Slc38a2
entrez
29642
canonical
uniprot
Q9JHE5
canonical
ensembl
ENSRNOG00000006305
resolver
ensembl
ENSRNOG00055012707
resolver
ensembl
ENSRNOG00060006650
resolver
ensembl
ENSRNOG00065019116
resolver
ensp
ENSRNOP00000031532
resolver
ensp
ENSRNOP00055017596
resolver
ensp
ENSRNOP00060008109
resolver
ensp
ENSRNOP00065025645
resolver
enst
ENSRNOT00000039002
resolver
enst
ENSRNOT00055021710
resolver
enst
ENSRNOT00060010897
resolver
enst
ENSRNOT00065032133
resolver
genesymbol
Slc38a2
resolver
genesymbol_syn
Ata2
resolver
genesymbol_syn
Sa1
resolver
genesymbol_syn
Sat2
resolver
genesymbol_syn
Snat2
resolver
uniprot
Q9JI88
resolver
uniprot_entry
S38A2_RAT
resolver
uniprot_sec
Q9JI88
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by N-methyl-D-glucamine (PubMed:10747860). Inhibited by choline (PubMed:10811809, PubMed:10859363, PubMed:11716780). Allosteric regulation of sodium ions binding by pH (PubMed:11756489, PubMed:16629640). {ECO:0000269|PubMed:10747860, ECO:0000269|PubMed:10811809, ECO:0000269|PubMed:10859363, ECO:0000269|PubMed:11716780, ECO:0000269|PubMed:11756489, ECO:0000269|PubMed:16629640}.
uniprot
proteins
amino_acid_sequence
MKKTEMGRFNISPDEDSSSYSSNGDFNYSYPTKQAALKSHYVDVDPENQNFLLESNLGKKKYETDFHPGTTSFGMSVFNLSNAIVGSGILGLSYAMANTGIALFIILLTFVSIFSLYSVHLLLKTANEGGSLLYEQLGHKAYGLAGKLAASGSITMQNIGAMSSYLFIVKYELPLVIKALMNIEDTNGLWYLNGDYLVLLVSFVLILPLSLLRNLGYLGYTSGLSLLCMIFFLIVVICKKFQIPCPVEVALMANETVNGTFTQVALAALASNSTAADTCRPRYFIFNSQTVYAVPILTFSFVCHPAVLPIYEELKSRSRRRMMNVSKISFFAMFLMYLLAALFGYLTFYEHVESELLHTYSAIVGTDILLLVVRLAVLVAVTLTVPVVIFPIRSSVTHLLCPTKEFSWFRHSVITVTILAFTNLLVIFVPTIRDIFGFIGASAAAMLIFILPSAFYIKLVKKEPMRSVQKIGALCFLLSGVVVMIGSMGLIVLDWVHDASAGGH
uniprot
proteins
function
FUNCTION: Symporter that cotransports neutral amino acids and sodium ions from the extracellular to the intracellular side of the cell membrane (PubMed:10747860, PubMed:10811809, PubMed:10859363, PubMed:11716780, PubMed:11756489, PubMed:12054432, PubMed:16629640, PubMed:18319257, PubMed:18330498, PubMed:18832333, PubMed:19589777, PubMed:21158741, PubMed:27355203). The transport is pH-sensitive, Li(+)-intolerant, electrogenic, driven by the Na(+) electrochemical gradient and cotransports of neutral amino acids and sodium ions with a stoichiometry of 1:1 (PubMed:10747860, PubMed:10811809, PubMed:10859363, PubMed:11716780, PubMed:11756489, PubMed:12054432, PubMed:16629640, PubMed:18319257, PubMed:19589777, PubMed:21158741). May function in the transport of amino acids at the blood-brain barrier (PubMed:12021389). May function in the transport of amino acids in the supply of maternal nutrients to the fetus through the placenta (By similarity). Maintains a key metabolic glutamine/glutamate balance underpinning retrograde signaling by dendritic release of the neurotransmitter glutamate (PubMed:18832333). Transports L-proline in differentiating osteoblasts for the efficient synthesis of proline-enriched proteins and provides proline essential for osteoblast differentiation and bone formation during bone development (By similarity). {ECO:0000250|UniProtKB:Q8CFE6, ECO:0000269|PubMed:10747860, ECO:0000269|PubMed:10811809, ECO:0000269|PubMed:10859363, ECO:0000269|PubMed:11716780, ECO:0000269|PubMed:11756489, ECO:0000269|PubMed:12021389, ECO:0000269|PubMed:12054432, ECO:0000269|PubMed:16629640, ECO:0000269|PubMed:18319257, ECO:0000269|PubMed:18330498, ECO:0000269|PubMed:18832333, ECO:0000269|PubMed:19589777, ECO:0000269|PubMed:21158741, ECO:0000269|PubMed:27355203}.
uniprot
proteins
mass_dalton
55554
uniprot
proteins
mutagenesis
MUTAGEN 82; /note="N->A: Impairs amino acid transport. Impairs the interaction of SNAT2 with the cotransported sodium ion."; /evidence="ECO:0000269|PubMed:18319257"; MUTAGEN 82; /note="N->S: Loss of amino acid transport activity. Loss of amino acid uptake activity. Reduces the amino acid affinity."; /evidence="ECO:0000269|PubMed:18319257"; MUTAGEN 228; /note="C->S: Reduces amino acid transport activity of 75%. Significantly decreases alanine transport activity."; /evidence="ECO:0000269|PubMed:27355203"; MUTAGEN 238; /note="C->S: Decreases alanine transport activity."; /evidence="ECO:0000269|PubMed:27355203"; MUTAGEN 245; /note="C->A: Does not affect cell membrane localization."; /evidence="ECO:0000269|PubMed:27355203"; MUTAGEN 245; /note="C->S: Does not affect amino acid transport activity. Significantly decreases alanine transport activity."; /evidence="ECO:0000269|PubMed:27355203"; MUTAGEN 254; /note="N->Q: Partially loss of glycosylation. Completely loss of glycosylation; when associated with Q-258 and Q-272. Decreases expression; when associated with Q-258 and Q-272. Does not affect cell membrane localization; when associated with Q-258 and Q-272."; /evidence="ECO:0000269|PubMed:29678469"; MUTAGEN 258; /note="N->Q: Partially loss of glycosylation. Dramatically loss of glycosylation; when associated with Q-272. Completely loss of glycosylation; when associated with Q-254 and Q-272. Decreases expression; when associated with Q-272. Decreases expression; when associated with Q-254 and Q-272. Does not affect cell membrane localization; when associated with Q-272. Does not affect cell membrane localization; when associated with Q-254 and Q-272."; /evidence="ECO:0000269|PubMed:29678469"; MUTAGEN 272; /note="N->Q: Partially loss of glycosylation. Dramatically loss of glycosylation; when associated with Q-258. Completely loss of glycosylation; when associated with Q-254 and Q-258. Decreases expression; when associated with Q-258. Decreases expression; when associated with Q-254 and Q-258. Does not affect cell membrane localization; when associated with Q-258. Does not affect cell membrane localization; when associated with Q-254 and Q-258."; /evidence="ECO:0000269|PubMed:29678469"; MUTAGEN 279; /note="C->A: Does not affect cell membrane localization."; /evidence="ECO:0000269|PubMed:27355203"; MUTAGEN 279; /note="C->S: Does not affect amino acid transport activity. Significantly decreases alanine transport activity."; /evidence="ECO:0000269|PubMed:27355203"; MUTAGEN 303; /note="C->S: Reduces amino acid transport activity of 75%. Significantly decreases alanine transport activity."; /evidence="ECO:0000269|PubMed:27355203"; MUTAGEN 337; /note="Y->A: Impairs transport current. Reduces the amino acid affinity."; /evidence="ECO:0000269|PubMed:18319257"; MUTAGEN 374; /note="R->Q: Does not affect the alanine-induced transport current. Reduces the amino acid affinity."; /evidence="ECO:0000269|PubMed:18319257"; MUTAGEN 384; /note="T->A: Does not affect cell membrane localization. Eliminates the sodium-induced anion leak current. Inhibits amino acid transport activity. Reduces affinity for sodium ion."; /evidence="ECO:0000269|PubMed:19589777"; MUTAGEN 401; /note="C->S: Does not affect alanine transport activity."; /evidence="ECO:0000269|PubMed:27355203"; MUTAGEN 475; /note="C->S: Significantly decreases alanine transport activity."; /evidence="ECO:0000269|PubMed:27355203"; MUTAGEN 504; /note="H->A: Modifies the transporter pH-sensitivity."; /evidence="ECO:0000269|PubMed:16629640
uniprot
proteins
post_translational_modification
PTM: Polyubiquitination by NEDD4L regulates the degradation and the activity of SLC38A2. {ECO:0000250|UniProtKB:Q8CFE6}.
uniprot
proteins
protein_family
Amino acid/polyamine transporter 2 family
uniprot
proteins
pubmed
10747860
uniprot
proteins
pubmed
10811809
uniprot
proteins
pubmed
10859363
uniprot
proteins
pubmed
11311116
uniprot
proteins
pubmed
11716780
uniprot
proteins
pubmed
11756489
uniprot
proteins
pubmed
11834730
uniprot
proteins
pubmed
12021389
uniprot
proteins
pubmed
12054432
uniprot
proteins
pubmed
15561425
uniprot
proteins
pubmed
16616430
uniprot
proteins
pubmed
16629640
uniprot
proteins
pubmed
17488712
uniprot
proteins
pubmed
18319257
uniprot
proteins
pubmed
18330498
uniprot
proteins
pubmed
18832333
uniprot
proteins
pubmed
19589777
uniprot
proteins
pubmed
21158741
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
27355203
uniprot
proteins
pubmed
29678469
uniprot
proteins
sequence_length
504
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11311116, ECO:0000269|PubMed:11834730, ECO:0000269|PubMed:12054432, ECO:0000269|PubMed:15561425, ECO:0000269|PubMed:19589777, ECO:0000269|PubMed:21158741, ECO:0000269|PubMed:27355203, ECO:0000269|PubMed:29678469, ECO:0000305|PubMed:10859363}; Multi-pass membrane protein {ECO:0000269|PubMed:17488712, ECO:0000269|PubMed:29678469}. Note=Insulin promotes recruitment to the plasma membrane from a pool localized in the trans-Golgi network or endosomes (PubMed:11834730). Enriched in the somatodendritic compartment of neurons, it is also detected at the axonal shaft but excluded from the nerve terminal (PubMed:15561425, PubMed:16616430, PubMed:18832333). {ECO:0000269|PubMed:11834730, ECO:0000269|PubMed:15561425, ECO:0000269|PubMed:16616430, ECO:0000269|PubMed:18832333}.
uniprot
proteins
transmembrane_region
TRANSMEM 77..96; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 103..123; /note="Helical"; /evidence="ECO:0000255, ECO:0000305|PubMed:29678469"; TRANSMEM 159..177; /note="Helical"; /evidence="ECO:0000255, ECO:0000305|PubMed:29678469"; TRANSMEM 189..209; /note="Helical"; /evidence="ECO:0000255, ECO:0000305|PubMed:29678469"; TRANSMEM 218..238; /note="Helical"; /evidence="ECO:0000255, ECO:0000305|PubMed:29678469"; TRANSMEM 291..311; /note="Helical"; /evidence="ECO:0000255, ECO:0000305|PubMed:29678469"; TRANSMEM 328..348; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 370..390; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 412..432; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 435..455; /note="Helical"; /evidence="ECO:0000255, ECO:0000305|PubMed:29678469"; TRANSMEM 471..493; /note="Helical"; /evidence="ECO:0000255, ECO:0000305|PubMed:29678469
uniprot
proteins