5HT1D_PIG
ID 5HT1D_PIG Reviewed; 291 AA.
AC P79400;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=5-hydroxytryptamine receptor 1D;
DE Short=5-HT-1D;
DE Short=5-HT1D;
DE AltName: Full=Serotonin receptor 1D;
DE Flags: Fragment;
GN Name=HTR1D;
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 [MRNA].
RC TISSUE=Brain cortex;
RA Wurch T., Lestienne F., Colpaert F.C., Pauwels P.J.;
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
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.
CC Regulates the release of 5-hydroxytryptamine in the brain, and thereby
CC affects neural activity. May also play a role in regulating the release
CC of other neurotransmitters. May play a role in vasoconstriction (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Heterodimer with HTR1B (By similarity).
CC {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; Y11868; CAA72616.1; -; mRNA.
DR AlphaFoldDB; P79400; -.
DR SMR; P79400; -.
DR STRING; 9823.ENSSSCP00000020202; -.
DR BindingDB; P79400; -.
DR ChEMBL; CHEMBL4105; -.
DR DrugCentral; P79400; -.
DR PaxDb; P79400; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; P79400; -.
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 GO; GO:0050795; P:regulation of behavior; IEA:InterPro.
DR GO; GO:0040012; P:regulation of locomotion; IEA:InterPro.
DR GO; GO:0006939; P:smooth muscle contraction; IEA:InterPro.
DR GO; GO:0042310; P:vasoconstriction; IEA:InterPro.
DR InterPro; IPR000505; 5HT1D_rcpt.
DR InterPro; IPR002231; 5HT_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR24247:SF17; PTHR24247:SF17; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00514; 5HT1DRECEPTR.
DR PRINTS; PR01101; 5HTRECEPTOR.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN <1..>291
FT /note="5-hydroxytryptamine receptor 1D"
FT /id="PRO_0000068929"
FT TRANSMEM <1..18
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 19..32
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 33..54
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 55..74
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 75..96
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 97..114
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 115..137
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 138..222
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 223..246
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 247..255
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 256..280
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 281..>291
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT MOTIF 55..57
FT /note="DRY motif; important for ligand-induced conformation
FT changes"
FT /evidence="ECO:0000250"
FT MOTIF 272..276
FT /note="NPxxY motif; important for ligand-induced
FT conformation changes and signaling"
FT /evidence="ECO:0000250"
FT BINDING 38
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P28222"
FT BINDING 43
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P28222"
FT BINDING 110
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P28222"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 31..108
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT NON_TER 1
FT NON_TER 291
SQ SEQUENCE 291 AA; 32669 MW; 71E798F3652651CB CRC64;
AMTDLLVSIL VMPISIPYTI TQTWSFGQLL CDIWLSSDIT CCTASILHLC VIALDRYWAI
TDALEYSKRR TAGHAAAMIA IVWAISICIS IPPLFWRQAR AHEEISDCLV NTSQISYTIY
STCGAFYIPS LLLIILYGRI YRAARNRILN PPSLYGKRFT TAHLITGSAG SSLCSLNPSL
HEGHSHSAGS PLFFNHVKIK LADSVLERKR ISAARERKAT KTLGIILGAF IICWLPFFVA
SLVLPICRDS CWIHPALFDF FTWLGYLNSL INPIIYTVFN EEFRQAFQKV V
