5HT1D_CANLF
ID 5HT1D_CANLF Reviewed; 377 AA.
AC P11614;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=5-hydroxytryptamine receptor 1D;
DE Short=5-HT-1D;
DE Short=5-HT1D;
DE AltName: Full=Serotonin receptor 1D;
GN Name=HTR1D; Synonyms=RDC4;
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 TISSUE=Thyroid;
RX PubMed=2541503; DOI=10.1126/science.2541503;
RA Libert F., Parmentier M., Lefort A., Dinsart C., van Sande J., Maenhaut C.,
RA Simons M.-J., Dumont J.E., Vassart G.;
RT "Selective amplification and cloning of four new members of the G protein-
RT coupled receptor family.";
RL Science 244:569-572(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Thyroid;
RX PubMed=2159630; DOI=10.1093/nar/18.7.1916;
RA Libert F., Parmentier M., Lefort A., Dumont J.E., Vassart G.;
RT "Complete nucleotide sequence of a putative G protein coupled receptor:
RT RDC4.";
RL Nucleic Acids Res. 18:1916-1916(1990).
RN [3]
RP FUNCTION.
RX PubMed=1659418; DOI=10.1016/s0006-291x(05)81360-9;
RA Maenhaut C., van Sande J., Massart C., Dinsart C., Libert F., Monferini E.,
RA Giraldo E., Ladinsky H., Vassart G., Dumont J.E.;
RT "The orphan receptor cDNA RDC4 encodes a 5-HT1D serotonin receptor.";
RL Biochem. Biophys. Res. Commun. 180:1460-1468(1991).
RN [4]
RP FUNCTION.
RX PubMed=1758439;
RA Zgombick J.M., Weinshank R.L., Macchi M., Schechter L.E., Branchek T.A.,
RA Hartig P.R.;
RT "Expression and pharmacological characterization of a canine 5-
RT hydroxytryptamine1D receptor subtype.";
RL Mol. Pharmacol. 40:1036-1042(1991).
CC -!- FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine
CC (serotonin). Also functions as a receptor for various alkaloids and
CC psychoactive substances. Ligand binding causes a conformation change
CC that triggers signaling via guanine nucleotide-binding proteins (G
CC proteins) and modulates the activity of down-stream effectors, such as
CC adenylate cyclase. Signaling inhibits adenylate cyclase activity.
CC Regulates the release of 5-hydroxytryptamine in the brain, and thereby
CC affects neural activity. May also play a role in regulating the release
CC of other neurotransmitters. May play a role in vasoconstriction.
CC {ECO:0000269|PubMed:1659418, ECO:0000269|PubMed:1758439}.
CC -!- SUBUNIT: Homodimer. Heterodimer with HTR1B (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; X14049; CAA32207.1; -; mRNA.
DR PIR; B30341; B30341.
DR RefSeq; NP_001003280.1; NM_001003280.1.
DR AlphaFoldDB; P11614; -.
DR SMR; P11614; -.
DR STRING; 9612.ENSCAFP00000019638; -.
DR BindingDB; P11614; -.
DR PaxDb; P11614; -.
DR GeneID; 403963; -.
DR KEGG; cfa:403963; -.
DR CTD; 3352; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; P11614; -.
DR OrthoDB; 703991at2759; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0004993; F:G protein-coupled serotonin receptor activity; ISS:UniProtKB.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0051378; F:serotonin binding; IBA:GO_Central.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007198; P:adenylate cyclase-inhibiting serotonin receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; IBA:GO_Central.
DR GO; GO:0050795; P:regulation of behavior; IEA:InterPro.
DR GO; GO:0040012; P:regulation of locomotion; IEA:InterPro.
DR GO; GO:0006939; P:smooth muscle contraction; IEA:InterPro.
DR GO; GO:0042310; P:vasoconstriction; IEA:InterPro.
DR InterPro; IPR000505; 5HT1D_rcpt.
DR InterPro; IPR002231; 5HT_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR24247:SF17; PTHR24247:SF17; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00514; 5HT1DRECEPTR.
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 Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..377
FT /note="5-hydroxytryptamine receptor 1D"
FT /id="PRO_0000068925"
FT TOPO_DOM 1..38
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 39..64
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 65..75
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 76..98
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 99..112
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 113..134
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 135..154
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 155..176
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 177..194
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 195..217
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 218..302
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 303..326
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 327..335
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 336..360
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 361..377
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT MOTIF 135..137
FT /note="DRY motif; important for ligand-induced conformation
FT changes"
FT /evidence="ECO:0000250"
FT MOTIF 352..356
FT /note="NPxxY motif; important for ligand-induced
FT conformation changes and signaling"
FT /evidence="ECO:0000250"
FT BINDING 118
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P28222"
FT BINDING 123
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P28222"
FT BINDING 190
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P28222"
FT CARBOHYD 5
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 17
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 21
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 111..188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 377 AA; 41883 MW; 8E6406DCE2123EE4 CRC64;
MSPPNQSLEG LLQEASNRSL NATETPEAWG PETLQALKIS LALLLSIITM ATALSNAFVL
TTIFLTRKLH TPANYLIGSL AMTDLLVSIL VMPISIAYTT TRTWSFGQIL CDIWLSSDIT
CCTASILHLC VIALDRYWAI TDALEYSKRR TAGRAAVMIA TVWVISICIS IPPLFWRQAK
AQEDMSDCQV NTSQISYTIY STCGAFYIPS VLLIILYGRI YVAARNRILN PPSLYGKRFT
TAQLITGSAG SSLCSLSPSL QEERSHAAGP PLFFNHVQVK LAEGVLERKR ISAARERKAT
KTLGIILGAF IVCWLPFFVA SLVLPICRAS CWLHPALFDF FTWLGYLNSL INPIIYTVFN
EEFRQAFQRV VHVRKAS
