ID   GBRP_MOUSE              Reviewed;         440 AA.
AC   Q8QZW7; Q3TUT6;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   24-JAN-2024, entry version 150.
DE   RecName: Full=Gamma-aminobutyric acid receptor subunit pi;
DE   AltName: Full=GABA(A) receptor subunit pi;
DE   Flags: Precursor;
GN   Name=Gabrp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown J.;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N, and FVB/N-3; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: GABA, the major inhibitory neurotransmitter in the vertebrate
CC       brain, mediates neuronal inhibition by binding to the
CC       GABA/benzodiazepine receptor and opening an integral chloride channel.
CC       In the uterus, the function of the receptor appears to be related to
CC       tissue contractility. The binding of this pI subunit with other GABA(A)
CC       receptor subunits alters the sensitivity of recombinant receptors to
CC       modulatory agents such as pregnanolone (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Generally pentameric. There are five types of GABA(A) receptor
CC       chains: alpha, beta, gamma, delta, and epsilon. A sixth class of
CC       subunit: Rho form homomeric GABA receptors that do not appear to
CC       coexist with GABA(A) receptor subunits but with GABA(C) receptor
CC       subunits. Subunit Pi can also bind this complex (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000250}; Multi-
CC       pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC       Gamma-aminobutyric acid receptor (TC 1.A.9.5) subfamily. GABRP sub-
CC       subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AK028946; BAC26209.1; -; mRNA.
DR   EMBL; AK160577; BAE35885.1; -; mRNA.
DR   EMBL; AL669814; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC023693; AAH23693.1; -; mRNA.
DR   EMBL; BC025550; AAH25550.1; -; mRNA.
DR   EMBL; BC027245; AAH27245.1; -; mRNA.
DR   EMBL; BC031196; AAH31196.1; -; mRNA.
DR   CCDS; CCDS24535.1; -.
DR   RefSeq; NP_666129.1; NM_146017.3.
DR   AlphaFoldDB; Q8QZW7; -.
DR   SMR; Q8QZW7; -.
DR   STRING; 10090.ENSMUSP00000020366; -.
DR   ChEMBL; CHEMBL2094133; -.
DR   DrugCentral; Q8QZW7; -.
DR   GlyCosmos; Q8QZW7; 5 sites, No reported glycans.
DR   GlyGen; Q8QZW7; 5 sites.
DR   PhosphoSitePlus; Q8QZW7; -.
DR   PaxDb; 10090-ENSMUSP00000020366; -.
DR   Antibodypedia; 4442; 108 antibodies from 20 providers.
DR   DNASU; 216643; -.
DR   Ensembl; ENSMUST00000020366.8; ENSMUSP00000020366.2; ENSMUSG00000020159.9.
DR   GeneID; 216643; -.
DR   KEGG; mmu:216643; -.
DR   UCSC; uc007ikm.1; mouse.
DR   AGR; MGI:2387597; -.
DR   CTD; 2568; -.
DR   MGI; MGI:2387597; Gabrp.
DR   VEuPathDB; HostDB:ENSMUSG00000020159; -.
DR   eggNOG; KOG3643; Eukaryota.
DR   GeneTree; ENSGT00940000160813; -.
DR   HOGENOM; CLU_010920_0_1_1; -.
DR   InParanoid; Q8QZW7; -.
DR   OMA; TTVTCNM; -.
DR   OrthoDB; 4265336at2759; -.
DR   PhylomeDB; Q8QZW7; -.
DR   TreeFam; TF315453; -.
DR   BioGRID-ORCS; 216643; 2 hits in 78 CRISPR screens.
DR   ChiTaRS; Gabrp; mouse.
DR   PRO; PR:Q8QZW7; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q8QZW7; Protein.
DR   Bgee; ENSMUSG00000020159; Expressed in trachea and 80 other cell types or tissues.
DR   ExpressionAtlas; Q8QZW7; baseline and differential.
DR   GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR   GO; GO:1902711; C:GABA-A receptor complex; IBA:GO_Central.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045202; C:synapse; IBA:GO_Central.
DR   GO; GO:0005254; F:chloride channel activity; IEA:UniProtKB-KW.
DR   GO; GO:0005230; F:extracellular ligand-gated monoatomic ion channel activity; IEA:InterPro.
DR   GO; GO:0004890; F:GABA-A receptor activity; IEA:Ensembl.
DR   GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR   GO; GO:1902476; P:chloride transmembrane transport; IBA:GO_Central.
DR   CDD; cd19058; LGIC_TM_GABAAR_pi; 1.
DR   Gene3D; 2.70.170.10; Neurotransmitter-gated ion-channel ligand-binding domain; 1.
DR   Gene3D; 1.20.58.390; Neurotransmitter-gated ion-channel transmembrane domain; 1.
DR   InterPro; IPR006028; GABAA/Glycine_rcpt.
DR   InterPro; IPR008100; GABAAp_rcpt.
DR   InterPro; IPR047032; GABAAR_pi_TM.
DR   InterPro; IPR006202; Neur_chan_lig-bd.
DR   InterPro; IPR036734; Neur_chan_lig-bd_sf.
DR   InterPro; IPR006201; Neur_channel.
DR   InterPro; IPR036719; Neuro-gated_channel_TM_sf.
DR   InterPro; IPR038050; Neuro_actylchol_rec.
DR   InterPro; IPR006029; Neurotrans-gated_channel_TM.
DR   InterPro; IPR018000; Neurotransmitter_ion_chnl_CS.
DR   NCBIfam; TIGR00860; LIC; 1.
DR   PANTHER; PTHR18945:SF33; GAMMA-AMINOBUTYRIC ACID RECEPTOR SUBUNIT PI; 1.
DR   PANTHER; PTHR18945; NEUROTRANSMITTER GATED ION CHANNEL; 1.
DR   Pfam; PF02931; Neur_chan_LBD; 1.
DR   Pfam; PF02932; Neur_chan_memb; 1.
DR   PRINTS; PR00253; GABAARECEPTR.
DR   PRINTS; PR01724; GABAARPI.
DR   PRINTS; PR00252; NRIONCHANNEL.
DR   SUPFAM; SSF90112; Neurotransmitter-gated ion-channel transmembrane pore; 1.
DR   SUPFAM; SSF63712; Nicotinic receptor ligand binding domain-like; 1.
DR   PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
DR   Genevisible; Q8QZW7; MM.
PE   2: Evidence at transcript level;
KW   Cell membrane; Chloride; Chloride channel; Disulfide bond; Glycoprotein;
KW   Ion channel; Ion transport; Membrane; Postsynaptic cell membrane;
KW   Reference proteome; Signal; Synapse; Transmembrane; Transmembrane helix;
KW   Transport.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..440
FT                   /note="Gamma-aminobutyric acid receptor subunit pi"
FT                   /id="PRO_0000000493"
FT   TOPO_DOM        22..242
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        243..266
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        270..292
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        305..327
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        328..416
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        417..438
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        43
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        102
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        145
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        196
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        228
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        160..174
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   440 AA;  50436 MW;  DF8D2AAB3300D445 CRC64;
     MSYSLYLAFL CLSLLTQRTC IQGNQVNVEV SRSDKLSLPG FENLTAGYNK FLRPNFGGDP
     VRIALTLDIA SISSISESNM DYTATIYLRQ RWTDPRLVFE GNKSFTLDAR LVEFLWVPDT
     YIVESKKSFL HEVTVGNRLI RLFSNGTVLY ALRITTTVTC NMDLSKYPMD TQTCKLQLES
     WGYDGNDVEF SWLRGNDSVR GLENLRLAQY TIQQYFTLVT VSQQETGNYT RLVLQFELRR
     NVLYFILETY VPSTFLVVLS WVSFWISLDS VPARTCIGVT TVLSMTTLMI GSRTSLPNTN
     CFIKAIDVYL GICFSFVFGA LLEYAVAHYS SLQQMAVKDR GPAKDSEEVN ITNIINSSIS
     SFKRKISFAS IEISGDNVNY SDLTMKASDK FKFVFREKIS RIIDYFTIQN PSNVDRYSKL
     LFPLIFMLAN VFYWAYYMYF
//