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Protein

Gamma-aminobutyric acid receptor subunit alpha-1

Gene

Gabra1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the heteropentameric receptor for GABA, the major inhibitory neurotransmitter in the vertebrate brain. Functions also as histamine receptor and mediates cellular responses to histamine. Functions as receptor for diazepines and various anesthetics, such as pentobarbital; these are bound at a separate allosteric effector binding site. Functions as ligand-gated chloride channel.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei225 – 2251AgonistBy similarity

GO - Molecular functioni

  • benzodiazepine receptor activity Source: RGD
  • chloride channel activity Source: UniProtKB-KW
  • drug binding Source: RGD
  • GABA-A receptor activity Source: RGD
  • inhibitory extracellular ligand-gated ion channel activity Source: RGD

GO - Biological processi

  • cellular response to histamine Source: UniProtKB
  • chemical synaptic transmission, postsynaptic Source: GOC
  • chloride transport Source: RGD
  • gamma-aminobutyric acid signaling pathway Source: RGD
  • ion transmembrane transport Source: GOC
  • synaptic transmission Source: Reactome
  • synaptic transmission, GABAergic Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Chloride channel, Ion channel, Ligand-gated ion channel, Receptor

Keywords - Biological processi

Ion transport, Transport

Keywords - Ligandi

Chloride

Enzyme and pathway databases

ReactomeiR-RNO-112314. Neurotransmitter Receptor Binding And Downstream Transmission In The Postsynaptic Cell.
R-RNO-975298. Ligand-gated ion channel transport.
R-RNO-977441. GABA A receptor activation.

Names & Taxonomyi

Protein namesi
Recommended name:
Gamma-aminobutyric acid receptor subunit alpha-1
Alternative name(s):
GABA(A) receptor subunit alpha-1
Gene namesi
Name:Gabra1
Synonyms:Gabra-1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 10

Organism-specific databases

RGDi61855. Gabra1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini28 – 250223ExtracellularCuratedAdd
BLAST
Transmembranei251 – 27222HelicalCuratedAdd
BLAST
Transmembranei278 – 29922HelicalCuratedAdd
BLAST
Transmembranei312 – 33322HelicalCuratedAdd
BLAST
Topological domaini334 – 42087CytoplasmicCuratedAdd
BLAST
Transmembranei421 – 44222HelicalCuratedAdd
BLAST

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • chloride channel complex Source: UniProtKB-KW
  • GABA receptor complex Source: BHF-UCL
  • integral component of plasma membrane Source: RGD
  • plasma membrane Source: Reactome
  • postsynaptic membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi91 – 911F → L: Strongly decreases the affinity for GABA-dependent channel gating. 1 Publication

Chemistry

ChEMBLiCHEMBL1907607.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727Sequence analysisAdd
BLAST
Chaini28 – 455428Gamma-aminobutyric acid receptor subunit alpha-1PRO_0000000430Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi37 – 371N-linked (GlcNAc...)Sequence analysis
Glycosylationi137 – 1371N-linked (GlcNAc...)Sequence analysis
Disulfide bondi165 ↔ 179By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP62813.
PRIDEiP62813.

PTM databases

iPTMnetiP62813.
PhosphoSiteiP62813.

Expressioni

Gene expression databases

GenevisibleiP62813. RN.

Interactioni

Subunit structurei

Interacts with TRAK1 (By similarity). Heteropentamer, formed by a combination of alpha, beta, gamma, delta and rho chains. Binds UBQLN1.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Pik3r1Q637874EBI-6258192,EBI-518443

Protein-protein interaction databases

BioGridi248322. 1 interaction.
IntActiP62813. 2 interactions.
MINTiMINT-3371441.
STRINGi10116.ENSRNOP00000004725.

Chemistry

BindingDBiP62813.

Structurei

3D structure databases

ProteinModelPortaliP62813.
SMRiP62813. Positions 45-339.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni120 – 1223Agonist bindingBy similarity
Regioni180 – 1823Agonist bindingBy similarity
Regioni290 – 31122Allosteric effector bindingBy similarityAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3642. Eukaryota.
ENOG410XNQG. LUCA.
GeneTreeiENSGT00760000119010.
HOGENOMiHOG000231337.
HOVERGENiHBG051707.
InParanoidiP62813.
KOiK05175.
OMAiINTIHFL.
OrthoDBiEOG7JX342.
PhylomeDBiP62813.
TreeFamiTF315453.

Family and domain databases

Gene3Di2.70.170.10. 1 hit.
InterProiIPR006028. GABAA/Glycine_rcpt.
IPR001390. GABAAa_rcpt.
IPR005431. GABBAa1_rcpt.
IPR006202. Neur_chan_lig-bd.
IPR006201. Neur_channel.
IPR006029. Neurotrans-gated_channel_TM.
IPR018000. Neurotransmitter_ion_chnl_CS.
[Graphical view]
PANTHERiPTHR18945. PTHR18945. 1 hit.
PfamiPF02931. Neur_chan_LBD. 1 hit.
PF02932. Neur_chan_memb. 1 hit.
[Graphical view]
PRINTSiPR01079. GABAARALPHA.
PR01614. GABAARALPHA1.
PR00253. GABAARECEPTR.
PR00252. NRIONCHANNEL.
SUPFAMiSSF63712. SSF63712. 1 hit.
SSF90112. SSF90112. 1 hit.
TIGRFAMsiTIGR00860. LIC. 1 hit.
PROSITEiPS00236. NEUROTR_ION_CHANNEL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P62813-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKSRGLSDY LWAWTLILST LSGRSYGQPS QDELKDNTTV FTRILDRLLD
60 70 80 90 100
GYDNRLRPGL GERVTEVKTD IFVTSFGPVS DHDMEYTIDV FFRQSWKDER
110 120 130 140 150
LKFKGPMTVL RLNNLMASKI WTPDTFFHNG KKSVAHNMTM PNKLLRITED
160 170 180 190 200
GTLLYTMRLT VRAECPMHLE DFPMDAHACP LKFGSYAYTR AEVVYEWTRE
210 220 230 240 250
PARSVVVAED GSRLNQYDLL GQTVDSGIVQ SSTGEYVVMT THFHLKRKIG
260 270 280 290 300
YFVIQTYLPC IMTVILSQVS FWLNRESVPA RTVFGVTTVL TMTTLSISAR
310 320 330 340 350
NSLPKVAYAT AMDWFIAVCY AFVFSALIEF ATVNYFTKRG YAWDGKSVVP
360 370 380 390 400
EKPKKVKDPL IKKNNTYAPT ATSYTPNLAR GDPGLATIAK SATIEPKEVK
410 420 430 440 450
PETKPPEPKK TFNSVSKIDR LSRIAFPLLF GIFNLVYWAT YLNREPQLKA

PTPHQ
Length:455
Mass (Da):51,754
Last modified:August 16, 2004 - v1
Checksum:iA270B43423B4086E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti91 – 911F → L no nucleotide entry (PubMed:1977069).Curated
Sequence conflicti435 – 4351L → I no nucleotide entry (PubMed:2540033).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L08490 Genomic DNA. Translation: AAC42029.1.
AY574250 mRNA. Translation: AAS90346.1.
BC100061 mRNA. Translation: AAI00062.1.
PIRiJQ0158.
RefSeqiNP_899155.1. NM_183326.2.
XP_006246185.1. XM_006246123.2.
XP_006246186.1. XM_006246124.2.
UniGeneiRn.28463.

Genome annotation databases

EnsembliENSRNOT00000004725; ENSRNOP00000004725; ENSRNOG00000003512.
GeneIDi29705.
KEGGirno:29705.
UCSCiRGD:61855. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L08490 Genomic DNA. Translation: AAC42029.1.
AY574250 mRNA. Translation: AAS90346.1.
BC100061 mRNA. Translation: AAI00062.1.
PIRiJQ0158.
RefSeqiNP_899155.1. NM_183326.2.
XP_006246185.1. XM_006246123.2.
XP_006246186.1. XM_006246124.2.
UniGeneiRn.28463.

3D structure databases

ProteinModelPortaliP62813.
SMRiP62813. Positions 45-339.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248322. 1 interaction.
IntActiP62813. 2 interactions.
MINTiMINT-3371441.
STRINGi10116.ENSRNOP00000004725.

Chemistry

BindingDBiP62813.
ChEMBLiCHEMBL1907607.

PTM databases

iPTMnetiP62813.
PhosphoSiteiP62813.

Proteomic databases

PaxDbiP62813.
PRIDEiP62813.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000004725; ENSRNOP00000004725; ENSRNOG00000003512.
GeneIDi29705.
KEGGirno:29705.
UCSCiRGD:61855. rat.

Organism-specific databases

CTDi2554.
RGDi61855. Gabra1.

Phylogenomic databases

eggNOGiKOG3642. Eukaryota.
ENOG410XNQG. LUCA.
GeneTreeiENSGT00760000119010.
HOGENOMiHOG000231337.
HOVERGENiHBG051707.
InParanoidiP62813.
KOiK05175.
OMAiINTIHFL.
OrthoDBiEOG7JX342.
PhylomeDBiP62813.
TreeFamiTF315453.

Enzyme and pathway databases

ReactomeiR-RNO-112314. Neurotransmitter Receptor Binding And Downstream Transmission In The Postsynaptic Cell.
R-RNO-975298. Ligand-gated ion channel transport.
R-RNO-977441. GABA A receptor activation.

Miscellaneous databases

PROiP62813.

Gene expression databases

GenevisibleiP62813. RN.

Family and domain databases

Gene3Di2.70.170.10. 1 hit.
InterProiIPR006028. GABAA/Glycine_rcpt.
IPR001390. GABAAa_rcpt.
IPR005431. GABBAa1_rcpt.
IPR006202. Neur_chan_lig-bd.
IPR006201. Neur_channel.
IPR006029. Neurotrans-gated_channel_TM.
IPR018000. Neurotransmitter_ion_chnl_CS.
[Graphical view]
PANTHERiPTHR18945. PTHR18945. 1 hit.
PfamiPF02931. Neur_chan_LBD. 1 hit.
PF02932. Neur_chan_memb. 1 hit.
[Graphical view]
PRINTSiPR01079. GABAARALPHA.
PR01614. GABAARALPHA1.
PR00253. GABAARECEPTR.
PR00252. NRIONCHANNEL.
SUPFAMiSSF63712. SSF63712. 1 hit.
SSF90112. SSF90112. 1 hit.
TIGRFAMsiTIGR00860. LIC. 1 hit.
PROSITEiPS00236. NEUROTR_ION_CHANNEL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, SUBUNIT.
  2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "GABAA-receptor expressed from rat brain alpha- and beta-subunit cDNAs displays potentiation by benzodiazepine receptor ligands."
    Malherbe P., Draguhn A., Multhaup G., Beyreuther K., Mohler H.
    Brain Res. Mol. Brain Res. 8:199-208(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "The GABAA receptor family: molecular and functional diversity."
    Seeburg P.H., Wisden W., Verdoorn T., Pritchett D., Werner P., Herb A., Lueddens H., Sprengel R., Sakmann B.
    Cold Spring Harb. Symp. Quant. Biol. 55:29-40(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Brain.
  5. Groot-Kormelink P.J.
    Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Brain.
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.
  7. "Point mutations affecting antagonist affinity and agonist dependent gating of GABAA receptor channels."
    Sigel E., Baur R., Kellenberger S., Malherbe P.
    EMBO J. 11:2017-2023(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF PHE-91, FUNCTION, SUBCELLULAR LOCATION.
  8. "GABA(A) receptor cell surface number and subunit stability are regulated by the ubiquitin-like protein Plic-1."
    Bedford F.K., Kittler J.T., Muller E., Thomas P., Uren J.M., Merlo D., Wisden W., Triller A., Smart T.G., Moss S.J.
    Nat. Neurosci. 4:908-916(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UBQLN1.
  9. "Histamine action on vertebrate GABAA receptors: direct channel gating and potentiation of GABA responses."
    Saras A., Gisselmann G., Vogt-Eisele A.K., Erlkamp K.S., Kletke O., Pusch H., Hatt H.
    J. Biol. Chem. 283:10470-10475(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT.

Entry informationi

Entry nameiGBRA1_RAT
AccessioniPrimary (citable) accession number: P62813
Secondary accession number(s): P18504, Q53YK4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: June 8, 2016
This is version 107 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.