Q9WV18 · GABR1_MOUSE
- ProteinGamma-aminobutyric acid type B receptor subunit 1
- GeneGabbr1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids960 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Component of a heterodimeric G-protein coupled receptor for GABA, formed by GABBR1 and GABBR2 (PubMed:10075644, PubMed:10773016).
Within the heterodimeric GABA receptor, only GABBR1 seems to bind agonists, while GABBR2 mediates coupling to G proteins (By similarity).
Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase (PubMed:10075644, PubMed:10773016).
Signaling inhibits adenylate cyclase, stimulates phospholipase A2, activates potassium channels, inactivates voltage-dependent calcium-channels and modulates inositol phospholipid hydrolysis (PubMed:10075644).
Calcium is required for high affinity binding to GABA (By similarity).
Plays a critical role in the fine-tuning of inhibitory synaptic transmission (By similarity).
Pre-synaptic GABA receptor inhibits neurotransmitter release by down-regulating high-voltage activated calcium channels, whereas postsynaptic GABA receptor decreases neuronal excitability by activating a prominent inwardly rectifying potassium (Kir) conductance that underlies the late inhibitory postsynaptic potentials (PubMed:10075644).
Not only implicated in synaptic inhibition but also in hippocampal long-term potentiation, slow wave sleep, muscle relaxation and antinociception (By similarity).
Within the heterodimeric GABA receptor, only GABBR1 seems to bind agonists, while GABBR2 mediates coupling to G proteins (By similarity).
Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase (PubMed:10075644, PubMed:10773016).
Signaling inhibits adenylate cyclase, stimulates phospholipase A2, activates potassium channels, inactivates voltage-dependent calcium-channels and modulates inositol phospholipid hydrolysis (PubMed:10075644).
Calcium is required for high affinity binding to GABA (By similarity).
Plays a critical role in the fine-tuning of inhibitory synaptic transmission (By similarity).
Pre-synaptic GABA receptor inhibits neurotransmitter release by down-regulating high-voltage activated calcium channels, whereas postsynaptic GABA receptor decreases neuronal excitability by activating a prominent inwardly rectifying potassium (Kir) conductance that underlies the late inhibitory postsynaptic potentials (PubMed:10075644).
Not only implicated in synaptic inhibition but also in hippocampal long-term potentiation, slow wave sleep, muscle relaxation and antinociception (By similarity).
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 246 | 4-aminobutanoate (UniProtKB | ChEBI); agonist | ||||
Sequence: S | ||||||
Binding site | 269 | 4-aminobutanoate (UniProtKB | ChEBI); agonist | ||||
Sequence: S | ||||||
Binding site | 286 | 4-aminobutanoate (UniProtKB | ChEBI); agonist | ||||
Sequence: H | ||||||
Binding site | 366 | 4-aminobutanoate (UniProtKB | ChEBI); agonist | ||||
Sequence: Y | ||||||
Binding site | 465 | 4-aminobutanoate (UniProtKB | ChEBI); agonist | ||||
Sequence: E |
GO annotations
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGamma-aminobutyric acid type B receptor subunit 1
- Short namesGABA-B receptor 1; GABA-B-R1; GABA-BR1; GABABR1; Gb1
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 accessionQ9WV18
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Postsynaptic cell membrane ; Multi-pass membrane protein
Note: Coexpression of GABBR1 and GABBR2 is required for GABBR1 maturation and transport to the plasma membrane. Colocalizes with ATF4 in hippocampal neuron dendritic membranes (By similarity).
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 20-590 | Extracellular | ||||
Sequence: QTPNVTSEGCQIIHPPWEGGIRYRGLTRDQVKAINFLPVDYEIEYVCRGEREVVGPKVRKCLANGSWTDMDTPSRCVRICSKSYLTLENGKVFLTGGDLPALDGARVDFRCDPDFHLVGSSRSICSQGQWSTPKPHCQVNRTPHSERRAVYIGALFPMSGGWPGGQACQPAVEMALEDVNSRRDILPDYELKLIHHDSKCDPGQATKYLYELLYNDPIKIILMPGCSSVSTLVAEAARMWNLIVLSYGSSSPALSNRQRFPTFFRTHPSATLHNPTRVKLFEKWGWKKIATIQQTTEVFTSTLDDLEERVKEAGIEITFRQSFFSDPAVPVKNLKRQDARIIVGLFYETEARKVFCEVYKERLFGKKYVWFLIGWYADNWFKTYDPSINCTVEEMTEAVEGHITTEIVMLNPANTRSISNMTSQEFVEKLTKRLKRHPEETGGFQEAPLAYDAIWALALALNKTSGGGGRSGVRLEDFNYNNQTITDQIYRAMNSSSFEGVSGHVVFDASGSRMAWTLIEQLQGGSYKKIGYYDSTKDDLSWSKTDKWIGGSPPADQTLVIKTFRFLSQKL | ||||||
Transmembrane | 591-611 | Helical; Name=1 | ||||
Sequence: FISVSVLSSLGIVLAVVCLSF | ||||||
Topological domain | 612-630 | Cytoplasmic | ||||
Sequence: NIYNSHVRYIQNSQPNLNN | ||||||
Transmembrane | 631-651 | Helical; Name=2 | ||||
Sequence: LTAVGCSLALAAVFPLGLDGY | ||||||
Topological domain | 652-666 | Extracellular | ||||
Sequence: HIGRSQFPFVCQARL | ||||||
Transmembrane | 667-687 | Helical; Name=3 | ||||
Sequence: WLLGLGFSLGYGSMFTKIWWV | ||||||
Topological domain | 688-709 | Cytoplasmic | ||||
Sequence: HTVFTKKEEKKEWRKTLEPWKL | ||||||
Transmembrane | 710-730 | Helical; Name=4 | ||||
Sequence: YATVGLLVGMDILTLAIWQIV | ||||||
Topological domain | 731-767 | Extracellular | ||||
Sequence: DPLHRTIETFAKEEPKEDIDVSILPQLEHCSSKKMNT | ||||||
Transmembrane | 768-788 | Helical; Name=5 | ||||
Sequence: WLGIFYGYKGLLLLLGIFLAY | ||||||
Topological domain | 789-803 | Cytoplasmic | ||||
Sequence: ETKSVSTEKINDHRA | ||||||
Transmembrane | 804-824 | Helical; Name=6 | ||||
Sequence: VGMAIYNVAVLCLITAPVTMI | ||||||
Topological domain | 825-832 | Extracellular | ||||
Sequence: LSSQQDAA | ||||||
Transmembrane | 833-853 | Helical; Name=7 | ||||
Sequence: FAFASLAIVFSSYITLVVLFV | ||||||
Topological domain | 854-960 | Cytoplasmic | ||||
Sequence: PKMRRLITRGEWQSEAQDTMKTGSSTNNNEEEKSRLLEKENRELEKIIAEKEERVSELRHQLQSRQQIRSRRHPPTPPDPSGGLPRGPSEPPDRLSCDGSRVHLLYK |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, glycosylation, disulfide bond, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-19 | |||||
Sequence: MLLLLLVPLFLRPLGAGGA | ||||||
Chain | PRO_0000012950 | 20-960 | Gamma-aminobutyric acid type B receptor subunit 1 | |||
Sequence: QTPNVTSEGCQIIHPPWEGGIRYRGLTRDQVKAINFLPVDYEIEYVCRGEREVVGPKVRKCLANGSWTDMDTPSRCVRICSKSYLTLENGKVFLTGGDLPALDGARVDFRCDPDFHLVGSSRSICSQGQWSTPKPHCQVNRTPHSERRAVYIGALFPMSGGWPGGQACQPAVEMALEDVNSRRDILPDYELKLIHHDSKCDPGQATKYLYELLYNDPIKIILMPGCSSVSTLVAEAARMWNLIVLSYGSSSPALSNRQRFPTFFRTHPSATLHNPTRVKLFEKWGWKKIATIQQTTEVFTSTLDDLEERVKEAGIEITFRQSFFSDPAVPVKNLKRQDARIIVGLFYETEARKVFCEVYKERLFGKKYVWFLIGWYADNWFKTYDPSINCTVEEMTEAVEGHITTEIVMLNPANTRSISNMTSQEFVEKLTKRLKRHPEETGGFQEAPLAYDAIWALALALNKTSGGGGRSGVRLEDFNYNNQTITDQIYRAMNSSSFEGVSGHVVFDASGSRMAWTLIEQLQGGSYKKIGYYDSTKDDLSWSKTDKWIGGSPPADQTLVIKTFRFLSQKLFISVSVLSSLGIVLAVVCLSFNIYNSHVRYIQNSQPNLNNLTAVGCSLALAAVFPLGLDGYHIGRSQFPFVCQARLWLLGLGFSLGYGSMFTKIWWVHTVFTKKEEKKEWRKTLEPWKLYATVGLLVGMDILTLAIWQIVDPLHRTIETFAKEEPKEDIDVSILPQLEHCSSKKMNTWLGIFYGYKGLLLLLGIFLAYETKSVSTEKINDHRAVGMAIYNVAVLCLITAPVTMILSSQQDAAFAFASLAIVFSSYITLVVLFVPKMRRLITRGEWQSEAQDTMKTGSSTNNNEEEKSRLLEKENRELEKIIAEKEERVSELRHQLQSRQQIRSRRHPPTPPDPSGGLPRGPSEPPDRLSCDGSRVHLLYK | ||||||
Glycosylation | 23 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 83 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 99↔144 | |||||
Sequence: CSKSYLTLENGKVFLTGGDLPALDGARVDFRCDPDFHLVGSSRSIC | ||||||
Disulfide bond | 130↔156 | |||||
Sequence: CDPDFHLVGSSRSICSQGQWSTPKPHC | ||||||
Disulfide bond | 219↔245 | |||||
Sequence: CDPGQATKYLYELLYNDPIKIILMPGC | ||||||
Disulfide bond | 375↔409 | |||||
Sequence: CEVYKERLFGKKYVWFLIGWYADNWFKTYDPSINC | ||||||
Glycosylation | 408 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 439 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 481 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 501 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 513 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 872 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 929 | Phosphothreonine | ||||
Sequence: T |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in neuronal tissue including cortex, cerebellum and spinal cord. Not detected in non-neuronal tissues including heart, liver, spleen and kidney.
Gene expression databases
Interaction
Subunit
Heterodimer of GABBR1 and GABBR2 (PubMed:10075644, PubMed:10773016, PubMed:9872744).
Homodimers may form, but are inactive (By similarity).
Interacts (via C-terminus) with ATF4 (via leucine zipper domain) (By similarity).
Interacts with JAKMIP1 (PubMed:14718537).
Interacts with KCTD8, KCTD12, KCTD12B and KCTD16; this interaction determines the pharmacology and kinetics of the receptor response, the KCTD proteins markedly accelerating the GABA-B response, although to different extents (PubMed:20400944).
Homodimers may form, but are inactive (By similarity).
Interacts (via C-terminus) with ATF4 (via leucine zipper domain) (By similarity).
Interacts with JAKMIP1 (PubMed:14718537).
Interacts with KCTD8, KCTD12, KCTD12B and KCTD16; this interaction determines the pharmacology and kinetics of the receptor response, the KCTD proteins markedly accelerating the GABA-B response, although to different extents (PubMed:20400944).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, compositional bias, region, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 29-95 | Sushi 1 | ||||
Sequence: CQIIHPPWEGGIRYRGLTRDQVKAINFLPVDYEIEYVCRGEREVVGPKVRKCLANGSWTDMDTPSRC | ||||||
Domain | 97-158 | Sushi 2 | ||||
Sequence: RICSKSYLTLENGKVFLTGGDLPALDGARVDFRCDPDFHLVGSSRSICSQGQWSTPKPHCQV | ||||||
Compositional bias | 866-883 | Polar residues | ||||
Sequence: QSEAQDTMKTGSSTNNNE | ||||||
Region | 866-891 | Disordered | ||||
Sequence: QSEAQDTMKTGSSTNNNEEEKSRLLE | ||||||
Coiled coil | 868-924 | |||||
Sequence: EAQDTMKTGSSTNNNEEEKSRLLEKENRELEKIIAEKEERVSELRHQLQSRQQIRSR | ||||||
Region | 887-915 | Interaction with ATF4 | ||||
Sequence: SRLLEKENRELEKIIAEKEERVSELRHQL | ||||||
Region | 908-960 | Disordered | ||||
Sequence: VSELRHQLQSRQQIRSRRHPPTPPDPSGGLPRGPSEPPDRLSCDGSRVHLLYK | ||||||
Compositional bias | 926-940 | Pro residues | ||||
Sequence: HPPTPPDPSGGLPRG |
Domain
Alpha-helical parts of the C-terminal intracellular region mediate heterodimeric interaction with GABBR2. The linker region between the transmembrane domain 3 (TM3) and the transmembrane domain 4 (TM4) probably plays a role in the specificity for G-protein coupling.
Sequence similarities
Belongs to the G-protein coupled receptor 3 family. GABA-B receptor subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Protein family/group databases
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative splicing.
Q9WV18-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1A
- Length960
- Mass (Da)108,216
- Last updated1999-11-01 v1
- ChecksumE4B5A9401E23E8B4
Q9WV18-2
- Name1B
- Differences from canonical
- 1-163: MLLLLLVPLFLRPLGAGGAQTPNVTSEGCQIIHPPWEGGIRYRGLTRDQVKAINFLPVDYEIEYVCRGEREVVGPKVRKCLANGSWTDMDTPSRCVRICSKSYLTLENGKVFLTGGDLPALDGARVDFRCDPDFHLVGSSRSICSQGQWSTPKPHCQVNRTPH → MGPGGPCTPVGWPLPLLLVMAAGVAPVWASHSPHLPRPHPRVPPHPS
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_002041 | 1-163 | in isoform 1B | |||
Sequence: MLLLLLVPLFLRPLGAGGAQTPNVTSEGCQIIHPPWEGGIRYRGLTRDQVKAINFLPVDYEIEYVCRGEREVVGPKVRKCLANGSWTDMDTPSRCVRICSKSYLTLENGKVFLTGGDLPALDGARVDFRCDPDFHLVGSSRSICSQGQWSTPKPHCQVNRTPH → MGPGGPCTPVGWPLPLLLVMAAGVAPVWASHSPHLPRPHPRVPPHPS | ||||||
Sequence conflict | 7-8 | in Ref. 1; AAD22194 | ||||
Sequence: VP → LL | ||||||
Sequence conflict | 46 | in Ref. 1; AAD22194 | ||||
Sequence: T → I | ||||||
Sequence conflict | 618 | in Ref. 1; AAD22194 | ||||
Sequence: V → A | ||||||
Sequence conflict | 642 | in Ref. 1; AAD22194 | ||||
Sequence: A → V | ||||||
Sequence conflict | 700 | in Ref. 4; AAH56990 | ||||
Sequence: W → R | ||||||
Sequence conflict | 721 | in Ref. 1; AAD22194 | ||||
Sequence: I → V | ||||||
Sequence conflict | 812 | in Ref. 2; AAG29338/AAG29341 | ||||
Sequence: A → P | ||||||
Compositional bias | 866-883 | Polar residues | ||||
Sequence: QSEAQDTMKTGSSTNNNE | ||||||
Sequence conflict | 869 | in Ref. 1; AAD22194 | ||||
Sequence: A → T | ||||||
Sequence conflict | 921 | in Ref. 1; AAD22194 | ||||
Sequence: I → L | ||||||
Compositional bias | 926-940 | Pro residues | ||||
Sequence: HPPTPPDPSGGLPRG |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF114168 EMBL· GenBank· DDBJ | AAD22194.2 EMBL· GenBank· DDBJ | mRNA | ||
AF008649 EMBL· GenBank· DDBJ | AAG29338.1 EMBL· GenBank· DDBJ | mRNA | ||
AF120255 EMBL· GenBank· DDBJ | AAG29341.1 EMBL· GenBank· DDBJ | mRNA | ||
AL078630 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC054735 EMBL· GenBank· DDBJ | AAH54735.1 EMBL· GenBank· DDBJ | mRNA | ||
BC056990 EMBL· GenBank· DDBJ | AAH56990.1 EMBL· GenBank· DDBJ | mRNA |