S15A3_RAT
ID S15A3_RAT Reviewed; 582 AA.
AC Q924V4;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Solute carrier family 15 member 3;
DE AltName: Full=Peptide transporter 3;
DE AltName: Full=Peptide/histidine transporter 2 {ECO:0000303|PubMed:11336635};
GN Name=Slc15a3; Synonyms=Pht2 {ECO:0000303|PubMed:11336635};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TRANSPORTER ACTIVITY, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11336635; DOI=10.1042/0264-6021:3560053;
RA Sakata K., Yamashita T., Maeda M., Moriyama Y., Shimada S., Tohyama M.;
RT "Cloning of a lymphatic peptide/histidine transporter.";
RL Biochem. J. 356:53-60(2001).
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:11336635). 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 (By
CC similarity). {ECO:0000250|UniProtKB:Q8BPX9,
CC ECO:0000250|UniProtKB:Q8IY34, ECO:0000269|PubMed:11336635}.
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:0000305|PubMed:11336635};
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:11336635};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64393;
CC Evidence={ECO:0000269|PubMed:11336635};
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:0000250|UniProtKB:Q8BPX9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64409;
CC Evidence={ECO:0000250|UniProtKB:Q8BPX9};
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:11336635};
CC Multi-pass membrane protein {ECO:0000255}. Endosome membrane
CC {ECO:0000250|UniProtKB:Q8BPX9}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Abundant expression in lung, spleen and thymus, and
CC detected faintly in brain, liver, adrenal gland and heart at protein
CC level. {ECO:0000269|PubMed:11336635}.
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; AB026665; BAB43942.1; -; mRNA.
DR RefSeq; NP_647557.1; NM_139341.1.
DR RefSeq; XP_017444273.1; XM_017588784.1.
DR AlphaFoldDB; Q924V4; -.
DR SMR; Q924V4; -.
DR STRING; 10116.ENSRNOP00000034275; -.
DR GlyGen; Q924V4; 5 sites.
DR PaxDb; Q924V4; -.
DR Ensembl; ENSRNOT00000029443; ENSRNOP00000034275; ENSRNOG00000021644.
DR GeneID; 246239; -.
DR KEGG; rno:246239; -.
DR UCSC; RGD:628663; rat.
DR CTD; 51296; -.
DR RGD; 628663; Slc15a3.
DR eggNOG; KOG1237; Eukaryota.
DR GeneTree; ENSGT00940000161889; -.
DR HOGENOM; CLU_009313_6_1_1; -.
DR InParanoid; Q924V4; -.
DR OMA; FPPINRI; -.
DR OrthoDB; 365203at2759; -.
DR PhylomeDB; Q924V4; -.
DR TreeFam; TF330897; -.
DR Reactome; R-RNO-427975; Proton/oligopeptide cotransporters.
DR PRO; PR:Q924V4; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000021644; Expressed in thymus and 18 other tissues.
DR Genevisible; Q924V4; RN.
DR GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005765; C:lysosomal membrane; IDA:RGD.
DR GO; GO:0071916; F:dipeptide transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0015647; F:peptidoglycan transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0005427; F:proton-dependent oligopeptide secondary active transmembrane transporter activity; TAS:RGD.
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; ISS:UniProtKB.
DR GO; GO:0070434; P:positive regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway; ISS:UniProtKB.
DR GO; GO:0030163; P:protein catabolic process; NAS:RGD.
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..582
FT /note="Solute carrier family 15 member 3"
FT /id="PRO_0000295914"
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 312..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 371..391
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 409..429
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 466..485
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 498..518
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 541..561
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 357
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 440
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 575
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 582 AA; 64593 MW; 6E317638D95BE5FC CRC64;
MSALRAEQQP SRSGERQPLV AQGRWGPRRW RRTAAAAVLL VEMLERAAFF GVTSNLVLYL
NSLNFNWDGE HASRATLLFL GASYLLAPVG GWLADVYLGR FLAISLSLLL YLAATGLLLT
TITDDGRRSF CGEMPELPLK PACPSANCQG SWSSPYCATT LYLVLLLLAL AASSVRSNLT
SFGADQVMDL GRDATRRFFN WFYWSINLGA ILSLLVVAFI EQNISFLQGY SIIVGLVGLA
FFIFLIATPV FITKPPTGSQ VSSMLNLAFQ NCCPGWQWWR RPSSRNSEGA HLLPDQRSNQ
PGPSPQEDMA NFQVLLKVLP VMVTLVPYWM VYFQMQSTYV LQGLHLHIPN IFRTNPNISL
PLRSDSSNYR IPEAWLLLAN VAVILILVPV KDHLIDPLLL RCKLLPSALQ KMALGMFFGF
TSIIVAGVLE KERLQYIAAN QTVPQLIGKD LYYAAPLSIW WQIPQYLLIG ISEIFASIPG
LEFAYSEAPR SMQGAIMGIF FCLSGVGSLL GSGLVALLSL PGGWMYCPKD FGNINNCRMD
LYFFLLAGIQ AVTAVLFLWI AGRYERTRQD PDSQNSTSRV RG
