ID   S15A1_MOUSE             Reviewed;         709 AA.
AC   Q9JIP7; E9QMX3;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   24-JAN-2024, entry version 144.
DE   RecName: Full=Solute carrier family 15 member 1 {ECO:0000305};
DE   AltName: Full=Intestinal H(+)/peptide cotransporter {ECO:0000303|PubMed:11004485};
DE   AltName: Full=Oligopeptide transporter, small intestine isoform {ECO:0000303|PubMed:11004485};
DE   AltName: Full=Peptide transporter 1 {ECO:0000303|PubMed:11004485};
DE   AltName: Full=Proton-coupled dipeptide cotransporter;
GN   Name=Slc15a1 {ECO:0000312|MGI:MGI:1861376};
GN   Synonyms=Pept1 {ECO:0000303|PubMed:11004485};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TRANSPORTER ACTIVITY.
RC   STRAIN=129/SvJ;
RX   PubMed=11004485; DOI=10.1016/s0167-4781(00)00101-9;
RA   Fei Y.-J., Sugawara M., Liu J.-C., Li H.W., Ganapathy V., Ganapathy M.E.,
RA   Leibach F.H.;
RT   "cDNA structure, genomic organization, and promoter analysis of the mouse
RT   intestinal peptide transporter PEPT1.";
RL   Biochim. Biophys. Acta 1492:145-154(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-439 AND ASN-515.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-linked
RT   cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [5] {ECO:0007744|PDB:5A9D}
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 391-579, DOMAIN, INTERACTION WITH
RP   TRYPSIN, AND MUTAGENESIS OF 453-HIS--GLU-456; 472-ARG--LYS-475; ASP-476;
RP   GLU-509; ASN-515; ASP-550 AND GLU-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).
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 (PubMed:11004485) (By
CC       similarity). Primarily responsible for the absorption of dietary
CC       di- and tripeptides from the small intestinal lumen (By similarity).
CC       Mediates transepithelial transport of muramyl and N-formylated
CC       bacterial dipeptides contributing to recognition of pathogenic bacteria
CC       by the mucosal immune system (By similarity).
CC       {ECO:0000250|UniProtKB:P36836, ECO:0000250|UniProtKB:P46059,
CC       ECO:0000269|PubMed:11004485, ECO:0000269|PubMed:26320580}.
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:0000250|UniProtKB:P46059};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64393;
CC         Evidence={ECO:0000250|UniProtKB:P46059};
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:0000250|UniProtKB:P46059};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64401;
CC         Evidence={ECO:0000250|UniProtKB:P46059};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+)(out) + L-alanyl-L-lysine(out) = H(+)(in) + L-alanyl-L-
CC         lysine(in); Xref=Rhea:RHEA:72611, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:192470; Evidence={ECO:0000250|UniProtKB:P46059};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72612;
CC         Evidence={ECO:0000250|UniProtKB:P46059};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+)(out) + L-alanyl-L-proline(out) = H(+)(in) + L-alanyl-L-
CC         proline(in); Xref=Rhea:RHEA:64420, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:155848; Evidence={ECO:0000250|UniProtKB:P46059};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64421;
CC         Evidence={ECO:0000250|UniProtKB:P46059};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+)(out) + L-alanyl-L-valine(out) = H(+)(in) + L-alanyl-L-
CC         valine(in); Xref=Rhea:RHEA:72615, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:192471; Evidence={ECO:0000250|UniProtKB:P46059};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72616;
CC         Evidence={ECO:0000250|UniProtKB:P36836};
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:0000250|UniProtKB:P46059};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64429;
CC         Evidence={ECO:0000250|UniProtKB:P46059};
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:11004485};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64397;
CC         Evidence={ECO:0000305|PubMed:11004485};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+)(out) + L-leucyl-L-leucine(out) = H(+)(in) + L-leucyl-L-
CC         leucine(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=H(+)(out) + L-leucyl-L-proline(out) = H(+)(in) + L-leucyl-L-
CC         proline(in); Xref=Rhea:RHEA:64424, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:155847; Evidence={ECO:0000250|UniProtKB:P46059};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64425;
CC         Evidence={ECO:0000250|UniProtKB:P46059};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+)(out) + L-phenylalanyl-L-leucine(out) = H(+)(in) + L-
CC         phenylalanyl-L-leucine(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=H(+)(out) + L-phenylalanyl-L-phenylalanine(out) = H(+)(in) +
CC         L-phenylalanyl-L-phenylalanine(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=H(+)(out) + L-lysyl-glycine(out) = H(+)(in) + L-lysyl-
CC         glycine(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=H(+)(out) + L-tyrosylglycine(out) = H(+)(in) + L-
CC         tyrosylglycine(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=2 H(+)(out) + L-alanyl-L-aspartate(out) = 2 H(+)(in) + L-
CC         alanyl-L-aspartate(in); Xref=Rhea:RHEA:71695, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:74363; Evidence={ECO:0000250|UniProtKB:P36836,
CC         ECO:0000250|UniProtKB:P46059};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71696;
CC         Evidence={ECO:0000250|UniProtKB:P36836,
CC         ECO:0000250|UniProtKB:P46059};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+)(out) + L-aspartyl-glycine(out) = 2 H(+)(in) + L-
CC         aspartyl-glycine(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=H(+)(out) + L-alanyl-L-leucyl-L-alanine(out) = H(+)(in) + L-
CC         alanyl-L-leucyl-L-alanine(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=H(+)(out) + L-alanyl-L-prolylglycine(out) = H(+)(in) + L-
CC         alanyl-L-prolylglycine(in); Xref=Rhea:RHEA:64432, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:155849; Evidence={ECO:0000250|UniProtKB:P46059};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64433;
CC         Evidence={ECO:0000250|UniProtKB:P46059};
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:0000250|UniProtKB:P46059};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64437;
CC         Evidence={ECO:0000250|UniProtKB:P46059};
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:0000250|UniProtKB:P46059};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64441;
CC         Evidence={ECO:0000250|UniProtKB:P46059};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+)(out) + L-methionyl-L-phenylalanyl-L-methionine(out) =
CC         H(+)(in) + L-methionyl-L-phenylalanyl-L-methionine(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=2 H(+)(out) + N-acetyl-D-muramoyl-L-alanyl-D-isoglutamine(out)
CC         = 2 H(+)(in) + N-acetyl-D-muramoyl-L-alanyl-D-isoglutamine(in);
CC         Xref=Rhea:RHEA:64408, ChEBI:CHEBI:15378, ChEBI:CHEBI:155830;
CC         Evidence={ECO:0000250|UniProtKB:P46059};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+)(out) + N-formyl-L-methionyl-L-leucyl-L-
CC         phenylalanine(out) = 2 H(+)(in) + N-formyl-L-methionyl-L-leucyl-L-
CC         phenylalanine(in); Xref=Rhea:RHEA:75399, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:194314; Evidence={ECO:0000250|UniProtKB:P46059};
CC   -!- SUBUNIT: Interacts (via extracellular domain region) with trypsin.
CC       {ECO:0000269|PubMed:26320580}.
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000250|UniProtKB:P46059}; Multi-pass membrane protein
CC       {ECO:0000255}. Note=Localized to the apical membrane of enterocytes.
CC       {ECO:0000250|UniProtKB:P46059}.
CC   -!- DOMAIN: The extracellular domain (ECD) region specifically binds
CC       trypsin. {ECO:0000269|PubMed:26320580}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. Proton-
CC       dependent oligopeptide transporter (POT/PTR) (TC 2.A.17) family.
CC       {ECO:0000305}.
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DR   EMBL; AF205540; AAF81666.1; -; mRNA.
DR   EMBL; AC126253; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC154618; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS37017.1; -.
DR   RefSeq; NP_444309.2; NM_053079.2.
DR   PDB; 5A9D; X-ray; 2.10 A; A/B=391-579.
DR   PDBsum; 5A9D; -.
DR   AlphaFoldDB; Q9JIP7; -.
DR   SMR; Q9JIP7; -.
DR   IntAct; Q9JIP7; 1.
DR   STRING; 10090.ENSMUSP00000085728; -.
DR   BindingDB; Q9JIP7; -.
DR   ChEMBL; CHEMBL2073714; -.
DR   GlyCosmos; Q9JIP7; 5 sites, No reported glycans.
DR   GlyGen; Q9JIP7; 6 sites.
DR   iPTMnet; Q9JIP7; -.
DR   PhosphoSitePlus; Q9JIP7; -.
DR   MaxQB; Q9JIP7; -.
DR   PaxDb; 10090-ENSMUSP00000085728; -.
DR   ProteomicsDB; 253351; -.
DR   Antibodypedia; 10820; 273 antibodies from 31 providers.
DR   DNASU; 56643; -.
DR   Ensembl; ENSMUST00000088386.8; ENSMUSP00000085728.7; ENSMUSG00000025557.11.
DR   GeneID; 56643; -.
DR   KEGG; mmu:56643; -.
DR   UCSC; uc007vad.1; mouse.
DR   AGR; MGI:1861376; -.
DR   CTD; 6564; -.
DR   MGI; MGI:1861376; Slc15a1.
DR   VEuPathDB; HostDB:ENSMUSG00000025557; -.
DR   eggNOG; KOG1237; Eukaryota.
DR   GeneTree; ENSGT00940000155995; -.
DR   HOGENOM; CLU_004790_3_0_1; -.
DR   InParanoid; Q9JIP7; -.
DR   OMA; FMTFDAD; -.
DR   OrthoDB; 930761at2759; -.
DR   PhylomeDB; Q9JIP7; -.
DR   TreeFam; TF330897; -.
DR   BRENDA; 7.4.2.5; 3474.
DR   Reactome; R-MMU-427975; Proton/oligopeptide cotransporters.
DR   BioGRID-ORCS; 56643; 1 hit in 76 CRISPR screens.
DR   PRO; PR:Q9JIP7; -.
DR   Proteomes; UP000000589; Chromosome 14.
DR   RNAct; Q9JIP7; Protein.
DR   Bgee; ENSMUSG00000025557; Expressed in epithelium of small intestine and 48 other cell types or tissues.
DR   GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR   GO; GO:0005903; C:brush border; IDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0016248; F:channel inhibitor activity; ISO:MGI.
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; IDA:MGI.
DR   GO; GO:0042937; F:tripeptide transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0140206; P:dipeptide import across plasma membrane; IDA:UniProtKB.
DR   GO; GO:0051956; P:negative regulation of amino acid transport; ISO:MGI.
DR   GO; GO:0006857; P:oligopeptide transport; IDA:MGI.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   CDD; cd17412; MFS_SLC15A1; 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   PANTHER; PTHR11654:SF89; SOLUTE CARRIER FAMILY 15 MEMBER 1; 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.
DR   Genevisible; Q9JIP7; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Glycoprotein; Membrane; Peptide transport;
KW   Protein transport; Reference proteome; Symport; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..709
FT                   /note="Solute carrier family 15 member 1"
FT                   /id="PRO_0000064305"
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..585
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        586..606
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        607..620
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        621..641
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        642..646
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        647..667
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        668..709
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          383..585
FT                   /note="Extracellular domain (ECD)"
FT                   /evidence="ECO:0000303|PubMed:26320580"
FT   REGION          690..709
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        50
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        406
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        439
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973"
FT   CARBOHYD        515
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19349973"
FT   CARBOHYD        532
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         453..456
FT                   /note="HDFE->AAFA,ERFR: Does not affect trypsin-binding."
FT                   /evidence="ECO:0000269|PubMed:26320580"
FT   MUTAGEN         472..475
FT                   /note="RVVK->AVVA,EVVE: Does not affect trypsin-binding."
FT                   /evidence="ECO:0000269|PubMed:26320580"
FT   MUTAGEN         476
FT                   /note="D->A: Does not affect trypsin-binding."
FT                   /evidence="ECO:0000269|PubMed:26320580"
FT   MUTAGEN         509
FT                   /note="E->R: Does not affect trypsin-binding."
FT                   /evidence="ECO:0000269|PubMed:26320580"
FT   MUTAGEN         515
FT                   /note="N->A: Does not affect trypsin-binding."
FT                   /evidence="ECO:0000269|PubMed:26320580"
FT   MUTAGEN         550
FT                   /note="D->A: Reduced trypsin-binding; when associated with
FT                   A-573."
FT                   /evidence="ECO:0000269|PubMed:26320580"
FT   MUTAGEN         573
FT                   /note="E->A: Reduced trypsin-binding; when associated with
FT                   A-550."
FT                   /evidence="ECO:0000269|PubMed:26320580"
FT   CONFLICT        287
FT                   /note="Y -> F (in Ref. 1; AAF81666)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        295
FT                   /note="A -> G (in Ref. 1; AAF81666)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        318
FT                   /note="I -> N (in Ref. 1; AAF81666)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        333..339
FT                   /note="IVIMVPI -> NVNNGPN (in Ref. 1; AAF81666)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        346..347
FT                   /note="PL -> RS (in Ref. 1; AAF81666)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        462
FT                   /note="T -> N (in Ref. 1; AAF81666)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        467
FT                   /note="N -> E (in Ref. 1; AAF81666)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        478
FT                   /note="L -> P (in Ref. 1; AAF81666)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        501
FT                   /note="I -> N (in Ref. 1; AAF81666)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        510..511
FT                   /note="NV -> KF (in Ref. 1; AAF81666)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        520..522
FT                   /note="QFF -> KFL (in Ref. 1; AAF81666)"
FT                   /evidence="ECO:0000305"
FT   STRAND          393..401
FT                   /evidence="ECO:0007829|PDB:5A9D"
FT   STRAND          403..405
FT                   /evidence="ECO:0007829|PDB:5A9D"
FT   STRAND          407..411
FT                   /evidence="ECO:0007829|PDB:5A9D"
FT   STRAND          414..418
FT                   /evidence="ECO:0007829|PDB:5A9D"
FT   STRAND          428..431
FT                   /evidence="ECO:0007829|PDB:5A9D"
FT   HELIX           432..434
FT                   /evidence="ECO:0007829|PDB:5A9D"
FT   STRAND          439..444
FT                   /evidence="ECO:0007829|PDB:5A9D"
FT   STRAND          448..450
FT                   /evidence="ECO:0007829|PDB:5A9D"
FT   STRAND          459..466
FT                   /evidence="ECO:0007829|PDB:5A9D"
FT   TURN            467..469
FT                   /evidence="ECO:0007829|PDB:5A9D"
FT   STRAND          470..480
FT                   /evidence="ECO:0007829|PDB:5A9D"
FT   STRAND          487..493
FT                   /evidence="ECO:0007829|PDB:5A9D"
FT   STRAND          495..497
FT                   /evidence="ECO:0007829|PDB:5A9D"
FT   STRAND          499..503
FT                   /evidence="ECO:0007829|PDB:5A9D"
FT   STRAND          506..511
FT                   /evidence="ECO:0007829|PDB:5A9D"
FT   STRAND          520..522
FT                   /evidence="ECO:0007829|PDB:5A9D"
FT   STRAND          528..532
FT                   /evidence="ECO:0007829|PDB:5A9D"
FT   STRAND          534..536
FT                   /evidence="ECO:0007829|PDB:5A9D"
FT   STRAND          543..545
FT                   /evidence="ECO:0007829|PDB:5A9D"
FT   STRAND          554..561
FT                   /evidence="ECO:0007829|PDB:5A9D"
FT   STRAND          565..574
FT                   /evidence="ECO:0007829|PDB:5A9D"
SQ   SEQUENCE   709 AA;  78560 MW;  7DF0D0F9068CD046 CRC64;
     MGMSKSRGCF GYPLSIFFIV VNEFCERFSY YGMRALLVLY FRNFLGWDDN LSTAIYHTFV
     ALCYLTPILG ALIADSWLGK FKTIVSLSIV YTIGQAVISV SSINDLTDHD HNGSPDSLPV
     HVALSMVGLA LIALGTGGIK PCVSAFGGDQ FEEGQEKQRN RFFSIFYLAI NGGSLLSTII
     TPILRVQQCG IHSQQACYPL AFGVPAALMA VALIVFVLGS GMYKKFQPQG NIMGKVAKCI
     GFAIKNRFRH RSKAYPKREH WLDWAKEKYD ERLISQIKMV TKVMFLYIPL PMFWALFDQQ
     GSRWTLQATT MNGKIGAIEI QPDQMQTVNA ILIVIMVPIV DAVVYPLIAK CGFNFTSLKK
     MTVGMFLASM AFVVAAIVQV EIDKTLPVFP GGNQVQIKVL NIGNNNMTVH FPGNSVTLAQ
     MSQTDTFMTF DIDKLTSINI SSSGSPGVTT VAHDFEQGHR HTLLVWNPSQ YRVVKDGLNQ
     KPEKGENGIR FVNTLNEMVT IKMSGKVYEN VTSHNASGYQ FFPSGEKQYT INTTAVAPTC
     LTDFKSSNLD FGSAYTYVIR RASDGCLEVK EFEDIPPNTV NMALQIPQYF LLTCGEVVFS
     VTGLEFSYSQ APSNMKSVLQ AGWLLTVAVG NIIVLIVAGA GHFPKQWAEY ILFASLLLVV
     CVIFAIMARF YTYINPAEIE AQFDEDEKKK GIGKENPYSS LEPVSQTNM
//