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

 GABR1_MOUSE             Reviewed;         960 AA.
Q9WV18; Q6PGJ2; Q9WU48; Q9WV15; Q9WV16; Q9WV17;
11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
30-AUG-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;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1A), FUNCTION, INTERACTION WITH
GABBR2, AND SUBCELLULAR LOCATION.
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).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1A AND 1B), AND TISSUE
SPECIFICITY.
PubMed=11306808;
Lamp K., Humeny A., Nikolic Z., Imai K., Adamski J., Schiebel K.,
Becker C.M.;
"The murine GABA(B) receptor 1: cDNA cloning, tissue distribution,
structure of the Gabbr1 gene, and mapping to chromosome 17.";
Cytogenet. Cell Genet. 92:116-121(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1A AND 1B).
STRAIN=C57BL/6J; TISSUE=Brain;
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).
[5]
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).
[6]
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).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-872 AND THR-929, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- 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:10773016}.
-!- 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 (By
similarity). Interacts with JAKMIP1. {ECO:0000250,
ECO:0000269|PubMed:10773016, ECO:0000269|PubMed:14718537,
ECO:0000269|PubMed:9872744}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass
membrane protein {ECO:0000250}. Cell junction, synapse,
postsynaptic cell membrane {ECO:0000250}; Multi-pass membrane
protein {ECO:0000250}. Cell projection, dendrite {ECO:0000250}.
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 (By similarity).
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1A;
IsoId=Q9WV18-1; Sequence=Displayed;
Name=1B;
IsoId=Q9WV18-2; Sequence=VSP_002041;
-!- TISSUE SPECIFICITY: Expressed in neuronal tissue including cortex,
cerebellum and spinal cord. Not detected in non-neuronal tissues
including heart, liver, spleen and kidney.
{ECO:0000269|PubMed:11306808}.
-!- 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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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF114168; AAD22194.2; -; mRNA.
EMBL; AF008649; AAG29338.1; -; mRNA.
EMBL; AF120255; AAG29341.1; -; mRNA.
EMBL; AL078630; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC054735; AAH54735.1; -; mRNA.
EMBL; BC056990; AAH56990.1; -; mRNA.
CCDS; CCDS37616.1; -. [Q9WV18-1]
RefSeq; NP_062312.3; NM_019439.3. [Q9WV18-1]
UniGene; Mm.32191; -.
ProteinModelPortal; Q9WV18; -.
SMR; Q9WV18; -.
BioGrid; 207643; 3.
IntAct; Q9WV18; 3.
STRING; 10090.ENSMUSP00000025338; -.
iPTMnet; Q9WV18; -.
PhosphoSitePlus; Q9WV18; -.
PaxDb; Q9WV18; -.
PeptideAtlas; Q9WV18; -.
PRIDE; Q9WV18; -.
Ensembl; ENSMUST00000025338; ENSMUSP00000025338; ENSMUSG00000024462. [Q9WV18-1]
Ensembl; ENSMUST00000172792; ENSMUSP00000134268; ENSMUSG00000024462. [Q9WV18-2]
GeneID; 54393; -.
KEGG; mmu:54393; -.
UCSC; uc008cma.1; mouse. [Q9WV18-1]
UCSC; uc008cmd.1; mouse. [Q9WV18-2]
CTD; 2550; -.
MGI; MGI:1860139; Gabbr1.
eggNOG; KOG1055; Eukaryota.
eggNOG; ENOG410XNN1; LUCA.
GeneTree; ENSGT00530000063129; -.
HOGENOM; HOG000016575; -.
HOVERGEN; HBG051688; -.
InParanoid; Q9WV18; -.
KO; K04615; -.
OMA; PKICQAR; -.
OrthoDB; EOG091G01WG; -.
PhylomeDB; Q9WV18; -.
TreeFam; TF313965; -.
Reactome; R-MMU-1296041; Activation of G protein gated Potassium channels.
Reactome; R-MMU-418594; G alpha (i) signalling events.
Reactome; R-MMU-420499; Class C/3 (Metabotropic glutamate/pheromone receptors).
Reactome; R-MMU-977444; GABA B receptor activation.
Reactome; R-MMU-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
ChiTaRS; Gabbr1; mouse.
PRO; PR:Q9WV18; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000024462; -.
CleanEx; MM_GABBR1; -.
ExpressionAtlas; Q9WV18; baseline and differential.
Genevisible; Q9WV18; MM.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
GO; GO:0038037; C:G-protein coupled receptor dimeric complex; IDA:MGI.
GO; GO:0038039; C:G-protein coupled receptor heterodimeric complex; ISS:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0045211; C:postsynaptic membrane; IDA:MGI.
GO; GO:0098793; C:presynapse; IDA:ParkinsonsUK-UCL.
GO; GO:0042734; C:presynaptic membrane; IDA:MGI.
GO; GO:0004965; F:G-protein coupled GABA receptor activity; ISS:UniProtKB.
GO; GO:0007193; P:adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway; ISS:UniProtKB.
GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IDA:MGI.
GO; GO:0007194; P:negative regulation of adenylate cyclase activity; ISO:MGI.
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;
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; Sushi; Synapse; Transducer; Transmembrane;
Transmembrane helix.
SIGNAL 1 16 {ECO:0000255}.
CHAIN 17 960 Gamma-aminobutyric acid type B receptor
subunit 1.
/FTId=PRO_0000012950.
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 731 767 Extracellular. {ECO:0000255}.
TRANSMEM 768 788 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 789 803 Cytoplasmic. {ECO:0000255}.
TRANSMEM 804 824 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 825 832 Extracellular. {ECO:0000255}.
TRANSMEM 833 853 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 854 960 Cytoplasmic. {ECO:0000255}.
DOMAIN 29 95 Sushi 1. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 97 158 Sushi 2. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
REGION 887 915 Interaction with ATF4. {ECO:0000250}.
COILED 868 924 {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 872 872 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 929 929 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
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}.
DISULFID 130 156 {ECO:0000255|PROSITE-ProRule:PRU00302}.
DISULFID 219 245 {ECO:0000255|PROSITE-ProRule:PRU00302}.
DISULFID 375 409 {ECO:0000255|PROSITE-ProRule:PRU00302}.
VAR_SEQ 1 163 MLLLLLVPLFLRPLGAGGAQTPNVTSEGCQIIHPPWEGGIR
YRGLTRDQVKAINFLPVDYEIEYVCRGEREVVGPKVRKCLA
NGSWTDMDTPSRCVRICSKSYLTLENGKVFLTGGDLPALDG
ARVDFRCDPDFHLVGSSRSICSQGQWSTPKPHCQVNRTPH
-> MGPGGPCTPVGWPLPLLLVMAAGVAPVWASHSPHLPRP
HPRVPPHPS (in isoform 1B).
{ECO:0000303|PubMed:11306808,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_002041.
CONFLICT 7 8 VP -> LL (in Ref. 1; AAD22194).
{ECO:0000305}.
CONFLICT 46 46 T -> I (in Ref. 1; AAD22194).
{ECO:0000305}.
CONFLICT 618 618 V -> A (in Ref. 1; AAD22194).
{ECO:0000305}.
CONFLICT 642 642 A -> V (in Ref. 1; AAD22194).
{ECO:0000305}.
CONFLICT 700 700 W -> R (in Ref. 4; AAH56990).
{ECO:0000305}.
CONFLICT 721 721 I -> V (in Ref. 1; AAD22194).
{ECO:0000305}.
CONFLICT 812 812 A -> P (in Ref. 2; AAG29338/AAG29341).
{ECO:0000305}.
CONFLICT 869 869 A -> T (in Ref. 1; AAD22194).
{ECO:0000305}.
CONFLICT 921 921 I -> L (in Ref. 1; AAD22194).
{ECO:0000305}.
SEQUENCE 960 AA; 108216 MW; E4B5A9401E23E8B4 CRC64;
MLLLLLVPLF LRPLGAGGAQ TPNVTSEGCQ IIHPPWEGGI RYRGLTRDQV KAINFLPVDY
EIEYVCRGER EVVGPKVRKC LANGSWTDMD TPSRCVRICS KSYLTLENGK VFLTGGDLPA
LDGARVDFRC DPDFHLVGSS RSICSQGQWS 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
ILTLAIWQIV DPLHRTIETF AKEEPKEDID VSILPQLEHC SSKKMNTWLG IFYGYKGLLL
LLGIFLAYET KSVSTEKIND HRAVGMAIYN VAVLCLITAP VTMILSSQQD AAFAFASLAI
VFSSYITLVV LFVPKMRRLI TRGEWQSEAQ DTMKTGSSTN NNEEEKSRLL EKENRELEKI
IAEKEERVSE LRHQLQSRQQ IRSRRHPPTP PDPSGGLPRG PSEPPDRLSC DGSRVHLLYK


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