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Database: UniProt
Entry: A0A093PQW6_9PASS
LinkDB: A0A093PQW6_9PASS
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ID   A0A093PQW6_9PASS        Unreviewed;       451 AA.
AC   A0A093PQW6;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   SubName: Full=Glycine receptor subunit alpha-2 {ECO:0000313|EMBL:KFW78831.1};
DE   Flags: Fragment;
GN   ORFNames=N305_14156 {ECO:0000313|EMBL:KFW78831.1};
OS   Manacus vitellinus (golden-collared manakin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Pipridae; Manacus.
OX   NCBI_TaxID=328815 {ECO:0000313|EMBL:KFW78831.1, ECO:0000313|Proteomes:UP000053258};
RN   [1] {ECO:0000313|EMBL:KFW78831.1, ECO:0000313|Proteomes:UP000053258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N305 {ECO:0000313|EMBL:KFW78831.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (JUN-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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU000687}.
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DR   EMBL; KL670369; KFW78831.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093PQW6; -.
DR   STRING; 328815.ENSMVIP00005022186; -.
DR   Proteomes; UP000053258; 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; IPR008129; Glycine_rcpt_A2.
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:SF28; GLYCINE RECEPTOR SUBUNIT ALPHA-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; PR01673; GLYRALPHA.
DR   PRINTS; PR01675; GLYRALPHA2.
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:KFW78831.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053258};
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        255..277
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        318..341
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        423..443
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   DOMAIN          48..253
FT                   /note="Neurotransmitter-gated ion-channel ligand-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02931"
FT   DOMAIN          260..346
FT                   /note="Neurotransmitter-gated ion-channel transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF02932"
FT   REGION          386..405
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         235..240
FT                   /ligand="strychnine"
FT                   /ligand_id="ChEBI:CHEBI:90700"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR608127-53"
FT   SITE            294
FT                   /note="Important for obstruction of the ion pore in the
FT                   closed conformation"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR608127-51"
FT   DISULFID        171..185
FT                   /evidence="ECO:0000256|PIRSR:PIRSR608127-52"
FT   DISULFID        231..242
FT                   /evidence="ECO:0000256|PIRSR:PIRSR608127-52"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFW78831.1"
FT   NON_TER         451
FT                   /evidence="ECO:0000313|EMBL:KFW78831.1"
SQ   SEQUENCE   451 AA;  51791 MW;  F964CEEF47AD10A1 CRC64;
     NFSILNTIEV KYQLMVANNL FRTTFCKEHD SRSGKSPSQT LSPSDFLDKL MGRTSGYDAR
     IRPNFKGPPV NVTCNIFINS FGSIAETTMD YRVNIFLRQQ WNDSRLAYSE YPDDSLDLDP
     SMLDSIWKPD LFFANEKGAN FHDVTTDNKL LRISKTGKVL YSIRLTLTLS CPMDLKNFPM
     DVQTCTMQLE SFGYTMNDLI FEWLSDGPVQ VAEGLTLPQF ILKEDKELGY CTKHYNTGKF
     TCIEVKFHLE RQMGYYLIQM YIPSLLIVIL SWVSFWINMD AAPARVALGI TTVLTMTTQS
     SGSRASLPKV SYVKAIDIWM AVCLLFVFAA LLEYAAVNFV SRQHKEFLRL RRRQRRQNKE
     DEVARDSRFN FSGYGMGHCL QVKDGTAVKA TPPNPPPAPP KDSDSIKKKF VDRAKRIDTI
     SRAAFPLAFL IFNIFYWITY KIIRHEDIHK K
//
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