Q7TSF2 · VGLU3_RAT
- ProteinVesicular glutamate transporter 3
- GeneSlc17a8
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids588 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Multifunctional transporter that transports L-glutamate as well as multiple ions such as chloride, sodium and phosphate (PubMed:12097496, PubMed:12388773, PubMed:27133463).
At the synaptic vesicle membrane, mainly functions as an uniporter that mediates the uptake of L-glutamate into synaptic vesicles at presynaptic nerve terminals of excitatory neural cells (PubMed:12097496, PubMed:12388773, PubMed:27133463).
The L-glutamate uniporter activity is electrogenic and is driven by the proton electrochemical gradient, mainly by the electrical gradient established by the vacuolar H+-ATPase across the synaptic vesicle membrane (PubMed:12097496, PubMed:12388773).
In addition, functions as a chloride channel that allows a chloride permeation through the synaptic vesicle membrane that affects the proton electrochemical gradient and promotes synaptic vesicles acidification (PubMed:27133463).
At the plasma membrane, following exocytosis, functions as a symporter of Na+ and phosphate from the extracellular space to the cytoplasm allowing synaptic phosphate homeostasis regulation (By similarity).
The symporter activity is electrogenic (By similarity).
Moreover, operates synergistically with SLC18A3/VACHT under a constant H+ gradient, thereby allowing striatal vesicular acetylcholine uptake (PubMed:18278042).
At the synaptic vesicle membrane, mainly functions as an uniporter that mediates the uptake of L-glutamate into synaptic vesicles at presynaptic nerve terminals of excitatory neural cells (PubMed:12097496, PubMed:12388773, PubMed:27133463).
The L-glutamate uniporter activity is electrogenic and is driven by the proton electrochemical gradient, mainly by the electrical gradient established by the vacuolar H+-ATPase across the synaptic vesicle membrane (PubMed:12097496, PubMed:12388773).
In addition, functions as a chloride channel that allows a chloride permeation through the synaptic vesicle membrane that affects the proton electrochemical gradient and promotes synaptic vesicles acidification (PubMed:27133463).
At the plasma membrane, following exocytosis, functions as a symporter of Na+ and phosphate from the extracellular space to the cytoplasm allowing synaptic phosphate homeostasis regulation (By similarity).
The symporter activity is electrogenic (By similarity).
Moreover, operates synergistically with SLC18A3/VACHT under a constant H+ gradient, thereby allowing striatal vesicular acetylcholine uptake (PubMed:18278042).
Catalytic activity
- L-glutamate(out) = L-glutamate(in)
- chloride(in) = chloride(out)
- 3 Na+(out) + phosphate(out) = 3 Na+(in) + phosphate(in)
Activity regulation
The L-glutamate uniporter activity exhibits a biphasic dependence on chloride concentration (PubMed:12388773).
Chloride channel activity is allosterically activated by lumenal H+ and Cl- leading to synaptic vesicles acidification (PubMed:27133463).
The glutamate transport activity is allosterically activated by lumenal H+ and Cl-, preventing non-vesicular L-glutamate release (PubMed:27133463).
Chloride channel activity is allosterically activated by lumenal H+ and Cl- leading to synaptic vesicles acidification (PubMed:27133463).
The glutamate transport activity is allosterically activated by lumenal H+ and Cl-, preventing non-vesicular L-glutamate release (PubMed:27133463).
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
0.52 mM | L-glutamate | |||||
1.5 mM | L-glutamate |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
20.3 pmol/min/mg | toward L-glutamate |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameVesicular glutamate transporter 3
- Short namesVGluT3
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionQ7TSF2
- 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 | 1-76 | Cytoplasmic | ||||
Sequence: MPFNAFDTFKEKILKPGKEGVKNAVGDSLGILQRKLDGTNEEGDAIELSEEGRPVQTSRARAPVCDCSCCGIPKRY | ||||||
Transmembrane | 77-97 | Helical | ||||
Sequence: IIAVMSGLGFCISFGIRCNLG | ||||||
Topological domain | 98-130 | Vesicular | ||||
Sequence: VAIVEMVNNSTVYVDGKPEIQTAQFNWDPETVG | ||||||
Transmembrane | 131-151 | Helical | ||||
Sequence: LIHGSFFWGYIVTQIPGGFIS | ||||||
Topological domain | 152-153 | Cytoplasmic | ||||
Sequence: NK | ||||||
Transmembrane | 154-174 | Helical | ||||
Sequence: FAANRVFGAAIFLTSTLNMFI | ||||||
Topological domain | 175-182 | Vesicular | ||||
Sequence: PSAARVHY | ||||||
Transmembrane | 183-203 | Helical | ||||
Sequence: GCVMCVRILQGLVEGVTYPAC | ||||||
Topological domain | 204-221 | Cytoplasmic | ||||
Sequence: HGMWSKWAPPLERSRLAT | ||||||
Transmembrane | 222-242 | Helical | ||||
Sequence: TSFCGSYAGAVVAMPLAGVLV | ||||||
Topological domain | 243-249 | Vesicular | ||||
Sequence: QYIGWAS | ||||||
Transmembrane | 250-270 | Helical | ||||
Sequence: VFYIYGMFGIIWYMFWLLQAY | ||||||
Topological domain | 271-314 | Cytoplasmic | ||||
Sequence: ECPAVHPTISNEERTYIETSIGEGANLASLSKFNTPWRRFFTSL | ||||||
Transmembrane | 315-335 | Helical | ||||
Sequence: PVYAIIVANFCRSWTFYLLLI | ||||||
Topological domain | 336-353 | Vesicular | ||||
Sequence: SQPAYFEEVFGFAISKVG | ||||||
Transmembrane | 354-374 | Helical | ||||
Sequence: LLSAVPHMVMTIVVPIGGQLA | ||||||
Topological domain | 375-390 | Cytoplasmic | ||||
Sequence: DYLRSRKILTTTAVRK | ||||||
Transmembrane | 391-411 | Helical | ||||
Sequence: IMNCGGFGMEATLLLVVGFSH | ||||||
Topological domain | 412-413 | Vesicular | ||||
Sequence: TK | ||||||
Transmembrane | 414-434 | Helical | ||||
Sequence: GVAISFLVLAVGFSGFAISGF | ||||||
Topological domain | 435-447 | Cytoplasmic | ||||
Sequence: NVNHLDIAPRYAS | ||||||
Transmembrane | 448-468 | Helical | ||||
Sequence: ILMGISNGVGTLSGMVCPLIV | ||||||
Topological domain | 469-481 | Vesicular | ||||
Sequence: GAMTKHKTREEWQ | ||||||
Transmembrane | 482-502 | Helical | ||||
Sequence: NVFLIAALVHYSGVIFYGVFA | ||||||
Topological domain | 503-585 | Cytoplasmic | ||||
Sequence: SGEKQDWADPENLSEEKCGIIDQDELAEETELNHEAFVSPRKKMSYGATTQNCEVQKTDRRQQRESAFEGEEPLSYQNEEDFS |
Keywords
- Cellular component
Phenotypes & Variants
Chemistry
PTM/Processing
Features
Showing features for chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000331616 | 1-588 | Vesicular glutamate transporter 3 | |||
Sequence: MPFNAFDTFKEKILKPGKEGVKNAVGDSLGILQRKLDGTNEEGDAIELSEEGRPVQTSRARAPVCDCSCCGIPKRYIIAVMSGLGFCISFGIRCNLGVAIVEMVNNSTVYVDGKPEIQTAQFNWDPETVGLIHGSFFWGYIVTQIPGGFISNKFAANRVFGAAIFLTSTLNMFIPSAARVHYGCVMCVRILQGLVEGVTYPACHGMWSKWAPPLERSRLATTSFCGSYAGAVVAMPLAGVLVQYIGWASVFYIYGMFGIIWYMFWLLQAYECPAVHPTISNEERTYIETSIGEGANLASLSKFNTPWRRFFTSLPVYAIIVANFCRSWTFYLLLISQPAYFEEVFGFAISKVGLLSAVPHMVMTIVVPIGGQLADYLRSRKILTTTAVRKIMNCGGFGMEATLLLVVGFSHTKGVAISFLVLAVGFSGFAISGFNVNHLDIAPRYASILMGISNGVGTLSGMVCPLIVGAMTKHKTREEWQNVFLIAALVHYSGVIFYGVFASGEKQDWADPENLSEEKCGIIDQDELAEETELNHEAFVSPRKKMSYGATTQNCEVQKTDRRQQRESAFEGEEPLSYQNEEDFSETS | ||||||
Glycosylation | 106 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in brain, kidney and liver. Expressed within the amygdala, brainstem, cerberal cortex, dorsal root ganglia, dorsal spinal cord, hippocampus, hypothalamus, retina, striatum and ventral spinal cord. Expressed within neurons of the caudate-putamen, olfactory tubercle, nucleus accumbens, hippocampus, interpeduncular nucleus and dorsal and medial raphe nuclei. Expressed in inner hair cells of the ear. Expressed at synaptic terminals within the lateral superior olive (LSO), a nucleus of the mammalian sound localization system, and in the medial nucleus of the trapezoid body (MNTB), which provides inhibitory input to the LSO.
Gene expression databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 539-588 | Disordered | ||||
Sequence: FVSPRKKMSYGATTQNCEVQKTDRRQQRESAFEGEEPLSYQNEEDFSETS |
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length588
- Mass (Da)64,755
- Last updated2008-04-29 v2
- Checksum9644C021D94286B5
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 4 | in Ref. 2; AAM50094 | ||||
Sequence: N → K |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ491795 EMBL· GenBank· DDBJ | CAD37138.1 EMBL· GenBank· DDBJ | mRNA | ||
AY117026 EMBL· GenBank· DDBJ | AAM50094.1 EMBL· GenBank· DDBJ | mRNA |