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 22-JUL-2015, entry version 134. 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; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; 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/c; 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 RT human 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 RT the 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 RT expression of 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 CC as a neurotransmitter, a hormone, and a mitogen. This receptor is CC a ligand-gated ion channel, which when activated causes fast, CC depolarizing responses in neurons. It is a cation-specific, but CC otherwise relatively nonselective, ion channel. CC {ECO:0000269|PubMed:12867984}. CC -!- SUBUNIT: Forms pentahomomeric complex as well as pentaheteromeric CC complex with HTR3B; homomeric complex is functional but exhibits CC low conductance with modified voltage dependence, and decreased CC agonist and antagonist affinity. Interacts with RIC3 (By CC similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell CC membrane; Multi-pass membrane protein. Cell membrane; Multi-pass CC 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 CC responsible for the low conductance of HTR3A homomers compared to CC that of HTR3A/HTR3B heteromers. CC -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) CC family. 5-hydroxytryptamine receptor (TC 1.A.9.2) subfamily. HTR3A CC sub-subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 UniGene; Mm.4831; -. DR PDB; 4PIR; X-ray; 3.50 A; A/B/C/D/E=32-485. DR PDBsum; 4PIR; -. DR ProteinModelPortal; P23979; -. DR SMR; P23979; 34-360. DR DIP; DIP-48769N; -. DR STRING; 10090.ENSMUSP00000003826; -. DR BindingDB; P23979; -. DR ChEMBL; CHEMBL4972; -. DR GuidetoPHARMACOLOGY; 373; -. DR PhosphoSite; P23979; -. DR MaxQB; P23979; -. DR PRIDE; P23979; -. DR GeneID; 15561; -. DR CTD; 3359; -. DR MGI; MGI:96282; Htr3a. DR eggNOG; NOG302526; -. DR HOGENOM; HOG000241519; -. DR HOVERGEN; HBG106638; -. DR InParanoid; P23979; -. DR PhylomeDB; P23979; -. DR NextBio; 288512; -. DR PRO; PR:P23979; -. DR Proteomes; UP000000589; Unplaced. DR CleanEx; MM_HTR3A; -. DR Genevisible; P23979; MM. DR GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. 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:0051378; F:serotonin binding; ISO:MGI. DR GO; GO:0004993; F:serotonin receptor activity; ISO:MGI. DR GO; GO:0007210; P:serotonin receptor signaling pathway; ISO:MGI. DR Gene3D; 1.20.120.370; -; 2. DR Gene3D; 2.70.170.10; -; 1. DR InterPro; IPR008132; 5HT3_rcpt. DR InterPro; IPR008133; 5HT3_rcpt_A. DR InterPro; IPR027361; Acetylcholine_rcpt_TM. DR InterPro; IPR006202; Neur_chan_lig-bd. DR InterPro; IPR006201; Neur_channel. 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 junction; Cell membrane; KW Complete proteome; Disulfide bond; Glycoprotein; Ion channel; KW Ion transport; Ligand-gated ion channel; Membrane; KW Postsynaptic cell membrane; Receptor; Reference proteome; Signal; KW Synapse; Transmembrane; Transmembrane helix; Transport. FT SIGNAL 1 23 {ECO:0000255}. FT CHAIN 24 487 5-hydroxytryptamine receptor 3A. FT /FTId=PRO_0000000409. FT TOPO_DOM 24 245 Extracellular. {ECO:0000255}. FT TRANSMEM 246 272 Helical; Name=1. {ECO:0000255}. FT TOPO_DOM 273 277 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 278 296 Helical; Name=2. {ECO:0000255}. FT TOPO_DOM 297 305 Extracellular. {ECO:0000255}. FT TRANSMEM 306 324 Helical; Name=3. {ECO:0000255}. FT TOPO_DOM 325 464 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 465 484 Helical; Name=4. {ECO:0000255}. FT TOPO_DOM 485 487 Extracellular. {ECO:0000255}. FT REGION 423 459 HA-stretch. FT CARBOHYD 108 108 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 174 174 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 190 190 N-linked (GlcNAc...). {ECO:0000255}. FT DISULFID 161 175 {ECO:0000250}. FT VAR_SEQ 383 388 Missing (in isoform 5-HT3R-AS). FT {ECO:0000305}. FT /FTId=VSP_000079. FT CONFLICT 31 31 E -> AR (in Ref. 3; CAA51089 and 4; FT CAA55870/CAA55871). {ECO:0000305}. FT CONFLICT 74 74 I -> V (in Ref. 3; CAA51089). FT {ECO:0000305}. FT CONFLICT 302 302 T -> TA (in Ref. 3; CAA51089 and 4; FT CAA55870/CAA55871). {ECO:0000305}. FT CONFLICT 384 384 S -> SS (in Ref. 2; CAA80453). FT {ECO:0000305}. FT CONFLICT 393 393 H -> T (in Ref. 4; CAA55870/CAA55871). FT {ECO:0000305}. FT HELIX 38 46 {ECO:0000244|PDB:4PIR}. FT STRAND 63 78 {ECO:0000244|PDB:4PIR}. FT TURN 79 82 {ECO:0000244|PDB:4PIR}. FT STRAND 83 95 {ECO:0000244|PDB:4PIR}. FT STRAND 106 108 {ECO:0000244|PDB:4PIR}. FT STRAND 111 115 {ECO:0000244|PDB:4PIR}. FT HELIX 116 118 {ECO:0000244|PDB:4PIR}. FT STRAND 124 126 {ECO:0000244|PDB:4PIR}. FT STRAND 129 131 {ECO:0000244|PDB:4PIR}. FT STRAND 140 144 {ECO:0000244|PDB:4PIR}. FT STRAND 148 160 {ECO:0000244|PDB:4PIR}. FT STRAND 166 168 {ECO:0000244|PDB:4PIR}. FT STRAND 172 183 {ECO:0000244|PDB:4PIR}. FT TURN 186 188 {ECO:0000244|PDB:4PIR}. FT STRAND 189 195 {ECO:0000244|PDB:4PIR}. FT HELIX 197 202 {ECO:0000244|PDB:4PIR}. FT STRAND 210 225 {ECO:0000244|PDB:4PIR}. FT STRAND 227 230 {ECO:0000244|PDB:4PIR}. FT STRAND 233 244 {ECO:0000244|PDB:4PIR}. FT HELIX 248 268 {ECO:0000244|PDB:4PIR}. FT TURN 272 274 {ECO:0000244|PDB:4PIR}. FT HELIX 276 294 {ECO:0000244|PDB:4PIR}. FT HELIX 310 332 {ECO:0000244|PDB:4PIR}. FT HELIX 343 349 {ECO:0000244|PDB:4PIR}. FT HELIX 352 358 {ECO:0000244|PDB:4PIR}. FT HELIX 428 482 {ECO:0000244|PDB:4PIR}. 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 //