Entry - *131398 - RIBONUCLEASE, RNase A FAMILY, 3; RNASE3 - OMIM
 
* 131398

RIBONUCLEASE, RNase A FAMILY, 3; RNASE3


Alternative titles; symbols

RNS3
EOSINOPHIL CATIONIC PROTEIN; ECP


HGNC Approved Gene Symbol: RNASE3

Cytogenetic location: 14q11.2     Genomic coordinates (GRCh38): 14:20,891,385-20,892,348 (from NCBI)


TEXT

Description

Eosinophil cationic protein (ECP) is a small, basic protein found in the matrix of the large specific granule of the eosinophil that has cytotoxic, helminthotoxic, and ribonuclease activity. It is a member of the ribonuclease multigene family (summary by Rosenberg et al., 1989).


Cloning and Expression

Rosenberg et al. (1989) isolated a full-length cDNA clone for eosinophil cationic protein. ECP encodes a deduced mature protein of 133 amino acids with an N-terminal leader sequence of 27 amino acids. The mature protein has a calculated molecular mass of 15.6 kD and shares 66% sequence identity with eosinophil-derived neuroxin (RNASE2; 131410).


Gene Structure

Hamann et al. (1990) demonstrated remarkable similarities of eosinophil-derived neurotoxin protein and eosinophil cationic protein in noncoding sequences, introns, and flanking regions, as well as the previously known coding regions. A single intron in the 5-prime untranslated region and an intronless coding region appear to be features common to many members of the RNase gene superfamily.


Mapping

Hamann et al. (1990) mapped the RNASE2 and RANASE23 genes to chromosome 14q24-q31 by a combination of analysis of somatic cell hybrids and in situ hybridization. Mastrianni et al. (1992) confirmed the assignment of these genes to chromosome 14 by Southern analysis of DNAs from mouse-human cell hybrids. They commented on the fact that another eosinophil granule protein is encoded by a gene on chromosome 19 (CLC; 153310) and yet another, eosinophil peroxidase (EPX; 131399), by a gene on chromosome 17.


REFERENCES

  1. Hamann, K. J., Ten, R. M., Loegering, D. A., Jenkins, R. B., Heise, M. T., Schad, C. R., Pease, L. R., Gleich, G. J., Barker, R. L. 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: 535-546, 1990. [PubMed: 2387583, related citations] [Full Text]

  2. Mastrianni, D. M., Eddy, R. L., Rosenberg, H. F., Corrette, S. E., Shows, T. B., Tenen, D. G., Ackerman, S. J. 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: 240-242, 1992. [PubMed: 1577491, related citations] [Full Text]

  3. Rosenberg, H. F., Ackerman, S. J., Tenen, D. G. Human eosinophil cationic protein: molecular cloning of a cytotoxin and helminthotoxin with ribonuclease activity. J. Exp. Med. 170: 163-176, 1989. [PubMed: 2473157, related citations] [Full Text]


Contributors:
Carol A. Bocchini - updated : 10/22/2014
Creation Date:
Victor A. McKusick : 8/22/1990
carol : 10/22/2014
carol : 10/22/2014
dholmes : 9/16/1997
dholmes : 9/16/1997
mark : 3/25/1997
carol : 5/22/1992
supermim : 3/16/1992
carol : 2/16/1992
carol : 8/22/1990

* 131398

RIBONUCLEASE, RNase A FAMILY, 3; RNASE3


Alternative titles; symbols

RNS3
EOSINOPHIL CATIONIC PROTEIN; ECP


HGNC Approved Gene Symbol: RNASE3

Cytogenetic location: 14q11.2     Genomic coordinates (GRCh38): 14:20,891,385-20,892,348 (from NCBI)


TEXT

Description

Eosinophil cationic protein (ECP) is a small, basic protein found in the matrix of the large specific granule of the eosinophil that has cytotoxic, helminthotoxic, and ribonuclease activity. It is a member of the ribonuclease multigene family (summary by Rosenberg et al., 1989).


Cloning and Expression

Rosenberg et al. (1989) isolated a full-length cDNA clone for eosinophil cationic protein. ECP encodes a deduced mature protein of 133 amino acids with an N-terminal leader sequence of 27 amino acids. The mature protein has a calculated molecular mass of 15.6 kD and shares 66% sequence identity with eosinophil-derived neuroxin (RNASE2; 131410).


Gene Structure

Hamann et al. (1990) demonstrated remarkable similarities of eosinophil-derived neurotoxin protein and eosinophil cationic protein in noncoding sequences, introns, and flanking regions, as well as the previously known coding regions. A single intron in the 5-prime untranslated region and an intronless coding region appear to be features common to many members of the RNase gene superfamily.


Mapping

Hamann et al. (1990) mapped the RNASE2 and RANASE23 genes to chromosome 14q24-q31 by a combination of analysis of somatic cell hybrids and in situ hybridization. Mastrianni et al. (1992) confirmed the assignment of these genes to chromosome 14 by Southern analysis of DNAs from mouse-human cell hybrids. They commented on the fact that another eosinophil granule protein is encoded by a gene on chromosome 19 (CLC; 153310) and yet another, eosinophil peroxidase (EPX; 131399), by a gene on chromosome 17.


REFERENCES

  1. Hamann, K. J., Ten, R. M., Loegering, D. A., Jenkins, R. B., Heise, M. T., Schad, C. R., Pease, L. R., Gleich, G. J., Barker, R. L. 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: 535-546, 1990. [PubMed: 2387583] [Full Text: https://doi.org/10.1016/0888-7543(90)90197-3]

  2. Mastrianni, D. M., Eddy, R. L., Rosenberg, H. F., Corrette, S. E., Shows, T. B., Tenen, D. G., Ackerman, S. J. 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: 240-242, 1992. [PubMed: 1577491] [Full Text: https://doi.org/10.1016/0888-7543(92)90237-m]

  3. Rosenberg, H. F., Ackerman, S. J., Tenen, D. G. Human eosinophil cationic protein: molecular cloning of a cytotoxin and helminthotoxin with ribonuclease activity. J. Exp. Med. 170: 163-176, 1989. [PubMed: 2473157] [Full Text: https://doi.org/10.1084/jem.170.1.163]


Contributors:
Carol A. Bocchini - updated : 10/22/2014

Creation Date:
Victor A. McKusick : 8/22/1990

Edit History:
carol : 10/22/2014
carol : 10/22/2014
dholmes : 9/16/1997
dholmes : 9/16/1997
mark : 3/25/1997
carol : 5/22/1992
supermim : 3/16/1992
carol : 2/16/1992
carol : 8/22/1990