5HT3B_MOUSE
ID 5HT3B_MOUSE Reviewed; 437 AA.
AC Q9JHJ5;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 154.
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 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 [GENOMIC DNA / MRNA].
RC STRAIN=129/SvJ, and BALB/cJ;
RX PubMed=10854267; DOI=10.1046/j.1471-4159.2000.0750240.x;
RA Hanna M.C., Davies P.A., Hales T.G., Kirkness E.F.;
RT "Evidence for expression of heteromeric serotonin 5-HT(3) receptors in
RT rodents.";
RL J. Neurochem. 75:240-247(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Stomach;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Olfactory epithelium;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION.
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. It is a cation-specific, but otherwise relatively
CC nonselective, ion channel. {ECO:0000269|PubMed:12867984}.
CC -!- SUBUNIT: Forms a pentaheteromeric complex with HTR3A. Not functional as
CC a homomeric complex (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC Note=Presumably retained within the endoplasmic reticulum unless
CC complexed with HTR3A. {ECO:0000250}.
CC -!- PTM: N-glycosylation is required for membrane localization.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC 5-hydroxytryptamine receptor (TC 1.A.9.2) subfamily. HTR3B sub-
CC subfamily. {ECO:0000305}.
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DR EMBL; AF155045; AAF73284.1; -; mRNA.
DR EMBL; AF155052; AAF73285.1; -; Genomic_DNA.
DR EMBL; AF155046; AAF73285.1; JOINED; Genomic_DNA.
DR EMBL; AF155047; AAF73285.1; JOINED; Genomic_DNA.
DR EMBL; AF155048; AAF73285.1; JOINED; Genomic_DNA.
DR EMBL; AF155049; AAF73285.1; JOINED; Genomic_DNA.
DR EMBL; AF155050; AAF73285.1; JOINED; Genomic_DNA.
DR EMBL; AF155051; AAF73285.1; JOINED; Genomic_DNA.
DR EMBL; AK085213; BAC39391.1; -; mRNA.
DR EMBL; BC046990; AAH46990.1; -; mRNA.
DR CCDS; CCDS23160.1; -.
DR RefSeq; NP_064670.1; NM_020274.4.
DR AlphaFoldDB; Q9JHJ5; -.
DR SMR; Q9JHJ5; -.
DR BioGRID; 208209; 1.
DR ComplexPortal; CPX-275; 5-hydroxytryptamine-3A/B receptor complex.
DR IntAct; Q9JHJ5; 1.
DR STRING; 10090.ENSMUSP00000008734; -.
DR BindingDB; Q9JHJ5; -.
DR ChEMBL; CHEMBL3781; -.
DR DrugCentral; Q9JHJ5; -.
DR GuidetoPHARMACOLOGY; 374; -.
DR GlyGen; Q9JHJ5; 4 sites.
DR iPTMnet; Q9JHJ5; -.
DR PhosphoSitePlus; Q9JHJ5; -.
DR PaxDb; Q9JHJ5; -.
DR PRIDE; Q9JHJ5; -.
DR ProteomicsDB; 296451; -.
DR Antibodypedia; 18362; 180 antibodies from 30 providers.
DR DNASU; 57014; -.
DR Ensembl; ENSMUST00000008734; ENSMUSP00000008734; ENSMUSG00000008590.
DR GeneID; 57014; -.
DR KEGG; mmu:57014; -.
DR UCSC; uc012gsr.1; mouse.
DR CTD; 9177; -.
DR MGI; MGI:1861899; Htr3b.
DR VEuPathDB; HostDB:ENSMUSG00000008590; -.
DR eggNOG; KOG3645; Eukaryota.
DR GeneTree; ENSGT00940000158478; -.
DR HOGENOM; CLU_018074_5_0_1; -.
DR InParanoid; Q9JHJ5; -.
DR OMA; FRSYLFM; -.
DR OrthoDB; 611108at2759; -.
DR PhylomeDB; Q9JHJ5; -.
DR TreeFam; TF315605; -.
DR Reactome; R-MMU-112314; Neurotransmitter receptors and postsynaptic signal transmission.
DR BioGRID-ORCS; 57014; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Htr3b; mouse.
DR PRO; PR:Q9JHJ5; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9JHJ5; protein.
DR Bgee; ENSMUSG00000008590; Expressed in lumbar dorsal root ganglion and 16 other tissues.
DR Genevisible; Q9JHJ5; MM.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:InterPro.
DR GO; GO:1904602; C:serotonin-activated cation-selective channel complex; ISO:MGI.
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:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0022850; F:serotonin-gated cation-selective channel activity; IDA: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; 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; IPR038050; Neuro_actylchol_rec.
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 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW Ligand-gated ion channel; Membrane; Receptor; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..437
FT /note="5-hydroxytryptamine receptor 3B"
FT /id="PRO_0000312290"
FT TOPO_DOM 22..238
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..264
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..282
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 283..292
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 314..410
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 411..431
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 432..437
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 377..409
FT /note="HA-stretch"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 151..165
FT /evidence="ECO:0000250"
SQ SEQUENCE 437 AA; 50321 MW; 60019008AF23F0FC CRC64;
MILLWSCLLV AVVGILGTAT PQPGNSSLHR LTRQLLQQYH KEVRPVYNWA EATTVYLDLC
VHAVLDVDVQ NQKLKTSVWY REVWNDEFLS WNSSLFDEIQ EISLPLSALW APDIIINEFV
DVERSPDLPY VYVNSSGTIR NHKPIQVVSA CSLQTYAFPF DIQNCSLTFN SILHTVEDID
LGFLRNREDI ENDKRAFMND SEWQLLSVSS TYHIRQSSAG DFAQIRFNVV IRRCPLAYVV
SLLIPSIFLM LVDLGSFYLP PNCRARIVFK TNVLVGYTVF RVNMSDEVPR SAGCTPLIGV
FFTVCMALLV LSLSKSILLI KFLYEERHSG QERPLMCLQG DSDAEESRLY LGAPRADVTE
SPVHQEHRVP SDTLKDFWFQ FRSINNSLRT RDQIHQKEVE WLAILYRFDQ LLFRIYLAVL
GLYTVTLCSL WALWSRM
