

PhylomeDB

P05113.

Enzyme and pathway databases

Pathway_Interaction_DB

nfat_tfpathway. Calcineurin-regulated NFAT-dependent transcription in lymphocytes.
il4_2pathway. IL4-mediated signaling events.
smad2_3nuclearpathway. Regulation of nuclear SMAD2/3 signaling.

Gene expression databases

ArrayExpress

P05113.

Bgee

P05113.

CleanEx

HS_IL5.

Genevestigator

P05113.

GermOnline

ENSG00000113525. Homo sapiens.

Family and domain databases

InterPro

IPR009079. 4_helix_cytokine-like_core.
IPR000186. Interleukin_5.
[Graphical view]

PANTHER

PTHR10525. Interleukin_5. 1 hit.

Pfam

PF02025. IL5. 1 hit.
[Graphical view]

PRINTS

PR00432. INTERLEUKIN5.

ProDom

PD006721. Interleukin_5. 1 hit.
[Graphical view] [Entries sharing at least one domain]

ProtoNet

Search...

Other Resources

DrugBank

DB01411. Pranlukast.

NextBio

13932.

SOURCE

Search...

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Entry information

Entry name

IL5_HUMAN

Accession

Primary (citable) accession number: P05113
Secondary accession number(s): Q13840

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	August 13, 1987
Last modified:	January 19, 2010
This is version 118 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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Relevant documents

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) 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