Eosinophil-derived neurotoxin

RNASE2

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
1GQV, 1HI2, 1HI3, 1HI4, 1HI5, 1K2A, 2BEX, 2BZZ, 2C01, 2C02, 2C05, 5E13

Identifiers

Aliases

RNASE2, EDN, RAF3, RNS2, ribonuclease A family member 2

External IDs

MGI: 1890465 HomoloGene: 121614 GeneCards: RNASE2

Gene ontology
Molecular function	• nuclease activity • endonuclease activity • hydrolase activity • ribonuclease A activity • nucleic acid binding • lipopolysaccharide binding • ribonuclease activity
Cellular component	• extracellular region • lysosome • extracellular exosome • azurophil granule lumen
Biological process	• chemotaxis • RNA catabolic process • RNA phosphodiester bond hydrolysis, endonucleolytic • positive regulation of protein targeting to mitochondrion • neutrophil degranulation • induction of bacterial agglutination • defense response to Gram-negative bacterium • defense response to Gram-positive bacterium • defense response to virus • RNA phosphodiester bond hydrolysis
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


6036


93726

Ensembl


ENSG00000169385


ENSMUSG00000047222

UniProt


P10153


Q8K196

RefSeq (mRNA)


NM_002934


NM_053113

RefSeq (protein)


NP_002925


NP_444343

Location (UCSC)

Chr 14: 20.96 – 20.96 Mb

Chr 14: 51.26 – 51.26 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

Eosinophil-derived neurotoxin is an enzyme that in humans is encoded by the RNASE2 gene.^[3]^[4]^[5]

The protein encoded by this gene is found in eosinophil granulocytes. It is closely related to the eosinophil cationic protein from which it diverged ~50 million years ago after the split between the old world and the new world monkeys.^[6] It is relatively neutral and has cytotoxic properties. It is capable of reducing the activity of single strand RNA viruses in culture through its enzymatic activity. It also serves as an attractant to immune cells.

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ Mastrianni DM, Eddy RL, Rosenberg HF, Corrette SE, Shows TB, Tenen DG, Ackerman SJ (Jun 1992). "Localization of the human eosinophil Charcot-Leyden crystal protein (lysophospholipase) gene (CLC) to chromosome 19 and the human ribonuclease 2 (eosinophil-derived neurotoxin) and ribonuclease 3 (eosinophil cationic protein) genes (RNS2 and RNS3) to chromosome 14". Genomics. 13 (1): 240–2. PMID 1577491. doi:10.1016/0888-7543(92)90237-M.
↑ Rosenberg HF, Tenen DG, Ackerman SJ (Jul 1989). "Molecular cloning of the human eosinophil-derived neurotoxin: a member of the ribonuclease gene family". Proc Natl Acad Sci U S A. 86 (12): 4460–4. PMC 287289 . PMID 2734298. doi:10.1073/pnas.86.12.4460.
↑ "Entrez Gene: RNASE2 ribonuclease, RNase A family, 2 (liver, eosinophil-derived neurotoxin)".
↑ Rosenberg, Helene F. (2008-05-01). "RNase A ribonucleases and host defense: an evolving story". Journal of Leukocyte Biology. 83 (5): 1079–1087. ISSN 1938-3673. PMC 2692241 . PMID 18211964. doi:10.1189/jlb.1107725. Retrieved 2013-12-19.

Rosenberg HF, Domachowske JB (2000). "Eosinophils, ribonucleases and host defense: solving the puzzle.". Immunol. Res. 20 (3): 261–74. PMID 10741866. doi:10.1007/BF02790409.
Abu-Ghazaleh RI, Dunnette SL, Loegering DA, et al. (1993). "Eosinophil granule proteins in peripheral blood granulocytes.". J. Leukoc. Biol. 52 (6): 611–8. PMID 1464733.
Sakakibara R, Hashida K, Kitahara T, Ishiguro M (1992). "Characterization of a unique nonsecretory ribonuclease from urine of pregnant women.". J. Biochem. 111 (3): 325–30. PMID 1587793.
Hamann KJ, Ten RM, Loegering DA, et al. (1990). "Structure and chromosome localization of the human eosinophil-derived neurotoxin and eosinophil cationic protein genes: evidence for intronless coding sequences in the ribonuclease gene superfamily.". Genomics. 7 (4): 535–46. PMID 2387583. doi:10.1016/0888-7543(90)90197-3.
Hamann KJ, Barker RL, Loegering DA, et al. (1990). "Sequence of human eosinophil-derived neurotoxin cDNA: identity of deduced amino acid sequence with human nonsecretory ribonucleases.". Gene. 83 (1): 161–7. PMID 2591744. doi:10.1016/0378-1119(89)90414-9.
Barker RL, Loegering DA, Ten RM, et al. (1989). "Eosinophil cationic protein cDNA. Comparison with other toxic cationic proteins and ribonucleases.". J. Immunol. 143 (3): 952–5. PMID 2745977.
Beintema JJ, Hofsteenge J, Iwama M, et al. (1988). "Amino acid sequence of the nonsecretory ribonuclease of human urine.". Biochemistry. 27 (12): 4530–8. PMID 3166997. doi:10.1021/bi00412a046.
Sorrentino S, Tucker GK, Glitz DG (1988). "Purification and characterization of a ribonuclease from human liver.". J. Biol. Chem. 263 (31): 16125–31. PMID 3182786.
Gleich GJ, Loegering DA, Bell MP, et al. (1986). "Biochemical and functional similarities between human eosinophil-derived neurotoxin and eosinophil cationic protein: homology with ribonuclease.". Proc. Natl. Acad. Sci. U.S.A. 83 (10): 3146–50. PMC 323469 . PMID 3458170. doi:10.1073/pnas.83.10.3146.
Niwata Y, Ohgi K, Sanda A, et al. (1985). "Purification and properties of bovine kidney ribonucleases.". J. Biochem. 97 (3): 923–34. PMID 3926759.
de Beer T, Vliegenthart JF, Löffler A, Hofsteenge J (1995). "The hexopyranosyl residue that is C-glycosidically linked to the side chain of tryptophan-7 in human RNase Us is alpha-mannopyranose.". Biochemistry. 34 (37): 11785–9. PMID 7547911. doi:10.1021/bi00037a016.
Hofsteenge J, Müller DR, de Beer T, et al. (1994). "New type of linkage between a carbohydrate and a protein: C-glycosylation of a specific tryptophan residue in human RNase Us.". Biochemistry. 33 (46): 13524–30. PMID 7947762. doi:10.1021/bi00250a003.
Kardana A, Bagshawe KD, Coles B, et al. (1993). "Characterisation of UGP and its relationship with beta-core fragment.". Br. J. Cancer. 67 (4): 686–92. PMC 1968365 . PMID 8471426. doi:10.1038/bjc.1993.127.
Mosimann SC, Newton DL, Youle RJ, James MN (1996). "X-ray crystallographic structure of recombinant eosinophil-derived neurotoxin at 1.83 A resolution.". J. Mol. Biol. 260 (4): 540–52. PMID 8759319. doi:10.1006/jmbi.1996.0420.
Krieg J, Hartmann S, Vicentini A, et al. (1998). "Recognition signal for C-mannosylation of Trp-7 in RNase 2 consists of sequence Trp-x-x-Trp.". Mol. Biol. Cell. 9 (2): 301–9. PMC 25254 . PMID 9450956. doi:10.1091/mbc.9.2.301.
Sur S, Glitz DG, Kita H, et al. (1998). "Localization of eosinophil-derived neurotoxin and eosinophil cationic protein in neutrophilic leukocytes.". J. Leukoc. Biol. 63 (6): 715–22. PMID 9620664.
Zhang J, Rosenberg HF (2001). "Sequence variation at two eosinophil-associated ribonuclease loci in humans.". Genetics. 156 (4): 1949–58. PMC 1461363 . PMID 11102386.

PDB gallery

1gqv: ATOMIC RESOLUTION (0.98A) STRUCTURE OF EOSINOPHIL-DERIVED NEUROTOXIN

1hi2: EOSINOPHIL-DERIVED NEUROTOXIN (EDN) - SULPHATE COMPLEX

1hi3: EOSINOPHIL-DERIVED NEUROTOXIN (EDN) -ADENOSINE-2'-5'-DIPHOSPHATE COMPLEX

1hi4: EOSINOPHIL-DERIVED NEUROTOXIN (EDN) -ADENOSINE-3'-5'-DIPHOSPHATE COMPLEX

1hi5: EOSINOPHIL-DERIVED NEUROTOXIN (EDN) -ADENOSINE-5'-DIPHOSPHATE COMPLEX

1k2a: Modified Form of Eosinophil-derived Neurotoxin

2bex: CRYSTAL STRUCTURE OF PLACENTAL RIBONUCLEASE INHIBITOR IN COMPLEX WITH HUMAN EOSINOPHIL DERIVED NEUROTOXIN AT 2A RESOLUTION

2bzz: CRYSTAL STRUCTURES OF EOSINOPHIL-DERIVED NEUROTOXIN IN COMPLEX WITH THE INHIBITORS 5'-ATP, AP3A, AP4A AND AP5A

2c01: CRYSTAL STRUCTURES OF EOSINOPHIL-DERIVED NEUROTOXIN IN COMPLEX WITH THE INHIBITORS 5'-ATP, AP3A, AP4A AND AP5A

2c02: CRYSTAL STRUCTURES OF EOSINOPHIL-DERIVED NEUROTOXIN IN COMPLEX WITH THE INHIBITORS 5'-ATP, AP3A, AP4A AND AP5A

2c05: CRYSTAL STRUCTURES OF EOSINOPHIL-DERIVED NEUROTOXIN IN COMPLEX WITH THE INHIBITORS 5'-ATP, AP3A, AP4A AND AP5A

External links

RNASE2 protein, human at the US National Library of Medicine Medical Subject Headings (MeSH)
Eosinophil-Derived Neurotoxin at the US National Library of Medicine Medical Subject Headings (MeSH)

Hydrolase: esterases (EC 3.1)

3.1.1: Carboxylic
ester hydrolases

Lipase

Phospholipase
- A1
- A2
- B

3.1.2: Thioesterase

3.1.3: Phosphatase

3.1.4:
Phosphodiesterase

3.1.6: Sulfatase

Nuclease (includes
deoxyribonuclease
and ribonuclease)

3.1.11-16:
Exonuclease

Exodeoxyribonuclease	RecBCD
Exoribonuclease	Oligonucleotidase

3.1.21-31:
Endonuclease

Endodeoxyribonuclease	Deoxyribonuclease I Deoxyribonuclease II Deoxyribonuclease IV Restriction enzyme UvrABC endonuclease
Endoribonuclease	RNase III RNase H 1 2A 2B 2C RNase P RNase A 1 2 3 4/5 RNase T1 RNA-induced silencing complex
either deoxy- or ribo-	Aspergillus nuclease S1 Micrococcal nuclease

Antimicrobial peptides: Granulocyte granule contents

Azurophilic granules (1°)

Myeloperoxidase
Defensins
neutral serine proteases (Proteinase 3)
Lysozyme
Bactericidal/permeability-increasing protein
Collagenase

Specific granules (2°)

Neutrophil	Alkaline phosphatase Lactoferrin Lysozyme NADPH oxidase Collagenase Cathelicidin
Eosinophil	Cathepsin Major basic protein Eosinophil cationic protein Eosinophil peroxidase Eosinophil-derived neurotoxin
Basophil	Heparin Histamine

see also platelet alpha-granule, dense granule

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Eosinophil-derived neurotoxin

See also

References

Further reading

External links