ID 5HT3B_HUMAN Reviewed; 441 AA. AC O95264; B0YJ23; Q0VJC3; DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 13-FEB-2019, entry version 151. DE RecName: Full=5-hydroxytryptamine receptor 3B; DE Short=5-HT3-B; DE Short=5-HT3B; DE AltName: Full=Serotonin receptor 3B; DE Flags: Precursor; GN Name=HTR3B; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY. RC TISSUE=Small intestine; RX PubMed=10521471; DOI=10.1074/jbc.274.43.30799; RA Dubin A.E., Huvar R., D'Andrea M.R., Pyati J., Zhu J.Y., Joy K.C., RA Wilson S.J., Galindo J.E., Glass C.A., Luo L., Jackson M.R., RA Lovenberg T.W., Erlander M.G.; RT "The pharmacological and functional characteristics of the serotonin RT 5-HT(3A) receptor are specifically modified by a 5-HT(3B) receptor RT subunit."; RL J. Biol. Chem. 274:30799-30810(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND RP SUBUNIT. RX PubMed=9950429; DOI=10.1038/16941; RA Davies P.A., Pistis M., Hanna M.C., Peters J.A., Lambert J.J., RA Hales T.G., Kirkness E.F.; RT "The 5-HT3B subunit is a major determinant of serotonin-receptor RT function."; RL Nature 397:359-363(1999). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT SER-129. RC TISSUE=Brain; RX PubMed=17010535; DOI=10.1016/j.gene.2006.08.002; RA Tzvetkov M.V., Meineke C., Oetjen E., Hirsch-Ernst K., Brockmoller J.; RT "Tissue-specific alternative promoters of the serotonin receptor gene RT HTR3B in human brain and intestine."; RL Gene 386:52-62(2007). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RG NHLBI resequencing and genotyping service (RS&G); RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] 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). RN [7] RP SUBUNIT. RX PubMed=17392525; DOI=10.1124/mol.106.032144; RA Niesler B., Walstab J., Combrink S., Moeller D., Kapeller J., RA Rietdorf J., Boenisch H., Goethert M., Rappold G., Bruess M.; RT "Characterization of the novel human serotonin receptor subunits 5- RT HT3C, 5-HT3D, and 5-HT3E."; RL Mol. Pharmacol. 72:8-17(2007). RN [8] RP SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-52; ASN-96; ASN-138; RP ASN-168 AND ASN-203, AND MUTAGENESIS OF ASN-52; ASN-96; ASN-138; RP ASN-168 AND ASN-203. RX PubMed=21138434; DOI=10.1111/j.1471-4159.2010.07129.x; RA Massoura A.N., Dover T.J., Newman A.S., Barnes N.M.; RT "The identification of N-glycosylated residues of the human 5-HT3B RT receptor subunit: importance for cell membrane expression."; RL J. Neurochem. 116:975-983(2011). RN [9] RP VARIANTS SER-129; ARG-156 AND ILE-183. RX PubMed=15389765; DOI=10.1002/ajmg.b.30070; RA Frank B., Niesler B., Noethen M.M., Neidt H., Propping P., Bondy B., RA Rietschel M., Maier W., Albus M., Rappold G.; RT "Investigation of the human serotonin receptor gene HTR3B in bipolar RT affective and schizophrenic patients."; RL Am. J. Med. Genet. B Neuropsychiatr. Genet. 131:1-5(2004). RN [10] RP VARIANTS SER-129; ARG-156 AND ILE-183. RX PubMed=15293096; DOI=10.1007/s10067-004-0927-2; RA Frank B., Niesler B., Bondy B., Spaeth M., Pongratz D.E., RA Ackenheil M., Fischer C., Rappold G.; RT "Mutational analysis of serotonin receptor genes: HTR3A and HTR3B in RT fibromyalgia patients."; RL Clin. Rheumatol. 23:338-344(2004). RN [11] RP VARIANTS SER-129; THR-143 AND ILE-183. RX PubMed=16487942; DOI=10.1016/j.biopsych.2005.11.008; RA Yamada K., Hattori E., Iwayama Y., Ohnishi T., Ohba H., Toyota T., RA Takao H., Minabe Y., Nakatani N., Higuchi T., Detera-Wadleigh S.D., RA Yoshikawa T.; RT "Distinguishable haplotype blocks in the HTR3A and HTR3B region in the RT Japanese reveal evidence of association of HTR3B with female major RT depression."; RL Biol. Psychiatry 60:192-201(2006). RN [12] RP VARIANT ARG-156. RX PubMed=21179162; DOI=10.1038/nature09629; RA Bevilacqua L., Doly S., Kaprio J., Yuan Q., Tikkanen R., Paunio T., RA Zhou Z., Wedenoja J., Maroteaux L., Diaz S., Belmer A., RA Hodgkinson C.A., Dell'osso L., Suvisaari J., Coccaro E., Rose R.J., RA Peltonen L., Virkkunen M., Goldman D.; RT "A population-specific HTR2B stop codon predisposes to severe RT impulsivity."; RL Nature 468:1061-1066(2010). 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. It is a cation-specific, but otherwise CC relatively nonselective, ion channel. CC {ECO:0000269|PubMed:12867984}. CC -!- SUBUNIT: Forms a pentaheteromeric complex with HTR3A. Not CC functional as a homomeric complex. {ECO:0000269|PubMed:17392525, CC ECO:0000269|PubMed:9950429}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21138434}; CC Multi-pass membrane protein {ECO:0000269|PubMed:21138434}. CC Note=Presumably retained within the endoplasmic reticulum unless CC complexed with HTR3A. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O95264-1; Sequence=Displayed; CC Name=2; CC IsoId=O95264-2; Sequence=VSP_029796; CC -!- TISSUE SPECIFICITY: Expressed in the brain cortex, in the caudate CC nucleus, the hyppocampus, the thalamus and the amygdala. Detected CC in the kidney and testis as well as in monocytes of the spleen, CC small and large intestine, uterus, prostate, ovary and placenta. CC {ECO:0000269|PubMed:10521471, ECO:0000269|PubMed:9950429}. CC -!- PTM: N-glycosylation required for membrane localization. CC {ECO:0000269|PubMed:21138434}. CC -!- MISCELLANEOUS: The HA-stretch region of HTR3B seems to confer CC increased conductance to HTR3A/HTR3B heteromers compared to that CC of HTR3A homomers. CC -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) CC family. 5-hydroxytryptamine receptor (TC 1.A.9.2) subfamily. HTR3B 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; AF169255; AAF03691.1; -; mRNA. DR EMBL; AF080582; AAD12242.1; -; mRNA. DR EMBL; AM293589; CAL25321.1; -; mRNA. DR EMBL; EF444985; ACA06001.1; -; Genomic_DNA. DR EMBL; AK314268; BAG36930.1; -; mRNA. DR CCDS; CCDS8364.1; -. [O95264-1] DR CCDS; CCDS86249.1; -. [O95264-2] DR RefSeq; NP_006019.1; NM_006028.4. [O95264-1] DR RefSeq; XP_011541365.1; XM_011543063.1. DR UniGene; Hs.241377; -. DR ProteinModelPortal; O95264; -. DR ComplexPortal; CPX-271; 5-hydroxytryptamine-3A/B receptor complex. DR IntAct; O95264; 1. DR STRING; 9606.ENSP00000260191; -. DR BindingDB; O95264; -. DR ChEMBL; CHEMBL2111332; -. DR DrugBank; DB01049; Ergoloid mesylate. DR DrugBank; DB00898; Ethanol. DR DrugBank; DB13025; Tiapride. DR GuidetoPHARMACOLOGY; 374; -. DR iPTMnet; O95264; -. DR PhosphoSitePlus; O95264; -. DR BioMuta; HTR3B; -. DR PaxDb; O95264; -. DR PeptideAtlas; O95264; -. DR PRIDE; O95264; -. DR ProteomicsDB; 50765; -. DR ProteomicsDB; 50766; -. [O95264-2] DR TopDownProteomics; O95264-1; -. [O95264-1] DR DNASU; 9177; -. DR Ensembl; ENST00000260191; ENSP00000260191; ENSG00000149305. [O95264-1] DR Ensembl; ENST00000537778; ENSP00000443118; ENSG00000149305. [O95264-2] DR GeneID; 9177; -. DR KEGG; hsa:9177; -. DR UCSC; uc001pok.4; human. [O95264-1] DR CTD; 9177; -. DR DisGeNET; 9177; -. DR EuPathDB; HostDB:ENSG00000149305.6; -. DR GeneCards; HTR3B; -. DR HGNC; HGNC:5298; HTR3B. DR HPA; HPA039559; -. DR MIM; 604654; gene. DR neXtProt; NX_O95264; -. DR OpenTargets; ENSG00000149305; -. DR PharmGKB; PA29556; -. DR eggNOG; KOG3645; Eukaryota. DR eggNOG; ENOG410XQGR; LUCA. DR GeneTree; ENSGT00940000158478; -. DR HOGENOM; HOG000241519; -. DR HOVERGEN; HBG106638; -. DR InParanoid; O95264; -. DR KO; K04819; -. DR OMA; VFRVNMS; -. DR OrthoDB; 1444868at2759; -. DR PhylomeDB; O95264; -. DR TreeFam; TF315605; -. DR Reactome; R-HSA-112314; Neurotransmitter receptors and postsynaptic signal transmission. DR ChiTaRS; HTR3B; human. DR GeneWiki; HTR3B; -. DR GenomeRNAi; 9177; -. DR PRO; PR:O95264; -. DR Proteomes; UP000005640; Chromosome 11. DR Bgee; ENSG00000149305; Expressed in 35 organ(s), highest expression level in right frontal lobe. DR ExpressionAtlas; O95264; baseline and differential. DR Genevisible; O95264; HS. DR GO; GO:0009986; C:cell surface; IDA:CACAO. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0043005; C:neuron projection; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0045211; C:postsynaptic membrane; IEA:InterPro. DR GO; GO:1904602; C:serotonin-activated cation-selective channel complex; IGI:GO_Central. DR GO; GO:0045202; C:synapse; IBA:GO_Central. DR GO; GO:0022850; F:serotonin-gated cation-selective channel activity; IGI:GO_Central. DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro. DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central. 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:0042391; P:regulation of membrane potential; IBA:GO_Central. DR GO; GO:0007165; P:signal transduction; IBA:GO_Central. DR Gene3D; 2.70.170.10; -; 1. DR InterPro; IPR008132; 5HT3_rcpt. DR InterPro; IPR008134; 5HT3_rcpt_B. 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; IPR006029; Neurotrans-gated_channel_TM. DR PANTHER; PTHR18945; PTHR18945; 1. DR Pfam; PF02931; Neur_chan_LBD; 1. DR Pfam; PF02932; Neur_chan_memb; 1. DR PRINTS; PR01710; 5HT3BRECEPTR. DR PRINTS; PR01708; 5HT3RECEPTOR. DR PRINTS; PR00252; NRIONCHANNEL. DR SUPFAM; SSF63712; SSF63712; 1. DR SUPFAM; SSF90112; SSF90112; 1. DR TIGRFAMs; TIGR00860; LIC; 1. PE 1: Evidence at protein level; KW Alternative splicing; Cell membrane; Complete proteome; KW Disulfide bond; Glycoprotein; Ion channel; Ion transport; KW Ligand-gated ion channel; Membrane; Polymorphism; Receptor; KW Reference proteome; Signal; Transmembrane; Transmembrane helix; KW Transport. FT SIGNAL 1 21 {ECO:0000255}. FT CHAIN 22 441 5-hydroxytryptamine receptor 3B. FT /FTId=PRO_0000312289. FT TOPO_DOM 22 238 Extracellular. {ECO:0000255}. FT TRANSMEM 239 259 Helical; Name=1. {ECO:0000255}. FT TOPO_DOM 260 268 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 269 286 Helical; Name=2. {ECO:0000255}. FT TOPO_DOM 287 303 Extracellular. {ECO:0000255}. FT TRANSMEM 304 324 Helical; Name=3. {ECO:0000255}. FT TOPO_DOM 325 414 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 415 435 Helical; Name=4. {ECO:0000255}. FT TOPO_DOM 436 441 Extracellular. {ECO:0000255}. FT REGION 381 413 HA-stretch. FT CARBOHYD 52 52 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:21138434}. FT CARBOHYD 96 96 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:21138434}. FT CARBOHYD 138 138 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:21138434}. FT CARBOHYD 168 168 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:21138434}. FT CARBOHYD 203 203 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:21138434}. FT CARBOHYD 287 287 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 155 169 {ECO:0000250}. FT VAR_SEQ 1 17 MLSSVMAPLWACILVAA -> MIVYFP (in isoform FT 2). {ECO:0000303|PubMed:17010535}. FT /FTId=VSP_029796. FT VARIANT 129 129 Y -> S (in dbSNP:rs1176744). FT {ECO:0000269|PubMed:15293096, FT ECO:0000269|PubMed:15389765, FT ECO:0000269|PubMed:16487942, FT ECO:0000269|PubMed:17010535}. FT /FTId=VAR_037472. FT VARIANT 143 143 I -> T (in dbSNP:rs34550504). FT {ECO:0000269|PubMed:16487942}. FT /FTId=VAR_037473. FT VARIANT 156 156 S -> R (in dbSNP:rs72466469). FT {ECO:0000269|PubMed:15293096, FT ECO:0000269|PubMed:15389765, FT ECO:0000269|PubMed:21179162}. FT /FTId=VAR_037474. FT VARIANT 183 183 V -> I (in dbSNP:rs17116138). FT {ECO:0000269|PubMed:15293096, FT ECO:0000269|PubMed:15389765, FT ECO:0000269|PubMed:16487942}. FT /FTId=VAR_037475. FT MUTAGEN 52 52 N->S: Reduced molecular weight. Very FT little expression in the cell membrane. FT {ECO:0000269|PubMed:21138434}. FT MUTAGEN 96 96 N->S: Reduced molecular weight. Very FT little expression in the cell membrane. FT {ECO:0000269|PubMed:21138434}. FT MUTAGEN 138 138 N->S: Reduced molecular weight. Very FT little expression in the cell membrane. FT {ECO:0000269|PubMed:21138434}. FT MUTAGEN 168 168 N->S: Reduced molecular weight and cell FT membrane expression. FT {ECO:0000269|PubMed:21138434}. FT MUTAGEN 203 203 N->S: Reduced molecular weight. Very FT little expression in the cell membrane. FT {ECO:0000269|PubMed:21138434}. SQ SEQUENCE 441 AA; 50292 MW; 2ED59E4E11400648 CRC64; MLSSVMAPLW ACILVAAGIL ATDTHHPQDS ALYHLSKQLL QKYHKEVRPV YNWTKATTVY LDLFVHAILD VDAENQILKT SVWYQEVWND EFLSWNSSMF DEIREISLPL SAIWAPDIII NEFVDIERYP DLPYVYVNSS GTIENYKPIQ VVSACSLETY AFPFDVQNCS LTFKSILHTV EDVDLAFLRS PEDIQHDKKA FLNDSEWELL SVSSTYSILQ SSAGGFAQIQ FNVVMRRHPL VYVVSLLIPS IFLMLVDLGS FYLPPNCRAR IVFKTSVLVG YTVFRVNMSN QVPRSVGSTP LIGHFFTICM AFLVLSLAKS IVLVKFLHDE QRGGQEQPFL CLRGDTDADR PRVEPRAQRA VVTESSLYGE HLAQPGTLKE VWSQLQSISN YLQTQDQTDQ QEAEWLVLLS RFDRLLFQSY LFMLGIYTIT LCSLWALWGG V //