GABR1_HUMAN
ID GABR1_HUMAN Reviewed; 961 AA.
AC Q9UBS5; B0UXY7; O95375; O95468; O95975; O96022; Q5STL4; Q5SUJ8; Q5SUL3;
AC Q71SG6; Q86W60; Q9UQQ0;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 207.
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; Synonyms=GPRC3A;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1A AND 1B), FUNCTION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DOMAIN.
RC TISSUE=Cerebellum {ECO:0000303|PubMed:9844003};
RX PubMed=9844003; DOI=10.1073/pnas.95.25.14991;
RA Kaupmann K., Schuler V., Mosbacher J., Bischoff S., Bittiger H., Heid J.,
RA Froestl W., Leonhard S., Pfaff T., Karschin A., Bettler B.;
RT "Human gamma-aminobutyric acid type B receptors are differentially
RT expressed and regulate inwardly rectifying K+ channels.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:14991-14996(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1A; 1B AND 1C), FUNCTION, SUBUNIT,
RP INTERACTION WITH GABBR2, AND SUBCELLULAR LOCATION.
RC TISSUE=Cerebellum {ECO:0000303|PubMed:9872316};
RX PubMed=9872316; DOI=10.1038/25354;
RA White J.H., Wise A., Main M.J., Green A., Fraser N.J., Disney G.H.,
RA Barnes A.A., Emson P., Foord S.M., Marshall F.H.;
RT "Heterodimerization is required for the formation of a functional GABA(B)
RT receptor.";
RL Nature 396:679-682(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1A).
RC TISSUE=Brain {ECO:0000303|Ref.3};
RA Stropp U., Raming K.;
RT "Human mRNA for GABA-B1a receptor.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1A), AND TISSUE SPECIFICITY.
RC TISSUE=Fetal brain {ECO:0000303|PubMed:9753614};
RX PubMed=9753614; DOI=10.1006/bbrc.1998.9296;
RA Grifa A., Totaro A., Rommens J.M., Carella M., Roetto A., Borgato L.,
RA Zelante L., Gasparini P.;
RT "GABA (gamma-amino-butyric acid) neurotransmission: identification and fine
RT mapping of the human GABAB receptor gene.";
RL Biochem. Biophys. Res. Commun. 250:240-245(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE (ISOFORM 1A).
RX PubMed=9798068; DOI=10.1016/s0006-3223(98)00244-3;
RA Goei V.L., Choi J., Ahn J., Bowlus C.L., Raha-Chowdhury R., Gruen J.R.;
RT "Human gamma-aminobutyric acid B receptor gene: complementary DNA cloning,
RT expression, chromosomal location, and genomic organization.";
RL Biol. Psychiatry 44:659-666(1998).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1C).
RC TISSUE=Cerebellum {ECO:0000303|Ref.6};
RA Fraser N.J.;
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1A AND 1B), AND VARIANTS VAL-20
RP AND SER-489.
RC TISSUE=Fetal brain {ECO:0000303|PubMed:9933300};
RX PubMed=9933300; DOI=10.1007/s100480050051;
RA Peters H.C., Kaemmer G., Volz A., Kaupmann K., Ziegler A., Bettler B.,
RA Epplen J.T., Sander T., Riess O.;
RT "Mapping, genomic structure, and polymorphisms of the human GABABR1
RT receptor gene: evaluation of its involvement in idiopathic generalized
RT epilepsy.";
RL Neurogenetics 2:47-54(1998).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1A).
RC TISSUE=Cerebellum {ECO:0000303|PubMed:9889352};
RX PubMed=9889352; DOI=10.1016/s0169-328x(98)00316-7;
RA Makoff A.;
RT "Molecular cloning of human GABABR1 and its tissue distribution.";
RL Brain Res. Mol. Brain Res. 64:137-140(1999).
RN [9]
RP NUCLEOTIDE SEQUENCE (ISOFORM 1E), FUNCTION, SUBUNIT, INTERACTION WITH
RP GABBR2, TISSUE SPECIFICITY, AND VARIANT SER-489.
RC TISSUE=Prostate {ECO:0000303|PubMed:10906333};
RX PubMed=10906333; DOI=10.1074/jbc.m005333200;
RA Schwarz D.A., Barry G., Eliasof S.D., Petroski R.E., Conlon P.J.,
RA Maki R.A.;
RT "Characterization of gamma-aminobutyric acid receptor GABAB(1e), a GABAB(1)
RT splice variant encoding a truncated receptor.";
RL J. Biol. Chem. 275:32174-32181(2000).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT VAL-20.
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1B).
RC 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 [13]
RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA Hillman R.T., Green R.E., Brenner S.E.;
RT "An unappreciated role for RNA surveillance.";
RL Genome Biol. 5:R8.1-R8.16(2004).
RN [14]
RP FUNCTION, AND INTERACTION WITH GABBR2.
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 [15]
RP FUNCTION.
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 [16]
RP FUNCTION, INTERACTION WITH GABBR2, TISSUE SPECIFICITY, AND DOMAIN.
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 [17]
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 [18]
RP FUNCTION, INTERACTION WITH GABBR2, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=15617512; DOI=10.1042/bj20041435;
RA Villemure J.F., Adam L., Bevan N.J., Gearing K., Chenier S., Bouvier M.;
RT "Subcellular distribution of GABA(B) receptor homo- and hetero-dimers.";
RL Biochem. J. 388:47-55(2005).
RN [19]
RP FUNCTION, AND INTERACTION WITH GABBR2.
RX PubMed=18165688; DOI=10.1074/jbc.m705202200;
RA Nomura R., Suzuki Y., Kakizuka A., Jingami H.;
RT "Direct detection of the interaction between recombinant soluble
RT extracellular regions in the heterodimeric metabotropic gamma-aminobutyric
RT acid receptor.";
RL J. Biol. Chem. 283:4665-4673(2008).
RN [20]
RP FUNCTION, PARTIAL PROTEIN SEQUENCE, AGONIST BINDING, MUTAGENESIS OF TYR-230
RP AND TYR-234, AND INTERACTION WITH GABBR2.
RX PubMed=22660477; DOI=10.1038/nn.3133;
RA Geng Y., Xiong D., Mosyak L., Malito D.L., Kniazeff J., Chen Y.,
RA Burmakina S., Quick M., Bush M., Javitch J.A., Pin J.P., Fan Q.R.;
RT "Structure and functional interaction of the extracellular domain of human
RT GABA(B) receptor GBR2.";
RL Nat. Neurosci. 15:970-978(2012).
RN [21] {ECO:0007744|PDB:4MQE, ECO:0007744|PDB:4MQF, ECO:0007744|PDB:4MR7, ECO:0007744|PDB:4MR8, ECO:0007744|PDB:4MR9, ECO:0007744|PDB:4MRM, ECO:0007744|PDB:4MS1, ECO:0007744|PDB:4MS3, ECO:0007744|PDB:4MS4}
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 165-576 IN COMPLEXES WITH GABBR2;
RP AGONISTS AND ANTAGONISTS, FUNCTION, SUBUNIT, DISULFIDE BOND, GLYCOSYLATION
RP AT ASN-440 AND ASN-482, AND MUTAGENESIS OF TRP-182; HIS-287; TYR-367 AND
RP TRP-395.
RX PubMed=24305054; DOI=10.1038/nature12725;
RA Geng Y., Bush M., Mosyak L., Wang F., Fan Q.R.;
RT "Structural mechanism of ligand activation in human GABA(B) receptor.";
RL Nature 504:254-259(2013).
RN [22]
RP VARIANTS VAL-20 AND SER-489.
RX PubMed=10402495;
RX DOI=10.1002/(sici)1096-8628(19990820)88:4<305::aid-ajmg5>3.0.co;2-x;
RA Sander T., Peters C., Kaemmer G., Samochowiec J., Zirra M., Mischke D.,
RA Ziegler A., Kaupmann K., Bettler B., Epplen J.T., Riess O.;
RT "Association analysis of exonic variants of the gene encoding the GABAB
RT receptor and idiopathic generalized epilepsy.";
RL Am. J. Med. Genet. 88:305-310(1999).
CC -!- FUNCTION: Component of a heterodimeric G-protein coupled receptor for
CC GABA, formed by GABBR1 and GABBR2 (PubMed:9872316, PubMed:9872744,
CC PubMed:15617512, PubMed:18165688, PubMed:22660477, PubMed:24305054).
CC Within the heterodimeric GABA receptor, only GABBR1 seems to bind
CC agonists, while GABBR2 mediates coupling to G proteins
CC (PubMed:18165688). Ligand binding causes a conformation change that
CC triggers signaling via guanine nucleotide-binding proteins (G proteins)
CC and modulates the activity of down-stream effectors, such as adenylate
CC cyclase (PubMed:10906333, PubMed:10773016, PubMed:10075644,
CC PubMed:9872744, PubMed:24305054). Signaling inhibits adenylate cyclase,
CC stimulates phospholipase A2, activates potassium channels, inactivates
CC voltage-dependent calcium-channels and modulates inositol phospholipid
CC hydrolysis (PubMed:10075644). Calcium is required for high affinity
CC binding to GABA (By similarity). Plays a critical role in the fine-
CC tuning of inhibitory synaptic transmission (PubMed:9844003). 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:9844003, PubMed:9872316, PubMed:10075644, PubMed:9872744,
CC PubMed:22660477). Not only implicated in synaptic inhibition but also
CC in hippocampal long-term potentiation, slow wave sleep, muscle
CC relaxation and antinociception (Probable). Activated by (-)-baclofen,
CC cgp27492 and blocked by phaclofen (PubMed:9844003, PubMed:9872316,
CC PubMed:24305054). {ECO:0000250|UniProtKB:Q9Z0U4,
CC ECO:0000269|PubMed:10075644, ECO:0000269|PubMed:10773016,
CC ECO:0000269|PubMed:10906333, ECO:0000269|PubMed:15617512,
CC ECO:0000269|PubMed:18165688, ECO:0000269|PubMed:22660477,
CC ECO:0000269|PubMed:24305054, ECO:0000269|PubMed:9844003,
CC ECO:0000269|PubMed:9872316, ECO:0000269|PubMed:9872744, ECO:0000305}.
CC -!- FUNCTION: Isoform 1E may regulate the formation of functional
CC GABBR1/GABBR2 heterodimers by competing for GABBR2 binding. This could
CC explain the observation that certain small molecule ligands exhibit
CC differential affinity for central versus peripheral sites.
CC -!- SUBUNIT: Heterodimer of GABBR1 and GABBR2 (PubMed:9872316,
CC PubMed:10773016, PubMed:9872744, PubMed:15617512, PubMed:18165688,
CC PubMed:22660477, PubMed:24305054). Homodimers may form, but are
CC inactive (PubMed:9872316, PubMed:15617512). Isoform 1E (without C-
CC terminal intracellular domain) is unable to dimerize via a coiled-coil
CC interaction with GABBR2 (PubMed:10906333). Interacts (via C-terminus)
CC with ATF4 (via leucine zipper domain) (By similarity). Interacts with
CC JAKMIP1 (PubMed:14718537). {ECO:0000250|UniProtKB:Q9Z0U4,
CC ECO:0000269|PubMed:10773016, ECO:0000269|PubMed:10906333,
CC ECO:0000269|PubMed:14718537, ECO:0000269|PubMed:15617512,
CC ECO:0000269|PubMed:18165688, ECO:0000269|PubMed:22660477,
CC ECO:0000269|PubMed:24305054, ECO:0000269|PubMed:9872316,
CC ECO:0000269|PubMed:9872744}.
CC -!- INTERACTION:
CC Q9UBS5; O75899: GABBR2; NbExp=4; IntAct=EBI-724156, EBI-715469;
CC Q9UBS5; O15354: GPR37; NbExp=2; IntAct=EBI-724156, EBI-15639515;
CC Q9UBS5; P61244: MAX; NbExp=3; IntAct=EBI-724156, EBI-751711;
CC Q9UBS5; P16333: NCK1; NbExp=3; IntAct=EBI-724156, EBI-389883;
CC Q9UBS5; P46459: NSF; NbExp=3; IntAct=EBI-724156, EBI-712251;
CC Q9UBS5-2; O75899: GABBR2; NbExp=6; IntAct=EBI-16084001, EBI-715469;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15617512};
CC Multi-pass membrane protein {ECO:0000305}. Postsynaptic cell membrane
CC {ECO:0000250|UniProtKB:Q9Z0U4}; Multi-pass membrane protein
CC {ECO:0000305}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q9Z0U4}. Note=Colocalizes with ATF4 in
CC hippocampal neuron dendritic membranes (By similarity). Coexpression of
CC GABBR1 and GABBR2 is required for GABBR1 maturation and transport to
CC the plasma membrane (PubMed:15617512). {ECO:0000250|UniProtKB:Q9Z0U4,
CC ECO:0000269|PubMed:15617512}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1E]: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Comment=Isoforms corresponding to the full receptor are essentially
CC found in the central nervous system (CNS).;
CC Name=1A;
CC IsoId=Q9UBS5-1; Sequence=Displayed;
CC Name=1B;
CC IsoId=Q9UBS5-2; Sequence=VSP_002037;
CC Name=1C;
CC IsoId=Q9UBS5-3; Sequence=VSP_002038;
CC Name=1D;
CC IsoId=Q9UBS5-4; Sequence=VSP_002040;
CC Name=1E; Synonyms=Truncated;
CC IsoId=Q9UBS5-5; Sequence=VSP_002039;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain (PubMed:9844003,
CC PubMed:9753614, PubMed:9872744). Weakly expressed in heart, small
CC intestine and uterus. Isoform 1A: Mainly expressed in granular cell and
CC molecular layer (PubMed:9844003). Isoform 1B: Mainly expressed in
CC Purkinje cells (PubMed:9844003). Isoform 1E: Predominantly expressed in
CC peripheral tissues as kidney, lung, trachea, colon, small intestine,
CC stomach, bone marrow, thymus and mammary gland (PubMed:10906333).
CC {ECO:0000269|PubMed:10906333, ECO:0000269|PubMed:9753614,
CC ECO:0000269|PubMed:9844003, ECO:0000269|PubMed:9872744}.
CC -!- DOMAIN: Alpha-helical parts of the C-terminal intracellular region
CC mediate heterodimeric interaction with GABBR2 (PubMed:9872744). The
CC linker region between the transmembrane domain 3 (TM3) and the
CC transmembrane domain 4 (TM4) probably plays a role in the specificity
CC for G-protein coupling (PubMed:9844003). {ECO:0000305|PubMed:9844003,
CC ECO:0000305|PubMed:9872744}.
CC -!- MISCELLANEOUS: [Isoform 1E]: Major isoform in almost all peripheral
CC tissues, although containing a premature stop codon in the mRNA and
CC thus being a potential target for nonsense-mediated mRNA decay. May act
CC as an antagonist of GABA-B receptors, being able to disrupt the normal
CC association between isoform 1A and GABBR2.
CC {ECO:0000269|PubMed:10906333}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family. GABA-B
CC receptor subfamily. {ECO:0000305}.
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DR EMBL; AJ225028; CAA12359.1; -; mRNA.
DR EMBL; AJ225029; CAA12360.1; -; mRNA.
DR EMBL; AJ012185; CAA09939.1; -; mRNA.
DR EMBL; AJ012186; CAA09940.1; -; mRNA.
DR EMBL; AF099148; AAC98508.1; -; mRNA.
DR EMBL; Y11044; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AJ012187; CAA09941.1; -; mRNA.
DR EMBL; AJ010170; CAA09031.1; -; Genomic_DNA.
DR EMBL; AJ010171; CAA09031.1; JOINED; Genomic_DNA.
DR EMBL; AJ010172; CAA09031.1; JOINED; Genomic_DNA.
DR EMBL; AJ010173; CAA09031.1; JOINED; Genomic_DNA.
DR EMBL; AJ010174; CAA09031.1; JOINED; Genomic_DNA.
DR EMBL; AJ010175; CAA09031.1; JOINED; Genomic_DNA.
DR EMBL; AJ010176; CAA09031.1; JOINED; Genomic_DNA.
DR EMBL; AJ010177; CAA09031.1; JOINED; Genomic_DNA.
DR EMBL; AJ010178; CAA09031.1; JOINED; Genomic_DNA.
DR EMBL; AJ010179; CAA09031.1; JOINED; Genomic_DNA.
DR EMBL; AJ010180; CAA09031.1; JOINED; Genomic_DNA.
DR EMBL; AJ010181; CAA09031.1; JOINED; Genomic_DNA.
DR EMBL; AJ010182; CAA09031.1; JOINED; Genomic_DNA.
DR EMBL; AJ010183; CAA09031.1; JOINED; Genomic_DNA.
DR EMBL; AJ010184; CAA09031.1; JOINED; Genomic_DNA.
DR EMBL; AJ010185; CAA09031.1; JOINED; Genomic_DNA.
DR EMBL; AJ010186; CAA09031.1; JOINED; Genomic_DNA.
DR EMBL; AJ010187; CAA09031.1; JOINED; Genomic_DNA.
DR EMBL; AJ010188; CAA09031.1; JOINED; Genomic_DNA.
DR EMBL; AJ010189; CAA09031.1; JOINED; Genomic_DNA.
DR EMBL; AJ010190; CAA09031.1; JOINED; Genomic_DNA.
DR EMBL; AJ010191; CAA09031.1; JOINED; Genomic_DNA.
DR EMBL; AJ012288; CAA09980.1; -; mRNA.
DR EMBL; AF301005; AAG23962.1; -; mRNA.
DR EMBL; AL031983; CAA21453.1; -; Genomic_DNA.
DR EMBL; AL031983; CAA21454.1; -; Genomic_DNA.
DR EMBL; AL645936; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL662826; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX000688; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR388210; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR759766; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR759870; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR788300; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR936483; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX03205.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX03210.1; -; Genomic_DNA.
DR EMBL; BC042598; AAH42598.1; -; mRNA.
DR EMBL; BC050532; AAH50532.2; -; mRNA.
DR CCDS; CCDS4663.1; -. [Q9UBS5-1]
DR CCDS; CCDS4664.1; -. [Q9UBS5-3]
DR CCDS; CCDS4665.1; -. [Q9UBS5-2]
DR PIR; JE0356; JE0356.
DR RefSeq; NP_001305982.1; NM_001319053.1.
DR RefSeq; NP_001461.1; NM_001470.3. [Q9UBS5-1]
DR RefSeq; NP_068703.1; NM_021903.2. [Q9UBS5-2]
DR RefSeq; NP_068704.2; NM_021904.3. [Q9UBS5-3]
DR PDB; 4MQE; X-ray; 2.35 A; A=165-576.
DR PDB; 4MQF; X-ray; 2.22 A; A=165-576.
DR PDB; 4MR7; X-ray; 2.15 A; A=165-576.
DR PDB; 4MR8; X-ray; 2.15 A; A=165-576.
DR PDB; 4MR9; X-ray; 2.35 A; A=165-576.
DR PDB; 4MRM; X-ray; 2.86 A; A=165-576.
DR PDB; 4MS1; X-ray; 2.25 A; A=165-576.
DR PDB; 4MS3; X-ray; 2.50 A; A=165-576.
DR PDB; 4MS4; X-ray; 1.90 A; A=165-576.
DR PDB; 4PAS; X-ray; 1.62 A; A=879-919.
DR PDB; 6HKC; NMR; -; A=26-98.
DR PDB; 6UO8; EM; 3.63 A; A=165-919.
DR PDB; 6UO9; EM; 4.80 A; A=165-919.
DR PDB; 6UOA; EM; 6.30 A; A=165-919.
DR PDB; 6VJM; EM; 3.97 A; A=165-919.
DR PDB; 6W2X; EM; 3.60 A; A=153-961.
DR PDB; 6W2Y; EM; 3.20 A; A/B=153-961.
DR PDB; 6WIV; EM; 3.30 A; A=153-919.
DR PDB; 7C7Q; EM; 3.00 A; A=15-862.
DR PDB; 7C7S; EM; 2.90 A; A=15-919.
DR PDB; 7CA3; EM; 4.50 A; A=165-900.
DR PDB; 7CA5; EM; 7.60 A; A=165-900.
DR PDB; 7CUM; EM; 3.52 A; A=165-900.
DR PDB; 7EB2; EM; 3.50 A; C=15-919.
DR PDBsum; 4MQE; -.
DR PDBsum; 4MQF; -.
DR PDBsum; 4MR7; -.
DR PDBsum; 4MR8; -.
DR PDBsum; 4MR9; -.
DR PDBsum; 4MRM; -.
DR PDBsum; 4MS1; -.
DR PDBsum; 4MS3; -.
DR PDBsum; 4MS4; -.
DR PDBsum; 4PAS; -.
DR PDBsum; 6HKC; -.
DR PDBsum; 6UO8; -.
DR PDBsum; 6UO9; -.
DR PDBsum; 6UOA; -.
DR PDBsum; 6VJM; -.
DR PDBsum; 6W2X; -.
DR PDBsum; 6W2Y; -.
DR PDBsum; 6WIV; -.
DR PDBsum; 7C7Q; -.
DR PDBsum; 7C7S; -.
DR PDBsum; 7CA3; -.
DR PDBsum; 7CA5; -.
DR PDBsum; 7CUM; -.
DR PDBsum; 7EB2; -.
DR AlphaFoldDB; Q9UBS5; -.
DR SMR; Q9UBS5; -.
DR BioGRID; 108825; 39.
DR ComplexPortal; CPX-2955; GABA-B receptor complex.
DR CORUM; Q9UBS5; -.
DR DIP; DIP-38394N; -.
DR IntAct; Q9UBS5; 16.
DR MINT; Q9UBS5; -.
DR STRING; 9606.ENSP00000366233; -.
DR BindingDB; Q9UBS5; -.
DR ChEMBL; CHEMBL2064; -.
DR DrugBank; DB00659; Acamprosate.
DR DrugBank; DB08891; Arbaclofen.
DR DrugBank; DB08892; Arbaclofen Placarbil.
DR DrugBank; DB00181; Baclofen.
DR DrugBank; DB02530; gamma-Aminobutyric acid.
DR DrugBank; DB00837; Progabide.
DR DrugBank; DB05010; SGS-742.
DR DrugBank; DB01956; Taurine.
DR DrugBank; DB06354; Tezampanel.
DR DrugCentral; Q9UBS5; -.
DR GuidetoPHARMACOLOGY; 240; -.
DR GlyGen; Q9UBS5; 7 sites.
DR iPTMnet; Q9UBS5; -.
DR PhosphoSitePlus; Q9UBS5; -.
DR BioMuta; GABBR1; -.
DR DMDM; 12643873; -.
DR jPOST; Q9UBS5; -.
DR MassIVE; Q9UBS5; -.
DR PaxDb; Q9UBS5; -.
DR PeptideAtlas; Q9UBS5; -.
DR PRIDE; Q9UBS5; -.
DR ProteomicsDB; 84047; -. [Q9UBS5-1]
DR ProteomicsDB; 84048; -. [Q9UBS5-2]
DR ProteomicsDB; 84049; -. [Q9UBS5-3]
DR ProteomicsDB; 84050; -. [Q9UBS5-4]
DR ProteomicsDB; 84051; -. [Q9UBS5-5]
DR ABCD; Q9UBS5; 1 sequenced antibody.
DR Antibodypedia; 50418; 546 antibodies from 44 providers.
DR DNASU; 2550; -.
DR Ensembl; ENST00000355973.7; ENSP00000348248.3; ENSG00000204681.11. [Q9UBS5-2]
DR Ensembl; ENST00000376977.7; ENSP00000366176.3; ENSG00000204681.11. [Q9UBS5-5]
DR Ensembl; ENST00000377012.8; ENSP00000366211.4; ENSG00000204681.11. [Q9UBS5-2]
DR Ensembl; ENST00000377016.8; ENSP00000366215.4; ENSG00000204681.11. [Q9UBS5-3]
DR Ensembl; ENST00000377034.9; ENSP00000366233.4; ENSG00000204681.11. [Q9UBS5-1]
DR Ensembl; ENST00000383537.8; ENSP00000373029.4; ENSG00000206466.10. [Q9UBS5-2]
DR Ensembl; ENST00000383541.8; ENSP00000373033.4; ENSG00000206466.10. [Q9UBS5-3]
DR Ensembl; ENST00000383542.8; ENSP00000373034.4; ENSG00000206466.10. [Q9UBS5-1]
DR Ensembl; ENST00000383543.7; ENSP00000373035.3; ENSG00000206466.10. [Q9UBS5-2]
DR Ensembl; ENST00000383636.8; ENSP00000373132.4; ENSG00000206511.10. [Q9UBS5-2]
DR Ensembl; ENST00000383637.8; ENSP00000373133.4; ENSG00000206511.10. [Q9UBS5-3]
DR Ensembl; ENST00000383638.8; ENSP00000373134.4; ENSG00000206511.10. [Q9UBS5-1]
DR Ensembl; ENST00000383639.6; ENSP00000373135.2; ENSG00000206511.10. [Q9UBS5-2]
DR Ensembl; ENST00000414980.6; ENSP00000406499.2; ENSG00000232632.8. [Q9UBS5-2]
DR Ensembl; ENST00000417759.5; ENSP00000391572.1; ENSG00000237112.8. [Q9UBS5-2]
DR Ensembl; ENST00000419674.5; ENSP00000399861.1; ENSG00000232569.8. [Q9UBS5-3]
DR Ensembl; ENST00000423604.6; ENSP00000388035.2; ENSG00000232632.8. [Q9UBS5-1]
DR Ensembl; ENST00000425097.6; ENSP00000411286.2; ENSG00000237112.8. [Q9UBS5-1]
DR Ensembl; ENST00000434660.6; ENSP00000412167.2; ENSG00000232632.8. [Q9UBS5-3]
DR Ensembl; ENST00000438094.5; ENSP00000406285.1; ENSG00000232632.8. [Q9UBS5-2]
DR Ensembl; ENST00000439457.5; ENSP00000406066.1; ENSG00000232569.8. [Q9UBS5-1]
DR Ensembl; ENST00000443440.6; ENSP00000399318.2; ENSG00000237112.8. [Q9UBS5-3]
DR Ensembl; ENST00000446436.6; ENSP00000394528.2; ENSG00000237112.8. [Q9UBS5-2]
DR Ensembl; ENST00000448754.5; ENSP00000405709.1; ENSG00000237051.8. [Q9UBS5-2]
DR Ensembl; ENST00000449163.5; ENSP00000411263.1; ENSG00000232569.8. [Q9UBS5-2]
DR Ensembl; ENST00000452300.6; ENSP00000408938.2; ENSG00000232569.8. [Q9UBS5-2]
DR Ensembl; ENST00000458612.6; ENSP00000416903.2; ENSG00000237051.8. [Q9UBS5-2]
DR Ensembl; ENST00000494877.5; ENSP00000419061.1; ENSG00000204681.11. [Q9UBS5-5]
DR Ensembl; ENST00000546913.2; ENSP00000448999.1; ENSG00000232569.8. [Q9UBS5-1]
DR Ensembl; ENST00000547410.5; ENSP00000448531.1; ENSG00000232569.8. [Q9UBS5-5]
DR Ensembl; ENST00000548767.2; ENSP00000446983.1; ENSG00000232632.8. [Q9UBS5-5]
DR Ensembl; ENST00000551140.2; ENSP00000448654.1; ENSG00000237112.8. [Q9UBS5-5]
DR Ensembl; ENST00000551423.2; ENSP00000449342.1; ENSG00000206511.10. [Q9UBS5-5]
DR Ensembl; ENST00000552399.2; ENSP00000449449.1; ENSG00000206466.10. [Q9UBS5-5]
DR GeneID; 2550; -.
DR KEGG; hsa:2550; -.
DR MANE-Select; ENST00000377034.9; ENSP00000366233.4; NM_001470.4; NP_001461.1.
DR UCSC; uc003nmp.5; human. [Q9UBS5-1]
DR CTD; 2550; -.
DR DisGeNET; 2550; -.
DR GeneCards; GABBR1; -.
DR HGNC; HGNC:4070; GABBR1.
DR HPA; ENSG00000204681; Low tissue specificity.
DR MIM; 603540; gene.
DR neXtProt; NX_Q9UBS5; -.
DR OpenTargets; ENSG00000204681; -.
DR PharmGKB; PA28484; -.
DR VEuPathDB; HostDB:ENSG00000204681; -.
DR eggNOG; KOG1055; Eukaryota.
DR GeneTree; ENSGT00940000157642; -.
DR HOGENOM; CLU_005240_2_0_1; -.
DR InParanoid; Q9UBS5; -.
DR OMA; WAGGEAC; -.
DR OrthoDB; 590810at2759; -.
DR PhylomeDB; Q9UBS5; -.
DR TreeFam; TF313965; -.
DR PathwayCommons; Q9UBS5; -.
DR Reactome; R-HSA-1296041; Activation of G protein gated Potassium channels.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR Reactome; R-HSA-420499; Class C/3 (Metabotropic glutamate/pheromone receptors).
DR Reactome; R-HSA-977444; GABA B receptor activation.
DR Reactome; R-HSA-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
DR SignaLink; Q9UBS5; -.
DR SIGNOR; Q9UBS5; -.
DR BioGRID-ORCS; 2550; 23 hits in 1084 CRISPR screens.
DR ChiTaRS; GABBR1; human.
DR GeneWiki; GABBR1; -.
DR GenomeRNAi; 2550; -.
DR Pharos; Q9UBS5; Tclin.
DR PRO; PR:Q9UBS5; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9UBS5; protein.
DR Bgee; ENSG00000204681; Expressed in right hemisphere of cerebellum and 126 other tissues.
DR ExpressionAtlas; Q9UBS5; baseline and differential.
DR Genevisible; Q9UBS5; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030673; C:axolemma; IEA:Ensembl.
DR GO; GO:0043198; C:dendritic shaft; IEA:Ensembl.
DR GO; GO:0043197; C:dendritic spine; IEA:Ensembl.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:1902712; C:G protein-coupled GABA receptor complex; IPI:ComplexPortal.
DR GO; GO:0038039; C:G protein-coupled receptor heterodimeric complex; IPI:UniProtKB.
DR GO; GO:0098982; C:GABA-ergic synapse; IEA:Ensembl.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IEA:Ensembl.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IEA:Ensembl.
DR GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR GO; GO:0008021; C:synaptic vesicle; IEA:Ensembl.
DR GO; GO:1990430; F:extracellular matrix protein binding; IEA:Ensembl.
DR GO; GO:0004965; F:G protein-coupled GABA receptor activity; IDA:UniProtKB.
DR GO; GO:0099579; F:G protein-coupled neurotransmitter receptor activity involved in regulation of postsynaptic membrane potential; IEA:Ensembl.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
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; IDA:UniProtKB.
DR GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IDA:UniProtKB.
DR GO; GO:0007194; P:negative regulation of adenylate cyclase activity; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0033602; P:negative regulation of dopamine secretion; IEA:Ensembl.
DR GO; GO:0032811; P:negative regulation of epinephrine secretion; IEA:Ensembl.
DR GO; GO:0014053; P:negative regulation of gamma-aminobutyric acid secretion; IEA:Ensembl.
DR GO; GO:0050805; P:negative regulation of synaptic transmission; IEA:Ensembl.
DR GO; GO:0150099; P:neuron-glial cell signaling; ISS:ARUK-UCL.
DR GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0014049; P:positive regulation of glutamate secretion; IEA:Ensembl.
DR GO; GO:0060124; P:positive regulation of growth hormone secretion; IEA:Ensembl.
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; IC:ComplexPortal.
DR CDD; cd15291; 7tmC_GABA-B-R1; 1.
DR CDD; cd00033; CCP; 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; PTHR10519; 1.
DR Pfam; PF00003; 7tm_3; 1.
DR Pfam; PF01094; ANF_receptor; 1.
DR Pfam; PF00084; Sushi; 1.
DR SMART; SM00032; CCP; 2.
DR SUPFAM; SSF53822; SSF53822; 1.
DR SUPFAM; SSF57535; SSF57535; 2.
DR PROSITE; PS50259; G_PROTEIN_RECEP_F3_4; 1.
DR PROSITE; PS50923; SUSHI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cell projection;
KW Coiled coil; Direct protein sequencing; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein;
KW Postsynaptic cell membrane; Receptor; Reference proteome; Repeat; Secreted;
KW Signal; Sushi; Synapse; Transducer; Transmembrane; Transmembrane helix.
FT SIGNAL 1..14
FT /evidence="ECO:0000255"
FT CHAIN 15..961
FT /note="Gamma-aminobutyric acid type B receptor subunit 1"
FT /id="PRO_0000012949"
FT TOPO_DOM 15..591
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 592..612
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 613..631
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 632..652
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 653..667
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 668..688
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 689..710
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 711..731
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 732..768
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 769..789
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 790..804
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 805..825
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 826..833
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 834..854
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 855..961
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 30..96
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 98..159
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT REGION 867..892
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 888..916
FT /note="Interaction with ATF4"
FT /evidence="ECO:0000250"
FT REGION 909..961
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 869..925
FT /evidence="ECO:0000255"
FT COMPBIAS 867..884
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 927..946
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 247
FT /ligand="4-aminobutanoate"
FT /ligand_id="ChEBI:CHEBI:59888"
FT /ligand_note="agonist"
FT /evidence="ECO:0000269|PubMed:24305054,
FT ECO:0007744|PDB:4MS3"
FT BINDING 247
FT /ligand="baclofen"
FT /ligand_id="ChEBI:CHEBI:187893"
FT /ligand_note="agonist"
FT /evidence="ECO:0000269|PubMed:24305054,
FT ECO:0007744|PDB:4MS4"
FT BINDING 247
FT /ligand="phaclofen"
FT /ligand_id="ChEBI:CHEBI:188150"
FT /ligand_note="antagonist"
FT /evidence="ECO:0000269|PubMed:24305054,
FT ECO:0007744|PDB:4MRM"
FT BINDING 270
FT /ligand="4-aminobutanoate"
FT /ligand_id="ChEBI:CHEBI:59888"
FT /ligand_note="agonist"
FT /evidence="ECO:0000269|PubMed:24305054,
FT ECO:0007744|PDB:4MS3"
FT BINDING 270
FT /ligand="baclofen"
FT /ligand_id="ChEBI:CHEBI:187893"
FT /ligand_note="agonist"
FT /evidence="ECO:0000269|PubMed:24305054,
FT ECO:0007744|PDB:4MS4"
FT BINDING 270
FT /ligand="phaclofen"
FT /ligand_id="ChEBI:CHEBI:188150"
FT /ligand_note="antagonist"
FT /evidence="ECO:0000269|PubMed:24305054,
FT ECO:0007744|PDB:4MRM"
FT BINDING 287
FT /ligand="4-aminobutanoate"
FT /ligand_id="ChEBI:CHEBI:59888"
FT /ligand_note="agonist"
FT /evidence="ECO:0000269|PubMed:24305054,
FT ECO:0007744|PDB:4MS3"
FT BINDING 287
FT /ligand="baclofen"
FT /ligand_id="ChEBI:CHEBI:187893"
FT /ligand_note="agonist"
FT /evidence="ECO:0000269|PubMed:24305054,
FT ECO:0007744|PDB:4MS4"
FT BINDING 287
FT /ligand="phaclofen"
FT /ligand_id="ChEBI:CHEBI:188150"
FT /ligand_note="antagonist"
FT /evidence="ECO:0000269|PubMed:24305054,
FT ECO:0007744|PDB:4MRM"
FT BINDING 367
FT /ligand="4-aminobutanoate"
FT /ligand_id="ChEBI:CHEBI:59888"
FT /ligand_note="agonist"
FT /evidence="ECO:0000269|PubMed:24305054,
FT ECO:0007744|PDB:4MS3"
FT BINDING 367
FT /ligand="baclofen"
FT /ligand_id="ChEBI:CHEBI:187893"
FT /ligand_note="agonist"
FT /evidence="ECO:0000269|PubMed:24305054,
FT ECO:0007744|PDB:4MS4"
FT BINDING 466
FT /ligand="4-aminobutanoate"
FT /ligand_id="ChEBI:CHEBI:59888"
FT /ligand_note="agonist"
FT /evidence="ECO:0000269|PubMed:24305054,
FT ECO:0007744|PDB:4MS3"
FT BINDING 466
FT /ligand="baclofen"
FT /ligand_id="ChEBI:CHEBI:187893"
FT /ligand_note="agonist"
FT /evidence="ECO:0000269|PubMed:24305054,
FT ECO:0007744|PDB:4MS4"
FT BINDING 466
FT /ligand="phaclofen"
FT /ligand_id="ChEBI:CHEBI:188150"
FT /ligand_note="antagonist"
FT /evidence="ECO:0000269|PubMed:24305054,
FT ECO:0007744|PDB:4MR7"
FT MOD_RES 873
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9WV18"
FT MOD_RES 930
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9WV18"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 409
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 440
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:24305054"
FT CARBOHYD 482
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:24305054"
FT CARBOHYD 502
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 514
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 100..145
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 131..157
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 220..246
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:24305054"
FT DISULFID 376..410
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:24305054"
FT VAR_SEQ 1..164
FT /note="MLLLLLLAPLFLRPPGAGGAQTPNATSEGCQIIHPPWEGGIRYRGLTRDQVK
FT AINFLPVDYEIEYVCRGEREVVGPKVRKCLANGSWTDMDTPSRCVRICSKSYLTLENGK
FT VFLTGGDLPALDGARVDFRCDPDFHLVGSSRSICSQGQWSTPKPHCQVNRTPH -> MG
FT PGAPFARVGWPLPLLVVMAAGVAPVWASHSPHLPRPHSRVPPHPS (in isoform
FT 1B)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9844003, ECO:0000303|PubMed:9872316"
FT /id="VSP_002037"
FT VAR_SEQ 98..159
FT /note="Missing (in isoform 1C)"
FT /evidence="ECO:0000303|PubMed:9872316, ECO:0000303|Ref.6"
FT /id="VSP_002038"
FT VAR_SEQ 570..961
FT /note="GGSPPADQTLVIKTFRFLSQKLFISVSVLSSLGIVLAVVCLSFNIYNSHVRY
FT IQNSQPNLNNLTAVGCSLALAAVFPLGLDGYHIGRNQFPFVCQARLWLLGLGFSLGYGS
FT MFTKIWWVHTVFTKKEEKKEWRKTLEPWKLYATVGLLVGMDVLTLAIWQIVDPLHRTIE
FT TFAKEEPKEDIDVSILPQLEHCSSRKMNTWLGIFYGYKGLLLLLGIFLAYETKSVSTEK
FT INDHRAVGMAIYNVAVLCLITAPVTMILSSQQDAAFAFASLAIVFSSYITLVVLFVPKM
FT RRLITRGEWQSEAQDTMKTGSSTNNNEEEKSRLLEKENRELEKIIAEKEERVSELRHQL
FT QSRQQLRSRRHPPTPPEPSGGLPRGPPEPPDRLSCDGSRVHLLYK -> VISRTHSPT
FT (in isoform 1E)"
FT /evidence="ECO:0000305"
FT /id="VSP_002039"
FT VAR_SEQ 905..961
FT /note="KEERVSELRHQLQSRQQLRSRRHPPTPPEPSGGLPRGPPEPPDRLSCDGSRV
FT HLLYK -> SGGLPRGPPEPPDRLSCDGSRVHLLYK (in isoform 1D)"
FT /evidence="ECO:0000305"
FT /id="VSP_002040"
FT VARIANT 20
FT /note="A -> V (in dbSNP:rs1805056)"
FT /evidence="ECO:0000269|PubMed:10402495,
FT ECO:0000269|PubMed:14574404, ECO:0000269|PubMed:9933300"
FT /id="VAR_010146"
FT VARIANT 489
FT /note="G -> S (in dbSNP:rs1805057)"
FT /evidence="ECO:0000269|PubMed:10402495,
FT ECO:0000269|PubMed:10906333, ECO:0000269|PubMed:9933300"
FT /id="VAR_010147"
FT VARIANT 645
FT /note="F -> L (in dbSNP:rs2076489)"
FT /id="VAR_049279"
FT MUTAGEN 182
FT /note="W->A: Abolishes signaling via G-proteins. Abolishes
FT antagonist binding."
FT /evidence="ECO:0000269|PubMed:24305054"
FT MUTAGEN 230
FT /note="Y->A: Slightly decreases signaling via G-proteins."
FT /evidence="ECO:0000269|PubMed:22660477"
FT MUTAGEN 234
FT /note="Y->A: Decreases signaling via G-proteins."
FT /evidence="ECO:0000269|PubMed:22660477"
FT MUTAGEN 287
FT /note="H->A: Strongly reduces signaling via G-proteins.
FT Abolishes antagonist binding."
FT /evidence="ECO:0000269|PubMed:24305054"
FT MUTAGEN 367
FT /note="Y->A: Strongly reduces signaling via G-proteins. No
FT effect on antagonist binding."
FT /evidence="ECO:0000269|PubMed:24305054"
FT MUTAGEN 395
FT /note="W->A: Strongly reduces signaling via G-proteins.
FT Strongly reduces antagonist binding."
FT /evidence="ECO:0000269|PubMed:24305054"
FT CONFLICT 2
FT /note="L -> M (in Ref. 4; Y11044)"
FT /evidence="ECO:0000305"
FT CONFLICT 21
FT /note="Q -> H (in Ref. 2; CAA09939/CAA09941)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="P -> L (in Ref. 3; AAC98508)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="V -> A (in Ref. 2; CAA09939)"
FT /evidence="ECO:0000305"
FT CONFLICT 322
FT /note="Missing (in Ref. 7; CAA09031)"
FT /evidence="ECO:0000305"
FT CONFLICT 542
FT /note="L -> P (in Ref. 4; Y11044)"
FT /evidence="ECO:0000305"
FT CONFLICT 691
FT /note="V -> G (in Ref. 4; Y11044)"
FT /evidence="ECO:0000305"
FT CONFLICT 905..934
FT /note="Missing (in Ref. 7; CAA09031)"
FT /evidence="ECO:0000305"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:6HKC"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:6HKC"
FT STRAND 62..67
FT /evidence="ECO:0007829|PDB:6HKC"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:6HKC"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:6HKC"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:6HKC"
FT STRAND 83..89
FT /evidence="ECO:0007829|PDB:6HKC"
FT STRAND 168..176
FT /evidence="ECO:0007829|PDB:4MS4"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:4MS4"
FT HELIX 185..200
FT /evidence="ECO:0007829|PDB:4MS4"
FT TURN 203..205
FT /evidence="ECO:0007829|PDB:4MS4"
FT STRAND 209..217
FT /evidence="ECO:0007829|PDB:4MS4"
FT HELIX 222..233
FT /evidence="ECO:0007829|PDB:4MS4"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:4MS4"
FT STRAND 240..243
FT /evidence="ECO:0007829|PDB:4MS4"
FT HELIX 247..256
FT /evidence="ECO:0007829|PDB:4MS4"
FT HELIX 257..260
FT /evidence="ECO:0007829|PDB:4MS4"
FT STRAND 263..268
FT /evidence="ECO:0007829|PDB:4MS4"
FT HELIX 272..275
FT /evidence="ECO:0007829|PDB:4MS4"
FT TURN 277..279
FT /evidence="ECO:0007829|PDB:4MS4"
FT STRAND 283..287
FT /evidence="ECO:0007829|PDB:4MS4"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:4MS4"
FT HELIX 293..303
FT /evidence="ECO:0007829|PDB:4MS4"
FT STRAND 308..316
FT /evidence="ECO:0007829|PDB:4MS4"
FT HELIX 317..332
FT /evidence="ECO:0007829|PDB:4MS4"
FT STRAND 336..345
FT /evidence="ECO:0007829|PDB:4MS4"
FT HELIX 348..356
FT /evidence="ECO:0007829|PDB:4MS4"
FT STRAND 361..365
FT /evidence="ECO:0007829|PDB:4MS4"
FT HELIX 368..381
FT /evidence="ECO:0007829|PDB:4MS4"
FT STRAND 385..387
FT /evidence="ECO:0007829|PDB:4MRM"
FT STRAND 389..393
FT /evidence="ECO:0007829|PDB:4MS4"
FT HELIX 400..402
FT /evidence="ECO:0007829|PDB:4MS4"
FT HELIX 412..419
FT /evidence="ECO:0007829|PDB:4MS4"
FT STRAND 423..427
FT /evidence="ECO:0007829|PDB:4MS4"
FT HELIX 443..453
FT /evidence="ECO:0007829|PDB:4MS4"
FT STRAND 454..456
FT /evidence="ECO:0007829|PDB:7C7Q"
FT HELIX 458..460
FT /evidence="ECO:0007829|PDB:4MS4"
FT TURN 462..466
FT /evidence="ECO:0007829|PDB:4MS4"
FT HELIX 467..484
FT /evidence="ECO:0007829|PDB:4MS4"
FT HELIX 495..497
FT /evidence="ECO:0007829|PDB:4MS4"
FT HELIX 504..514
FT /evidence="ECO:0007829|PDB:4MS4"
FT STRAND 517..520
FT /evidence="ECO:0007829|PDB:4MS4"
FT STRAND 523..526
FT /evidence="ECO:0007829|PDB:4MS4"
FT TURN 529..531
FT /evidence="ECO:0007829|PDB:4MS4"
FT STRAND 536..543
FT /evidence="ECO:0007829|PDB:4MS4"
FT STRAND 546..554
FT /evidence="ECO:0007829|PDB:4MS4"
FT TURN 555..558
FT /evidence="ECO:0007829|PDB:4MS4"
FT STRAND 559..562
FT /evidence="ECO:0007829|PDB:4MS4"
FT HELIX 569..571
FT /evidence="ECO:0007829|PDB:4MS4"
FT STRAND 580..584
FT /evidence="ECO:0007829|PDB:7C7S"
FT HELIX 589..615
FT /evidence="ECO:0007829|PDB:7C7S"
FT TURN 616..618
FT /evidence="ECO:0007829|PDB:7C7S"
FT STRAND 619..625
FT /evidence="ECO:0007829|PDB:7C7S"
FT HELIX 627..648
FT /evidence="ECO:0007829|PDB:7C7S"
FT TURN 651..653
FT /evidence="ECO:0007829|PDB:7C7S"
FT TURN 656..658
FT /evidence="ECO:0007829|PDB:6W2Y"
FT HELIX 659..692
FT /evidence="ECO:0007829|PDB:7C7S"
FT HELIX 707..731
FT /evidence="ECO:0007829|PDB:7C7S"
FT STRAND 735..740
FT /evidence="ECO:0007829|PDB:7C7S"
FT STRAND 749..751
FT /evidence="ECO:0007829|PDB:7C7Q"
FT STRAND 753..762
FT /evidence="ECO:0007829|PDB:7C7S"
FT HELIX 766..790
FT /evidence="ECO:0007829|PDB:7C7S"
FT STRAND 797..799
FT /evidence="ECO:0007829|PDB:7C7S"
FT HELIX 802..825
FT /evidence="ECO:0007829|PDB:7C7S"
FT HELIX 826..828
FT /evidence="ECO:0007829|PDB:6W2Y"
FT HELIX 830..858
FT /evidence="ECO:0007829|PDB:7C7S"
FT TURN 859..861
FT /evidence="ECO:0007829|PDB:7C7S"
FT HELIX 885..917
FT /evidence="ECO:0007829|PDB:4PAS"
SQ SEQUENCE 961 AA; 108320 MW; 54E7349CD02B633F CRC64;
MLLLLLLAPL FLRPPGAGGA QTPNATSEGC QIIHPPWEGG IRYRGLTRDQ VKAINFLPVD
YEIEYVCRGE REVVGPKVRK CLANGSWTDM DTPSRCVRIC SKSYLTLENG KVFLTGGDLP
ALDGARVDFR CDPDFHLVGS SRSICSQGQW STPKPHCQVN RTPHSERRAV YIGALFPMSG
GWPGGQACQP AVEMALEDVN SRRDILPDYE LKLIHHDSKC DPGQATKYLY ELLYNDPIKI
ILMPGCSSVS TLVAEAARMW NLIVLSYGSS SPALSNRQRF PTFFRTHPSA TLHNPTRVKL
FEKWGWKKIA TIQQTTEVFT STLDDLEERV KEAGIEITFR QSFFSDPAVP VKNLKRQDAR
IIVGLFYETE ARKVFCEVYK ERLFGKKYVW FLIGWYADNW FKIYDPSINC TVDEMTEAVE
GHITTEIVML NPANTRSISN MTSQEFVEKL TKRLKRHPEE TGGFQEAPLA YDAIWALALA
LNKTSGGGGR SGVRLEDFNY NNQTITDQIY RAMNSSSFEG VSGHVVFDAS GSRMAWTLIE
QLQGGSYKKI GYYDSTKDDL SWSKTDKWIG GSPPADQTLV IKTFRFLSQK LFISVSVLSS
LGIVLAVVCL SFNIYNSHVR YIQNSQPNLN NLTAVGCSLA LAAVFPLGLD GYHIGRNQFP
FVCQARLWLL GLGFSLGYGS MFTKIWWVHT VFTKKEEKKE WRKTLEPWKL YATVGLLVGM
DVLTLAIWQI VDPLHRTIET FAKEEPKEDI DVSILPQLEH CSSRKMNTWL GIFYGYKGLL
LLLGIFLAYE TKSVSTEKIN DHRAVGMAIY NVAVLCLITA PVTMILSSQQ DAAFAFASLA
IVFSSYITLV VLFVPKMRRL ITRGEWQSEA QDTMKTGSST NNNEEEKSRL LEKENRELEK
IIAEKEERVS ELRHQLQSRQ QLRSRRHPPT PPEPSGGLPR GPPEPPDRLS CDGSRVHLLY
K
