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O88871 (GABR2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Gamma-aminobutyric acid type B receptor subunit 2

Short name=GABA-B receptor 2
Short name=GABA-B-R2
Short name=GABA-BR2
Short name=GABABR2
Short name=Gb2
Alternative name(s):
G-protein coupled receptor 51
Gene names
Name:Gabbr2
Synonyms:Gpr51
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length940 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. 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. Ref.2

Subunit structure

Heterodimer of GABBR1 and GABBR2. Homodimers may form, but are inactive. Interacts with ATF4 via its C-terminal region. Ref.2 Ref.5 Ref.6

Subcellular location

Cell membrane; Multi-pass membrane protein. Cell junctionsynapsepostsynaptic cell membrane; Multi-pass membrane protein. 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. Ref.2

Tissue specificity

Expressed in brain cortex, hippocampus, medial habenula, thalamus and cerebellum. Coexpression is seen in cerebellum. Ref.2 Ref.3

Developmental stage

Abundant in brain cortex and cerebellum throughout postnatal development whereas its expression in spinal cord gradually decreases.

Domain

Alpha-helical parts of the C-terminal intracellular region mediate heterodimeric interaction with GABA-B receptor 1.

Sequence similarities

Belongs to the G-protein coupled receptor 3 family. GABA-B receptor subfamily.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Cacna1dP277326EBI-7090239,EBI-8072674
Gabbr1Q9Z0U48EBI-7090239,EBI-7090268

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4040 Potential
Chain41 – 940900Gamma-aminobutyric acid type B receptor subunit 2
PRO_0000012953

Regions

Topological domain41 – 482442Extracellular Potential
Transmembrane483 – 50321Helical; Name=1; Potential
Topological domain504 – 52118Cytoplasmic Potential
Transmembrane522 – 54221Helical; Name=2; Potential
Topological domain543 – 5508Extracellular Potential
Transmembrane551 – 57121Helical; Name=3; Potential
Topological domain572 – 59625Cytoplasmic Potential
Transmembrane597 – 61721Helical; Name=4; Potential
Topological domain618 – 65336Extracellular Potential
Transmembrane654 – 67421Helical; Name=5; Potential
Topological domain675 – 69016Cytoplasmic Potential
Transmembrane691 – 71121Helical; Name=6; Potential
Topological domain712 – 7198Extracellular Potential
Transmembrane720 – 74021Helical; Name=7; Potential
Topological domain741 – 940200Cytoplasmic Potential
Coiled coil780 – 81839 Potential

Amino acid modifications

Modified residue8831Phosphoserine By similarity
Glycosylation891N-linked (GlcNAc...) Potential
Glycosylation2971N-linked (GlcNAc...) Potential
Glycosylation3881N-linked (GlcNAc...) Potential
Glycosylation4031N-linked (GlcNAc...) Potential
Glycosylation4521N-linked (GlcNAc...) Potential
Disulfide bond107 ↔ 134 By similarity
Disulfide bond236 ↔ 265 By similarity
Disulfide bond264 ↔ 301 By similarity

Natural variations

Natural variant191P → PP. Ref.5
Natural variant191P → R.
Natural variant3371F → Y. Ref.5

Experimental info

Sequence conflict3431S → T in CAA09592. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O88871 [UniParc].

Last modified January 11, 2001. Version 2.
Checksum: 77BB42D833C7505D

FASTA940105,751
        10         20         30         40         50         60 
MASPPSSGQP RPPPPPPPPA RLLLPLLLSL LLWLAPGAWG WTRGAPRPPP SSPPLSIMGL 

        70         80         90        100        110        120 
MPLTKEVAKG SIGRGVLPAV ELAIEQIRNE SLLRPYFLDL RLYDTECDNA KGLKAFYDAI 

       130        140        150        160        170        180 
KYGPNHLMVF GGVCPSVTSI IAESLQGWNL VQLSFAATTP VLADKKKYPY FFRTVPSDNA 

       190        200        210        220        230        240 
VNPAILKLLK HFRWRRVGTL TQDVQRFSEV RNDLTGVLYG EDIEISDTES FSNDPCTSVK 

       250        260        270        280        290        300 
KLKGNDVRII LGQFDQNMAA KVFCCAFEES MFGSKYQWII PGWYEPAWWE QVHVEANSSR 

       310        320        330        340        350        360 
CLRRSLLAAM EGYIGVDFEP LSSKQIKTIS GKTPQQFERE YNSKRSGVGP SKFHGYAYDG 

       370        380        390        400        410        420 
IWVIAKTLQR AMETLHASSR HQRIQDFNYT DHTLGKIILN AMNETNFFGV TGQVVFRNGE 

       430        440        450        460        470        480 
RMGTIKFTQF QDSREVKVGE YNAVADTLEI INDTIRFQGS EPPKDKTIIL EQLRKISLPL 

       490        500        510        520        530        540 
YSILSALTIL GMIMASAFLF FNIKNRNQKL IKMSSPYMNN LIILGGMLSY ASIFLFGLDG 

       550        560        570        580        590        600 
SFVSEKTFET LCTVRTWILT VGYTTAFGAM FAKTWRVHAI FKNVKMKKKI IKDQKLLVIV 

       610        620        630        640        650        660 
GGMLLIDLCI LICWQAVDPL RRTVERYSME PDPAGRDISI RPLLEHCENT HMTIWLGIVY 

       670        680        690        700        710        720 
AYKGLLMLFG CFLAWETRNV SIPALNDSKY IGMSVYNVGI MCIIGAAVSF LTRDQPNVQF 

       730        740        750        760        770        780 
CIVALVIIFC STITLCLVFV PKLITLRTNP DAATQNRRFQ FTQNQKKEDS KTSTSVTSVN 

       790        800        810        820        830        840 
QASTSRLEGL QSENHRLRMK ITELDKDLEE VTMQLQDTPE KTTYIKQNHY QELNDILSLG 

       850        860        870        880        890        900 
NFTESTDGGK AILKNHLDQN PQLQWNTTEP SRTCKDPIED INSPEHIQRR LSLQLPILHH 

       910        920        930        940 
AYLPSIGGVD ASCVSPCVSP TASPRHRHVP PSFRVMVSGL 

« Hide

References

[1]"GABA(B) receptors function as a heteromeric assembly of the subunits GABA(B)R1 and GABA(B)R2."
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.
Nature 396:674-679(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Hypothalamus.
[2]"GABA-B receptor subtypes assemble into functional heteromeric complexes."
Kaupmann K., Malitschek B., Schuler V., Heid J., Froestl W., Beck P., Mosbacher J., Bischoff S., Kulik A., Shigemoto R., Karschin A., Bettler B.
Nature 396:683-687(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INTERACTION WITH GABBR1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Brain cortex and Cerebellum.
[3]"Distribution of the GABA(B) receptor subunit gb2 in rat CNS."
Clark J.A., Mezey E., Lam A.S., Bonner T.I.
Brain Res. 860:41-52(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Tissue: Brain cortex.
[4]Borowsky B., Laz T., Gerald C.
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Hypothalamus.
[5]"Role of heteromer formation in GABAB receptor function."
Kuner R., Koehr G., Gruenewald S., Eisenhardt G., Bach A., Kornau H.-C.
Science 283:74-77(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GABBR1, VARIANTS PRO-19 INS AND TYR-337.
Tissue: Hippocampus.
[6]"The metabotropic GABAB receptor directly interacts with the activating transcription factor 4."
Nehring R.B., Horikawa H.P.M., El Far O., Kneussel M., Brandstatter J.H., Stamm S., Wischmeyer E., Betz H., Karschin A.
J. Biol. Chem. 275:35185-35191(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATF4.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF074482 mRNA. Translation: AAD03335.1.
AJ011318 Genomic DNA. Translation: CAA09592.1.
AF058795 mRNA. Translation: AAC63994.1.
AF109405 mRNA. Translation: AAD03338.1.
RefSeqNP_113990.1. NM_031802.1.
UniGeneRn.162814.

3D structure databases

ProteinModelPortalO88871.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid249797. 2 interactions.
IntActO88871. 3 interactions.
MINTMINT-1889821.

Chemistry

BindingDBO88871.
ChEMBLCHEMBL2111474.
GuidetoPHARMACOLOGY241.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteO88871.

Proteomic databases

PaxDbO88871.
PRIDEO88871.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID83633.
KEGGrno:83633.
UCSCRGD:619864. rat.

Organism-specific databases

CTD9568.
RGD619864. Gabbr2.

Phylogenomic databases

eggNOGNOG273984.
HOGENOMHOG000112688.
HOVERGENHBG080355.
InParanoidO88871.
KOK04615.
PhylomeDBO88871.
TreeFamTF313965.

Gene expression databases

ArrayExpressO88871.
GenevestigatorO88871.

Family and domain databases

InterProIPR001828. ANF_lig-bd_rcpt.
IPR002455. GPCR3_GABA-B.
IPR000337. GPCR_3.
IPR017978. GPCR_3_C.
IPR017979. GPCR_3_CS.
IPR002457. GPCR_3_GABA_rcpt_B2.
IPR028082. Peripla_BP_I.
[Graphical view]
PANTHERPTHR10519. PTHR10519. 1 hit.
PfamPF00003. 7tm_3. 1 hit.
PF01094. ANF_receptor. 1 hit.
[Graphical view]
PRINTSPR01178. GABAB2RECPTR.
PR00248. GPCRMGR.
SUPFAMSSF53822. SSF53822. 1 hit.
PROSITEPS00981. G_PROTEIN_RECEP_F3_3. 1 hit.
PS50259. G_PROTEIN_RECEP_F3_4. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio616227.
PROO88871.

Entry information

Entry nameGABR2_RAT
AccessionPrimary (citable) accession number: O88871
Secondary accession number(s): Q9JK36, Q9QWU2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: January 11, 2001
Last modified: July 9, 2014
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries