SB0131 : Vesicular GABA transporter
[ CaMP Format ]
* Basic Information
| Organism | Rattus norvegicus (Norway rat) |
| Protein Names | vesicular inhibitory amino acid transporter [Rattus norvegicus]; vesicular inhibitory amino acid transporter; rGVAT; vesicular GABA transporter; GABA and glycine transporter; solute carrier family 32 member 1; Vesicular inhibitory amino acid transporter; Solute carrier family 32 member 1; Vesicular GABA transporter |
| Gene Names | Slc32a1; Vgat, Viaat; Vgat; Viaat; solute carrier family 32 (GABA vesicular transporter), member 1 |
| Gene Locus | 3q42; chromosome 3 |
| GO Function | Not available |
* Information From OMIM
Not Available.
* Structure Information
1. Primary Information
Length: 525 aa
Average Mass: 57.407 kDa
Monoisotopic Mass: 57.370 kDa
2. Domain Information
Annotated Domains: interpro / pfam / smart / prosite
Computationally Assigned Domains (Pfam+HMMER):
| domain name | begin | end | score | e-value |
|---|---|---|---|---|
| --- cleavage 51 --- | ||||
| --- cleavage 59 --- | ||||
| Transmembrane amino acid transporter protein 1. | 115 | 510 | 2.0 | 20.2 |
3. Sequence Information
Fasta Sequence: SB0131.fasta
Amino Acid Sequence and Secondary Structures (PsiPred):
4. 3D Information
Not Available.
* Cleavage Information
2 [sites] cleaved by Calpain 1
Source Reference: [PubMed ID: 21430162] Gomes JR, Lobo AC, Melo CV, Inacio AR, Takano J, Iwata N, Saido TC, de Almeida LP, Wieloch T, Duarte CB, Cleavage of the vesicular GABA transporter under excitotoxic conditions is followed by accumulation of the truncated transporter in nonsynaptic sites. J Neurosci. 2011 Mar 23;31(12):4622-35. doi: 10.1523/JNEUROSCI.3541-10.2011.
Cleavage sites (±10aa)
[Site 1] VGFAHCDDLD51-FEHRQGLQMD
Asp51 
Phe
 |
|||||||||
| P10 | P9 | P8 | P7 | P6 | P5 | P4 | P3 | P2 | P1 |
|---|---|---|---|---|---|---|---|---|---|
| Val42 | Gly43 | Phe44 | Ala45 | His46 | Cys47 | Asp48 | Asp49 | Leu50 | Asp51 |
 |
|||||||||
| P1' | P2' | P3' | P4' | P5' | P6' | P7' | P8' | P9' | P10' |
| Phe52 | Glu53 | His54 | Arg55 | Gln56 | Gly57 | Leu58 | Gln59 | Met60 | Asp61 |
Sequence conservation (by blast)
[Site 2] LDFEHRQGLQ59-MDILKSEGEP
Gln59 Met
|
|||||||||
| P10 | P9 | P8 | P7 | P6 | P5 | P4 | P3 | P2 | P1 |
|---|---|---|---|---|---|---|---|---|---|
| Leu50 | Asp51 | Phe52 | Glu53 | His54 | Arg55 | Gln56 | Gly57 | Leu58 | Gln59 |
|
|||||||||
| P1' | P2' | P3' | P4' | P5' | P6' | P7' | P8' | P9' | P10' |
| Met60 | Asp61 | Ile62 | Leu63 | Lys64 | Ser65 | Glu66 | Gly67 | Glu68 | Pro69 |
Sequence conservation (by blast)
* References
[PubMed ID: 19914352] Levinson JN, Li R, Kang R, Moukhles H, El-Husseini A, Bamji SX, Postsynaptic scaffolding molecules modulate the localization of neuroligins. Neuroscience. 2010 Feb 3;165(3):782-93. doi: 10.1016/j.neuroscience.2009.11.016.