ID S15A1_HUMAN Reviewed; 708 AA. AC P46059; Q5VW82; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 10-JUN-2026, entry version 190. DE RecName: Full=Solute carrier family 15 member 1 {ECO:0000305}; DE AltName: Full=Intestinal H(+)/peptide cotransporter {ECO:0000303|PubMed:7896779}; DE AltName: Full=Oligopeptide transporter, small intestine isoform {ECO:0000303|PubMed:7896779}; DE AltName: Full=Peptide transporter 1 {ECO:0000303|PubMed:7896779}; GN Name=SLC15A1 {ECO:0000312|HGNC:HGNC:10920}; GN Synonyms=PEPT1 {ECO:0000303|PubMed:7896779}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TRANSPORTER ACTIVITY. RC TISSUE=Intestine; RX PubMed=7896779; DOI=10.1074/jbc.270.12.6456; RA Liang R., Fei Y.-J., Prasad P.D., Ramamoorthy S., Han H., Yang-Feng T.L., RA Hediger M.A., Ganapathy V., Leibach F.H.; RT "Human intestinal H+/peptide cotransporter. Cloning, functional expression, RT and chromosomal localization."; RL J. Biol. Chem. 270:6456-6463(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057823; DOI=10.1038/nature02379; RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L., RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., RA Frankish A.G., Frankland J., French L., Garner P., Garnett J., RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., RA Rogers J., Ross M.T.; RT "The DNA sequence and analysis of human chromosome 13."; RL Nature 428:522-528(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP FUNCTION, AND TRANSPORTER ACTIVITY. RX PubMed=8914574; DOI=10.1016/s0005-2736(96)00170-8; RA Mackenzie B., Fei Y.J., Ganapathy V., Leibach F.H.; RT "The human intestinal H+/oligopeptide cotransporter hPEPT1 transports RT differently-charged dipeptides with identical electrogenic properties."; RL Biochim. Biophys. Acta 1284:125-128(1996). RN [5] RP FUNCTION, AND TRANSPORTER ACTIVITY. RX PubMed=9835627; DOI=10.1172/jci4179; RA Merlin D., Steel A., Gewirtz A.T., Si-Tahar M., Hediger M.A., Madara J.L.; RT "hPepT1-mediated epithelial transport of bacteria-derived chemotactic RT peptides enhances neutrophil-epithelial interactions."; RL J. Clin. Invest. 102:2011-2018(1998). RN [6] RP FUNCTION, AND TRANSPORTER ACTIVITY. RX PubMed=15521010; DOI=10.1053/j.gastro.2004.07.024; RA Vavricka S.R., Musch M.W., Chang J.E., Nakagawa Y., Phanvijhitsiri K., RA Waypa T.S., Merlin D., Schneewind O., Chang E.B.; RT "hPepT1 transports muramyl dipeptide, activating NF-kappaB and stimulating RT IL-8 secretion in human colonic Caco2/bbe cells."; RL Gastroenterology 127:1401-1409(2004). RN [7] RP FUNCTION, AND TRANSPORTER ACTIVITY. RX PubMed=18367661; DOI=10.1152/ajprenal.00030.2008; RA Sala-Rabanal M., Loo D.D., Hirayama B.A., Wright E.M.; RT "Molecular mechanism of dipeptide and drug transport by the human renal RT H+/oligopeptide cotransporter hPEPT2."; RL Am. J. Physiol. 294:F1422-F1432(2008). RN [8] RP FUNCTION, TRANSPORTER ACTIVITY, AND MUTAGENESIS OF TYR-588; GLY-594 AND RP GLU-595. RX PubMed=19685173; DOI=10.1007/s11095-009-9952-9; RA Xu L., Haworth I.S., Kulkarni A.A., Bolger M.B., Davies D.L.; RT "Mutagenesis and cysteine scanning of transmembrane domain 10 of the human RT dipeptide transporter."; RL Pharm. Res. 26:2358-2366(2009). RN [9] RP FUNCTION, TRANSPORTER ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND RP MUTAGENESIS OF ASP-573. RX PubMed=26320580; DOI=10.1016/j.str.2015.07.016; RA Beale J.H., Parker J.L., Samsudin F., Barrett A.L., Senan A., Bird L.E., RA Scott D., Owens R.J., Sansom M.S.P., Tucker S.J., Meredith D., Fowler P.W., RA Newstead S.; RT "Crystal structures of the extracellular domain from PepT1 and PepT2 RT provide novel insights into mammalian peptide transport."; RL Structure 23:1889-1899(2015). RN [10] RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=28408210; DOI=10.1016/j.xphs.2017.04.001; RA Keiser M., Kaltheuner L., Wildberg C., Mueller J., Grube M., Partecke L.I., RA Heidecke C.D., Oswald S.; RT "The Organic Anion-Transporting Peptide 2B1 Is Localized in the Basolateral RT Membrane of the Human Jejunum and Caco-2 Monolayers."; RL J. Pharm. Sci. 106:2657-2663(2017). RN [11] RP VARIANTS ASN-117 AND ALA-419. RX PubMed=12436193; DOI=10.1007/s100380200088; RA Saito S., Iida A., Sekine A., Ogawa C., Kawauchi S., Higuchi S., RA Nakamura Y.; RT "Catalog of 238 variations among six human genes encoding solute carriers RT (hSLCs) in the Japanese population."; RL J. Hum. Genet. 47:576-584(2002). RN [12] RP VARIANTS ILE-21; TYR-28; ASN-117; ARG-117; MET-122; ALA-419; ILE-450; RP ASN-451 AND SER-537. RX PubMed=16258023; DOI=10.1124/jpet.105.094615; RA Anderle P., Nielsen C.U., Pinsonneault J., Krog P.L., Brodin B., Sadee W.; RT "Genetic variants of the human dipeptide transporter PEPT1."; RL J. Pharmacol. Exp. Ther. 316:636-646(2006). CC -!- FUNCTION: Electrogenic proton-coupled amino-acid transporter that CC transports oligopeptides of 2 to 4 amino acids with a preference for CC dipeptides. Transports neutral and monovalently charged peptides with a CC proton to peptide stoichiometry of 1:1 or 2:1 (By similarity) CC (PubMed:15521010, PubMed:18367661, PubMed:19685173, PubMed:26320580, CC PubMed:7896779, PubMed:8914574, PubMed:9835627). Primarily responsible CC for the absorption of dietary di- and tripeptides from the small CC intestinal lumen (By similarity). Mediates transepithelial transport of CC muramyl and N-formylated bacterial dipeptides contributing to CC recognition of pathogenic bacteria by the mucosal immune system CC (PubMed:15521010, PubMed:9835627). {ECO:0000250|UniProtKB:P36836, CC ECO:0000269|PubMed:15521010, ECO:0000269|PubMed:18367661, CC ECO:0000269|PubMed:19685173, ECO:0000269|PubMed:7896779, CC ECO:0000269|PubMed:8914574, ECO:0000269|PubMed:9835627}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a dipeptide(out) + H(+)(out) = a dipeptide(in) + H(+)(in); CC Xref=Rhea:RHEA:64392, ChEBI:CHEBI:15378, ChEBI:CHEBI:90799; CC Evidence={ECO:0000269|PubMed:15521010, ECO:0000269|PubMed:18367661, CC ECO:0000269|PubMed:19685173, ECO:0000269|PubMed:7896779, CC ECO:0000269|PubMed:8914574}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64393; CC Evidence={ECO:0000305|PubMed:15521010, ECO:0000305|PubMed:18367661, CC ECO:0000305|PubMed:19685173, ECO:0000305|PubMed:7896779, CC ECO:0000305|PubMed:8914574}; CC -!- CATALYTIC ACTIVITY: CC Reaction=an L-amino acid tripeptide(out) + H(+)(out) = an L-amino acid CC tripeptide(in) + H(+)(in); Xref=Rhea:RHEA:64400, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:155837; Evidence={ECO:0000269|PubMed:7896779, CC ECO:0000269|PubMed:9835627}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64401; CC Evidence={ECO:0000305|PubMed:7896779, ECO:0000305|PubMed:9835627}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-alanyl-L-lysine(out) + H(+)(out) = L-alanyl-L-lysine(in) + CC H(+)(in); Xref=Rhea:RHEA:72611, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:192470; Evidence={ECO:0000269|PubMed:8914574}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72612; CC Evidence={ECO:0000305|PubMed:8914574}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-alanyl-L-proline(out) + H(+)(out) = L-alanyl-L-proline(in) + CC H(+)(in); Xref=Rhea:RHEA:64420, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:155848; Evidence={ECO:0000269|PubMed:7896779}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64421; CC Evidence={ECO:0000305|PubMed:7896779}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-alanyl-L-valine(out) + H(+)(out) = L-alanyl-L-valine(in) + CC H(+)(in); Xref=Rhea:RHEA:72615, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:192471; Evidence={ECO:0000269|PubMed:8914574}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72616; CC Evidence={ECO:0000305|PubMed:8914574}; CC -!- CATALYTIC ACTIVITY: CC Reaction=carnosine(out) + H(+)(out) = carnosine(in) + H(+)(in); CC Xref=Rhea:RHEA:64404, ChEBI:CHEBI:15378, ChEBI:CHEBI:57485; CC Evidence={ECO:0000250|UniProtKB:P36836}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64405; CC Evidence={ECO:0000250|UniProtKB:P36836}; CC -!- CATALYTIC ACTIVITY: CC Reaction=glycyl-L-glutamine(out) + H(+)(out) = glycyl-L-glutamine(in) + CC H(+)(in); Xref=Rhea:RHEA:71671, ChEBI:CHEBI:15378, ChEBI:CHEBI:74392; CC Evidence={ECO:0000250|UniProtKB:P36836}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71672; CC Evidence={ECO:0000250|UniProtKB:P36836}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71673; CC Evidence={ECO:0000250|UniProtKB:P36836}; CC -!- CATALYTIC ACTIVITY: CC Reaction=glycyl-L-leucine(out) + H(+)(out) = glycyl-L-leucine(in) + CC H(+)(in); Xref=Rhea:RHEA:71675, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:143163; Evidence={ECO:0000250|UniProtKB:P36836}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71676; CC Evidence={ECO:0000250|UniProtKB:P36836}; CC -!- CATALYTIC ACTIVITY: CC Reaction=glycyl-L-proline(out) + H(+)(out) = glycyl-L-proline(in) + CC H(+)(in); Xref=Rhea:RHEA:64428, ChEBI:CHEBI:15378, ChEBI:CHEBI:73779; CC Evidence={ECO:0000269|PubMed:7896779}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64429; CC Evidence={ECO:0000305|PubMed:7896779}; CC -!- CATALYTIC ACTIVITY: CC Reaction=glycyl-sarcosine(out) + H(+)(out) = glycyl-sarcosine(in) + CC H(+)(in); Xref=Rhea:RHEA:64396, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:155838; Evidence={ECO:0000269|PubMed:15521010, CC ECO:0000269|PubMed:18367661, ECO:0000269|PubMed:19685173, CC ECO:0000269|PubMed:26320580, ECO:0000269|PubMed:7896779, CC ECO:0000269|PubMed:9835627}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64397; CC Evidence={ECO:0000305|PubMed:15521010, ECO:0000305|PubMed:18367661, CC ECO:0000305|PubMed:19685173, ECO:0000305|PubMed:26320580, CC ECO:0000305|PubMed:7896779, ECO:0000305|PubMed:9835627}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-leucyl-L-leucine(out) + H(+)(out) = L-leucyl-L-leucine(in) + CC H(+)(in); Xref=Rhea:RHEA:71715, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:191208; Evidence={ECO:0000250|UniProtKB:P36836}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71716; CC Evidence={ECO:0000250|UniProtKB:P36836}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-leucyl-L-proline(out) + H(+)(out) = L-leucyl-L-proline(in) + CC H(+)(in); Xref=Rhea:RHEA:64424, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:155847; Evidence={ECO:0000269|PubMed:7896779}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64425; CC Evidence={ECO:0000305|PubMed:7896779}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-phenylalanyl-L-leucine(out) + H(+)(out) = L-phenylalanyl-L- CC leucine(in) + H(+)(in); Xref=Rhea:RHEA:71699, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:190710; Evidence={ECO:0000250|UniProtKB:P36836}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71700; CC Evidence={ECO:0000250|UniProtKB:P36836}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-phenylalanyl-L-phenylalanine(out) + H(+)(out) = L- CC phenylalanyl-L-phenylalanine(in) + H(+)(in); Xref=Rhea:RHEA:71707, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:191205; CC Evidence={ECO:0000250|UniProtKB:P36836}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71708; CC Evidence={ECO:0000250|UniProtKB:P36836}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-lysyl-glycine(out) + H(+)(out) = L-lysyl-glycine(in) + CC H(+)(in); Xref=Rhea:RHEA:71679, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:191202; Evidence={ECO:0000250|UniProtKB:P36836}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71680; CC Evidence={ECO:0000250|UniProtKB:P36836}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71681; CC Evidence={ECO:0000250|UniProtKB:P36836}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-tyrosylglycine(out) + H(+)(out) = L-tyrosylglycine(in) + CC H(+)(in); Xref=Rhea:RHEA:71711, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:191210; Evidence={ECO:0000250|UniProtKB:P36836}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71712; CC Evidence={ECO:0000250|UniProtKB:P36836}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-alanyl-L-aspartate(out) + 2 H(+)(out) = L-alanyl-L- CC aspartate(in) + 2 H(+)(in); Xref=Rhea:RHEA:71695, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:74363; Evidence={ECO:0000250|UniProtKB:P36836, CC ECO:0000269|PubMed:8914574}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71696; CC Evidence={ECO:0000250|UniProtKB:P36836, ECO:0000305|PubMed:8914574}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-aspartyl-glycine(out) + 2 H(+)(out) = L-aspartyl-glycine(in) CC + 2 H(+)(in); Xref=Rhea:RHEA:71683, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:191203; Evidence={ECO:0000250|UniProtKB:P36836}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71684; CC Evidence={ECO:0000250|UniProtKB:P36836}; CC -!- CATALYTIC ACTIVITY: CC Reaction=glycyl-L-aspartate(out) + 2 H(+)(out) = glycyl-L-aspartate(in) CC + 2 H(+)(in); Xref=Rhea:RHEA:71687, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:191204; Evidence={ECO:0000250|UniProtKB:P36836}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71688; CC Evidence={ECO:0000250|UniProtKB:P36836}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:71689; CC Evidence={ECO:0000250|UniProtKB:P36836}; CC -!- CATALYTIC ACTIVITY: CC Reaction=glycyl-L-glutamate(out) + 2 H(+)(out) = glycyl-L-glutamate(in) CC + 2 H(+)(in); Xref=Rhea:RHEA:71691, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:73784; Evidence={ECO:0000250|UniProtKB:P36836}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71692; CC Evidence={ECO:0000250|UniProtKB:P36836}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-alanyl-L-leucyl-L-alanine(out) + H(+)(out) = L-alanyl-L- CC leucyl-L-alanine(in) + H(+)(in); Xref=Rhea:RHEA:71723, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:191212; CC Evidence={ECO:0000250|UniProtKB:P36836}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71724; CC Evidence={ECO:0000250|UniProtKB:P36836}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-alanyl-L-prolylglycine(out) + H(+)(out) = L-alanyl-L- CC prolylglycine(in) + H(+)(in); Xref=Rhea:RHEA:64432, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:155849; CC Evidence={ECO:0000269|PubMed:7896779}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64433; CC Evidence={ECO:0000305|PubMed:7896779}; CC -!- CATALYTIC ACTIVITY: CC Reaction=glycylglycyl-L-isoleucine(out) + H(+)(out) = glycylglycyl-L- CC isoleucine(in) + H(+)(in); Xref=Rhea:RHEA:64436, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:155850; Evidence={ECO:0000269|PubMed:7896779}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64437; CC Evidence={ECO:0000305|PubMed:7896779}; CC -!- CATALYTIC ACTIVITY: CC Reaction=glycylglycyl-L-proline(out) + H(+)(out) = glycylglycyl-L- CC proline(in) + H(+)(in); Xref=Rhea:RHEA:64440, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:155851; Evidence={ECO:0000269|PubMed:7896779}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64441; CC Evidence={ECO:0000305|PubMed:7896779}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-methionyl-L-phenylalanyl-L-methionine(out) + H(+)(out) = L- CC methionyl-L-phenylalanyl-L-methionine(in) + H(+)(in); CC Xref=Rhea:RHEA:71719, ChEBI:CHEBI:15378, ChEBI:CHEBI:191211; CC Evidence={ECO:0000250|UniProtKB:P36836}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71720; CC Evidence={ECO:0000250|UniProtKB:P36836}; CC -!- CATALYTIC ACTIVITY: CC Reaction=N-acetyl-D-muramoyl-L-alanyl-D-isoglutamine(out) + 2 H(+)(out) CC = N-acetyl-D-muramoyl-L-alanyl-D-isoglutamine(in) + 2 H(+)(in); CC Xref=Rhea:RHEA:64408, ChEBI:CHEBI:15378, ChEBI:CHEBI:155830; CC Evidence={ECO:0000269|PubMed:15521010}; CC -!- CATALYTIC ACTIVITY: CC Reaction=N(alpha)-formyl-L-methionyl-L-leucyl-L-phenylalanine(out) + 2 CC H(+)(out) = N(alpha)-formyl-L-methionyl-L-leucyl-L-phenylalanine(in) CC + 2 H(+)(in); Xref=Rhea:RHEA:75399, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:194314; Evidence={ECO:0000269|PubMed:9835627}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.78 mM for glycyl-sarcosine {ECO:0000269|PubMed:26320580}; CC -!- SUBUNIT: Interacts (via extracellular domain region) with trypsin. CC {ECO:0000250|UniProtKB:Q9JIP7}. CC -!- SUBCELLULAR LOCATION: Apical cell membrane CC {ECO:0000269|PubMed:28408210}; Multi-pass membrane protein CC {ECO:0000255}. Note=Localized to the apical membrane of enterocytes. CC {ECO:0000269|PubMed:28408210}. CC -!- TISSUE SPECIFICITY: Expressed in small intestine. CC {ECO:0000269|PubMed:28408210}. CC -!- DOMAIN: The extracellular domain (ECD) region specifically binds CC trypsin. {ECO:0000250|UniProtKB:Q9JIP7}. CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Proton- CC dependent oligopeptide transporter (POT/PTR) (TC 2.A.17) family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U13173; AAB61693.1; -; mRNA. DR EMBL; U21936; AAA63797.1; -; mRNA. DR EMBL; AL391670; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL353574; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC096328; AAH96328.1; -; mRNA. DR EMBL; BC096329; AAH96329.1; -; mRNA. DR CCDS; CCDS9489.1; -. DR PIR; A56163; A56163. DR RefSeq; NP_005064.1; NM_005073.4. DR PDB; 7PMW; EM; 4.10 A; A=1-708. DR PDB; 7PMX; EM; 3.50 A; A=1-708. DR PDB; 7PN1; EM; 3.90 A; A=1-708. DR PDBsum; 7PMW; -. DR PDBsum; 7PMX; -. DR PDBsum; 7PN1; -. DR AlphaFoldDB; P46059; -. DR EMDB; EMD-13542; -. DR EMDB; EMD-13543; -. DR EMDB; EMD-13545; -. DR SMR; P46059; -. DR BioGRID; 112452; 107. DR FunCoup; P46059; 200. DR IntAct; P46059; 106. DR STRING; 9606.ENSP00000365686; -. DR BindingDB; P46059; -. DR ChEMBL; CHEMBL4605; -. DR DrugBank; DB00855; Aminolevulinic acid. DR DrugBank; DB01060; Amoxicillin. DR DrugBank; DB00415; Ampicillin. DR DrugBank; DB08795; Azidocillin. DR DrugBank; DB00542; Benazepril. DR DrugBank; DB03793; Benzoic acid. DR DrugBank; DB01053; Benzylpenicillin. DR DrugBank; DB01197; Captopril. DR DrugBank; DB00833; Cefaclor. DR DrugBank; DB01140; Cefadroxil. DR DrugBank; DB00456; Cefalotin. DR DrugBank; DB00535; Cefdinir. DR DrugBank; DB01413; Cefepime. DR DrugBank; DB00671; Cefixime. DR DrugBank; DB00274; Cefmetazole. DR DrugBank; DB00493; Cefotaxime. DR DrugBank; DB01333; Cefradine. DR DrugBank; DB01415; Ceftibuten. DR DrugBank; DB01332; Ceftizoxime. DR DrugBank; DB01212; Ceftriaxone. DR DrugBank; DB01112; Cefuroxime. DR DrugBank; DB00567; Cephalexin. DR DrugBank; DB00672; Chlorpropamide. DR DrugBank; DB01340; Cilazapril. DR DrugBank; DB01147; Cloxacillin. DR DrugBank; DB01000; Cyclacillin. DR DrugBank; DB09213; Dexibuprofen. DR DrugBank; DB00485; Dicloxacillin. DR DrugBank; DB00584; Enalapril. DR DrugBank; DB01095; Fluvastatin. DR DrugBank; DB00492; Fosinopril. DR DrugBank; DB01016; Glyburide. DR DrugBank; DB01235; Levodopa. DR DrugBank; DB01255; Lisdexamfetamine. DR DrugBank; DB00722; Lisinopril. DR DrugBank; DB00447; Loracarbef. DR DrugBank; DB00563; Methotrexate. DR DrugBank; DB00968; Methyldopa. DR DrugBank; DB00211; Midodrine. DR DrugBank; DB00691; Moexipril. DR DrugBank; DB00731; Nateglinide. DR DrugBank; DB00198; Oseltamivir. DR DrugBank; DB00713; Oxacillin. DR DrugBank; DB00790; Perindopril. DR DrugBank; DB00417; Phenoxymethylpenicillin. DR DrugBank; DB00881; Quinapril. DR DrugBank; DB00178; Ramipril. DR DrugBank; DB01348; Spirapril. DR DrugBank; DB01956; Taurine. DR DrugBank; DB08836; Temocapril. DR DrugBank; DB01124; Tolbutamide. DR DrugBank; DB00519; Trandolapril. DR DrugBank; DB03424; Ubenimex. DR DrugBank; DB00577; Valaciclovir. DR DrugBank; DB01610; Valganciclovir. DR DrugCentral; P46059; -. DR GuidetoPHARMACOLOGY; 984; -. DR TCDB; 2.A.17.4.9; the proton-dependent oligopeptide transporter (pot/ptr) family. DR GlyCosmos; P46059; 7 sites, No reported glycans. DR GlyGen; P46059; 7 sites. DR iPTMnet; P46059; -. DR PhosphoSitePlus; P46059; -. DR BioMuta; SLC15A1; -. DR DMDM; 1172435; -. DR jPOST; P46059; -. DR MassIVE; P46059; -. DR PaxDb; 9606-ENSP00000365686; -. DR PeptideAtlas; P46059; -. DR ProteomicsDB; 55711; -. DR Antibodypedia; 10820; 214 antibodies from 31 providers. DR DNASU; 6564; -. DR Ensembl; ENST00000376503.10; ENSP00000365686.4; ENSG00000088386.18. DR GeneID; 6564; -. DR KEGG; hsa:6564; -. DR MANE-Select; ENST00000376503.10; ENSP00000365686.4; NM_005073.4; NP_005064.1. DR UCSC; uc001vno.4; human. DR AGR; HGNC:10920; -. DR ClinPGx; PA323; -. DR CTD; 6564; -. DR DisGeNET; 6564; -. DR GeneCards; SLC15A1; -. DR HGNC; HGNC:10920; SLC15A1. DR HPA; ENSG00000088386; Tissue enriched (intestine). DR MIM; 600544; gene. DR OpenTargets; ENSG00000088386; -. DR VEuPathDB; HostDB:ENSG00000088386; -. DR eggNOG; KOG1237; Eukaryota. DR GeneTree; ENSGT00940000155995; -. DR HOGENOM; CLU_004790_3_0_1; -. DR InParanoid; P46059; -. DR OMA; FMTFDAD; -. DR OrthoDB; 205993at2759; -. DR PAN-GO; P46059; 4 GO annotations based on evolutionary models. DR PhylomeDB; P46059; -. DR BRENDA; 7.4.2.9; 2681. DR PathwayCommons; P46059; -. DR Reactome; R-HSA-427975; Proton/oligopeptide cotransporters. DR SignaLink; P46059; -. DR BioGRID-ORCS; 6564; 11 hits in 1140 CRISPR screens. DR ChiTaRS; SLC15A1; human. DR GeneWiki; Peptide_transporter_1; -. DR GenomeRNAi; 6564; -. DR Pharos; P46059; Tchem. DR PRO; PR:P46059; -. DR Proteomes; UP000005640; Chromosome 13. DR RNAct; P46059; protein. DR Bgee; ENSG00000088386; Expressed in duodenum and 106 other cell types or tissues. DR ExpressionAtlas; P46059; baseline and differential. DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB. DR GO; GO:0005903; C:brush border; IEA:Ensembl. DR GO; GO:0016020; C:membrane; ISS:ARUK-UCL. DR GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL. DR GO; GO:0071916; F:dipeptide transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0015333; F:peptide:proton symporter activity; IDA:UniProtKB. DR GO; GO:0005427; F:proton-dependent oligopeptide secondary active transmembrane transporter activity; IEA:Ensembl. DR GO; GO:0042937; F:tripeptide transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0140206; P:dipeptide import across plasma membrane; IDA:UniProtKB. DR GO; GO:0035672; P:oligopeptide transmembrane transport; TAS:Reactome. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR GO; GO:0140207; P:tripeptide import across plasma membrane; ISS:ARUK-UCL. DR CDD; cd17412; MFS_SLC15A1; 1. DR FunFam; 1.20.1250.20:FF:000049; Solute carrier family 15 member 2; 1. DR FunFam; 1.20.1250.20:FF:000205; Solute carrier family 15 oligopeptide transporter member 1; 1. DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 2. DR InterPro; IPR036259; MFS_trans_sf. DR InterPro; IPR004768; Oligopep_transport. DR InterPro; IPR000109; POT_fam. DR InterPro; IPR018456; PTR2_symporter_CS. DR NCBIfam; TIGR00926; 2A1704; 1. DR PANTHER; PTHR11654; OLIGOPEPTIDE TRANSPORTER-RELATED; 1. DR Pfam; PF00854; PTR2; 2. DR SUPFAM; SSF103473; MFS general substrate transporter; 1. DR PROSITE; PS01022; PTR2_1; 1. DR PROSITE; PS01023; PTR2_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Glycoprotein; Membrane; Peptide transport; KW Protein transport; Proteomics identification; Reference proteome; Symport; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..708 FT /note="Solute carrier family 15 member 1" FT /id="PRO_0000064304" FT TRANSMEM 1..21 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 22..53 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 54..74 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 75..82 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 83..103 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 104..118 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 119..139 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 140..161 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 162..182 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 183..198 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 199..219 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 220..276 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 277..297 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 298..327 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 328..348 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 349..361 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 362..382 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 383..584 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 585..605 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 606..619 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 620..640 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 641..645 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 646..666 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 667..708 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REGION 383..584 FT /note="Extracellular domain (ECD)" FT /evidence="ECO:0000250|UniProtKB:Q9JIP7" FT CARBOHYD 50 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 404 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 408 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 439 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 509 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 514 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 562 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VARIANT 21 FT /note="V -> I (in dbSNP:rs8187818)" FT /evidence="ECO:0000269|PubMed:16258023" FT /id="VAR_029321" FT VARIANT 28 FT /note="F -> Y (in dbSNP:rs8187817)" FT /evidence="ECO:0000269|PubMed:16258023" FT /id="VAR_029322" FT VARIANT 117 FT /note="S -> N (in dbSNP:rs2297322)" FT /evidence="ECO:0000269|PubMed:12436193, FT ECO:0000269|PubMed:16258023" FT /id="VAR_022147" FT VARIANT 117 FT /note="S -> R (in dbSNP:rs8187821)" FT /evidence="ECO:0000269|PubMed:16258023" FT /id="VAR_029323" FT VARIANT 122 FT /note="V -> M (in dbSNP:rs8187820)" FT /evidence="ECO:0000269|PubMed:16258023" FT /id="VAR_020456" FT VARIANT 419 FT /note="G -> A (in dbSNP:rs4646227)" FT /evidence="ECO:0000269|PubMed:12436193, FT ECO:0000269|PubMed:16258023" FT /id="VAR_020457" FT VARIANT 450 FT /note="V -> I (in dbSNP:rs2274828)" FT /evidence="ECO:0000269|PubMed:16258023" FT /id="VAR_022148" FT VARIANT 451 FT /note="T -> N (in dbSNP:rs8187838)" FT /evidence="ECO:0000269|PubMed:16258023" FT /id="VAR_020458" FT VARIANT 459 FT /note="R -> C (in dbSNP:rs2274827)" FT /id="VAR_022149" FT VARIANT 537 FT /note="P -> S (in dbSNP:rs8187830)" FT /evidence="ECO:0000269|PubMed:16258023" FT /id="VAR_029324" FT MUTAGEN 573 FT /note="D->A: Does not affect peptide transporter activity." FT /evidence="ECO:0000269|PubMed:26320580" FT MUTAGEN 588 FT /note="Y->C: Reduced peptide transporter activity." FT /evidence="ECO:0000269|PubMed:19685173" FT MUTAGEN 594 FT /note="G->A: Does not affect peptide transporter activity." FT /evidence="ECO:0000269|PubMed:19685173" FT MUTAGEN 594 FT /note="G->C: Nearly abolished peptide transporter FT activity." FT /evidence="ECO:0000269|PubMed:19685173" FT MUTAGEN 594 FT /note="G->V: Abolished peptide transporter activity." FT /evidence="ECO:0000269|PubMed:19685173" FT MUTAGEN 595 FT /note="E->C: Nearly abolished peptide transporter FT activity." FT /evidence="ECO:0000269|PubMed:19685173" FT MUTAGEN 595 FT /note="E->D: Does not affect peptide transporter activity." FT /evidence="ECO:0000269|PubMed:19685173" FT MUTAGEN 595 FT /note="E->K,R: Abolished peptide transporter activity." FT /evidence="ECO:0000269|PubMed:19685173" FT HELIX 13..44 FT /evidence="ECO:0007829|PDB:7PMX" FT HELIX 51..55 FT /evidence="ECO:0007829|PDB:7PMX" FT STRAND 56..58 FT /evidence="ECO:0007829|PDB:7PMX" FT TURN 59..61 FT /evidence="ECO:0007829|PDB:7PMX" FT HELIX 62..65 FT /evidence="ECO:0007829|PDB:7PMX" FT HELIX 67..74 FT /evidence="ECO:0007829|PDB:7PMX" FT TURN 75..78 FT /evidence="ECO:0007829|PDB:7PMX" FT HELIX 79..107 FT /evidence="ECO:0007829|PDB:7PMX" FT HELIX 118..148 FT /evidence="ECO:0007829|PDB:7PMX" FT HELIX 156..184 FT /evidence="ECO:0007829|PDB:7PMX" FT HELIX 198..218 FT /evidence="ECO:0007829|PDB:7PMX" FT TURN 219..222 FT /evidence="ECO:0007829|PDB:7PMX" FT HELIX 232..248 FT /evidence="ECO:0007829|PDB:7PMX" FT HELIX 262..265 FT /evidence="ECO:0007829|PDB:7PMX" FT TURN 266..268 FT /evidence="ECO:0007829|PDB:7PMX" FT HELIX 271..285 FT /evidence="ECO:0007829|PDB:7PMX" FT HELIX 290..292 FT /evidence="ECO:0007829|PDB:7PMX" FT HELIX 293..297 FT /evidence="ECO:0007829|PDB:7PMX" FT HELIX 299..310 FT /evidence="ECO:0007829|PDB:7PMX" FT HELIX 322..324 FT /evidence="ECO:0007829|PDB:7PMX" FT HELIX 327..339 FT /evidence="ECO:0007829|PDB:7PMX" FT HELIX 340..344 FT /evidence="ECO:0007829|PDB:7PMX" FT HELIX 345..350 FT /evidence="ECO:0007829|PDB:7PMX" FT HELIX 357..383 FT /evidence="ECO:0007829|PDB:7PMX" FT STRAND 394..401 FT /evidence="ECO:0007829|PDB:7PMX" FT STRAND 403..405 FT /evidence="ECO:0007829|PDB:7PMX" FT STRAND 407..411 FT /evidence="ECO:0007829|PDB:7PMX" FT STRAND 414..418 FT /evidence="ECO:0007829|PDB:7PMX" FT STRAND 428..431 FT /evidence="ECO:0007829|PDB:7PMX" FT HELIX 432..434 FT /evidence="ECO:0007829|PDB:7PMX" FT STRAND 439..441 FT /evidence="ECO:0007829|PDB:7PMX" FT STRAND 458..466 FT /evidence="ECO:0007829|PDB:7PMX" FT STRAND 469..474 FT /evidence="ECO:0007829|PDB:7PMX" FT HELIX 482..484 FT /evidence="ECO:0007829|PDB:7PMX" FT STRAND 486..492 FT /evidence="ECO:0007829|PDB:7PMX" FT STRAND 494..496 FT /evidence="ECO:0007829|PDB:7PMX" FT STRAND 498..502 FT /evidence="ECO:0007829|PDB:7PMX" FT STRAND 505..510 FT /evidence="ECO:0007829|PDB:7PMX" FT HELIX 516..518 FT /evidence="ECO:0007829|PDB:7PMX" FT STRAND 519..521 FT /evidence="ECO:0007829|PDB:7PMX" FT STRAND 527..535 FT /evidence="ECO:0007829|PDB:7PMX" FT STRAND 542..544 FT /evidence="ECO:0007829|PDB:7PMX" FT STRAND 553..560 FT /evidence="ECO:0007829|PDB:7PMX" FT STRAND 566..574 FT /evidence="ECO:0007829|PDB:7PMX" FT HELIX 575..577 FT /evidence="ECO:0007829|PDB:7PMX" FT HELIX 581..584 FT /evidence="ECO:0007829|PDB:7PMX" FT HELIX 585..609 FT /evidence="ECO:0007829|PDB:7PMX" FT HELIX 615..636 FT /evidence="ECO:0007829|PDB:7PMX" FT HELIX 644..650 FT /evidence="ECO:0007829|PDB:7PMX" FT HELIX 653..657 FT /evidence="ECO:0007829|PDB:7PMX" FT HELIX 658..667 FT /evidence="ECO:0007829|PDB:7PMX" FT HELIX 671..673 FT /evidence="ECO:0007829|PDB:7PMX" FT HELIX 676..679 FT /evidence="ECO:0007829|PDB:7PMX" FT HELIX 680..682 FT /evidence="ECO:0007829|PDB:7PMX" SQ SEQUENCE 708 AA; 78806 MW; A75475789177A907 CRC64; MGMSKSHSFF GYPLSIFFIV VNEFCERFSY YGMRAILILY FTNFISWDDN LSTAIYHTFV ALCYLTPILG ALIADSWLGK FKTIVSLSIV YTIGQAVTSV SSINDLTDHN HDGTPDSLPV HVVLSLIGLA LIALGTGGIK PCVSAFGGDQ FEEGQEKQRN RFFSIFYLAI NAGSLLSTII TPMLRVQQCG IHSKQACYPL AFGVPAALMA VALIVFVLGS GMYKKFKPQG NIMGKVAKCI GFAIKNRFRH RSKAFPKREH WLDWAKEKYD ERLISQIKMV TRVMFLYIPL PMFWALFDQQ GSRWTLQATT MSGKIGALEI QPDQMQTVNA ILIVIMVPIF DAVLYPLIAK CGFNFTSLKK MAVGMVLASM AFVVAAIVQV EIDKTLPVFP KGNEVQIKVL NIGNNTMNIS LPGEMVTLGP MSQTNAFMTF DVNKLTRINI SSPGSPVTAV TDDFKQGQRH TLLVWAPNHY QVVKDGLNQK PEKGENGIRF VNTFNELITI TMSGKVYANI SSYNASTYQF FPSGIKGFTI SSTEIPPQCQ PNFNTFYLEF GSAYTYIVQR KNDSCPEVKV FEDISANTVN MALQIPQYFL LTCGEVVFSV TGLEFSYSQA PSNMKSVLQA GWLLTVAVGN IIVLIVAGAG QFSKQWAEYI LFAALLLVVC VIFAIMARFY TYINPAEIEA QFDEDEKKNR LEKSNPYFMS GANSQKQM //