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Database: UniProt
Entry: A0A3B5QIG0_XIPMA
LinkDB: A0A3B5QIG0_XIPMA
Original site: A0A3B5QIG0_XIPMA 
ID   A0A3B5QIG0_XIPMA        Unreviewed;       442 AA.
AC   A0A3B5QIG0;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Gamma-aminobutyric acid receptor subunit beta-2-like {ECO:0000313|Ensembl:ENSXMAP00000031339.1};
GN   Name=GABRB2 {ECO:0000313|Ensembl:ENSXMAP00000031339.1};
OS   Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Xiphophorus.
OX   NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000031339.1, ECO:0000313|Proteomes:UP000002852};
RN   [1] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA   Walter R., Schartl M., Warren W.;
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX   PubMed=23542700; DOI=10.1038/ng.2604;
RA   Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA   Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA   Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA   Postlethwait J.H., Warren W.C.;
RT   "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT   evolutionary adaptation and several complex traits.";
RL   Nat. Genet. 45:567-572(2013).
RN   [3] {ECO:0000313|Ensembl:ENSXMAP00000031339.1}
RP   IDENTIFICATION.
RC   STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000031339.1};
RG   Ensembl;
RL   Submitted (NOV-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; A0A3B5QIG0; -.
DR   Ensembl; ENSXMAT00000036948.1; ENSXMAP00000031339.1; ENSXMAG00000012500.2.
DR   GeneTree; ENSGT00940000154245; -.
DR   Proteomes; UP000002852; Unassembled WGS sequence.
DR   GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0031410; C:cytoplasmic vesicle; 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   CDD; cd19053; LGIC_TM_GABAAR_beta; 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; IPR002289; GABAAb_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   NCBIfam; TIGR00860; LIC; 1.
DR   PANTHER; PTHR18945:SF571; GAMMA-AMINOBUTYRIC ACID RECEPTOR SUBUNIT BETA-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; PR01160; GABAARBETA.
DR   PRINTS; PR00253; GABAARECEPTR.
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   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   Reference proteome {ECO:0000313|Proteomes:UP000002852};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
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   TRANSMEM        210..234
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        275..298
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        423..440
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   DOMAIN          6..209
FT                   /note="Neurotransmitter-gated ion-channel ligand-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02931"
FT   DOMAIN          217..437
FT                   /note="Neurotransmitter-gated ion-channel transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF02932"
SQ   SEQUENCE   442 AA;  51015 MW;  7016FF6EC9DA51A0 CRC64;
     MPLVKETVDR LLKGYDIRLR PDFGGPPVGV GMNIDIASID MVSEVNMDYT LTMYFQQAWR
     DKRLSYSEIS LNLTLDNRVA DQLWVPDTYF LNDKKSFVHG VTVKNRMIRL HPDGTVLYGL
     RITTTAACMM DLRRYPLDEQ NCTLEIESYG YTTDDIEFYW RGGNNAVTGV DKIELPQFSI
     VDHKLISKNV VFSTGSYPRL SLSFKLKRNI GYFILQTYMP SILITILSWV SFWINYDASA
     ARVALGITTV LTMTTINTHL RETLPKIPYV KAIDMYLMGC FVFVFLALLE YALVNYIFFG
     QGPQRQKKAA EKTATANNEK MRMDSNKMDT HENILLGTLD IKNDMGVTEL ALGLNDPRNT
     MLTYDSSNLQ YRKSGLTRHN FGRNALERHM TQKKSRLRRR ASQLKITIPD LTDVNSIDKW
     SRMIFPTVFS FFNIVYWLYY VN
//
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