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   02-SEP-2026, entry version 167.
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) (PubMed:19912901, PubMed:8978753). Also functions as a
CC       receptor for ergot alkaloid derivatives, various anxiolytic and
CC       antidepressant drugs and other psychoactive substances (By similarity).
CC       Ligand binding causes a conformation change that triggers signaling via
CC       guanine nucleotide-binding proteins (G proteins) and modulates the
CC       activity of downstream effectors, such as adenylate cyclase (By
CC       similarity). HTR1D is coupled to G(i)/G(o) G alpha proteins and
CC       mediates inhibitory neurotransmission by inhibiting adenylate cyclase
CC       activity (By similarity). Regulates the release of 5-hydroxytryptamine
CC       in the brain, and thereby affects neural activity (By similarity). May
CC       also play a role in regulating the release of other neurotransmitters
CC       (By similarity). May play a role in vasoconstriction (By similarity).
CC       {ECO:0000250|UniProtKB:P28221, ECO:0000269|PubMed:19912901,
CC       ECO:0000269|PubMed:8978753}.
CC   -!- SUBUNIT: Homodimer. Heterodimer with HTR1B.
CC       {ECO:0000250|UniProtKB:P28221}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19912901,
CC       ECO:0000269|PubMed:8978753}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:P28221}.
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_012852.2.
DR   AlphaFoldDB; P28565; -.
DR   SMR; P28565; -.
DR   FunCoup; P28565; 184.
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; ENSRNOT00000016046.4; ENSRNOP00000016047.1; ENSRNOG00000012038.4.
DR   Ensembl; ENSRNOT00000171476.1; ENSRNOP00000104073.1; ENSRNOG00000012038.4.
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; 5956310at2759; -.
DR   PhylomeDB; P28565; -.
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   ExpressionAtlas; P28565; baseline and differential.
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; EXP:UniProtKB.
DR   GO; GO:0004993; F:G protein-coupled serotonin receptor activity; ISS:UniProtKB.
DR   GO; GO:0001586; F:Gi/o-coupled serotonin receptor activity; ISO:RGD.
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; ISO:RGD.
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:SF196; 5-HYDROXYTRYPTAMINE RECEPTOR 1D; 1.
DR   PANTHER; PTHR24248; ADRENERGIC RECEPTOR-RELATED G-PROTEIN COUPLED RECEPTOR; 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.
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   TRANSMEM        36..61
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000250|UniProtKB:P28221"
FT   TRANSMEM        73..94
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000250|UniProtKB:P28221"
FT   TRANSMEM        107..131
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000250|UniProtKB:P28221"
FT   TRANSMEM        152..173
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000250|UniProtKB:P28221"
FT   TRANSMEM        192..215
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000250|UniProtKB:P28221"
FT   TRANSMEM        298..323
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250|UniProtKB:P28221"
FT   TRANSMEM        333..356
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000250|UniProtKB:P28221"
FT   MOTIF           132..134
FT                   /note="DRY motif; important for ligand-induced conformation
FT                   changes"
FT                   /evidence="ECO:0000250|UniProtKB:P41595"
FT   MOTIF           349..353
FT                   /note="NPxxY motif; important for ligand-induced
FT                   conformation changes and signaling"
FT                   /evidence="ECO:0000250|UniProtKB:P41595"
FT   BINDING         115
FT                   /ligand="serotonin"
FT                   /ligand_id="ChEBI:CHEBI:350546"
FT                   /evidence="ECO:0000250|UniProtKB:P28221"
FT   BINDING         119
FT                   /ligand="serotonin"
FT                   /ligand_id="ChEBI:CHEBI:350546"
FT                   /evidence="ECO:0000250|UniProtKB:P28221"
FT   BINDING         318
FT                   /ligand="serotonin"
FT                   /ligand_id="ChEBI:CHEBI:350546"
FT                   /evidence="ECO:0000250|UniProtKB:P28221"
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
//