Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Gamma-aminobutyric acid type B receptor subunit 1 (GABA-B receptor 1) (GABA-B-R1) (GABA-BR1) (GABABR1) (Gb1)

 GABR1_RAT               Reviewed;         991 AA.
Q9Z0U4; O08620; O08621; Q9Z0F9; Q9Z308;
11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
25-OCT-2017, entry version 160.
RecName: Full=Gamma-aminobutyric acid type B receptor subunit 1;
Short=GABA-B receptor 1;
Short=GABA-B-R1;
Short=GABA-BR1;
Short=GABABR1;
Short=Gb1;
Flags: Precursor;
Name=Gabbr1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1A AND 1B), FUNCTION, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
STRAIN=RICO;
TISSUE=Brain cortex, and Cerebellum {ECO:0000303|PubMed:9069281};
PubMed=9069281; DOI=10.1038/386239a0;
Kaupmann K., Huggel K., Heid J., Flor P.J., Bischoff S., Mickel S.J.,
McMaster G., Angst C., Bittiger H., Froestl W., Bettler B.;
"Expression cloning of GABA(B) receptors uncovers similarity to
metabotropic glutamate receptors.";
Nature 386:239-246(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1C AND 1D), AND TISSUE
SPECIFICITY.
TISSUE=Cerebellum {ECO:0000303|PubMed:9875211};
PubMed=9875211; DOI=10.1006/bbrc.1998.9706;
Isomoto S., Kaibara M., Sakurai-Yamashita Y., Nagayama Y., Uezono Y.,
Yano K., Taniyama K.;
"Cloning and tissue distribution of novel splice variants of the rat
GABAB receptor.";
Biochem. Biophys. Res. Commun. 253:10-15(1998).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1E), ALTERNATIVE SPLICING
(ISOFORM 1E), FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
STRAIN=Wistar; TISSUE=Hippocampus {ECO:0000303|PubMed:10457184};
PubMed=10457184; DOI=10.1046/j.1460-9568.1999.00704.x;
Pfaff T., Malitschek B., Kaupmann K., Prezeau L., Pin J.-P.,
Bettler B., Karschin A.;
"Alternative splicing generates a novel isoform of the rat
metabotropic GABA(B)R1 receptor.";
Eur. J. Neurosci. 11:2874-2882(1999).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1A), AND FUNCTION.
TISSUE=Brain {ECO:0000303|PubMed:10075644};
PubMed=10075644; DOI=10.1074/jbc.274.12.7607;
Ng G.Y.K., Clark J., Coulombe N., Ethier N., Hebert T.E., Sullivan R.,
Kargman S., Chateauneuf A., Tsukamoto N., McDonald T., Whiting P.,
Mezey E., Johnson M.P., Liu Q., Kolakowski L.F. Jr., Evans J.F.,
Bonner T.I., O'Neill G.P.;
"Identification of a GABAB receptor subunit, gb2, required for
functional GABAB receptor activity.";
J. Biol. Chem. 274:7607-7610(1999).
[5]
FUNCTION, INTERACTION WITH GABBR2, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
TISSUE=Hypothalamus {ECO:0000303|PubMed:9872315};
PubMed=9872315; DOI=10.1038/25348;
Jones K.A., Borowsky B., Tamm J.A., Craig D.A., Durkin M.M., Dai M.,
Yao W.-J., Johnson M., Gunwaldsen C.A., Huang L.-Y., Tang C., Shen Q.,
Salon J.A., Morse K., Laz T., Smith K.E., Nagarathnam D., Noble S.A.,
Branchek T.A., Gerald C.;
"GABA(B) receptors function as a heteromeric assembly of the subunits
GABA(B)R1 and GABA(B)R2.";
Nature 396:674-679(1998).
[6]
FUNCTION, INTERACTION WITH GABBR2, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
TISSUE=Brain cortex, and Cerebellum {ECO:0000303|PubMed:9872317};
PubMed=9872317; DOI=10.1038/25360;
Kaupmann K., Malitschek B., Schuler V., Heid J., Froestl W., Beck P.,
Mosbacher J., Bischoff S., Kulik A., Shigemoto R., Karschin A.,
Bettler B.;
"GABA-B receptor subtypes assemble into functional heteromeric
complexes.";
Nature 396:683-687(1998).
[7]
TISSUE SPECIFICITY.
PubMed=10658574; DOI=10.1016/S0968-0896(99)00214-X;
Belley M., Sullivan R., Reeves A., Evans J.F., O'Neill G.P.,
Ng G.Y.K.;
"Synthesis of the nanomolar photoaffinity GABA(B) receptor ligand CGP
71872 reveals diversity in the tissue distribution of GABA(B) receptor
forms.";
Bioorg. Med. Chem. 7:2697-2704(1999).
[8]
FUNCTION, INTERACTION WITH GABBR2, TISSUE SPECIFICITY, AND
DEVELOPMENTAL STAGE.
PubMed=9872744; DOI=10.1126/science.283.5398.74;
Kuner R., Koehr G., Gruenewald S., Eisenhardt G., Bach A.,
Kornau H.-C.;
"Role of heteromer formation in GABAB receptor function.";
Science 283:74-77(1999).
[9]
TISSUE SPECIFICITY.
TISSUE=Brain cortex {ECO:0000303|PubMed:10727622};
PubMed=10727622; DOI=10.1016/S0006-8993(00)01958-2;
Clark J.A., Mezey E., Lam A.S., Bonner T.I.;
"Distribution of the GABA(B) receptor subunit gb2 in rat CNS.";
Brain Res. 860:41-52(2000).
[10]
FUNCTION, INTERACTION WITH ATF4, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=10924501; DOI=10.1074/jbc.M002727200;
Nehring R.B., Horikawa H.P.M., El Far O., Kneussel M.,
Brandstatter J.H., Stamm S., Wischmeyer E., Betz H., Karschin A.;
"The metabotropic GABAB receptor directly interacts with the
activating transcription factor 4.";
J. Biol. Chem. 275:35185-35191(2000).
[11]
FUNCTION, AND MUTAGENESIS OF SER-247; SER-268 AND SER-269.
PubMed=10692480;
Galvez T., Urwyler S., Prezeau L., Mosbacher J., Joly C.,
Malitschek B., Heid J., Brabet I., Froestl W., Bettler B.,
Kaupmann K., Pin J.-P.;
"Ca(2+) requirement for high-affinity gamma-aminobutyric acid (GABA)
binding at GABA(B) receptors: involvement of serine 269 of the
GABA(B)R1 subunit.";
Mol. Pharmacol. 57:419-426(2000).
[12]
INTERACTION WITH JAKMIP1, AND SUBCELLULAR LOCATION.
PubMed=14718537; DOI=10.1074/jbc.M311737200;
Couve A., Restituito S., Brandon J.M., Charles K.J., Bawagan H.,
Freeman K.B., Pangalos M.N., Calver A.R., Moss S.J.;
"Marlin-1, a novel RNA-binding protein associates with GABA
receptors.";
J. Biol. Chem. 279:13934-13943(2004).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-960, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[14]
STRUCTURE BY NMR OF 96-159, AND DISULFIDE BONDS.
PubMed=15304491; DOI=10.1074/jbc.M406540200;
Blein S., Ginham R., Uhrin D., Smith B.O., Soares D.C., Veltel S.,
McIlhinney R.A., White J.H., Barlow P.N.;
"Structural analysis of the complement control protein (CCP) modules
of GABA(B) receptor 1a: only one of the two CCP modules is compactly
folded.";
J. Biol. Chem. 279:48292-48306(2004).
-!- FUNCTION: Component of a heterodimeric G-protein coupled receptor
for GABA, formed by GABBR1 and GABBR2 (PubMed:9872315,
PubMed:9872317, PubMed:9872744). Within the heterodimeric GABA
receptor, only GABBR1 seems to bind agonists, while GABBR2
mediates coupling to G proteins (PubMed:9872317, PubMed:10658574).
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:9872315, PubMed:9872744,
PubMed:10924501). Signaling inhibits adenylate cyclase, stimulates
phospholipase A2, activates potassium channels, inactivates
voltage-dependent calcium-channels and modulates inositol
phospholipid hydrolysis (PubMed:9069281, PubMed:10457184,
PubMed:9872315, PubMed:9872744, PubMed:10924501, PubMed:10692480).
Calcium is required for high affinity binding to GABA
(PubMed:10692480). Plays a critical role in the fine-tuning of
inhibitory synaptic transmission (PubMed:9872744). 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:9872744,
PubMed:10924501, PubMed:10692480). Not only implicated in synaptic
inhibition but also in hippocampal long-term potentiation, slow
wave sleep, muscle relaxation and antinociception (By similarity).
{ECO:0000250|UniProtKB:Q9UBS5, ECO:0000269|PubMed:10075644,
ECO:0000269|PubMed:10457184, ECO:0000269|PubMed:10658574,
ECO:0000269|PubMed:10692480, ECO:0000269|PubMed:10924501,
ECO:0000269|PubMed:9069281, ECO:0000269|PubMed:9872315,
ECO:0000269|PubMed:9872744}.
-!- SUBUNIT: Heterodimer of GABBR1 and GABBR2 (PubMed:9872315,
PubMed:9872317, PubMed:9872744). Homodimers may form, but are
inactive (PubMed:9872317). Interacts (via C-terminus) with ATF4
(via leucine zipper domain) (PubMed:10924501). Interacts with
JAKMIP1 (PubMed:14718537). {ECO:0000269|PubMed:10924501,
ECO:0000269|PubMed:14718537, ECO:0000269|PubMed:9872315,
ECO:0000269|PubMed:9872317, ECO:0000269|PubMed:9872744}.
-!- INTERACTION:
O88871:Gabbr2; NbExp=8; IntAct=EBI-7090268, EBI-7090239;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10457184,
ECO:0000269|PubMed:14718537, ECO:0000269|PubMed:9069281,
ECO:0000269|PubMed:9872315}; Multi-pass membrane protein
{ECO:0000305}. Cell junction, synapse, postsynaptic cell membrane
{ECO:0000269|PubMed:10924501}; Multi-pass membrane protein
{ECO:0000305}. Cell projection, dendrite
{ECO:0000269|PubMed:10924501, ECO:0000269|PubMed:9872317}.
Perikaryon {ECO:0000269|PubMed:14718537}. Note=Coexpression of
GABBR1 and GABBR2 is required for GABBR1 maturation and transport
to the plasma membrane (PubMed:10457184). Colocalizes with ATF4 in
hippocampal neuron dendritic membranes (PubMed:10924501).
{ECO:0000269|PubMed:10924501, ECO:0000305|PubMed:10457184}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1E {ECO:0000312|RGD:621537}; Synonyms=1C
{ECO:0000303|PubMed:10457184};
IsoId=Q9Z0U4-1; Sequence=Displayed;
Name=1A;
IsoId=Q9Z0U4-2; Sequence=VSP_002045;
Name=1B;
IsoId=Q9Z0U4-3; Sequence=VSP_002044, VSP_002045;
Name=1C;
IsoId=Q9Z0U4-4; Sequence=VSP_002044;
Name=1D;
IsoId=Q9Z0U4-5; Sequence=VSP_002044, VSP_002045, VSP_002046;
-!- TISSUE SPECIFICITY: Ubiquitously expressed in tissues including
the forebrain, cerebellum, eye, atrium, ventricle, lung, stomach,
small intestine, colon, liver, spleen, kidney, urinary bladder and
skeletal muscle (PubMed:9875211). Expressed at low levels in
testis, and more highly in brain regions (PubMed:9069281).
Expression is high the brain regions including cerebral cortical
layers, with higher expression in VIb than in the II-V layers,
pyramidal CA1-CA3 cell layers and granular cell layers of the
hippocampus, granular cell layers of the dentate gyrus, including
the caudate, putamen, nucleus accumbens and olfactory tubercle,
the granular layer cell layers of the medial habenula, in the
cerebellum, predominantly in Purkinje cells, and in the granule
cell layer (PubMed:9069281, PubMed:9872315 PubMed:9872744,
PubMed:10727622). Also expressed in areas of the brain including
the medial geniculate nucleus, substantia nigra, pars compacta,
the ventral tegmental area, and in several thalamic, amygdaloid
and hypothalamic nuclei, such as the arcuate nucleus of the
hypothalamus and mammilary bodies of the hypothalamus
(PubMed:9069281, PubMed:9872744). Expressed in the amacrine cell
of the retina (PubMed:10924501). Isoform 1A: Expressed in the
brain, spinal cord, stomach, testis, adrenal gland, pituitary,
spleen and prostate (PubMed:10658574). Isoform 1B: Expressed in
the brain, spinal cord, stomach, testis, kidney and liver
(PubMed:10658574). Expressed in Isoform 1C: Ubiquitously expressed
(PubMed:9875211). Isoform 1D: Expressed in the forebrain,
cerebellum, eye, kidney and urinary bladder (PubMed:9875211).
Isoform 1E: Ubiquitously expressed with high expression the
pyramidal CA1-CA3 cell layers of the hippocampus, the granule cell
layers of the dentate gyrus and olfactory tubercle, the whole
cortex, and Purkinje cells of the cerebellum (PubMed:10457184).
Moderate expression in the granule cell layer of the cerebellum
(PubMed:10457184). {ECO:0000269|PubMed:10457184,
ECO:0000269|PubMed:10658574, ECO:0000269|PubMed:10727622,
ECO:0000269|PubMed:10924501, ECO:0000269|PubMed:9069281,
ECO:0000269|PubMed:9872315, ECO:0000269|PubMed:9872744,
ECO:0000269|PubMed:9875211}.
-!- DEVELOPMENTAL STAGE: At E17 during embryonic development, highly
expressed in brain regions including the striatum, olfactory bulb,
septal nuclei, lateral habenula, pyramidal CA1-CA2 cell layers of
the hippocampus and in the neuroepithelial cells of the
ventricular zone. On the day of birth, expressed in the regions of
the brain including hippocampus, thalamic nuclei, cortex and
cerebellum. {ECO:0000269|PubMed:9872744}.
-!- 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.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family.
GABA-B receptor subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; Y10369; CAA71398.1; -; mRNA.
EMBL; Y10370; CAA71399.1; -; mRNA.
EMBL; AB016160; BAA34708.1; -; mRNA.
EMBL; AB016161; BAA34709.1; -; mRNA.
EMBL; AF110797; AAD19656.1; -; Genomic_DNA.
EMBL; AF110796; AAD19656.1; JOINED; Genomic_DNA.
EMBL; AF110797; AAD19657.1; -; Genomic_DNA.
EMBL; AF110796; AAD19657.1; JOINED; Genomic_DNA.
EMBL; AF110797; AAD19658.1; -; Genomic_DNA.
EMBL; AF110796; AAD19658.1; JOINED; Genomic_DNA.
EMBL; AF110797; AAD19659.1; -; Genomic_DNA.
EMBL; AF110796; AAD19659.1; JOINED; Genomic_DNA.
RefSeq; NP_112290.2; NM_031028.3. [Q9Z0U4-2]
RefSeq; XP_006255941.1; XM_006255879.3. [Q9Z0U4-1]
UniGene; Rn.30059; -.
PDB; 1SRZ; NMR; -; A=96-159.
PDB; 1SS2; NMR; -; A=96-159.
PDBsum; 1SRZ; -.
PDBsum; 1SS2; -.
DisProt; DP00463; -.
ProteinModelPortal; Q9Z0U4; -.
SMR; Q9Z0U4; -.
BioGrid; 249557; 2.
CORUM; Q9Z0U4; -.
IntAct; Q9Z0U4; 2.
STRING; 10116.ENSRNOP00000047788; -.
BindingDB; Q9Z0U4; -.
ChEMBL; CHEMBL2753; -.
GuidetoPHARMACOLOGY; 240; -.
iPTMnet; Q9Z0U4; -.
PhosphoSitePlus; Q9Z0U4; -.
UniCarbKB; Q9Z0U4; -.
PaxDb; Q9Z0U4; -.
PRIDE; Q9Z0U4; -.
Ensembl; ENSRNOT00000051634; ENSRNOP00000047498; ENSRNOG00000000774. [Q9Z0U4-2]
Ensembl; ENSRNOT00000082545; ENSRNOP00000075630; ENSRNOG00000000774. [Q9Z0U4-5]
Ensembl; ENSRNOT00000084582; ENSRNOP00000075610; ENSRNOG00000000774. [Q9Z0U4-3]
Ensembl; ENSRNOT00000085050; ENSRNOP00000075181; ENSRNOG00000000774. [Q9Z0U4-4]
Ensembl; ENSRNOT00000088396; ENSRNOP00000072226; ENSRNOG00000000774. [Q9Z0U4-3]
GeneID; 81657; -.
KEGG; rno:81657; -.
UCSC; RGD:621537; rat. [Q9Z0U4-1]
CTD; 2550; -.
RGD; 621537; Gabbr1.
eggNOG; KOG1055; Eukaryota.
eggNOG; ENOG410XNN1; LUCA.
GeneTree; ENSGT00530000063129; -.
HOGENOM; HOG000016575; -.
HOVERGEN; HBG051688; -.
InParanoid; Q9Z0U4; -.
KO; K04615; -.
PhylomeDB; Q9Z0U4; -.
TreeFam; TF313965; -.
Reactome; R-RNO-1296041; Activation of G protein gated Potassium channels.
Reactome; R-RNO-418594; G alpha (i) signalling events.
Reactome; R-RNO-420499; Class C/3 (Metabotropic glutamate/pheromone receptors).
Reactome; R-RNO-977444; GABA B receptor activation.
Reactome; R-RNO-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
EvolutionaryTrace; Q9Z0U4; -.
PRO; PR:Q9Z0U4; -.
Proteomes; UP000002494; Chromosome 20.
Bgee; ENSRNOG00000000774; -.
ExpressionAtlas; Q9Z0U4; baseline and differential.
GO; GO:0030673; C:axolemma; IDA:RGD.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0043198; C:dendritic shaft; IDA:RGD.
GO; GO:0043197; C:dendritic spine; IDA:RGD.
GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:RGD.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0038039; C:G-protein coupled receptor heterodimeric complex; ISS:UniProtKB.
GO; GO:1902710; C:GABA receptor complex; IDA:CAFA.
GO; GO:0005887; C:integral component of plasma membrane; IDA:CAFA.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
GO; GO:0045121; C:membrane raft; IDA:RGD.
GO; GO:0031966; C:mitochondrial membrane; IDA:RGD.
GO; GO:0043005; C:neuron projection; IDA:RGD.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:0097060; C:synaptic membrane; IDA:CAFA.
GO; GO:0008021; C:synaptic vesicle; IDA:RGD.
GO; GO:1990430; F:extracellular matrix protein binding; IMP:CAFA.
GO; GO:0004965; F:G-protein coupled GABA receptor activity; IDA:RGD.
GO; GO:0046982; F:protein heterodimerization activity; IPI:CAFA.
GO; GO:0008134; F:transcription factor binding; IPI:RGD.
GO; GO:0007193; P:adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway; ISS:UniProtKB.
GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; ISS:UniProtKB.
GO; GO:0007194; P:negative regulation of adenylate cyclase activity; IDA:MGI.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:RGD.
GO; GO:0033602; P:negative regulation of dopamine secretion; IDA:RGD.
GO; GO:0032811; P:negative regulation of epinephrine secretion; IMP:RGD.
GO; GO:0014053; P:negative regulation of gamma-aminobutyric acid secretion; IMP:RGD.
GO; GO:0050805; P:negative regulation of synaptic transmission; IDA:RGD.
GO; GO:0001649; P:osteoblast differentiation; IMP:RGD.
GO; GO:0014049; P:positive regulation of glutamate secretion; IMP:RGD.
GO; GO:0060124; P:positive regulation of growth hormone secretion; IMP:RGD.
GO; GO:0030817; P:regulation of cAMP biosynthetic process; IDA:RGD.
GO; GO:0014048; P:regulation of glutamate secretion; IDA:RGD.
GO; GO:0045471; P:response to ethanol; IEP:RGD.
GO; GO:0035094; P:response to nicotine; IEP:RGD.
CDD; cd15291; 7tmC_GABA-B-R1; 1.
CDD; cd00033; CCP; 1.
InterPro; IPR001828; ANF_lig-bd_rcpt.
InterPro; IPR002455; GPCR3_GABA-B.
InterPro; IPR017978; GPCR_3_C.
InterPro; IPR002456; GPCR_3_GABA_rcpt_B1.
InterPro; IPR028082; Peripla_BP_I.
InterPro; IPR035976; Sushi/SCR/CCP_sf.
InterPro; IPR000436; Sushi_SCR_CCP_dom.
PANTHER; PTHR10519; PTHR10519; 1.
Pfam; PF00003; 7tm_3; 1.
Pfam; PF01094; ANF_receptor; 1.
Pfam; PF00084; Sushi; 1.
PRINTS; PR01177; GABAB1RECPTR.
SMART; SM00032; CCP; 2.
SUPFAM; SSF53822; SSF53822; 1.
SUPFAM; SSF57535; SSF57535; 2.
PROSITE; PS50259; G_PROTEIN_RECEP_F3_4; 1.
PROSITE; PS50923; SUSHI; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell junction; Cell membrane;
Cell projection; Coiled coil; Complete proteome; Disulfide bond;
G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein;
Postsynaptic cell membrane; Receptor; Reference proteome; Repeat;
Signal; Synapse; Transducer; Transmembrane; Transmembrane helix.
SIGNAL 1 16 {ECO:0000255}.
CHAIN 17 991 Gamma-aminobutyric acid type B receptor
subunit 1.
/FTId=PRO_0000012951.
TOPO_DOM 17 590 Extracellular. {ECO:0000255}.
TRANSMEM 591 611 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 612 630 Cytoplasmic. {ECO:0000255}.
TRANSMEM 631 651 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 652 666 Extracellular. {ECO:0000255}.
TRANSMEM 667 687 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 688 709 Cytoplasmic. {ECO:0000255}.
TRANSMEM 710 730 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 731 797 Extracellular. {ECO:0000255}.
TRANSMEM 798 818 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 819 834 Cytoplasmic. {ECO:0000255}.
TRANSMEM 835 855 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 856 863 Extracellular. {ECO:0000255}.
TRANSMEM 864 884 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 885 991 Cytoplasmic. {ECO:0000255}.
DOMAIN 29 95 Sushi 1. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 97 158 Sushi 2. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
REGION 918 946 Interaction with ATF4.
{ECO:0000269|PubMed:10924501}.
COILED 901 955 {ECO:0000255}.
BINDING 246 246 Agonist. {ECO:0000250}.
BINDING 269 269 Agonist. {ECO:0000250}.
BINDING 286 286 Agonist. {ECO:0000250}.
BINDING 366 366 Agonist. {ECO:0000250}.
BINDING 394 394 Agonist. {ECO:0000250}.
BINDING 465 465 Agonist. {ECO:0000250}.
MOD_RES 903 903 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9WV18}.
MOD_RES 960 960 Phosphothreonine.
{ECO:0000244|PubMed:22673903}.
CARBOHYD 23 23 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 83 83 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 408 408 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 439 439 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 481 481 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 501 501 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 513 513 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 99 144 {ECO:0000255|PROSITE-ProRule:PRU00302,
ECO:0000269|PubMed:15304491}.
DISULFID 130 156 {ECO:0000255|PROSITE-ProRule:PRU00302,
ECO:0000269|PubMed:15304491}.
DISULFID 219 245 {ECO:0000255|PROSITE-ProRule:PRU00302}.
DISULFID 375 409 {ECO:0000255|PROSITE-ProRule:PRU00302}.
VAR_SEQ 1 163 MLLLLLVPLFLRPLGAGGAQTPNATSEGCQIIHPPWEGGIR
YRGLTRDQVKAINFLPVDYEIEYVCRGEREVVGPKVRKCLA
NGSWTDMDTPSRCVRICSKSYLTLENGKVFLTGGDLPALDG
ARVEFRCDPDFHLVGSSRSVCSQGQWSTPKPHCQVNRTPH
-> MGPGGPCTPVGWPLPLLLVMAAGVAPVWASHSPHLPRP
HPRVPPHPS (in isoform 1B, isoform 1C and
isoform 1D). {ECO:0000303|PubMed:9069281,
ECO:0000303|PubMed:9875211}.
/FTId=VSP_002044.
VAR_SEQ 771 801 Missing (in isoform 1A, isoform 1B and
isoform 1D).
{ECO:0000303|PubMed:10075644,
ECO:0000303|PubMed:9069281,
ECO:0000303|PubMed:9875211}.
/FTId=VSP_002045.
VAR_SEQ 935 991 KEERVSELRHQLQSRQQLRSRRHPPTPPDPSGGLPRGPSEP
PDRLSCDGSRVHLLYK -> VCGDKQPGPPVSEGGLPVVGP
SIEV (in isoform 1D).
{ECO:0000303|PubMed:9875211}.
/FTId=VSP_002046.
MUTAGEN 247 247 S->A: No change in the affinity for GABA.
{ECO:0000269|PubMed:10692480}.
MUTAGEN 268 268 S->A: No change in the affinity for GABA.
{ECO:0000269|PubMed:10692480}.
MUTAGEN 269 269 S->A: Decrease in the affinity for GABA.
{ECO:0000269|PubMed:10692480}.
STRAND 96 98 {ECO:0000244|PDB:1SRZ}.
HELIX 101 104 {ECO:0000244|PDB:1SRZ}.
STRAND 109 112 {ECO:0000244|PDB:1SRZ}.
TURN 120 123 {ECO:0000244|PDB:1SRZ}.
STRAND 125 130 {ECO:0000244|PDB:1SRZ}.
STRAND 134 136 {ECO:0000244|PDB:1SRZ}.
STRAND 141 145 {ECO:0000244|PDB:1SRZ}.
STRAND 148 151 {ECO:0000244|PDB:1SRZ}.
STRAND 156 158 {ECO:0000244|PDB:1SRZ}.
SEQUENCE 991 AA; 111534 MW; 012CD293D4B444A2 CRC64;
MLLLLLVPLF LRPLGAGGAQ TPNATSEGCQ IIHPPWEGGI RYRGLTRDQV KAINFLPVDY
EIEYVCRGER EVVGPKVRKC LANGSWTDMD TPSRCVRICS KSYLTLENGK VFLTGGDLPA
LDGARVEFRC DPDFHLVGSS RSVCSQGQWS TPKPHCQVNR TPHSERRAVY IGALFPMSGG
WPGGQACQPA VEMALEDVNS RRDILPDYEL KLIHHDSKCD PGQATKYLYE LLYNDPIKII
LMPGCSSVST LVAEAARMWN LIVLSYGSSS PALSNRQRFP TFFRTHPSAT LHNPTRVKLF
EKWGWKKIAT IQQTTEVFTS TLDDLEERVK EAGIEITFRQ SFFSDPAVPV KNLKRQDARI
IVGLFYETEA RKVFCEVYKE RLFGKKYVWF LIGWYADNWF KTYDPSINCT VEEMTEAVEG
HITTEIVMLN PANTRSISNM TSQEFVEKLT KRLKRHPEET GGFQEAPLAY DAIWALALAL
NKTSGGGGRS GVRLEDFNYN NQTITDQIYR AMNSSSFEGV SGHVVFDASG SRMAWTLIEQ
LQGGSYKKIG YYDSTKDDLS WSKTDKWIGG SPPADQTLVI KTFRFLSQKL FISVSVLSSL
GIVLAVVCLS FNIYNSHVRY IQNSQPNLNN LTAVGCSLAL AAVFPLGLDG YHIGRSQFPF
VCQARLWLLG LGFSLGYGSM FTKIWWVHTV FTKKEEKKEW RKTLEPWKLY ATVGLLVGMD
VLTLAIWQIV DPLHRTIETF AKEEPKEDID VSILPQLEHC SSKKMNTWLG ELWSFAVSSD
VQRRATVGGD SPICVWPAPE SIFYGYKGLL LLLGIFLAYE TKSVSTEKIN DHRAVGMAIY
NVAVLCLITA PVTMILSSQQ DAAFAFASLA IVFSSYITLV VLFVPKMRRL ITRGEWQSET
QDTMKTGSST NNNEEEKSRL LEKENRELEK IIAEKEERVS ELRHQLQSRQ QLRSRRHPPT
PPDPSGGLPR GPSEPPDRLS CDGSRVHLLY K


Related products :

Catalog number Product name Quantity
U2151m CLIA GABA-B receptor 1,GABABR1,GABA-BR1,GABA-B-R1,Gabbr1,Gamma-aminobutyric acid type B receptor subunit 1,Gb1,Mouse,Mus musculus 96T
E2151r ELISA kit GABA-B receptor 1,GABABR1,GABA-BR1,GABA-B-R1,Gabbr1,Gamma-aminobutyric acid type B receptor subunit 1,Gb1,Rat,Rattus norvegicus 96T
U2151r CLIA GABA-B receptor 1,GABABR1,GABA-BR1,GABA-B-R1,Gabbr1,Gamma-aminobutyric acid type B receptor subunit 1,Gb1,Rat,Rattus norvegicus 96T
E2151m ELISA kit GABA-B receptor 1,GABABR1,GABA-BR1,GABA-B-R1,Gabbr1,Gamma-aminobutyric acid type B receptor subunit 1,Gb1,Mouse,Mus musculus 96T
E2151m ELISA GABA-B receptor 1,GABABR1,GABA-BR1,GABA-B-R1,Gabbr1,Gamma-aminobutyric acid type B receptor subunit 1,Gb1,Mouse,Mus musculus 96T
E2151r ELISA GABA-B receptor 1,GABABR1,GABA-BR1,GABA-B-R1,Gabbr1,Gamma-aminobutyric acid type B receptor subunit 1,Gb1,Rat,Rattus norvegicus 96T
U2151m CLIA kit GABA-B receptor 1,GABABR1,GABA-BR1,GABA-B-R1,Gabbr1,Gamma-aminobutyric acid type B receptor subunit 1,Gb1,Mouse,Mus musculus 96T
U2151r CLIA kit GABA-B receptor 1,GABABR1,GABA-BR1,GABA-B-R1,Gabbr1,Gamma-aminobutyric acid type B receptor subunit 1,Gb1,Rat,Rattus norvegicus 96T
E2151h ELISA GABA-B receptor 1,GABABR1,GABA-BR1,GABA-B-R1,GABBR1,Gamma-aminobutyric acid type B receptor subunit 1,Gb1,GPRC3A,Homo sapiens,Human 96T
E2151h ELISA kit GABA-B receptor 1,GABABR1,GABA-BR1,GABA-B-R1,GABBR1,Gamma-aminobutyric acid type B receptor subunit 1,Gb1,GPRC3A,Homo sapiens,Human 96T
U2151h CLIA kit GABA-B receptor 1,GABABR1,GABA-BR1,GABA-B-R1,GABBR1,Gamma-aminobutyric acid type B receptor subunit 1,Gb1,GPRC3A,Homo sapiens,Human 96T
U2151h CLIA GABA-B receptor 1,GABABR1,GABA-BR1,GABA-B-R1,GABBR1,Gamma-aminobutyric acid type B receptor subunit 1,Gb1,GPRC3A,Homo sapiens,Human 96T
18-001-30022 Gamma-aminobutyric acid type B receptor. subunit 2 - GABA-B receptor 2; GABA-B-R2; Gb2; GABABR2; G-protein coupled receptor 51 Polyclonal 0.1 mg
18-662-20062 Gamma-aminobutyric acid type B receptor. subunit 2 - GABA-B receptor 2; GABA-B-R2; Gb2; GABABR2; G-protein coupled receptor 51 Polyclonal 0.1 ml
27-228 GABRG2 is a gamma-aminobutyric acid (GABA) receptor. GABA is the major inhibitory neurotransmitter in the mammlian brain, where it acts at GABA-A receptors, which are ligand-gated chloride channels. G 0.05 mg
28-313 Gamma-aminobutyric acid (GABA), the major inhibitory neurotransmitter in the brain, mediates neuronal inhibition by binding to GABA receptors. The type A GABA receptors are pentameric chloride channel 0.1 mg
31-104 The gamma-aminobutyric acid (GABA) A receptor is a multisubunit chloride channel that mediates the fastest inhibitory synaptic transmission in the central nervous system. This gene encodes GABA A rece 0.1 mg
28-272 The gamma-aminobutyric acid (GABA) A receptor is a multisubunit chloride channel that mediates the fastest inhibitory synaptic transmission in the central nervous system. This gene encodes GABA A rece 0.1 mg
28-229 The gamma-aminobutyric acid (GABA) A receptor is a multisubunit chloride channel that mediates the fastest inhibitory synaptic transmission in the central nervous system. GABRB2 encodes GABA A recepto 0.05 mg
28-265 The gamma-aminobutyric acid (GABA) A receptor is a multisubunit chloride channel that mediates the fastest inhibitory synaptic transmission in the central nervous system. This gene encodes GABA A rece 0.05 mg
18-003-42956 Gamma-aminobutyric-acid receptor pi subunit - GABA(A) receptor Polyclonal 0.1 mg Protein A
18-003-42957 Gamma-aminobutyric-acid receptor pi subunit - GABA(A) receptor Polyclonal 0.1 mg Protein A
18-003-42955 Gamma-aminobutyric-acid receptor pi subunit - GABA(A) receptor Polyclonal 0.1 mg Protein A
18-003-42956 Gamma-aminobutyric-acid receptor pi subunit - GABA(A) receptor Polyclonal 0.05 mg Aff Pur
18-003-42955 Gamma-aminobutyric-acid receptor pi subunit - GABA(A) receptor Polyclonal 0.05 mg Aff Pur


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur