P31650 · S6A11_MOUSE
- ProteinSodium- and chloride-dependent GABA transporter 3
- GeneSlc6a11
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids627 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Mediates sodium- and chloride-dependent transport of gamma-aminobutyric acid (GABA) (PubMed:30270321, PubMed:8420981).
Can also mediate transport of beta-alanine and to a lower extent that of taurine and hypotaurine (PubMed:30270321, PubMed:8420981).
Can also mediate transport of beta-alanine and to a lower extent that of taurine and hypotaurine (PubMed:30270321, PubMed:8420981).
Catalytic activity
- 4-aminobutanoate(out) + chloride(out) + 2 Na+(out) = 4-aminobutanoate(in) + chloride(in) + 2 Na+(in)This reaction proceeds in the forward direction.4-aminobutanoate (out)CHEBI:59888
+ chloride (out)CHEBI:17996+ 2 Na+ (out)CHEBI:29101= 4-aminobutanoate (in)CHEBI:59888+ chloride (in)CHEBI:17996+ 2 Na+ (in)CHEBI:29101 - chloride(out) + 2 Na+(out) + taurine(out) = chloride(in) + 2 Na+(in) + taurine(in)This reaction proceeds in the forward direction.
- beta-alanine(out) + chloride(out) + 2 Na+(out) = beta-alanine(in) + chloride(in) + 2 Na+(in)This reaction proceeds in the forward direction.
- chloride(out) + hypotaurine(out) + 2 Na+(out) = chloride(in) + hypotaurine(in) + 2 Na+(in)This reaction proceeds in the forward direction.
Activity regulation
GABA transport is inhibited by beta-alanine, taurine, hypotaurine, beta-guanidinopropionic acid and 2,3-diaminopropionic acid (PubMed:8420981).
Beta-alanine transport is inhibited by GABA (PubMed:8420981).
Beta-alanine transport is inhibited by GABA (PubMed:8420981).
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.8 μM | GABA | |||||
2.24 μM | GABA | |||||
99 μM | beta-alanine | |||||
1.4 mM | taurine |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cell projection | |
Cellular Component | GABA-ergic synapse | |
Cellular Component | plasma membrane | |
Cellular Component | postsynaptic membrane | |
Cellular Component | presynaptic membrane | |
Cellular Component | synapse | |
Molecular Function | amino acid binding | |
Molecular Function | amino acid:sodium symporter activity | |
Molecular Function | gamma-aminobutyric acid:sodium:chloride symporter activity | |
Molecular Function | taurine:sodium symporter activity | |
Biological Process | amino acid transport | |
Biological Process | neurotransmitter transport | |
Biological Process | neurotransmitter uptake | |
Biological Process | response to xenobiotic stimulus | |
Biological Process | sodium ion transmembrane transport |
Keywords
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameSodium- and chloride-dependent GABA transporter 3
- Short namesGAT-3
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP31650
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-53 | Cytoplasmic | ||||
Sequence: MTAEQALPLGNGKAAEEARGSETLGGGGGGAAGTREARDKAVHERGHWNNKVE | ||||||
Transmembrane | 54-74 | Helical; Name=1 | ||||
Sequence: FVLSVAGEIIGLGNVWRFPYL | ||||||
Transmembrane | 82-101 | Helical; Name=2 | ||||
Sequence: AFLIPYVVFFICCGIPVFFL | ||||||
Transmembrane | 126-146 | Helical; Name=3 | ||||
Sequence: GIGYATQVIEAHLNVYYIIIL | ||||||
Topological domain | 147-220 | Extracellular | ||||
Sequence: AWAIFYLSNCFTTELPWATCGHEWNTEKCVEFQKLNFSNYSHVSLQNATSPVMEFWERRVLAISDGIEHIGNLR | ||||||
Transmembrane | 221-239 | Helical; Name=4 | ||||
Sequence: WELALCLLAAWTICYFCIW | ||||||
Transmembrane | 248-265 | Helical; Name=5 | ||||
Sequence: VVYVTATFPYIMLLILLI | ||||||
Transmembrane | 301-318 | Helical; Name=6 | ||||
Sequence: IFFSYAICLGCLTALGSY | ||||||
Transmembrane | 330-351 | Helical; Name=7 | ||||
Sequence: IMLCCLNSGTSFVAGFAIFSVL | ||||||
Transmembrane | 384-403 | Helical; Name=8 | ||||
Sequence: MPLSPLWATLFFMMLIFLGL | ||||||
Transmembrane | 433-451 | Helical; Name=9 | ||||
Sequence: LLILALSIISYFLGLVMLT | ||||||
Transmembrane | 468-488 | Helical; Name=10 | ||||
Sequence: GMCLLFVAIFECVCIGWVYGS | ||||||
Transmembrane | 509-528 | Helical; Name=11 | ||||
Sequence: WCWKVVTPGICAGIFIFFLV | ||||||
Transmembrane | 548-566 | Helical; Name=12 | ||||
Sequence: IGWLMALSSMLCIPLWIFI | ||||||
Topological domain | 567-627 | Cytoplasmic | ||||
Sequence: KLWKTEGTLPEKLQKLTVPSADLKMRGKLGASPRTVTVNDCEAKVKGDGTISAITEKETHF |
Keywords
- Cellular component
Phenotypes & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 20 variants from UniProt as well as other sources including ClinVar and dbSNP.
Chemistry
PTM/Processing
Features
Showing features for chain, modified residue, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000214785 | 1-627 | Sodium- and chloride-dependent GABA transporter 3 | |||
Sequence: MTAEQALPLGNGKAAEEARGSETLGGGGGGAAGTREARDKAVHERGHWNNKVEFVLSVAGEIIGLGNVWRFPYLCYKNGGGAFLIPYVVFFICCGIPVFFLETALGQFTSEGGITCWRRVCPLFEGIGYATQVIEAHLNVYYIIILAWAIFYLSNCFTTELPWATCGHEWNTEKCVEFQKLNFSNYSHVSLQNATSPVMEFWERRVLAISDGIEHIGNLRWELALCLLAAWTICYFCIWKGTKSTGKVVYVTATFPYIMLLILLIRGVTLPGASEGIKFYLYPDLSRLSDPQVWVDAGTQIFFSYAICLGCLTALGSYNNYNNNCYRDCIMLCCLNSGTSFVAGFAIFSVLGFMAYEQGVPIAEVAESGPGLAFIAYPKAVTMMPLSPLWATLFFMMLIFLGLDSQFVCVESLVTAVVDMYPKVFRRGYRRELLILALSIISYFLGLVMLTEGGMYIFQLFDSYAASGMCLLFVAIFECVCIGWVYGSNRFYDNIEDMIGYRPLSLIKWCWKVVTPGICAGIFIFFLVKYKPLKYNNVYTYPAWGYGIGWLMALSSMLCIPLWIFIKLWKTEGTLPEKLQKLTVPSADLKMRGKLGASPRTVTVNDCEAKVKGDGTISAITEKETHF | ||||||
Modified residue | 21 | Phosphoserine | ||||
Sequence: S | ||||||
Glycosylation | 182 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 185 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 193 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-36 | Disordered | ||||
Sequence: MTAEQALPLGNGKAAEEARGSETLGGGGGGAAGTRE |
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length627
- Mass (Da)69,961
- Last updated2011-07-27 v2
- Checksum7BCCFA2000DB024F
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L04662 EMBL· GenBank· DDBJ | - | mRNA | No translation available. | |
AK053078 EMBL· GenBank· DDBJ | BAC35259.1 EMBL· GenBank· DDBJ | mRNA | ||
AK140423 EMBL· GenBank· DDBJ | BAE24379.1 EMBL· GenBank· DDBJ | mRNA | ||
CH466523 EMBL· GenBank· DDBJ | EDK99507.1 EMBL· GenBank· DDBJ | Genomic DNA |