HTR2C
entrez
3358
canonical
uniprot
P28335
canonical
ensembl
ENSG00000147246
resolver
ensp
ENSP00000276198
resolver
ensp
ENSP00000361018
resolver
ensp
ENSP00000361019
resolver
genesymbol
HTR2C
resolver
genesymbol_syn
HTR1C
resolver
hgnc
HGNC:5295
resolver
uniprot
B1AMW4
resolver
uniprot
K9J958
resolver
uniprot
Q5VUF8
resolver
uniprot
Q9NP28
resolver
uniprot_entry
5HT2C_HUMAN
resolver
uniprot_entry
K9J958_HUMAN
resolver
uniprot_sec
B1AMW4
resolver
uniprot_sec
Q5VUF8
resolver
uniprot_sec
Q9NP28
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by inverse agonist ritanserin. {ECO:0000269|PubMed:29398112}.
uniprot
proteins
amino_acid_sequence
MVNLRNAVHSFLVHLIGLLVWQSDISVSPVAAIVTDIFNTSDGGRFKFPDGVQNWPALSIVIIIIMTIGGNILVIMAVSMEKKLHNATNYFLMSLAIADMLVGLLVMPLSLLAILYDYVWPLPRYLCPVWISLDVLFSTASIMHLCAISLDRYVAIRNPIEHSRFNSRTKAIMKIAIVWAISIGVSVPIPVIGLRDEEKVFVNNTTCVLNDPNFVLIGSFVAFFIPLTIMVITYCLTIYVLRRQALMLLHGHTEEPPGLSLDFLKCCKRNTAEEENSANPNQDQNARRRKKKERRPRGTMQAINNERKASKVLGIVFFVFLIMWCPFFITNILSVLCEKSCNQKLMEKLLNVFVWIGYVCSGINPLVYTLFNKIYRRAFSNYLRCNYKVEKKPPVRQIPRVAATALSGRELNVNIYRHTNEPVIEKASDNEPGIEMQVENLELPVNPSSVVSERISSV
uniprot
proteins
function
FUNCTION: G protein-coupled receptor for 5-hydroxytryptamine (serotonin) (PubMed:12970106, PubMed:18703043, PubMed:19057895, PubMed:29398112, PubMed:7895773). Also functions as a receptor for various drugs and psychoactive substances, including ergot alkaloid derivatives, 1-2,5,-dimethoxy-4-iodophenyl-2-aminopropane (DOI) and lysergic acid diethylamide (LSD) (PubMed:19057895, PubMed:29398112). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of downstream effectors (PubMed:18703043, PubMed:29398112). HTR2C is coupled to G(q)/G(11) G alpha proteins and activates phospholipase C-beta, releasing diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) second messengers that modulate the activity of phosphatidylinositol 3-kinase and promote the release of Ca(2+) ions from intracellular stores, respectively (PubMed:18703043, PubMed:29398112). Beta-arrestin family members inhibit signaling via G proteins and mediate activation of alternative signaling pathways (PubMed:29398112). Regulates neuronal activity via the activation of short transient receptor potential calcium channels in the brain, and thereby modulates the activation of pro-opiomelanocortin neurons and the release of CRH that then regulates the release of corticosterone (By similarity). Plays a role in the regulation of appetite and eating behavior, responses to anxiogenic stimuli and stress (By similarity). Plays a role in insulin sensitivity and glucose homeostasis (By similarity). {ECO:0000250|UniProtKB:P34968, ECO:0000269|PubMed:12970106, ECO:0000269|PubMed:18703043, ECO:0000269|PubMed:19057895, ECO:0000269|PubMed:29398112, ECO:0000269|PubMed:7895773}.
uniprot
proteins
mass_dalton
51805
uniprot
proteins
mutagenesis
MUTAGEN 159; /note="P->A: Decreases interaction with ARRB2."; /evidence="ECO:0000269|PubMed:16319069"; MUTAGEN 218; /note="G->A,S: Decreased binding to inverse agonist ritanserin."; /evidence="ECO:0000269|PubMed:29398112"; MUTAGEN 223; /note="F->L: Decreased binding to inverse agonist ritanserin."; /evidence="ECO:0000269|PubMed:29398112"; MUTAGEN 320; /note="F->L: Decreased binding to inverse agonist ritanserin."; /evidence="ECO:0000269|PubMed:29398112"; MUTAGEN 324; /note="W->L,F,Y: Decreased binding to inverse agonist ritanserin."; /evidence="ECO:0000269|PubMed:29398112"; MUTAGEN 354; /note="V->N: Decreased binding to inverse agonist ritanserin."; /evidence="ECO:0000269|PubMed:29398112"; MUTAGEN 456; /note="S->A: Loss of interaction with MPDZ."; /evidence="ECO:0000269|PubMed:11150294"; MUTAGEN 456; /note="S->T: No effect on interaction with MPDZ."; /evidence="ECO:0000269|PubMed:11150294"; MUTAGEN 457; /note="S->A: No effect on interaction with MPDZ."; /evidence="ECO:0000269|PubMed:11150294"; MUTAGEN 458; /note="V->A: Loss of interaction with MPDZ."; /evidence="ECO:0000269|PubMed:11150294
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. {ECO:0000269|PubMed:11150294}.
uniprot
proteins
protein_family
G protein-coupled receptor 1 family
uniprot
proteins
pubmed
10206230
uniprot
proteins
pubmed
10391209
uniprot
proteins
pubmed
10581480
uniprot
proteins
pubmed
11150294
uniprot
proteins
pubmed
12970106
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14988405
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15772651
uniprot
proteins
pubmed
16319069
uniprot
proteins
pubmed
16914526
uniprot
proteins
pubmed
1722404
uniprot
proteins
pubmed
18703043
uniprot
proteins
pubmed
19057895
uniprot
proteins
pubmed
20945968
uniprot
proteins
pubmed
22497996
uniprot
proteins
pubmed
29398112
uniprot
proteins
pubmed
7557992
uniprot
proteins
pubmed
7895773
uniprot
proteins
pubmed
8812491
uniprot
proteins
pubmed
9928237
uniprot
proteins
sequence_length
458
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12970106, ECO:0000269|PubMed:18703043, ECO:0000269|PubMed:19057895, ECO:0000269|PubMed:7895773}; Multi-pass membrane protein {ECO:0000269|PubMed:12970106, ECO:0000269|PubMed:18703043, ECO:0000269|PubMed:19057895, ECO:0000269|PubMed:7895773}.
uniprot
proteins
transmembrane_region
TRANSMEM 56..80; /note="Helical; Name=1"; /evidence="ECO:0000269|PubMed:29398112, ECO:0000312|PDB:6BQG"; TRANSMEM 87..111; /note="Helical; Name=2"; /evidence="ECO:0000269|PubMed:29398112, ECO:0000312|PDB:6BQG"; TRANSMEM 129..151; /note="Helical; Name=3"; /evidence="ECO:0000269|PubMed:29398112, ECO:0000312|PDB:6BQG"; TRANSMEM 168..189; /note="Helical; Name=4"; /evidence="ECO:0000269|PubMed:29398112, ECO:0000312|PDB:6BQG"; TRANSMEM 214..236; /note="Helical; Name=5"; /evidence="ECO:0000269|PubMed:29398112, ECO:0000312|PDB:6BQG"; TRANSMEM 312..336; /note="Helical; Name=6"; /evidence="ECO:0000269|PubMed:29398112, ECO:0000312|PDB:6BQG"; TRANSMEM 348..370; /note="Helical; Name=7"; /evidence="ECO:0000269|PubMed:29398112, ECO:0000312|PDB:6BQG
uniprot
proteins