ID A0A3B3QKB6_9TELE Unreviewed; 467 AA.
AC A0A3B3QKB6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Gamma-aminobutyric acid type A receptor subunit gamma3 {ECO:0000313|Ensembl:ENSPKIP00000007182.1};
GN Name=GABRG3 {ECO:0000313|Ensembl:ENSPKIP00000007182.1};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000007182.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000007182.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Postsynaptic
CC cell membrane {ECO:0000256|ARBA:ARBA00034104}; Multi-pass membrane
CC protein {ECO:0000256|ARBA:ARBA00034104}. Synaptic cell membrane
CC {ECO:0000256|ARBA:ARBA00034099}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00034099}.
CC -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC {ECO:0000256|RuleBase:RU000687}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU000687}.
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DR AlphaFoldDB; A0A3B3QKB6; -.
DR Ensembl; ENSPKIT00000031227.1; ENSPKIP00000007182.1; ENSPKIG00000023170.1.
DR GeneTree; ENSGT00940000155607; -.
DR OrthoDB; 4265336at2759; -.
DR Proteomes; UP000261540; Unplaced.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
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:InterPro.
DR GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IEA:InterPro.
DR CDD; cd19000; LGIC_ECD_GABAAR_G; 1.
DR CDD; cd19054; LGIC_TM_GABAAR_gamma; 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; IPR005440; GABBAg3_rcpt.
DR InterPro; IPR005437; GABRG-1/4.
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:SF195; GAMMA-AMINOBUTYRIC ACID RECEPTOR SUBUNIT GAMMA-3; 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; PR01620; GABAARGAMMA.
DR PRINTS; PR01623; GABAARGAMMA3.
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.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Chloride {ECO:0000256|ARBA:ARBA00023214};
KW Chloride channel {ECO:0000256|ARBA:ARBA00023173};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR605437-50};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303, ECO:0000256|RuleBase:RU000687};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU000687};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU000687};
KW Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00023257};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU000687};
KW Synapse {ECO:0000256|ARBA:ARBA00023018};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000687};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU000687};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000687}.
FT SIGNAL 1..36
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT CHAIN 37..467
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT /id="PRO_5022261616"
FT TRANSMEM 267..291
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 330..352
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 447..466
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT DOMAIN 62..267
FT /note="Neurotransmitter-gated ion-channel ligand-binding"
FT /evidence="ECO:0000259|Pfam:PF02931"
FT DOMAIN 274..375
FT /note="Neurotransmitter-gated ion-channel transmembrane"
FT /evidence="ECO:0000259|Pfam:PF02932"
FT DISULFID 185..199
FT /evidence="ECO:0000256|PIRSR:PIRSR605437-50"
SQ SEQUENCE 467 AA; 53960 MW; 083257F1108B6A3D CRC64;
MIDATNSSPS YLLINMSTKL LLYVLLLSVL SACSQTIEYE EEYEDVTVNQ MLAPKTQETD
ATQILNNLLK EYDKKLRPDI GIKPTVIDVD IYVNSIGPVS SINMEYQIDI IFAQTWTDSR
LRYNSTMKIL TLNSNMVGLI WVPDTIFRNS KNADAHWITT PNQLLRIWND GKILYTLRLT
INAECQLQLH NFPMDEHSCP LIFSSYGYPR DEMIYKWRKN SVEAADQKSW RLYQFDFMGL
RNTSDIVRTS AGDYVVMTVY FDLSRRMGYF TIQTYIPCIL TVVLSWVSFW IKKDATPART
ALEEHVGEGI TTVLTMTTLS TVARTSLPRV SYVTAMDLFV TVCFLFVFAA LMEYATLNYY
SYSARKPTCT KTRRANYSVL DVAPSPTVIT LNNAMYWQEF EEACLYECLD GKDCQSFFCC
YEECKGGAWR RGRVHIDILE LDAYSRVFFP TSFLLFNVVY WVGYLYL
//
