ID 5HT1A_HUMAN Reviewed; 422 AA. AC P08908; Q6LAE7; DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 3. DT 27-MAR-2024, entry version 208. DE RecName: Full=5-hydroxytryptamine receptor 1A; DE Short=5-HT-1A; DE Short=5-HT1A; DE AltName: Full=G-21; DE AltName: Full=Serotonin receptor 1A; GN Name=HTR1A; Synonyms=ADRB2RL1, ADRBRL1; 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], TISSUE SPECIFICITY, AND SUBCELLULAR RP LOCATION. RX PubMed=3041227; DOI=10.1038/329075a0; RA Kobilka B.K., Frielle T., Collins S., Yang-Feng T.L., Kobilka T.S., RA Francke U., Lefkowitz R.J., Caron M.G.; RT "An intronless gene encoding a potential member of the family of receptors RT coupled to guanine nucleotide regulatory proteins."; RL Nature 329:75-79(1987). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Saltzman A.G., Morse B., Felder S.; RT "Nucleotide and deduced amino acid sequence of the human serotonin 5-HT1a RT receptor gene."; RL Submitted (FEB-1991) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Levy F.O., Gudermann T., Birnbaumer M., Kaumann A.J., Birnbaumer L.; RL Submitted (MAY-1992) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=15014171; DOI=10.1093/molbev/msh100; RA Kitano T., Liu Y.-H., Ueda S., Saitou N.; RT "Human-specific amino acid changes found in 103 protein-coding genes."; RL Mol. Biol. Evol. 21:936-944(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9. RX PubMed=1766875; DOI=10.1093/nar/19.25.7155; RA Parks C.L., Chang L.S., Shenk T.; RT "A polymerase chain reaction mediated by a single primer: cloning of RT genomic sequences adjacent to a serotonin receptor protein coding region."; RL Nucleic Acids Res. 19:7155-7160(1991). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 200-365, FUNCTION, SUBCELLULAR LOCATION, AND RP TISSUE SPECIFICITY. RX PubMed=8393041; RA Aune T.M., McGrath K.M., Sarr T., Bombara M.P., Kelley K.A.; RT "Expression of 5HT1a receptors on activated human T cells. Regulation of RT cyclic AMP levels and T cell proliferation by 5-hydroxytryptamine."; RL J. Immunol. 151:1175-1183(1993). RN [9] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=3138543; DOI=10.1038/335358a0; RA Fargin A., Raymond J.R., Lohse M.L., Kobilka B.K., Caron M.G., RA Lefkowitz R.J.; RT "The genomic clone G-21 which resembles a beta-adrenergic receptor sequence RT encodes the 5-HT1A receptor."; RL Nature 335:358-360(1988). RN [10] RP FUNCTION. RX PubMed=8138923; RA Harrington M.A., Shaw K., Zhong P., Ciaranello R.D.; RT "Agonist-induced desensitization and loss of high-affinity binding sites of RT stably expressed human 5-HT1A receptors."; RL J. Pharmacol. Exp. Ther. 268:1098-1106(1994). RN [11] 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 [12] RP REVIEW. RX PubMed=20363322; DOI=10.1016/j.cellsig.2010.03.019; RA Polter A.M., Li X.; RT "5-HT1A receptor-regulated signal transduction pathways in brain."; RL Cell. Signal. 22:1406-1412(2010). RN [13] 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 [14] RP INVOLVEMENT IN PFMC. RX PubMed=21990073; DOI=10.1002/humu.21622; RA Jiang Y.C., Wu H.M., Cheng K.H., Sunny Sun H.; RT "Menstrual cycle-dependent febrile episode mediated by sequence-specific RT repression of poly(ADP-ribose) polymerase-1 on the transcription of the RT human serotonin receptor 1A gene."; RL Hum. Mutat. 33:209-217(2012). RN [15] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=22957663; DOI=10.1111/jnc.12008; RA Singh P., Paila Y.D., Chattopadhyay A.; RT "Role of glycosphingolipids in the function of human serotonin(1)A RT receptors."; RL J. Neurochem. 123:716-724(2012). RN [16] RP SUBUNIT. RX PubMed=23300088; DOI=10.1074/jbc.m112.412478; RA Akama K.T., Thompson L.I., Milner T.A., McEwen B.S.; RT "Post-synaptic density-95 (PSD-95) binding capacity of G-protein-coupled RT receptor 30 (GPR30), an estrogen receptor that can be identified in RT hippocampal dendritic spines."; RL J. Biol. Chem. 288:6438-6450(2013). RN [17] RP VARIANTS SER-22 AND VAL-28. RX PubMed=7755630; DOI=10.1006/bbrc.1995.1692; RA Nakhai B., Nielsen D.A., Linnoila M., Goldman D.; RT "Two naturally occurring amino acid substitutions in the human 5-HT1A RT receptor: glycine 22 to serine 22 and isoleucine 28 to valine 28."; RL Biochem. Biophys. Res. Commun. 210:530-536(1995). RN [18] RP SUBCELLULAR LOCATION, AND INTERACTION WITH GRP39 AND GALR1. RX PubMed=26365466; DOI=10.1016/j.bbadis.2015.09.003; RA Tena-Campos M., Ramon E., Borroto-Escuela D.O., Fuxe K., Garriga P.; RT "The zinc binding receptor GPR39 interacts with 5-HT1A and GalR1 to form RT dynamic heteroreceptor complexes with signaling diversity."; RL Biochim. Biophys. Acta 1852:2585-2592(2015). RN [19] RP VARIANTS LEU-16 AND ASP-273. RX PubMed=9754630; RX DOI=10.1002/(sici)1096-8628(19980907)81:5<434::aid-ajmg13>3.0.co;2-d; RA Kawanishi Y., Harada S., Tachikawa H., Okubo T., Shiraishi H.; RT "Novel mutations in the promoter and coding region of the human 5-HT1A RT receptor gene and association analysis in schizophrenia."; RL Am. J. Med. Genet. 81:434-439(1998). CC -!- FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine CC (serotonin). Also functions as a receptor for various drugs 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. Beta-arrestin family members inhibit signaling via G CC proteins and mediate activation of alternative signaling pathways. CC Signaling inhibits adenylate cyclase activity and activates a CC phosphatidylinositol-calcium second messenger system that regulates the CC release of Ca(2+) ions from intracellular stores. Plays a role in the CC regulation of 5-hydroxytryptamine release and in the regulation of CC dopamine and 5-hydroxytryptamine metabolism. Plays a role in the CC regulation of dopamine and 5-hydroxytryptamine levels in the brain, and CC thereby affects neural activity, mood and behavior. Plays a role in the CC response to anxiogenic stimuli. {ECO:0000269|PubMed:22957663, CC ECO:0000269|PubMed:3138543, ECO:0000269|PubMed:8138923, CC ECO:0000269|PubMed:8393041}. CC -!- SUBUNIT: Heterodimer; heterodimerizes with GPER1. Interacts with YIF1B CC (By similarity). Interacts with GPR39 and GALR1 (PubMed:26365466). CC {ECO:0000250|UniProtKB:P19327, ECO:0000269|PubMed:23300088, CC ECO:0000269|PubMed:26365466}. CC -!- INTERACTION: CC P08908; P11362: FGFR1; NbExp=9; IntAct=EBI-6570214, EBI-1028277; CC P08908; O43194: GPR39; NbExp=4; IntAct=EBI-6570214, EBI-7165599; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22957663, CC ECO:0000269|PubMed:26365466, ECO:0000269|PubMed:3041227, CC ECO:0000269|PubMed:3138543, ECO:0000269|PubMed:8393041}; Multi-pass CC membrane protein {ECO:0000269|PubMed:22957663, CC ECO:0000269|PubMed:3041227, ECO:0000269|PubMed:3138543, CC ECO:0000269|PubMed:8393041}. Cell projection, dendrite CC {ECO:0000250|UniProtKB:P19327}. CC -!- TISSUE SPECIFICITY: Detected in lymph nodes, thymus and spleen. CC Detected in activated T-cells, but not in resting T-cells. CC {ECO:0000269|PubMed:3041227, ECO:0000269|PubMed:8393041}. CC -!- DISEASE: Periodic fever, menstrual cycle-dependent (PFMC) [MIM:614674]: CC A condition characterized by recurrent fevers up to 40 degrees Celsius CC associated with the luteal phase of the menstrual cycle. Women show CC menstrual cycle-dependent physiologic changes in relation to sex CC hormone levels. Because ovulation triggers a significant change in the CC hormonal milieu that is similar to local inflammation, a 0.5 to 1.0 CC degree Celsius increase in basal body temperature after ovulation is CC commonly associated with progesterone secretion and is believed to be CC triggered by the induction of several inflammatory cytokines. CC {ECO:0000269|PubMed:21990073}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. 5- CC hydroxytryptamine receptor subfamily. HTR1A sub-subfamily. 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; M28269; AAA36440.1; -; Genomic_DNA. DR EMBL; X13556; CAA31908.1; -; Genomic_DNA. DR EMBL; X57829; CAA40962.1; -; Genomic_DNA. DR EMBL; M83181; AAA66493.1; -; Genomic_DNA. DR EMBL; AB041403; BAA94488.1; -; Genomic_DNA. DR EMBL; AF498978; AAM21125.1; -; mRNA. DR EMBL; BC069159; AAH69159.1; -; mRNA. DR EMBL; Z11168; CAA77560.1; -; Genomic_DNA. DR CCDS; CCDS34168.1; -. DR PIR; I38209; I38209. DR RefSeq; NP_000515.2; NM_000524.3. DR PDB; 7E2X; EM; 3.00 A; R=25-422. DR PDB; 7E2Y; EM; 3.00 A; R=25-422. DR PDB; 7E2Z; EM; 3.10 A; R=25-422. DR PDB; 8JSP; EM; 3.65 A; R=35-415. DR PDB; 8W8B; EM; 3.00 A; R=22-422. DR PDBsum; 7E2X; -. DR PDBsum; 7E2Y; -. DR PDBsum; 7E2Z; -. DR PDBsum; 8JSP; -. DR PDBsum; 8W8B; -. DR AlphaFoldDB; P08908; -. DR EMDB; EMD-36626; -. DR EMDB; EMD-37351; -. DR SMR; P08908; -. DR BioGRID; 109582; 28. DR CORUM; P08908; -. DR IntAct; P08908; 6. DR STRING; 9606.ENSP00000316244; -. DR BindingDB; P08908; -. DR ChEMBL; CHEMBL214; -. DR DrugBank; DB14010; 5-methoxy-N,N-dimethyltryptamine. DR DrugBank; DB01614; Acepromazine. DR DrugBank; DB00866; Alprenolol. DR DrugBank; DB01616; Alverine. DR DrugBank; DB00321; Amitriptyline. DR DrugBank; DB00543; Amoxapine. DR DrugBank; DB00714; Apomorphine. DR DrugBank; DB01238; Aripiprazole. DR DrugBank; DB14185; Aripiprazole lauroxil. DR DrugBank; DB06216; Asenapine. DR DrugBank; DB04888; Bifeprunox. DR DrugBank; DB08807; Bopindolol. DR DrugBank; DB09128; Brexpiprazole. DR DrugBank; DB01200; Bromocriptine. DR DrugBank; DB00490; Buspirone. DR DrugBank; DB00248; Cabergoline. DR DrugBank; DB09061; Cannabidiol. DR DrugBank; DB06016; Cariprazine. DR DrugBank; DB00477; Chlorpromazine. DR DrugBank; DB01239; Chlorprothixene. DR DrugBank; DB08810; Cinitapride. DR DrugBank; DB00363; Clozapine. DR DrugBank; DB04884; Dapoxetine. DR DrugBank; DB01151; Desipramine. DR DrugBank; DB11273; Dihydroergocornine. DR DrugBank; DB13345; Dihydroergocristine. DR DrugBank; DB00320; Dihydroergotamine. DR DrugBank; DB00988; Dopamine. DR DrugBank; DB09167; Dosulepin. DR DrugBank; DB06446; Dotarizine. DR DrugBank; DB01142; Doxepin. DR DrugBank; DB00216; Eletriptan. DR DrugBank; DB01049; Ergoloid mesylate. DR DrugBank; DB00696; Ergotamine. DR DrugBank; DB01175; Escitalopram. DR DrugBank; DB00574; Fenfluramine. DR DrugBank; DB04908; Flibanserin. DR DrugBank; DB12141; Gilteritinib. DR DrugBank; DB00502; Haloperidol. DR DrugBank; DB04946; Iloperidone. DR DrugBank; DB00458; Imipramine. DR DrugBank; DB01221; Ketamine. DR DrugBank; DB12540; Lecozotan. DR DrugBank; DB04970; Lesopitron. DR DrugBank; DB05509; LI-301. DR DrugBank; DB00589; Lisuride. DR DrugBank; DB04948; Lofexidine. DR DrugBank; DB00408; Loxapine. DR DrugBank; DB08815; Lurasidone. DR DrugBank; DB04829; Lysergic acid diethylamide. DR DrugBank; DB14009; Medical Cannabis. DR DrugBank; DB00422; Methylphenidate. DR DrugBank; DB00247; Methysergide. DR DrugBank; DB06148; Mianserin. DR DrugBank; DB05339; MN-305. DR DrugBank; DB01618; Molindone. DR DrugBank; DB14011; Nabiximols. DR DrugBank; DB05562; Naluzotan. DR DrugBank; DB00952; Naratriptan. DR DrugBank; DB01149; Nefazodone. DR DrugBank; DB00540; Nortriptyline. DR DrugBank; DB00334; Olanzapine. DR DrugBank; DB00904; Ondansetron. DR DrugBank; DB00935; Oxymetazoline. DR DrugBank; DB01267; Paliperidone. DR DrugBank; DB12061; Pardoprunox. DR DrugBank; DB00715; Paroxetine. DR DrugBank; DB01359; Penbutolol. DR DrugBank; DB01186; Pergolide. DR DrugBank; DB08922; Perospirone. DR DrugBank; DB00960; Pindolol. DR DrugBank; DB01621; Pipotiazine. DR DrugBank; DB09244; Pirlindole. DR DrugBank; DB06153; Pizotifen. DR DrugBank; DB00413; Pramipexole. DR DrugBank; DB00571; Propranolol. DR DrugBank; DB01224; Quetiapine. DR DrugBank; DB06506; Repinotan. DR DrugBank; DB00734; Risperidone. DR DrugBank; DB06538; Robalzotan. DR DrugBank; DB05271; Rotigotine. DR DrugBank; DB06454; Sarizotan. DR DrugBank; DB15665; SEP-363856. DR DrugBank; DB16629; Serdexmethylphenidate. DR DrugBank; DB09304; Setiptiline. DR DrugBank; DB00669; Sumatriptan. DR DrugBank; DB11755; Tetrahydrocannabivarin. DR DrugBank; DB09289; Tianeptine. DR DrugBank; DB13025; Tiapride. DR DrugBank; DB00656; Trazodone. DR DrugBank; DB00726; Trimipramine. DR DrugBank; DB06684; Vilazodone. DR DrugBank; DB09068; Vortioxetine. DR DrugBank; DB06393; Xaliproden. DR DrugBank; DB01392; Yohimbine. DR DrugBank; DB00246; Ziprasidone. DR DrugBank; DB00315; Zolmitriptan. DR DrugCentral; P08908; -. DR GuidetoPHARMACOLOGY; 1; -. DR TCDB; 9.A.14.3.14; the g-protein-coupled receptor (gpcr) family. DR GlyCosmos; P08908; 3 sites, No reported glycans. DR GlyGen; P08908; 5 sites, 1 O-linked glycan (2 sites). DR iPTMnet; P08908; -. DR PhosphoSitePlus; P08908; -. DR SwissPalm; P08908; -. DR BioMuta; HTR1A; -. DR DMDM; 231454; -. DR MassIVE; P08908; -. DR PaxDb; 9606-ENSP00000316244; -. DR PeptideAtlas; P08908; -. DR ProteomicsDB; 52173; -. DR Antibodypedia; 2959; 367 antibodies from 39 providers. DR DNASU; 3350; -. DR Ensembl; ENST00000323865.5; ENSP00000316244.4; ENSG00000178394.5. DR GeneID; 3350; -. DR KEGG; hsa:3350; -. DR MANE-Select; ENST00000323865.5; ENSP00000316244.4; NM_000524.4; NP_000515.2. DR AGR; HGNC:5286; -. DR CTD; 3350; -. DR DisGeNET; 3350; -. DR GeneCards; HTR1A; -. DR HGNC; HGNC:5286; HTR1A. DR HPA; ENSG00000178394; Group enriched (brain, ovary). DR MalaCards; HTR1A; -. DR MIM; 109760; gene. DR MIM; 614674; phenotype. DR neXtProt; NX_P08908; -. DR OpenTargets; ENSG00000178394; -. DR Orphanet; 498251; Menstrual cycle-dependent periodic fever. DR PharmGKB; PA192; -. DR VEuPathDB; HostDB:ENSG00000178394; -. DR eggNOG; KOG3656; Eukaryota. DR GeneTree; ENSGT00940000154484; -. DR HOGENOM; CLU_009579_11_1_1; -. DR InParanoid; P08908; -. DR OMA; CAESCYM; -. DR OrthoDB; 2999405at2759; -. DR PhylomeDB; P08908; -. DR TreeFam; TF316350; -. DR PathwayCommons; P08908; -. DR Reactome; R-HSA-390666; Serotonin receptors. DR SignaLink; P08908; -. DR SIGNOR; P08908; -. DR BioGRID-ORCS; 3350; 9 hits in 1151 CRISPR screens. DR GenomeRNAi; 3350; -. DR Pharos; P08908; Tclin. DR PRO; PR:P08908; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; P08908; Protein. DR Bgee; ENSG00000178394; Expressed in entorhinal cortex and 48 other cell types or tissues. DR ExpressionAtlas; P08908; baseline and differential. 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; IDA:UniProtKB. DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central. DR GO; GO:0090722; F:receptor-receptor interaction; IDA:ParkinsonsUK-UCL. DR GO; GO:0051378; F:serotonin binding; IBA:GO_Central. DR GO; GO:0007198; P:adenylate cyclase-inhibiting serotonin receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0001662; P:behavioral fear response; ISS:UniProtKB. DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central. DR GO; GO:0035640; P:exploration behavior; ISS:UniProtKB. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:UniProtKB. DR GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; IBA:GO_Central. DR GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IEA:Ensembl. DR GO; GO:0008284; P:positive regulation of cell population proliferation; TAS:ProtInc. DR GO; GO:0050795; P:regulation of behavior; IEA:InterPro. DR GO; GO:0042053; P:regulation of dopamine metabolic process; ISS:UniProtKB. DR GO; GO:0046883; P:regulation of hormone secretion; IEA:InterPro. DR GO; GO:0014062; P:regulation of serotonin secretion; ISS:UniProtKB. DR GO; GO:0019229; P:regulation of vasoconstriction; IEA:InterPro. DR GO; GO:0042428; P:serotonin metabolic process; ISS:UniProtKB. DR GO; GO:0007210; P:serotonin receptor signaling pathway; ISS:UniProtKB. DR CDD; cd15330; 7tmA_5-HT1A_vertebrates; 1. DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1. DR InterPro; IPR000610; 5HT1A_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; PR00512; 5HT1ARECEPTR. 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; P08908; HS. PE 1: Evidence at protein level; KW 3D-structure; Behavior; Cell membrane; Cell projection; Disulfide bond; KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor; KW Reference proteome; Transducer; Transmembrane; Transmembrane helix. FT CHAIN 1..422 FT /note="5-hydroxytryptamine receptor 1A" FT /id="PRO_0000068903" FT TOPO_DOM 1..36 FT /note="Extracellular" FT /evidence="ECO:0000250" FT TRANSMEM 37..62 FT /note="Helical; Name=1" FT /evidence="ECO:0000250" FT TOPO_DOM 63..73 FT /note="Cytoplasmic" FT /evidence="ECO:0000250" FT TRANSMEM 74..98 FT /note="Helical; Name=2" FT /evidence="ECO:0000250" FT TOPO_DOM 99..110 FT /note="Extracellular" FT /evidence="ECO:0000250" FT TRANSMEM 111..132 FT /note="Helical; Name=3" FT /evidence="ECO:0000250" FT TOPO_DOM 133..152 FT /note="Cytoplasmic" FT /evidence="ECO:0000250" FT TRANSMEM 153..178 FT /note="Helical; Name=4" FT /evidence="ECO:0000250" FT TOPO_DOM 179..191 FT /note="Extracellular" FT /evidence="ECO:0000250" FT TRANSMEM 192..217 FT /note="Helical; Name=5" FT /evidence="ECO:0000250" FT TOPO_DOM 218..345 FT /note="Cytoplasmic" FT /evidence="ECO:0000250" FT TRANSMEM 346..367 FT /note="Helical; Name=6" FT /evidence="ECO:0000250" FT TOPO_DOM 368..378 FT /note="Extracellular" FT /evidence="ECO:0000250" FT TRANSMEM 379..403 FT /note="Helical; Name=7" FT /evidence="ECO:0000250" FT TOPO_DOM 404..422 FT /note="Cytoplasmic" FT /evidence="ECO:0000250" FT REGION 1..23 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 235..262 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 133..135 FT /note="DRY motif; important for ligand-induced conformation FT changes" FT /evidence="ECO:0000250" FT MOTIF 396..400 FT /note="NPxxY motif; important for ligand-induced FT conformation changes and signaling" FT /evidence="ECO:0000250" FT BINDING 116 FT /ligand="ergotamine" FT /ligand_id="ChEBI:CHEBI:190463" FT /ligand_note="agonist" FT /evidence="ECO:0000250|UniProtKB:P28222" FT BINDING 121 FT /ligand="ergotamine" FT /ligand_id="ChEBI:CHEBI:190463" FT /ligand_note="agonist" FT /evidence="ECO:0000250|UniProtKB:P28222" FT BINDING 189 FT /ligand="ergotamine" FT /ligand_id="ChEBI:CHEBI:190463" FT /ligand_note="agonist" FT /evidence="ECO:0000250|UniProtKB:P28222" FT CARBOHYD 10 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 11 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 24 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 109..187 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521" FT VARIANT 16 FT /note="P -> L (in dbSNP:rs1800041)" FT /evidence="ECO:0000269|PubMed:9754630" FT /id="VAR_003446" FT VARIANT 22 FT /note="G -> S (in dbSNP:rs1799920)" FT /evidence="ECO:0000269|PubMed:7755630" FT /id="VAR_011826" FT VARIANT 28 FT /note="I -> V (in dbSNP:rs1799921)" FT /evidence="ECO:0000269|PubMed:7755630" FT /id="VAR_011827" FT VARIANT 184 FT /note="P -> L (in dbSNP:rs1800043)" FT /id="VAR_011828" FT VARIANT 220 FT /note="R -> L (in dbSNP:rs1800044)" FT /id="VAR_011829" FT VARIANT 273 FT /note="G -> D (in dbSNP:rs1800042)" FT /evidence="ECO:0000269|PubMed:9754630" FT /id="VAR_011830" FT CONFLICT 152..154 FT /note="RAA -> PR (in Ref. 1; AAA36440/CAA31908)" FT /evidence="ECO:0000305" FT CONFLICT 172 FT /note="M -> I (in Ref. 1; AAA36440/CAA31908)" FT /evidence="ECO:0000305" FT CONFLICT 200..202 FT /note="TFG -> RPR (in Ref. 8; no nucleotide entry)" FT /evidence="ECO:0000305" FT CONFLICT 228 FT /note="K -> R (in Ref. 8; no nucleotide entry)" FT /evidence="ECO:0000305" FT CONFLICT 244 FT /note="A -> AA (in Ref. 8; no nucleotide entry)" FT /evidence="ECO:0000305" FT CONFLICT 355 FT /note="I -> T (in Ref. 8; no nucleotide entry)" FT /evidence="ECO:0000305" FT CONFLICT 363..365 FT /note="IVA -> MRP (in Ref. 8; no nucleotide entry)" FT /evidence="ECO:0000305" FT CONFLICT 418 FT /note="K -> N (in Ref. 1; AAA36440/CAA31908)" FT /evidence="ECO:0000305" FT HELIX 36..63 FT /evidence="ECO:0007829|PDB:7E2X" FT HELIX 65..67 FT /evidence="ECO:0007829|PDB:7E2X" FT HELIX 70..99 FT /evidence="ECO:0007829|PDB:7E2X" FT HELIX 106..139 FT /evidence="ECO:0007829|PDB:7E2X" FT HELIX 141..146 FT /evidence="ECO:0007829|PDB:7E2X" FT HELIX 150..173 FT /evidence="ECO:0007829|PDB:7E2X" FT HELIX 193..203 FT /evidence="ECO:0007829|PDB:7E2X" FT HELIX 205..227 FT /evidence="ECO:0007829|PDB:7E2X" FT HELIX 325..367 FT /evidence="ECO:0007829|PDB:7E2X" FT HELIX 368..370 FT /evidence="ECO:0007829|PDB:7E2X" FT HELIX 372..374 FT /evidence="ECO:0007829|PDB:7E2Z" FT HELIX 379..400 FT /evidence="ECO:0007829|PDB:7E2X" FT STRAND 402..404 FT /evidence="ECO:0007829|PDB:7E2X" FT HELIX 405..414 FT /evidence="ECO:0007829|PDB:7E2X" SQ SEQUENCE 422 AA; 46107 MW; 762664FCF62CFD8F CRC64; MDVLSPGQGN NTTSPPAPFE TGGNTTGISD VTVSYQVITS LLLGTLIFCA VLGNACVVAA IALERSLQNV ANYLIGSLAV TDLMVSVLVL PMAALYQVLN KWTLGQVTCD LFIALDVLCC TSSILHLCAI ALDRYWAITD PIDYVNKRTP RRAAALISLT WLIGFLISIP PMLGWRTPED RSDPDACTIS KDHGYTIYST FGAFYIPLLL MLVLYGRIFR AARFRIRKTV KKVEKTGADT RHGASPAPQP KKSVNGESGS RNWRLGVESK AGGALCANGA VRQGDDGAAL EVIEVHRVGN SKEHLPLPSE AGPTPCAPAS FERKNERNAE AKRKMALARE RKTVKTLGII MGTFILCWLP FFIVALVLPF CESSCHMPTL LGAIINWLGY SNSLLNPVIY AYFNKDFQNA FKKIIKCKFC RQ //