ID   GABR1_MOUSE             Reviewed;         960 AA.
AC   Q9WV18; Q6PGJ2; Q9WU48; Q9WV15; Q9WV16; Q9WV17;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   27-MAR-2024, entry version 200.
DE   RecName: Full=Gamma-aminobutyric acid type B receptor subunit 1;
DE            Short=GABA-B receptor 1;
DE            Short=GABA-B-R1;
DE            Short=GABA-BR1;
DE            Short=GABABR1;
DE            Short=Gb1;
DE   Flags: Precursor;
GN   Name=Gabbr1;
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 [MRNA] (ISOFORM 1A), FUNCTION, INTERACTION WITH GABBR2,
RP   AND SUBCELLULAR LOCATION.
RX   PubMed=10773016;
RA   Sullivan R., Chateauneuf A., Coulombe N., Kolakowski L.F. Jr.,
RA   Johnson M.P., Hebert T.E., Ethier N., Belley M., Metters K., Abramovitz M.,
RA   O'Neill G.P., Ng G.Y.K.;
RT   "Coexpression of full-length gamma-aminobutyric acid(B) (GABA(B)) receptors
RT   with truncated receptors and metabotropic glutamate receptor 4 supports the
RT   GABA(B) heterodimer as the functional receptor.";
RL   J. Pharmacol. Exp. Ther. 293:460-467(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1A AND 1B), AND TISSUE SPECIFICITY.
RX   PubMed=11306808; DOI=10.1159/000056880;
RA   Lamp K., Humeny A., Nikolic Z., Imai K., Adamski J., Schiebel K.,
RA   Becker C.M.;
RT   "The murine GABA(B) receptor 1: cDNA cloning, tissue distribution,
RT   structure of the Gabbr1 gene, and mapping to chromosome 17.";
RL   Cytogenet. Cell Genet. 92:116-121(2001).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1A AND 1B).
RC   STRAIN=C57BL/6J; TISSUE=Brain {ECO:0000303|PubMed:15489334};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   FUNCTION, AND INTERACTION WITH GABBR2.
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   [6]
RP   INTERACTION WITH GABBR2.
RX   PubMed=9872744; DOI=10.1126/science.283.5398.74;
RA   Kuner R., Koehr G., Gruenewald S., Eisenhardt G., Bach A., Kornau H.-C.;
RT   "Role of heteromer formation in GABAB receptor function.";
RL   Science 283:74-77(1999).
RN   [7]
RP   INTERACTION WITH JAKMIP1.
RX   PubMed=14718537; DOI=10.1074/jbc.m311737200;
RA   Couve A., Restituito S., Brandon J.M., Charles K.J., Bawagan H.,
RA   Freeman K.B., Pangalos M.N., Calver A.R., Moss S.J.;
RT   "Marlin-1, a novel RNA-binding protein associates with GABA receptors.";
RL   J. Biol. Chem. 279:13934-13943(2004).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-872 AND THR-929, AND
RP   IDENTIFICATION 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).
RN   [9]
RP   INTERACTION WITH KCTD8; KCTD12; KCTD12B AND KCTD16, FUNCTION, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=20400944; DOI=10.1038/nature08964;
RA   Schwenk J., Metz M., Zolles G., Turecek R., Fritzius T., Bildl W.,
RA   Tarusawa E., Kulik A., Unger A., Ivankova K., Seddik R., Tiao J.Y.,
RA   Rajalu M., Trojanova J., Rohde V., Gassmann M., Schulte U., Fakler B.,
RA   Bettler B.;
RT   "Native GABA(B) receptors are heteromultimers with a family of auxiliary
RT   subunits.";
RL   Nature 465:231-235(2010).
CC   -!- FUNCTION: Component of a heterodimeric G-protein coupled receptor for
CC       GABA, formed by GABBR1 and GABBR2 (PubMed:10773016, PubMed:10075644).
CC       Within the heterodimeric GABA receptor, only GABBR1 seems to bind
CC       agonists, while GABBR2 mediates coupling to G proteins (By similarity).
CC       Ligand binding causes a conformation change that triggers signaling via
CC       guanine nucleotide-binding proteins (G proteins) and modulates the
CC       activity of down-stream effectors, such as adenylate cyclase
CC       (PubMed:10773016, PubMed:10075644). Signaling inhibits adenylate
CC       cyclase, stimulates phospholipase A2, activates potassium channels,
CC       inactivates voltage-dependent calcium-channels and modulates inositol
CC       phospholipid hydrolysis (PubMed:10075644). Calcium is required for high
CC       affinity binding to GABA (By similarity). Plays a critical role in the
CC       fine-tuning of inhibitory synaptic transmission (By similarity). Pre-
CC       synaptic GABA receptor inhibits neurotransmitter release by down-
CC       regulating high-voltage activated calcium channels, whereas
CC       postsynaptic GABA receptor decreases neuronal excitability by
CC       activating a prominent inwardly rectifying potassium (Kir) conductance
CC       that underlies the late inhibitory postsynaptic potentials
CC       (PubMed:10075644). Not only implicated in synaptic inhibition but also
CC       in hippocampal long-term potentiation, slow wave sleep, muscle
CC       relaxation and antinociception (By similarity).
CC       {ECO:0000250|UniProtKB:Q9UBS5, ECO:0000250|UniProtKB:Q9Z0U4,
CC       ECO:0000269|PubMed:10075644, ECO:0000269|PubMed:10773016}.
CC   -!- SUBUNIT: Heterodimer of GABBR1 and GABBR2 (PubMed:10773016,
CC       PubMed:10075644, PubMed:9872744). Homodimers may form, but are inactive
CC       (By similarity). Interacts (via C-terminus) with ATF4 (via leucine
CC       zipper domain) (By similarity). Interacts with JAKMIP1
CC       (PubMed:14718537). Interacts with KCTD8, KCTD12, KCTD12B and KCTD16;
CC       this interaction determines the pharmacology and kinetics of the
CC       receptor response, the KCTD proteins markedly accelerating the GABA-B
CC       response, although to different extents (PubMed:20400944).
CC       {ECO:0000250|UniProtKB:Q9Z0U4, ECO:0000269|PubMed:10075644,
CC       ECO:0000269|PubMed:10773016, ECO:0000269|PubMed:14718537,
CC       ECO:0000269|PubMed:20400944, ECO:0000269|PubMed:9872744}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20400944};
CC       Multi-pass membrane protein {ECO:0000250}. Postsynaptic cell membrane
CC       {ECO:0000269|PubMed:20400944}; Multi-pass membrane protein
CC       {ECO:0000250}. Cell projection, dendrite {ECO:0000250}.
CC       Note=Coexpression of GABBR1 and GABBR2 is required for GABBR1
CC       maturation and transport to the plasma membrane. Colocalizes with ATF4
CC       in hippocampal neuron dendritic membranes (By similarity).
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1A;
CC         IsoId=Q9WV18-1; Sequence=Displayed;
CC       Name=1B;
CC         IsoId=Q9WV18-2; Sequence=VSP_002041;
CC   -!- TISSUE SPECIFICITY: Expressed in neuronal tissue including cortex,
CC       cerebellum and spinal cord. Not detected in non-neuronal tissues
CC       including heart, liver, spleen and kidney.
CC       {ECO:0000269|PubMed:11306808}.
CC   -!- DOMAIN: Alpha-helical parts of the C-terminal intracellular region
CC       mediate heterodimeric interaction with GABBR2. The linker region
CC       between the transmembrane domain 3 (TM3) and the transmembrane domain 4
CC       (TM4) probably plays a role in the specificity for G-protein coupling.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family. GABA-B
CC       receptor subfamily. {ECO:0000305}.
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DR   EMBL; AF114168; AAD22194.2; -; mRNA.
DR   EMBL; AF008649; AAG29338.1; -; mRNA.
DR   EMBL; AF120255; AAG29341.1; -; mRNA.
DR   EMBL; AL078630; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC054735; AAH54735.1; -; mRNA.
DR   EMBL; BC056990; AAH56990.1; -; mRNA.
DR   CCDS; CCDS37616.1; -. [Q9WV18-1]
DR   RefSeq; NP_062312.3; NM_019439.3. [Q9WV18-1]
DR   AlphaFoldDB; Q9WV18; -.
DR   SMR; Q9WV18; -.
DR   BioGRID; 207643; 10.
DR   ComplexPortal; CPX-2990; GABA-B receptor complex.
DR   IntAct; Q9WV18; 4.
DR   MINT; Q9WV18; -.
DR   STRING; 10090.ENSMUSP00000025338; -.
DR   GlyConnect; 2328; 9 N-Linked glycans (5 sites).
DR   GlyCosmos; Q9WV18; 8 sites, 8 glycans.
DR   GlyGen; Q9WV18; 9 sites, 8 N-linked glycans (5 sites), 1 O-linked glycan (1 site).
DR   iPTMnet; Q9WV18; -.
DR   PhosphoSitePlus; Q9WV18; -.
DR   SwissPalm; Q9WV18; -.
DR   MaxQB; Q9WV18; -.
DR   PaxDb; 10090-ENSMUSP00000025338; -.
DR   PeptideAtlas; Q9WV18; -.
DR   ProteomicsDB; 273410; -. [Q9WV18-1]
DR   ProteomicsDB; 273411; -. [Q9WV18-2]
DR   Pumba; Q9WV18; -.
DR   ABCD; Q9WV18; 1 sequenced antibody.
DR   Antibodypedia; 50418; 628 antibodies from 44 providers.
DR   DNASU; 54393; -.
DR   Ensembl; ENSMUST00000025338.16; ENSMUSP00000025338.10; ENSMUSG00000024462.18. [Q9WV18-1]
DR   Ensembl; ENSMUST00000172792.8; ENSMUSP00000134268.2; ENSMUSG00000024462.18. [Q9WV18-2]
DR   GeneID; 54393; -.
DR   KEGG; mmu:54393; -.
DR   UCSC; uc008cma.1; mouse. [Q9WV18-1]
DR   UCSC; uc008cmd.1; mouse. [Q9WV18-2]
DR   AGR; MGI:1860139; -.
DR   CTD; 2550; -.
DR   MGI; MGI:1860139; Gabbr1.
DR   VEuPathDB; HostDB:ENSMUSG00000024462; -.
DR   eggNOG; KOG1055; Eukaryota.
DR   GeneTree; ENSGT00940000157642; -.
DR   HOGENOM; CLU_005240_2_0_1; -.
DR   InParanoid; Q9WV18; -.
DR   OMA; WAGGEAC; -.
DR   OrthoDB; 2970339at2759; -.
DR   PhylomeDB; Q9WV18; -.
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; 54393; 3 hits in 80 CRISPR screens.
DR   ChiTaRS; Gabbr1; mouse.
DR   PRO; PR:Q9WV18; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; Q9WV18; Protein.
DR   Bgee; ENSMUSG00000024462; Expressed in habenula and 256 other cell types or tissues.
DR   ExpressionAtlas; Q9WV18; baseline and differential.
DR   GO; GO:0030673; C:axolemma; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0043198; C:dendritic shaft; ISO:MGI.
DR   GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR   GO; GO:0005615; C:extracellular space; ISO:MGI.
DR   GO; GO:1902712; C:G protein-coupled GABA receptor complex; ISO:MGI.
DR   GO; GO:0038037; C:G protein-coupled receptor dimeric complex; IDA: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; IDA:SynGO.
DR   GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0031966; C:mitochondrial membrane; ISO:MGI.
DR   GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0045211; C:postsynaptic membrane; IDA:MGI.
DR   GO; GO:0098793; C:presynapse; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0042734; C:presynaptic membrane; IDA:MGI.
DR   GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR   GO; GO:0097060; C:synaptic membrane; ISO:MGI.
DR   GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
DR   GO; GO:1990430; F:extracellular matrix protein binding; ISO:MGI.
DR   GO; GO:0004965; F:G protein-coupled GABA receptor activity; ISO:MGI.
DR   GO; GO:0099579; F:G protein-coupled neurotransmitter receptor activity involved in regulation of postsynaptic membrane potential; IDA:SynGO.
DR   GO; GO:0150047; F:G protein-coupled neurotransmitter receptor activity involved in regulation of presynaptic membrane potential; IDA:SynGO.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR   GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IDA:MGI.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR   GO; GO:0033602; P:negative regulation of dopamine secretion; ISO:MGI.
DR   GO; GO:0032811; P:negative regulation of epinephrine secretion; ISO:MGI.
DR   GO; GO:0014053; P:negative regulation of gamma-aminobutyric acid secretion; ISO:MGI.
DR   GO; GO:0050805; P:negative regulation of synaptic transmission; ISO:MGI.
DR   GO; GO:0150099; P:neuron-glial cell signaling; ISO:MGI.
DR   GO; GO:0001649; P:osteoblast differentiation; ISO:MGI.
DR   GO; GO:0014049; P:positive regulation of glutamate secretion; ISO:MGI.
DR   GO; GO:0060124; P:positive regulation of growth hormone secretion; ISO:MGI.
DR   GO; GO:0014048; P:regulation of glutamate secretion; ISO:MGI.
DR   GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR   GO; GO:0035094; P:response to nicotine; IEA:Ensembl.
DR   GO; GO:0051932; P:synaptic transmission, GABAergic; NAS:ComplexPortal.
DR   CDD; cd15291; 7tmC_GABA-B-R1; 1.
DR   CDD; cd00033; CCP; 1.
DR   CDD; cd06366; PBP1_GABAb_receptor; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   Gene3D; 2.10.70.10; Complement Module, domain 1; 1.
DR   InterPro; IPR001828; ANF_lig-bd_rcpt.
DR   InterPro; IPR002455; GPCR3_GABA-B.
DR   InterPro; IPR017978; GPCR_3_C.
DR   InterPro; IPR002456; GPCR_3_GABA_rcpt_B1.
DR   InterPro; IPR028082; Peripla_BP_I.
DR   InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR   InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR   PANTHER; PTHR10519; GABA-B RECEPTOR; 1.
DR   PANTHER; PTHR10519:SF76; GAMMA-AMINOBUTYRIC ACID TYPE B RECEPTOR SUBUNIT 1; 1.
DR   Pfam; PF00003; 7tm_3; 1.
DR   Pfam; PF01094; ANF_receptor; 1.
DR   Pfam; PF00084; Sushi; 1.
DR   PRINTS; PR01177; GABAB1RECPTR.
DR   PRINTS; PR01176; GABABRECEPTR.
DR   SMART; SM00032; CCP; 2.
DR   SUPFAM; SSF57535; Complement control module/SCR domain; 2.
DR   SUPFAM; SSF53822; Periplasmic binding protein-like I; 1.
DR   PROSITE; PS50259; G_PROTEIN_RECEP_F3_4; 1.
DR   PROSITE; PS50923; SUSHI; 1.
DR   Genevisible; Q9WV18; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Cell projection; Coiled coil;
KW   Disulfide bond; G-protein coupled receptor; Glycoprotein; Membrane;
KW   Phosphoprotein; Postsynaptic cell membrane; Receptor; Reference proteome;
KW   Repeat; Signal; Sushi; Synapse; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..960
FT                   /note="Gamma-aminobutyric acid type B receptor subunit 1"
FT                   /id="PRO_0000012950"
FT   TOPO_DOM        17..590
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        591..611
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        612..630
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        631..651
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        652..666
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        667..687
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        688..709
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        710..730
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        731..767
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        768..788
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        789..803
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        804..824
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        825..832
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        833..853
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        854..960
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          29..95
FT                   /note="Sushi 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DOMAIN          97..158
FT                   /note="Sushi 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   REGION          866..891
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          887..915
FT                   /note="Interaction with ATF4"
FT                   /evidence="ECO:0000250"
FT   REGION          908..960
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          868..924
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        866..883
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        926..940
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         246
FT                   /ligand="4-aminobutanoate"
FT                   /ligand_id="ChEBI:CHEBI:59888"
FT                   /ligand_note="agonist"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UBS5"
FT   BINDING         269
FT                   /ligand="4-aminobutanoate"
FT                   /ligand_id="ChEBI:CHEBI:59888"
FT                   /ligand_note="agonist"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UBS5"
FT   BINDING         286
FT                   /ligand="4-aminobutanoate"
FT                   /ligand_id="ChEBI:CHEBI:59888"
FT                   /ligand_note="agonist"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UBS5"
FT   BINDING         366
FT                   /ligand="4-aminobutanoate"
FT                   /ligand_id="ChEBI:CHEBI:59888"
FT                   /ligand_note="agonist"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UBS5"
FT   BINDING         465
FT                   /ligand="4-aminobutanoate"
FT                   /ligand_id="ChEBI:CHEBI:59888"
FT                   /ligand_note="agonist"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UBS5"
FT   MOD_RES         872
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         929
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CARBOHYD        23
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        83
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        408
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        439
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        481
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        501
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        513
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        99..144
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        130..156
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        219..245
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   DISULFID        375..409
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT   VAR_SEQ         1..163
FT                   /note="MLLLLLVPLFLRPLGAGGAQTPNVTSEGCQIIHPPWEGGIRYRGLTRDQVKA
FT                   INFLPVDYEIEYVCRGEREVVGPKVRKCLANGSWTDMDTPSRCVRICSKSYLTLENGKV
FT                   FLTGGDLPALDGARVDFRCDPDFHLVGSSRSICSQGQWSTPKPHCQVNRTPH -> MGP
FT                   GGPCTPVGWPLPLLLVMAAGVAPVWASHSPHLPRPHPRVPPHPS (in isoform
FT                   1B)"
FT                   /evidence="ECO:0000303|PubMed:11306808,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_002041"
FT   CONFLICT        7..8
FT                   /note="VP -> LL (in Ref. 1; AAD22194)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        46
FT                   /note="T -> I (in Ref. 1; AAD22194)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        618
FT                   /note="V -> A (in Ref. 1; AAD22194)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        642
FT                   /note="A -> V (in Ref. 1; AAD22194)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        700
FT                   /note="W -> R (in Ref. 4; AAH56990)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        721
FT                   /note="I -> V (in Ref. 1; AAD22194)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        812
FT                   /note="A -> P (in Ref. 2; AAG29338/AAG29341)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        869
FT                   /note="A -> T (in Ref. 1; AAD22194)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        921
FT                   /note="I -> L (in Ref. 1; AAD22194)"
FT                   /evidence="ECO:0000305"
SQ   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
//