ID T0RG20_SAPDV Unreviewed; 521 AA. AC T0RG20; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 27-NOV-2024, entry version 35. DE RecName: Full=Lysosomal dipeptide transporter MFSD1 {ECO:0000256|ARBA:ARBA00044985}; DE AltName: Full=Major facilitator superfamily domain-containing protein 1 {ECO:0000256|ARBA:ARBA00045018}; GN ORFNames=SDRG_11151 {ECO:0000313|EMBL:EQC31228.1}; OS Saprolegnia diclina (strain VS20). OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae; OC Saprolegnia. OX NCBI_TaxID=1156394 {ECO:0000313|EMBL:EQC31228.1, ECO:0000313|Proteomes:UP000030762}; RN [1] {ECO:0000313|EMBL:EQC31228.1, ECO:0000313|Proteomes:UP000030762} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VS20 {ECO:0000313|EMBL:EQC31228.1, RC ECO:0000313|Proteomes:UP000030762}; RG The Broad Institute Genome Sequencing Platform; RA Russ C., Nusbaum C., Tyler B., van West P., Dieguez-Uribeondo J., RA de Bruijn I., Tripathy S., Jiang R., Young S.K., Zeng Q., Gargeya S., RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., RA Berlin A., Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M., RA Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A., Murphy C., RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., RA Sykes S., Wortman J., Nusbaum C., Birren B.; RT "The Genome Sequence of Saprolegnia declina VS20."; RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Lysosomal dipeptide uniporter that selectively exports CC lysine, arginine or histidine-containing dipeptides with a net positive CC charge from the lysosome lumen into the cytosol. Could play a role in a CC specific type of protein O-glycosylation indirectly regulating CC macrophages migration and tissue invasion. Also essential for liver CC homeostasis. {ECO:0000256|ARBA:ARBA00045709}. CC -!- CATALYTIC ACTIVITY: CC Reaction=L-alanyl-L-lysine(out) = L-alanyl-L-lysine(in); CC Xref=Rhea:RHEA:79415, ChEBI:CHEBI:192470; CC Evidence={ECO:0000256|ARBA:ARBA00044919}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-alpha-aminoacyl-L-arginine(out) = L-alpha-aminoacyl-L- CC arginine(in); Xref=Rhea:RHEA:79367, ChEBI:CHEBI:229968; CC Evidence={ECO:0000256|ARBA:ARBA00044881}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-alpha-aminoacyl-L-histidine(out) = L-alpha-aminoacyl-L- CC histidine(in); Xref=Rhea:RHEA:79375, ChEBI:CHEBI:229967; CC Evidence={ECO:0000256|ARBA:ARBA00044884}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-alpha-aminoacyl-L-lysine(out) = L-alpha-aminoacyl-L- CC lysine(in); Xref=Rhea:RHEA:79383, ChEBI:CHEBI:229966; CC Evidence={ECO:0000256|ARBA:ARBA00044893}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-arginyl-L-alpha-amino acid(out) = L-arginyl-L-alpha-amino CC acid(in); Xref=Rhea:RHEA:79371, ChEBI:CHEBI:84315; CC Evidence={ECO:0000256|ARBA:ARBA00044899}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-arginyl-glycine(out) = L-arginyl-glycine(in); CC Xref=Rhea:RHEA:79391, ChEBI:CHEBI:229955; CC Evidence={ECO:0000256|ARBA:ARBA00044903}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-aspartyl-L-lysine(out) = L-aspartyl-L-lysine(in); CC Xref=Rhea:RHEA:79411, ChEBI:CHEBI:229953; CC Evidence={ECO:0000256|ARBA:ARBA00044898}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-histidyl-L-alpha-amino acid(out) = L-histidyl-L-alpha-amino CC acid(in); Xref=Rhea:RHEA:79379, ChEBI:CHEBI:229964; CC Evidence={ECO:0000256|ARBA:ARBA00044912}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-histidyl-glycine(out) = L-histidyl-glycine(in); CC Xref=Rhea:RHEA:79395, ChEBI:CHEBI:229957; CC Evidence={ECO:0000256|ARBA:ARBA00044878}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-lysyl-L-alanine(out) = L-lysyl-L-alanine(in); CC Xref=Rhea:RHEA:79399, ChEBI:CHEBI:229954; CC Evidence={ECO:0000256|ARBA:ARBA00044876}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-lysyl-L-alpha-amino acid(out) = L-lysyl-L-alpha-amino CC acid(in); Xref=Rhea:RHEA:79387, ChEBI:CHEBI:229965; CC Evidence={ECO:0000256|ARBA:ARBA00044891}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-lysyl-L-lysine(out) = L-lysyl-L-lysine(in); CC Xref=Rhea:RHEA:79403, ChEBI:CHEBI:229956; CC Evidence={ECO:0000256|ARBA:ARBA00044900}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-lysyl-glycine(out) = L-lysyl-glycine(in); CC Xref=Rhea:RHEA:79407, ChEBI:CHEBI:191202; CC Evidence={ECO:0000256|ARBA:ARBA00044924}; CC -!- SUBUNIT: Homodimer. Interacts with lysosomal protein GLMP (via lumenal CC domain); the interaction starts while both proteins are still in the CC endoplasmic reticulum and is required for stabilization of MFSD1 in CC lysosomes but has no direct effect on its targeting to lysosomes or CC transporter activity. {ECO:0000256|ARBA:ARBA00046376}. CC -!- SUBCELLULAR LOCATION: Lysosome membrane CC {ECO:0000256|ARBA:ARBA00004155}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004155}. CC -!- SIMILARITY: Belongs to the major facilitator superfamily. CC {ECO:0000256|ARBA:ARBA00008335}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; JH767170; EQC31228.1; -; Genomic_DNA. DR RefSeq; XP_008615401.1; XM_008617179.1. DR AlphaFoldDB; T0RG20; -. DR STRING; 1156394.T0RG20; -. DR EnsemblProtists; EQC31228; EQC31228; SDRG_11151. DR GeneID; 19951878; -. DR VEuPathDB; FungiDB:SDRG_11151; -. DR eggNOG; KOG4686; Eukaryota. DR InParanoid; T0RG20; -. DR OMA; WGGAVLC; -. DR OrthoDB; 1387029at2759; -. DR Proteomes; UP000030762; Unassembled WGS sequence. DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell. DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro. DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 2. DR InterPro; IPR011701; MFS. DR InterPro; IPR020846; MFS_dom. DR InterPro; IPR036259; MFS_trans_sf. DR InterPro; IPR052187; MFSD1. DR PANTHER; PTHR23512; MAJOR FACILITATOR SUPERFAMILY DOMAIN-CONTAINING PROTEIN 1; 1. DR PANTHER; PTHR23512:SF3; MAJOR FACILITATOR SUPERFAMILY DOMAIN-CONTAINING PROTEIN 1; 1. DR Pfam; PF07690; MFS_1; 2. DR SUPFAM; SSF103473; MFS general substrate transporter; 2. DR PROSITE; PS50850; MFS; 1. PE 3: Inferred from homology; KW Lysosome {ECO:0000256|ARBA:ARBA00023228}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000030762}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}. FT SIGNAL 1..25 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 26..521 FT /note="Lysosomal dipeptide transporter MFSD1" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5004583952" FT TRANSMEM 57..75 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 82..101 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 107..127 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 165..194 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 221..241 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 373..394 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 401..423 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 435..455 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 467..489 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..494 FT /note="Major facilitator superfamily (MFS) profile" FT /evidence="ECO:0000259|PROSITE:PS50850" SQ SEQUENCE 521 AA; 56006 MW; 7F3DB9B0C88D5612 CRC64; MRGSAWQRRS VLALSSLFVL GSTYCYDNPG ALKTQLQQHF GRTIPRAEFE VYFNLSYSLY SVPNVLLPFF GGVLIDTYGV SFMALVLASL ILAGQVVTAL GSSFENIYLL LAGRVLFGLG GETMWVAQTT FVTHWFSPME LGFAIGINNC VATLGTLLND VLSPWIAAAF DVTFALWVGS FVCVFSLCAT ILLVRLESTL PFERASPAAP VRLWDLRRFS LGFWLIAVLY IVINACTGPF ANVAGSVLLE RNYFIEPPID CRRCGLGAYL NHTCETLAPS CPMSPPFAWP LPQLAANCSI VSAFDQFKCK KGPPYLQDDQ INCDATAWRH GPLTHIYCSK KIDATAKATA MMAITPLVSA VFSPLSGSLV DGLGARASLG LVADVAIAAG HVLVRYTTSD VALALTLSGI GQSLFAAAMW SAIPFVVPPR YVSTAFGAIT SLSNVGLATV PLIVAHVYSR QQHYLPSVAN VFVVLSACGV VLGLCLLVAD ATVLRRALSR REVAEASAST EQLLDASDRD L //