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GBRP_RAT
ID   GBRP_RAT                Reviewed;         440 AA.
AC   O09028;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=Gamma-aminobutyric acid receptor subunit pi;
DE   AltName: Full=GABA(A) receptor subunit pi;
DE   Flags: Precursor;
GN   Name=Gabrp;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9182563; DOI=10.1074/jbc.272.24.15346;
RA   Hedblom E., Kirkness E.F.;
RT   "A novel class of GABAA receptor subunit in tissues of the reproductive
RT   system.";
RL   J. Biol. Chem. 272:15346-15350(1997).
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.
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.
CC   -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane
CC       protein. Cell membrane; Multi-pass membrane protein.
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}.
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DR   EMBL; U95368; AAC53255.1; -; mRNA.
DR   RefSeq; NP_112291.1; NM_031029.1.
DR   AlphaFoldDB; O09028; -.
DR   SMR; O09028; -.
DR   STRING; 10116.ENSRNOP00000048081; -.
DR   ChEMBL; CHEMBL1907607; -.
DR   DrugCentral; O09028; -.
DR   GlyGen; O09028; 5 sites.
DR   PaxDb; O09028; -.
DR   PRIDE; O09028; -.
DR   Ensembl; ENSRNOT00000043036; ENSRNOP00000048081; ENSRNOG00000032417.
DR   GeneID; 81658; -.
DR   KEGG; rno:81658; -.
DR   UCSC; RGD:620532; rat.
DR   CTD; 2568; -.
DR   RGD; 620532; Gabrp.
DR   eggNOG; KOG3643; Eukaryota.
DR   GeneTree; ENSGT00940000160813; -.
DR   InParanoid; O09028; -.
DR   OrthoDB; 480926at2759; -.
DR   PhylomeDB; O09028; -.
DR   PRO; PR:O09028; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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:0005887; C:integral component of plasma membrane; 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:0005231; F:excitatory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR   GO; GO:0004890; F:GABA-A receptor activity; IEA:InterPro.
DR   GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR   GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IBA:GO_Central.
DR   GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR   GO; GO:1902476; P:chloride transmembrane transport; IBA:GO_Central.
DR   GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR   GO; GO:0050877; P:nervous system process; IBA:GO_Central.
DR   GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   Gene3D; 1.20.58.390; -; 1.
DR   Gene3D; 2.70.170.10; -; 1.
DR   InterPro; IPR006028; GABAA/Glycine_rcpt.
DR   InterPro; IPR008100; GABAAp_rcpt.
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   PANTHER; PTHR18945; PTHR18945; 1.
DR   PANTHER; PTHR18945:SF33; PTHR18945:SF33; 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; SSF63712; SSF63712; 1.
DR   SUPFAM; SSF90112; SSF90112; 1.
DR   TIGRFAMs; TIGR00860; LIC; 1.
DR   PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
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..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..440
FT                   /note="Gamma-aminobutyric acid receptor subunit pi"
FT                   /id="PRO_0000000494"
FT   TOPO_DOM        17..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;  50481 MW;  B4C7AE8923E43853 CRC64;
     MSYSLYLAFV CLNLLAQRMC IQGNQFNVEV SRSDKLSLPG FENLTAGYNK FLRPNFGGDP
     VRIALTLDIA SISSISESNM DYTATIYLRQ RWTDPRLVFE GNKSFTLDAR LVEFLWVPDT
     YIVESKKSFL HEVTVGNRLI RLFSNGTVLY ALRITTTVTC NMDLSKYPMD TQTCKLQLES
     WGYDGNDVEF SWLRGNDSVR GLENLRLAQY TIQQYFTLVT VSQQETGNYT RLVLQFELRR
     NVLYFILETY VPSTFLVVLS WVSFWISLES VPARTCIGVT TVLSMTTLMI GSRTSLPNTN
     CFIKAIDVYL GICFSFVFGA LLEYAVAHYS SLQQMAVKDR GPAKDSEEVN ITNIINSSIS
     SFKRKISFAS IEISGDNVNY SDLTMKASDK FKFVFREKIG RIIDYFTIQN PSNVDRYSKL
     LFPLIFMLAN VFYWAYYMYF
 
 
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