ID H0VTX0_CAVPO Unreviewed; 457 AA.
AC H0VTX0;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Glycine receptor alpha 4 {ECO:0000313|Ensembl:ENSCPOP00000014136.3};
GN Name=Glra4 {ECO:0000313|Ensembl:ENSCPOP00000014136.3};
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000014136.3, ECO:0000313|Proteomes:UP000005447};
RN [1] {ECO:0000313|Proteomes:UP000005447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSCPOP00000014136.3}
RP IDENTIFICATION.
RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000014136.3};
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 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 EMBL; AAKN02029003; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003471021.1; XM_003470973.3.
DR AlphaFoldDB; H0VTX0; -.
DR STRING; 10141.ENSCPOP00000014136; -.
DR Ensembl; ENSCPOT00000015830.3; ENSCPOP00000014136.3; ENSCPOG00000015675.4.
DR GeneID; 100723095; -.
DR KEGG; cpoc:100723095; -.
DR CTD; 441509; -.
DR VEuPathDB; HostDB:ENSCPOG00000015675; -.
DR eggNOG; KOG3644; Eukaryota.
DR GeneTree; ENSGT00940000158789; -.
DR HOGENOM; CLU_010920_1_4_1; -.
DR InParanoid; H0VTX0; -.
DR OMA; IQTCTMH; -.
DR OrthoDB; 4265336at2759; -.
DR TreeFam; TF315453; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000015675; Expressed in frontal cortex.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0098690; C:glycinergic synapse; IEA:Ensembl.
DR GO; GO:0099634; C:postsynaptic specialization membrane; IEA:Ensembl.
DR GO; GO:0016934; F:extracellularly glycine-gated chloride channel activity; IEA:Ensembl.
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 GO; GO:0043200; P:response to amino acid; 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; 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|ARBA:ARBA00023157,
KW 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 Reference proteome {ECO:0000313|Proteomes:UP000005447};
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..28
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT CHAIN 29..457
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT /id="PRO_5022248533"
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; 52771 MW; C5D7CB915EAEAE70 CRC64;
MTTLVPATLS FFLLWTLPGQ ILLRVALAKE DVRSGTKDSQ PMSPSDFLDK LMGRTSGYDA
RIRPNFKGPP VNVTCNIFIN SFGSVTETTM DYRVNVFLRQ QWNDPRLAYQ EYPDDSLDLD
PSMLDSIWKP DLFFANEKGA NFHEVTTDNK LLRIFKNGNV LYSIRLTLIL SCPMDLKNFP
MDIQTCTMQL ESFGYTMNDL VFEWLEDAPA VQVAEGLTLP QFILRDEKDL GYCTKNYNTG
KFTCIEVKFH LERQMGYYLI QMYIPSLLIV ILSWVSFWIN MDAAPARVGL GITTVLTMTT
QSSGSRASLP KVSYVKAIDI WMAVCLLFVF AALLEYAAVN FVSRQHKEFM RLRRRQRRQR
IEEDIIRESR FYFRGYGLGH CLQGKDRGPM KGSTIYSPQP PAPLLKEGEI MRKLYVDRAK
RIDTISRAVF PFTFLIFNIF YWVVYKVLRS EDIHQAL
//
