Slc38a3
entrez
252919
canonical
uniprot
Q9JHZ9
canonical
ensembl
ENSRNOG00000016827
resolver
ensembl
ENSRNOG00055013368
resolver
ensembl
ENSRNOG00060029424
resolver
ensembl
ENSRNOG00065008326
resolver
ensp
ENSRNOP00000023623
resolver
ensp
ENSRNOP00055018583
resolver
ensp
ENSRNOP00060042496
resolver
ensp
ENSRNOP00065009785
resolver
enst
ENSRNOT00000023623
resolver
enst
ENSRNOT00055022921
resolver
enst
ENSRNOT00060051083
resolver
enst
ENSRNOT00065013218
resolver
genesymbol
Slc38a3
resolver
genesymbol_syn
Snat3
resolver
uniprot
Q66HS0
resolver
uniprot_entry
S38A3_RAT
resolver
uniprot_sec
Q66HS0
resolver
activity_regulation
ACTIVITY REGULATION: L-glutamine efflux and L-glutamine uptake are regulated by CO2/HCO3(-) through SLC4A4 leading to modulation of cytosolic pH and Na(+)concentration. {ECO:0000269|PubMed:17909850}.
uniprot
proteins
amino_acid_sequence
MEIPRQTEMVELVPNGKHLEGLLPVGMPTADTQRAEDAQHCGEGKGFLQQSSSKEPHFTDFEGKTSFGMSVFNLSNAIMGSGILGLAYAMANTGIILFLFLLTAVALLSSYSIHLLLKSSGIVGIRAYEQLGYRAFGTPGKLAAALAITLQNIGAMSSYLYIIKSELPLVIQTFLNLEKPTPVWYMDGNYLVILVSVIIILPLALMRQLGYLGYSSGFSLSCMVFFLIAVIYKKFQVPCPLAHNLVNATGNFSHMVVVEEKSQLQSEPDTAEAFCTPSYFTLNSQTAYTIPIMAFAFVCHPEVLPIYTELKDPSKRKMQHISNLSIAVMYVMYFLAALFGYLTFYDGVESELLHTYSKVDPFDVLILCVRVAVLIAVTLTVPIVLFPVRRAIQQMLFQNQEFSWLRHVLIATGLLTCINLLVIFAPNILGIFGIIGATSAPCLIFIFPAIFYFRIMPTEKEPVRSTPKILALCFAAVGFLLMTMSLSFIITDWVSGTSQHGGNH
uniprot
proteins
function
FUNCTION: Symporter that cotransports specific neutral amino acids and sodium ions, coupled to an H(+) antiporter activity (PubMed:10619430, PubMed:10823827, PubMed:11742981, PubMed:11850497, PubMed:16249471, PubMed:17148440, PubMed:19596860, PubMed:21525297, PubMed:28272791, PubMed:29561757). Mainly participates in the glutamate-GABA-glutamine cycle in brain where it transports L-glutamine from astrocytes in the intercellular space for the replenishment of both neurotransmitters glutamate and gamma-aminobutyric acid (GABA) in neurons (PubMed:10619430, PubMed:28272791, PubMed:29561757). Also functions as the major influx transporter in ganglion cells mediating the uptake of glutamine (By similarity). The transport activity is specific for L-glutamine, L-histidine and L-asparagine (PubMed:10619430, PubMed:10823827, PubMed:11742981, PubMed:11850497, PubMed:16249471, PubMed:17148440, PubMed:19596860, PubMed:21525297, PubMed:28272791, PubMed:29561757). The transport is electroneutral coupled to the cotransport of 1 Na(+) and the antiport of 1 H(+), pH dependent, saturable, Li(+) tolerant and functions in both direction depending on the concentration gradients of its substrates and cotransported ions (PubMed:10619430, PubMed:10823827, PubMed:11742981, PubMed:11850497, PubMed:16249471, PubMed:17148440, PubMed:17909850, PubMed:19596860, PubMed:28272791). Also mediates an amino acid-gated H(+) conductance that is not stoichiometrically coupled to the amino acid transport but which influences the ionic gradients that drive the amino acid transport (PubMed:11742981). In addition, may play a role in nitrogen metabolism, amino acid homeostasis, glucose metabolism and renal ammoniagenesis (By similarity). {ECO:0000250|UniProtKB:Q9DCP2, ECO:0000269|PubMed:10619430, ECO:0000269|PubMed:10823827, ECO:0000269|PubMed:11742981, ECO:0000269|PubMed:11850497, ECO:0000269|PubMed:16249471, ECO:0000269|PubMed:17148440, ECO:0000269|PubMed:17909850, ECO:0000269|PubMed:19596860, ECO:0000269|PubMed:21525297, ECO:0000269|PubMed:28272791, ECO:0000269|PubMed:29561757}.
uniprot
proteins
mass_dalton
55637
uniprot
proteins
mutagenesis
MUTAGEN 32; /note="T->A: Does not affect phosphorylation by PKC."; /evidence="ECO:0000269|PubMed:21525297"; MUTAGEN 51..53; /note="SSS->AAA: Loss of phosphorylation by PKC."; /evidence="ECO:0000269|PubMed:21525297"; MUTAGEN 51; /note="S->A: Does not affect phosphorylation by PKC."; /evidence="ECO:0000269|PubMed:21525297"; MUTAGEN 52; /note="S->A: Loss of phosphorylation by PKC. Reduces glutamine uptake upon phorbol-12-myristate-13-acetate (PMA) stimulation."; /evidence="ECO:0000269|PubMed:21525297"; MUTAGEN 53; /note="S->A: Does not affect phosphorylation by PKC."; /evidence="ECO:0000269|PubMed:21525297"; MUTAGEN 59; /note="T->A: Does not affect phosphorylation by PKC."; /evidence="ECO:0000269|PubMed:21525297"; MUTAGEN 76; /note="N->D: Abolishes L-glutamine transport activity. Induces a chloride transport. Increases the alkali-induced substrate-independent conductance. Does not affect cell membrane localization."; /evidence="ECO:0000269|PubMed:19596860"; MUTAGEN 76; /note="N->E: Abolishes L-glutamine transport activity. Induces a chloride transport. Increases the alkali-induced substrate-independent conductance. Does not affect cell membrane localization."; /evidence="ECO:0000269|PubMed:19596860"; MUTAGEN 76; /note="N->H: Abolishes L-glutamine transport activity. Inhibits asparagine transport activity. Increases the alkali-induced substrate-independent conductance. Significantly slow proton antiport activity. Affects cell membrane localization."; /evidence="ECO:0000269|PubMed:17148440, ECO:0000269|PubMed:19596860"; MUTAGEN 76; /note="N->Q: Abolishes glutamine transport activity. Increases the alkali-induced substrate-independent conductance. Does not affect cell membrane localization."; /evidence="ECO:0000269|PubMed:19596860"; MUTAGEN 76; /note="N->S: Abolishes glutamine transport activity. Increases the alkali-induced substrate-independent conductance. Does not affect cell membrane localization."; /evidence="ECO:0000269|PubMed:19596860"; MUTAGEN 210; /note="G->A: Does not affect L-glutamine transport activity. Does not affect cell membrane localization."; /evidence="ECO:0000269|PubMed:17148440"; MUTAGEN 215; /note="S->A: Does not affect L-glutamine transport activity. Does not affect cell membrane localization."; /evidence="ECO:0000269|PubMed:17148440"; MUTAGEN 300; /note="H->Q: Does not affect L-glutamine transport activity. Does not affect cell membrane localization."; /evidence="ECO:0000269|PubMed:17148440"; MUTAGEN 343; /note="T->A: Does not affect L-glutamine transport activity. Does not affect cell membrane localization."; /evidence="ECO:0000269|PubMed:17148440"; MUTAGEN 370; /note="R->Q: Does not affect L-glutamine transport activity. Does not affect cell membrane localization."; /evidence="ECO:0000269|PubMed:17148440"; MUTAGEN 380; /note="T->A: Significantly decreases L-glutamine transport activity. Does not affect cell membrane localization. Removes the cation conductance at pH 7.4. Does not affect the proton conductance at pH 8.4. Significantly dereases transport activity with LiCl."; /evidence="ECO:0000269|PubMed:17148440
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Ser-52 induces internalization and sequestration into an intracellular reservoir (PubMed:21525297, PubMed:29561757). During dephosphorylation by protein phosphatases, can recycle back to the plasma membrane and regain activity. Prolonged phosphorylation results in its degradation (PubMed:21525297). {ECO:0000269|PubMed:21525297, ECO:0000269|PubMed:29561757}.
uniprot
proteins
protein_family
Amino acid/polyamine transporter 2 family
uniprot
proteins
pubmed
10619430
uniprot
proteins
pubmed
10823827
uniprot
proteins
pubmed
11742981
uniprot
proteins
pubmed
11850497
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15716335
uniprot
proteins
pubmed
16249471
uniprot
proteins
pubmed
17148440
uniprot
proteins
pubmed
17909850
uniprot
proteins
pubmed
19596860
uniprot
proteins
pubmed
21525297
uniprot
proteins
pubmed
28272791
uniprot
proteins
pubmed
29561757
uniprot
proteins
sequence_length
504
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10619430, ECO:0000269|PubMed:17148440, ECO:0000269|PubMed:19596860, ECO:0000269|PubMed:21525297, ECO:0000269|PubMed:29561757}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000269|PubMed:15716335}. Note=The localization appears to be basolateral in the plasma membrane of hepatocytes surrounding the central vein. Localized at the cerebrospinal fluid (CSF)-facing membrane of the choroid plexus epithelial cells. In astrocytes, the localization at cell membrane is decreased by ammonia through the PKC signaling. Expressed in both luminal and abluminal plasma membranes of larger microvessels and blood brain barrier (BBB) capillaries (By similarity). Restricted to the basolateral membranes of S3 segment cells of the proximal tubules (PubMed:15716335). {ECO:0000250|UniProtKB:Q9DCP2, ECO:0000269|PubMed:15716335}.
uniprot
proteins
transmembrane_region
TRANSMEM 82..102; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 105..125; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 143..163; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 186..206; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 212..232; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 287..307; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 324..344; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 366..386; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 408..428; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 431..451; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 469..489; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins