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5HT3A_CAVPO
ID   5HT3A_CAVPO             Reviewed;         490 AA.
AC   O70212; O70213;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=5-hydroxytryptamine receptor 3A;
DE            Short=5-HT3-A;
DE            Short=5-HT3A;
DE   AltName: Full=5-hydroxytryptamine receptor 3;
DE            Short=5-HT-3;
DE            Short=5-HT3R;
DE   AltName: Full=Serotonin receptor 3A;
DE   AltName: Full=Serotonin-gated ion channel receptor;
DE   Flags: Precursor;
GN   Name=HTR3A; Synonyms=5HT3R, HTR3;
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:0000312|EMBL:AAC06136.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE
RP   SPECIFICITY, AND PHARMACOLOGICAL CHARACTERIZATION.
RC   TISSUE=Small intestine;
RX   PubMed=9463477; DOI=10.1124/mol.53.2.202;
RA   Lankiewicz S., Lobitz N., Wetzel C.H.R., Rupprecht R., Gisselmann G.,
RA   Hatt H.;
RT   "Molecular cloning, functional expression, and pharmacological
RT   characterization of 5-hydroxytryptamine3 receptor cDNA and its splice
RT   variants from guinea pig.";
RL   Mol. Pharmacol. 53:202-212(1998).
CC   -!- FUNCTION: This is one of the several different receptors for 5-
CC       hydroxytryptamine (serotonin), a biogenic hormone that functions as a
CC       neurotransmitter, a hormone, and a mitogen. This receptor is a ligand-
CC       gated ion channel, which when activated causes fast, depolarizing
CC       responses in neurons. It is a cation-specific, but otherwise relatively
CC       nonselective, ion channel. {ECO:0000269|PubMed:9463477}.
CC   -!- SUBUNIT: Forms pentahomomeric complex as well as pentaheteromeric
CC       complex with HTR3B or HTR3C or HTR3D or HTR3E; homomeric complex is
CC       functional but exhibits low conductance with modified voltage
CC       dependence, and decreased agonist and antagonist affinity. Interacts
CC       with RIC3 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane
CC       protein. Cell membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=5-HT3R-L;
CC         IsoId=O70212-1; Sequence=Displayed;
CC       Name=2; Synonyms=5-HT3R-S;
CC         IsoId=O70212-2; Sequence=VSP_000077;
CC   -!- TISSUE SPECIFICITY: Expressed in cortex, intestine and liver. Not
CC       expressed in muscle or spleen. {ECO:0000269|PubMed:9463477}.
CC   -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC       5-hydroxytryptamine receptor (TC 1.A.9.2) subfamily. HTR3A sub-
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AF006461; AAC06136.1; -; mRNA.
DR   EMBL; AF006462; AAC06137.1; -; mRNA.
DR   RefSeq; NP_001166178.1; NM_001172707.1. [O70212-1]
DR   AlphaFoldDB; O70212; -.
DR   SMR; O70212; -.
DR   STRING; 10141.ENSCPOP00000009728; -.
DR   BindingDB; O70212; -.
DR   ChEMBL; CHEMBL3666; -.
DR   DrugCentral; O70212; -.
DR   iPTMnet; O70212; -.
DR   GeneID; 100135547; -.
DR   KEGG; cpoc:100135547; -.
DR   CTD; 3359; -.
DR   eggNOG; KOG3645; Eukaryota.
DR   InParanoid; O70212; -.
DR   OrthoDB; 611108at2759; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0030285; C:integral component of synaptic vesicle membrane; IDA:UniProtKB.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005230; F:extracellular ligand-gated ion channel activity; IEA:InterPro.
DR   GO; GO:0004890; F:GABA-A receptor activity; IDA:UniProtKB.
DR   GO; GO:0006812; P:cation transport; IDA:UniProtKB.
DR   Gene3D; 1.20.58.390; -; 1.
DR   Gene3D; 2.70.170.10; -; 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   PANTHER; PTHR18945; PTHR18945; 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; SSF63712; SSF63712; 1.
DR   SUPFAM; SSF90112; SSF90112; 1.
DR   TIGRFAMs; TIGR00860; LIC; 1.
DR   PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW   Ion channel; Ion transport; Ligand-gated ion channel; Membrane;
KW   Postsynaptic cell membrane; Receptor; Reference proteome; Signal; Synapse;
KW   Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..490
FT                   /note="5-hydroxytryptamine receptor 3A"
FT                   /id="PRO_0000000407"
FT   TOPO_DOM        20..249
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        250..270
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        271..285
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        286..306
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        307..312
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        313..333
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        334..467
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        468..488
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        489..490
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   REGION          401..422
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          426..462
FT                   /note="HA-stretch"
FT   CARBOHYD        33
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        109
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        175
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        191
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        162..176
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         386..391
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:9463477"
FT                   /id="VSP_000077"
SQ   SEQUENCE   490 AA;  55656 MW;  EDB32F8597494F61 CRC64;
     MVLWLQLALL ALLLPTSLAQ GEVRGKGTAQ AHNSTRPALQ RLSDHLLADY RKSVRPVRDW
     RKPTTVSIDA IVYAILSVDE KNQVLTTYIW YRQFWTDEFL QWNPEDFDNI TKLSIPTDSI
     WVPDILINEF VDVGKSPNIP YVYVRHQGEV QNYKPLQVVT ACSLDIYNFP FDVQNCSLTF
     TSWLHTIQDI NISLWRLPEK VKSDKSVFMN QGEWELLGVL TEFLEFSDRE SRGSFAEMKF
     YVVIRRRPLF YAVTLLLPSI FLMIVDIVGF YLPPDSGERV SFKITLLLGY SVFLIIVSDT
     LPATAIGTPL ISVYFVVCMA LLVISLAETI LIVRLVHKQD LQQPVPLWLR HLVLERIAGL
     LCLGEQLTSH RGPATLQATK TDDFSGSTLL PAMGNHCGPL GGPQDLEKTS RGRGSPPPPP
     REASLAMCGL LQELASIRHF LEKREETREV ARDWLRVGSV LDKLLFRVYL LAVLAYSITL
     VTLWSVWHYA
 
 
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