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Q8BHJ7 (GBRA5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Gamma-aminobutyric acid receptor subunit alpha-5
Alternative name(s):
GABA(A) receptor subunit alpha-5
Gene names
Name:Gabra5
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length463 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel By similarity.

Subunit structure

Generally pentameric. There are five types of GABA(A) receptor chains: alpha, beta, gamma, delta, and rho By similarity.

Subcellular location

Cell junctionsynapsepostsynaptic cell membrane; Multi-pass membrane protein By similarity. Cell membrane; Multi-pass membrane protein By similarity.

Sequence similarities

Belongs to the ligand-gated ion channel (TC 1.A.9) family. Gamma-aminobutyric acid receptor (TC 1.A.9.5) subfamily. GABRA5 sub-subfamily. [View classification]

Ontologies

Keywords
   Biological processIon transport
Transport
   Cellular componentCell junction
Cell membrane
Membrane
Postsynaptic cell membrane
Synapse
   DomainSignal
Transmembrane
Transmembrane helix
   LigandChloride
   Molecular functionChloride channel
Ion channel
Ligand-gated ion channel
Receptor
   PTMDisulfide bond
Glycoprotein
Isopeptide bond
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processassociative learning

Inferred from mutant phenotype PubMed 12084936. Source: MGI

behavioral fear response

Inferred from mutant phenotype PubMed 12084936. Source: MGI

brain development

Inferred from electronic annotation. Source: Ensembl

cochlea development

Inferred from mutant phenotype PubMed 17021187. Source: DFLAT

gamma-aminobutyric acid signaling pathway

Inferred from electronic annotation. Source: InterPro

inner ear receptor cell development

Inferred from mutant phenotype PubMed 17021187. Source: DFLAT

innervation

Inferred from mutant phenotype PubMed 17021187. Source: DFLAT

negative regulation of neuron apoptotic process

Inferred from mutant phenotype PubMed 17021187. Source: DFLAT

neuron development

Inferred from mutant phenotype PubMed 17021187. Source: DFLAT

regulation of neuron apoptotic process

Inferred from mutant phenotype PubMed 17021187. Source: DFLAT

sensory perception of sound

Inferred from mutant phenotype PubMed 17021187. Source: DFLAT

synaptic transmission

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcell body

Inferred from direct assay PubMed 9682826. Source: MGI

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

chloride channel complex

Inferred from electronic annotation. Source: UniProtKB-KW

dendrite

Inferred from direct assay PubMed 9682826. Source: MGI

neuronal cell body membrane

Inferred from electronic annotation. Source: Ensembl

postsynaptic membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

receptor complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionGABA-A receptor activity

Inferred from electronic annotation. Source: Ensembl

chloride channel activity

Inferred from electronic annotation. Source: UniProtKB-KW

extracellular ligand-gated ion channel activity

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction PubMed 16467845. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RdxQ5WQV54EBI-8069233,EBI-8069271From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Chain26 – 463438Gamma-aminobutyric acid receptor subunit alpha-5
PRO_0000000445

Regions

Topological domain26 – 259234Extracellular Potential
Transmembrane260 – 28122Helical; Potential
Transmembrane286 – 30722Helical; Potential
Transmembrane319 – 34123Helical; Potential
Topological domain342 – 42887Cytoplasmic Potential
Transmembrane429 – 45022Helical; Potential

Amino acid modifications

Glycosylation451N-linked (GlcNAc...) Potential
Glycosylation1451N-linked (GlcNAc...) Potential
Glycosylation2071N-linked (GlcNAc...) Potential
Glycosylation2361N-linked (GlcNAc...) Potential
Disulfide bond173 ↔ 187 By similarity
Cross-link355Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8BHJ7 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 12C677403D326378

FASTA46352,274
        10         20         30         40         50         60 
MDNGMLSRFI MTQTLLVFCI SMTLSSHFGF SQMPTSSVQD ETNDNITIFT RILDGLLDGY 

        70         80         90        100        110        120 
DNRLRPGLGE RITQVRTDIY VTSFGPVSDT EMEYTIDVFF RQSWKDERLR FKGPMQRLPL 

       130        140        150        160        170        180 
NNLLASKIWT PDTFFHNGKK SIAHNMTTPN KLLRLEDDGT LLYTMRLTIS AECPMQLEDF 

       190        200        210        220        230        240 
PMDAHACPLK FGSYAYPNSE VVYVWTNGST KSVVVAEDGS RLNQYHLMGQ TVGTENISTS 

       250        260        270        280        290        300 
TGEYTIMTAH FHLKRKIGYF VIQTYLPCIM TVILSQVSFW LNRESVPART VFGVTTVLTM 

       310        320        330        340        350        360 
TTLSISARNS LPKVAYATAM DWFIAVCYAF VFSALIEFAT VNYFTKRGWA WDGKKALEAA 

       370        380        390        400        410        420 
KIKKKERELI LNKSTNAFTT GKLTHPPNIP KEQPPAGTAN APTVSIKASE EKTAESKKTY 

       430        440        450        460 
NSISKIDKMS RIVFPILFGT FNLVYWATYL NREPVIKGAT SPK 

« Hide

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Hippocampus and Hypothalamus.
[2]"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].
Strain: C57BL/6.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK038476 mRNA. Translation: BAC30012.1.
AK083185 mRNA. Translation: BAC38799.1.
BC062112 mRNA. Translation: AAH62112.1.
CCDSCCDS21322.1.
RefSeqNP_795916.1. NM_176942.4.
XP_006540619.1. XM_006540556.1.
XP_006540620.1. XM_006540557.1.
XP_006540621.1. XM_006540558.1.
XP_006540622.1. XM_006540559.1.
XP_006540623.1. XM_006540560.1.
UniGeneMm.273114.

3D structure databases

ProteinModelPortalQ8BHJ7.
SMRQ8BHJ7. Positions 59-367.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8BHJ7. 1 interaction.
MINTMINT-1789015.
STRING10090.ENSMUSP00000063276.

Chemistry

BindingDBQ8BHJ7.
ChEMBLCHEMBL2304.
GuidetoPHARMACOLOGY408.

PTM databases

PhosphoSiteQ8BHJ7.

Proteomic databases

PaxDbQ8BHJ7.
PRIDEQ8BHJ7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000068456; ENSMUSP00000063276; ENSMUSG00000055078.
GeneID110886.
KEGGmmu:110886.
UCSCuc009heb.1. mouse.

Organism-specific databases

CTD2558.
MGIMGI:95617. Gabra5.

Phylogenomic databases

eggNOGNOG238757.
GeneTreeENSGT00550000074441.
HOGENOMHOG000231337.
HOVERGENHBG051707.
InParanoidQ8BHJ7.
KOK05175.
OMAWTNGTTK.
OrthoDBEOG7JX342.
PhylomeDBQ8BHJ7.
TreeFamTF315453.

Gene expression databases

BgeeQ8BHJ7.
GenevestigatorQ8BHJ7.

Family and domain databases

Gene3D2.70.170.10. 1 hit.
InterProIPR006028. GABAA/Glycine_rcpt.
IPR001390. GABAAa_rcpt.
IPR005435. GABBAa5_rcpt.
IPR006202. Neur_chan_lig-bd.
IPR006201. Neur_channel.
IPR006029. Neurotrans-gated_channel_TM.
IPR018000. Neurotransmitter_ion_chnl_CS.
[Graphical view]
PANTHERPTHR18945. PTHR18945. 1 hit.
PfamPF02931. Neur_chan_LBD. 1 hit.
PF02932. Neur_chan_memb. 2 hits.
[Graphical view]
PRINTSPR01079. GABAARALPHA.
PR01618. GABAARALPHA5.
PR00253. GABAARECEPTR.
PR00252. NRIONCHANNEL.
SUPFAMSSF63712. SSF63712. 1 hit.
SSF90112. SSF90112. 1 hit.
TIGRFAMsTIGR00860. LIC. 1 hit.
PROSITEPS00236. NEUROTR_ION_CHANNEL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio364867.
PROQ8BHJ7.
SOURCESearch...

Entry information

Entry nameGBRA5_MOUSE
AccessionPrimary (citable) accession number: Q8BHJ7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 24, 2005
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot