ID G3W3E9_SARHA Unreviewed; 450 AA.
AC G3W3E9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 2.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=Glycine receptor alpha 1 {ECO:0000313|Ensembl:ENSSHAP00000009954.2};
GN Name=GLRA1 {ECO:0000313|Ensembl:ENSSHAP00000009954.2};
OS Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus.
OX NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000009954.2, ECO:0000313|Proteomes:UP000007648};
RN [1] {ECO:0000313|Ensembl:ENSSHAP00000009954.2, ECO:0000313|Proteomes:UP000007648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21709235; DOI=10.1073/pnas.1102838108;
RA Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., Miller J.,
RA Walenz B., Knight J., Qi J., Zhao F., Wang Q., Bedoya-Reina O.C.,
RA Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., Woodbridge P.,
RA Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., Helgen K.M.,
RA Lesk A.M., Pringle T.H., Patterson N., Zhang Y., Kreiss A., Woods G.M.,
RA Jones M.E., Schuster S.C.;
RT "Genetic diversity and population structure of the endangered marsupial
RT Sarcophilus harrisii (Tasmanian devil).";
RL Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011).
RN [2] {ECO:0000313|Ensembl:ENSSHAP00000009954.2}
RP IDENTIFICATION.
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 projection, dendrite
CC {ECO:0000256|ARBA:ARBA00004279}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}. Perikaryon
CC {ECO:0000256|ARBA:ARBA00004484}. 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 Glycine receptor (TC 1.A.9.3) subfamily. GLRA1 sub-subfamily.
CC {ECO:0000256|ARBA:ARBA00010129}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU000687}.
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DR AlphaFoldDB; G3W3E9; -.
DR STRING; 9305.ENSSHAP00000009954; -.
DR Ensembl; ENSSHAT00000010041.2; ENSSHAP00000009954.2; ENSSHAG00000008615.2.
DR eggNOG; KOG3644; Eukaryota.
DR GeneTree; ENSGT00940000159047; -.
DR HOGENOM; CLU_010920_1_4_1; -.
DR InParanoid; G3W3E9; -.
DR TreeFam; TF315453; -.
DR Proteomes; UP000007648; Unassembled WGS sequence.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0098690; C:glycinergic synapse; IEA:Ensembl.
DR GO; GO:0060077; C:inhibitory synapse; IEA:Ensembl.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:Ensembl.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
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:Ensembl.
DR GO; GO:0099507; F:ligand-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential; IEA:Ensembl.
DR GO; GO:0030977; F:taurine binding; IEA:Ensembl.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:1904315; F:transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR GO; GO:0007340; P:acrosome reaction; IEA:Ensembl.
DR GO; GO:0007628; P:adult walking behavior; IEA:Ensembl.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl.
DR GO; GO:0071361; P:cellular response to ethanol; IEA:Ensembl.
DR GO; GO:0071294; P:cellular response to zinc ion; IEA:Ensembl.
DR GO; GO:0060080; P:inhibitory postsynaptic potential; IEA:Ensembl.
DR GO; GO:0006936; P:muscle contraction; IEA:Ensembl.
DR GO; GO:0051970; P:negative regulation of transmission of nerve impulse; IEA:Ensembl.
DR GO; GO:0050884; P:neuromuscular process controlling posture; IEA:Ensembl.
DR GO; GO:0019228; P:neuronal action potential; IEA:Ensembl.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IEA:Ensembl.
DR GO; GO:2000344; P:positive regulation of acrosome reaction; IEA:Ensembl.
DR GO; GO:0002087; P:regulation of respiratory gaseous exchange by nervous system process; IEA:Ensembl.
DR GO; GO:0060013; P:righting reflex; IEA:Ensembl.
DR GO; GO:0001964; P:startle response; IEA:Ensembl.
DR GO; GO:0060012; P:synaptic transmission, glycinergic; IEA:Ensembl.
DR GO; GO:0007601; P:visual perception; 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; IPR008128; Glycine_rcpt_A1.
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:SF213; GLYCINE RECEPTOR SUBUNIT ALPHA-1; 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; PR01674; GLYRALPHA1.
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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00023257};
KW Reference proteome {ECO:0000313|Proteomes:UP000007648};
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};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT CHAIN 29..450
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT /id="PRO_5029943827"
FT TRANSMEM 251..273
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 314..337
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 422..442
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT DOMAIN 44..249
FT /note="Neurotransmitter-gated ion-channel ligand-binding"
FT /evidence="ECO:0000259|Pfam:PF02931"
FT DOMAIN 256..346
FT /note="Neurotransmitter-gated ion-channel transmembrane"
FT /evidence="ECO:0000259|Pfam:PF02932"
FT REGION 384..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 231..236
FT /ligand="strychnine"
FT /ligand_id="ChEBI:CHEBI:90700"
FT /evidence="ECO:0000256|PIRSR:PIRSR608127-53"
FT SITE 290
FT /note="Important for obstruction of the ion pore in the
FT closed conformation"
FT /evidence="ECO:0000256|PIRSR:PIRSR608127-51"
FT DISULFID 167..181
FT /evidence="ECO:0000256|PIRSR:PIRSR608127-52"
FT DISULFID 227..238
FT /evidence="ECO:0000256|PIRSR:PIRSR608127-52"
SQ SEQUENCE 450 AA; 51770 MW; 0A3F1E48696075EB CRC64;
MCSFNTLRLY LWETIVFFSL AASKEAEAAA RSAPKPMSPS DFLDKLMGRT SGYDARIRPN
FKGPPVNVSC NIFINSFGSI AETTMDYRVN IFLRQQWNDP RLAYNEYPDD SLDLDPSMLD
SIWKPDLFFA NEKGAHFHEI TTDNKLLRIS RNGNVLYSIR ITLTLACPMD LKNFPMDVQT
CIMQLESFGY TMNDLIFQWQ EQGAVQVADD LTLPQFILKE EKDLRYCTKH YNTGKFTCIE
ARFHLERQMG YYLIQMYIPS LLIVILSWIS FWINMDAAPA RVGLGITTVL TMTTQSSGSR
ASLPKVSYVK AIDIWMAVCL LFVFSALLEY AAVNFVSRQH KELLRFRRKR RHHKEDEAGE
GRFNFSAYGM GPACLQAKDG ISVKGANNNN TGNPPPPPSK SPEEMRKLFI QRAKKIDKMS
RIGFPMAFLI FNIFYWIIYK IVRREDVHNQ
//
