ID 5HT1A_RAT Reviewed; 422 AA.
AC P19327;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 27-MAR-2024, entry version 166.
DE RecName: Full=5-hydroxytryptamine receptor 1A {ECO:0000305};
DE Short=5-HT-1A;
DE Short=5-HT1A;
DE AltName: Full=Serotonin receptor 1A;
GN Name=Htr1a {ECO:0000312|RGD:2845}; Synonyms=5ht1a;
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=2156831; DOI=10.1016/s0021-9258(19)39437-2;
RA Albert P.R., Zhou Q.-Y., van Tol H.H.M., Bunzow J.R., Civelli O.;
RT "Cloning, functional expression, and mRNA tissue distribution of the rat 5-
RT hydroxytryptamine1A receptor gene.";
RL J. Biol. Chem. 265:5825-5832(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2167416; DOI=10.1016/0024-3205(90)90225-g;
RA Fujiwara Y., Nelson D.L., Kashihara K., Varga E., Roeske W.R.,
RA Yamamura H.I.;
RT "Role of cytochrome P450 in the control of the production of
RT erythropoietin.";
RL Life Sci. 47:127-134(1990).
RN [3]
RP FUNCTION.
RX PubMed=2140514; DOI=10.1016/0896-6273(90)90201-p;
RA Penington N.J., Kelly J.S.;
RT "Serotonin receptor activation reduces calcium current in an acutely
RT dissociated adult central neuron.";
RL Neuron 4:751-758(1990).
RN [4]
RP TISSUE SPECIFICITY, INTERACTION WITH YIF1B, AND SUBCELLULAR LOCATION.
RX PubMed=18685031; DOI=10.1523/jneurosci.4487-07.2008;
RA Carrel D., Masson J., Al Awabdh S., Capra C.B., Lenkei Z., Hamon M.,
RA Emerit M.B., Darmon M.;
RT "Targeting of the 5-HT1A serotonin receptor to neuronal dendrites is
RT mediated by Yif1B.";
RL J. Neurosci. 28:8063-8073(2008).
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:2140514,
CC ECO:0000269|PubMed:2156831}.
CC -!- SUBUNIT: Heterodimer; heterodimerizes with GPER1. Interacts with YIF1B
CC (PubMed:18685031). Interacts with GPR39 and GALR1 (By similarity).
CC {ECO:0000250|UniProtKB:P08908, ECO:0000269|PubMed:18685031}.
CC -!- INTERACTION:
CC P19327; Q04589: Fgfr1; NbExp=5; IntAct=EBI-6570156, EBI-2480918;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2156831};
CC Multi-pass membrane protein {ECO:0000269|PubMed:2156831}. Cell
CC projection, dendrite {ECO:0000269|PubMed:18685031}.
CC -!- TISSUE SPECIFICITY: Detected in hypothalamus, mesencephalon, amygdala,
CC medulla, thalamus, septum and hippocampus.
CC {ECO:0000269|PubMed:18685031, ECO:0000269|PubMed:2156831}.
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; J05276; AAA40612.1; -; Genomic_DNA.
DR PIR; JH0315; JH0315.
DR RefSeq; NP_036717.1; NM_012585.1.
DR AlphaFoldDB; P19327; -.
DR SMR; P19327; -.
DR IntAct; P19327; 2.
DR STRING; 10116.ENSRNOP00000013618; -.
DR BindingDB; P19327; -.
DR ChEMBL; CHEMBL273; -.
DR DrugCentral; P19327; -.
DR GuidetoPHARMACOLOGY; 1; -.
DR GlyCosmos; P19327; 3 sites, No reported glycans.
DR GlyGen; P19327; 3 sites.
DR iPTMnet; P19327; -.
DR PhosphoSitePlus; P19327; -.
DR PaxDb; 10116-ENSRNOP00000013618; -.
DR GeneID; 24473; -.
DR KEGG; rno:24473; -.
DR UCSC; RGD:2845; rat.
DR AGR; RGD:2845; -.
DR CTD; 3350; -.
DR RGD; 2845; Htr1a.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; P19327; -.
DR OrthoDB; 2999405at2759; -.
DR PhylomeDB; P19327; -.
DR Reactome; R-RNO-390666; Serotonin receptors.
DR PRO; PR:P19327; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0043203; C:axon hillock; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0042734; C:presynaptic membrane; IDA:SynGO.
DR GO; GO:0004993; F:G protein-coupled serotonin receptor activity; IDA:RGD.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; IPI:RGD.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0090722; F:receptor-receptor interaction; ISO:RGD.
DR GO; GO:0051378; F:serotonin binding; IDA:RGD.
DR GO; GO:0005102; F:signaling receptor binding; IPI:RGD.
DR GO; GO:0007198; P:adenylate cyclase-inhibiting serotonin receptor signaling pathway; IMP:RGD.
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; ISO:RGD.
DR GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; IBA:GO_Central.
DR GO; GO:0098664; P:G protein-coupled serotonin receptor signaling pathway; ISO:RGD.
DR GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; ISO:RGD.
DR GO; GO:0014053; P:negative regulation of gamma-aminobutyric acid secretion; IMP:CACAO.
DR GO; GO:0097114; P:NMDA glutamate receptor clustering; IDA:RGD.
DR GO; GO:0031117; P:positive regulation of microtubule depolymerization; IDA:RGD.
DR GO; GO:0099171; P:presynaptic modulation of chemical synaptic transmission; IDA:SynGO.
DR GO; GO:0042053; P:regulation of dopamine metabolic process; ISS:UniProtKB.
DR GO; GO:0060259; P:regulation of feeding behavior; IDA:RGD.
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; IMP:RGD.
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.
PE 1: Evidence at protein level;
KW 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_0000068907"
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 235..261
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 COMPBIAS 239..253
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 CONFLICT 373
FT /note="S -> N (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 422 AA; 46429 MW; 19C2731834C4BBC9 CRC64;
MDVFSFGQGN NTTASQEPFG TGGNVTSISD VTFSYQVITS LLLGTLIFCA VLGNACVVAA
IALERSLQNV ANYLIGSLAV TDLMVSVLVL PMAALYQVLN KWTLGQVTCD LFIALDVLCC
TSSILHLCAI ALDRYWAITD PIDYVNKRTP RRAAALISLT WLIGFLISIP PMLGWRTPED
RSDPDACTIS KDHGYTIYST FGAFYIPLLL MLVLYGRIFR AARFRIRKTV RKVEKKGAGT
SLGTSSAPPP KKSLNGQPGS GDWRRCAENR AVGTPCTNGA VRQGDDEATL EVIEVHRVGN
SKEHLPLPSE SGSNSYAPAC LERKNERNAE AKRKMALARE RKTVKTLGII MGTFILCWLP
FFIVALVLPF CESSCHMPAL LGAIINWLGY SNSLLNPVIY AYFNKDFQNA FKKIIKCKFC
RR
//
