* 602058

PROTEASE INHIBITOR 10; PI10


Alternative titles; symbols

BOMAPIN
SERPIN PEPTIDASE INHIBITOR, CLADE B (OVALBUMIN), MEMBER 10; SERPINB10


HGNC Approved Gene Symbol: SERPINB10

Cytogenetic location: 18q22.1     Genomic coordinates (GRCh38): 18:63,907,958-63,936,111 (from NCBI)


TEXT

Description

The superfamily of high molecular weight serine proteinase inhibitors (serpins) regulate a diverse set of intracellular and extracellular processes such as complement activation, fibrinolysis, coagulation, cellular differentiation, tumor suppression, apoptosis, and cell migration. Serpins are characterized by a well-conserved tertiary structure that consists of 3 beta sheets and 8 or 9 alpha helices (Huber and Carrell, 1989). A critical portion of the molecule, the reactive center loop connects beta sheets A and C. Protease inhibitor-10 (PI10; SERPINB10) is a member of the ov-serpin subfamily, which, relative to the archetypal serpin PI1 (107400), is characterized by a high degree of homology to chicken ovalbumin, lack of N- and C-terminal extensions, absence of a signal peptide, and a serine rather than an asparagine residue at the penultimate position (summary by Bartuski et al., 1997).


Cloning and Expression

Riewald and Schleef (1995) cloned PI10, which they called bomapin, from a human bone marrow cDNA library. The deduced 397-amino acid protein has a calculated molecular mass of 45 kD and shares 48% sequence identity with PAI2 (173390) and elastase inhibitor (SERPINB1; 130135), A single 2.3-kb PI10 transcript was highly expressed in human bone marrow cells but was undetectable in all other analyzed human tissues.


Gene Function

Riewald and Schleef (1995) demonstrated that PI10 was able to form SDS-stable complexes with thrombin and trypsin. They suggested that PI10 may play a role in the regulation of protease activities during hematopoiesis.


Mapping

Bartuski et al. (1997) found that the bomapin gene maps to 18q21.3 where at least 5 other ov-serpins map.


REFERENCES

  1. Bartuski, A. J., Kamachi, Y., Schick, C., Overhauser, J., Silverman, G. A. Cytoplasmic antiproteinase 2 (PI8) and bomapin (PI10) map to the serpin cluster at 18q21.3. Genomics 43: 321-328, 1997. [PubMed: 9268635, related citations] [Full Text]

  2. Huber, R., Carrell, R. W. Implications of the three-dimensional structure of alpha 1-antitrypsin for structure and function of serpins. Biochemistry 28: 8951-8966, 1989. [PubMed: 2690952, related citations] [Full Text]

  3. Riewald, M., Schleef, R. R. Molecular cloning of bomapin (protease inhibitor 10), a novel human serpin that is expressed specifically in the bone marrow. J. Biol. Chem. 270: 26754-26757, 1995. [PubMed: 7592909, related citations] [Full Text]


Creation Date:
Victor A. McKusick : 10/16/1997
carol : 01/06/2010
carol : 12/1/2000
kayiaros : 7/13/1999
dholmes : 10/23/1997
mark : 10/16/1997

* 602058

PROTEASE INHIBITOR 10; PI10


Alternative titles; symbols

BOMAPIN
SERPIN PEPTIDASE INHIBITOR, CLADE B (OVALBUMIN), MEMBER 10; SERPINB10


HGNC Approved Gene Symbol: SERPINB10

Cytogenetic location: 18q22.1     Genomic coordinates (GRCh38): 18:63,907,958-63,936,111 (from NCBI)


TEXT

Description

The superfamily of high molecular weight serine proteinase inhibitors (serpins) regulate a diverse set of intracellular and extracellular processes such as complement activation, fibrinolysis, coagulation, cellular differentiation, tumor suppression, apoptosis, and cell migration. Serpins are characterized by a well-conserved tertiary structure that consists of 3 beta sheets and 8 or 9 alpha helices (Huber and Carrell, 1989). A critical portion of the molecule, the reactive center loop connects beta sheets A and C. Protease inhibitor-10 (PI10; SERPINB10) is a member of the ov-serpin subfamily, which, relative to the archetypal serpin PI1 (107400), is characterized by a high degree of homology to chicken ovalbumin, lack of N- and C-terminal extensions, absence of a signal peptide, and a serine rather than an asparagine residue at the penultimate position (summary by Bartuski et al., 1997).


Cloning and Expression

Riewald and Schleef (1995) cloned PI10, which they called bomapin, from a human bone marrow cDNA library. The deduced 397-amino acid protein has a calculated molecular mass of 45 kD and shares 48% sequence identity with PAI2 (173390) and elastase inhibitor (SERPINB1; 130135), A single 2.3-kb PI10 transcript was highly expressed in human bone marrow cells but was undetectable in all other analyzed human tissues.


Gene Function

Riewald and Schleef (1995) demonstrated that PI10 was able to form SDS-stable complexes with thrombin and trypsin. They suggested that PI10 may play a role in the regulation of protease activities during hematopoiesis.


Mapping

Bartuski et al. (1997) found that the bomapin gene maps to 18q21.3 where at least 5 other ov-serpins map.


REFERENCES

  1. Bartuski, A. J., Kamachi, Y., Schick, C., Overhauser, J., Silverman, G. A. Cytoplasmic antiproteinase 2 (PI8) and bomapin (PI10) map to the serpin cluster at 18q21.3. Genomics 43: 321-328, 1997. [PubMed: 9268635] [Full Text: https://doi.org/10.1006/geno.1997.4827]

  2. Huber, R., Carrell, R. W. Implications of the three-dimensional structure of alpha 1-antitrypsin for structure and function of serpins. Biochemistry 28: 8951-8966, 1989. [PubMed: 2690952] [Full Text: https://doi.org/10.1021/bi00449a001]

  3. Riewald, M., Schleef, R. R. Molecular cloning of bomapin (protease inhibitor 10), a novel human serpin that is expressed specifically in the bone marrow. J. Biol. Chem. 270: 26754-26757, 1995. [PubMed: 7592909] [Full Text: https://doi.org/10.1074/jbc.270.45.26754]


Creation Date:
Victor A. McKusick : 10/16/1997

Edit History:
carol : 01/06/2010
carol : 12/1/2000
kayiaros : 7/13/1999
dholmes : 10/23/1997
mark : 10/16/1997