5HT1A_HUMAN
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 03-AUG-2022, entry version 199.
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 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). {ECO:0000250|UniProtKB:P19327,
CC ECO:0000269|PubMed:23300088}.
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:3041227, ECO:0000269|PubMed:3138543,
CC ECO:0000269|PubMed:8393041}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:22957663, ECO:0000269|PubMed:3041227,
CC ECO:0000269|PubMed:3138543, ECO:0000269|PubMed:8393041}. Cell
CC projection, dendrite {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}.
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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 PDBsum; 7E2X; -.
DR PDBsum; 7E2Y; -.
DR PDBsum; 7E2Z; -.
DR AlphaFoldDB; P08908; -.
DR SMR; P08908; -.
DR BioGRID; 109582; 7.
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; 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 GlyGen; P08908; 3 sites.
DR iPTMnet; P08908; -.
DR PhosphoSitePlus; P08908; -.
DR SwissPalm; P08908; -.
DR BioMuta; HTR1A; -.
DR DMDM; 231454; -.
DR MassIVE; P08908; -.
DR PaxDb; P08908; -.
DR PeptideAtlas; P08908; -.
DR PRIDE; P08908; -.
DR ProteomicsDB; 52173; -.
DR Antibodypedia; 2959; 333 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 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; 703991at2759; -.
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; 8 hits in 1067 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 tissues.
DR ExpressionAtlas; P08908; baseline and differential.
DR Genevisible; P08908; HS.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
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 InterPro; IPR000610; 5HT1A_rcpt.
DR InterPro; IPR002231; 5HT_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR24247:SF20; PTHR24247:SF20; 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 PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
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
