ID   Q80XC0_MOUSE            Unreviewed;       259 AA.
AC   Q80XC0; E9Q329;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 113.
DE   RecName: Full=Solute carrier family 15 member 2 {ECO:0000256|ARBA:ARBA00041092};
DE   AltName: Full=Peptide transporter 2 {ECO:0000256|ARBA:ARBA00042838};
GN   Name=Slc15a2 {ECO:0000313|EMBL:AAH51199.1,
GN   ECO:0000313|Ensembl:ENSMUSP00000132029.3,
GN   ECO:0000313|MGI:MGI:1890457};
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 {ECO:0000313|EMBL:AAH51199.1};
RN   [1] {ECO:0000313|EMBL:AAH51199.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary gland {ECO:0000313|EMBL:AAH51199.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RA   Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA   Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA   Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA   Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA   Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA   Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA   Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA   Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA   Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA   Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA   Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA   Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA   Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA   Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA   Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA   Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA   Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA   Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA   Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
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   [2] {ECO:0000313|Ensembl:ENSMUSP00000132029.3, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000132029.3,
RC   ECO:0000313|Proteomes:UP000000589};
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] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   [4] {ECO:0000313|Ensembl:ENSMUSP00000132029.3}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000132029.3};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+)(out) + L-alanyl-L-alanine(out) = 2 H(+)(in) + L-alanyl-
CC         L-alanine(in); Xref=Rhea:RHEA:76183, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:195181; Evidence={ECO:0000256|ARBA:ARBA00036666};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76184;
CC         Evidence={ECO:0000256|ARBA:ARBA00036666};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3 H(+)(out) + N-acetyl-D-muramoyl-L-alanyl-D-isoglutamine(out)
CC         = 3 H(+)(in) + N-acetyl-D-muramoyl-L-alanyl-D-isoglutamine(in);
CC         Xref=Rhea:RHEA:76375, ChEBI:CHEBI:15378, ChEBI:CHEBI:155830;
CC         Evidence={ECO:0000256|ARBA:ARBA00036457};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76376;
CC         Evidence={ECO:0000256|ARBA:ARBA00036457};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a dipeptide(out) + 2 H(+)(out) = a dipeptide(in) + 2 H(+)(in);
CC         Xref=Rhea:RHEA:76179, ChEBI:CHEBI:15378, ChEBI:CHEBI:90799;
CC         Evidence={ECO:0000256|ARBA:ARBA00036620};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76180;
CC         Evidence={ECO:0000256|ARBA:ARBA00036620};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an L-amino acid tripeptide(out) + 2 H(+)(out) = an L-amino
CC         acid tripeptide(in) + 2 H(+)(in); Xref=Rhea:RHEA:76187,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:155837;
CC         Evidence={ECO:0000256|ARBA:ARBA00035821};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76188;
CC         Evidence={ECO:0000256|ARBA:ARBA00035821};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=carnosine(out) + 2 H(+)(out) = carnosine(in) + 2 H(+)(in);
CC         Xref=Rhea:RHEA:76191, ChEBI:CHEBI:15378, ChEBI:CHEBI:57485;
CC         Evidence={ECO:0000256|ARBA:ARBA00036391};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76192;
CC         Evidence={ECO:0000256|ARBA:ARBA00036391};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycyl-L-glutamate(out) + 3 H(+)(out) = glycyl-L-glutamate(in)
CC         + 3 H(+)(in); Xref=Rhea:RHEA:76175, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:73784; Evidence={ECO:0000256|ARBA:ARBA00036032};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76176;
CC         Evidence={ECO:0000256|ARBA:ARBA00036032};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycyl-L-leucine(out) + 2 H(+)(out) = glycyl-L-leucine + 2
CC         H(+)(in); Xref=Rhea:RHEA:76167, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:143163; Evidence={ECO:0000256|ARBA:ARBA00036955};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76168;
CC         Evidence={ECO:0000256|ARBA:ARBA00036955};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycyl-L-lysine(out) + 2 H(+)(out) = glycyl-L-lysine(in) + 2
CC         H(+)(in); Xref=Rhea:RHEA:76171, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:194323; Evidence={ECO:0000256|ARBA:ARBA00035916};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:76172;
CC         Evidence={ECO:0000256|ARBA:ARBA00035916};
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000256|ARBA:ARBA00004424}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004424}. Cell membrane
CC       {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004651}. Cytoplasmic vesicle, phagosome
CC       membrane {ECO:0000256|ARBA:ARBA00004265}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004265}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003755}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141,
CC       ECO:0000256|RuleBase:RU003755}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. Proton-
CC       dependent oligopeptide transporter (POT/PTR) (TC 2.A.17) family.
CC       {ECO:0000256|ARBA:ARBA00005982, ECO:0000256|RuleBase:RU003755}.
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DR   EMBL; BC051199; AAH51199.1; -; mRNA.
DR   RefSeq; NP_001139371.1; NM_001145899.1.
DR   ProteomicsDB; 348781; -.
DR   Antibodypedia; 32862; 98 antibodies from 22 providers.
DR   DNASU; 57738; -.
DR   Ensembl; ENSMUST00000164579.9; ENSMUSP00000132029.3; ENSMUSG00000022899.11.
DR   GeneID; 57738; -.
DR   KEGG; mmu:57738; -.
DR   UCSC; uc012afh.1; mouse.
DR   AGR; MGI:1890457; -.
DR   CTD; 6565; -.
DR   MGI; MGI:1890457; Slc15a2.
DR   VEuPathDB; HostDB:ENSMUSG00000022899; -.
DR   GeneTree; ENSGT00940000156507; -.
DR   OrthoDB; 930761at2759; -.
DR   BioGRID-ORCS; 57738; 2 hits in 78 CRISPR screens.
DR   ChiTaRS; Slc15a2; mouse.
DR   Proteomes; UP000000589; Chromosome 16.
DR   Bgee; ENSMUSG00000022899; Expressed in epithelium of lens and 233 other cell types or tissues.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0006857; P:oligopeptide transport; IEA:InterPro.
DR   Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   InterPro; IPR000109; POT_fam.
DR   InterPro; IPR018456; PTR2_symporter_CS.
DR   PANTHER; PTHR11654; OLIGOPEPTIDE TRANSPORTER-RELATED; 1.
DR   PANTHER; PTHR11654:SF603; SOLUTE CARRIER FAMILY 15 MEMBER 2; 1.
DR   Pfam; PF00854; PTR2; 1.
DR   SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR   PROSITE; PS01022; PTR2_1; 1.
DR   PROSITE; PS01023; PTR2_2; 1.
DR   Genevisible; E9Q329; MM.
PE   1: Evidence at protein level;
KW   Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Immunity {ECO:0000256|ARBA:ARBA00022859};
KW   Innate immunity {ECO:0000256|ARBA:ARBA00022588};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Peptide transport {ECO:0000256|ARBA:ARBA00022856};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW   Proteomics identification {ECO:0007829|MaxQB:Q80XC0,
KW   ECO:0007829|ProteomicsDB:Q80XC0};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW   Symport {ECO:0000256|ARBA:ARBA00022847};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU003755};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003755}.
FT   TRANSMEM        69..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        99..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        126..148
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        154..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        196..216
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        228..246
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..27
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   259 AA;  28452 MW;  A785D4A1B6213A06 CRC64;
     MLEERESKEP AMNPFQKNES KETLFSPVST EEMLPGPPSP PKKSTPKLFG SSYPLSIAFI
     VVNEFCERFS YYGMKAVLTL YFLYFLHWNE DTSTSVYHAF SSLCYFTPIL GAAIADSWLG
     KFKTIIYLSL VYVLGHVFKS LGAIPILGGK MLHTILSLVG LSLIALGTGG IKPCVAAFGG
     DQFEEEHAEA RTRYFSVFYL SINAGSLIST FITPMLRGDV KCFGEDCYAL AFGIPGLLMV
     LALGEWSGKG CEQPLIPAT
//