Eosinophil-derived neurotoxin

Protein-coding gene in the species Homo sapiens
RNASE2
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1GQV, 1HI2, 1HI3, 1HI4, 1HI5, 1K2A, 2BEX, 2BZZ, 2C01, 2C02, 2C05, 5E13

Identifiers
AliasesRNASE2, EDN, RAF3, RNS2, ribonuclease A family member 2
External IDsOMIM: 131410; MGI: 1858598; HomoloGene: 121614; GeneCards: RNASE2; OMA:RNASE2 - orthologs
Gene location (Human)
Chromosome 14 (human)
Chr.Chromosome 14 (human)[1]
Chromosome 14 (human)
Genomic location for RNASE2
Genomic location for RNASE2
Band14q11.2Start20,955,487 bp[1]
End20,956,436 bp[1]
Gene location (Mouse)
Chromosome 14 (mouse)
Chr.Chromosome 14 (mouse)[2]
Chromosome 14 (mouse)
Genomic location for RNASE2
Genomic location for RNASE2
Band14|14 C1Start51,399,717 bp[2]
End51,400,475 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • trabecular bone

  • bone marrow

  • bone marrow cells

  • monocyte

  • granulocyte

  • blood

  • right lung

  • spleen

  • germinal epithelium

  • right adrenal cortex
Top expressed in
  • lip

  • skin of external ear

  • skin of abdomen

  • esophagus

  • skin of back

  • gastrula

  • cervix

  • perirhinal cortex

  • CA3 field

  • entorhinal cortex
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • nuclease activity
  • endonuclease activity
  • hydrolase activity
  • ribonuclease A activity
  • nucleic acid binding
  • lipopolysaccharide binding
  • ribonuclease activity
  • lyase 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
  • RNA phosphodiester bond hydrolysis
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

6036

54159

Ensembl

ENSG00000169385

ENSMUSG00000059606

UniProt

P10153

O35292

RefSeq (mRNA)

NM_002934

NM_019398

RefSeq (protein)

NP_002925

NP_062271

Location (UCSC)Chr 14: 20.96 – 20.96 MbChr 14: 51.4 – 51.4 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Eosinophil-derived neurotoxin is an enzyme that in humans is encoded by the RNASE2 gene.[5][6][7]

The protein encoded by this gene is found in eosinophil granulocytes. It is closely related to the eosinophil cationic protein (RNASE3) from which it diverged ~50 million years ago after the split between the old world and the new world monkeys.[8] 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.

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000169385 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000059606 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ 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. doi:10.1016/0888-7543(92)90237-M. PMID 1577491.
  6. ^ 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. Bibcode:1989PNAS...86.4460R. doi:10.1073/pnas.86.12.4460. PMC 287289. PMID 2734298.
  7. ^ "Entrez Gene: RNASE2 ribonuclease, RNase A family, 2 (liver, eosinophil-derived neurotoxin)".
  8. ^ Rosenberg HF (2008-05-01). "RNase A ribonucleases and host defense: an evolving story". Journal of Leukocyte Biology. 83 (5): 1079–1087. doi:10.1189/jlb.1107725. ISSN 1938-3673. PMC 2692241. PMID 18211964.

Further reading

  • Rosenberg HF, Domachowske JB (2000). "Eosinophils, ribonucleases and host defense: solving the puzzle". Immunol. Res. 20 (3): 261–74. doi:10.1007/BF02790409. PMID 10741866. S2CID 688286.
  • Abu-Ghazaleh RI, Dunnette SL, Loegering DA, et al. (1993). "Eosinophil granule proteins in peripheral blood granulocytes". J. Leukoc. Biol. 52 (6): 611–8. doi:10.1002/jlb.52.6.611. PMID 1464733. S2CID 28601297.
  • 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. doi:10.1093/oxfordjournals.jbchem.a123757. 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. doi:10.1016/0888-7543(90)90197-3. PMID 2387583.
  • 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. doi:10.1016/0378-1119(89)90414-9. PMID 2591744.
  • 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. doi:10.4049/jimmunol.143.3.952. 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. doi:10.1021/bi00412a046. PMID 3166997.
  • Sorrentino S, Tucker GK, Glitz DG (1988). "Purification and characterization of a ribonuclease from human liver". J. Biol. Chem. 263 (31): 16125–31. doi:10.1016/S0021-9258(18)37567-7. 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. Bibcode:1986PNAS...83.3146G. doi:10.1073/pnas.83.10.3146. PMC 323469. PMID 3458170.
  • Niwata Y, Ohgi K, Sanda A, et al. (1985). "Purification and properties of bovine kidney ribonucleases". J. Biochem. 97 (3): 923–34. doi:10.1093/oxfordjournals.jbchem.a135134. 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. doi:10.1021/bi00037a016. hdl:1874/5760. PMID 7547911. S2CID 22324479.
  • 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. doi:10.1021/bi00250a003. hdl:1874/5472. PMID 7947762. S2CID 13538645.
  • 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. doi:10.1038/bjc.1993.127. PMC 1968365. PMID 8471426.
  • 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. doi:10.1006/jmbi.1996.0420. PMID 8759319.
  • 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. doi:10.1091/mbc.9.2.301. PMC 25254. PMID 9450956.
  • 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. doi:10.1002/jlb.63.6.715. PMID 9620664.
  • Zhang J, Rosenberg HF (2001). "Sequence variation at two eosinophil-associated ribonuclease loci in humans". Genetics. 156 (4): 1949–58. doi:10.1093/genetics/156.4.1949. PMC 1461363. PMID 11102386.

External links

  • RNASE2+protein,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
  • Eosinophil-Derived+Neurotoxin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
  • PDBe-KB provides an overview of all the structure information available in the PDB for Human Eosinophil-derived neurotoxin


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  • 1gqv: ATOMIC RESOLUTION (0.98A) STRUCTURE OF EOSINOPHIL-DERIVED NEUROTOXIN
    1gqv: ATOMIC RESOLUTION (0.98A) STRUCTURE OF EOSINOPHIL-DERIVED NEUROTOXIN
  • 1hi2: EOSINOPHIL-DERIVED NEUROTOXIN (EDN) - SULPHATE COMPLEX
    1hi2: EOSINOPHIL-DERIVED NEUROTOXIN (EDN) - SULPHATE COMPLEX
  • 1hi3: EOSINOPHIL-DERIVED NEUROTOXIN (EDN) -ADENOSINE-2'-5'-DIPHOSPHATE COMPLEX
    1hi3: EOSINOPHIL-DERIVED NEUROTOXIN (EDN) -ADENOSINE-2'-5'-DIPHOSPHATE COMPLEX
  • 1hi4: EOSINOPHIL-DERIVED NEUROTOXIN (EDN) -ADENOSINE-3'-5'-DIPHOSPHATE COMPLEX
    1hi4: EOSINOPHIL-DERIVED NEUROTOXIN (EDN) -ADENOSINE-3'-5'-DIPHOSPHATE COMPLEX
  • 1hi5: EOSINOPHIL-DERIVED NEUROTOXIN (EDN) -ADENOSINE-5'-DIPHOSPHATE COMPLEX
    1hi5: EOSINOPHIL-DERIVED NEUROTOXIN (EDN) -ADENOSINE-5'-DIPHOSPHATE COMPLEX
  • 1k2a: Modified Form of Eosinophil-derived Neurotoxin
    1k2a: Modified Form of Eosinophil-derived Neurotoxin
  • 2bex: CRYSTAL STRUCTURE OF PLACENTAL RIBONUCLEASE INHIBITOR IN COMPLEX WITH HUMAN EOSINOPHIL DERIVED NEUROTOXIN AT 2A RESOLUTION
    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
    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
    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
    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
    2c05: CRYSTAL STRUCTURES OF EOSINOPHIL-DERIVED NEUROTOXIN IN COMPLEX WITH THE INHIBITORS 5'-ATP, AP3A, AP4A AND AP5A
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3.1.1: Carboxylic
ester hydrolases
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
Exoribonuclease
3.1.21-31:
Endonuclease
Endodeoxyribonuclease
Endoribonuclease
either deoxy- or ribo-    
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