5HT1D_RAT
ID 5HT1D_RAT Reviewed; 374 AA.
AC P28565;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 149.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=19912901; DOI=10.1016/1044-7431(92)90070-i;
RA Hamblin M.W., McGuffin R.W., Metcalf M.A., Dorsa D.M., Merchant K.M.;
RT "Distinct 5-HT1B and 5-HT1D serotonin receptors in rat: structural and
RT pharmacological comparison of the two cloned receptors.";
RL Mol. Cell. Neurosci. 3:578-587(1992).
RN [2]
RP FUNCTION, AND SUBCELLULAR LOCATION.
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).
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:19912901, ECO:0000269|PubMed:8978753}.
CC -!- SUBUNIT: Homodimer. Heterodimer with HTR1B (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19912901,
CC ECO:0000269|PubMed:8978753}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:19912901, ECO:0000269|PubMed:8978753}.
CC -!- TISSUE SPECIFICITY: Detected in dorsal raphe.
CC {ECO:0000269|PubMed:19912901}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; M89953; AAA40614.1; -; Genomic_DNA.
DR PIR; I77467; I77467.
DR RefSeq; NP_036984.1; NM_012852.1.
DR RefSeq; XP_008762430.1; XM_008764208.2.
DR RefSeq; XP_017448642.1; XM_017593153.1.
DR RefSeq; XP_017448643.1; XM_017593154.1.
DR RefSeq; XP_017448644.1; XM_017593155.1.
DR RefSeq; XP_017448645.1; XM_017593156.1.
DR RefSeq; XP_017448646.1; XM_017593157.1.
DR RefSeq; XP_017448647.1; XM_017593158.1.
DR AlphaFoldDB; P28565; -.
DR SMR; P28565; -.
DR STRING; 10116.ENSRNOP00000016047; -.
DR BindingDB; P28565; -.
DR ChEMBL; CHEMBL5450; -.
DR DrugCentral; P28565; -.
DR GuidetoPHARMACOLOGY; 3; -.
DR GlyGen; P28565; 3 sites.
DR PhosphoSitePlus; P28565; -.
DR PaxDb; P28565; -.
DR PRIDE; P28565; -.
DR Ensembl; ENSRNOT00000016046; ENSRNOP00000016047; ENSRNOG00000012038.
DR GeneID; 25323; -.
DR KEGG; rno:25323; -.
DR UCSC; RGD:2847; rat.
DR CTD; 3352; -.
DR RGD; 2847; Htr1d.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01010000222287; -.
DR HOGENOM; CLU_009579_11_1_1; -.
DR InParanoid; P28565; -.
DR OMA; YTAFNEE; -.
DR OrthoDB; 703991at2759; -.
DR PhylomeDB; P28565; -.
DR TreeFam; TF316350; -.
DR Reactome; R-RNO-390666; Serotonin receptors.
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR PRO; PR:P28565; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000012038; Expressed in brain and 2 other tissues.
DR Genevisible; P28565; RN.
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; ISO:RGD.
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:0014827; P:intestine smooth muscle contraction; ISO:RGD.
DR GO; GO:0050795; P:regulation of behavior; IEA:InterPro.
DR GO; GO:0040012; P:regulation of locomotion; IEA:InterPro.
DR GO; GO:0009636; P:response to toxic substance; ISO:RGD.
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..374
FT /note="5-hydroxytryptamine receptor 1D"
FT /id="PRO_0000068931"
FT TOPO_DOM 1..35
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 36..61
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 62..72
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 73..95
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 96..109
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 110..131
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 132..151
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 152..173
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 174..191
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 192..214
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 215..299
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 300..323
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 324..332
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 333..357
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 358..374
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT MOTIF 132..134
FT /note="DRY motif; important for ligand-induced conformation
FT changes"
FT /evidence="ECO:0000250"
FT MOTIF 349..353
FT /note="NPxxY motif; important for ligand-induced
FT conformation changes and signaling"
FT /evidence="ECO:0000250"
FT BINDING 115
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P28222"
FT BINDING 120
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P28222"
FT BINDING 187
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 108..185
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 374 AA; 41540 MW; 345CBD528317DA21 CRC64;
MSLPNQSLEG LPQEASNRSL NATGAWDPEV LQALRISLVV VLSIITLATV LSNAFVLTTI
LLTKKLHTPA NYLIGSLATT DLLVSILVMP ISIAYTTTRT WNFGQILCDI WVSSDITCCT
ASILHLCVIA LDRYWAITDA LEYSKRRTAG HAAAMIAAVW AISICISIPP LFWRQATAHE
EMSDCLVNTS QISYTIYSTC GAFYIPSILL IILYGRIYVA ARSRILNPPS LYGKRFTTAQ
LITGSAGSSL CSLNPSLHES HTHTVGSPLF FNQVKIKLAD SILERKRISA ARERKATKTL
GIILGAFIIC WLPFFVVSLV LPICRDSCWI HPALFDFFTW LGYLNSLINP VIYTVFNEDF
RQAFQRVVHF RKAS
