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Database: UniProt
Entry: A0A1S3AK21_ERIEU
LinkDB: A0A1S3AK21_ERIEU
Original site: A0A1S3AK21_ERIEU 
ID   A0A1S3AK21_ERIEU        Unreviewed;       457 AA.
AC   A0A1S3AK21;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Glycine receptor subunit alpha-4 {ECO:0000313|RefSeq:XP_007536449.1};
GN   Name=GLRA4 {ECO:0000313|RefSeq:XP_007536449.1};
OS   Erinaceus europaeus (Western European hedgehog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC   Erinaceus.
OX   NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_007536449.1};
RN   [1] {ECO:0000313|RefSeq:XP_007536449.1}
RP   IDENTIFICATION.
RG   RefSeq;
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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU000687}.
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DR   RefSeq; XP_007536449.1; XM_007536387.1.
DR   AlphaFoldDB; A0A1S3AK21; -.
DR   STRING; 9365.ENSEEUP00000013600; -.
DR   GeneID; 103125581; -.
DR   eggNOG; KOG3644; Eukaryota.
DR   InParanoid; A0A1S3AK21; -.
DR   OrthoDB; 4265336at2759; -.
DR   Proteomes; UP000079721; Unplaced.
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:SF211; GLYCINE RECEPTOR SUBUNIT ALPHA-4; 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:0000313|RefSeq:XP_007536449.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000079721};
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..23
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   CHAIN           24..457
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT                   /id="PRO_5022268864"
FT   TRANSMEM        255..277
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        320..343
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   TRANSMEM        428..448
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU000687"
FT   DOMAIN          49..255
FT                   /note="Neurotransmitter-gated ion-channel ligand-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02931"
FT   DOMAIN          262..358
FT                   /note="Neurotransmitter-gated ion-channel transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF02932"
FT   BINDING         237..242
FT                   /ligand="strychnine"
FT                   /ligand_id="ChEBI:CHEBI:90700"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR608127-53"
FT   SITE            296
FT                   /note="Important for obstruction of the ion pore in the
FT                   closed conformation"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR608127-51"
FT   DISULFID        172..186
FT                   /evidence="ECO:0000256|PIRSR:PIRSR608127-52"
FT   DISULFID        233..244
FT                   /evidence="ECO:0000256|PIRSR:PIRSR608127-52"
SQ   SEQUENCE   457 AA;  52642 MW;  339460DC90F5B99A CRC64;
     MTTLFPATLS FLLLLTLPGQ VLLRVAFAKE EIKSGTKGSQ PMSPSDFLDK LMGRTSGYDA
     RIRPNFKGPP VNVTCNIFIN SFGSVTETTM DYRVNVFLRQ QWNDPRLAYR EYPDDSLDLD
     PSMLDSIWKP DLFFANEKGA SFHEVTTDNK LLRIFKNGNV LYSIRLTLIL SCPMDLKNFP
     MDIQTCTMQL ESFGYTMNDL VFEWLEDAPA VQVAEGLTLP QFILRDEKDL GYCTKYYNTG
     KFTCIEVKFH LERQMGYYLI QMYIPSLLIV ILSWVSFWIN MDAAPARVGL GITTVLTMTT
     QSSGSRASLP KVSYVKAIDI WMAVCLLFVF AALLEYAAVN FVSRQHKEFI RLRRRQRRQR
     MEEDIIREGR FYFRGYGLGH CLQARDGGPV EGSGIYSPQP PTPFLREGET MRKLYVDRAK
     RIDTISRAVF PFTFLIFNIF YWVVYKVLRS EDIHQAL
//
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