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Q8QZW7 (GBRP_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 88. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Gamma-aminobutyric acid receptor subunit pi
Alternative name(s):
GABA(A) receptor subunit pi
Gene names
Name:Gabrp
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length440 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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. In the uterus, the function of the receptor appears to be related to tissue contractility. The binding of this pI subunit with other GABA(A) receptor subunits alters the sensitivity of recombinant receptors to modulatory agents such as pregnanolone By similarity.

Subunit structure

Generally pentameric. There are five types of GABA(A) receptor chains: alpha, beta, gamma, delta, and epsilon. A sixth class of subunit: Rho form homomeric GABA receptors that do not appear to coexist with GABA(A) receptor subunits but with GABA(C) receptor subunits. Subunit Pi can also bind this complex By similarity.

Subcellular location

Cell junction › synapse › postsynaptic 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. GABRP sub-subfamily. [View classification]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 440419Gamma-aminobutyric acid receptor subunit pi
PRO_0000000493

Regions

Topological domain22 – 242221Extracellular Potential
Transmembrane243 – 26624Helical; Potential
Transmembrane270 – 29223Helical; Potential
Transmembrane305 – 32723Helical; Potential
Topological domain328 – 41689Cytoplasmic Potential
Transmembrane417 – 43822Helical; Potential

Amino acid modifications

Glycosylation431N-linked (GlcNAc...) Potential
Glycosylation1021N-linked (GlcNAc...) Potential
Glycosylation1451N-linked (GlcNAc...) Potential
Glycosylation1961N-linked (GlcNAc...) Potential
Glycosylation2281N-linked (GlcNAc...) Potential
Disulfide bond160 ↔ 174 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8QZW7 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: DF8D2AAB3300D445

FASTA44050,436
        10         20         30         40         50         60 
MSYSLYLAFL CLSLLTQRTC IQGNQVNVEV SRSDKLSLPG FENLTAGYNK FLRPNFGGDP 

        70         80         90        100        110        120 
VRIALTLDIA SISSISESNM DYTATIYLRQ RWTDPRLVFE GNKSFTLDAR LVEFLWVPDT 

       130        140        150        160        170        180 
YIVESKKSFL HEVTVGNRLI RLFSNGTVLY ALRITTTVTC NMDLSKYPMD TQTCKLQLES 

       190        200        210        220        230        240 
WGYDGNDVEF SWLRGNDSVR GLENLRLAQY TIQQYFTLVT VSQQETGNYT RLVLQFELRR 

       250        260        270        280        290        300 
NVLYFILETY VPSTFLVVLS WVSFWISLDS VPARTCIGVT TVLSMTTLMI GSRTSLPNTN 

       310        320        330        340        350        360 
CFIKAIDVYL GICFSFVFGA LLEYAVAHYS SLQQMAVKDR GPAKDSEEVN ITNIINSSIS 

       370        380        390        400        410        420 
SFKRKISFAS IEISGDNVNY SDLTMKASDK FKFVFREKIS RIIDYFTIQN PSNVDRYSKL 

       430        440 
LFPLIFMLAN VFYWAYYMYF

« 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: Skin.
[2]Brown J.
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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: FVB/N and FVB/N-3.
Tissue: Mammary tumor.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK028946 mRNA. Translation: BAC26209.1.
AK160577 mRNA. Translation: BAE35885.1.
AL669814 Genomic DNA. Translation: CAI25681.1.
BC023693 mRNA. Translation: AAH23693.1.
BC025550 mRNA. Translation: AAH25550.1.
BC027245 mRNA. Translation: AAH27245.1.
BC031196 mRNA. Translation: AAH31196.1.
IPIIPI00154070.
RefSeqNP_666129.1. NM_146017.3.
UniGeneMm.99989.

3D structure databases

ProteinModelPortalQ8QZW7.
SMRQ8QZW7. Positions 44-338.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000020366.

PTM databases

PhosphoSiteQ8QZW7.

Proteomic databases

PRIDEQ8QZW7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000020366; ENSMUSP00000020366; ENSMUSG00000020159.
GeneID216643.
KEGGmmu:216643.
UCSCuc007ikm.1. mouse.

Organism-specific databases

CTD2568.
MGIMGI:2387597. Gabrp.

Phylogenomic databases

eggNOGNOG255582.
GeneTreeENSGT00630000089571.
HOGENOMHOG000231335.
HOVERGENHBG051707.
InParanoidQ8QZW7.
KOK05189.
OMAISESDMD.
OrthoDBEOG4N04F2.

Gene expression databases

ArrayExpressQ8QZW7.
BgeeQ8QZW7.
CleanExMM_GABRP.
GenevestigatorQ8QZW7.
GermOnlineENSMUSG00000020159. Mus musculus.

Family and domain databases

Gene3D2.70.170.10. 1 hit.
InterProIPR006028. GABAA_rcpt.
IPR008100. GABAAp_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. 1 hit.
[Graphical view]
PRINTSPR00253. GABAARECEPTR.
PR01724. GABAARPI.
PR00252. NRIONCHANNEL.
SUPFAMSSF90112. Neu_channel_TM. 1 hit.
SSF63712. Neur_chan_LBD. 1 hit.
TIGRFAMsTIGR00860. LIC. 1 hit.
PROSITEPS00236. NEUROTR_ION_CHANNEL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBQ8QZW7.
ChEMBLCHEMBL2746.
NextBio375250.
SOURCESearch...

Entry information

Entry nameGBRP_MOUSE
AccessionPrimary (citable) accession number: Q8QZW7
Secondary accession number(s): Q3TUT6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: June 1, 2002
Last modified: May 1, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents