D3ZJ25
uniprot
D3ZJ25
canonical
activity_regulation
ACTIVITY REGULATION: Down-regulated at acidic pH. {ECO:0000269|PubMed:10698697}.
uniprot
proteins
amino_acid_sequence
MAVDPPKADPKGVVAVDPTANCGSGLKSREDQGAKAGGCCSSRDQVCRCLRANLLVLLTVAAAVAGVVLGLGVSAAGGAEALGHARFTAFAFPGELLLRLLEMIILPLVVCSLIGGAASLDPSALGRLGAWALLFFLVTTLLSSALGVALALALKPGAAFAAINSSVVDSSVHRAPTKEVLDSFLELLRNMFPSNLVSASAAFRIFATSYVSKDINTSGIHPCGACPQRSNATMDQPHCEMKMNILGLVVFAIVFGVALRKLGPEGELLIRFFNSFNDATMVLVSWIMWYAPIGILFLVAGKIVEMKDIRQLFIGLGKYIVCCLLGHAIHGLLVLPLIYFLFTRKNPYRFLWGIVTPLATAFGTSSSSATLPLMMKCVEEKNGVAKHISRFILPIGATVNMDGAALFQCVAAVFIAQLNGMSLDFVKIITILVTATASSVGAAGIPAGGVLTLAIILEAISLPVKDISLILAVDWLVDRSCTVLNVEGDAFGAGLLQSYVDRTKMPSSEPELIQVKNDVSLKPLPLATEEGNPLLKQCREPSGDSSATCEKESVM
uniprot
proteins
function
FUNCTION: Sodium-coupled antiporter of neutral amino acids. In a tri-substrate transport cycle, exchanges neutral amino acids between the extracellular and intracellular compartments, coupled to the inward cotransport of at least one sodium ion (By similarity) (PubMed:10698697). The preferred substrate is the essential amino acid L-glutamine, a precursor for biosynthesis of proteins, nucleotides and amine sugars as well as an alternative fuel for mitochondrial oxidative phosphorylation. Exchanges L-glutamine with other neutral amino acids such as L-serine, L-threonine and L-asparagine in a bidirectional way. Provides L-glutamine to proliferating stem and activated cells driving the metabolic switch toward cell differentiation (By similarity). The transport cycle is usually pH-independent, with the exception of L-glutamate. Transports extracellular L-glutamate coupled to the cotransport of one proton and one sodium ion in exchange for intracellular L-glutamine counter-ion. May provide for L-glutamate uptake in glial cells regulating glutamine/glutamate cycle in the nervous system (By similarity). Part of transport systems for D-amino acids. Mediates D-serine release from the retinal glia potentially affecting NMDA receptor function in retinal neurons. May contribute to D-serine reabsorption at the brush border of renal proximal tubules thus modulating the dynamics of urinary versus blood D-serine levels (By similarity). Displays sodium- and amino acid-dependent but uncoupled channel-like anion conductance with a preference SCN(-) >> NO3(-) > I(-) > Cl(-) (PubMed:10698697). Through binding of the fusogenic protein syncytin-1/ERVW-1 may mediate trophoblasts syncytialization, the spontaneous fusion of their plasma membranes, an essential process in placental development (By similarity). {ECO:0000250|UniProtKB:Q15758, ECO:0000269|PubMed:10698697}.
uniprot
proteins
mass_dalton
58477
uniprot
proteins
protein_family
Dicarboxylate/amino acid:cation symporter (DAACS) (TC 2.A.23) family
uniprot
proteins
pubmed
10698697
uniprot
proteins
pubmed
15057822
uniprot
proteins
sequence_length
555
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q15758}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:P51912}; Multi-pass membrane protein {ECO:0000255}. Melanosome {ECO:0000250|UniProtKB:Q15758}. Note=Restricted to the apical cell membrane of proximal tubule epithelial cells. {ECO:0000250|UniProtKB:P51912}.
uniprot
proteins
transmembrane_region
TRANSMEM 53..82; /note="Helical; Name=1"; /evidence="ECO:0000250|UniProtKB:P43003"; TRANSMEM 96..117; /note="Helical; Name=2"; /evidence="ECO:0000250|UniProtKB:P43003"; TRANSMEM 132..154; /note="Helical; Name=3"; /evidence="ECO:0000250|UniProtKB:P43003"; TRANSMEM 240..262; /note="Helical; Name=4"; /evidence="ECO:0000250|UniProtKB:P43003"; TRANSMEM 272..299; /note="Helical; Name=5"; /evidence="ECO:0000250|UniProtKB:P43003"; TRANSMEM 321..342; /note="Helical; Name=6"; /evidence="ECO:0000250|UniProtKB:P43003"; TRANSMEM 388..414; /note="Helical; Name=7"; /evidence="ECO:0000250|UniProtKB:P43003"; TRANSMEM 475..496; /note="Helical; Name=8"; /evidence="ECO:0000250|UniProtKB:P43003
uniprot
proteins