5HT2A_HUMAN
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 03-AUG-2022, entry version 216.
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]
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 [24]
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 [25]
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 [26]
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";
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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; 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; 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 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 GlyGen; P28223; 5 sites.
DR iPTMnet; P28223; -.
DR PhosphoSitePlus; P28223; -.
DR BioMuta; HTR2A; -.
DR DMDM; 543727; -.
DR MassIVE; P28223; -.
DR PaxDb; P28223; -.
DR PeptideAtlas; P28223; -.
DR PRIDE; P28223; -.
DR ProteomicsDB; 24094; -.
DR ProteomicsDB; 54453; -. [P28223-1]
DR ABCD; P28223; 1 sequenced antibody.
DR Antibodypedia; 2927; 378 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 CTD; 3356; -.
DR DisGeNET; 3356; -.
DR GeneCards; HTR2A; -.
DR HGNC; HGNC:5293; HTR2A.
DR HPA; ENSG00000102468; Tissue enhanced (brain, choroid plexus).
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; RLYNNDF; -.
DR OrthoDB; 962038at2759; -.
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 1071 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 tissues.
DR ExpressionAtlas; P28223; baseline and differential.
DR Genevisible; P28223; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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:0005829; C:cytosol; IEA:Ensembl.
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:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IEA:Ensembl.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
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: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:0007568; P:aging; IEA:Ensembl.
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:0008219; P:cell death; IEA:Ensembl.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IDA:UniProtKB.
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: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:0018108; P:peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; 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:0043406; P:positive regulation of MAP kinase activity; 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:0044380; P:protein localization to cytoskeleton; IEA:Ensembl.
DR GO; GO:0014059; P:regulation of dopamine secretion; IEA:Ensembl.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; 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:0030431; P:sleep; IEA:Ensembl.
DR GO; GO:0001659; P:temperature homeostasis; IEA:Ensembl.
DR GO; GO:0014832; P:urinary bladder smooth muscle contraction; IEA:Ensembl.
DR InterPro; IPR000455; 5HT2A_rcpt.
DR InterPro; IPR002231; 5HT_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR24247:SF30; PTHR24247:SF30; 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 PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
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 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 S-
FT 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 S-
FT 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..282
FT /evidence="ECO:0007829|PDB:7WC8"
FT HELIX 293..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
