ID 5HT2A_HUMAN Reviewed; 471 AA. AC P28223; B2RAC5; B4DZ79; F5GWE8; Q5T8C0; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 2. DT 24-JAN-2024, entry version 224. DE RecName: Full=5-hydroxytryptamine receptor 2A; DE Short=5-HT-2; DE Short=5-HT-2A; DE AltName: Full=Serotonin receptor 2A; GN Name=HTR2A; Synonyms=HTR2; 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=Brain stem; RX PubMed=1722404; DOI=10.1016/0006-291x(91)92105-s; RA Saltzman A.G., Morse B., Whitman M.M., Ivanshchenko Y., Jaye M., Felder S.; RT "Cloning of the human serotonin 5-HT2 and 5-HT1C receptor subtypes."; RL Biochem. Biophys. Res. Commun. 181:1469-1478(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1323014; DOI=10.1016/0169-328x(92)90005-v; RA Chen K., Yang W., Grimsby J., Shih J.C.; RT "The human 5-HT2 receptor is encoded by a multiple intron-exon gene."; RL Brain Res. Mol. Brain Res. 14:20-26(1992). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Platelet; RX PubMed=8035173; DOI=10.1046/j.1471-4159.1994.63020465.x; RA Cook E.H. Jr., Fletcher K.E., Wainwright M., Marks N., Yan S.Y., RA Leventhal B.L.; RT "Primary structure of the human platelet serotonin 5-HT2A receptor: RT identify with frontal cortex serotonin 5-HT2A receptor."; RL J. Neurochem. 63:465-469(1994). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Testis, and Thalamus; 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057823; DOI=10.1038/nature02379; RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L., RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., RA Frankish A.G., Frankland J., French L., Garner P., Garnett J., RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., RA Rogers J., Ross M.T.; RT "The DNA sequence and analysis of human chromosome 13."; RL Nature 428:522-528(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.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 [8] 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 [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 9-464 (ISOFORM 1). RC TISSUE=Brain; RA Tritch R.J., Robinson D.L., Sahagan B.G., Horlick R.A.; RT "Cloning and nucleotide sequence of the human(5HT) type 2 receptor."; RL Submitted (MAY-1992) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 105-218, FUNCTION, AND SUBCELLULAR RP LOCATION. RX PubMed=1330647; DOI=10.1016/0922-4106(92)90123-d; RA Stam N.J., van Huizen F., van Alebeek C., Brands J., Dijkema R., RA Tonnaer J.A., Olijve W.; RT "Genomic organization, coding sequence and functional expression of human RT 5-HT2 and 5-HT1A receptor genes."; RL Eur. J. Pharmacol. 227:153-162(1992). RN [11] RP INTERACTION WITH MPDZ. RX PubMed=11150294; DOI=10.1074/jbc.m008089200; RA Becamel C., Figge A., Poliak S., Dumuis A., Peles E., Bockaert J., RA Luebbert H., Ullmer C.; RT "Interaction of serotonin 5-hydroxytryptamine type 2C receptors with PDZ10 RT of the multi-PDZ domain protein MUPP1."; RL J. Biol. Chem. 276:12974-12982(2001). RN [12] RP INTERACTION WITH PATJ; MPP3; PRDX6; DLG4; DLG1; CASK; APBA1 AND MAGI2, AND RP MUTAGENESIS OF GLY-463; ASN-465; CYS-470 AND VAL-471. RX PubMed=14988405; DOI=10.1074/jbc.m312106200; RA Becamel C., Gavarini S., Chanrion B., Alonso G., Galeotti N., Dumuis A., RA Bockaert J., Marin P.; RT "The serotonin 5-HT2A and 5-HT2C receptors interact with specific sets of RT PDZ proteins."; RL J. Biol. Chem. 279:20257-20266(2004). RN [13] RP REVIEW. RX PubMed=18476671; DOI=10.1021/cr078224o; RA Nichols D.E., Nichols C.D.; RT "Serotonin receptors."; RL Chem. Rev. 108:1614-1641(2008). RN [14] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=18703043; DOI=10.1016/j.ejphar.2008.07.040; RA Cussac D., Boutet-Robinet E., Ailhaud M.C., Newman-Tancredi A., RA Martel J.C., Danty N., Rauly-Lestienne I.; RT "Agonist-directed trafficking of signalling at serotonin 5-HT2A, 5-HT2B and RT 5-HT2C-VSV receptors mediated Gq/11 activation and calcium mobilisation in RT CHO cells."; RL Eur. J. Pharmacol. 594:32-38(2008). RN [15] RP INTERACTION WITH GRM2, FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR RP LOCATION. RX PubMed=18297054; DOI=10.1038/nature06612; RA Gonzalez-Maeso J., Ang R.L., Yuen T., Chan P., Weisstaub N.V., RA Lopez-Gimenez J.F., Zhou M., Okawa Y., Callado L.F., Milligan G., RA Gingrich J.A., Filizola M., Meana J.J., Sealfon S.C.; RT "Identification of a serotonin/glutamate receptor complex implicated in RT psychosis."; RL Nature 452:93-97(2008). RN [16] RP FUNCTION. RX PubMed=19057895; DOI=10.1007/s00210-008-0378-4; RA Knauer C.S., Campbell J.E., Chio C.L., Fitzgerald L.W.; RT "Pharmacological characterization of mitogen-activated protein kinase RT activation by recombinant human 5-HT2C, 5-HT2A, and 5-HT2B receptors."; RL Naunyn Schmiedebergs Arch. Pharmacol. 379:461-471(2009). RN [17] RP INTERACTION WITH DRD2, FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=21645528; DOI=10.1016/j.neuropharm.2011.05.023; RA Albizu L., Holloway T., Gonzalez-Maeso J., Sealfon S.C.; RT "Functional crosstalk and heteromerization of serotonin 5-HT2A and dopamine RT D2 receptors."; RL Neuropharmacology 61:770-777(2011). RN [18] RP REVIEW. RX PubMed=20945968; DOI=10.33549/physiolres.931903; RA Pytliak M., Vargova V., Mechirova V., Felsoci M.; RT "Serotonin receptors - from molecular biology to clinical applications."; RL Physiol. Res. 60:15-25(2011). RN [19] RP INTERACTION WITH GRM2, FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=22300836; DOI=10.1016/j.neuropharm.2012.01.010; RA Delille H.K., Becker J.M., Burkhardt S., Bleher B., Terstappen G.C., RA Schmidt M., Meyer A.H., Unger L., Marek G.J., Mezler M.; RT "Heterocomplex formation of 5-HT2A-mGlu2 and its relevance for cellular RT signaling cascades."; RL Neuropharmacology 62:2184-2191(2012). RN [20] RP PHOSPHORYLATION AT SER-280, AND MUTAGENESIS OF SER-280. RX PubMed=24637012; DOI=10.1074/mcp.m113.036558; RA Karaki S., Becamel C., Murat S., Mannoury la Cour C., Millan M.J., RA Prezeau L., Bockaert J., Marin P., Vandermoere F.; RT "Quantitative phosphoproteomics unravels biased phosphorylation of RT serotonin 2A receptor at Ser280 by hallucinogenic versus nonhallucinogenic RT agonists."; RL Mol. Cell. Proteomics 13:1273-1285(2014). RN [21] RP FUNCTION (MICROBIAL INFECTION). RX PubMed=24089568; DOI=10.1128/jvi.02252-13; RA Assetta B., Maginnis M.S., Gracia Ahufinger I., Haley S.A., Gee G.V., RA Nelson C.D., O'Hara B.A., Allen Ramdial S.A., Atwood W.J.; RT "5-HT2 receptors facilitate JC polyomavirus entry."; RL J. Virol. 87:13490-13498(2013). RN [22] RP FUNCTION, AND MUTAGENESIS OF LEU-229. RX PubMed=28129538; DOI=10.1016/j.cell.2016.12.033; RA Wacker D., Wang S., McCorvy J.D., Betz R.M., Venkatakrishnan A.J., RA Levit A., Lansu K., Schools Z.L., Che T., Nichols D.E., Shoichet B.K., RA Dror R.O., Roth B.L.; RT "Crystal structure of an LSD-bound human serotonin receptor."; RL Cell 168:377-389(2017). RN [23] {ECO:0007744|PDB:7RAN} RP STRUCTURE BY ELECTRON MICROSCOPY (3.45 ANGSTROMS) OF 66-404 IN COMPLEX WITH RP GNAI2/GNAS CHIMERA; GNB1; GNG2; STABILIZING ANTIBODY AND SYNTHETIC HTR2A RP TETRAHYDROPYRIDINE AGONIST, AND DISULFIDE BOND. RX PubMed=36171289; DOI=10.1038/s41586-022-05258-z; RA Kaplan A.L., Confair D.N., Kim K., Barros-Alvarez X., Rodriguiz R.M., RA Yang Y., Kweon O.S., Che T., McCorvy J.D., Kamber D.N., Phelan J.P., RA Martins L.C., Pogorelov V.M., DiBerto J.F., Slocum S.T., Huang X.P., RA Kumar J.M., Robertson M.J., Panova O., Seven A.B., Wetsel A.Q., RA Wetsel W.C., Irwin J.J., Skiniotis G., Shoichet B.K., Roth B.L., RA Ellman J.A.; RT "Bespoke library docking for 5-HT2A receptor agonists with antidepressant RT activity."; RL Nature 610:582-591(2022). RN [24] RP VARIANTS ASN-25 AND TYR-452. RX PubMed=8655141; DOI=10.1007/bf02281871; RA Erdmann J., Shimron-Abarbanell D., Rietschel M., Albus M., Maier W., RA Koerner J., Bondy B., Chen K., Shih J.C., Knapp M., Propping P., RA Noethen M.M.; RT "Systematic screening for mutations in the human serotonin-2A (5-HT2A) RT receptor gene: identification of two naturally occurring receptor variants RT and association analysis in schizophrenia."; RL Hum. Genet. 97:614-619(1996). RN [25] RP VARIANTS ASN-25 AND TYR-452. RX PubMed=10581480; RX DOI=10.1002/(sici)1096-8628(19991215)88:6<621::aid-ajmg9>3.0.co;2-h; RA Marshall S.E., Bird T.G., Hart K., Welsh K.I.; RT "Unified approach to the analysis of genetic variation in serotonergic RT pathways."; RL Am. J. Med. Genet. 88:621-627(1999). RN [26] RP VARIANTS VAL-197; VAL-447 AND TYR-452. RX PubMed=10391209; DOI=10.1038/10290; RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., RA Lander E.S.; RT "Characterization of single-nucleotide polymorphisms in coding regions of RT human genes."; RL Nat. Genet. 22:231-238(1999). RN [27] RP ERRATUM OF PUBMED:10391209. RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., RA Lander E.S.; RL Nat. Genet. 23:373-373(1999). CC -!- FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine CC (serotonin) (PubMed:1330647, PubMed:18703043, PubMed:19057895). Also CC functions as a receptor for various drugs and psychoactive substances, CC including mescaline, psilocybin, 1-(2,5-dimethoxy-4-iodophenyl)-2- CC aminopropane (DOI) and lysergic acid diethylamide (LSD) CC (PubMed:28129538). Ligand binding causes a conformation change that CC triggers signaling via guanine nucleotide-binding proteins (G proteins) CC and modulates the activity of down-stream effectors (PubMed:28129538). CC Beta-arrestin family members inhibit signaling via G proteins and CC mediate activation of alternative signaling pathways (PubMed:28129538). CC Signaling activates phospholipase C and a phosphatidylinositol-calcium CC second messenger system that modulates the activity of CC phosphatidylinositol 3-kinase and promotes the release of Ca(2+) ions CC from intracellular stores (PubMed:18703043, PubMed:28129538). Affects CC neural activity, perception, cognition and mood (PubMed:18297054). CC Plays a role in the regulation of behavior, including responses to CC anxiogenic situations and psychoactive substances. Plays a role in CC intestinal smooth muscle contraction, and may play a role in arterial CC vasoconstriction. {ECO:0000269|PubMed:1330647, CC ECO:0000269|PubMed:18297054, ECO:0000269|PubMed:18703043, CC ECO:0000269|PubMed:19057895, ECO:0000269|PubMed:21645528, CC ECO:0000269|PubMed:22300836, ECO:0000269|PubMed:28129538}. CC -!- FUNCTION: (Microbial infection) Acts as a receptor for human JC CC polyomavirus/JCPyV. {ECO:0000269|PubMed:24089568}. CC -!- SUBUNIT: Interacts (via C-terminus) with MPDZ and PATJ CC (PubMed:11150294, PubMed:14988405). May interact (via C-terminus) with CC MPP3, PRDX6, DLG4, DLG1, CASK, APBA1 and MAGI2 (PubMed:14988405). CC Interacts with GRM2 and DRD2; this may affect signaling CC (PubMed:18297054, PubMed:21645528, PubMed:22300836). CC {ECO:0000269|PubMed:11150294, ECO:0000269|PubMed:14988405, CC ECO:0000269|PubMed:18297054, ECO:0000269|PubMed:21645528, CC ECO:0000269|PubMed:22300836}. CC -!- INTERACTION: CC P28223; P28223: HTR2A; NbExp=3; IntAct=EBI-6656333, EBI-6656333; CC P28223; P41595: HTR2B; NbExp=3; IntAct=EBI-6656333, EBI-7474947; CC P28223; P28335: HTR2C; NbExp=5; IntAct=EBI-6656333, EBI-994141; CC P28223-1; Q14416: GRM2; NbExp=4; IntAct=EBI-15573967, EBI-10232876; CC P28223-1; P28335-1: HTR2C; NbExp=3; IntAct=EBI-15573967, EBI-21299643; CC P28223-1; P18654: Rps6ka3; Xeno; NbExp=2; IntAct=EBI-15573967, EBI-397744; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28129538}; CC Multi-pass membrane protein {ECO:0000305}. Cell projection, dendrite CC {ECO:0000250|UniProtKB:P35363}. Cell projection, axon CC {ECO:0000250|UniProtKB:P14842}. Cytoplasmic vesicle CC {ECO:0000250|UniProtKB:P14842}. Membrane, caveola CC {ECO:0000250|UniProtKB:P14842}. Presynapse CC {ECO:0000250|UniProtKB:P14842}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P28223-1; Sequence=Displayed; CC Name=2; CC IsoId=P28223-2; Sequence=VSP_046663; CC -!- TISSUE SPECIFICITY: Detected in brain cortex (at protein level). CC Detected in blood platelets. {ECO:0000269|PubMed:18297054}. CC -!- DOMAIN: The PDZ domain-binding motif is involved in the interaction CC with PATJ, CASK, APBA1, DLG1 and DLG4. {ECO:0000269|PubMed:11150294, CC ECO:0000269|PubMed:14988405}. CC -!- MISCELLANEOUS: Binds lysergic acid diethylamine (LSD) in the CC orthosteric pocket (Probable). Bound LSD dissociates extremely slowly, CC with a residence time of about 221 minutes at 37 degrees Celsius. CC {ECO:0000269|PubMed:28129538}. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC {ECO:0000255|PROSITE-ProRule:PRU00521}. CC -!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and CC polymorphism database; CC URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=C&genename=HTR2A"; 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; X57830; CAA40963.1; -; mRNA. DR EMBL; S42168; AAB22791.2; -; Genomic_DNA. DR EMBL; S42165; AAB22791.2; JOINED; Genomic_DNA. DR EMBL; S42167; AAB22791.2; JOINED; Genomic_DNA. DR EMBL; S71229; AAB31320.1; -; mRNA. DR EMBL; AF498982; AAM21129.1; -; mRNA. DR EMBL; AK302787; BAG63991.1; -; mRNA. DR EMBL; AK314132; BAG36822.1; -; mRNA. DR EMBL; AL160397; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL136958; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471075; EAX08770.1; -; Genomic_DNA. DR EMBL; BC069356; AAH69356.1; -; mRNA. DR EMBL; BC069576; AAH69576.1; -; mRNA. DR EMBL; BC074848; AAH74848.1; -; mRNA. DR EMBL; BC074849; AAH74849.1; -; mRNA. DR EMBL; BC096839; AAH96839.1; -; mRNA. DR EMBL; M86841; AAA58354.1; -; mRNA. DR EMBL; S50130; AAB24166.2; -; Genomic_DNA. DR EMBL; S49737; AAB24166.2; JOINED; Genomic_DNA. DR EMBL; S50113; AAB24166.2; JOINED; Genomic_DNA. DR CCDS; CCDS9405.1; -. [P28223-1] DR PIR; A43956; A43956. DR RefSeq; NP_000612.1; NM_000621.4. [P28223-1] DR RefSeq; NP_001159419.1; NM_001165947.2. DR PDB; 6A93; X-ray; 3.00 A; A/B=70-265, A/B=313-403. DR PDB; 6A94; X-ray; 2.90 A; A/B=70-265, A/B=313-403. DR PDB; 6WGT; X-ray; 3.40 A; A/B/C=66-265, A/B/C=311-405. DR PDB; 6WH4; X-ray; 3.40 A; A/B/C=66-265, A/B/C=311-405. DR PDB; 6WHA; EM; 3.36 A; A=66-404. DR PDB; 7RAN; EM; 3.45 A; A=66-404. DR PDB; 7VOD; X-ray; 3.30 A; A=70-265, A=313-403. DR PDB; 7VOE; X-ray; 2.90 A; A=70-265, A=313-403. DR PDB; 7WC4; X-ray; 3.20 A; A=67-403. DR PDB; 7WC5; X-ray; 3.20 A; A=67-403. DR PDB; 7WC6; X-ray; 2.60 A; A=67-403. DR PDB; 7WC7; X-ray; 2.60 A; A=67-403. DR PDB; 7WC8; X-ray; 2.45 A; A=67-403. DR PDB; 7WC9; X-ray; 2.50 A; A=67-403. DR PDBsum; 6A93; -. DR PDBsum; 6A94; -. DR PDBsum; 6WGT; -. DR PDBsum; 6WH4; -. DR PDBsum; 6WHA; -. DR PDBsum; 7RAN; -. DR PDBsum; 7VOD; -. DR PDBsum; 7VOE; -. DR PDBsum; 7WC4; -. DR PDBsum; 7WC5; -. DR PDBsum; 7WC6; -. DR PDBsum; 7WC7; -. DR PDBsum; 7WC8; -. DR PDBsum; 7WC9; -. DR AlphaFoldDB; P28223; -. DR EMDB; EMD-24378; -. DR SMR; P28223; -. DR BioGRID; 109588; 8. DR DIP; DIP-41844N; -. DR IntAct; P28223; 21. DR MINT; P28223; -. DR STRING; 9606.ENSP00000437737; -. DR BindingDB; P28223; -. DR ChEMBL; CHEMBL224; -. DR DrugBank; DB13940; 2,5-Dimethoxy-4-ethylthioamphetamine. DR DrugBank; DB01537; 4-Bromo-2,5-dimethoxyphenethylamine. DR DrugBank; DB14010; 5-methoxy-N,N-dimethyltryptamine. DR DrugBank; DB01614; Acepromazine. DR DrugBank; DB06288; Amisulpride. DR DrugBank; DB00321; Amitriptyline. DR DrugBank; DB00543; Amoxapine. DR DrugBank; DB08927; Amperozide. DR DrugBank; DB04599; Aniracetam. DR DrugBank; DB05227; APD791. DR DrugBank; DB00714; Apomorphine. DR DrugBank; DB01238; Aripiprazole. DR DrugBank; DB14185; Aripiprazole lauroxil. DR DrugBank; DB06216; Asenapine. DR DrugBank; DB05687; BL-1020. DR DrugBank; DB09223; Blonanserin. DR DrugBank; DB09128; Brexpiprazole. DR DrugBank; DB01200; Bromocriptine. DR DrugBank; DB09016; Butriptyline. DR DrugBank; DB00248; Cabergoline. DR DrugBank; DB09061; Cannabidiol. DR DrugBank; DB06016; Cariprazine. DR DrugBank; DB00477; Chlorpromazine. DR DrugBank; DB01239; Chlorprothixene. DR DrugBank; DB08810; Cinitapride. DR DrugBank; DB00604; Cisapride. DR DrugBank; DB01242; Clomipramine. DR DrugBank; DB00363; Clozapine. DR DrugBank; DB00924; Cyclobenzaprine. DR DrugBank; DB00434; Cyproheptadine. DR DrugBank; DB06512; Deramciclane. DR DrugBank; DB01151; Desipramine. DR DrugBank; DB11273; Dihydroergocornine. DR DrugBank; DB13345; Dihydroergocristine. DR DrugBank; DB00320; Dihydroergotamine. DR DrugBank; DB01488; Dimethyltryptamine. DR DrugBank; DB00843; Donepezil. DR DrugBank; DB09167; Dosulepin. DR DrugBank; DB06446; Dotarizine. DR DrugBank; DB01142; Doxepin. DR DrugBank; DB05492; Epicept NP-1. DR DrugBank; DB00751; Epinastine. DR DrugBank; DB12177; Eplivanserin. DR DrugBank; DB01049; Ergoloid mesylate. DR DrugBank; DB00696; Ergotamine. DR DrugBank; DB01175; Escitalopram. DR DrugBank; DB06678; Esmirtazapine. DR DrugBank; DB09194; Etoperidone. DR DrugBank; DB00574; Fenfluramine. DR DrugBank; DB04908; Flibanserin. DR DrugBank; DB00875; Flupentixol. DR DrugBank; DB00623; Fluphenazine. DR DrugBank; DB04842; Fluspirilene. DR DrugBank; DB12141; Gilteritinib. DR DrugBank; DB00502; Haloperidol. DR DrugBank; DB05079; HY10275. DR DrugBank; DB04946; Iloperidone. DR DrugBank; DB00458; Imipramine. DR DrugBank; DB01221; Ketamine. DR DrugBank; DB12465; Ketanserin. DR DrugBank; DB00555; Lamotrigine. DR DrugBank; DB00589; Lisuride. DR DrugBank; DB09195; Lorpiprazole. DR DrugBank; DB00408; Loxapine. DR DrugBank; DB06077; Lumateperone. DR DrugBank; DB08815; Lurasidone. DR DrugBank; DB00934; Maprotiline. DR DrugBank; DB14009; Medical Cannabis. DR DrugBank; DB00933; Mesoridazine. DR DrugBank; DB01403; Methotrimeprazine. DR DrugBank; DB00247; Methysergide. DR DrugBank; DB06148; Mianserin. DR DrugBank; DB01454; Midomafetamine. DR DrugBank; DB00805; Minaprine. DR DrugBank; DB00370; Mirtazapine. DR DrugBank; DB01442; MMDA. DR DrugBank; DB01618; Molindone. DR DrugBank; DB13948; N-(2-hydroxybenzyl)-2,5-dimethoxy-4-cyanophenylethylamine. DR DrugBank; DB14011; Nabiximols. DR DrugBank; DB08804; Nandrolone decanoate. DR DrugBank; DB01149; Nefazodone. DR DrugBank; DB12555; Nelotanserin. DR DrugBank; DB00540; Nortriptyline. DR DrugBank; DB06229; Ocaperidone. DR DrugBank; DB00334; Olanzapine. DR DrugBank; DB01267; Paliperidone. DR DrugBank; DB00715; Paroxetine. DR DrugBank; DB01186; Pergolide. DR DrugBank; DB08922; Perospirone. DR DrugBank; DB05316; Pimavanserin. DR DrugBank; DB09286; Pipamperone. DR DrugBank; DB01621; Pipotiazine. DR DrugBank; DB06153; Pizotifen. DR DrugBank; DB00420; Promazine. DR DrugBank; DB00777; Propiomazine. DR DrugBank; DB01224; Quetiapine. DR DrugBank; DB00409; Remoxipride. DR DrugBank; DB00734; Risperidone. DR DrugBank; DB12693; Ritanserin. DR DrugBank; DB12163; Sarpogrelate. DR DrugBank; DB08839; Serotonin. DR DrugBank; DB06144; Sertindole. DR DrugBank; DB09304; Setiptiline. DR DrugBank; DB01079; Tegaserod. DR DrugBank; DB00679; Thioridazine. DR DrugBank; DB01623; Thiothixene. DR DrugBank; DB13025; Tiapride. DR DrugBank; DB00656; Trazodone. DR DrugBank; DB00726; Trimipramine. DR DrugBank; DB16351; Volinanserin. DR DrugBank; DB06109; YKP-1358. DR DrugBank; DB01392; Yohimbine. DR DrugBank; DB00246; Ziprasidone. DR DrugBank; DB00315; Zolmitriptan. DR DrugBank; DB09225; Zotepine. DR DrugBank; DB01624; Zuclopenthixol. DR DrugCentral; P28223; -. DR GuidetoPHARMACOLOGY; 6; -. DR TCDB; 9.A.14.3.17; the g-protein-coupled receptor (gpcr) family. DR GlyCosmos; P28223; 5 sites, No reported glycans. DR GlyGen; P28223; 5 sites. DR iPTMnet; P28223; -. DR PhosphoSitePlus; P28223; -. DR BioMuta; HTR2A; -. DR DMDM; 543727; -. DR MassIVE; P28223; -. DR PaxDb; 9606-ENSP00000437737; -. DR PeptideAtlas; P28223; -. DR ProteomicsDB; 24094; -. DR ProteomicsDB; 54453; -. [P28223-1] DR ABCD; P28223; 1 sequenced antibody. DR Antibodypedia; 2927; 471 antibodies from 34 providers. DR DNASU; 3356; -. DR Ensembl; ENST00000542664.4; ENSP00000437737.1; ENSG00000102468.11. [P28223-1] DR GeneID; 3356; -. DR KEGG; hsa:3356; -. DR MANE-Select; ENST00000542664.4; ENSP00000437737.1; NM_000621.5; NP_000612.1. DR UCSC; uc001vbr.5; human. [P28223-1] DR AGR; HGNC:5293; -. DR CTD; 3356; -. DR DisGeNET; 3356; -. DR GeneCards; HTR2A; -. DR HGNC; HGNC:5293; HTR2A. DR HPA; ENSG00000102468; Tissue enriched (brain). DR MalaCards; HTR2A; -. DR MIM; 182135; gene. DR neXtProt; NX_P28223; -. DR OpenTargets; ENSG00000102468; -. DR PharmGKB; PA193; -. DR VEuPathDB; HostDB:ENSG00000102468; -. DR eggNOG; KOG3656; Eukaryota. DR GeneTree; ENSGT01050000244937; -. DR HOGENOM; CLU_009579_11_3_1; -. DR InParanoid; P28223; -. DR OMA; VTIGIHH; -. DR OrthoDB; 2880253at2759; -. DR PhylomeDB; P28223; -. DR TreeFam; TF316350; -. DR PathwayCommons; P28223; -. DR Reactome; R-HSA-390666; Serotonin receptors. DR Reactome; R-HSA-416476; G alpha (q) signalling events. DR SignaLink; P28223; -. DR SIGNOR; P28223; -. DR BioGRID-ORCS; 3356; 7 hits in 1155 CRISPR screens. DR GeneWiki; 5-HT2A_receptor; -. DR GenomeRNAi; 3356; -. DR Pharos; P28223; Tclin. DR PRO; PR:P28223; -. DR Proteomes; UP000005640; Chromosome 13. DR RNAct; P28223; Protein. DR Bgee; ENSG00000102468; Expressed in buccal mucosa cell and 131 other cell types or tissues. DR ExpressionAtlas; P28223; baseline and differential. DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell. DR GO; GO:0005901; C:caveola; IEA:UniProtKB-SubCell. DR GO; GO:0070852; C:cell body fiber; IEA:Ensembl. DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW. DR GO; GO:0030425; C:dendrite; IBA:GO_Central. DR GO; GO:0043198; C:dendritic shaft; IEA:Ensembl. DR GO; GO:0098666; C:G protein-coupled serotonin receptor complex; IDA:UniProtKB. DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl. DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0045211; C:postsynaptic membrane; IEA:Ensembl. DR GO; GO:0042734; C:presynaptic membrane; IEA:Ensembl. DR GO; GO:0071886; F:1-(4-iodo-2,5-dimethoxyphenyl)propan-2-amine binding; IDA:UniProtKB. DR GO; GO:0004993; F:G protein-coupled serotonin receptor activity; IDA:UniProtKB. DR GO; GO:0001587; F:Gq/11-coupled serotonin receptor activity; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central. DR GO; GO:0030296; F:protein tyrosine kinase activator activity; IEA:Ensembl. DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl. DR GO; GO:0051378; F:serotonin binding; IDA:UniProtKB. DR GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW. DR GO; GO:0007202; P:activation of phospholipase C activity; IDA:UniProtKB. DR GO; GO:0014824; P:artery smooth muscle contraction; IEA:Ensembl. DR GO; GO:0048148; P:behavioral response to cocaine; IEA:Ensembl. DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central. DR GO; GO:0050966; P:detection of mechanical stimulus involved in sensory perception of pain; IEA:Ensembl. DR GO; GO:0050965; P:detection of temperature stimulus involved in sensory perception of pain; IEA:Ensembl. DR GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; IBA:GO_Central. DR GO; GO:0098664; P:G protein-coupled serotonin receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0006096; P:glycolytic process; IEA:Ensembl. DR GO; GO:0006874; P:intracellular calcium ion homeostasis; IDA:UniProtKB. DR GO; GO:0007613; P:memory; IEA:Ensembl. DR GO; GO:0043267; P:negative regulation of potassium ion transport; IEA:Ensembl. DR GO; GO:0051967; P:negative regulation of synaptic transmission, glutamatergic; IEA:Ensembl. DR GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; IDA:UniProtKB. DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IBA:GO_Central. DR GO; GO:0007208; P:phospholipase C-activating serotonin receptor signaling pathway; IEA:Ensembl. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl. DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl. DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:UniProtKB. DR GO; GO:0045600; P:positive regulation of fat cell differentiation; IEA:Ensembl. DR GO; GO:0045821; P:positive regulation of glycolytic process; IEA:Ensembl. DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Ensembl. DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl. DR GO; GO:0010513; P:positive regulation of phosphatidylinositol biosynthetic process; IDA:UniProtKB. DR GO; GO:0045907; P:positive regulation of vasoconstriction; IEA:Ensembl. DR GO; GO:0099171; P:presynaptic modulation of chemical synaptic transmission; IEA:Ensembl. DR GO; GO:0044380; P:protein localization to cytoskeleton; IEA:Ensembl. DR GO; GO:0014059; P:regulation of dopamine secretion; IEA:Ensembl. DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IDA:UniProtKB. DR GO; GO:0009410; P:response to xenobiotic stimulus; IDA:UniProtKB. DR GO; GO:0007210; P:serotonin receptor signaling pathway; TAS:ProtInc. DR GO; GO:0001659; P:temperature homeostasis; IEA:Ensembl. DR GO; GO:0014832; P:urinary bladder smooth muscle contraction; IEA:Ensembl. DR CDD; cd15304; 7tmA_5-HT2A; 1. DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1. DR InterPro; IPR000455; 5HT2A_rcpt. DR InterPro; IPR002231; 5HT_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR017452; GPCR_Rhodpsn_7TM. DR PANTHER; PTHR24247; 5-HYDROXYTRYPTAMINE RECEPTOR; 1. DR PANTHER; PTHR24247:SF30; 5-HYDROXYTRYPTAMINE RECEPTOR 2A; 1. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00516; 5HT2ARECEPTR. DR PRINTS; PR01101; 5HTRECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR SMART; SM01381; 7TM_GPCR_Srsx; 1. DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1. DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1. DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1. DR Genevisible; P28223; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Behavior; Cell membrane; KW Cell projection; Cytoplasmic vesicle; Disulfide bond; KW G-protein coupled receptor; Glycoprotein; KW Host cell receptor for virus entry; Host-virus interaction; Membrane; KW Phosphoprotein; Receptor; Reference proteome; Synapse; Transducer; KW Transmembrane; Transmembrane helix. FT CHAIN 1..471 FT /note="5-hydroxytryptamine receptor 2A" FT /id="PRO_0000068946" FT TOPO_DOM 1..75 FT /note="Extracellular" FT /evidence="ECO:0000250" FT TRANSMEM 76..99 FT /note="Helical; Name=1" FT /evidence="ECO:0000250" FT TOPO_DOM 100..110 FT /note="Cytoplasmic" FT /evidence="ECO:0000250" FT TRANSMEM 111..132 FT /note="Helical; Name=2" FT /evidence="ECO:0000250" FT TOPO_DOM 133..148 FT /note="Extracellular" FT /evidence="ECO:0000250" FT TRANSMEM 149..171 FT /note="Helical; Name=3" FT /evidence="ECO:0000250" FT TOPO_DOM 172..191 FT /note="Cytoplasmic" FT /evidence="ECO:0000250" FT TRANSMEM 192..215 FT /note="Helical; Name=4" FT /evidence="ECO:0000250" FT TOPO_DOM 216..233 FT /note="Extracellular" FT /evidence="ECO:0000250" FT TRANSMEM 234..254 FT /note="Helical; Name=5" FT /evidence="ECO:0000250" FT TOPO_DOM 255..324 FT /note="Cytoplasmic" FT /evidence="ECO:0000250" FT TRANSMEM 325..346 FT /note="Helical; Name=6" FT /evidence="ECO:0000250" FT TOPO_DOM 347..362 FT /note="Extracellular" FT /evidence="ECO:0000250" FT TRANSMEM 363..384 FT /note="Helical; Name=7" FT /evidence="ECO:0000250" FT TOPO_DOM 385..471 FT /note="Cytoplasmic" FT /evidence="ECO:0000250" FT REGION 450..471 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 172..174 FT /note="DRY motif; important for ligand-induced conformation FT changes" FT /evidence="ECO:0000250|UniProtKB:P41595" FT MOTIF 376..380 FT /note="NPxxY motif; important for ligand-induced FT conformation changes and signaling" FT /evidence="ECO:0000250|UniProtKB:P41595" FT MOTIF 469..471 FT /note="PDZ-binding" FT /evidence="ECO:0000269|PubMed:11150294, FT ECO:0000269|PubMed:14988405" FT BINDING 155 FT /ligand="ergotamine" FT /ligand_id="ChEBI:CHEBI:190463" FT /ligand_note="agonist" FT /evidence="ECO:0000250|UniProtKB:P41595" FT BINDING 160 FT /ligand="ergotamine" FT /ligand_id="ChEBI:CHEBI:190463" FT /ligand_note="agonist" FT /evidence="ECO:0000250|UniProtKB:P41595" FT BINDING 229 FT /ligand="ergotamine" FT /ligand_id="ChEBI:CHEBI:190463" FT /ligand_note="agonist" FT /evidence="ECO:0000250|UniProtKB:P41595" FT SITE 229 FT /note="Hydrophobic barrier that decreases the speed of FT ligand binding and dissociation" FT /evidence="ECO:0000269|PubMed:28129538" FT MOD_RES 280 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:24637012" FT CARBOHYD 8 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 38 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 44 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 51 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 54 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 148..227 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521, FT ECO:0000269|PubMed:36171289, ECO:0007744|PDB:7RAN" FT DISULFID 349..353 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521" FT VAR_SEQ 1..138 FT /note="MDILCEENTSLSSTTNSLMQLNDDTRLYSNDFNSGEANTSDAFNWTVDSENR FT TNLSCEGCLSPSCLSLLHLQEKNWSALLTAVVIILTIAGNILVIMAVSLEKKLQNATNY FT FLMSLAIADMLLGFLVMPVSMLTILYG -> MQFLKSAKQKPNYYHIMLVEDQEEGTLH FT QFNYCERCSESQNNKCISCVDPEDKW (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_046663" FT VARIANT 25 FT /note="T -> N (in dbSNP:rs1805055)" FT /evidence="ECO:0000269|PubMed:10581480, FT ECO:0000269|PubMed:8655141" FT /id="VAR_003448" FT VARIANT 197 FT /note="I -> V (in dbSNP:rs6304)" FT /evidence="ECO:0000269|PubMed:10391209" FT /id="VAR_013901" FT VARIANT 447 FT /note="A -> V (in dbSNP:rs6308)" FT /evidence="ECO:0000269|PubMed:10391209" FT /id="VAR_013902" FT VARIANT 452 FT /note="H -> Y (in dbSNP:rs6314)" FT /evidence="ECO:0000269|PubMed:10391209, FT ECO:0000269|PubMed:10581480, ECO:0000269|PubMed:8655141" FT /id="VAR_003449" FT MUTAGEN 229 FT /note="L->A: Strongly increases dissociation of bound FT lysergic acid diethylamine, without affecting binding FT affinity. Reduces signaling via arrestins, but has no FT effect on signaling via the phosphatidylinositol-calcium FT second messenger system." FT /evidence="ECO:0000269|PubMed:28129538" FT MUTAGEN 280 FT /note="S->A: Increased ability of hallucinogens to FT desensitize the receptor." FT /evidence="ECO:0000269|PubMed:24637012" FT MUTAGEN 280 FT /note="S->D: Reduced receptor desensitization by FT nonhallucinogenic agonists." FT /evidence="ECO:0000269|PubMed:24637012" FT MUTAGEN 463 FT /note="G->V: Loss of interaction with PATJ." FT /evidence="ECO:0000269|PubMed:14988405" FT MUTAGEN 465 FT /note="N->S: No effect on interaction with PATJ. Acquires FT the binding properties of HTR2C; when associated with FT S-470." FT /evidence="ECO:0000269|PubMed:14988405" FT MUTAGEN 470 FT /note="C->S: No effect on interaction with PATJ. Acquires FT the binding properties of HTR2C; when associated with FT S-465." FT /evidence="ECO:0000269|PubMed:14988405" FT MUTAGEN 471 FT /note="V->A: Loss of interaction with PATJ, CASK, APBA1, FT DLG1 and DLG4." FT /evidence="ECO:0000269|PubMed:14988405" FT HELIX 72..75 FT /evidence="ECO:0007829|PDB:6WH4" FT HELIX 77..101 FT /evidence="ECO:0007829|PDB:7WC8" FT HELIX 103..105 FT /evidence="ECO:0007829|PDB:7WC8" FT HELIX 108..126 FT /evidence="ECO:0007829|PDB:7WC8" FT HELIX 128..135 FT /evidence="ECO:0007829|PDB:7WC8" FT TURN 136..139 FT /evidence="ECO:0007829|PDB:7WC8" FT HELIX 147..178 FT /evidence="ECO:0007829|PDB:7WC8" FT TURN 180..183 FT /evidence="ECO:0007829|PDB:6A94" FT HELIX 189..207 FT /evidence="ECO:0007829|PDB:7WC8" FT HELIX 209..214 FT /evidence="ECO:0007829|PDB:7WC8" FT HELIX 218..220 FT /evidence="ECO:0007829|PDB:7WC8" FT STRAND 222..225 FT /evidence="ECO:0007829|PDB:7WC6" FT STRAND 226..228 FT /evidence="ECO:0007829|PDB:7WC8" FT HELIX 232..242 FT /evidence="ECO:0007829|PDB:7WC8" FT HELIX 244..265 FT /evidence="ECO:0007829|PDB:7WC8" FT HELIX 312..348 FT /evidence="ECO:0007829|PDB:7WC8" FT TURN 350..352 FT /evidence="ECO:0007829|PDB:7WC9" FT HELIX 355..383 FT /evidence="ECO:0007829|PDB:7WC8" FT HELIX 385..395 FT /evidence="ECO:0007829|PDB:7WC8" FT CONFLICT P28223-2:49 FT /note="D -> N (in Ref. 5; BAG63991)" FT /evidence="ECO:0000305" SQ SEQUENCE 471 AA; 52603 MW; EF8AAC0BC5379DA2 CRC64; MDILCEENTS LSSTTNSLMQ LNDDTRLYSN DFNSGEANTS DAFNWTVDSE NRTNLSCEGC LSPSCLSLLH LQEKNWSALL TAVVIILTIA GNILVIMAVS LEKKLQNATN YFLMSLAIAD MLLGFLVMPV SMLTILYGYR WPLPSKLCAV WIYLDVLFST ASIMHLCAIS LDRYVAIQNP IHHSRFNSRT KAFLKIIAVW TISVGISMPI PVFGLQDDSK VFKEGSCLLA DDNFVLIGSF VSFFIPLTIM VITYFLTIKS LQKEATLCVS DLGTRAKLAS FSFLPQSSLS SEKLFQRSIH REPGSYTGRR TMQSISNEQK ACKVLGIVFF LFVVMWCPFF ITNIMAVICK ESCNEDVIGA LLNVFVWIGY LSSAVNPLVY TLFNKTYRSA FSRYIQCQYK ENKKPLQLIL VNTIPALAYK SSQLQMGQKK NSKQDAKTTD NDCSMVALGK QHSEEASKDN SDGVNEKVSC V //