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Q9Z0U4

- GABR1_RAT

UniProt

Q9Z0U4 - GABR1_RAT

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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

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. 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
Complete GO annotation...

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-KW
  15. synaptic vesicle Source: RGD
Complete GO annotation...

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

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

        10         20         30         40         50
MLLLLLVPLF LRPLGAGGAQ TPNATSEGCQ IIHPPWEGGI RYRGLTRDQV
60 70 80 90 100
KAINFLPVDY EIEYVCRGER EVVGPKVRKC LANGSWTDMD TPSRCVRICS
110 120 130 140 150
KSYLTLENGK VFLTGGDLPA LDGARVEFRC DPDFHLVGSS RSVCSQGQWS
160 170 180 190 200
TPKPHCQVNR TPHSERRAVY IGALFPMSGG WPGGQACQPA VEMALEDVNS
210 220 230 240 250
RRDILPDYEL KLIHHDSKCD PGQATKYLYE LLYNDPIKII LMPGCSSVST
260 270 280 290 300
LVAEAARMWN LIVLSYGSSS PALSNRQRFP TFFRTHPSAT LHNPTRVKLF
310 320 330 340 350
EKWGWKKIAT IQQTTEVFTS TLDDLEERVK EAGIEITFRQ SFFSDPAVPV
360 370 380 390 400
KNLKRQDARI IVGLFYETEA RKVFCEVYKE RLFGKKYVWF LIGWYADNWF
410 420 430 440 450
KTYDPSINCT VEEMTEAVEG HITTEIVMLN PANTRSISNM TSQEFVEKLT
460 470 480 490 500
KRLKRHPEET GGFQEAPLAY DAIWALALAL NKTSGGGGRS GVRLEDFNYN
510 520 530 540 550
NQTITDQIYR AMNSSSFEGV SGHVVFDASG SRMAWTLIEQ LQGGSYKKIG
560 570 580 590 600
YYDSTKDDLS WSKTDKWIGG SPPADQTLVI KTFRFLSQKL FISVSVLSSL
610 620 630 640 650
GIVLAVVCLS FNIYNSHVRY IQNSQPNLNN LTAVGCSLAL AAVFPLGLDG
660 670 680 690 700
YHIGRSQFPF VCQARLWLLG LGFSLGYGSM FTKIWWVHTV FTKKEEKKEW
710 720 730 740 750
RKTLEPWKLY ATVGLLVGMD VLTLAIWQIV DPLHRTIETF AKEEPKEDID
760 770 780 790 800
VSILPQLEHC SSKKMNTWLG ELWSFAVSSD VQRRATVGGD SPICVWPAPE
810 820 830 840 850
SIFYGYKGLL LLLGIFLAYE TKSVSTEKIN DHRAVGMAIY NVAVLCLITA
860 870 880 890 900
PVTMILSSQQ DAAFAFASLA IVFSSYITLV VLFVPKMRRL ITRGEWQSET
910 920 930 940 950
QDTMKTGSST NNNEEEKSRL LEKENRELEK IIAEKEERVS ELRHQLQSRQ
960 970 980 990
QLRSRRHPPT PPDPSGGLPR GPSEPPDRLS CDGSRVHLLY K
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_006255879.2. [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_006255879.2. [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

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 29, 2014
This is version 138 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