5HT2C_CANLF
ID 5HT2C_CANLF Reviewed; 458 AA.
AC Q60F97;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=5-hydroxytryptamine receptor 2C;
DE Short=5-HT-2C;
DE Short=5-HT2C;
DE Short=5-HTR2C;
DE AltName: Full=Serotonin receptor 2C;
DE Flags: Precursor;
GN Name=HTR2C;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Beagle;
RX PubMed=15353848; DOI=10.1292/jvms.66.965;
RA Masuda K., Hashizume C., Ogata N., Kikusui T., Takeuchi Y., Mori Y.;
RT "Sequencing of canine 5-hydroxytriptamine receptor (5-HTR) 1B, 2A, 2C genes
RT and identification of polymorphisms in the 5-HTR1B gene.";
RL J. Vet. Med. Sci. 66:965-972(2004).
CC -!- FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine
CC (serotonin). Also functions as a receptor for various drugs and
CC psychoactive substances, including ergot alkaloid derivatives, 1-2,5,-
CC dimethoxy-4-iodophenyl-2-aminopropane (DOI) and lysergic acid
CC diethylamide (LSD). 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. Beta-arrestin
CC family members inhibit signaling via G proteins and mediate activation
CC of alternative signaling pathways. Signaling activates a
CC phosphatidylinositol-calcium second messenger system that modulates the
CC activity of phosphatidylinositol 3-kinase and down-stream signaling
CC cascades and promotes the release of Ca(2+) ions from intracellular
CC stores. Regulates neuronal activity via the activation of short
CC transient receptor potential calcium channels in the brain, and thereby
CC modulates the activation of pro-opiomelacortin neurons and the release
CC of CRH that then regulates the release of corticosterone. Plays a role
CC in the regulation of appetite and feeding behavior, responses to
CC anxiogenic stimuli and stress. Plays a role in insulin sensitivity and
CC glucose homeostasis (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with MPDZ. Interacts with ARRB2 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- DOMAIN: The PDZ domain-binding motif is involved in the interaction
CC with MPDZ. {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AB193091; BAD60921.1; -; mRNA.
DR RefSeq; NP_001006649.1; NM_001006648.1.
DR AlphaFoldDB; Q60F97; -.
DR SMR; Q60F97; -.
DR STRING; 9612.ENSCAFP00000043222; -.
DR BindingDB; Q60F97; -.
DR ChEMBL; CHEMBL1770041; -.
DR PaxDb; Q60F97; -.
DR GeneID; 450240; -.
DR KEGG; cfa:450240; -.
DR CTD; 3358; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; Q60F97; -.
DR PRO; PR:Q60F97; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0001587; F:Gq/11-coupled serotonin receptor activity; ISS:UniProtKB.
DR GO; GO:0001662; P:behavioral fear response; ISS:UniProtKB.
DR GO; GO:0007631; P:feeding behavior; ISS:UniProtKB.
DR GO; GO:0007626; P:locomotory behavior; IEA:InterPro.
DR GO; GO:0007208; P:phospholipase C-activating serotonin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling pathway; ISS:UniProtKB.
DR GO; GO:0032098; P:regulation of appetite; ISS:UniProtKB.
DR GO; GO:0043397; P:regulation of corticotropin-releasing hormone secretion; ISS:UniProtKB.
DR GO; GO:0031644; P:regulation of nervous system process; ISS:UniProtKB.
DR InterPro; IPR000377; 5HT2C_rcpt.
DR InterPro; IPR002231; 5HT_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR24247:SF32; PTHR24247:SF32; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00517; 5HT2CRECEPTR.
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 2: Evidence at transcript level;
KW Behavior; Cell membrane; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Membrane; Receptor; Reference proteome; Signal; Transducer;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..32
FT /evidence="ECO:0000250"
FT CHAIN 33..458
FT /note="5-hydroxytryptamine receptor 2C"
FT /id="PRO_0000068957"
FT TOPO_DOM 33..52
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 53..78
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 79..89
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 90..110
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 111..127
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 128..150
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 151..170
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 171..193
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 194..213
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 214..235
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 236..311
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 312..333
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 334..348
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 349..371
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 372..458
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 272..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 151..153
FT /note="DRY motif; important for ligand-induced conformation
FT changes"
FT /evidence="ECO:0000250"
FT MOTIF 364..368
FT /note="NPxxY motif; important for ligand-induced
FT conformation changes and signaling"
FT /evidence="ECO:0000250"
FT MOTIF 456..458
FT /note="PDZ-binding"
FT BINDING 134
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P41595"
FT BINDING 139
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P41595"
FT BINDING 209
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P41595"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 127..207
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 337..341
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 458 AA; 51836 MW; 5A03245262B6C7BB CRC64;
MVNLRKAVHS FLVHLIGLLV WQCDISVSPV AALVTDIFNT SDGGRFKFPD GVQNWPALSI
VIIIILTIGG NILVIMAVSL EKKLHNATNY FLMSLAIADM LVGLLVMPLS LLAILYDYVW
PLPRYLCPVW ISLDVLFSTA SIMHLCAISL DRYVAIRNPV EHSRFNSRTK AIMKIAIVWA
ISIGVSVPIP VIGLRDEEKV FVNNTTCVLN DPNFVLIGSF VAFFIPLTIM VITYCLTIHV
LRRQALMLLH GHVEEPPRIN LDFLKCCRRN GTEEENSANP NQDSNPRRRK KKERRPRGTM
QAINNERKAS KVLGIVFFVF LVMWCPFFIT NILSVLCGKA CNQKLMEKLL NVFVWIGYVC
SGINPLVYTL FNKIYRRAFS NYLRCNYKPE KKPPVRQMPR VAATALSGRE LNVNIYRHTN
EPVLKKANDK EPGIEMQVEN LELPVNPSSV VSERISSV
