* 114860

CARBOXYPEPTIDASE M; CPM


HGNC Approved Gene Symbol: CPM

Cytogenetic location: 12q15     Genomic coordinates (GRCh38): 12:68,842,197-68,963,469 (from NCBI)


TEXT

Description

Carboxypeptidases specifically remove COOH-terminal basic amino acids (arginine or lysine). They have important functions in many biologic processes, including activation, inactivation, or modulation of peptide hormone activity and alteration of physical properties of proteins and enzymes. Carboxypeptidase M is a membrane-bound arginine/lysine carboxypeptidase found in many tissues and cultured cells. Rehli et al. (1995) found that its expression associated with monocyte to macrophage differentiation.


Cloning and Expression

Tan et al. (1989) described the molecular cloning and sequencing of the cDNA for human carboxypeptidase M from a human placental cDNA library. The 2-kb cDNA contained an open reading frame of 1,317 basepairs, encoding a 439-amino acid protein. Sequence analysis revealed hydrophobic regions at the NH(2) and carboxy termini. There are 6 potential asparagine-linked glycosylation sites. Observed sequence homologies with other carboxypeptidases were as follows: human plasma carboxypeptidase N (212070), 41%; bovine carboxypeptidase H (114855), 41%; and bovine pancreatic carboxypeptidases A and B, 15%. The active site residues of carboxypeptidases A and B are conserved in carboxypeptidase M.


Mapping

In constructing a YAC contig from the region of the high-mobility group protein gene (600698) on chromosome 12, Kas et al. (1995) found an STS with a stretch of 135 nucleotides that matched perfectly with known cDNA sequences of the CPM gene, which had not been previously localized. They initially mapped the CPM gene to 12q31-qter by chromosome assignment using somatic cell hybrids analysis (CASH). The YAC clone containing the sequence was shown to map to 12q15 by fluorescence in situ hybridization analysis.


REFERENCES

  1. Kas, K., Schoenmakers, E. F. P. M., Van de Ven, W. J. M. Physical map location of the human carboxypeptidase M gene (CPM) distal to D12S375 and proximal to D12S8 at chromosome 12q15. Genomics 30: 403-405, 1995. [PubMed: 8586455, related citations]

  2. Rehli, M., Krause, S. W., Kreutz, M., Andreesen, R. Carboxypeptidase M is identical to the MAX.1 antigen and its expression is associated with monocyte to macrophage differentiation. J. Biol. Chem. 270: 15644-15649, 1995. [PubMed: 7797563, related citations] [Full Text]

  3. Tan, F., Chan, S. J., Steiner, D. F., Schilling, J. W., Skidgel, R. A. Molecular cloning and sequencing of the cDNA for human membrane-bound carboxypeptidase M: comparison with carboxypeptidases A, B, H, and N. J. Biol. Chem. 264: 13165-13170, 1989. [PubMed: 2753907, related citations]


Creation Date:
Victor A. McKusick : 10/6/1989
carol : 04/16/2021
alopez : 08/18/1998
terry : 6/18/1998
terry : 2/6/1996
mark : 1/14/1996
supermim : 3/16/1992
supermim : 3/20/1990
carol : 3/10/1990
ddp : 10/26/1989
root : 10/6/1989

* 114860

CARBOXYPEPTIDASE M; CPM


HGNC Approved Gene Symbol: CPM

Cytogenetic location: 12q15     Genomic coordinates (GRCh38): 12:68,842,197-68,963,469 (from NCBI)


TEXT

Description

Carboxypeptidases specifically remove COOH-terminal basic amino acids (arginine or lysine). They have important functions in many biologic processes, including activation, inactivation, or modulation of peptide hormone activity and alteration of physical properties of proteins and enzymes. Carboxypeptidase M is a membrane-bound arginine/lysine carboxypeptidase found in many tissues and cultured cells. Rehli et al. (1995) found that its expression associated with monocyte to macrophage differentiation.


Cloning and Expression

Tan et al. (1989) described the molecular cloning and sequencing of the cDNA for human carboxypeptidase M from a human placental cDNA library. The 2-kb cDNA contained an open reading frame of 1,317 basepairs, encoding a 439-amino acid protein. Sequence analysis revealed hydrophobic regions at the NH(2) and carboxy termini. There are 6 potential asparagine-linked glycosylation sites. Observed sequence homologies with other carboxypeptidases were as follows: human plasma carboxypeptidase N (212070), 41%; bovine carboxypeptidase H (114855), 41%; and bovine pancreatic carboxypeptidases A and B, 15%. The active site residues of carboxypeptidases A and B are conserved in carboxypeptidase M.


Mapping

In constructing a YAC contig from the region of the high-mobility group protein gene (600698) on chromosome 12, Kas et al. (1995) found an STS with a stretch of 135 nucleotides that matched perfectly with known cDNA sequences of the CPM gene, which had not been previously localized. They initially mapped the CPM gene to 12q31-qter by chromosome assignment using somatic cell hybrids analysis (CASH). The YAC clone containing the sequence was shown to map to 12q15 by fluorescence in situ hybridization analysis.


REFERENCES

  1. Kas, K., Schoenmakers, E. F. P. M., Van de Ven, W. J. M. Physical map location of the human carboxypeptidase M gene (CPM) distal to D12S375 and proximal to D12S8 at chromosome 12q15. Genomics 30: 403-405, 1995. [PubMed: 8586455]

  2. Rehli, M., Krause, S. W., Kreutz, M., Andreesen, R. Carboxypeptidase M is identical to the MAX.1 antigen and its expression is associated with monocyte to macrophage differentiation. J. Biol. Chem. 270: 15644-15649, 1995. [PubMed: 7797563] [Full Text: https://doi.org/10.1074/jbc.270.26.15644]

  3. Tan, F., Chan, S. J., Steiner, D. F., Schilling, J. W., Skidgel, R. A. Molecular cloning and sequencing of the cDNA for human membrane-bound carboxypeptidase M: comparison with carboxypeptidases A, B, H, and N. J. Biol. Chem. 264: 13165-13170, 1989. [PubMed: 2753907]


Creation Date:
Victor A. McKusick : 10/6/1989

Edit History:
carol : 04/16/2021
alopez : 08/18/1998
terry : 6/18/1998
terry : 2/6/1996
mark : 1/14/1996
supermim : 3/16/1992
supermim : 3/20/1990
carol : 3/10/1990
ddp : 10/26/1989
root : 10/6/1989