GBRP_BOVIN
ID GBRP_BOVIN Reviewed; 440 AA.
AC Q5EA06;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Gamma-aminobutyric acid receptor subunit pi;
DE AltName: Full=GABA(A) receptor subunit pi;
DE Flags: Precursor;
GN Name=GABRP;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
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; Multi-pass membrane
CC protein. Cell membrane {ECO:0000250}; Multi-pass membrane protein
CC {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}.
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DR EMBL; BT020763; AAX08780.1; -; mRNA.
DR RefSeq; NP_001015618.1; NM_001015618.1.
DR AlphaFoldDB; Q5EA06; -.
DR SMR; Q5EA06; -.
DR STRING; 9913.ENSBTAP00000003604; -.
DR PaxDb; Q5EA06; -.
DR PRIDE; Q5EA06; -.
DR Ensembl; ENSBTAT00000003604; ENSBTAP00000003604; ENSBTAG00000002779.
DR Ensembl; ENSBTAT00000071262; ENSBTAP00000065944; ENSBTAG00000002779.
DR GeneID; 517459; -.
DR KEGG; bta:517459; -.
DR CTD; 2568; -.
DR VEuPathDB; HostDB:ENSBTAG00000002779; -.
DR VGNC; VGNC:29201; GABRP.
DR eggNOG; KOG3643; Eukaryota.
DR GeneTree; ENSGT00940000160813; -.
DR HOGENOM; CLU_010920_0_1_1; -.
DR InParanoid; Q5EA06; -.
DR OMA; TTVTCNM; -.
DR OrthoDB; 480926at2759; -.
DR TreeFam; TF315453; -.
DR Proteomes; UP000009136; Chromosome 20.
DR Bgee; ENSBTAG00000002779; Expressed in zone of skin and 41 other tissues.
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_0000318941"
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; 50430 MW; B6AE04A01668A9BF CRC64;
MKRSLHLTFV CLSLFSARMC VQGNQFNIEV SRSNKLSLPG FENLTAGYNK FLRPNFGGEP
VQIALTLDVA SISSISESNM DYTATIYLRQ RWTDQRLVFE GNKSFTLDAR LVEFLWVPDT
YIVESKKSFL HEVTVGNRLI RLFSNGTVLY ALRITTTVAC NMDLSKYPMD TQTCKLQLES
WGYDGNDVEF SWLRGNDSVR GLENLRLAQY TIQQYFTSVT RSQQETGNYT RLVLQFELQR
NVLYFILETY VPSTFLVVLS WVSFWISLDS VPARTCIGVT TVLSMTTLMI GSRTSLPNTN
CFIKAIDVYL GICFSFVFGA LLEYAVAHYS SLQQMAAKDR GKAKEVEEVN ITNIINSSIS
SFKRKISFAS IEISGDNVDY SDLTMKTSDK VKFVFRDKLG RIVDYFTIQN PSNVDRYSKL
LFPLIFMLAN VFYWAYYMYF
