5HT3A_MOUSE
ID 5HT3A_MOUSE Reviewed; 487 AA.
AC P23979; Q61225; Q61226;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 174.
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=5ht3, Htr3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1718042; DOI=10.1126/science.1718042;
RA Maricq A.V., Peterson A.S., Brake A.J., Myers R.M., Julius D.;
RT "Primary structure and functional expression of the 5HT3 receptor, a
RT serotonin-gated ion channel.";
RL Science 254:432-437(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=8112471; DOI=10.1016/0014-5793(94)80435-4;
RA Uetz P., Abdelatty F., Villarroel A., Gundrun R., Weiss B., Koenen M.;
RT "Organisation of the murine 5-HT3 receptor gene and assignment to human
RT chromosome 11.";
RL FEBS Lett. 339:302-306(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=A/J;
RX PubMed=7683998; DOI=10.1016/0922-4106(93)90128-v;
RA Hope A.G., Downie D.L., Sutherland L., Lambert J.J., Peters J.A.,
RA Burchell B.;
RT "Cloning and functional expression of an apparent splice variant of the
RT murine 5-HT3 receptor A subunit.";
RL Eur. J. Pharmacol. 245:187-192(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=129/Sv;
RX PubMed=7854052; DOI=10.1016/0169-328x(94)90095-7;
RA Werner P., Kawashima E., Reid J., Hussy N., Lundstrom K., Buell G.,
RA Humbert Y., Jones K.A.;
RT "Organization of the mouse 5-HT3 receptor gene and functional expression of
RT two splice variants.";
RL Brain Res. Mol. Brain Res. 26:233-241(1994).
RN [5]
RP FUNCTION, AND REGION.
RX PubMed=12867984; DOI=10.1038/nature01788;
RA Kelley S.P., Dunlop J.I., Kirkness E.F., Lambert J.J., Peters J.A.;
RT "A cytoplasmic region determines single-channel conductance in 5-HT3
RT receptors.";
RL Nature 424:321-324(2003).
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:12867984}.
CC -!- SUBUNIT: Forms pentahomomeric complex as well as pentaheteromeric
CC complex with HTR3B; homomeric complex is functional but exhibits low
CC conductance with modified voltage dependence, and decreased agonist and
CC antagonist affinity. Interacts with RIC3 (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC P23979-1; P23979-1: Htr3a; NbExp=7; IntAct=EBI-15824923, EBI-15824923;
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=5-HT3R-A;
CC IsoId=P23979-1; Sequence=Displayed;
CC Name=5-HT3R-AS;
CC IsoId=P23979-2; Sequence=VSP_000079;
CC -!- TISSUE SPECIFICITY: Brain, spinal cord, and heart.
CC -!- MISCELLANEOUS: The HA-stretch region of HTR3A seems to be responsible
CC for the low conductance of HTR3A homomers compared to that of
CC HTR3A/HTR3B heteromers.
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; M74425; AAA37124.1; -; mRNA.
DR EMBL; Z22772; CAA80453.1; -; Genomic_DNA.
DR EMBL; Z22773; CAA80453.1; JOINED; Genomic_DNA.
DR EMBL; X72395; CAA51089.1; -; mRNA.
DR EMBL; X79283; CAA55870.1; -; Genomic_DNA.
DR EMBL; X79283; CAA55871.1; -; Genomic_DNA.
DR PIR; S41757; S41757.
DR RefSeq; NP_038589.2; NM_013561.2.
DR PDB; 4PIR; X-ray; 3.50 A; A/B/C/D/E=32-485.
DR PDB; 6BE1; EM; 4.31 A; A/B/C/D/E=32-487.
DR PDB; 6DG7; EM; 3.32 A; A/B/C/D/E=34-487.
DR PDB; 6DG8; EM; 3.89 A; A/B/C/D/E=34-487.
DR PDB; 6HIN; EM; 4.10 A; A/B/C/D/E=36-484.
DR PDB; 6HIO; EM; 4.20 A; A/B/C/D/E=35-483.
DR PDB; 6HIQ; EM; 3.20 A; A/B/C/D/E=35-485.
DR PDB; 6NP0; EM; 2.92 A; A/B/C/D/E=1-487.
DR PDB; 6W1J; EM; 2.92 A; A/B/C/D/E=33-487.
DR PDB; 6W1M; EM; 3.06 A; A/B/C/D/E=33-487.
DR PDB; 6W1Y; EM; 3.35 A; A/B/C/D/E=33-487.
DR PDB; 6Y1Z; EM; 2.82 A; A/B/C/D/E=21-487.
DR PDBsum; 4PIR; -.
DR PDBsum; 6BE1; -.
DR PDBsum; 6DG7; -.
DR PDBsum; 6DG8; -.
DR PDBsum; 6HIN; -.
DR PDBsum; 6HIO; -.
DR PDBsum; 6HIQ; -.
DR PDBsum; 6NP0; -.
DR PDBsum; 6W1J; -.
DR PDBsum; 6W1M; -.
DR PDBsum; 6W1Y; -.
DR PDBsum; 6Y1Z; -.
DR AlphaFoldDB; P23979; -.
DR SMR; P23979; -.
DR ComplexPortal; CPX-274; 5-hydroxytryptamine-3A receptor complex.
DR ComplexPortal; CPX-275; 5-hydroxytryptamine-3A/B receptor complex.
DR DIP; DIP-48769N; -.
DR STRING; 10090.ENSMUSP00000003826; -.
DR BindingDB; P23979; -.
DR ChEMBL; CHEMBL4972; -.
DR DrugCentral; P23979; -.
DR GuidetoPHARMACOLOGY; 373; -.
DR GlyGen; P23979; 3 sites.
DR PhosphoSitePlus; P23979; -.
DR SwissPalm; P23979; -.
DR MaxQB; P23979; -.
DR PaxDb; P23979; -.
DR PRIDE; P23979; -.
DR ProteomicsDB; 285992; -. [P23979-1]
DR ProteomicsDB; 285993; -. [P23979-2]
DR ABCD; P23979; 1 sequenced antibody.
DR DNASU; 15561; -.
DR GeneID; 15561; -.
DR KEGG; mmu:15561; -.
DR CTD; 3359; -.
DR MGI; MGI:96282; Htr3a.
DR eggNOG; KOG3645; Eukaryota.
DR InParanoid; P23979; -.
DR OrthoDB; 611108at2759; -.
DR PhylomeDB; P23979; -.
DR Reactome; R-MMU-112314; Neurotransmitter receptors and postsynaptic signal transmission.
DR BioGRID-ORCS; 15561; 1 hit in 73 CRISPR screens.
DR PRO; PR:P23979; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P23979; protein.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0032154; C:cleavage furrow; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; ISO:MGI.
DR GO; GO:0099056; C:integral component of presynaptic membrane; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:1904602; C:serotonin-activated cation-selective channel complex; IPI:ComplexPortal.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0005231; F:excitatory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0051378; F:serotonin binding; ISO:MGI.
DR GO; GO:0022850; F:serotonin-gated cation-selective channel activity; ISO:MGI.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IBA:GO_Central.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0098662; P:inorganic cation transmembrane transport; ISO:MGI.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0050877; P:nervous system process; IBA:GO_Central.
DR GO; GO:0032414; P:positive regulation of ion transmembrane transporter activity; ISO:MGI.
DR GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR GO; GO:0007210; P:serotonin receptor signaling pathway; ISO:MGI.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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 3D-structure; Alternative splicing; Cell membrane; Disulfide bond;
KW Glycoprotein; Ion channel; Ion transport; Ligand-gated ion channel;
KW Membrane; Postsynaptic cell membrane; Receptor; Reference proteome; Signal;
KW Synapse; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..487
FT /note="5-hydroxytryptamine receptor 3A"
FT /id="PRO_0000000409"
FT TOPO_DOM 24..245
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 246..272
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 273..277
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..296
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 297..305
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..324
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 325..464
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 465..484
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 485..487
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 423..459
FT /note="HA-stretch"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 161..175
FT /evidence="ECO:0000250"
FT VAR_SEQ 383..388
FT /note="Missing (in isoform 5-HT3R-AS)"
FT /evidence="ECO:0000305"
FT /id="VSP_000079"
FT CONFLICT 31
FT /note="E -> AR (in Ref. 3; CAA51089 and 4; CAA55870/
FT CAA55871)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="I -> V (in Ref. 3; CAA51089)"
FT /evidence="ECO:0000305"
FT CONFLICT 302
FT /note="T -> TA (in Ref. 3; CAA51089 and 4; CAA55870/
FT CAA55871)"
FT /evidence="ECO:0000305"
FT CONFLICT 384
FT /note="S -> SS (in Ref. 2; CAA80453)"
FT /evidence="ECO:0000305"
FT CONFLICT 393
FT /note="H -> T (in Ref. 4; CAA55870/CAA55871)"
FT /evidence="ECO:0000305"
FT HELIX 39..46
FT /evidence="ECO:0007829|PDB:6Y1Z"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:6W1Y"
FT STRAND 63..78
FT /evidence="ECO:0007829|PDB:6Y1Z"
FT TURN 79..82
FT /evidence="ECO:0007829|PDB:6Y1Z"
FT STRAND 83..95
FT /evidence="ECO:0007829|PDB:6Y1Z"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:6W1Y"
FT TURN 103..108
FT /evidence="ECO:0007829|PDB:6Y1Z"
FT STRAND 111..115
FT /evidence="ECO:0007829|PDB:6Y1Z"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:6Y1Z"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:6Y1Z"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:6Y1Z"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:6Y1Z"
FT STRAND 147..160
FT /evidence="ECO:0007829|PDB:6Y1Z"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:6Y1Z"
FT STRAND 172..183
FT /evidence="ECO:0007829|PDB:6Y1Z"
FT TURN 186..188
FT /evidence="ECO:0007829|PDB:6Y1Z"
FT STRAND 189..195
FT /evidence="ECO:0007829|PDB:6Y1Z"
FT HELIX 197..201
FT /evidence="ECO:0007829|PDB:6Y1Z"
FT STRAND 210..228
FT /evidence="ECO:0007829|PDB:6Y1Z"
FT STRAND 231..244
FT /evidence="ECO:0007829|PDB:6Y1Z"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:6Y1Z"
FT HELIX 250..267
FT /evidence="ECO:0007829|PDB:6Y1Z"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:6Y1Z"
FT HELIX 277..295
FT /evidence="ECO:0007829|PDB:6Y1Z"
FT TURN 296..298
FT /evidence="ECO:0007829|PDB:6Y1Z"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:6W1M"
FT HELIX 308..333
FT /evidence="ECO:0007829|PDB:6Y1Z"
FT STRAND 335..337
FT /evidence="ECO:0007829|PDB:6DG7"
FT HELIX 344..353
FT /evidence="ECO:0007829|PDB:6Y1Z"
FT HELIX 423..482
FT /evidence="ECO:0007829|PDB:6Y1Z"
SQ SEQUENCE 487 AA; 56056 MW; D0148867C8536D66 CRC64;
MRLCIPQVLL ALFLSMLTAP GEGSRRRATQ EDTTQPALLR LSDHLLANYK KGVRPVRDWR
KPTTVSIDVI MYAILNVDEK NQVLTTYIWY RQYWTDEFLQ WTPEDFDNVT KLSIPTDSIW
VPDILINEFV DVGKSPNIPY VYVHHRGEVQ NYKPLQLVTA CSLDIYNFPF DVQNCSLTFT
SWLHTIQDIN ITLWRSPEEV RSDKSIFINQ GEWELLEVFP QFKEFSIDIS NSYAEMKFYV
IIRRRPLFYA VSLLLPSIFL MVVDIVGFCL PPDSGERVSF KITLLLGYSV FLIIVSDTLP
ATIGTPLIGV YFVVCMALLV ISLAETIFIV RLVHKQDLQR PVPDWLRHLV LDRIAWILCL
GEQPMAHRPP ATFQANKTDD CSGSDLLPAM GNHCSHVGGP QDLEKTPRGR GSPLPPPREA
SLAVRGLLQE LSSIRHFLEK RDEMREVARD WLRVGYVLDR LLFRIYLLAV LAYSITLVTL
WSIWHYS
