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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.
30-AUG-2017, entry version 158.
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;
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;
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], AND ALTERNATIVE SPLICING (ISOFORM
1E).
STRAIN=Wistar; TISSUE=Hippocampus;
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 INTERACTION WITH GABBR2.
TISSUE=Brain;
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]
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).
[6]
INTERACTION WITH GABBR2.
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).
[7]
INTERACTION WITH ATF4, AND SUBCELLULAR LOCATION.
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).
[8]
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).
[9]
INTERACTION WITH JAKMIP1.
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).
[10]
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).
[11]
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. Within the heterodimeric
GABA receptor, only GABBR1 seems to bind agonists, while GABBR2
mediates coupling to G proteins. 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.
Signaling inhibits adenylate cyclase, stimulates phospholipase A2,
activates potassium channels, inactivates voltage-dependent
calcium-channels and modulates inositol phospholipid hydrolysis.
Calcium is required for high affinity binding to GABA. Plays a
critical role in the fine-tuning of inhibitory synaptic
transmission. 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. Not only implicated in synaptic
inhibition but also in hippocampal long-term potentiation, slow
wave sleep, muscle relaxation and antinociception.
{ECO:0000269|PubMed:9069281}.
-!- SUBUNIT: Heterodimer of GABBR1 and GABBR2. Homodimers may form,
but are inactive. Interacts with the leucine zipper of the C-
terminal bZIP domain of ATF4 via its C-terminal region. Interacts
with JAKMIP1. {ECO:0000269|PubMed:10075644,
ECO:0000269|PubMed:10924501, ECO:0000269|PubMed:14718537,
ECO:0000269|PubMed:9872744}.
-!- INTERACTION:
O88871:Gabbr2; NbExp=8; IntAct=EBI-7090268, EBI-7090239;
-!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
Cell junction, synapse, postsynaptic cell membrane; Multi-pass
membrane protein. Cell projection, dendrite. 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.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1E; Synonyms=1C;
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: Isoform 1A, isoform 1B and isoform 1C are
expressed in testis, stomach, spinal cord and brain including
cerebral cortical layers, pyramidal cell layers of the
hippocampus, granular cell layers of the dentate gyrus, basal
ganglia, cerebellum (predominantly in Purkinje cells followed by
granular layer). Isoform 1B is also expressed in kidney and liver.
Isoform 1D is expressed in forebrain, cerebellum, eye, kidney, and
urinary bladder. {ECO:0000269|PubMed:10658574,
ECO:0000269|PubMed:9069281, ECO:0000269|PubMed:9875211}.
-!- 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}.
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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.
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: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; IPR000436; Sushi_SCR_CCP_dom.
PANTHER; PTHR10519; PTHR10519; 1.
PANTHER; PTHR10519:SF50; PTHR10519:SF50; 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


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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


 

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