ID   5HT1D_HUMAN             Reviewed;         377 AA.
AC   P28221;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   02-SEP-2026, entry version 204.
DE   RecName: Full=5-hydroxytryptamine receptor 1D {ECO:0000303|PubMed:1652050};
DE            Short=5-HT-1D {ECO:0000303|PubMed:1652050};
DE            Short=5-HT1D {ECO:0000303|PubMed:1652050};
DE   AltName: Full=Serotonin 1D alpha receptor {ECO:0000303|PubMed:1652050};
DE            Short=5-HT-1D-alpha {ECO:0000303|PubMed:1652050};
DE   AltName: Full=Serotonin receptor 1D {ECO:0000303|PubMed:1652050};
GN   Name=HTR1D {ECO:0000312|HGNC:HGNC:5289}; Synonyms=HTR1DA, HTRL;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=1652050; DOI=10.1016/s0026-895x(25)12918-0;
RA   Hamblin M.W., Metcalf M.A.;
RT   "Primary structure and functional characterization of a human 5-HT1D-type
RT   serotonin receptor.";
RL   Mol. Pharmacol. 40:143-148(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC   TISSUE=Placenta;
RX   PubMed=1565658; DOI=10.1073/pnas.89.8.3630;
RA   Weinshank R.L., Zgombick J.M., Macchi M.J., Branchek T.A., Hartig P.R.;
RT   "Human serotonin 1D receptor is encoded by a subfamily of two distinct
RT   genes: 5-HT1D alpha and 5-HT1D beta.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:3630-3634(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT   "cDNA clones of human proteins involved in signal transduction sequenced by
RT   the Guthrie cDNA resource center (www.cdna.org).";
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   TISSUE SPECIFICITY.
RX   PubMed=1828434; DOI=10.1016/0014-4886(91)90142-y;
RA   Gonzalez-Heydrich J., Peroutka S.J.;
RT   "Postsynaptic localization of 5-HT1D receptor binding sites in human
RT   caudate.";
RL   Exp. Neurol. 113:28-30(1991).
RN   [8]
RP   FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=10452531; DOI=10.1016/s0014-5793(99)00918-7;
RA   Xie Z., Lee S.P., O'Dowd B.F., George S.R.;
RT   "Serotonin 5-HT1B and 5-HT1D receptors form homodimers when expressed alone
RT   and heterodimers when co-expressed.";
RL   FEBS Lett. 456:63-67(1999).
RN   [9]
RP   REVIEW.
RX   PubMed=18476671; DOI=10.1021/cr078224o;
RA   Nichols D.E., Nichols C.D.;
RT   "Serotonin receptors.";
RL   Chem. Rev. 108:1614-1641(2008).
RN   [10]
RP   REVIEW.
RX   PubMed=20945968; DOI=10.33549/physiolres.931903;
RA   Pytliak M., Vargova V., Mechirova V., Felsoci M.;
RT   "Serotonin receptors - from molecular biology to clinical applications.";
RL   Physiol. Res. 60:15-25(2011).
RN   [11] {ECO:0007744|PDB:7E32}
RP   STRUCTURE BY ELECTRON MICROSCOPY (2.99 ANGSTROMS) OF 2-377 IN COMPLEX WITH
RP   SEROTONON; GNB1; GNG2 AND GNAI1, DISULFIDE BOND, AND FUNCTION.
RX   PubMed=33762731; DOI=10.1038/s41586-021-03376-8;
RA   Xu P., Huang S., Zhang H., Mao C., Zhou X.E., Cheng X., Simon I.A.,
RA   Shen D.D., Yen H.Y., Robinson C.V., Harpsoee K., Svensson B., Guo J.,
RA   Jiang H., Gloriam D.E., Melcher K., Jiang Y., Zhang Y., Xu H.E.;
RT   "Structural insights into the lipid and ligand regulation of serotonin
RT   receptors.";
RL   Nature 592:469-473(2021).
RN   [12]
RP   VARIANT LEU-265.
RX   PubMed=10391209; DOI=10.1038/10290;
RA   Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
RA   Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
RA   Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
RA   Lander E.S.;
RT   "Characterization of single-nucleotide polymorphisms in coding regions of
RT   human genes.";
RL   Nat. Genet. 22:231-238(1999).
RN   [13]
RP   ERRATUM OF PUBMED:10391209.
RA   Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
RA   Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
RA   Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
RA   Lander E.S.;
RL   Nat. Genet. 23:373-373(1999).
CC   -!- FUNCTION: G protein-coupled receptor for 5-hydroxytryptamine
CC       (serotonin) (PubMed:10452531, PubMed:1565658, PubMed:1652050,
CC       PubMed:33762731). Also functions as a receptor for ergot alkaloid
CC       derivatives, various anxiolytic and antidepressant drugs and other
CC       psychoactive substances (PubMed:10452531, PubMed:1565658,
CC       PubMed:1652050, PubMed:33762731). Ligand binding causes a conformation
CC       change that triggers signaling via guanine nucleotide-binding proteins
CC       (G proteins) and modulates the activity of downstream effectors, such
CC       as adenylate cyclase (PubMed:10452531, PubMed:1565658, PubMed:1652050,
CC       PubMed:33762731). HTR1D is coupled to G(i)/G(o) G alpha proteins and
CC       mediates inhibitory neurotransmission by inhibiting adenylate cyclase
CC       activity (PubMed:33762731). Regulates the release of 5-
CC       hydroxytryptamine in the brain, and thereby affects neural activity
CC       (PubMed:18476671, PubMed:20945968). May also play a role in regulating
CC       the release of other neurotransmitters (PubMed:18476671,
CC       PubMed:20945968). May play a role in vasoconstriction (PubMed:18476671,
CC       PubMed:20945968). {ECO:0000269|PubMed:10452531,
CC       ECO:0000269|PubMed:1565658, ECO:0000269|PubMed:1652050,
CC       ECO:0000269|PubMed:33762731, ECO:0000303|PubMed:18476671,
CC       ECO:0000303|PubMed:20945968}.
CC   -!- SUBUNIT: Homodimer. Heterodimer with HTR1B.
CC       {ECO:0000269|PubMed:10452531}.
CC   -!- INTERACTION:
CC       P28221; O60896: RAMP3; NbExp=2; IntAct=EBI-67111268, EBI-720447;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10452531,
CC       ECO:0000269|PubMed:1565658, ECO:0000269|PubMed:1652050}; Multi-pass
CC       membrane protein {ECO:0000269|PubMed:10452531,
CC       ECO:0000269|PubMed:1565658, ECO:0000269|PubMed:1652050}.
CC   -!- TISSUE SPECIFICITY: Detected in brain neocortex and caudate nucleus (at
CC       protein level). {ECO:0000269|PubMed:1828434}.
CC   -!- SIMILARITY: Belongs to the G protein-coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; M89955; AAA35491.1; -; Genomic_DNA.
DR   EMBL; M81589; AAA60315.1; -; mRNA.
DR   EMBL; AF498979; AAM21126.1; -; mRNA.
DR   EMBL; BT007027; AAP35673.1; -; mRNA.
DR   EMBL; AL049576; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC007720; AAH07720.1; -; mRNA.
DR   CCDS; CCDS231.1; -.
DR   PIR; A53279; A53279.
DR   RefSeq; NP_000855.1; NM_000864.5.
DR   PDB; 7E32; EM; 2.90 A; R=2-377.
DR   AlphaFoldDB; P28221; -.
DR   EMDB; EMD-30974; -.
DR   SMR; P28221; -.
DR   BioGRID; 109584; 3.
DR   CORUM; P28221; -.
DR   FunCoup; P28221; 920.
DR   IntAct; P28221; 3.
DR   NDEx; IQUERY-CP-HTR1D; 5 NDEx IQuery Curated Pathways.
DR   STRING; 9606.ENSP00000363748; -.
DR   BindingDB; P28221; -.
DR   ChEMBL; CHEMBL1983; -.
DR   DrugBank; DB01465; 2,5-Dimethoxyamphetamine.
DR   DrugBank; DB00918; Almotriptan.
DR   DrugBank; DB20494; Alniditan.
DR   DrugBank; DB00321; Amitriptyline.
DR   DrugBank; DB00714; Apomorphine.
DR   DrugBank; DB01238; Aripiprazole.
DR   DrugBank; DB14185; Aripiprazole lauroxil.
DR   DrugBank; DB20150; Avitriptan.
DR   DrugBank; DB01484; Brolamfetamine.
DR   DrugBank; DB01200; Bromocriptine.
DR   DrugBank; DB01445; Bufotenine.
DR   DrugBank; DB00248; Cabergoline.
DR   DrugBank; DB01239; Chlorprothixene.
DR   DrugBank; DB00363; Clozapine.
DR   DrugBank; DB11273; Dihydroergocornine.
DR   DrugBank; DB13345; Dihydroergocristine.
DR   DrugBank; DB00320; Dihydroergotamine.
DR   DrugBank; DB20163; Donitriptan.
DR   DrugBank; DB00216; Eletriptan.
DR   DrugBank; DB01049; Ergoloid mesylate.
DR   DrugBank; DB00696; Ergotamine.
DR   DrugBank; DB19706; Etisulergine.
DR   DrugBank; DB00574; Fenfluramine.
DR   DrugBank; DB00998; Frovatriptan.
DR   DrugBank; DB01221; Ketamine.
DR   DrugBank; DB12540; Lecozotan.
DR   DrugBank; DB00589; Lisuride.
DR   DrugBank; DB04948; Lofexidine.
DR   DrugBank; DB00408; Loxapine.
DR   DrugBank; DB12110; m-Chlorophenylpiperazine.
DR   DrugBank; DB13520; Metergoline.
DR   DrugBank; DB00952; Naratriptan.
DR   DrugBank; DB06096; NXN-188.
DR   DrugBank; DB00334; Olanzapine.
DR   DrugBank; DB00935; Oxymetazoline.
DR   DrugBank; DB01267; Paliperidone.
DR   DrugBank; DB01186; Pergolide.
DR   DrugBank; DB12288; Piromelatine.
DR   DrugBank; DB01224; Quetiapine.
DR   DrugBank; DB19963; Quipazine.
DR   DrugBank; DB00734; Risperidone.
DR   DrugBank; DB00953; Rizatriptan.
DR   DrugBank; DB08839; Serotonin.
DR   DrugBank; DB09304; Setiptiline.
DR   DrugBank; DB00669; Sumatriptan.
DR   DrugBank; DB13025; Tiapride.
DR   DrugBank; DB20677; Tidembersat.
DR   DrugBank; DB06578; Tonabersat.
DR   DrugBank; DB00726; Trimipramine.
DR   DrugBank; DB01392; Yohimbine.
DR   DrugBank; DB00246; Ziprasidone.
DR   DrugBank; DB00315; Zolmitriptan.
DR   DrugCentral; P28221; -.
DR   GuidetoPHARMACOLOGY; 3; -.
DR   GlyCosmos; P28221; 3 sites, No reported glycans.
DR   GlyGen; P28221; 3 sites.
DR   iPTMnet; P28221; -.
DR   PhosphoSitePlus; P28221; -.
DR   BioMuta; HTR1D; -.
DR   DMDM; 112819; -.
DR   PaxDb; 9606-ENSP00000363748; -.
DR   Antibodypedia; 15559; 228 antibodies from 31 providers.
DR   DNASU; 3352; -.
DR   Ensembl; ENST00000374619.2; ENSP00000363748.1; ENSG00000179546.6.
DR   Ensembl; ENST00000918575.1; ENSP00000588634.1; ENSG00000179546.6.
DR   Ensembl; ENST00000918576.1; ENSP00000588635.1; ENSG00000179546.6.
DR   Ensembl; ENST00000918577.1; ENSP00000588636.1; ENSG00000179546.6.
DR   Ensembl; ENST00000918578.1; ENSP00000588637.1; ENSG00000179546.6.
DR   Ensembl; ENST00000918579.1; ENSP00000588638.1; ENSG00000179546.6.
DR   Ensembl; ENST00000918580.1; ENSP00000588639.1; ENSG00000179546.6.
DR   Ensembl; ENST00000918581.1; ENSP00000588640.1; ENSG00000179546.6.
DR   Ensembl; ENST00000918582.1; ENSP00000588641.1; ENSG00000179546.6.
DR   Ensembl; ENST00000918583.1; ENSP00000588642.1; ENSG00000179546.6.
DR   Ensembl; ENST00000918584.1; ENSP00000588643.1; ENSG00000179546.6.
DR   Ensembl; ENST00000918585.1; ENSP00000588644.1; ENSG00000179546.6.
DR   Ensembl; ENST00000918586.1; ENSP00000588645.1; ENSG00000179546.6.
DR   GeneID; 3352; -.
DR   KEGG; hsa:3352; -.
DR   MANE-Select; ENST00000374619.2; ENSP00000363748.1; NM_000864.5; NP_000855.1.
DR   UCSC; uc001bgn.3; human.
DR   AGR; HGNC:5289; -.
DR   ClinPGx; PA29550; -.
DR   CTD; 3352; -.
DR   DisGeNET; 3352; -.
DR   GeneCards; HTR1D; -.
DR   HGNC; HGNC:5289; HTR1D.
DR   HPA; ENSG00000179546; Group enriched (brain, intestine).
DR   MIM; 182133; gene.
DR   OpenTargets; ENSG00000179546; -.
DR   VEuPathDB; HostDB:ENSG00000179546; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT00940000154484; -.
DR   HOGENOM; CLU_009579_11_1_1; -.
DR   InParanoid; P28221; -.
DR   OMA; VWMISIS; -.
DR   OrthoDB; 5956310at2759; -.
DR   PAN-GO; P28221; 7 GO annotations based on evolutionary models.
DR   PhylomeDB; P28221; -.
DR   PathwayCommons; P28221; -.
DR   Reactome; R-HSA-390666; Serotonin receptors.
DR   Reactome; R-HSA-418594; G alpha (i) signalling events.
DR   SignaLink; P28221; -.
DR   SIGNOR; P28221; -.
DR   Agora; ENSG00000179546; -.
DR   BioGRID-ORCS; 3352; 8 hits in 1156 CRISPR screens.
DR   GeneWiki; 5-HT1D_receptor; -.
DR   GenomeRNAi; 3352; -.
DR   Pharos; P28221; Tclin.
DR   PRO; PR:P28221; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; P28221; protein.
DR   Bgee; ENSG00000179546; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 57 other cell types or tissues.
DR   GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0045202; C:synapse; IEA:GOC.
DR   GO; GO:0004993; F:G protein-coupled serotonin receptor activity; IMP:UniProtKB.
DR   GO; GO:0001586; F:Gi/o-coupled serotonin receptor activity; IDA:UniProtKB.
DR   GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR   GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IMP:UniProtKB.
DR   GO; GO:0007198; P:adenylate cyclase-inhibiting serotonin receptor signaling pathway; IDA:UniProtKB.
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; IMP:UniProtKB.
DR   GO; GO:0050795; P:regulation of behavior; IEA:InterPro.
DR   GO; GO:0040012; P:regulation of locomotion; IEA:InterPro.
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.
DR   PDBsum; 7E32; -.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Disulfide bond; G protein-coupled receptor;
KW   Glycoprotein; Membrane; Receptor; Reference proteome; Transducer;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..377
FT                   /note="5-hydroxytryptamine receptor 1D"
FT                   /id="PRO_0000068927"
FT   TOPO_DOM        1..38
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000269|PubMed:33762731,
FT                   ECO:0007744|PDB:7E32"
FT   TRANSMEM        39..64
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000269|PubMed:33762731,
FT                   ECO:0007744|PDB:7E32"
FT   TOPO_DOM        65..75
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:33762731,
FT                   ECO:0007744|PDB:7E32"
FT   TRANSMEM        76..97
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000269|PubMed:33762731,
FT                   ECO:0007744|PDB:7E32"
FT   TOPO_DOM        98..109
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000269|PubMed:33762731,
FT                   ECO:0007744|PDB:7E32"
FT   TRANSMEM        110..134
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000269|PubMed:33762731,
FT                   ECO:0007744|PDB:7E32"
FT   TOPO_DOM        135..154
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:33762731,
FT                   ECO:0007744|PDB:7E32"
FT   TRANSMEM        155..176
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000269|PubMed:33762731,
FT                   ECO:0007744|PDB:7E32"
FT   TOPO_DOM        177..194
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000269|PubMed:33762731,
FT                   ECO:0007744|PDB:7E32"
FT   TRANSMEM        195..218
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000269|PubMed:33762731,
FT                   ECO:0007744|PDB:7E32"
FT   TOPO_DOM        219..300
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:33762731,
FT                   ECO:0007744|PDB:7E32"
FT   TRANSMEM        301..326
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000269|PubMed:33762731,
FT                   ECO:0007744|PDB:7E32"
FT   TOPO_DOM        327..335
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000269|PubMed:33762731,
FT                   ECO:0007744|PDB:7E32"
FT   TRANSMEM        336..359
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000269|PubMed:33762731,
FT                   ECO:0007744|PDB:7E32"
FT   TOPO_DOM        360..377
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:33762731,
FT                   ECO:0007744|PDB:7E32"
FT   REGION          1..23
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|UniProtKB:P41595"
FT   MOTIF           352..356
FT                   /note="NPxxY motif; important for ligand-induced
FT                   conformation changes and signaling"
FT                   /evidence="ECO:0000250|UniProtKB:P41595"
FT   BINDING         118
FT                   /ligand="serotonin"
FT                   /ligand_id="ChEBI:CHEBI:350546"
FT                   /evidence="ECO:0000269|PubMed:33762731,
FT                   ECO:0007744|PDB:7E32"
FT   BINDING         122
FT                   /ligand="serotonin"
FT                   /ligand_id="ChEBI:CHEBI:350546"
FT                   /evidence="ECO:0000269|PubMed:33762731,
FT                   ECO:0007744|PDB:7E32"
FT   BINDING         321
FT                   /ligand="serotonin"
FT                   /ligand_id="ChEBI:CHEBI:350546"
FT                   /evidence="ECO:0000269|PubMed:33762731,
FT                   ECO:0007744|PDB:7E32"
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                   ECO:0000269|PubMed:33762731, ECO:0007744|PDB:7E32"
FT   VARIANT         265
FT                   /note="S -> L (in dbSNP:rs6299)"
FT                   /evidence="ECO:0000269|PubMed:10391209"
FT                   /id="VAR_011834"
FT   HELIX           36..65
FT                   /evidence="ECO:0007829|PDB:7E32"
FT   HELIX           67..69
FT                   /evidence="ECO:0007829|PDB:7E32"
FT   HELIX           72..86
FT                   /evidence="ECO:0007829|PDB:7E32"
FT   HELIX           87..91
FT                   /evidence="ECO:0007829|PDB:7E32"
FT   HELIX           92..101
FT                   /evidence="ECO:0007829|PDB:7E32"
FT   HELIX           107..141
FT                   /evidence="ECO:0007829|PDB:7E32"
FT   HELIX           143..149
FT                   /evidence="ECO:0007829|PDB:7E32"
FT   HELIX           152..170
FT                   /evidence="ECO:0007829|PDB:7E32"
FT   HELIX           172..176
FT                   /evidence="ECO:0007829|PDB:7E32"
FT   HELIX           195..202
FT                   /evidence="ECO:0007829|PDB:7E32"
FT   HELIX           203..207
FT                   /evidence="ECO:0007829|PDB:7E32"
FT   HELIX           208..229
FT                   /evidence="ECO:0007829|PDB:7E32"
FT   HELIX           285..326
FT                   /evidence="ECO:0007829|PDB:7E32"
FT   STRAND          328..330
FT                   /evidence="ECO:0007829|PDB:7E32"
FT   HELIX           335..358
FT                   /evidence="ECO:0007829|PDB:7E32"
FT   HELIX           361..370
FT                   /evidence="ECO:0007829|PDB:7E32"
SQ   SEQUENCE   377 AA;  41907 MW;  0A4FCF81FFE2322A CRC64;
     MSPLNQSAEG LPQEASNRSL NATETSEAWD PRTLQALKIS LAVVLSVITL ATVLSNAFVL
     TTILLTRKLH TPANYLIGSL ATTDLLVSIL VMPISIAYTI THTWNFGQIL CDIWLSSDIT
     CCTASILHLC VIALDRYWAI TDALEYSKRR TAGHAATMIA IVWAISICIS IPPLFWRQAK
     AQEEMSDCLV NTSQISYTIY STCGAFYIPS VLLIILYGRI YRAARNRILN PPSLYGKRFT
     TAHLITGSAG SSLCSLNSSL HEGHSHSAGS PLFFNHVKIK LADSALERKR ISAARERKAT
     KILGIILGAF IICWLPFFVV SLVLPICRDS CWIHPALFDF FTWLGYLNSL INPIIYTVFN
     EEFRQAFQKI VPFRKAS
//