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Gamma-aminobutyric acid type B receptor subunit 2 (GABA-B receptor 2) (GABA-B-R2) (GABA-BR2) (GABABR2) (Gb2) (G-protein coupled receptor 51) (HG20)

 GABR2_HUMAN             Reviewed;         941 AA.
O75899; O75974; O75975; Q5VXZ2; Q8WX04; Q9P1R2; Q9UNR1; Q9UNS9;
11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
25-OCT-2017, entry version 170.
RecName: Full=Gamma-aminobutyric acid type B receptor subunit 2;
Short=GABA-B receptor 2;
Short=GABA-B-R2;
Short=GABA-BR2;
Short=GABABR2;
Short=Gb2;
AltName: Full=G-protein coupled receptor 51;
AltName: Full=HG20;
Flags: Precursor;
Name=GABBR2; Synonyms=GPR51, GPRC3B;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, INTERACTION WITH
GABBR1, AND SUBCELLULAR LOCATION.
TISSUE=Cerebellum {ECO:0000303|PubMed:9872316};
PubMed=9872316; DOI=10.1038/25354;
White J.H., Wise A., Main M.J., Green A., Fraser N.J., Disney G.H.,
Barnes A.A., Emson P., Foord S.M., Marshall F.H.;
"Heterodimerization is required for the formation of a functional
GABA(B) receptor.";
Nature 396:679-682(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Fetal brain {ECO:0000303|PubMed:10087195};
PubMed=10087195; DOI=10.1006/geno.1998.5706;
Ng G.Y.K., McDonald T., Bonnert T., Rigby M., Heavens R., Whiting P.,
Chateauneuf A., Coulombe N., Kargman S., Caskey T., Evans J.F.,
O'Neill G.P., Liu Q.;
"Cloning of a novel G-protein-coupled receptor GPR 51 resembling GABAB
receptors expressed predominantly in nervous tissues and mapped
proximal to the hereditary sensory neuropathy type 1 locus on
chromosome 9.";
Genomics 56:288-295(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND VARIANTS PHE-628 AND ALA-869.
TISSUE=Brain {ECO:0000303|PubMed:10328880};
PubMed=10328880; DOI=10.1006/mcne.1999.0741;
Martin S.C., Russek S.J., Farb D.H.;
"Molecular identification of the human GABABR2: cell surface
expression and coupling to adenylyl cyclase in the absence of
GABABR1.";
Mol. Cell. Neurosci. 13:180-191(1999).
[4]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Brain {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).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
Liu M., Parker R., McCrea K., Watson J., Baker E., Sutherland G.,
Herzog H.;
"Cloning and characterization of a novel human GABA-B receptor subtype
with high affinity for GABA and low affinity for baclofen.";
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Hippocampus {ECO:0000303|Ref.6};
Borowsky B., Laz T., Gerald C.;
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 14-941.
TISSUE=Hippocampus {ECO:0000303|PubMed:15489334};
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
FUNCTION.
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).
[10]
FUNCTION, INTERACTION WITH GABBR1, TISSUE SPECIFICITY, AND DOMAIN.
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).
[11]
FUNCTION, AND INTERACTION WITH GABBR1.
PubMed=10906333; DOI=10.1074/jbc.M005333200;
Schwarz D.A., Barry G., Eliasof S.D., Petroski R.E., Conlon P.J.,
Maki R.A.;
"Characterization of gamma-aminobutyric acid receptor GABAB(1e), a
GABAB(1) splice variant encoding a truncated receptor.";
J. Biol. Chem. 275:32174-32181(2000).
[12]
FUNCTION, AND INTERACTION WITH GABBR1.
PubMed=10773016;
Sullivan R., Chateauneuf A., Coulombe N., Kolakowski L.F. Jr.,
Johnson M.P., Hebert T.E., Ethier N., Belley M., Metters K.,
Abramovitz M., O'Neill G.P., Ng G.Y.K.;
"Coexpression of full-length gamma-aminobutyric acid(B) (GABA(B))
receptors with truncated receptors and metabotropic glutamate receptor
4 supports the GABA(B) heterodimer as the functional receptor.";
J. Pharmacol. Exp. Ther. 293:460-467(2000).
[13]
VARIANT THR-567.
PubMed=26740508; DOI=10.1136/jmedgenet-2015-103568;
Lopes F., Barbosa M., Ameur A., Soares G., de Sa J., Dias A.I.,
Oliveira G., Cabral P., Temudo T., Calado E., Cruz I.F., Vieira J.P.,
Oliveira R., Esteves S., Sauer S., Jonasson I., Syvaenen A.C.,
Gyllensten U., Pinto D., Maciel P.;
"Identification of novel genetic causes of Rett syndrome-like
phenotypes.";
J. Med. Genet. 53:190-199(2016).
[14]
FUNCTION, INTERACTION WITH GABBR1, SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=15617512; DOI=10.1042/BJ20041435;
Villemure J.F., Adam L., Bevan N.J., Gearing K., Chenier S.,
Bouvier M.;
"Subcellular distribution of GABA(B) receptor homo- and hetero-
dimers.";
Biochem. J. 388:47-55(2005).
[15]
FUNCTION, SUBUNIT, AND INTERACTION WITH GABBR1.
PubMed=18165688; DOI=10.1074/jbc.M705202200;
Nomura R., Suzuki Y., Kakizuka A., Jingami H.;
"Direct detection of the interaction between recombinant soluble
extracellular regions in the heterodimeric metabotropic gamma-
aminobutyric acid receptor.";
J. Biol. Chem. 283:4665-4673(2008).
[16]
X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 42-466, PARTIAL PROTEIN
SEQUENCE, FUNCTION, INTERACTION WITH GABBR1, MUTAGENESIS OF TYR-118,
GLYCOSYLATION AT ASN-90; ASN-389; ASN-404 AND ASN-453, AND DISULFIDE
BONDS.
PubMed=22660477; DOI=10.1038/nn.3133;
Geng Y., Xiong D., Mosyak L., Malito D.L., Kniazeff J., Chen Y.,
Burmakina S., Quick M., Bush M., Javitch J.A., Pin J.P., Fan Q.R.;
"Structure and functional interaction of the extracellular domain of
human GABA(B) receptor GBR2.";
Nat. Neurosci. 15:970-978(2012).
[17]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 42-466 IN COMPLEXES WITH
GABBR1; AGONISTS AND ANTAGONISTS, FUNCTION, SUBUNIT, GLYCOSYLATION AT
ASN-404, AND DISULFIDE BOND.
PubMed=24305054; DOI=10.1038/nature12725;
Geng Y., Bush M., Mosyak L., Wang F., Fan Q.R.;
"Structural mechanism of ligand activation in human GABA(B)
receptor.";
Nature 504:254-259(2013).
-!- FUNCTION: Component of a heterodimeric G-protein coupled receptor
for GABA, formed by GABBR1 and GABBR2 (PubMed:9872316,
PubMed:9872744, PubMed:15617512, PubMed:18165688, PubMed:22660477,
PubMed:24305054). Within the heterodimeric GABA receptor, only
GABBR1 seems to bind agonists, while GABBR2 mediates coupling to G
proteins (PubMed:18165688). 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, PubMed:24305054). Signaling inhibits adenylate
cyclase, stimulates phospholipase A2, activates potassium
channels, inactivates voltage-dependent calcium-channels and
modulates inositol phospholipid hydrolysis (PubMed:10075644,
PubMed:9872744, PubMed:10906333, PubMed:10773016). Plays a
critical role in the fine-tuning of inhibitory synaptic
transmission (PubMed:9872744, PubMed:22660477). 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:9872316,
PubMed:10075644, PubMed:9872744, PubMed:22660477). Not only
implicated in synaptic inhibition but also in hippocampal long-
term potentiation, slow wave sleep, muscle relaxation and
antinociception (Probable). {ECO:0000269|PubMed:10075644,
ECO:0000269|PubMed:10328880, ECO:0000269|PubMed:15617512,
ECO:0000269|PubMed:18165688, ECO:0000269|PubMed:22660477,
ECO:0000269|PubMed:24305054, ECO:0000269|PubMed:9872316,
ECO:0000269|PubMed:9872744, ECO:0000305}.
-!- SUBUNIT: Heterodimer of GABBR1 and GABBR2 (PubMed:9872316,
PubMed:9872744, PubMed:10906333, PubMed:10773016, PubMed:15617512,
PubMed:18165688, PubMed:22660477, PubMed:24305054). Homodimers may
form, but are inactive (PubMed:15617512). Interacts (via C-
terminus) with ATF4 (via leucine zipper domain) (By similarity).
{ECO:0000250|UniProtKB:Q9Z0U4, ECO:0000269|PubMed:10773016,
ECO:0000269|PubMed:15617512, ECO:0000269|PubMed:18165688,
ECO:0000269|PubMed:22660477, ECO:0000269|PubMed:24305054,
ECO:0000269|PubMed:9872316, ECO:0000269|PubMed:9872744}.
-!- INTERACTION:
Q9UBS5:GABBR1; NbExp=2; IntAct=EBI-715469, EBI-724156;
Q9UBS5-2:GABBR1; NbExp=3; IntAct=EBI-715469, EBI-16084001;
P46459:NSF; NbExp=4; IntAct=EBI-715469, EBI-712251;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10328880,
ECO:0000269|PubMed:15617512, ECO:0000269|PubMed:9872316}; Multi-
pass membrane protein {ECO:0000305}. Cell junction, synapse,
postsynaptic cell membrane {ECO:0000250|UniProtKB:O88871}; Multi-
pass membrane protein {ECO:0000305}. Note=Coexpression of GABBR1
and GABBR2 is required for GABBR1 maturation and transport to the
plasma membrane. In contrast, GABBR2 does not depend on GABBR1 for
transport to the cell membrane. {ECO:0000269|PubMed:15617512}.
-!- TISSUE SPECIFICITY: Highly expressed in brain, especially in
cerebral cortex, thalamus, hippocampus, frontal, occipital and
temporal lobe, occipital pole and cerebellum, followed by corpus
callosum, caudate nucleus, spinal cord, amygdala and medulla
(PubMed:10087195, PubMed:10328880, PubMed:10727622,
PubMed:9872744). Weakly expressed in heart, testis and skeletal
muscle (PubMed:10087195, PubMed:10727622).
{ECO:0000269|PubMed:10087195, ECO:0000269|PubMed:10328880,
ECO:0000269|PubMed:10727622, ECO:0000269|PubMed:9872744}.
-!- DOMAIN: Alpha-helical parts of the C-terminal intracellular region
mediate heterodimeric interaction with GABBR1.
{ECO:0000305|PubMed:9872744}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family.
GABA-B receptor subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH35071.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AJ012188; CAA09942.1; -; mRNA.
EMBL; AF069755; AAC99345.1; -; mRNA.
EMBL; AF099033; AAD45867.1; -; mRNA.
EMBL; AF056085; AAC63228.1; -; mRNA.
EMBL; AF095784; AAD30389.1; -; mRNA.
EMBL; AF074483; AAD03336.1; -; mRNA.
EMBL; AL445495; CAD13322.2; -; Genomic_DNA.
EMBL; AL353782; CAD13322.2; JOINED; Genomic_DNA.
EMBL; AL356282; CAD13322.2; JOINED; Genomic_DNA.
EMBL; AL591502; CAD13322.2; JOINED; Genomic_DNA.
EMBL; AL353782; CAH71298.1; -; Genomic_DNA.
EMBL; AL356282; CAH71298.1; JOINED; Genomic_DNA.
EMBL; AL445495; CAH71298.1; JOINED; Genomic_DNA.
EMBL; AL591502; CAH71298.1; JOINED; Genomic_DNA.
EMBL; AL356282; CAH72233.1; -; Genomic_DNA.
EMBL; AL353782; CAH72233.1; JOINED; Genomic_DNA.
EMBL; AL445495; CAH72233.1; JOINED; Genomic_DNA.
EMBL; AL591502; CAH72233.1; JOINED; Genomic_DNA.
EMBL; AL591502; CAI12581.1; -; Genomic_DNA.
EMBL; AL353782; CAI12581.1; JOINED; Genomic_DNA.
EMBL; AL356282; CAI12581.1; JOINED; Genomic_DNA.
EMBL; AL445495; CAI12581.1; JOINED; Genomic_DNA.
EMBL; BC035071; AAH35071.2; ALT_INIT; mRNA.
CCDS; CCDS6736.1; -.
RefSeq; NP_005449.5; NM_005458.7.
UniGene; Hs.198612; -.
PDB; 4F11; X-ray; 2.38 A; A=42-466.
PDB; 4F12; X-ray; 3.02 A; A=42-466.
PDB; 4MQE; X-ray; 2.35 A; B=42-466.
PDB; 4MQF; X-ray; 2.22 A; B=42-466.
PDB; 4MR7; X-ray; 2.15 A; B=42-466.
PDB; 4MR8; X-ray; 2.15 A; B=42-466.
PDB; 4MR9; X-ray; 2.35 A; B=42-466.
PDB; 4MRM; X-ray; 2.86 A; B=42-466.
PDB; 4MS1; X-ray; 2.25 A; B=42-466.
PDB; 4MS3; X-ray; 2.50 A; B=42-466.
PDB; 4MS4; X-ray; 1.90 A; B=42-466.
PDB; 4PAS; X-ray; 1.62 A; B=779-819.
PDBsum; 4F11; -.
PDBsum; 4F12; -.
PDBsum; 4MQE; -.
PDBsum; 4MQF; -.
PDBsum; 4MR7; -.
PDBsum; 4MR8; -.
PDBsum; 4MR9; -.
PDBsum; 4MRM; -.
PDBsum; 4MS1; -.
PDBsum; 4MS3; -.
PDBsum; 4MS4; -.
PDBsum; 4PAS; -.
ProteinModelPortal; O75899; -.
SMR; O75899; -.
BioGrid; 114938; 7.
CORUM; O75899; -.
DIP; DIP-42851N; -.
IntAct; O75899; 6.
MINT; MINT-1398863; -.
STRING; 9606.ENSP00000259455; -.
BindingDB; O75899; -.
ChEMBL; CHEMBL5034; -.
DrugBank; DB08891; Arbaclofen.
DrugBank; DB08892; Arbaclofen Placarbil.
DrugBank; DB00181; Baclofen.
DrugBank; DB05010; SGS742.
GuidetoPHARMACOLOGY; 241; -.
TCDB; 9.A.14.15.1; the g-protein-coupled receptor (gpcr) family.
iPTMnet; O75899; -.
PhosphoSitePlus; O75899; -.
BioMuta; GABBR2; -.
EPD; O75899; -.
PaxDb; O75899; -.
PeptideAtlas; O75899; -.
PRIDE; O75899; -.
DNASU; 9568; -.
Ensembl; ENST00000259455; ENSP00000259455; ENSG00000136928.
GeneID; 9568; -.
KEGG; hsa:9568; -.
UCSC; uc004ays.4; human.
CTD; 9568; -.
DisGeNET; 9568; -.
EuPathDB; HostDB:ENSG00000136928.5; -.
GeneCards; GABBR2; -.
HGNC; HGNC:4507; GABBR2.
HPA; HPA013820; -.
HPA; HPA031684; -.
MalaCards; GABBR2; -.
MIM; 607340; gene.
neXtProt; NX_O75899; -.
OpenTargets; ENSG00000136928; -.
PharmGKB; PA28896; -.
eggNOG; KOG1055; Eukaryota.
eggNOG; ENOG410XNN1; LUCA.
GeneTree; ENSGT00530000063129; -.
HOVERGEN; HBG080355; -.
InParanoid; O75899; -.
KO; K04615; -.
OMA; NWSRVGT; -.
OrthoDB; EOG091G01WG; -.
PhylomeDB; O75899; -.
TreeFam; TF313965; -.
Reactome; R-HSA-1296041; Activation of G protein gated Potassium channels.
Reactome; R-HSA-418594; G alpha (i) signalling events.
Reactome; R-HSA-420499; Class C/3 (Metabotropic glutamate/pheromone receptors).
Reactome; R-HSA-977444; GABA B receptor activation.
Reactome; R-HSA-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
ChiTaRS; GABBR2; human.
GeneWiki; GABBR2; -.
GenomeRNAi; 9568; -.
PRO; PR:O75899; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000136928; -.
CleanEx; HS_GABBR2; -.
ExpressionAtlas; O75899; baseline and differential.
Genevisible; O75899; HS.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
GO; GO:0038039; C:G-protein coupled receptor heterodimeric complex; IPI:UniProtKB.
GO; GO:1902710; C:GABA receptor complex; IDA:CAFA.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0043005; C:neuron projection; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:0004965; F:G-protein coupled GABA receptor activity; TAS:ProtInc.
GO; GO:0046982; F:protein heterodimerization activity; IPI:CAFA.
GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:ProtInc.
GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IDA:UniProtKB.
GO; GO:0007194; P:negative regulation of adenylate cyclase activity; TAS:ProtInc.
CDD; cd15294; 7tmC_GABA-B-R2; 1.
InterPro; IPR001828; ANF_lig-bd_rcpt.
InterPro; IPR002455; GPCR3_GABA-B.
InterPro; IPR000337; GPCR_3.
InterPro; IPR017978; GPCR_3_C.
InterPro; IPR017979; GPCR_3_CS.
InterPro; IPR002457; GPCR_3_GABA_rcpt_B2.
InterPro; IPR028082; Peripla_BP_I.
PANTHER; PTHR10519; PTHR10519; 1.
Pfam; PF00003; 7tm_3; 1.
Pfam; PF01094; ANF_receptor; 1.
PRINTS; PR01178; GABAB2RECPTR.
PRINTS; PR00248; GPCRMGR.
SUPFAM; SSF53822; SSF53822; 1.
PROSITE; PS00981; G_PROTEIN_RECEP_F3_3; 1.
PROSITE; PS50259; G_PROTEIN_RECEP_F3_4; 1.
1: Evidence at protein level;
3D-structure; Cell junction; Cell membrane; Coiled coil;
Complete proteome; Direct protein sequencing; Disulfide bond;
G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein;
Polymorphism; Postsynaptic cell membrane; Receptor;
Reference proteome; Signal; Synapse; Transducer; Transmembrane;
Transmembrane helix.
SIGNAL 1 41 {ECO:0000255}.
CHAIN 42 941 Gamma-aminobutyric acid type B receptor
subunit 2.
/FTId=PRO_0000012952.
TOPO_DOM 42 483 Extracellular. {ECO:0000255}.
TRANSMEM 484 504 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 505 522 Cytoplasmic. {ECO:0000255}.
TRANSMEM 523 543 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 544 551 Extracellular. {ECO:0000255}.
TRANSMEM 552 572 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 573 597 Cytoplasmic. {ECO:0000255}.
TRANSMEM 598 618 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 619 654 Extracellular. {ECO:0000255}.
TRANSMEM 655 675 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 676 691 Cytoplasmic. {ECO:0000255}.
TRANSMEM 692 712 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 713 720 Extracellular. {ECO:0000255}.
TRANSMEM 721 741 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 742 941 Cytoplasmic. {ECO:0000255}.
COILED 781 819 {ECO:0000255}.
MOD_RES 776 776 Phosphoserine.
{ECO:0000250|UniProtKB:Q80T41}.
MOD_RES 779 779 Phosphoserine.
{ECO:0000250|UniProtKB:Q80T41}.
MOD_RES 819 819 Phosphothreonine.
{ECO:0000250|UniProtKB:Q80T41}.
MOD_RES 884 884 Phosphoserine.
{ECO:0000250|UniProtKB:Q80T41}.
MOD_RES 893 893 Phosphoserine.
{ECO:0000250|UniProtKB:Q80T41}.
MOD_RES 913 913 Phosphoserine.
{ECO:0000250|UniProtKB:Q80T41}.
MOD_RES 916 916 Phosphoserine.
{ECO:0000250|UniProtKB:Q80T41}.
MOD_RES 920 920 Phosphoserine.
{ECO:0000250|UniProtKB:Q80T41}.
MOD_RES 924 924 Phosphoserine.
{ECO:0000250|UniProtKB:Q80T41}.
CARBOHYD 90 90 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:22660477}.
CARBOHYD 298 298 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 389 389 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:22660477}.
CARBOHYD 404 404 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:22660477,
ECO:0000269|PubMed:24305054}.
CARBOHYD 453 453 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:22660477}.
DISULFID 108 135
DISULFID 237 266
DISULFID 265 302
VARIANT 163 163 L -> P (in dbSNP:rs35449008).
/FTId=VAR_049280.
VARIANT 567 567 A -> T (found in a patient with Rett
syndrome-like phenotype; unknown
pathological significance).
{ECO:0000269|PubMed:26740508}.
/FTId=VAR_079029.
VARIANT 628 628 Y -> F. {ECO:0000269|PubMed:10328880}.
/FTId=VAR_010148.
VARIANT 869 869 T -> A (in dbSNP:rs10985765).
{ECO:0000269|PubMed:10328880}.
/FTId=VAR_010149.
MUTAGEN 118 118 Y->A: Impairs interaction with GABBR1.
Decreases signaling via G-proteins.
{ECO:0000269|PubMed:22660477}.
CONFLICT 6 6 S -> R (in Ref. 2; AAC99345).
{ECO:0000305}.
CONFLICT 12 12 P -> R (in Ref. 2; AAC99345).
{ECO:0000305}.
CONFLICT 424 424 G -> E (in Ref. 5; AAD30389).
{ECO:0000305}.
CONFLICT 797 797 R -> H (in Ref. 8; AAH35071).
{ECO:0000305}.
STRAND 55 62 {ECO:0000244|PDB:4MS4}.
STRAND 66 68 {ECO:0000244|PDB:4MQE}.
HELIX 71 90 {ECO:0000244|PDB:4MS4}.
TURN 91 96 {ECO:0000244|PDB:4MS4}.
STRAND 98 105 {ECO:0000244|PDB:4MS4}.
HELIX 110 123 {ECO:0000244|PDB:4MS4}.
STRAND 128 132 {ECO:0000244|PDB:4MS4}.
HELIX 136 145 {ECO:0000244|PDB:4MS4}.
HELIX 146 149 {ECO:0000244|PDB:4MS4}.
STRAND 152 157 {ECO:0000244|PDB:4MS4}.
HELIX 161 164 {ECO:0000244|PDB:4MS4}.
TURN 166 168 {ECO:0000244|PDB:4MS4}.
STRAND 172 176 {ECO:0000244|PDB:4MS4}.
HELIX 179 181 {ECO:0000244|PDB:4MS4}.
HELIX 182 192 {ECO:0000244|PDB:4MS4}.
STRAND 197 205 {ECO:0000244|PDB:4MS4}.
HELIX 206 219 {ECO:0000244|PDB:4MS4}.
TURN 220 223 {ECO:0000244|PDB:4MS4}.
STRAND 225 234 {ECO:0000244|PDB:4MS4}.
HELIX 237 245 {ECO:0000244|PDB:4MS4}.
STRAND 250 254 {ECO:0000244|PDB:4MS4}.
HELIX 257 269 {ECO:0000244|PDB:4MS4}.
STRAND 278 283 {ECO:0000244|PDB:4MS4}.
TURN 287 290 {ECO:0000244|PDB:4MS4}.
HELIX 304 311 {ECO:0000244|PDB:4MS4}.
STRAND 315 319 {ECO:0000244|PDB:4MS4}.
HELIX 335 345 {ECO:0000244|PDB:4MS4}.
TURN 346 348 {ECO:0000244|PDB:4MR7}.
HELIX 355 372 {ECO:0000244|PDB:4MS4}.
HELIX 378 387 {ECO:0000244|PDB:4MS4}.
HELIX 393 404 {ECO:0000244|PDB:4MS4}.
STRAND 407 410 {ECO:0000244|PDB:4MS4}.
STRAND 413 418 {ECO:0000244|PDB:4MS4}.
STRAND 421 423 {ECO:0000244|PDB:4MS4}.
STRAND 425 431 {ECO:0000244|PDB:4MS4}.
STRAND 436 443 {ECO:0000244|PDB:4MS4}.
TURN 444 447 {ECO:0000244|PDB:4MS4}.
STRAND 448 451 {ECO:0000244|PDB:4MS4}.
TURN 453 455 {ECO:0000244|PDB:4MS4}.
STRAND 459 462 {ECO:0000244|PDB:4MS4}.
HELIX 780 816 {ECO:0000244|PDB:4PAS}.
SEQUENCE 941 AA; 105821 MW; 09F1773DB0673C5D CRC64;
MASPRSSGQP GPPPPPPPPP ARLLLLLLLP LLLPLAPGAW GWARGAPRPP PSSPPLSIMG
LMPLTKEVAK GSIGRGVLPA VELAIEQIRN ESLLRPYFLD LRLYDTECDN AKGLKAFYDA
IKYGPNHLMV FGGVCPSVTS IIAESLQGWN LVQLSFAATT PVLADKKKYP YFFRTVPSDN
AVNPAILKLL KHYQWKRVGT LTQDVQRFSE VRNDLTGVLY GEDIEISDTE SFSNDPCTSV
KKLKGNDVRI ILGQFDQNMA AKVFCCAYEE NMYGSKYQWI IPGWYEPSWW EQVHTEANSS
RCLRKNLLAA MEGYIGVDFE PLSSKQIKTI SGKTPQQYER EYNNKRSGVG PSKFHGYAYD
GIWVIAKTLQ RAMETLHASS RHQRIQDFNY TDHTLGRIIL NAMNETNFFG VTGQVVFRNG
ERMGTIKFTQ FQDSREVKVG EYNAVADTLE IINDTIRFQG SEPPKDKTII LEQLRKISLP
LYSILSALTI LGMIMASAFL FFNIKNRNQK LIKMSSPYMN NLIILGGMLS YASIFLFGLD
GSFVSEKTFE TLCTVRTWIL TVGYTTAFGA MFAKTWRVHA IFKNVKMKKK IIKDQKLLVI
VGGMLLIDLC ILICWQAVDP LRRTVEKYSM EPDPAGRDIS IRPLLEHCEN THMTIWLGIV
YAYKGLLMLF GCFLAWETRN VSIPALNDSK YIGMSVYNVG IMCIIGAAVS FLTRDQPNVQ
FCIVALVIIF CSTITLCLVF VPKLITLRTN PDAATQNRRF QFTQNQKKED SKTSTSVTSV
NQASTSRLEG LQSENHRLRM KITELDKDLE EVTMQLQDTP EKTTYIKQNH YQELNDILNL
GNFTESTDGG KAILKNHLDQ NPQLQWNTTE PSRTCKDPIE DINSPEHIQR RLSLQLPILH
HAYLPSIGGV DASCVSPCVS PTASPRHRHV PPSFRVMVSG L


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