Peptide transporter 1

Last updated
SLC15A1
Identifiers
Aliases SLC15A1 , HPECT1, HPEPT1, PEPT1, Peptide transporter 1, solute carrier family 15 member 1
External IDs OMIM: 600544 MGI: 1861376 HomoloGene: 38006 GeneCards: SLC15A1
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_005073

NM_053079

RefSeq (protein)

NP_005064

NP_444309

Location (UCSC) Chr 13: 98.68 – 98.75 Mb Chr 14: 121.46 – 121.51 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Peptide transporter 1 (PepT 1) also known as solute carrier family 15 member 1 (SLC15A1) is a protein that in humans is encoded by SLC15A1 gene. [5] [6] PepT 1 is a solute carrier for oligopeptides. It functions in renal oligopeptide reabsorption and in the intestines in a proton dependent way, hence acting like a cotransporter. [7]

Contents

Function

SLC15A1is localized to the brush border membrane of the intestinal epithelium and mediates the uptake of di- and tripeptides from the lumen into the enterocytes. This protein plays an important role in the uptake and digestion of dietary proteins. This protein also facilitates the absorption of numerous peptidomimetic drugs. [5] [7] Peptide transporter 1 functions in nutrient and drug transport have been studied using intestinal organoids. [8] [9]

See also

Related Research Articles

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Monocarboxylate transporter 10

Monocarboxylate transporter 10, also known as aromatic amino acid transporter 1 and T-type amino acid transporter 1 (TAT1) and solute carrier family 16 member 10 (SLC16A10), is a protein that in humans is encoded by the SLC16A10 gene. SLC16A10 is a member of the solute carrier family.

Proteins of the Proton-dependent Oligopeptide Transporter (POT) Family are found in animals, plants, yeast, archaea and both Gram-negative and Gram-positive bacteria, and are part of the major facilitator superfamily. The transport of peptides into cells is a well-documented biological phenomenon which is accomplished by specific, energy-dependent transporters found in a number of organisms as diverse as bacteria and humans. The proton-dependent oligopeptide transporter (PTR) family of proteins is distinct from the ABC-type peptide transporters and was uncovered by sequence analyses of a number of recently discovered peptide transport proteins. These proteins that seem to be mainly involved in the intake of small peptides with the concomitant uptake of a proton.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000088386 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000025557 - 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. 1 2 "Entrez Gene: SLC15A1 Solute carrier family 15 (oligopeptide transporter), member 1".
  6. Liang R, Fei YJ, Prasad PD, Ramamoorthy S, Han H, Yang-Feng TL, Hediger MA, Ganapathy V, Leibach FH (March 1995). "Human intestinal H+/peptide cotransporter. Cloning, functional expression, and chromosomal localization". J. Biol. Chem. 270 (12): 6456–63. doi: 10.1074/jbc.270.12.6456 . PMID   7896779.
  7. 1 2 Adibi SA (July 1997). "The oligopeptide transporter (Pept-1) in human intestine: biology and function". Gastroenterology. 113 (1): 332–40. doi:10.1016/S0016-5085(97)70112-4. PMID   9207295.
  8. Zietek T, Rath E, Haller D, Daniel H (November 2015). "Intestinal organoids for assessing nutrient transport, sensing and incretin secretion". Scientific Reports. 5 (1): 16831. doi: 10.1038/srep16831 . PMC   4652176 . PMID   26582215.
  9. Zietek T, Giesbertz P, Ewers M, Reichart F, Weinmüller M, Demir IE, et al. (2020). "Organoids to Study Intestinal Nutrient Transport, Drug Uptake and Metabolism – Update to the Human Model and Expansion of Applications". Frontiers in Bioengineering and Biotechnology. 8: 577656. doi: 10.3389/fbioe.2020.577656 . PMC   7516017 . PMID   33015026.

Further reading

This article incorporates text from the United States National Library of Medicine, which is in the public domain.