5HT1D_CAVPO
ID 5HT1D_CAVPO Reviewed; 376 AA.
AC Q60484; O08891;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 121.
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;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=Hartley; TISSUE=Brain;
RX PubMed=8978753; DOI=10.1046/j.1471-4159.1997.68010410.x;
RA Wurch T., Palmier C., Colpaert F.C., Pauwels P.J.;
RT "Sequence and functional analysis of cloned guinea pig and rat serotonin 5-
RT HT1D receptors: common pharmacological features within the 5-HT1D receptor
RT subfamily.";
RL J. Neurochem. 68:410-418(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Liver;
RX PubMed=9225276; DOI=10.1016/s0028-3908(97)00023-3;
RA Zgombick J.M., Bard J.A., Kucharewicz S.A., Urquhart D.A., Weinshank R.L.,
RA Branchek T.A.;
RT "Molecular cloning and pharmacological characterization of guinea pig 5-
RT HT1B and 5-HT1D receptors.";
RL Neuropharmacology 36:513-524(1997).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15189767; DOI=10.1016/j.ejphar.2004.04.029;
RA Pullar I.A., Boot J.R., Broadmore R.J., Eyre T.A., Cooper J., Sanger G.J.,
RA Wedley S., Mitchell S.N.;
RT "The role of the 5-HT1D receptor as a presynaptic autoreceptor in the
RT guinea pig.";
RL Eur. J. Pharmacol. 493:85-93(2004).
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:15189767, ECO:0000269|PubMed:8978753,
CC ECO:0000269|PubMed:9225276}.
CC -!- SUBUNIT: Homodimer. Heterodimer with HTR1B (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15189767,
CC ECO:0000269|PubMed:8978753, ECO:0000269|PubMed:9225276}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:15189767,
CC ECO:0000269|PubMed:8978753, ECO:0000269|PubMed:9225276}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X94436; CAA64210.1; -; Genomic_DNA.
DR EMBL; U82174; AAB58499.1; -; Genomic_DNA.
DR RefSeq; NP_001166889.1; NM_001173418.1.
DR RefSeq; XP_013009218.1; XM_013153764.1.
DR AlphaFoldDB; Q60484; -.
DR SMR; Q60484; -.
DR STRING; 10141.ENSCPOP00000004168; -.
DR BindingDB; Q60484; -.
DR ChEMBL; CHEMBL2304407; -.
DR GeneID; 100379622; -.
DR KEGG; cpoc:100379622; -.
DR CTD; 3352; -.
DR eggNOG; KOG3656; Eukaryota.
DR HOGENOM; CLU_009579_11_1_1; -.
DR InParanoid; Q60484; -.
DR OrthoDB; 703991at2759; -.
DR TreeFam; TF316350; -.
DR PRO; PR:Q60484; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
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:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007268; P:chemical synaptic transmission; IEA:InterPro.
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 3: Inferred from homology;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..376
FT /note="5-hydroxytryptamine receptor 1D"
FT /id="PRO_0000068926"
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..301
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 302..325
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 326..334
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 335..359
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 360..376
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 135..137
FT /note="DRY motif; important for ligand-induced conformation
FT changes"
FT /evidence="ECO:0000250"
FT MOTIF 351..355
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"
FT CONFLICT 222
FT /note="R -> A (in Ref. 2; AAB58499)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 376 AA; 41769 MW; 531D4E1C2C819035 CRC64;
MSPPNQSEEG LPQEASNRSL NATETPGDWD PGLLQALKVS LVVVLSIITL ATVLSNAFVL
TTILLTRKLH TPANYLIGSL ATTDLLVSIL VMPISIAYTT TRTWNFGQIL CDIWVSSDIT
CCTASILHLC VIALDRYWAI TDALEYSKRR TAGHAGAMIA AVWVISICIS IPPLFWRQAQ
AQEEMSDCLV NTSQISYTIY STCGAFYIPS VLLIILYSRI YRAARSRILN PPSLSGKRFT
TAHLITGSAG SSLCSLNPSL HEGHMHPGSP LFFNHVRIKL ADSVLERKRI SAARERKATK
TLGIILGAFI VCWLPFFVVS LVLPICRDSC WIHPALFDFF TWLGYLNSLI NPIIYTVFNE
DFRQAFQKVV HFRKAS
