5HT1E_PIG
ID 5HT1E_PIG Reviewed; 149 AA.
AC Q29003;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=5-hydroxytryptamine receptor 1E;
DE Short=5-HT-1E;
DE Short=5-HT1E;
DE AltName: Full=Serotonin receptor 1E;
DE Flags: Fragment;
GN Name=HTR1E;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7656980; DOI=10.1016/0014-5793(95)00828-w;
RA Ullmer C., Schmuck K., Kalkman H.O., Luebbert H.;
RT "Expression of serotonin receptor mRNAs in blood vessels.";
RL FEBS Lett. 370:215-221(1995).
CC -!- FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine
CC (serotonin). Also functions as a receptor for various alkaloids 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. Signaling inhibits adenylate cyclase activity (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; Z48151; CAA88168.1; -; Genomic_DNA.
DR PIR; S66490; S66490.
DR AlphaFoldDB; Q29003; -.
DR SMR; Q29003; -.
DR STRING; 9823.ENSSSCP00000022846; -.
DR PaxDb; Q29003; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; Q29003; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0004993; F:G protein-coupled serotonin receptor activity; ISS:UniProtKB.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0051378; F:serotonin binding; IBA:GO_Central.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007198; P:adenylate cyclase-inhibiting serotonin receptor signaling pathway; IBA:GO_Central.
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 InterPro; IPR027425; 5HT1E_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR24247:SF33; PTHR24247:SF33; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 3: Inferred from homology;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Membrane;
KW Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN <1..>149
FT /note="5-hydroxytryptamine receptor 1E"
FT /id="PRO_0000068935"
FT TOPO_DOM <1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 7..29
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 30..43
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 44..65
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 66..85
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 86..106
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 107..126
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 127..149
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT MOTIF 66..68
FT /note="DRY motif; important for ligand-induced conformation
FT changes"
FT /evidence="ECO:0000250"
FT BINDING 49
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P28222"
FT BINDING 54
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P28222"
FT BINDING 122
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P28222"
FT DISULFID 42..120
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT NON_TER 1
FT NON_TER 149
SQ SEQUENCE 149 AA; 17116 MW; 67BCFEE083E41721 CRC64;
HQPANYLICS LAVTDLLVAV LVMPLSIMYI VMDSWRLGYF ICEVWLSVDM TCCTCSILHL
CVIALDRYWA ITNAIEYARK RTAKRAGLMI LTVWTISIFI SMPPLFWRSH RQLSPPPSQC
AIQHDHVIYT IYSTLGAFYI PLTLILILY
