Q9WV18 · GABR1_MOUSE

  • Protein
    Gamma-aminobutyric acid type B receptor subunit 1
  • Gene
    Gabbr1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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).

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site2464-aminobutanoate (UniProtKB | ChEBI); agonist
Binding site2694-aminobutanoate (UniProtKB | ChEBI); agonist
Binding site2864-aminobutanoate (UniProtKB | ChEBI); agonist
Binding site3664-aminobutanoate (UniProtKB | ChEBI); agonist
Binding site4654-aminobutanoate (UniProtKB | ChEBI); agonist

GO annotations

AspectTerm
Cellular Componentaxolemma
Cellular Componentcytoplasm
Cellular Componentdendritic shaft
Cellular Componentdendritic spine
Cellular Componentendoplasmic reticulum membrane
Cellular Componentextracellular space
Cellular ComponentG protein-coupled GABA receptor complex
Cellular ComponentG protein-coupled receptor dimeric complex
Cellular ComponentG protein-coupled receptor heterodimeric complex
Cellular ComponentGABA receptor complex
Cellular ComponentGABA-ergic synapse
Cellular Componentglutamatergic synapse
Cellular Componentmembrane
Cellular Componentmitochondrial membrane
Cellular Componentneuronal cell body
Cellular Componentplasma membrane
Cellular Componentpostsynaptic membrane
Cellular Componentpresynapse
Cellular Componentpresynaptic membrane
Cellular ComponentSchaffer collateral - CA1 synapse
Cellular Componentsynaptic membrane
Cellular Componentsynaptic vesicle
Molecular Functionextracellular matrix protein binding
Molecular FunctionG protein-coupled GABA receptor activity
Molecular FunctionG protein-coupled neurotransmitter receptor activity involved in regulation of postsynaptic membrane potential
Molecular FunctionG protein-coupled neurotransmitter receptor activity involved in regulation of presynaptic membrane potential
Molecular Functionprotein heterodimerization activity
Biological Processadenylate cyclase-inhibiting G protein-coupled receptor signaling pathway
Biological Processgamma-aminobutyric acid signaling pathway
Biological Processnegative regulation of cell population proliferation
Biological Processnegative regulation of dopamine secretion
Biological Processnegative regulation of epinephrine secretion
Biological Processnegative regulation of gamma-aminobutyric acid secretion
Biological Processnegative regulation of synaptic transmission
Biological Processneuron-glial cell signaling
Biological Processosteoblast differentiation
Biological Processpositive regulation of glutamate secretion
Biological Processpositive regulation of growth hormone secretion
Biological Processregulation of glutamate secretion
Biological Processresponse to ethanol
Biological Processresponse to nicotine
Biological Processsynaptic transmission, GABAergic

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Gamma-aminobutyric acid type B receptor subunit 1
  • Short names
    GABA-B receptor 1; GABA-B-R1; GABA-BR1; GABABR1; Gb1

Gene names

    • Name
      Gabbr1

Organism names

  • Taxonomic identifier
  • Strain
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q9WV18
  • Secondary accessions
    • Q6PGJ2
    • Q9WU48
    • Q9WV15
    • Q9WV16
    • Q9WV17

Proteomes

Organism-specific databases

Subcellular Location

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain20-590Extracellular
Transmembrane591-611Helical; Name=1
Topological domain612-630Cytoplasmic
Transmembrane631-651Helical; Name=2
Topological domain652-666Extracellular
Transmembrane667-687Helical; Name=3
Topological domain688-709Cytoplasmic
Transmembrane710-730Helical; Name=4
Topological domain731-767Extracellular
Transmembrane768-788Helical; Name=5
Topological domain789-803Cytoplasmic
Transmembrane804-824Helical; Name=6
Topological domain825-832Extracellular
Transmembrane833-853Helical; Name=7
Topological domain854-960Cytoplasmic

Keywords

PTM/Processing

Features

Showing features for signal, chain, glycosylation, disulfide bond, modified residue.

TypeIDPosition(s)Description
Signal1-19
ChainPRO_000001295020-960Gamma-aminobutyric acid type B receptor subunit 1
Glycosylation23N-linked (GlcNAc...) asparagine
Glycosylation83N-linked (GlcNAc...) asparagine
Disulfide bond99↔144
Disulfide bond130↔156
Disulfide bond219↔245
Disulfide bond375↔409
Glycosylation408N-linked (GlcNAc...) asparagine
Glycosylation439N-linked (GlcNAc...) asparagine
Glycosylation481N-linked (GlcNAc...) asparagine
Glycosylation501N-linked (GlcNAc...) asparagine
Glycosylation513N-linked (GlcNAc...) asparagine
Modified residue872Phosphothreonine
Modified residue929Phosphothreonine

Keywords

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).

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for domain, compositional bias, region, coiled coil.

TypeIDPosition(s)Description
Domain29-95Sushi 1
Domain97-158Sushi 2
Compositional bias866-883Polar residues
Region866-891Disordered
Coiled coil868-924
Region887-915Interaction with ATF4
Region908-960Disordered
Compositional bias926-940Pro residues

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

Keywords

Phylogenomic databases

Family and domain databases

Protein family/group databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete
  • Sequence processing
    The 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.

  • Length
    960
  • Mass (Da)
    108,216
  • Last updated
    1999-11-01 v1
  • Checksum
    E4B5A9401E23E8B4
MLLLLLVPLFLRPLGAGGAQTPNVTSEGCQIIHPPWEGGIRYRGLTRDQVKAINFLPVDYEIEYVCRGEREVVGPKVRKCLANGSWTDMDTPSRCVRICSKSYLTLENGKVFLTGGDLPALDGARVDFRCDPDFHLVGSSRSICSQGQWSTPKPHCQVNRTPHSERRAVYIGALFPMSGGWPGGQACQPAVEMALEDVNSRRDILPDYELKLIHHDSKCDPGQATKYLYELLYNDPIKIILMPGCSSVSTLVAEAARMWNLIVLSYGSSSPALSNRQRFPTFFRTHPSATLHNPTRVKLFEKWGWKKIATIQQTTEVFTSTLDDLEERVKEAGIEITFRQSFFSDPAVPVKNLKRQDARIIVGLFYETEARKVFCEVYKERLFGKKYVWFLIGWYADNWFKTYDPSINCTVEEMTEAVEGHITTEIVMLNPANTRSISNMTSQEFVEKLTKRLKRHPEETGGFQEAPLAYDAIWALALALNKTSGGGGRSGVRLEDFNYNNQTITDQIYRAMNSSSFEGVSGHVVFDASGSRMAWTLIEQLQGGSYKKIGYYDSTKDDLSWSKTDKWIGGSPPADQTLVIKTFRFLSQKLFISVSVLSSLGIVLAVVCLSFNIYNSHVRYIQNSQPNLNNLTAVGCSLALAAVFPLGLDGYHIGRSQFPFVCQARLWLLGLGFSLGYGSMFTKIWWVHTVFTKKEEKKEWRKTLEPWKLYATVGLLVGMDILTLAIWQIVDPLHRTIETFAKEEPKEDIDVSILPQLEHCSSKKMNTWLGIFYGYKGLLLLLGIFLAYETKSVSTEKINDHRAVGMAIYNVAVLCLITAPVTMILSSQQDAAFAFASLAIVFSSYITLVVLFVPKMRRLITRGEWQSEAQDTMKTGSSTNNNEEEKSRLLEKENRELEKIIAEKEERVSELRHQLQSRQQIRSRRHPPTPPDPSGGLPRGPSEPPDRLSCDGSRVHLLYK

Q9WV18-2

  • Name
    1B
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 1-163: MLLLLLVPLFLRPLGAGGAQTPNVTSEGCQIIHPPWEGGIRYRGLTRDQVKAINFLPVDYEIEYVCRGEREVVGPKVRKCLANGSWTDMDTPSRCVRICSKSYLTLENGKVFLTGGDLPALDGARVDFRCDPDFHLVGSSRSICSQGQWSTPKPHCQVNRTPH → MGPGGPCTPVGWPLPLLLVMAAGVAPVWASHSPHLPRPHPRVPPHPS

Computationally mapped potential isoform sequences

There are 3 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
Q3TWR2Q3TWR2_MOUSEGabbr1229
G3UZ52G3UZ52_MOUSEGabbr1213
G3UXR6G3UXR6_MOUSEGabbr1177

Features

Showing features for alternative sequence, sequence conflict, compositional bias.

TypeIDPosition(s)Description
Alternative sequenceVSP_0020411-163in isoform 1B
Sequence conflict7-8in Ref. 1; AAD22194
Sequence conflict46in Ref. 1; AAD22194
Sequence conflict618in Ref. 1; AAD22194
Sequence conflict642in Ref. 1; AAD22194
Sequence conflict700in Ref. 4; AAH56990
Sequence conflict721in Ref. 1; AAD22194
Sequence conflict812in Ref. 2; AAG29338/AAG29341
Compositional bias866-883Polar residues
Sequence conflict869in Ref. 1; AAD22194
Sequence conflict921in Ref. 1; AAD22194
Compositional bias926-940Pro residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

Disclaimer

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