ID A0A2P4WXP4_9STRA Unreviewed; 246 AA. AC A0A2P4WXP4; DT 23-MAY-2018, integrated into UniProtKB/TrEMBL. DT 23-MAY-2018, sequence version 1. DT 27-NOV-2024, entry version 21. 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}; DE Flags: Fragment; GN ORFNames=PHPALM_37358 {ECO:0000313|EMBL:POM58049.1}; OS Phytophthora palmivora. OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae; OC Phytophthora. OX NCBI_TaxID=4796 {ECO:0000313|EMBL:POM58049.1, ECO:0000313|Proteomes:UP000237271}; RN [1] {ECO:0000313|EMBL:POM58049.1, ECO:0000313|Proteomes:UP000237271} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=sbr112.9 {ECO:0000313|Proteomes:UP000237271}; RX PubMed=28186564; RA Ali S.S., Shao J., Lary D.J., Kronmiller B., Shen D., Strem M.D., RA Amoako-Attah I., Akrofi A.Y., Begoude B.A., Ten Hoopen G.M., Coulibaly K., RA Kebe B.I., Melnick R.L., Guiltinan M.J., Tyler B.M., Meinhardt L.W., RA Bailey B.A.; RT "Phytophthora megakarya and P. palmivora, closely related causal agents of RT cacao black pod rot, underwent increases in genome sizes and gene numbers RT by different mechanisms."; RL Genome Biol. Evol. 9:536-557(2017). 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:POM58049.1}. 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; NCKW01020383; POM58049.1; -; Genomic_DNA. DR AlphaFoldDB; A0A2P4WXP4; -. DR OrthoDB; 73329at2759; -. DR Proteomes; UP000237271; 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; 1. 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; 1. DR SUPFAM; SSF103473; MFS general substrate transporter; 1. 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:UP000237271}; 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 TRANSMEM 55..72 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 92..112 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 124..141 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 147..172 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 184..211 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 217..240 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 54..246 FT /note="Major facilitator superfamily (MFS) profile" FT /evidence="ECO:0000259|PROSITE:PS50850" FT REGION 1..34 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 246 FT /evidence="ECO:0000313|EMBL:POM58049.1" SQ SEQUENCE 246 AA; 26971 MW; 5B88BEA1D0054AD2 CRC64; MAPKQKESTD PSELTPLVYD ASPNGDGGAL TPPRSPLQRA PVWQFWRTTS PPHRFYLLLL MSFIPFGGHF VKNGMSSLEQ LMLDDPDFPI TNTMYGALLS AVSVPNMFLP LLGGRLLDKS GHRSIRFFLA WICVGQAIFA IGMELKLYWL ALFGRVFFGV GEGSVVVGAR VFIASWFRNK ELTFAMGVSV AVTNVSKMLA KATVAPIALY FGGYVQALWY GVAVCVASAL VGVLVCHYTL NLKRIV //