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Database: UniProt
Entry: A0A091F974_CORBR
LinkDB: A0A091F974_CORBR
Original site: A0A091F974_CORBR 
ID   A0A091F974_CORBR        Unreviewed;       463 AA.
AC   A0A091F974;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   SubName: Full=Glycine receptor subunit alpha-3 {ECO:0000313|EMBL:KFO65074.1};
GN   ORFNames=N302_04179 {ECO:0000313|EMBL:KFO65074.1};
OS   Corvus brachyrhynchos (American crow).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Corvoidea; Corvidae;
OC   Corvus.
OX   NCBI_TaxID=85066 {ECO:0000313|EMBL:KFO65074.1, ECO:0000313|Proteomes:UP000052976};
RN   [1] {ECO:0000313|EMBL:KFO65074.1, ECO:0000313|Proteomes:UP000052976}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N302 {ECO:0000313|EMBL:KFO65074.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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: 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}. 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; KK719676; KFO65074.1; -; Genomic_DNA.
DR   RefSeq; XP_008639785.1; XM_008641563.2.
DR   AlphaFoldDB; A0A091F974; -.
DR   STRING; 85066.A0A091F974; -.
DR   GeneID; 103622586; -.
DR   KEGG; cbrc:103622586; -.
DR   CTD; 8001; -.
DR   OrthoDB; 4265336at2759; -.
DR   Proteomes; UP000052976; Unassembled WGS sequence.
DR   GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR   GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016934; F:extracellularly glycine-gated chloride channel activity; IEA:InterPro.
DR   GO; GO:0016594; F:glycine binding; IEA:InterPro.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR   GO; GO:0022824; F:transmitter-gated monoatomic ion channel activity; IEA:InterPro.
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   3: Inferred from homology;
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|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   Receptor {ECO:0000313|EMBL:KFO65074.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000052976};
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        20..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        436..456
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   DOMAIN          70..269
FT                   /note="Neurotransmitter-gated ion-channel ligand-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02931"
FT   DOMAIN          276..362
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   463 AA;  52783 MW;  9EBF6ED00E012BAE CRC64;
     MPPTPPLPGS AASPSSMARI RYLRAAVSGF YLWEAAVLLS LVATKETDSA RSRSMPMSPS
     DFLDKLMGRM SGYDARIRPN FKGPPVNVTC NIFINSFGSI AETTMDYRVN IFLRQNWNDP
     RLAYSEYPDD SLDLDPSMLD SIWKPDLFFA NEKGANFHEV TTDNKLLRIF KNGNVLYSIR
     LTLILSCPMD LKNFPMDVQT CIMQLESFGY TMNDLIFEGQ EKGAFQVAEG LTLPQFLLKE
     EKDLCYCTKH YNTGKFTCIE VRFHLERQMG YYLIQMYIPS LLIVILSWVS FWINMDAAPA
     RVALGITTVL TMTTQSSGSR ASLPKVSYVK AIDIWMAVCL LFVFSALLEY AAVNFVSRQH
     KELLRFRRKR KKSKDDDTRD SQFSITAYGV GPCVPAKDGM TQKGPNNPVQ AVPKSPDEMR
     KVFIDRAKKI DTISRACFPL AFLIFNIFYW VIYKIIRHED IHQ
//
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