Entry - *600544 - SOLUTE CARRIER FAMILY 15 (OLIGOPEPTIDE TRANSPORTER), MEMBER 1; SLC15A1 - OMIM
 
* 600544

SOLUTE CARRIER FAMILY 15 (OLIGOPEPTIDE TRANSPORTER), MEMBER 1; SLC15A1


Alternative titles; symbols

HYDROGEN ION/PEPTIDE COTRANSPORTER, INTESTINAL; HPEPT1


HGNC Approved Gene Symbol: SLC15A1

Cytogenetic location: 13q32.2-q32.3     Genomic coordinates (GRCh38): 13:98,683,801-98,752,672 (from NCBI)


TEXT

Cloning and Expression

In mammalian small intestine, the proton-coupled peptide transporter is responsible for the absorption of small peptides arising from digestion of dietary proteins. Fei et al. (1994) isolated a cDNA clone encoding a hydrogen ion/peptide cotransporter from a rabbit intestinal cDNA library. Liang et al. (1995) screened a human intestinal cDNA library with a probe derived from the rabbit cotransporter cDNA and identified a cDNA (SLC15A1) encoding a deduced 708-amino acid protein with 12 membrane-spanning domains and 2 putative sites for protein kinase C-dependent phosphorylation. The human cotransporter showed 81% identity and 92% similarity to the rabbit cotransporter, but only a weak homology to the proton-coupled peptide transport proteins present in bacteria and yeast.


Mapping

By analysis of somatic cell hybrids and by isotopic in situ hybridization, Liang et al. (1995) mapped the SLC15A1 gene to 13q33-q34.


Gene Function

Liang et al. (1995) found that expression of SLC15A1 in HeLa cells or in Xenopus laevis oocytes induced proton-dependent peptide transport activity. The cDNA-induced transport process accepted dipeptides, tripeptides, and amino beta-lactam antibiotics as substrates, but could not transport free amino acids.

Adibi (1997) reviewed the biology and function of the human intestinal oligopeptide transporter, which he symbolized PEPT1. Studies indicated that it transports dipeptides and tripeptides but not free amino acids or peptides with more than 3 amino acid residues and that its driving force for uphill transport requires proton binding and presence of an inside-negative membrane potential. Adibi (1997) pointed out the importance of the transporter in nutritional and pharmacologic therapies; for example, it has allowed the use of oligopeptides as a source of nitrogen for enteral feeding and the use of the oral route for delivery of peptidomimetic drugs such as beta-lactam antibiotics.


REFERENCES

  1. Adibi, S. A. The oligopeptide transporter (Pept-1) in human intestine: biology and function. Gastroenterology 113: 332-340, 1997. [PubMed: 9207295, related citations] [Full Text]

  2. Fei, Y. -J., Kanai, Y., Nussberger, S., Ganapathy, V., Leibach, F. H., Romero, M. F., Singh, S. K., Boron, W. F., Hediger, M. A. Expression cloning of a mammalian proton-coupled oligopeptide transporter. Nature 368: 563-566, 1994. [PubMed: 8139693, related citations] [Full Text]

  3. Liang, R., Fei, Y.-J., Prasad, P. D., Ramamoorthy, S., Han, H., Yang-Feng, T. L., Hediger, M. A., Ganapathy, V., Leibach, F. H. Human intestinal H(+)/peptide cotransporter: cloning, functional expression, and chromosomal localization. J. Biol. Chem. 270: 6456-6463, 1995. [PubMed: 7896779, related citations] [Full Text]


Contributors:
Victor A. McKusick - updated : 9/16/1997
Creation Date:
Victor A. McKusick : 5/21/1995
carol : 02/01/2011
terry : 3/28/2002
alopez : 12/2/1997
mark : 9/22/1997
terry : 9/16/1997
mark : 7/27/1995
mark : 5/23/1995
mark : 5/21/1995

* 600544

SOLUTE CARRIER FAMILY 15 (OLIGOPEPTIDE TRANSPORTER), MEMBER 1; SLC15A1


Alternative titles; symbols

HYDROGEN ION/PEPTIDE COTRANSPORTER, INTESTINAL; HPEPT1


HGNC Approved Gene Symbol: SLC15A1

Cytogenetic location: 13q32.2-q32.3     Genomic coordinates (GRCh38): 13:98,683,801-98,752,672 (from NCBI)


TEXT

Cloning and Expression

In mammalian small intestine, the proton-coupled peptide transporter is responsible for the absorption of small peptides arising from digestion of dietary proteins. Fei et al. (1994) isolated a cDNA clone encoding a hydrogen ion/peptide cotransporter from a rabbit intestinal cDNA library. Liang et al. (1995) screened a human intestinal cDNA library with a probe derived from the rabbit cotransporter cDNA and identified a cDNA (SLC15A1) encoding a deduced 708-amino acid protein with 12 membrane-spanning domains and 2 putative sites for protein kinase C-dependent phosphorylation. The human cotransporter showed 81% identity and 92% similarity to the rabbit cotransporter, but only a weak homology to the proton-coupled peptide transport proteins present in bacteria and yeast.


Mapping

By analysis of somatic cell hybrids and by isotopic in situ hybridization, Liang et al. (1995) mapped the SLC15A1 gene to 13q33-q34.


Gene Function

Liang et al. (1995) found that expression of SLC15A1 in HeLa cells or in Xenopus laevis oocytes induced proton-dependent peptide transport activity. The cDNA-induced transport process accepted dipeptides, tripeptides, and amino beta-lactam antibiotics as substrates, but could not transport free amino acids.

Adibi (1997) reviewed the biology and function of the human intestinal oligopeptide transporter, which he symbolized PEPT1. Studies indicated that it transports dipeptides and tripeptides but not free amino acids or peptides with more than 3 amino acid residues and that its driving force for uphill transport requires proton binding and presence of an inside-negative membrane potential. Adibi (1997) pointed out the importance of the transporter in nutritional and pharmacologic therapies; for example, it has allowed the use of oligopeptides as a source of nitrogen for enteral feeding and the use of the oral route for delivery of peptidomimetic drugs such as beta-lactam antibiotics.


REFERENCES

  1. Adibi, S. A. The oligopeptide transporter (Pept-1) in human intestine: biology and function. Gastroenterology 113: 332-340, 1997. [PubMed: 9207295] [Full Text: https://doi.org/10.1016/s0016-5085(97)70112-4]

  2. Fei, Y. -J., Kanai, Y., Nussberger, S., Ganapathy, V., Leibach, F. H., Romero, M. F., Singh, S. K., Boron, W. F., Hediger, M. A. Expression cloning of a mammalian proton-coupled oligopeptide transporter. Nature 368: 563-566, 1994. [PubMed: 8139693] [Full Text: https://doi.org/10.1038/368563a0]

  3. Liang, R., Fei, Y.-J., Prasad, P. D., Ramamoorthy, S., Han, H., Yang-Feng, T. L., Hediger, M. A., Ganapathy, V., Leibach, F. H. Human intestinal H(+)/peptide cotransporter: cloning, functional expression, and chromosomal localization. J. Biol. Chem. 270: 6456-6463, 1995. [PubMed: 7896779] [Full Text: https://doi.org/10.1074/jbc.270.12.6456]


Contributors:
Victor A. McKusick - updated : 9/16/1997

Creation Date:
Victor A. McKusick : 5/21/1995

Edit History:
carol : 02/01/2011
terry : 3/28/2002
alopez : 12/2/1997
mark : 9/22/1997
terry : 9/16/1997
mark : 7/27/1995
mark : 5/23/1995
mark : 5/21/1995