Q9H2H9 · S38A1_HUMAN
- ProteinSodium-coupled neutral amino acid symporter 1
- GeneSLC38A1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids487 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Symporter that cotransports short-chain neutral amino acids and sodium ions from the extraccellular to the intracellular side of the cell membrane (PubMed:10891391, PubMed:20599747).
The transport is elctrogenic, pH dependent and driven by the Na+ electrochemical gradient (PubMed:10891391).
Participates in the astroglia-derived glutamine transport into GABAergic interneurons for neurotransmitter GABA de novo synthesis (By similarity).
May also contributes to amino acid transport in placental trophoblasts (PubMed:20599747).
Also regulates synaptic plasticity (PubMed:12388062).
The transport is elctrogenic, pH dependent and driven by the Na+ electrochemical gradient (PubMed:10891391).
Participates in the astroglia-derived glutamine transport into GABAergic interneurons for neurotransmitter GABA de novo synthesis (By similarity).
May also contributes to amino acid transport in placental trophoblasts (PubMed:20599747).
Also regulates synaptic plasticity (PubMed:12388062).
Catalytic activity
- L-glutamine(in) + Na+(in) = L-glutamine(out) + Na+(out)This reaction proceeds in the backward direction.L-glutamine (in)CHEBI:58359
+ Na+ (in)CHEBI:29101= L-glutamine (out)CHEBI:58359+ Na+ (out)CHEBI:29101 - L-alanine(in) + Na+(in) = L-alanine(out) + Na+(out)This reaction proceeds in the backward direction.
- L-asparagine(in) + Na+(in) = L-asparagine(out) + Na+(out)This reaction proceeds in the backward direction.
- L-histidine(in) + Na+(in) = L-histidine(out) + Na+(out)This reaction proceeds in the backward direction.
- L-serine(in) + Na+(in) = L-serine(out) + Na+(out)This reaction proceeds in the backward direction.
- L-cysteine(in) + Na+(in) = L-cysteine(out) + Na+(out)This reaction proceeds in the backward direction.
- L-methionine(in) + Na+(in) = L-methionine(out) + Na+(out)This reaction proceeds in the backward direction.
- glycine(in) + Na+(in) = glycine(out) + Na+(out)This reaction proceeds in the backward direction.
- L-threonine(in) + Na+(in) = L-threonine(out) + Na+(out)This reaction proceeds in the backward direction.
- L-proline(in) + Na+(in) = L-proline(out) + Na+(out)This reaction proceeds in the backward direction.
Activity regulation
Inhibited by alpha-(methylamino)isobutyric acid (MeAIB). Inhibited by lithium, potassium, choline ions, N-methylglucamine. The pH dependence has an allosteric effect on the transport.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
890 μM | alpha-(methylamino)isobutyric acid (MeAIB) | 8.5 |
GO annotations
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameSodium-coupled neutral amino acid symporter 1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9H2H9
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Note: Restricted to the somatodendritic compartment of neurons. Found in the cellular processes of neurons in the developing brain.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-74 | Cytoplasmic | ||||
Sequence: MMHFKSGLELTELQNMTVPEDDNISNDSNDFTEVENGQINSKFISDRESRRSLTNSHLEKKKCDEYIPGTTSLG | ||||||
Transmembrane | 75-97 | Helical | ||||
Sequence: MSVFNLSNAIMGSGILGLAFALA | ||||||
Topological domain | 98-112 | Extracellular | ||||
Sequence: NTGILLFLVLLTSVT | ||||||
Transmembrane | 113-133 | Helical | ||||
Sequence: LLSIYSINLLLICSKETGCMV | ||||||
Topological domain | 134-147 | Cytoplasmic | ||||
Sequence: YEKLGEQVFGTTGK | ||||||
Transmembrane | 148-168 | Helical | ||||
Sequence: FVIFGATSLQNTGAMLSYLFI | ||||||
Topological domain | 169-188 | Extracellular | ||||
Sequence: VKNELPSAIKFLMGKEETFS | ||||||
Transmembrane | 189-211 | Helical | ||||
Sequence: AWYVDGRVLVVIVTFGIILPLCL | ||||||
Topological domain | 212-216 | Cytoplasmic | ||||
Sequence: LKNLG | ||||||
Transmembrane | 217-237 | Helical | ||||
Sequence: YLGYTSGFSLSCMVFFLIVVI | ||||||
Topological domain | 238-275 | Extracellular | ||||
Sequence: YKKFQIPCIVPELNSTISANSTNADTCTPKYVTFNSKT | ||||||
Transmembrane | 276-296 | Helical | ||||
Sequence: VYALPTIAFAFVCHPSVLPIY | ||||||
Topological domain | 297-312 | Cytoplasmic | ||||
Sequence: SELKDRSQKKMQMVSN | ||||||
Transmembrane | 313-333 | Helical | ||||
Sequence: ISFFAMFVMYFLTAIFGYLTF | ||||||
Topological domain | 334-350 | Extracellular | ||||
Sequence: YDNVQSDLLHKYQSKDD | ||||||
Transmembrane | 351-371 | Helical | ||||
Sequence: ILILTVRLAVIVAVILTVPVL | ||||||
Topological domain | 372-393 | Cytoplasmic | ||||
Sequence: FFTVRSSLFELAKKTKFNLCRH | ||||||
Transmembrane | 394-414 | Helical | ||||
Sequence: TVVTCILLVVINLLVIFIPSM | ||||||
Topological domain | 415-416 | Extracellular | ||||
Sequence: KD | ||||||
Transmembrane | 417-437 | Helical | ||||
Sequence: IFGVVGVTSANMLIFILPSSL | ||||||
Topological domain | 438-452 | Cytoplasmic | ||||
Sequence: YLKITDQDGDKGTQR | ||||||
Transmembrane | 453-473 | Helical | ||||
Sequence: IWAALFLGLGVLFSLVSIPLV | ||||||
Topological domain | 474-487 | Extracellular | ||||
Sequence: IYDWACSSSSDEGH |
Keywords
- Cellular component
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 528 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data), disulfide bond, glycosylation.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000310475 | 1-487 | UniProt | Sodium-coupled neutral amino acid symporter 1 | |||
Sequence: MMHFKSGLELTELQNMTVPEDDNISNDSNDFTEVENGQINSKFISDRESRRSLTNSHLEKKKCDEYIPGTTSLGMSVFNLSNAIMGSGILGLAFALANTGILLFLVLLTSVTLLSIYSINLLLICSKETGCMVYEKLGEQVFGTTGKFVIFGATSLQNTGAMLSYLFIVKNELPSAIKFLMGKEETFSAWYVDGRVLVVIVTFGIILPLCLLKNLGYLGYTSGFSLSCMVFFLIVVIYKKFQIPCIVPELNSTISANSTNADTCTPKYVTFNSKTVYALPTIAFAFVCHPSVLPIYSELKDRSQKKMQMVSNISFFAMFVMYFLTAIFGYLTFYDNVQSDLLHKYQSKDDILILTVRLAVIVAVILTVPVLFFTVRSSLFELAKKTKFNLCRHTVVTCILLVVINLLVIFIPSMKDIFGVVGVTSANMLIFILPSSLYLKITDQDGDKGTQRIWAALFLGLGVLFSLVSIPLVIYDWACSSSSDEGH | |||||||
Modified residue | 6 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 11 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 25 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 25 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 28 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 28 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 32 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 49 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 49 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 52 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 52 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 54 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 54 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 56 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 56 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Disulfide bond | 245↔264 | UniProt | |||||
Sequence: CIVPELNSTISANSTNADTC | |||||||
Glycosylation | 251 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 257 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
N-glycosylation plays an important role in the L-glutamine transport.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in the cerebral cortex by pyramidal and GABAergic neurons, astrocytes and other non-neuronal cells (at protein level). Expressed in placenta, heart, lung, skeletal muscle, spleen, stomach and testis (PubMed:10891391, PubMed:12388062, PubMed:15054072, PubMed:16148032).
Highly expressed in cytotrophoblast cells from term placenta (PubMed:20599747).
Highly expressed in cytotrophoblast cells from term placenta (PubMed:20599747).
Induction
Down-regulated by bacterial lipopolysaccharides (LPS) in glial cells (PubMed:12388062).
Down-regulated upon hypoxia (PubMed:16583402).
Down-regulated upon hypoxia (PubMed:16583402).
Gene expression databases
Organism-specific databases
Interaction
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Sequence
- Sequence statusComplete
- Length487
- Mass (Da)54,048
- Last updated2001-03-01 v1
- Checksum5CBC96880D7BDE03
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 107 | in Ref. 3; BAB55394 | ||||
Sequence: L → P | ||||||
Sequence conflict | 203 | in Ref. 4; BAC11310 | ||||
Sequence: F → V | ||||||
Sequence conflict | 375 | in Ref. 2; AAG44546 | ||||
Sequence: V → D | ||||||
Sequence conflict | 483-484 | in Ref. 2; AAG44546 | ||||
Sequence: SD → NG |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF271070 EMBL· GenBank· DDBJ | AAG39354.1 EMBL· GenBank· DDBJ | mRNA | ||
AF247166 EMBL· GenBank· DDBJ | AAG44546.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
AK027825 EMBL· GenBank· DDBJ | BAB55394.1 EMBL· GenBank· DDBJ | mRNA | ||
AK074758 EMBL· GenBank· DDBJ | BAC11186.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK074949 EMBL· GenBank· DDBJ | BAC11310.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471111 EMBL· GenBank· DDBJ | EAW57895.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC010620 EMBL· GenBank· DDBJ | AAH10620.1 EMBL· GenBank· DDBJ | mRNA |