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Q9Z0U4

- GABR1_RAT

UniProt

Q9Z0U4 - GABR1_RAT

Protein

Gamma-aminobutyric acid type B receptor subunit 1

Gene

Gabbr1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    Functioni

    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.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei246 – 2461AgonistBy similarity
    Binding sitei269 – 2691AgonistBy similarity
    Binding sitei286 – 2861AgonistBy similarity
    Binding sitei366 – 3661AgonistBy similarity
    Binding sitei394 – 3941AgonistBy similarity
    Binding sitei465 – 4651AgonistBy similarity

    GO - Molecular functioni

    1. G-protein coupled GABA receptor activity Source: RGD
    2. protein binding Source: IntAct
    3. transcription factor binding Source: RGD

    GO - Biological processi

    1. adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway Source: UniProtKB
    2. gamma-aminobutyric acid signaling pathway Source: UniProtKB
    3. negative regulation of adenylate cyclase activity Source: MGI
    4. negative regulation of cell proliferation Source: RGD
    5. negative regulation of dopamine secretion Source: RGD
    6. negative regulation of epinephrine secretion Source: RGD
    7. negative regulation of gamma-aminobutyric acid secretion Source: RGD
    8. negative regulation of synaptic transmission Source: RGD
    9. osteoblast differentiation Source: RGD
    10. positive regulation of glutamate secretion Source: RGD
    11. positive regulation of growth hormone secretion Source: RGD
    12. regulation of cAMP biosynthetic process Source: RGD
    13. regulation of glutamate secretion Source: RGD
    14. response to ethanol Source: RGD
    15. response to nicotine Source: RGD

    Keywords - Molecular functioni

    G-protein coupled receptor, Receptor, Transducer

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Gamma-aminobutyric acid type B receptor subunit 1
    Short name:
    GABA-B receptor 1
    Short name:
    GABA-B-R1
    Short name:
    GABA-BR1
    Short name:
    GABABR1
    Short name:
    Gb1
    Gene namesi
    Name:Gabbr1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi621537. Gabbr1.

    Subcellular locationi

    Cell membrane; Multi-pass membrane protein. Cell junctionsynapsepostsynaptic cell membrane; Multi-pass membrane protein. Cell projectiondendrite
    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.

    GO - Cellular componenti

    1. axolemma Source: RGD
    2. cell junction Source: UniProtKB-KW
    3. dendritic shaft Source: RGD
    4. dendritic spine Source: RGD
    5. endoplasmic reticulum membrane Source: RGD
    6. extracellular space Source: RGD
    7. G-protein coupled receptor heterodimeric complex Source: UniProtKB
    8. integral component of plasma membrane Source: UniProtKB
    9. intracellular membrane-bounded organelle Source: RGD
    10. membrane raft Source: RGD
    11. mitochondrial membrane Source: RGD
    12. neuronal cell body Source: RGD
    13. neuron projection Source: RGD
    14. postsynaptic membrane Source: UniProtKB-SubCell
    15. synaptic vesicle Source: RGD

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cell projection, Membrane, Postsynaptic cell membrane, Synapse

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi247 – 2471S → A: No change in the affinity for GABA. 1 Publication
    Mutagenesisi268 – 2681S → A: No change in the affinity for GABA. 1 Publication
    Mutagenesisi269 – 2691S → A: Decrease in the affinity for GABA. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1616Sequence AnalysisAdd
    BLAST
    Chaini17 – 991975Gamma-aminobutyric acid type B receptor subunit 1PRO_0000012951Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi23 – 231N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi83 – 831N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi99 ↔ 1441 PublicationPROSITE-ProRule annotation
    Disulfide bondi130 ↔ 1561 PublicationPROSITE-ProRule annotation
    Disulfide bondi219 ↔ 245PROSITE-ProRule annotation
    Disulfide bondi375 ↔ 409PROSITE-ProRule annotation
    Glycosylationi408 – 4081N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi439 – 4391N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi481 – 4811N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi501 – 5011N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi513 – 5131N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ9Z0U4.
    PRIDEiQ9Z0U4.

    PTM databases

    PhosphoSiteiQ9Z0U4.

    Expressioni

    Tissue specificityi

    Isoform 1A, isoform 1B and isoform 1C are expressed in testis, stomach, spinal cord and brain including cerebral cortical layers, pyramidal cell layers of the hippocampus, granular cell layers of the dentate gyrus, basal ganglia, cerebellum (predominantly in Purkinje cells followed by granular layer). Isoform 1B is also expressed in kidney and liver. Isoform 1D is expressed in forebrain, cerebellum, eye, kidney, and urinary bladder.3 Publications

    Gene expression databases

    ArrayExpressiQ9Z0U4.
    GenevestigatoriQ9Z0U4.

    Interactioni

    Subunit structurei

    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. Interacts with JAKMIP1.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Gabbr2O888718EBI-7090268,EBI-7090239

    Protein-protein interaction databases

    BioGridi249557. 2 interactions.
    IntActiQ9Z0U4. 1 interaction.

    Structurei

    Secondary structure

    1
    991
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi96 – 983
    Helixi101 – 1044
    Beta strandi109 – 1124
    Turni120 – 1234
    Beta strandi125 – 1306
    Beta strandi134 – 1363
    Beta strandi141 – 1455
    Beta strandi148 – 1514
    Beta strandi156 – 1583

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1SRZNMR-A96-159[»]
    1SS2NMR-A96-159[»]
    DisProtiDP00463.
    ProteinModelPortaliQ9Z0U4.
    SMRiQ9Z0U4. Positions 96-159.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Z0U4.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini17 – 590574ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini612 – 63019CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini652 – 66615ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini688 – 70922CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini731 – 79767ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini819 – 83416CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini856 – 8638ExtracellularSequence Analysis
    Topological domaini885 – 991107CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei591 – 61121Helical; Name=1Sequence AnalysisAdd
    BLAST
    Transmembranei631 – 65121Helical; Name=2Sequence AnalysisAdd
    BLAST
    Transmembranei667 – 68721Helical; Name=3Sequence AnalysisAdd
    BLAST
    Transmembranei710 – 73021Helical; Name=4Sequence AnalysisAdd
    BLAST
    Transmembranei798 – 81821Helical; Name=5Sequence AnalysisAdd
    BLAST
    Transmembranei835 – 85521Helical; Name=6Sequence AnalysisAdd
    BLAST
    Transmembranei864 – 88421Helical; Name=7Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini29 – 9567Sushi 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini97 – 15862Sushi 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni918 – 94629Interaction with ATF4Add
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili901 – 95555Sequence AnalysisAdd
    BLAST

    Domaini

    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.

    Sequence similaritiesi

    Contains 2 Sushi (CCP/SCR) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0683.
    HOGENOMiHOG000016575.
    HOVERGENiHBG051688.
    InParanoidiQ9Z0U4.
    KOiK04615.
    PhylomeDBiQ9Z0U4.
    TreeFamiTF313965.

    Family and domain databases

    InterProiIPR001828. ANF_lig-bd_rcpt.
    IPR002455. GPCR3_GABA-B.
    IPR017978. GPCR_3_C.
    IPR002456. GPCR_3_GABA_rcpt_B1.
    IPR028082. Peripla_BP_I.
    IPR000436. Sushi_SCR_CCP.
    [Graphical view]
    PANTHERiPTHR10519. PTHR10519. 1 hit.
    PfamiPF00003. 7tm_3. 1 hit.
    PF01094. ANF_receptor. 1 hit.
    PF00084. Sushi. 2 hits.
    [Graphical view]
    PRINTSiPR01177. GABAB1RECPTR.
    SMARTiSM00032. CCP. 2 hits.
    [Graphical view]
    SUPFAMiSSF53822. SSF53822. 1 hit.
    SSF57535. SSF57535. 2 hits.
    PROSITEiPS50259. G_PROTEIN_RECEP_F3_4. 1 hit.
    PS50923. SUSHI. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1E (identifier: Q9Z0U4-1) [UniParc]FASTAAdd to Basket

    Also known as: 1C

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MLLLLLVPLF LRPLGAGGAQ TPNATSEGCQ IIHPPWEGGI RYRGLTRDQV    50
    KAINFLPVDY EIEYVCRGER EVVGPKVRKC LANGSWTDMD TPSRCVRICS 100
    KSYLTLENGK VFLTGGDLPA LDGARVEFRC DPDFHLVGSS RSVCSQGQWS 150
    TPKPHCQVNR TPHSERRAVY IGALFPMSGG WPGGQACQPA VEMALEDVNS 200
    RRDILPDYEL KLIHHDSKCD PGQATKYLYE LLYNDPIKII LMPGCSSVST 250
    LVAEAARMWN LIVLSYGSSS PALSNRQRFP TFFRTHPSAT LHNPTRVKLF 300
    EKWGWKKIAT IQQTTEVFTS TLDDLEERVK EAGIEITFRQ SFFSDPAVPV 350
    KNLKRQDARI IVGLFYETEA RKVFCEVYKE RLFGKKYVWF LIGWYADNWF 400
    KTYDPSINCT VEEMTEAVEG HITTEIVMLN PANTRSISNM TSQEFVEKLT 450
    KRLKRHPEET GGFQEAPLAY DAIWALALAL NKTSGGGGRS GVRLEDFNYN 500
    NQTITDQIYR AMNSSSFEGV SGHVVFDASG SRMAWTLIEQ LQGGSYKKIG 550
    YYDSTKDDLS WSKTDKWIGG SPPADQTLVI KTFRFLSQKL FISVSVLSSL 600
    GIVLAVVCLS FNIYNSHVRY IQNSQPNLNN LTAVGCSLAL AAVFPLGLDG 650
    YHIGRSQFPF VCQARLWLLG LGFSLGYGSM FTKIWWVHTV FTKKEEKKEW 700
    RKTLEPWKLY ATVGLLVGMD VLTLAIWQIV DPLHRTIETF AKEEPKEDID 750
    VSILPQLEHC SSKKMNTWLG ELWSFAVSSD VQRRATVGGD SPICVWPAPE 800
    SIFYGYKGLL LLLGIFLAYE TKSVSTEKIN DHRAVGMAIY NVAVLCLITA 850
    PVTMILSSQQ DAAFAFASLA IVFSSYITLV VLFVPKMRRL ITRGEWQSET 900
    QDTMKTGSST NNNEEEKSRL LEKENRELEK IIAEKEERVS ELRHQLQSRQ 950
    QLRSRRHPPT PPDPSGGLPR GPSEPPDRLS CDGSRVHLLY K 991
    Length:991
    Mass (Da):111,534
    Last modified:May 1, 1999 - v1
    Checksum:i012CD293D4B444A2
    GO
    Isoform 1A (identifier: Q9Z0U4-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         771-801: Missing.

    Show »
    Length:960
    Mass (Da):108,204
    Checksum:i05B7FBBCBE9DBF94
    GO
    Isoform 1B (identifier: Q9Z0U4-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-163: MLLLLLVPLF...PHCQVNRTPH → MGPGGPCTPV...PHPRVPPHPS
         771-801: Missing.

    Show »
    Length:844
    Mass (Da):95,038
    Checksum:iB3417F53BE4877E9
    GO
    Isoform 1C (identifier: Q9Z0U4-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-163: MLLLLLVPLF...PHCQVNRTPH → MGPGGPCTPV...PHPRVPPHPS

    Show »
    Length:875
    Mass (Da):98,368
    Checksum:iE7E9EDA9132D37F2
    GO
    Isoform 1D (identifier: Q9Z0U4-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-163: MLLLLLVPLF...PHCQVNRTPH → MGPGGPCTPV...PHPRVPPHPS
         771-801: Missing.
         935-991: KEERVSELRH...DGSRVHLLYK → VCGDKQPGPPVSEGGLPVVGPSIEV

    Show »
    Length:812
    Mass (Da):90,921
    Checksum:i5EFD7B169A727FDE
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 163163MLLLL…NRTPH → MGPGGPCTPVGWPLPLLLVM AAGVAPVWASHSPHLPRPHP RVPPHPS in isoform 1B, isoform 1C and isoform 1D. 2 PublicationsVSP_002044Add
    BLAST
    Alternative sequencei771 – 80131Missing in isoform 1A, isoform 1B and isoform 1D. 3 PublicationsVSP_002045Add
    BLAST
    Alternative sequencei935 – 99157KEERV…HLLYK → VCGDKQPGPPVSEGGLPVVG PSIEV in isoform 1D. 1 PublicationVSP_002046Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y10369 mRNA. Translation: CAA71398.1.
    Y10370 mRNA. Translation: CAA71399.1.
    AB016160 mRNA. Translation: BAA34708.1.
    AB016161 mRNA. Translation: BAA34709.1.
    AF110797, AF110796 Genomic DNA. Translation: AAD19656.1.
    AF110797, AF110796 Genomic DNA. Translation: AAD19657.1.
    AF110797, AF110796 Genomic DNA. Translation: AAD19658.1.
    AF110797, AF110796 Genomic DNA. Translation: AAD19659.1.
    RefSeqiNP_112290.2. NM_031028.3. [Q9Z0U4-2]
    XP_006255941.1. XM_006255879.1. [Q9Z0U4-1]
    UniGeneiRn.30059.

    Genome annotation databases

    GeneIDi81657.
    KEGGirno:81657.
    UCSCiRGD:621537. rat. [Q9Z0U4-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y10369 mRNA. Translation: CAA71398.1 .
    Y10370 mRNA. Translation: CAA71399.1 .
    AB016160 mRNA. Translation: BAA34708.1 .
    AB016161 mRNA. Translation: BAA34709.1 .
    AF110797 , AF110796 Genomic DNA. Translation: AAD19656.1 .
    AF110797 , AF110796 Genomic DNA. Translation: AAD19657.1 .
    AF110797 , AF110796 Genomic DNA. Translation: AAD19658.1 .
    AF110797 , AF110796 Genomic DNA. Translation: AAD19659.1 .
    RefSeqi NP_112290.2. NM_031028.3. [Q9Z0U4-2 ]
    XP_006255941.1. XM_006255879.1. [Q9Z0U4-1 ]
    UniGenei Rn.30059.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1SRZ NMR - A 96-159 [» ]
    1SS2 NMR - A 96-159 [» ]
    DisProti DP00463.
    ProteinModelPortali Q9Z0U4.
    SMRi Q9Z0U4. Positions 96-159.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 249557. 2 interactions.
    IntActi Q9Z0U4. 1 interaction.

    Chemistry

    BindingDBi Q9Z0U4.
    ChEMBLi CHEMBL2753.
    GuidetoPHARMACOLOGYi 240.

    Protein family/group databases

    GPCRDBi Search...

    PTM databases

    PhosphoSitei Q9Z0U4.

    Proteomic databases

    PaxDbi Q9Z0U4.
    PRIDEi Q9Z0U4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 81657.
    KEGGi rno:81657.
    UCSCi RGD:621537. rat. [Q9Z0U4-1 ]

    Organism-specific databases

    CTDi 2550.
    RGDi 621537. Gabbr1.

    Phylogenomic databases

    eggNOGi COG0683.
    HOGENOMi HOG000016575.
    HOVERGENi HBG051688.
    InParanoidi Q9Z0U4.
    KOi K04615.
    PhylomeDBi Q9Z0U4.
    TreeFami TF313965.

    Miscellaneous databases

    EvolutionaryTracei Q9Z0U4.
    NextBioi 615214.
    PROi Q9Z0U4.

    Gene expression databases

    ArrayExpressi Q9Z0U4.
    Genevestigatori Q9Z0U4.

    Family and domain databases

    InterProi IPR001828. ANF_lig-bd_rcpt.
    IPR002455. GPCR3_GABA-B.
    IPR017978. GPCR_3_C.
    IPR002456. GPCR_3_GABA_rcpt_B1.
    IPR028082. Peripla_BP_I.
    IPR000436. Sushi_SCR_CCP.
    [Graphical view ]
    PANTHERi PTHR10519. PTHR10519. 1 hit.
    Pfami PF00003. 7tm_3. 1 hit.
    PF01094. ANF_receptor. 1 hit.
    PF00084. Sushi. 2 hits.
    [Graphical view ]
    PRINTSi PR01177. GABAB1RECPTR.
    SMARTi SM00032. CCP. 2 hits.
    [Graphical view ]
    SUPFAMi SSF53822. SSF53822. 1 hit.
    SSF57535. SSF57535. 2 hits.
    PROSITEi PS50259. G_PROTEIN_RECEP_F3_4. 1 hit.
    PS50923. SUSHI. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Expression cloning of GABA(B) receptors uncovers similarity to metabotropic glutamate receptors."
      Kaupmann K., Huggel K., Heid J., Flor P.J., Bischoff S., Mickel S.J., McMaster G., Angst C., Bittiger H., Froestl W., Bettler B.
      Nature 386:239-246(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1A AND 1B), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Strain: RICO.
      Tissue: Brain cortex and Cerebellum.
    2. "Cloning and tissue distribution of novel splice variants of the rat GABAB receptor."
      Isomoto S., Kaibara M., Sakurai-Yamashita Y., Nagayama Y., Uezono Y., Yano K., Taniyama K.
      Biochem. Biophys. Res. Commun. 253:10-15(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1C AND 1D), TISSUE SPECIFICITY.
      Tissue: Cerebellum.
    3. "Alternative splicing generates a novel isoform of the rat metabotropic GABA(B)R1 receptor."
      Pfaff T., Malitschek B., Kaupmann K., Prezeau L., Pin J.-P., Bettler B., Karschin A.
      Eur. J. Neurosci. 11:2874-2882(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 1E).
      Strain: Wistar.
      Tissue: Hippocampus.
    4. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1A), INTERACTION WITH GABBR2.
      Tissue: Brain.
    5. "Synthesis of the nanomolar photoaffinity GABA(B) receptor ligand CGP 71872 reveals diversity in the tissue distribution of GABA(B) receptor forms."
      Belley M., Sullivan R., Reeves A., Evans J.F., O'Neill G.P., Ng G.Y.K.
      Bioorg. Med. Chem. 7:2697-2704(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    6. "Role of heteromer formation in GABAB receptor function."
      Kuner R., Koehr G., Gruenewald S., Eisenhardt G., Bach A., Kornau H.-C.
      Science 283:74-77(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GABBR2.
    7. "The metabotropic GABAB receptor directly interacts with the activating transcription factor 4."
      Nehring R.B., Horikawa H.P.M., El Far O., Kneussel M., Brandstatter J.H., Stamm S., Wischmeyer E., Betz H., Karschin A.
      J. Biol. Chem. 275:35185-35191(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ATF4, SUBCELLULAR LOCATION.
    8. "Ca(2+) requirement for high-affinity gamma-aminobutyric acid (GABA) binding at GABA(B) receptors: involvement of serine 269 of the GABA(B)R1 subunit."
      Galvez T., Urwyler S., Prezeau L., Mosbacher J., Joly C., Malitschek B., Heid J., Brabet I., Froestl W., Bettler B., Kaupmann K., Pin J.-P.
      Mol. Pharmacol. 57:419-426(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF SER-247; SER-268 AND SER-269.
    9. Cited for: INTERACTION WITH JAKMIP1.
    10. "Structural analysis of the complement control protein (CCP) modules of GABA(B) receptor 1a: only one of the two CCP modules is compactly folded."
      Blein S., Ginham R., Uhrin D., Smith B.O., Soares D.C., Veltel S., McIlhinney R.A., White J.H., Barlow P.N.
      J. Biol. Chem. 279:48292-48306(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 96-159, DISULFIDE BONDS.

    Entry informationi

    Entry nameiGABR1_RAT
    AccessioniPrimary (citable) accession number: Q9Z0U4
    Secondary accession number(s): O08620
    , O08621, Q9Z0F9, Q9Z308
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 11, 2001
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 137 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. 7-transmembrane G-linked receptors
      List of 7-transmembrane G-linked receptor entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3