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
