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   26-FEB-2020, entry version 188.
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.
CC       {ECO:0000269|PubMed:23300088}.
CC   -!- INTERACTION:
CC       P11362:FGFR1; NbExp=9; IntAct=EBI-6570214, EBI-1028277;
CC       P47211:GALR1; NbExp=4; IntAct=EBI-6570214, EBI-6624741;
CC       O43194:GPR39; NbExp=4; IntAct=EBI-6570214, EBI-7165599;
CC       P28223:HTR2A; NbExp=3; IntAct=EBI-6570214, EBI-6656333;
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}.
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 mutations
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   BioGrid; 109582; 6.
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; DB08810; Cinitapride.
DR   DrugBank; DB00363; Clozapine.
DR   DrugBank; DB04884; Dapoxetine.
DR   DrugBank; DB01151; Desipramine.
DR   DrugBank; DB11273; Dihydroergocornine.
DR   DrugBank; DB13345; Dihydroergocristine.
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; DB04908; Flibanserin.
DR   DrugBank; DB12141; Gilteritinib.
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; DB01267; Paliperidone.
DR   DrugBank; DB12061; Pardoprunox.
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; DB09304; Setiptiline.
DR   DrugBank; DB00669; Sumatriptan.
DR   DrugBank; DB11755; Tetrahydrocannabivarin.
DR   DrugBank; DB01622; Thioproperazine.
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   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   DNASU; 3350; -.
DR   Ensembl; ENST00000323865; ENSP00000316244; ENSG00000178394.
DR   GeneID; 3350; -.
DR   KEGG; hsa:3350; -.
DR   CTD; 3350; -.
DR   DisGeNET; 3350; -.
DR   GeneCards; HTR1A; -.
DR   HGNC; HGNC:5286; HTR1A.
DR   HPA; HPA018073; -.
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   eggNOG; KOG3656; Eukaryota.
DR   eggNOG; ENOG410XRW9; LUCA.
DR   GeneTree; ENSGT00940000154484; -.
DR   HOGENOM; CLU_009579_11_1_1; -.
DR   InParanoid; P08908; -.
DR   KO; K04153; -.
DR   OMA; DPGYTIY; -.
DR   OrthoDB; 703991at2759; -.
DR   PhylomeDB; P08908; -.
DR   TreeFam; TF316350; -.
DR   Reactome; R-HSA-390666; Serotonin receptors.
DR   Reactome; R-HSA-418594; G alpha (i) signalling events.
DR   SIGNOR; P08908; -.
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 temporal lobe and 22 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:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
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:0008283; P:cell population proliferation; IEA:InterPro.
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: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:0042428; P:serotonin metabolic process; ISS:UniProtKB.
DR   GO; GO:0007210; P:serotonin receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0042310; P:vasoconstriction; IEA:InterPro.
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   Behavior; Cell membrane; Disulfide bond; G-protein coupled receptor;
KW   Glycoprotein; Membrane; Polymorphism; Receptor; Reference proteome;
KW   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          112..121
FT                   /note="Agonist binding"
FT                   /evidence="ECO:0000250"
FT   REGION          358..362
FT                   /note="Agonist binding"
FT                   /evidence="ECO:0000250"
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   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"
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
//