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5-hydroxytryptamine receptor 2A (5-HT-2) (5-HT-2A) (5-hydroxytryptamine receptor) (Serotonin receptor 2A)

 5HT2A_CANLF             Reviewed;         470 AA.
O46635; Q50DZ9; Q60F96;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
12-APR-2005, sequence version 2.
25-OCT-2017, entry version 114.
RecName: Full=5-hydroxytryptamine receptor 2A;
Short=5-HT-2;
Short=5-HT-2A;
Short=5-hydroxytryptamine receptor;
AltName: Full=Serotonin receptor 2A;
Name=HTR2A; Synonyms=5-HTR2A;
Canis lupus familiaris (Dog) (Canis familiaris).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
Canis.
NCBI_TaxID=9615;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Beagle;
PubMed=15353848; DOI=10.1292/jvms.66.965;
Masuda K., Hashizume C., Ogata N., Kikusui T., Takeuchi Y., Mori Y.;
"Sequencing of canine 5-hydroxytriptamine receptor (5-HTR) 1B, 2A, 2C
genes and identification of polymorphisms in the 5-HTR1B gene.";
J. Vet. Med. Sci. 66:965-972(2004).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=15862800; DOI=10.1016/j.ejphar.2005.03.013;
Bonaventure P., Nepomuceno D., Miller K., Chen J., Kuei C., Kamme F.,
Tran D.T., Lovenberg T.W., Liu C.;
"Molecular and pharmacological characterization of serotonin 5-HT(2A)
and 5-HT(2B) receptor subtypes in dog.";
Eur. J. Pharmacol. 513:181-192(2005).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 120-307.
TISSUE=Femoral artery;
Sgard F.;
Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine
(serotonin). Also functions as a receptor for various drugs and
psychoactive substances, including mescaline, psilocybin, 1-(2,5-
dimethoxy-4-iodophenyl)-2-aminopropane (DOI) and lysergic acid
diethylamide (LSD). Ligand binding causes a conformation change
that triggers signaling via guanine nucleotide-binding proteins (G
proteins) and modulates the activity of down-stream effectors.
Beta-arrestin family members inhibit signaling via G proteins and
mediate activation of alternative signaling pathways. Signaling
activates phospholipase C and a phosphatidylinositol-calcium
second messenger system that modulates the activity of
phosphatidylinositol 3-kinase and promotes the release of Ca(2+)
ions from intracellular stores. Affects neural activity,
perception, cognition and mood. Plays a role in the regulation of
behavior, including responses to anxiogenic situations and
psychoactive substances. Plays a role in intestinal smooth muscle
contraction, and may play a role in arterial vasoconstriction.
{ECO:0000269|PubMed:15862800}.
-!- SUBUNIT: Interacts (via C-terminus) with MPDZ and PATJ. May
interact (via C-terminus) with MPP3, PRDX6, DLG4, DLG1, CASK,
APBA1 and MAGI2. Interacts with GRM2 and DRD2; this may affect
signaling. {ECO:0000250|UniProtKB:P28223}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15862800};
Multi-pass membrane protein {ECO:0000269|PubMed:15862800}. Cell
projection, dendrite {ECO:0000250}. Cell projection, axon
{ECO:0000250|UniProtKB:P14842}. Cytoplasmic vesicle
{ECO:0000250|UniProtKB:P14842}. Membrane, caveola
{ECO:0000250|UniProtKB:P14842}. Note=Localizes to the postsynaptic
thickening of axo-dendritic synapses. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15862800}.
-!- DOMAIN: The PDZ domain-binding motif is involved in the
interaction with PATJ, CASK, APBA1, DLG1 and DLG4.
{ECO:0000250|UniProtKB:P28223}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
{ECO:0000255|PROSITE-ProRule:PRU00521}.
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EMBL; AB193092; BAD60922.1; -; mRNA.
EMBL; AY832858; AAX39385.1; -; mRNA.
EMBL; Y16134; CAA76080.1; -; mRNA.
RefSeq; NP_001005869.1; NM_001005869.1.
UniGene; Cfa.8880; -.
ProteinModelPortal; O46635; -.
SMR; O46635; -.
BindingDB; O46635; -.
ChEMBL; CHEMBL5781; -.
GeneID; 403882; -.
KEGG; cfa:403882; -.
CTD; 3356; -.
HOGENOM; HOG000240378; -.
HOVERGEN; HBG107487; -.
InParanoid; O46635; -.
KO; K04157; -.
PRO; PR:O46635; -.
Proteomes; UP000002254; Unplaced.
GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
GO; GO:0005901; C:caveola; IEA:UniProtKB-SubCell.
GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
GO; GO:0043198; C:dendritic shaft; IEA:InterPro.
GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0008144; F:drug binding; IDA:UniProtKB.
GO; GO:0004993; F:G-protein coupled serotonin receptor activity; IDA:UniProtKB.
GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
GO; GO:0051378; F:serotonin binding; IDA:UniProtKB.
GO; GO:0007610; P:behavior; IEA:UniProtKB-KW.
GO; GO:0007200; P:phospholipase C-activating G-protein coupled receptor signaling pathway; IBA:GO_Central.
GO; GO:0050795; P:regulation of behavior; IEA:InterPro.
GO; GO:0046883; P:regulation of hormone secretion; IEA:InterPro.
GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IDA:UniProtKB.
GO; GO:0042493; P:response to drug; IDA:UniProtKB.
GO; GO:0006939; P:smooth muscle contraction; IEA:InterPro.
InterPro; IPR000455; 5HT2A_rcpt.
InterPro; IPR002231; 5HT_rcpt.
InterPro; IPR000276; GPCR_Rhodpsn.
InterPro; IPR017452; GPCR_Rhodpsn_7TM.
PANTHER; PTHR24247:SF30; PTHR24247:SF30; 1.
Pfam; PF00001; 7tm_1; 1.
PRINTS; PR00516; 5HT2ARECEPTR.
PRINTS; PR01101; 5HTRECEPTOR.
PRINTS; PR00237; GPCRRHODOPSN.
SMART; SM01381; 7TM_GPCR_Srsx; 1.
PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
2: Evidence at transcript level;
Behavior; Cell membrane; Cell projection; Complete proteome;
Cytoplasmic vesicle; Disulfide bond; G-protein coupled receptor;
Glycoprotein; Membrane; Phosphoprotein; Receptor; Reference proteome;
Transducer; Transmembrane; Transmembrane helix.
CHAIN 1 470 5-hydroxytryptamine receptor 2A.
/FTId=PRO_0000068943.
TOPO_DOM 1 75 Extracellular. {ECO:0000250}.
TRANSMEM 76 99 Helical; Name=1. {ECO:0000250}.
TOPO_DOM 100 110 Cytoplasmic. {ECO:0000250}.
TRANSMEM 111 132 Helical; Name=2. {ECO:0000250}.
TOPO_DOM 133 148 Extracellular. {ECO:0000250}.
TRANSMEM 149 171 Helical; Name=3. {ECO:0000250}.
TOPO_DOM 172 191 Cytoplasmic. {ECO:0000250}.
TRANSMEM 192 215 Helical; Name=4. {ECO:0000250}.
TOPO_DOM 216 233 Extracellular. {ECO:0000250}.
TRANSMEM 234 254 Helical; Name=5. {ECO:0000250}.
TOPO_DOM 255 323 Cytoplasmic. {ECO:0000250}.
TRANSMEM 324 345 Helical; Name=6. {ECO:0000250}.
TOPO_DOM 346 361 Extracellular. {ECO:0000250}.
TRANSMEM 362 383 Helical; Name=7. {ECO:0000250}.
TOPO_DOM 384 470 Cytoplasmic. {ECO:0000250}.
REGION 155 160 Agonist binding.
{ECO:0000250|UniProtKB:P41595}.
REGION 335 339 Agonist binding.
{ECO:0000250|UniProtKB:P41595}.
MOTIF 172 174 DRY motif; important for ligand-induced
conformation changes.
{ECO:0000250|UniProtKB:P41595}.
MOTIF 375 379 NPxxY motif; important for ligand-induced
conformation changes and signaling.
{ECO:0000250|UniProtKB:P41595}.
MOTIF 468 470 PDZ-binding.
{ECO:0000250|UniProtKB:P28223}.
SITE 229 229 Hydrophobic barrier that decreases the
speed of ligand binding and dissociation.
{ECO:0000250|UniProtKB:P28223}.
MOD_RES 280 280 Phosphoserine.
{ECO:0000250|UniProtKB:P28223}.
CARBOHYD 38 38 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 44 44 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 51 51 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 54 54 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 148 227 {ECO:0000255|PROSITE-ProRule:PRU00521}.
DISULFID 348 352 {ECO:0000255|PROSITE-ProRule:PRU00521}.
SEQUENCE 470 AA; 52378 MW; 5C654F81E88B92E3 CRC64;
MDVLFEDNAP LSPTTSSLMP SNGDPRLYGN DLNAGDANTS DAFNWTVDAE NRTNLSCEGC
LSPPCFSLLH LQEKNWSALL TAVVIILTIA GNILVIMAVS LEKKLQNATN YFLMSLAIAD
MLLGFLVMPV SMLTILYGYR WPLPSKLCAV WIYLDVLFST ASIMHLCAIS LDRYVAIQNP
IHHSRFNSRT KAFLKIIAVW TISVGISMPI PVFGLQDDSK VFKEGSCLLA DDNFVLIGSF
VSFFIPLTIM VITYFLTIKS LQKEATLCVS DPGTRAKLAS FSFLPQSSLS SEKLFQRSIH
REPGSYGRRT MQSISNEQKA CKVLGIVFFL FVVMWCPFFI TNIMAVICKE SCNEDIIGAL
LNVFVWIGYL SSAVNPLVYT LFNKTYRSAF SRYIQCQYKE NKKPLQLILV NTIPALAYKS
SQLQMGQKKN SKKDAKSTDN DYSMVALGKQ HSEDAPTDNI NTVNEKVSCV


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