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   27-MAR-2024, entry version 158.
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   GlyCosmos; P28565; 3 sites, No reported glycans.
DR   GlyGen; P28565; 3 sites.
DR   PhosphoSitePlus; P28565; -.
DR   PaxDb; 10116-ENSRNOP00000016047; -.
DR   Ensembl; ENSRNOT00000016046.3; ENSRNOP00000016047.1; ENSRNOG00000012038.3.
DR   Ensembl; ENSRNOT00055042452; ENSRNOP00055034668; ENSRNOG00055024659.
DR   Ensembl; ENSRNOT00060055687; ENSRNOP00060046050; ENSRNOG00060032149.
DR   Ensembl; ENSRNOT00065038164; ENSRNOP00065030897; ENSRNOG00065022383.
DR   GeneID; 25323; -.
DR   KEGG; rno:25323; -.
DR   UCSC; RGD:2847; rat.
DR   AGR; RGD:2847; -.
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; VWMISIS; -.
DR   OrthoDB; 2999405at2759; -.
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 cell types or tissues.
DR   GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0098992; C:neuronal dense core vesicle; IDA:SynGO.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
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:2000300; P:regulation of synaptic vesicle exocytosis; IDA:SynGO.
DR   GO; GO:0009636; P:response to toxic substance; ISO:RGD.
DR   GO; GO:0042310; P:vasoconstriction; IEA:InterPro.
DR   CDD; cd15333; 7tmA_5-HT1B_1D; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR000505; 5HT1D_rcpt.
DR   InterPro; IPR002231; 5HT_rcpt.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   PANTHER; PTHR24248; ADRENERGIC RECEPTOR-RELATED G-PROTEIN COUPLED RECEPTOR; 1.
DR   PANTHER; PTHR24248:SF191; G-PROTEIN COUPLED RECEPTORS FAMILY 1 PROFILE DOMAIN-CONTAINING PROTEIN; 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   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR   Genevisible; P28565; RN.
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
//