S15A4_XENLA
ID S15A4_XENLA Reviewed; 569 AA.
AC Q68F72;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Solute carrier family 15 member 4 {ECO:0000305};
GN Name=slc15a4 {ECO:0000250|UniProtKB:Q8N697};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Proton-coupled amino-acid transporter that mediates the
CC transmembrane transport of L-histidine and some di- and tripeptides
CC from inside the lysosome to the cytosol, and plays a key role in innate
CC immune response. Able to transport a variety of di- and tripeptides,
CC including carnosine and some peptidoglycans (By similarity).
CC Transporter activity is pH-dependent and maximized in the acidic
CC lysosomal environment (By similarity). {ECO:0000250|UniProtKB:O09014,
CC ECO:0000250|UniProtKB:Q8N697}.
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:Q8N697};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37048;
CC Evidence={ECO:0000250|UniProtKB:Q8N697};
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:Q8N697};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64393;
CC Evidence={ECO:0000250|UniProtKB:Q8N697};
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:Q8N697};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64401;
CC Evidence={ECO:0000250|UniProtKB:Q8N697};
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:Q8N697};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64409;
CC Evidence={ECO:0000250|UniProtKB:Q8N697};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(out) + L-alanyl-gamma-D-glutamyl-meso-
CC diaminoheptanedioate(out) = H(+)(in) + L-alanyl-gamma-D-glutamyl-
CC meso-diaminoheptanedioate(in); Xref=Rhea:RHEA:64412,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:61401;
CC Evidence={ECO:0000250|UniProtKB:Q8N697};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64413;
CC Evidence={ECO:0000250|UniProtKB:Q8N697};
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:0000250|UniProtKB:Q8N697};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64397;
CC Evidence={ECO:0000250|UniProtKB:Q8N697};
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:Q8N697};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64405;
CC Evidence={ECO:0000250|UniProtKB:Q8N697};
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q8N697};
CC Multi-pass membrane protein {ECO:0000255}. Endosome membrane
CC {ECO:0000250|UniProtKB:Q8N697}; Multi-pass membrane protein
CC {ECO:0000255}. Early endosome membrane {ECO:0000250|UniProtKB:Q91W98};
CC Multi-pass membrane protein {ECO:0000255}.
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; BC079971; AAH79971.1; -; mRNA.
DR RefSeq; NP_001087468.1; NM_001093999.1.
DR AlphaFoldDB; Q68F72; -.
DR SMR; Q68F72; -.
DR PRIDE; Q68F72; -.
DR DNASU; 447292; -.
DR GeneID; 447292; -.
DR KEGG; xla:447292; -.
DR CTD; 447292; -.
DR Xenbase; XB-GENE-986488; slc15a4.L.
DR OrthoDB; 365203at2759; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 447292; Expressed in egg cell and 19 other tissues.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0036020; C:endolysosome membrane; ISS:UniProtKB.
DR GO; GO:1905103; C:integral component of lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0071916; F:dipeptide transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0005290; F:L-histidine transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0015333; F:peptide:proton symporter activity; ISS:UniProtKB.
DR GO; GO:0015647; F:peptidoglycan transmembrane transporter activity; ISS:UniProtKB.
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:0033023; P:mast cell homeostasis; ISS:UniProtKB.
DR GO; GO:0015835; P:peptidoglycan transport; ISS:UniProtKB.
DR GO; GO:0045089; P:positive regulation of innate immune response; ISS:UniProtKB.
DR GO; GO:0070430; P:positive regulation of nucleotide-binding oligomerization domain containing 1 signaling pathway; ISS:UniProtKB.
DR GO; GO:0070434; P:positive regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway; ISS:UniProtKB.
DR GO; GO:0034157; P:positive regulation of toll-like receptor 7 signaling pathway; ISS:UniProtKB.
DR GO; GO:0034161; P:positive regulation of toll-like receptor 8 signaling pathway; ISS:UniProtKB.
DR GO; GO:0034165; P:positive regulation of toll-like receptor 9 signaling pathway; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0048302; P:regulation of isotype switching to IgG isotypes; ISS:UniProtKB.
DR GO; GO:0070424; P:regulation of nucleotide-binding oligomerization domain containing signaling pathway; ISS:UniProtKB.
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; Immunity; Innate immunity; Lysosome; Membrane; Peptide transport;
KW Phosphoprotein; Protein transport; Reference proteome; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..569
FT /note="Solute carrier family 15 member 4"
FT /id="PRO_0000338602"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 364..384
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 460..480
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 488..508
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 536..556
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 569 AA; 63087 MW; C75ADF6C5970F689 CRC64;
MASRDPSERS PLLGGRSEPP VPAGSVFSGR GLACAAVLLS ELLERVAFYG ITSNLVLFLN
GQIFGWEGTQ ASQALLLFMG ITYLVSPFAG WLADALLGRF YVILGSMVLY LLGMLLFPMV
SYSGTRTAFC GDIQWAQIEN CSRSNASSDD TCPEPSRRYC APALFLGLII VGLGVGSVKA
NITPFGADQV KDRGPEATRR FFNWFYWSIN LGAIISLGGV AYVQQNVEFL IGYIIPAVCI
GVSFLVFLCG KTVFVTKPAD GSAFTDMVKI LAYFCCSRKH TRENTRNIQN NQHRHKQSRL
DMAKASHGGP FREDKVEDVK ALVKIIPVFL ALIPYWTVYF QMQTTYVLQS LHLRIPQIFN
NNHTLPAAWL TMFDAVLILI LIPLKDKLVD PFLKKRGLLP SPLKRIAVGM FFVMCSVLAA
GILESERLEI VKRDKIQQQI GNVTYYAANL TVWWQLPQYI LIGISEIFAS IAGLEFAYSA
APKSMQSVIM GLFFFFSGIG SFVGSGLLAL VSIPQIGWMS NHSDLGNING CTLNYYFFLL
AAVQAATLLL FLIISVKYER QQSKTYRRL
