ID   G5E811_MOUSE            Unreviewed;       480 AA.
AC   G5E811;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   SubName: Full=Glycine receptor subunit alpha-3 {ECO:0000313|Ensembl:ENSMUSP00000000275};
DE   SubName: Full=Glycine receptor, alpha 3 subunit {ECO:0000313|Ensembl:ENSMUSP00000159349.2};
GN   Name=Glra3 {ECO:0000313|Ensembl:ENSMUSP00000000275,
GN   ECO:0000313|MGI:MGI:95749};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000000275, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0000313|Ensembl:ENSMUSP00000000275, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000000275,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [3] {ECO:0000313|Ensembl:ENSMUSP00000000275}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000000275};
RG   Ensembl;
RL   Submitted (OCT-2011) to UniProtKB.
RN   [4] {ECO:0000313|Ensembl:ENSMUSP00000159349.2}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000159349.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823,
CC         ChEBI:CHEBI:17996; Evidence={ECO:0000256|ARBA:ARBA00024167};
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}. Synapse
CC       {ECO:0000256|ARBA:ARBA00034103}. 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}.
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DR   EMBL; AC117729; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC119900; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_536686.2; NM_080438.2.
DR   ProteomicsDB; 334454; -.
DR   Antibodypedia; 28583; 120 antibodies from 23 providers.
DR   DNASU; 110304; -.
DR   Ensembl; ENSMUST00000000275; ENSMUSP00000000275; ENSMUSG00000038257.
DR   Ensembl; ENSMUST00000239388.2; ENSMUSP00000159349.2; ENSMUSG00000038257.11.
DR   GeneID; 110304; -.
DR   KEGG; mmu:110304; -.
DR   UCSC; uc009lsn.1; mouse.
DR   AGR; MGI:95749; -.
DR   CTD; 8001; -.
DR   MGI; MGI:95749; Glra3.
DR   VEuPathDB; HostDB:ENSMUSG00000038257; -.
DR   GeneTree; ENSGT00940000158368; -.
DR   HOGENOM; CLU_010920_1_4_1; -.
DR   OrthoDB; 4265336at2759; -.
DR   TreeFam; TF315453; -.
DR   BioGRID-ORCS; 110304; 3 hits in 77 CRISPR screens.
DR   ChiTaRS; Glra3; mouse.
DR   Proteomes; UP000000589; Chromosome 8.
DR   Bgee; ENSMUSG00000038257; Expressed in substantia nigra and 55 other cell types or tissues.
DR   GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR   GO; GO:0016935; C:glycine-gated chloride channel complex; IEA:Ensembl.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:Ensembl.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016934; F:extracellularly glycine-gated chloride channel activity; IEA:Ensembl.
DR   GO; GO:0016594; F:glycine binding; IEA:InterPro.
DR   GO; GO:0022852; F:glycine-gated chloride ion channel activity; IEA:Ensembl.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR   GO; GO:0051260; P:protein homooligomerization; IEA:Ensembl.
DR   CDD; cd19009; LGIC_ECD_GlyR_alpha; 1.
DR   CDD; cd19060; LGIC_TM_GlyR_alpha; 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; IPR008127; Glycine_rcpt_A.
DR   InterPro; IPR008130; Glycine_rcpt_A3.
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:SF455; GLYCINE RECEPTOR SUBUNIT ALPHA-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; PR01673; GLYRALPHA.
DR   PRINTS; PR01676; GLYRALPHA3.
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   Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW   Chloride {ECO:0000256|ARBA:ARBA00023214};
KW   Chloride channel {ECO:0000256|ARBA:ARBA00023173};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW   ECO:0000256|PIRSR:PIRSR608127-52};
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|ProteomicsDB:G5E811};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589};
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        23..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        271..293
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        334..357
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        450..470
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   DOMAIN          64..269
FT                   /note="Neurotransmitter-gated ion-channel ligand-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02931"
FT   DOMAIN          276..387
FT                   /note="Neurotransmitter-gated ion-channel transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF02932"
FT   BINDING         251..256
FT                   /ligand="strychnine"
FT                   /ligand_id="ChEBI:CHEBI:90700"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR608127-53"
FT   SITE            310
FT                   /note="Important for obstruction of the ion pore in the
FT                   closed conformation"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR608127-51"
FT   DISULFID        187..201
FT                   /evidence="ECO:0000256|PIRSR:PIRSR608127-52"
FT   DISULFID        247..258
FT                   /evidence="ECO:0000256|PIRSR:PIRSR608127-52"
SQ   SEQUENCE   480 AA;  55654 MW;  FE164C5C486A4507 CRC64;
     MPWIRLLSGS WISFRIMAHV RHFRTLVSGF YFWEAALLLS LVATKETNSA RSRSAPMSPS
     DFLDKLMGRT SGYDARIRPN FKGPPVNVTC NIFINSFGSI AETTMDYRVN IFLRQKWNDP
     RLAYSEYPDD SLDLDPSMLD SIWKPDLFFA NEKGANFHEV TTDNKLLRIF KNGNVLYSIR
     LTLTLSCPMD LKNFPMDVQT CIMQLESFGY TMNDLIFEWQ DEAPVQVAEG LTLPQFLLKE
     EKDLRYCTKH YNTGKFTCIE VRFHLERQMG YYLIQMYIPS LLIVILSWVS FWINMDAAPA
     RVALGITTVL TMTTQSSGSR ASLPKVSYVK AIDIWMAVCL LFVFSALLEY AAVNFVSRQH
     KELLRFRRKR KNKTEAFALE KFYRFSDTDD EVRESRFSFT AYGMGPCLQA KDGVVPKGPN
     HAVQVMPKSP DEMRKVFIDR AKKIDTISRA CFPLAFLIFN IFYWVIYKIL RHEDIHQQQD
//