P51912
uniprot
P51912
canonical
activity_regulation
ACTIVITY REGULATION: Down-regulated at acidic pH, with the exception of L-glutamate transport which is up-regulated instead. {ECO:0000269|PubMed:8662767}.
uniprot
proteins
amino_acid_sequence
MAVDPPKADPKGVAVDSSRRCPALGSREDQSAKAGGCCGSRDRVRRCIRANLLVLLTVAAVVAGVGLGLGVSAAGGADALGPARLTRFAFPGELLLRLLKMIILPLVVCSLIGGAASLDPSALGRVGAWALLFFLVTTLLASALGVGLALALKPGAAVTAITSINDSVVDPCARSAPTKEALDSFLDLVRNIFPSNLVSAAFRSFATSYEPKDNSCKIPQSCIQREINSTMVQLLCEVEGMNILGLVVFAIVFGVALRKLGPEGELLIRFFNSFNDATMVLVSWIMWYAPVGILFLVASKIVEMKDVRQLFISLGKYILCCLLGHAIHGLLVLPLIYFLFTRKNPYRFLWGIMTPLATAFGTSSSSATLPLMMKCVEEKNGVAKHISRFILPIGATVNMDGAALFQCVAAVFIAQLNGVSLDFVKIITILVTATASSVGAAGIPAGGVLTLAIILEAVSLPVKDISLILAVDWLVDRSCTVLNVEGDAFGAGLLQSYVDRTKMPSSEPELIQVKNEVSLNPLPLATEEGNPLLKQYQGPTGDSSATFEKESVM
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:7702599, PubMed:8662767). 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 (By similarity). 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 (Probable). Displays sodium- and amino acid-dependent but uncoupled channel-like anion conductance with a preference SCN(-) >> NO3(-) > I(-) > Cl(-) (By similarity). 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:D3ZJ25, ECO:0000250|UniProtKB:Q15758, ECO:0000269|PubMed:7702599, ECO:0000269|PubMed:8662767, ECO:0000305|PubMed:38650461}.
uniprot
proteins
mass_dalton
58483
uniprot
proteins
protein_family
Dicarboxylate/amino acid:cation symporter (DAACS) (TC 2.A.23) family
uniprot
proteins
protein_family
SLC1A5 subfamily
uniprot
proteins
pubmed
17094966
uniprot
proteins
pubmed
19144319
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
31535081
uniprot
proteins
pubmed
38650461
uniprot
proteins
pubmed
7702599
uniprot
proteins
pubmed
8662767
uniprot
proteins
sequence_length
553
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7702599, ECO:0000269|PubMed:8662767}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:38650461}; Multi-pass membrane protein {ECO:0000255}. Melanosome {ECO:0000250|UniProtKB:Q15758}. Note=Restricted to the apical cell membrane of proximal tubule epithelial cells. {ECO:0000269|PubMed:38650461}.
uniprot
proteins
transmembrane_region
TRANSMEM 51..80; /note="Helical; Name=1"; /evidence="ECO:0000250|UniProtKB:P43003"; TRANSMEM 94..115; /note="Helical; Name=2"; /evidence="ECO:0000250|UniProtKB:P43003"; TRANSMEM 130..152; /note="Helical; Name=3"; /evidence="ECO:0000250|UniProtKB:P43003"; TRANSMEM 237..260; /note="Helical; Name=4"; /evidence="ECO:0000250|UniProtKB:P43003"; TRANSMEM 270..297; /note="Helical; Name=5"; /evidence="ECO:0000250|UniProtKB:P43003"; TRANSMEM 319..340; /note="Helical; Name=6"; /evidence="ECO:0000250|UniProtKB:P43003"; TRANSMEM 386..412; /note="Helical; Name=7"; /evidence="ECO:0000250|UniProtKB:P43003"; TRANSMEM 473..494; /note="Helical; Name=8"; /evidence="ECO:0000250|UniProtKB:P43003
uniprot
proteins