ID H3CNY0_TETNG Unreviewed; 485 AA.
AC H3CNY0;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=5-hydroxytryptamine (serotonin) receptor 3A {ECO:0000313|Ensembl:ENSTNIP00000009963.1};
GN Name=HTR3A {ECO:0000313|Ensembl:ENSTNIP00000009963.1};
OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS nigroviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000009963.1, ECO:0000313|Proteomes:UP000007303};
RN [1] {ECO:0000313|Proteomes:UP000007303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15496914; DOI=10.1038/nature03025;
RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT early vertebrate proto-karyotype.";
RL Nature 431:946-957(2004).
RN [2] {ECO:0000313|Ensembl:ENSTNIP00000009963.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Forms serotonin (5-hydroxytryptamine/5-HT3)-activated cation-
CC selective channel complexes, which when activated cause fast,
CC depolarizing responses in neurons. {ECO:0000256|ARBA:ARBA00037540}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Ca(2+)(in) = Ca(2+)(out); Xref=Rhea:RHEA:29671,
CC ChEBI:CHEBI:29108; Evidence={ECO:0000256|ARBA:ARBA00036634};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103;
CC Evidence={ECO:0000256|ARBA:ARBA00034430};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963,
CC ChEBI:CHEBI:29101; Evidence={ECO:0000256|ARBA:ARBA00036239};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC {ECO:0000256|RuleBase:RU000687}.
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DR AlphaFoldDB; H3CNY0; -.
DR STRING; 99883.ENSTNIP00000009963; -.
DR Ensembl; ENSTNIT00000010142.1; ENSTNIP00000009963.1; ENSTNIG00000007161.1.
DR GeneTree; ENSGT00940000157705; -.
DR HOGENOM; CLU_018074_5_0_1; -.
DR InParanoid; H3CNY0; -.
DR OMA; VGNHCSH; -.
DR TreeFam; TF315605; -.
DR Proteomes; UP000007303; Unassembled WGS sequence.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:InterPro.
DR GO; GO:0005230; F:extracellular ligand-gated monoatomic ion channel activity; IEA:InterPro.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR CDD; cd19011; LGIC_ECD_5-HT3A; 1.
DR CDD; cd19063; LGIC_TM_5-HT3; 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; IPR008132; 5HT3_rcpt.
DR InterPro; IPR008133; 5HT3_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:SF52; 5-HYDROXYTRYPTAMINE RECEPTOR 3A; 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; PR01709; 5HT3ARECEPTR.
DR PRINTS; PR01708; 5HT3RECEPTOR.
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 Ion channel {ECO:0000256|RuleBase:RU000687};
KW Ion transport {ECO:0000256|RuleBase:RU000687};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU000687};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000007303};
KW Signal {ECO:0000256|RuleBase:RU000687};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000687};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU000687}; Transport {ECO:0000256|RuleBase:RU000687}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT CHAIN 20..485
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT /id="PRO_5022272237"
FT TRANSMEM 248..271
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 283..304
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 310..332
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT TRANSMEM 459..482
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU000687"
FT DOMAIN 41..247
FT /note="Neurotransmitter-gated ion-channel ligand-binding"
FT /evidence="ECO:0000259|Pfam:PF02931"
FT DOMAIN 254..474
FT /note="Neurotransmitter-gated ion-channel transmembrane"
FT /evidence="ECO:0000259|Pfam:PF02932"
FT REGION 375..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 485 AA; 55447 MW; 6FA81128F49ACF61 CRC64;
MRASPAWTLL LLLLAPTAAR GCAVKKSGSS SGRFSNATLV RLSEFLSAGY KKGVRPVKDW
RTSTSVAIDL MVYSILNVDE KNQVLTTYVW YRQSWTDEFL VWNPEDFDEV KQVSMPTANV
WVPDILINEF VDVGKSPDIP YVYVSHDGLV RNYKPIQVVT ACTLNIYNFP FDVQKCSLTF
QSWLHTIDDI NITLLRSPEE LREDKSVFMN QGEWELLHIL SKYKSFSVDN DDYYAEMKFH
VVIRRRPLFY TVNLLLPSIF LMVMDIVGFY LPPDSGERVS FKITLLLGYS VFLIIVSDTL
PATAIGTPLI GVYFVVCMAL LVISLTETVL IVRLVHKQDL RPVPDWLKYL VLERAPALFC
IHRKHRLCSR LSSQGSDLDR YKDSSYGTSK DGPQQTLSQH EREGGLLRLG LPPHRDPTPP
VMSNILREVT AIRSFLEKRD RCREVAKEWL QVGYVLDVLL FRVYLVAVVT YSITLGTLWS
VWQVA
//