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5HT3A_HUMAN
ID   5HT3A_HUMAN             Reviewed;         478 AA.
AC   P46098; B4DSY6; G5E986; O60854; Q7KZM7; Q99918; Q9BSZ9;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 212.
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   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Hippocampus;
RX   PubMed=7565620;
RA   Miyake A., Mochizuki S., Takemoto Y., Akuzawa S.;
RT   "Molecular cloning of human 5-hydroxytryptamine3 receptor: heterogeneity in
RT   distribution and function among species.";
RL   Mol. Pharmacol. 48:407-416(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Amygdala;
RX   PubMed=8848005;
RA   Belelli D., Balcarek J.M., Hope A.G., Peters J.A., Lambert J.J.,
RA   Blackburn T.P.;
RT   "Cloning and functional expression of a human 5-hydroxytryptamine type 3AS
RT   receptor subunit.";
RL   Mol. Pharmacol. 48:1054-1062(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Amygdala, and Hippocampus;
RX   PubMed=9928262; DOI=10.1111/j.1749-6632.1998.tb10196.x;
RA   Bruess M., Goethert M., Hayer M., Bonisch H.;
RT   "Molecular cloning of alternatively spliced human 5HT3 receptor cDNAs.";
RL   Ann. N. Y. Acad. Sci. 861:234-235(1998).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Blood;
RX   PubMed=10670426; DOI=10.1016/s0028-3908(99)00116-1;
RA   Bruess M., Eucker T., Goethert M., Bonisch H.;
RT   "Exon-intron organization of the human 5-HT3A receptor gene.";
RL   Neuropharmacology 39:308-315(2000).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT   "cDNA clones of human proteins involved in signal transduction sequenced by
RT   the Guthrie cDNA resource center (www.cdna.org).";
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RX   PubMed=15028279; DOI=10.1016/j.ygeno.2003.09.023;
RA   Jin P., Fu G.K., Wilson A.D., Yang J., Chien D., Hawkins P.R., Au-Young J.,
RA   Stuve L.L.;
RT   "PCR isolation and cloning of novel splice variant mRNAs from known drug
RT   target genes.";
RL   Genomics 83:566-571(2004).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., 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., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   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   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA   Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA   Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA   Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA   Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [11]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Lung;
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   [12]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=9950429; DOI=10.1038/16941;
RA   Davies P.A., Pistis M., Hanna M.C., Peters J.A., Lambert J.J., Hales T.G.,
RA   Kirkness E.F.;
RT   "The 5-HT3B subunit is a major determinant of serotonin-receptor
RT   function.";
RL   Nature 397:359-363(1999).
RN   [13]
RP   SUBUNIT, 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 5-
RT   HT(3A) receptor are specifically modified by a 5-HT(3B) receptor subunit.";
RL   J. Biol. Chem. 274:30799-30810(1999).
RN   [14]
RP   FUNCTION, REGION, AND MUTAGENESIS OF ARG-432; ARG-436 AND ARG-440.
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   [15]
RP   INTERACTION WITH RIC3.
RX   PubMed=15809299; DOI=10.1074/jbc.m414341200;
RA   Cheng A., McDonald N.A., Connolly C.N.;
RT   "Cell surface expression of 5-hydroxytryptamine type 3 receptors is
RT   promoted by RIC-3.";
RL   J. Biol. Chem. 280:22502-22507(2005).
RN   [16]
RP   SUBUNIT, AND MUTAGENESIS OF TRP-178.
RX   PubMed=17392525; DOI=10.1124/mol.106.032144;
RA   Niesler B., Walstab J., Combrink S., Moeller D., Kapeller J., Rietdorf J.,
RA   Boenisch H., Goethert M., Rappold G., Bruess M.;
RT   "Characterization of the novel human serotonin receptor subunits 5-HT3C, 5-
RT   HT3D, and 5-HT3E.";
RL   Mol. Pharmacol. 72:8-17(2007).
RN   [17]
RP   VARIANT THR-33.
RX   PubMed=15293096; DOI=10.1007/s10067-004-0927-2;
RA   Frank B., Niesler B., Bondy B., Spaeth M., Pongratz D.E., Ackenheil M.,
RA   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   [18]
RP   VARIANTS HIS-344; ARG-391 AND GLN-409.
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).
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       ECO:0000269|PubMed:9950429}.
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. {ECO:0000269|PubMed:10521471, ECO:0000269|PubMed:15809299,
CC       ECO:0000269|PubMed:17392525, ECO:0000269|PubMed:9950429}.
CC   -!- INTERACTION:
CC       P46098; Q8WXA8: HTR3C; NbExp=5; IntAct=EBI-9008743, EBI-9008753;
CC       P46098; Q70Z44: HTR3D; NbExp=5; IntAct=EBI-9008743, EBI-9008717;
CC       P46098; A5X5Y0-1: HTR3E; NbExp=5; IntAct=EBI-9008743, EBI-11174612;
CC       P46098; A5X5Y0-3: HTR3E; NbExp=3; IntAct=EBI-9008743, EBI-11163690;
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=5;
CC       Name=1; Synonyms=5-HT3R-AS;
CC         IsoId=P46098-1; Sequence=Displayed;
CC       Name=2; Synonyms=5-HT3R-AL;
CC         IsoId=P46098-2; Sequence=VSP_000078;
CC       Name=3;
CC         IsoId=P46098-3; Sequence=VSP_042214;
CC       Name=4;
CC         IsoId=P46098-4; Sequence=VSP_043484;
CC       Name=5;
CC         IsoId=P46098-5; Sequence=VSP_043484, VSP_000078;
CC   -!- TISSUE SPECIFICITY: Expressed in cerebral cortex, amygdala,
CC       hippocampus, and testis. Detected in monocytes of the spleen and
CC       tonsil, in small and large intestine, uterus, prostate, ovary and
CC       placenta. {ECO:0000269|PubMed:10521471}.
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; D49394; BAA08387.1; -; mRNA.
DR   EMBL; S82612; AAB37533.2; -; mRNA.
DR   EMBL; AJ003078; CAA05851.1; -; mRNA.
DR   EMBL; AJ003079; CAA05852.1; -; mRNA.
DR   EMBL; AJ005205; CAA06442.3; -; Genomic_DNA.
DR   EMBL; AF498984; AAM21131.1; -; mRNA.
DR   EMBL; BT007204; AAP35868.1; -; mRNA.
DR   EMBL; CD014118; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK299973; BAG61798.1; -; mRNA.
DR   EMBL; AP000908; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471065; EAW67238.1; -; Genomic_DNA.
DR   EMBL; CH471065; EAW67240.1; -; Genomic_DNA.
DR   EMBL; BC002354; AAH02354.1; -; mRNA.
DR   EMBL; BC004453; AAH04453.2; -; mRNA.
DR   CCDS; CCDS53710.1; -. [P46098-3]
DR   CCDS; CCDS8365.2; -. [P46098-1]
DR   CCDS; CCDS8366.2; -. [P46098-2]
DR   RefSeq; NP_000860.2; NM_000869.5. [P46098-1]
DR   RefSeq; NP_001155244.1; NM_001161772.2. [P46098-3]
DR   RefSeq; NP_998786.2; NM_213621.3. [P46098-2]
DR   AlphaFoldDB; P46098; -.
DR   SMR; P46098; -.
DR   BioGRID; 109591; 118.
DR   ComplexPortal; CPX-2175; 5-hydroxytryptamine-3A receptor complex.
DR   ComplexPortal; CPX-271; 5-hydroxytryptamine-3A/B receptor complex.
DR   ComplexPortal; CPX-272; 5-hydroxytryptamine-3A/D receptor complex.
DR   ComplexPortal; CPX-273; 5-hydroxytryptamine-3A/E receptor complex.
DR   ComplexPortal; CPX-276; 5-hydroxytryptamine-3A/C receptor complex.
DR   IntAct; P46098; 101.
DR   STRING; 9606.ENSP00000347754; -.
DR   BindingDB; P46098; -.
DR   ChEMBL; CHEMBL1899; -.
DR   DrugBank; DB00969; Alosetron.
DR   DrugBank; DB00543; Amoxapine.
DR   DrugBank; DB01238; Aripiprazole.
DR   DrugBank; DB14185; Aripiprazole lauroxil.
DR   DrugBank; DB01156; Bupropion.
DR   DrugBank; DB09061; Cannabidiol.
DR   DrugBank; DB01239; Chlorprothixene.
DR   DrugBank; DB04885; Cilansetron.
DR   DrugBank; DB00604; Cisapride.
DR   DrugBank; DB00363; Clozapine.
DR   DrugBank; DB05642; DDP-225.
DR   DrugBank; DB05049; DDP733.
DR   DrugBank; DB11273; Dihydroergocornine.
DR   DrugBank; DB13345; Dihydroergocristine.
DR   DrugBank; DB00757; Dolasetron.
DR   DrugBank; DB00988; Dopamine.
DR   DrugBank; DB01049; Ergoloid mesylate.
DR   DrugBank; DB00898; Ethanol.
DR   DrugBank; DB12141; Gilteritinib.
DR   DrugBank; DB00889; Granisetron.
DR   DrugBank; DB01221; Ketamine.
DR   DrugBank; DB00555; Lamotrigine.
DR   DrugBank; DB00408; Loxapine.
DR   DrugBank; DB01043; Memantine.
DR   DrugBank; DB00333; Methadone.
DR   DrugBank; DB01233; Metoclopramide.
DR   DrugBank; DB00334; Olanzapine.
DR   DrugBank; DB00904; Ondansetron.
DR   DrugBank; DB00377; Palonosetron.
DR   DrugBank; DB00715; Paroxetine.
DR   DrugBank; DB00721; Procaine.
DR   DrugBank; DB01224; Quetiapine.
DR   DrugBank; DB09290; Ramosetron.
DR   DrugBank; DB04917; Renzapride.
DR   DrugBank; DB00728; Rocuronium.
DR   DrugBank; DB08839; Serotonin.
DR   DrugBank; DB09304; Setiptiline.
DR   DrugBank; DB06204; Tapentadol.
DR   DrugBank; DB13025; Tiapride.
DR   DrugBank; DB06422; Ticalopride.
DR   DrugBank; DB00726; Trimipramine.
DR   DrugBank; DB11699; Tropisetron.
DR   DrugBank; DB01199; Tubocurarine.
DR   DrugBank; DB09068; Vortioxetine.
DR   DrugBank; DB00246; Ziprasidone.
DR   DrugCentral; P46098; -.
DR   GuidetoPHARMACOLOGY; 373; -.
DR   TCDB; 1.A.9.2.1; the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family.
DR   GlyGen; P46098; 4 sites.
DR   iPTMnet; P46098; -.
DR   PhosphoSitePlus; P46098; -.
DR   BioMuta; HTR3A; -.
DR   DMDM; 1168222; -.
DR   MassIVE; P46098; -.
DR   PeptideAtlas; P46098; -.
DR   PRIDE; P46098; -.
DR   Antibodypedia; 18364; 425 antibodies from 36 providers.
DR   DNASU; 3359; -.
DR   Ensembl; ENST00000299961.5; ENSP00000299961.4; ENSG00000166736.12. [P46098-3]
DR   Ensembl; ENST00000355556.6; ENSP00000347754.2; ENSG00000166736.12. [P46098-5]
DR   Ensembl; ENST00000375498.6; ENSP00000364648.2; ENSG00000166736.12. [P46098-4]
DR   Ensembl; ENST00000504030.7; ENSP00000424189.2; ENSG00000166736.12. [P46098-1]
DR   Ensembl; ENST00000506841.6; ENSP00000424776.2; ENSG00000166736.12. [P46098-2]
DR   GeneID; 3359; -.
DR   KEGG; hsa:3359; -.
DR   MANE-Select; ENST00000504030.7; ENSP00000424189.2; NM_000869.6; NP_000860.3.
DR   UCSC; uc010rxa.3; human. [P46098-1]
DR   CTD; 3359; -.
DR   DisGeNET; 3359; -.
DR   GeneCards; HTR3A; -.
DR   HGNC; HGNC:5297; HTR3A.
DR   HPA; ENSG00000166736; Tissue enhanced (lymphoid tissue, pancreas, salivary gland).
DR   MIM; 182139; gene.
DR   neXtProt; NX_P46098; -.
DR   OpenTargets; ENSG00000166736; -.
DR   PharmGKB; PA29555; -.
DR   VEuPathDB; HostDB:ENSG00000166736; -.
DR   eggNOG; KOG3645; Eukaryota.
DR   GeneTree; ENSGT00940000157705; -.
DR   HOGENOM; CLU_018074_5_0_1; -.
DR   InParanoid; P46098; -.
DR   OMA; FLMLMDI; -.
DR   PhylomeDB; P46098; -.
DR   TreeFam; TF315605; -.
DR   PathwayCommons; P46098; -.
DR   Reactome; R-HSA-112314; Neurotransmitter receptors and postsynaptic signal transmission.
DR   SignaLink; P46098; -.
DR   SIGNOR; P46098; -.
DR   BioGRID-ORCS; 3359; 7 hits in 1071 CRISPR screens.
DR   GeneWiki; HTR3A; -.
DR   GenomeRNAi; 3359; -.
DR   Pharos; P46098; Tclin.
DR   PRO; PR:P46098; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; P46098; protein.
DR   Bgee; ENSG00000166736; Expressed in dorsal root ganglion and 92 other tissues.
DR   ExpressionAtlas; P46098; baseline and differential.
DR   Genevisible; P46098; HS.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0032154; C:cleavage furrow; IDA:HGNC.
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:UniProtKB-SubCell.
DR   GO; GO:1904602; C:serotonin-activated cation-selective channel complex; IDA:GO_Central.
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:0051378; F:serotonin binding; IDA:MGI.
DR   GO; GO:0022850; F:serotonin-gated cation-selective channel activity; IDA:GO_Central.
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; IDA:ComplexPortal.
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:0007210; P:serotonin receptor signaling pathway; IDA:ComplexPortal.
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   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..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..478
FT                   /note="5-hydroxytryptamine receptor 3A"
FT                   /id="PRO_0000000408"
FT   TOPO_DOM        24..241
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        242..268
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        269..273
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        274..292
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        293..302
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        303..321
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        322..455
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        456..475
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        476..478
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   REGION          389..408
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          414..450
FT                   /note="HA-stretch"
FT   CARBOHYD        28
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        104
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        170
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        186
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        157..171
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         1..22
FT                   /note="MLLWVQQALLALLLPTLLAQGE -> MHRSFLQ (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_042214"
FT   VAR_SEQ         1
FT                   /note="M -> MLGKLAM (in isoform 4 and isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:15028279, ECO:0000303|Ref.6"
FT                   /id="VSP_043484"
FT   VAR_SEQ         306
FT                   /note="G -> GKAPPGSRAQSGEKPAPSHLLHVSLASALGCTG (in isoform 2
FT                   and isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:15028279,
FT                   ECO:0000303|PubMed:9928262"
FT                   /id="VSP_000078"
FT   VARIANT         33
FT                   /note="A -> T (in dbSNP:rs117793058)"
FT                   /evidence="ECO:0000269|PubMed:15293096"
FT                   /id="VAR_037398"
FT   VARIANT         253
FT                   /note="S -> N (in dbSNP:rs4938063)"
FT                   /id="VAR_037399"
FT   VARIANT         344
FT                   /note="R -> H (in dbSNP:rs35815285)"
FT                   /evidence="ECO:0000269|PubMed:16487942"
FT                   /id="VAR_037400"
FT   VARIANT         391
FT                   /note="P -> R"
FT                   /evidence="ECO:0000269|PubMed:16487942"
FT                   /id="VAR_037401"
FT   VARIANT         409
FT                   /note="R -> Q (in dbSNP:rs183698487)"
FT                   /evidence="ECO:0000269|PubMed:16487942"
FT                   /id="VAR_037402"
FT   MUTAGEN         178
FT                   /note="W->S: Abolished ligand binding to the heteromeric
FT                   receptor."
FT                   /evidence="ECO:0000269|PubMed:17392525"
FT   MUTAGEN         432
FT                   /note="R->Q: Little effect on conductance. Massive increase
FT                   of conductance; when associated with D-436 and A-440."
FT                   /evidence="ECO:0000269|PubMed:12867984"
FT   MUTAGEN         436
FT                   /note="R->D: Increased conductance. Massive increase of
FT                   conductance; when associated with Q-432 and A-440."
FT                   /evidence="ECO:0000269|PubMed:12867984"
FT   MUTAGEN         440
FT                   /note="R->A: Increased conductance. Massive increase of
FT                   conductance; when associated with Q-432 and D-436."
FT                   /evidence="ECO:0000269|PubMed:12867984"
FT   CONFLICT        46
FT                   /note="R -> T (in Ref. 2; AAB37533)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        125
FT                   /note="F -> L (in Ref. 2; AAB37533)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        321
FT                   /note="A -> T (in Ref. 2; AAB37533)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        386
FT                   /note="S -> T (in Ref. 2; AAB37533)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        P46098-5:342
FT                   /note="C -> W (in Ref. 7; CD014118)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   478 AA;  55280 MW;  24CA9A232286FBC9 CRC64;
     MLLWVQQALL ALLLPTLLAQ GEARRSRNTT RPALLRLSDY LLTNYRKGVR PVRDWRKPTT
     VSIDVIVYAI LNVDEKNQVL TTYIWYRQYW TDEFLQWNPE DFDNITKLSI PTDSIWVPDI
     LINEFVDVGK SPNIPYVYIR HQGEVQNYKP LQVVTACSLD IYNFPFDVQN CSLTFTSWLH
     TIQDINISLW RLPEKVKSDR SVFMNQGEWE LLGVLPYFRE FSMESSNYYA EMKFYVVIRR
     RPLFYVVSLL LPSIFLMVMD IVGFYLPPNS GERVSFKITL LLGYSVFLII VSDTLPATAI
     GTPLIGVYFV VCMALLVISL AETIFIVRLV HKQDLQQPVP AWLRHLVLER IAWLLCLREQ
     STSQRPPATS QATKTDDCSA MGNHCSHMGG PQDFEKSPRD RCSPPPPPRE ASLAVCGLLQ
     ELSSIRQFLE KRDEIREVAR DWLRVGSVLD KLLFHIYLLA VLAYSITLVM LWSIWQYA
 
 
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