S15A3_MOUSE
ID S15A3_MOUSE Reviewed; 578 AA.
AC Q8BPX9; Q9WU80;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Solute carrier family 15 member 3 {ECO:0000305};
DE AltName: Full=Peptide transporter 3 {ECO:0000250|UniProtKB:Q8IY34};
DE AltName: Full=Peptide/histidine transporter 2 {ECO:0000250|UniProtKB:Q8IY34};
DE AltName: Full=cAMP-inducible gene 1 protein {ECO:0000303|PubMed:11004510};
GN Name=Slc15a3 {ECO:0000303|PubMed:24695226, ECO:0000312|MGI:MGI:1929691};
GN Synonyms=Ci1 {ECO:0000303|PubMed:11004510},
GN Pht2 {ECO:0000250|UniProtKB:Q8IY34};
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], AND TISSUE SPECIFICITY.
RX PubMed=11004510; DOI=10.1016/s0167-4781(00)00133-0;
RA Takahashi Y., Miyata M., Zheng P., Imazato T., Horwitz A., Smith J.D.;
RT "Identification of cAMP analogue inducible genes in RAW264 macrophages.";
RL Biochim. Biophys. Acta 1492:385-394(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Eye;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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, TRANSPORTER ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=24695226; DOI=10.1038/nature13133;
RA Nakamura N., Lill J.R., Phung Q., Jiang Z., Bakalarski C., de Maziere A.,
RA Klumperman J., Schlatter M., Delamarre L., Mellman I.;
RT "Endosomes are specialized platforms for bacterial sensing and NOD2
RT signalling.";
RL Nature 509:240-244(2014).
CC -!- FUNCTION: Proton-coupled amino-acid transporter that transports free
CC histidine and certain di- and tripeptides, and is involved in innate
CC immune response (PubMed:24695226). Also able to transport carnosine (By
CC similarity). Involved in the detection of microbial pathogens by toll-
CC like receptors (TLRs) and NOD-like receptors (NLRs), probably by
CC mediating transport of bacterial peptidoglycans across the
CC endolysosomal membrane: catalyzes the transport of certain bacterial
CC peptidoglycans, such as muramyl dipeptide (MDP), the NOD2 ligand
CC (PubMed:24695226). {ECO:0000250|UniProtKB:Q8IY34,
CC ECO:0000269|PubMed:24695226}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(out) + L-histidine(out) = H(+)(in) + L-histidine(in);
CC Xref=Rhea:RHEA:37047, ChEBI:CHEBI:15378, ChEBI:CHEBI:57595;
CC Evidence={ECO:0000250|UniProtKB:Q924V4};
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:Q924V4};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64393;
CC Evidence={ECO:0000250|UniProtKB:Q924V4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(out) + N-acetylmuramyl-L-alanyl-D-isoglutamine(out) =
CC H(+)(in) + N-acetylmuramyl-L-alanyl-D-isoglutamine(in);
CC Xref=Rhea:RHEA:64408, ChEBI:CHEBI:15378, ChEBI:CHEBI:155830;
CC Evidence={ECO:0000269|PubMed:24695226};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64409;
CC Evidence={ECO:0000269|PubMed:24695226};
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:Q8IY34};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64405;
CC Evidence={ECO:0000250|UniProtKB:Q8IY34};
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:24695226};
CC Multi-pass membrane protein {ECO:0000255}. Endosome membrane
CC {ECO:0000269|PubMed:24695226}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed highly in bone marrow derived
CC macrophages, and weakly in spleen and lung (PubMed:11004510). Expressed
CC in plasmacytoid dendritic cells (pDCs) in response to toll-like
CC receptors (TLR) stimulation (PubMed:24695226).
CC {ECO:0000269|PubMed:11004510, ECO:0000269|PubMed:24695226}.
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; AF121080; AAD24570.1; -; mRNA.
DR EMBL; AK051941; BAC34816.1; -; mRNA.
DR EMBL; BC051940; AAH51940.1; -; mRNA.
DR CCDS; CCDS29588.1; -.
DR RefSeq; NP_075531.2; NM_023044.2.
DR AlphaFoldDB; Q8BPX9; -.
DR SMR; Q8BPX9; -.
DR BioGRID; 211140; 3.
DR STRING; 10090.ENSMUSP00000025646; -.
DR GlyGen; Q8BPX9; 3 sites.
DR iPTMnet; Q8BPX9; -.
DR PhosphoSitePlus; Q8BPX9; -.
DR SwissPalm; Q8BPX9; -.
DR MaxQB; Q8BPX9; -.
DR PaxDb; Q8BPX9; -.
DR PeptideAtlas; Q8BPX9; -.
DR PRIDE; Q8BPX9; -.
DR ProteomicsDB; 260969; -.
DR Antibodypedia; 50766; 103 antibodies from 16 providers.
DR DNASU; 65221; -.
DR Ensembl; ENSMUST00000025646; ENSMUSP00000025646; ENSMUSG00000024737.
DR GeneID; 65221; -.
DR KEGG; mmu:65221; -.
DR UCSC; uc008gra.2; mouse.
DR CTD; 51296; -.
DR MGI; MGI:1929691; Slc15a3.
DR VEuPathDB; HostDB:ENSMUSG00000024737; -.
DR eggNOG; KOG1237; Eukaryota.
DR GeneTree; ENSGT00940000161889; -.
DR HOGENOM; CLU_009313_6_1_1; -.
DR InParanoid; Q8BPX9; -.
DR OMA; FPPINRI; -.
DR OrthoDB; 365203at2759; -.
DR PhylomeDB; Q8BPX9; -.
DR TreeFam; TF330897; -.
DR Reactome; R-MMU-427975; Proton/oligopeptide cotransporters.
DR BioGRID-ORCS; 65221; 2 hits in 74 CRISPR screens.
DR PRO; PR:Q8BPX9; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q8BPX9; protein.
DR Bgee; ENSMUSG00000024737; Expressed in granulocyte and 75 other tissues.
DR Genevisible; Q8BPX9; MM.
DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0071916; F:dipeptide transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0015647; F:peptidoglycan transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0140206; P:dipeptide import across plasma membrane; ISS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0015835; P:peptidoglycan transport; IDA:UniProtKB.
DR GO; GO:0070434; P:positive regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway; IDA:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR000109; POT_fam.
DR InterPro; IPR018456; PTR2_symporter_CS.
DR PANTHER; PTHR11654; PTHR11654; 1.
DR Pfam; PF00854; PTR2; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS01023; PTR2_2; 1.
PE 2: Evidence at transcript level;
KW Endosome; Glycoprotein; Immunity; Innate immunity; Lysosome; Membrane;
KW Peptide transport; Protein transport; Reference proteome; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..578
FT /note="Solute carrier family 15 member 3"
FT /id="PRO_0000295913"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 308..328
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 367..387
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 405..425
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 462..481
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 494..514
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 538..558
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 436
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 277
FT /note="R -> K (in Ref. 1; AAD24570)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 578 AA; 64051 MW; 048B0A511245B399 CRC64;
MSAPRAEEQP SRSGERQPLV ARGPRGPRRW RRTAAAAVLL VQMLERAAFF GVTSNLVLYL
NSLNFNWDGQ QASRATLLFL GASYLLAPVG GWLADVYLGR FLTISLSLLL YLAASGLLLT
TITNDGRRSF CGEMPELPLE PACPSSSCQG SWSSPYCATT LYLVLLLLAL AASSVRSTLT
SFGADQVMDL GRDATRRFFN WFYWSINLGA ILSLLVVAFI EQNISFLWGY SIIVGLVGLA
FFIFLFATPV FITKPPTGSQ VSSMLKLAFQ NCCPCRRSSS RDSESAHLLP DQRSNQPGPS
PQEDMANFQV LVKILPVMVT LVPYWMVYFQ MQSTYVLQGL HLHIPNIFRT NPNISLLLRS
DSSNYRIPEA WLLLANVAVI LILIPVKDHL IDPLLLRCKL LPSSLQKMAL GMFFGFTSII
VAGVLEKERL QYIAANQTVP QLIGKDLYYA APLSIWWQIP QYLLIGVSEI FASIPGLEFA
YSEAPRSMQG AIMGIFFCLS GVGSLLGSGL VALLSFPGGW MYCPKDFGNI NNCQMDRYFF
LLAGIEAVTA VLFLWIAGRY ERTRQDPASQ RSSSRVRG
