A0A257R752 · A0A257R752_9GAMM

  • Protein
    Lysosomal dipeptide transporter MFSD1
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

Function

function

Lysosomal dipeptide uniporter that selectively exports lysine, arginine or histidine-containing dipeptides with a net positive charge from the lysosome lumen into the cytosol. Could play a role in a specific type of protein O-glycosylation indirectly regulating macrophages migration and tissue invasion. Also essential for liver homeostasis.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

  • L-alanyl-L-lysine(out) = L-alanyl-L-lysine(in)
  • L-alpha-aminoacyl-L-arginine(out) = L-alpha-aminoacyl-L-arginine(in)
  • L-alpha-aminoacyl-L-histidine(out) = L-alpha-aminoacyl-L-histidine(in)
  • L-alpha-aminoacyl-L-lysine(out) = L-alpha-aminoacyl-L-lysine(in)
  • L-arginyl-L-alpha-amino acid(out) = L-arginyl-L-alpha-amino acid(in)
  • L-arginyl-glycine(out) = L-arginyl-glycine(in)
  • L-aspartyl-L-lysine(out) = L-aspartyl-L-lysine(in)
  • L-histidyl-L-alpha-amino acid(out) = L-histidyl-L-alpha-amino acid(in)
  • L-histidyl-glycine(out) = L-histidyl-glycine(in)
  • L-lysyl-L-alanine(out) = L-lysyl-L-alanine(in)
  • L-lysyl-L-alpha-amino acid(out) = L-lysyl-L-alpha-amino acid(in)
  • L-lysyl-L-lysine(out) = L-lysyl-L-lysine(in)
  • L-lysyl-glycine(out) = L-lysyl-glycine(in)

GO annotations

AspectTerm
Cellular Componentlysosomal membrane
Molecular Functiontransmembrane transporter activity

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Lysosomal dipeptide transporter MFSD1
  • Alternative names
    • Major facilitator superfamily domain-containing protein 1

Gene names

    • ORF names
      B7X00_00465

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • 21-45-4
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Legionellales > Legionellaceae > Legionella

Accessions

  • Primary accession
    A0A257R752

Proteomes

Subcellular Location

Lysosome membrane
; Multi-pass membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane12-34Helical
Transmembrane46-65Helical
Transmembrane85-102Helical
Transmembrane114-132Helical
Transmembrane139-157Helical
Transmembrane169-193Helical
Transmembrane214-240Helical
Transmembrane260-282Helical
Transmembrane289-308Helical
Transmembrane314-338Helical
Transmembrane350-373Helical
Transmembrane393-414Helical

Keywords

Interaction

Subunit

Homodimer. Interacts with lysosomal protein GLMP (via lumenal domain); the interaction starts while both proteins are still in the endoplasmic reticulum and is required for stabilization of MFSD1 in lysosomes but has no direct effect on its targeting to lysosomes or transporter activity.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain15-419Major facilitator superfamily (MFS) profile

Sequence similarities

Belongs to the major facilitator superfamily.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    423
  • Mass (Da)
    46,663
  • Last updated
    2017-11-22 v1
  • Checksum
    1E7103B6A49DBD2C
MRTPIEHSQKRLLWGIVACVMGAFFYCYEFVLRIVPGALQSELCEAFGNISAATFGQIAAMYYFAYSPMQFPVGMLMDRFGPRRLLTFACLCCTLGSTIFGYSNSLLVVSFGRFLVGLGSSFAFVGVLSLALHWLPRRYFSLVTGLVTTLAMLGVVYGEVKITELTVRFGLHEVLGLLVLIGAVLSGLIFLMVKDGSDSHPVHSDSISVFLRQVWQVLISSEVWLIGFVGACLYTSLSVFGELWGKSYLEQAHHLNKIDAARAISMMFLGWAVGAPIAGFLSDWSARRVLPIVIGALMSFICISTILYCQNLSFFMLNLLLFFYGVFSGTEIIVFIMAKENTRSLVSGTVFAAVNMIVSLVGAIFQPLIGFLLDMFGNGRVLGEEHFYAAHDYQLALSIIPLSLLMVILLSFFLKDADSRHDA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
NCAV01000030
EMBL· GenBank· DDBJ
OYV55926.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help