P05113 (IL5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Interleukin-5
Short name=IL-5

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

Gene names

Name:

IL5

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

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

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.

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 Reference proteome
Gene Ontology (GO)
Biological_process	cytokine-mediated signaling pathway Inferred from electronic annotation. Source: Compara immune response Inferred from electronic annotation. Source: InterPro inflammatory response Traceable author statement Ref.3. Source: ProtInc positive regulation of B cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of JAK-STAT cascade Inferred from electronic annotation. Source: Compara positive regulation of eosinophil differentiation Inferred from electronic annotation. Source: Compara positive regulation of immunoglobulin secretion Inferred from electronic annotation. Source: Compara positive regulation of peptidyl-tyrosine phosphorylation Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of podosome assembly Inferred from direct assay PubMed 15220135. Source: BHF-UCL positive regulation of sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: Compara positive regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: Compara
Cellular_component	extracellular space Traceable author statement Ref.1. Source: UniProtKB
Molecular_function	interleukin-5 receptor binding Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CSF2RB	P32927	2	EBI-2435811,EBI-1809771
IL5RA	Q01344	2	EBI-2435811,EBI-1759442

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

19

Ref.8

Chain

20 – 134

115

Interleukin-5

PRO_0000015560

Sites

Site

90

1

Not glycosylated

Amino acid modifications

Glycosylation

22

1

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

Glycosylation

47

1

N-linked (GlcNAc...) Probable

Disulfide bond

63

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

88

1

F → L in CAA31210. Ref.5

Secondary structure

1

.

.

.

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.

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.

.

.

.

.

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.

.

.

.

.

134

Helix Strand Turn

Details...

Helix

26 – 39

14

Helix

41 – 45

5

Beta strand

51 – 54

4

Beta strand

56 – 58

3

Helix

60 – 62

3

Helix

64 – 75

12

Helix

84 – 103

20

Beta strand

106 – 111

6

Helix

112 – 128

17

Sequences

	Sequence		Length	Mass (Da)
	P05113 [UniParc]. Last modified August 13, 1987. Version 1. Checksum: DC984467179556A3	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

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), DISULFIDE BONDS.
+	Additional computationally mapped references.

Web resources

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

Wikipedia

Interleukin-5 entry

SeattleSNPs

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. NM_000879.2.

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	[»]
3QT2	X-ray	2.55	C/D/E/F	19-134	[»]
3VA2	X-ray	2.70	A/B	23-134	[»]

ProteinModelPortal

P05113.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-28N.

IntAct

P05113. 2 interactions.

STRING

9606.ENSP00000231454.

Polymorphism databases

DMDM

124341.

Proteomic databases

PaxDb

P05113.

PeptideAtlas

P05113.

PRIDE

P05113.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000231454; ENSP00000231454; ENSG00000113525.

GeneID

3567.

KEGG

hsa:3567.

UCSC

uc003kxe.1. human.

Organism-specific databases

CTD

3567.

GeneCards

GC05M131881.

HGNC

HGNC:6016. IL5.

HPA

CAB010304.

MIM

147850. gene.

neXtProt

NX_P05113.

PharmGKB

PA29833.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG41650.

HOGENOM

HOG000074049.

HOVERGEN

HBG003865.

InParanoid

P05113.

KO

K05428.

OMA

GVINTEW.

OrthoDB

EOG4FJ8B7.

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.

Reactome

REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P05113.

Bgee

P05113.

CleanEx

HS_IL5.

Genevestigator

P05113.

GermOnline

ENSG00000113525. Homo sapiens.

Family and domain databases

Gene3D

1.20.1250.10. 1 hit.

InterPro

IPR009079. 4_helix_cytokine-like_core.
IPR012351. 4_helix_cytokine_core.
IPR000186. Interleukin_5.
[Graphical view]

PANTHER

PTHR10525. PTHR10525. 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]

SUPFAM

SSF47266. 4_helix_cytokine. 1 hit.

ProtoNet

Search...

Other

BindingDB

P05113.

ChEMBL

CHEMBL1169600.

ChiTaRS

IL5. human.

DrugBank

DB01411. Pranlukast.

EvolutionaryTrace

P05113.

GenomeRNAi

3567.

NextBio

13932.

SOURCE

Search...

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:	May 1, 2013
This is version 146 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.