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Database: UniProt
Entry: A0A087XDE7_POEFO
LinkDB: A0A087XDE7_POEFO
Original site: A0A087XDE7_POEFO 
ID   A0A087XDE7_POEFO        Unreviewed;       430 AA.
AC   A0A087XDE7;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 2.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Glycine receptor, alpha 2 {ECO:0000313|Ensembl:ENSPFOP00000003800.2};
OS   Poecilia formosa (Amazon molly) (Limia formosa).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000003800.2, ECO:0000313|Proteomes:UP000028760};
RN   [1] {ECO:0000313|Proteomes:UP000028760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA   Schartl M., Warren W.;
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPFOP00000003800.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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: 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; AYCK01002162; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A087XDE7; -.
DR   STRING; 48698.ENSPFOP00000003800; -.
DR   Ensembl; ENSPFOT00000003808.2; ENSPFOP00000003800.2; ENSPFOG00000003718.2.
DR   eggNOG; KOG3644; Eukaryota.
DR   GeneTree; ENSGT00940000158730; -.
DR   OMA; LVFWLEP; -.
DR   Proteomes; UP000028760; 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:0005254; F:chloride channel activity; IEA:UniProtKB-KW.
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; 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; 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:0000256|ARBA:ARBA00023170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028760};
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        218..240
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        281..304
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        402..422
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   DOMAIN          17..216
FT                   /note="Neurotransmitter-gated ion-channel ligand-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02931"
FT   DOMAIN          223..344
FT                   /note="Neurotransmitter-gated ion-channel transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF02932"
FT   BINDING         198..203
FT                   /ligand="strychnine"
FT                   /ligand_id="ChEBI:CHEBI:90700"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR608127-53"
FT   SITE            257
FT                   /note="Important for obstruction of the ion pore in the
FT                   closed conformation"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR608127-51"
FT   DISULFID        134..148
FT                   /evidence="ECO:0000256|PIRSR:PIRSR608127-52"
FT   DISULFID        194..205
FT                   /evidence="ECO:0000256|PIRSR:PIRSR608127-52"
SQ   SEQUENCE   430 AA;  49539 MW;  F8061C1A67055C5E CRC64;
     SSNMSPSDFL DSLMGRTSGY DARIRPNFKG PPVNVTCNIF INSFGSIAET TMDYRVNIFL
     RQKWNDPRLA YSKYPDSSLD LDPSMLDSIW KPDLFFANEK GANFHDVTTD NKLLRIFKDG
     NVLYSIRLTL ILSCPMDLKN FPMDVQTCTM QLESFGYTMN DLIFEWLENG AVQVSEGLTL
     PQFIMKEEKE LGYCTKHYNT GKFTCIEVKF HLERQMGYYL IQMYIPSLLI VILSWVSFWI
     NMDAAPARVA LGITTVLTMT TQSSGSRASL PKVSYVKAID IWMAVCLLFV FAALLEYAGV
     NFVSRQQKEF LRLRRRQTTK RRGLCSTKRY KFTRQYTNNQ EDEGRFNLTG YNMSQCMPTK
     DGSAVKNAVP ATNPQPSTPK DIDAMRKKFV DRAKRIDTIS RAAFPLAFLI FNVFYWITYK
     IIRHEDVHKQ
//
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