GABR2_MOUSE
ID GABR2_MOUSE Reviewed; 940 AA.
AC Q80T41; A2AL05;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Gamma-aminobutyric acid type B receptor subunit 2;
DE Short=GABA-B receptor 2;
DE Short=GABA-B-R2;
DE Short=GABA-BR2;
DE Short=GABABR2;
DE Short=Gb2;
DE AltName: Full=G-protein coupled receptor 51;
DE Flags: Precursor;
GN Name=Gabbr2; Synonyms=Gm425, Gpr51;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 869-940.
RX PubMed=12679517; DOI=10.1073/pnas.0230374100;
RA Vassilatis D.K., Hohmann J.G., Zeng H., Li F., Ranchalis J.E.,
RA Mortrud M.T., Brown A., Rodriguez S.S., Weller J.R., Wright A.C.,
RA Bergmann J.E., Gaitanaris G.A.;
RT "The G protein-coupled receptor repertoires of human and mouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:4903-4908(2003).
RN [3]
RP FUNCTION, AND INTERACTION WITH GABBR1.
RX PubMed=10075644; DOI=10.1074/jbc.274.12.7607;
RA Ng G.Y.K., Clark J., Coulombe N., Ethier N., Hebert T.E., Sullivan R.,
RA Kargman S., Chateauneuf A., Tsukamoto N., McDonald T., Whiting P.,
RA Mezey E., Johnson M.P., Liu Q., Kolakowski L.F. Jr., Evans J.F.,
RA Bonner T.I., O'Neill G.P.;
RT "Identification of a GABAB receptor subunit, gb2, required for functional
RT GABAB receptor activity.";
RL J. Biol. Chem. 274:7607-7610(1999).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-883, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-775; SER-778; THR-818;
RP SER-883; SER-892; SER-912; SER-915; SER-919 AND SER-923, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Component of a heterodimeric G-protein coupled receptor for
CC GABA, formed by GABBR1 and GABBR2 (PubMed:10075644). Within the
CC heterodimeric GABA receptor, only GABBR1 seems to bind agonists, while
CC GABBR2 mediates coupling to G proteins (By similarity). Ligand binding
CC causes a conformation change that triggers signaling via guanine
CC nucleotide-binding proteins (G proteins) and modulates the activity of
CC down-stream effectors, such as adenylate cyclase (PubMed:10075644).
CC Signaling inhibits adenylate cyclase, stimulates phospholipase A2,
CC activates potassium channels, inactivates voltage-dependent calcium-
CC channels and modulates inositol phospholipid hydrolysis
CC (PubMed:10075644). Plays a critical role in the fine-tuning of
CC inhibitory synaptic transmission (By similarity). Pre-synaptic GABA
CC receptor inhibits neurotransmitter release by down-regulating high-
CC voltage activated calcium channels, whereas postsynaptic GABA receptor
CC decreases neuronal excitability by activating a prominent inwardly
CC rectifying potassium (Kir) conductance that underlies the late
CC inhibitory postsynaptic potentials (PubMed:10075644). Not only
CC implicated in synaptic inhibition but also in hippocampal long-term
CC potentiation, slow wave sleep, muscle relaxation and antinociception
CC (By similarity). {ECO:0000250|UniProtKB:O75899,
CC ECO:0000269|PubMed:10075644}.
CC -!- SUBUNIT: Heterodimer of GABBR1 and GABBR2 (PubMed:10075644). Homodimers
CC may form, but are inactive (By similarity). Interacts (via C-terminus)
CC with ATF4 (via leucine zipper domain) (By similarity).
CC {ECO:0000250|UniProtKB:O88871, ECO:0000269|PubMed:10075644}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Postsynaptic cell membrane {ECO:0000250}; Multi-
CC pass membrane protein {ECO:0000250}. Note=Coexpression of GABBR1 and
CC GABBR2 is required for GABBR1 maturation and transport to the plasma
CC membrane. In contrast, GABBR2 does not depend on GABBR1 for transport
CC to the cell membrane (By similarity). {ECO:0000250}.
CC -!- DOMAIN: Alpha-helical parts of the C-terminal intracellular region
CC mediate heterodimeric interaction with GABBR1. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family. GABA-B
CC receptor subfamily. {ECO:0000305}.
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DR EMBL; AL772399; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL831741; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL844224; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX005247; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX571848; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY255605; AAO85117.1; -; mRNA.
DR CCDS; CCDS38758.1; -.
DR RefSeq; NP_001074610.1; NM_001081141.1.
DR AlphaFoldDB; Q80T41; -.
DR SMR; Q80T41; -.
DR BioGRID; 232404; 7.
DR ComplexPortal; CPX-2990; GABA-B receptor complex.
DR IntAct; Q80T41; 4.
DR MINT; Q80T41; -.
DR STRING; 10090.ENSMUSP00000103378; -.
DR GlyConnect; 2329; 3 N-Linked glycans (1 site).
DR GlyGen; Q80T41; 5 sites, 3 N-linked glycans (1 site).
DR iPTMnet; Q80T41; -.
DR PhosphoSitePlus; Q80T41; -.
DR MaxQB; Q80T41; -.
DR PaxDb; Q80T41; -.
DR PeptideAtlas; Q80T41; -.
DR PRIDE; Q80T41; -.
DR ProteomicsDB; 268837; -.
DR ABCD; Q80T41; 2 sequenced antibodies.
DR Antibodypedia; 2939; 588 antibodies from 42 providers.
DR Ensembl; ENSMUST00000107749; ENSMUSP00000103378; ENSMUSG00000039809.
DR GeneID; 242425; -.
DR KEGG; mmu:242425; -.
DR UCSC; uc008sug.1; mouse.
DR CTD; 9568; -.
DR MGI; MGI:2386030; Gabbr2.
DR VEuPathDB; HostDB:ENSMUSG00000039809; -.
DR eggNOG; KOG1055; Eukaryota.
DR GeneTree; ENSGT00940000155783; -.
DR HOGENOM; CLU_005240_0_0_1; -.
DR InParanoid; Q80T41; -.
DR OMA; LLKHYHW; -.
DR OrthoDB; 590810at2759; -.
DR PhylomeDB; Q80T41; -.
DR TreeFam; TF313965; -.
DR Reactome; R-MMU-1296041; Activation of G protein gated Potassium channels.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR Reactome; R-MMU-420499; Class C/3 (Metabotropic glutamate/pheromone receptors).
DR Reactome; R-MMU-977444; GABA B receptor activation.
DR Reactome; R-MMU-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
DR BioGRID-ORCS; 242425; 2 hits in 76 CRISPR screens.
DR PRO; PR:Q80T41; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q80T41; protein.
DR Bgee; ENSMUSG00000039809; Expressed in dentate gyrus of hippocampal formation granule cell and 35 other tissues.
DR ExpressionAtlas; Q80T41; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:1902712; C:G protein-coupled GABA receptor complex; ISO:MGI.
DR GO; GO:0038039; C:G protein-coupled receptor heterodimeric complex; ISS:UniProtKB.
DR GO; GO:1902710; C:GABA receptor complex; ISO:MGI.
DR GO; GO:0098982; C:GABA-ergic synapse; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; ISO:MGI.
DR GO; GO:0099056; C:integral component of presynaptic membrane; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; IDA:MGI.
DR GO; GO:0004965; F:G protein-coupled GABA receptor activity; ISO:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; ISS:UniProtKB.
DR GO; GO:0150099; P:neuron-glial cell signaling; ISO:MGI.
DR GO; GO:0051932; P:synaptic transmission, GABAergic; IC:ComplexPortal.
DR InterPro; IPR001828; ANF_lig-bd_rcpt.
DR InterPro; IPR041689; GBR2_CC.
DR InterPro; IPR002455; GPCR3_GABA-B.
DR InterPro; IPR000337; GPCR_3.
DR InterPro; IPR017978; GPCR_3_C.
DR InterPro; IPR017979; GPCR_3_CS.
DR InterPro; IPR002457; GPCR_3_GABA_rcpt_B2.
DR InterPro; IPR028082; Peripla_BP_I.
DR PANTHER; PTHR10519; PTHR10519; 1.
DR Pfam; PF00003; 7tm_3; 1.
DR Pfam; PF01094; ANF_receptor; 1.
DR Pfam; PF18455; GBR2_CC; 1.
DR PRINTS; PR01178; GABAB2RECPTR.
DR PRINTS; PR00248; GPCRMGR.
DR SUPFAM; SSF53822; SSF53822; 1.
DR PROSITE; PS00981; G_PROTEIN_RECEP_F3_3; 1.
DR PROSITE; PS50259; G_PROTEIN_RECEP_F3_4; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Coiled coil; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Membrane; Phosphoprotein; Postsynaptic cell membrane;
KW Receptor; Reference proteome; Signal; Synapse; Transducer; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..40
FT /evidence="ECO:0000255"
FT CHAIN 41..940
FT /note="Gamma-aminobutyric acid type B receptor subunit 2"
FT /id="PRO_0000306250"
FT TOPO_DOM 41..482
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 483..503
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 504..521
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 522..542
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 543..550
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 551..571
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 572..596
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 597..617
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 618..653
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 654..674
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 675..690
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 691..711
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 712..719
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 720..740
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 741..940
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 762..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 781..818
FT /evidence="ECO:0000255"
FT MOD_RES 775
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 778
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 818
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 883
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 892
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 912
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 915
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 919
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 923
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 388
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 403
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 452
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 107..134
FT /evidence="ECO:0000250"
FT DISULFID 236..265
FT /evidence="ECO:0000250"
FT DISULFID 264..301
FT /evidence="ECO:0000250"
SQ SEQUENCE 940 AA; 105666 MW; B364DC0A54EE9206 CRC64;
MASPPSSGQP RPPPPPPPPA RLLLPLLLSL LLSLAPGAWG WARGAPRPPP SSPPLSIMGL
MPLTKEVAKG SIGRGVLPAV ELAIEQIRNE SLLRPYFLDL RLYDTECDNA KGLKAFYDAI
KYGPNHLMVF GGVCPSVTSI IAESLQGWNL VQLSFAATTP VLADKKKYPY FFRTVPSDNA
VNPAILKLLK HFRWRRVGTL TQDVQRFSEV RNDLTGVLYG EDIEISDTES FSNDPCTSVK
KLKGNDVRII LGQFDQNMAA KVFCCAFEES MFGSKYQWII PGWYEPAWWE QVHVEANSSR
CLRRSLLAAM EGYIGVDFEP LSSKQIKTIS GKTPQQYERE YNSKRSGVGP SKFHGYAYDG
IWVIAKTLQR AMETLHASSR HQRIQDFNYT DHTLGRIILN AMNETNFFGV TGQVVFRNGE
RMGTIKFTQF QDSREVKVGE YNAVADTLEI INDTIRFQGS EPPKDKTIIL EQLRKISLPL
YSILSALTIL GMIMASAFLF FNIKNRNQKL IKMSSPYMNN LIILGGMLSY ASIFLFGLDG
SFVSEKTFET LCTVRTWILT VGYTTAFGAM FAKTWRVHAI FKNVKMKKKI IKDQKLLVIV
GGMLLIDLCI LICWQAVDPL RRTVERYSME PDPAGRDISI RPLLEHCENT HMTIWLGIVY
AYKGLLMLFG CFLAWETRNV SIPALNDSKY IGMSVYNVGI MCIIGAAVSF LTRDQPNVQF
CIVALVIIFC STITLCLVFV PKLITLRTNP DAATQNRRFQ FTQNQKKEDS KTSTSVTSVN
QASTSRLEGL QSENHRLRMK ITELDKDLEE VTMQLQDTPE KTTYIKQNHY QELNDILSLG
NFTESTDGGK AILKNHLDQN PQLQWNTTEP SRTCKDPIED INSPEHIQRR LSLQLPILHH
AYLPSIGGVD ASCVSPCVSP TASPRHRHVP PSFRVMVSGL
