ID A0A1W2PQX1_HUMAN Unreviewed; 397 AA.
AC A0A1W2PQX1;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Gamma-aminobutyric acid type A receptor subunit gamma2 {ECO:0000313|Ensembl:ENSP00000491958.1};
DE Flags: Fragment;
GN Name=GABRG2 {ECO:0000313|Ensembl:ENSP00000491958.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000491958.1, ECO:0000313|Proteomes:UP000005640};
RN [1] {ECO:0000313|Ensembl:ENSP00000491958.1, ECO:0000313|Proteomes:UP000005640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [2] {ECO:0000313|Ensembl:ENSP00000491958.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}. Postsynaptic cell membrane
CC {ECO:0000256|ARBA:ARBA00034104}; Multi-pass membrane protein
CC {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 EMBL; AC008611; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC091926; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC091984; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A1W2PQX1; -.
DR EMDB; EMD-14072; -.
DR SMR; A0A1W2PQX1; -.
DR MassIVE; A0A1W2PQX1; -.
DR PeptideAtlas; A0A1W2PQX1; -.
DR Ensembl; ENST00000639278.1; ENSP00000491958.1; ENSG00000113327.17.
DR HGNC; HGNC:4087; GABRG2.
DR VEuPathDB; HostDB:ENSG00000113327; -.
DR GeneTree; ENSGT00940000156685; -.
DR ChiTaRS; GABRG2; human.
DR Proteomes; UP000005640; Chromosome 5.
DR Bgee; ENSG00000113327; Expressed in middle temporal gyrus and 138 other cell types or tissues.
DR ExpressionAtlas; A0A1W2PQX1; baseline and differential.
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; 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:SF498; GAMMA-AMINOBUTYRIC ACID RECEPTOR SUBUNIT GAMMA-2; 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; 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 1: Evidence at protein level;
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 Proteomics identification {ECO:0007829|PeptideAtlas:A0A1W2PQX1,
KW ECO:0007829|ProteomicsDB:A0A1W2PQX1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005640};
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..16
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT CHAIN 17..397
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT /id="PRO_5022258176"
FT TRANSMEM 248..272
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 313..336
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT DOMAIN 45..248
FT /note="Neurotransmitter-gated ion-channel ligand-binding"
FT /evidence="ECO:0000259|Pfam:PF02931"
FT DOMAIN 255..355
FT /note="Neurotransmitter-gated ion-channel transmembrane"
FT /evidence="ECO:0000259|Pfam:PF02932"
FT DISULFID 166..180
FT /evidence="ECO:0000256|PIRSR:PIRSR605437-50"
FT NON_TER 1
FT /evidence="ECO:0000313|Ensembl:ENSP00000491958.1"
SQ SEQUENCE 397 AA; 45661 MW; 0BC22BA0DC9A8784 CRC64;
VWILLLLSLY PGFTSQKSDD DYEDYASNKT WVLTPKVPEG DVTVILNNLL EGYDNKLRPD
IGVKPTLIHT DMYVNSIGPV NAINMEYTID IFFAQTWYDR RLKFNSTIKV LRLNSNMVGK
IWIPDTFFRN SKKADAHWIT TPNRMLRIWN DGRVLYTLRL TIDAECQLQL HNFPMDEHSC
PLEFSSYGYP REEIVYQWKR SSVEVGDTRS WRLYQFSFVG LRNTTEVVKT TSGDYVVMSV
YFDLSRRMGY FTIQTYIPCT LIVVLSWVSF WINKDAVPAR TSLGITTVLT MTTLSTIARK
SLPKVSYVTA MDLFVSVCFI FVFSALVEYG TLHYFVSNRK PSKDKDKKKK NPKVVLLRVG
ILPASYNKDM RTGFQTSSDE SFGKSPLALS VSYAIAE
//
