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Protein

Gamma-aminobutyric acid receptor alpha-like

Gene

Grd

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

GABA, an inhibitory neurotransmitter, mediates neuronal inhibition by binding to the GABA receptor and opening an integral chloride channel. May combine with the ligand-gated ion channel subunit Lcch3 to form cation-selective GABA-gated ion channels.1 Publication

GO - Molecular functioni

  • cation channel activity Source: UniProtKB
  • chloride channel activity Source: UniProtKB-KW
  • extracellular-glycine-gated ion channel activity Source: FlyBase
  • GABA-A receptor activity Source: UniProtKB
  • ligand-gated ion channel activity Source: UniProtKB

GO - Biological processi

  • cation transmembrane transport Source: GOC
  • ion transmembrane transport Source: GOC
  • ion transport Source: UniProtKB
  • signal transduction Source: GOC
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-DME-975298. Ligand-gated ion channel transport.
R-DME-977441. GABA A receptor activation.

Names & Taxonomyi

Protein namesi
Recommended name:
Gamma-aminobutyric acid receptor alpha-like
Alternative name(s):
GABA(A) receptor alpha-like and glycine receptor-like subunit of Drosophila
Short name:
GRD
Gene namesi
Name:Grd
ORF Names:CG7446
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0001134. Grd.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini97 – 393297ExtracellularSequence analysisAdd
BLAST
Transmembranei394 – 41421HelicalSequence analysisAdd
BLAST
Transmembranei424 – 44118HelicalSequence analysisAdd
BLAST
Transmembranei456 – 47621HelicalSequence analysisAdd
BLAST
Topological domaini477 – 650174CytoplasmicSequence analysisAdd
BLAST
Transmembranei651 – 67121HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • chloride channel complex Source: UniProtKB-KW
  • integral component of membrane Source: UniProtKB
  • plasma membrane Source: FlyBase
  • postsynaptic membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 5858Sequence analysisAdd
BLAST
Chaini59 – 686628Gamma-aminobutyric acid receptor alpha-likePRO_0000000451Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi108 – 1081N-linked (GlcNAc...)Sequence analysis
Disulfide bondi233 ↔ 247By similarity
Glycosylationi292 – 2921N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ24352.
PRIDEiQ24352.

Expressioni

Gene expression databases

BgeeiQ24352.
GenevisibleiQ24352. DM.

Interactioni

Subunit structurei

Generally pentameric. There are five types of GABA(A) receptor chains: alpha, beta, gamma, delta, and rho. Interacts with Lcch3 (beta chain).1 Publication

Protein-protein interaction databases

STRINGi7227.FBpp0074905.

Structurei

3D structure databases

ProteinModelPortaliQ24352.
SMRiQ24352. Positions 109-481.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi589 – 60921Ala-richAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3642. Eukaryota.
ENOG410XNQG. LUCA.
GeneTreeiENSGT00760000119010.
InParanoidiQ24352.
OMAiTHHPSEY.
OrthoDBiEOG7JX342.
PhylomeDBiQ24352.

Family and domain databases

Gene3Di2.70.170.10. 2 hits.
InterProiIPR006028. GABAA/Glycine_rcpt.
IPR006202. Neur_chan_lig-bd.
IPR006201. Neur_channel.
IPR006029. Neurotrans-gated_channel_TM.
IPR018000. Neurotransmitter_ion_chnl_CS.
[Graphical view]
PANTHERiPTHR18945. PTHR18945. 5 hits.
PfamiPF02931. Neur_chan_LBD. 1 hit.
PF02932. Neur_chan_memb. 1 hit.
[Graphical view]
PRINTSiPR00253. GABAARECEPTR.
PR00252. NRIONCHANNEL.
SUPFAMiSSF63712. SSF63712. 1 hit.
SSF90112. SSF90112. 2 hits.
PROSITEiPS00236. NEUROTR_ION_CHANNEL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q24352-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCTMPATRDA SGSGDASTDL IAARSLSSHQ GQRSNLRIFK LLISCCLLML
60 70 80 90 100
CIYPNAWPWS IGPGSGPFSV SADSIKGRGD THRLGEMGTS LSSSLPSSWL
110 120 130 140 150
TQSNNHANIS ELLDNLLRGY DNSIRPDFGG PPATIEVDIM VRSMGPISEV
160 170 180 190 200
DMTYSMDCYF RQSWVDKRLA FEGAQDTLAL SVSMLARIWK PDTYFYNGKQ
210 220 230 240 250
SYLHTITTPN KFVRIYQNGR VLYSSRLTIK AGCPMNLADF PMDIQKCPLK
260 270 280 290 300
FGSFGYTTSD VIYRWNKERP PVAIAEDMKL SQFDLVDCPA GNLTDIVYKA
310 320 330 340 350
AAPRPQRRPF NNKDPPRPTS KVMTTFAGPA AKNQHVRGTG LKLDKGAFGT
360 370 380 390 400
GRDATGGSGS TTGLSGTITL ETNHPSEYSM LMVNFHLQRH MGNFLIQVYG
410 420 430 440 450
PCCLLVVLSW VSFWLNREAT ADRVSLGITT VLTMTFLGLE ARTDLPKVSY
460 470 480 490 500
PTALDFFVFL SFGFIFATIL QFAVVHYYTK YGSGECYFII EELDSESGES
510 520 530 540 550
ETEPLTSDFR GSTESKIYEV IPLSMCAISM PPPPTRLGML TSRNRRPRNR
560 570 580 590 600
RHGLWSMKLL GLFDWRRRRK PPRADSDEDE DDEQTQLRAN EAPTTSAAAA
610 620 630 640 650
AAQAAAQAAR ISPPTGGRRR MSYYRREEME ARRKGKRTPQ YNSVSKIDRA
660 670 680
SRIVFPLLFI LINVFYWYGY LSRSSRILAN TPDAST
Length:686
Mass (Da):76,558
Last modified:November 1, 1996 - v1
Checksum:iE2BD771B7E3BAC7A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78349 mRNA. Translation: CAA55144.1.
AE014296 Genomic DNA. Translation: AAF49298.2.
PIRiS60749.
RefSeqiNP_524131.1. NM_079407.3.
UniGeneiDm.2530.

Genome annotation databases

EnsemblMetazoaiFBtr0075139; FBpp0074905; FBgn0001134.
GeneIDi39984.
KEGGidme:Dmel_CG7446.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78349 mRNA. Translation: CAA55144.1.
AE014296 Genomic DNA. Translation: AAF49298.2.
PIRiS60749.
RefSeqiNP_524131.1. NM_079407.3.
UniGeneiDm.2530.

3D structure databases

ProteinModelPortaliQ24352.
SMRiQ24352. Positions 109-481.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7227.FBpp0074905.

Proteomic databases

PaxDbiQ24352.
PRIDEiQ24352.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0075139; FBpp0074905; FBgn0001134.
GeneIDi39984.
KEGGidme:Dmel_CG7446.

Organism-specific databases

CTDi39984.
FlyBaseiFBgn0001134. Grd.

Phylogenomic databases

eggNOGiKOG3642. Eukaryota.
ENOG410XNQG. LUCA.
GeneTreeiENSGT00760000119010.
InParanoidiQ24352.
OMAiTHHPSEY.
OrthoDBiEOG7JX342.
PhylomeDBiQ24352.

Enzyme and pathway databases

ReactomeiR-DME-975298. Ligand-gated ion channel transport.
R-DME-977441. GABA A receptor activation.

Miscellaneous databases

GenomeRNAii39984.
PROiQ24352.

Gene expression databases

BgeeiQ24352.
GenevisibleiQ24352. DM.

Family and domain databases

Gene3Di2.70.170.10. 2 hits.
InterProiIPR006028. GABAA/Glycine_rcpt.
IPR006202. Neur_chan_lig-bd.
IPR006201. Neur_channel.
IPR006029. Neurotrans-gated_channel_TM.
IPR018000. Neurotransmitter_ion_chnl_CS.
[Graphical view]
PANTHERiPTHR18945. PTHR18945. 5 hits.
PfamiPF02931. Neur_chan_LBD. 1 hit.
PF02932. Neur_chan_memb. 1 hit.
[Graphical view]
PRINTSiPR00253. GABAARECEPTR.
PR00252. NRIONCHANNEL.
SUPFAMiSSF63712. SSF63712. 1 hit.
SSF90112. SSF90112. 2 hits.
PROSITEiPS00236. NEUROTR_ION_CHANNEL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence of a Drosophila ligand-gated ion-channel polypeptide with an unusual amino-terminal extracellular domain."
    Harvey R.J., Schmitt B., Hermans-Borgmeyer I., Gundelfinger E.D., Betz H., Darlison M.G.
    J. Neurochem. 62:2480-2483(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Berlin.
    Tissue: Head and Salivary gland.
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. "Drosophila melanogaster GRD and LCCH3 subunits form heteromultimeric GABA-gated cation channels."
    Gisselmann G., Plonka J., Pusch H., Hatt H.
    Br. J. Pharmacol. 142:409-413(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH LCCH3.

Entry informationi

Entry nameiGBRAL_DROME
AccessioniPrimary (citable) accession number: Q24352
Secondary accession number(s): Q9TX50, Q9VVL3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. 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.