5HT1D_RABIT
ID 5HT1D_RABIT Reviewed; 377 AA.
AC P49145; O02823;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=5-hydroxytryptamine receptor 1D;
DE Short=5-HT-1D;
DE Short=5-HT1D;
DE AltName: Full=5-HT-1D-alpha;
DE AltName: Full=Serotonin receptor 1D;
GN Name=HTR1D;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Liver;
RX PubMed=8543023; DOI=10.1016/0014-5793(95)01308-3;
RA Harwood G.S., Lockyer M., Giles H., Fairweather N.;
RT "Cloning and characterisation of the rabbit 5-HT1D alpha and 5-HT1D beta
RT receptors.";
RL FEBS Lett. 377:73-76(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=New Zealand white;
RX PubMed=8878052; DOI=10.1007/bf00171053;
RA Bard J.A., Kucharewicz S.A., Zgombick J.M., Weinshank R.L., Branchek T.A.,
RA Cohen M.L.;
RT "Differences in ligand binding profiles between cloned rabbit and human 5-
RT HT1D alpha and 5-HT1D beta receptors: ketanserin and methiothepin
RT distinguish rabbit 5-HT1D receptor subtypes.";
RL Naunyn Schmiedebergs Arch. Pharmacol. 354:237-244(1996).
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, ECO:0000269|PubMed:8543023,
CC ECO:0000269|PubMed:8878052}.
CC -!- SUBUNIT: Homodimer. Heterodimer with HTR1B (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8543023,
CC ECO:0000269|PubMed:8878052}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:8543023, ECO:0000269|PubMed:8878052}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z50162; CAA90530.1; -; Genomic_DNA.
DR EMBL; U60825; AAB58466.1; -; Genomic_DNA.
DR PIR; S68423; S68423.
DR RefSeq; NP_001164624.1; NM_001171153.1.
DR RefSeq; XP_017201009.1; XM_017345520.1.
DR RefSeq; XP_017201010.1; XM_017345521.1.
DR RefSeq; XP_017201011.1; XM_017345522.1.
DR RefSeq; XP_017201013.1; XM_017345524.1.
DR AlphaFoldDB; P49145; -.
DR SMR; P49145; -.
DR STRING; 9986.ENSOCUP00000009551; -.
DR PRIDE; P49145; -.
DR Ensembl; ENSOCUT00000011099; ENSOCUP00000009551; ENSOCUG00000011102.
DR GeneID; 100328964; -.
DR KEGG; ocu:100328964; -.
DR CTD; 3352; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01010000222287; -.
DR HOGENOM; CLU_009579_11_1_1; -.
DR InParanoid; P49145; -.
DR OMA; YTAFNEE; -.
DR OrthoDB; 703991at2759; -.
DR TreeFam; TF316350; -.
DR Proteomes; UP000001811; Chromosome 13.
DR Bgee; ENSOCUG00000011102; Expressed in adult mammalian kidney and 2 other tissues.
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:0051378; F:serotonin binding; IEA:Ensembl.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007268; P:chemical synaptic transmission; IEA:InterPro.
DR GO; GO:0050795; P:regulation of behavior; IEA:InterPro.
DR GO; GO:0040012; P:regulation of locomotion; IEA:InterPro.
DR GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
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 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 3: Inferred from homology;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..377
FT /note="5-hydroxytryptamine receptor 1D"
FT /id="PRO_0000068930"
FT TOPO_DOM 1..38
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 39..64
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 65..75
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 76..98
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 99..112
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 113..134
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 135..154
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 155..176
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 177..194
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 195..217
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 218..302
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 303..326
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 327..335
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 336..360
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 361..377
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT MOTIF 135..137
FT /note="DRY motif; important for ligand-induced conformation
FT changes"
FT /evidence="ECO:0000250"
FT MOTIF 352..356
FT /note="NPxxY motif; important for ligand-induced
FT conformation changes and signaling"
FT /evidence="ECO:0000250"
FT BINDING 118
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P28222"
FT BINDING 123
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P28222"
FT BINDING 190
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P28222"
FT CARBOHYD 5
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 17
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 21
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 111..188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 28
FT /note="A -> I (in Ref. 2; AAB58466)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 377 AA; 41500 MW; FC1441678AB82B0A CRC64;
MSPSNQSAEG LPQEAANRSL NATGTPEAWD PGTLQALKIS LAVVLSIITV ATVLSNTFVL
TTILLTRKLH TPANYLIGSL ATTDLLVSIL VMPISIAYTI THTWNFGQVL CDIWVSSDIT
CCTASILHLC VIALDRYWAI TDALEYSKRR TAGHAAAMIA VVWAISICIS IPPLFWRQAK
AHEEVSDCLV NTSQISYTIY STCGAFYIPS VLLIVLYGRI YMAARNRILN PPSLYGKRFT
TAHLITGSAG SSLCSLSPSL GEGHSHSAGS PLFFNPVRIK LADSVLERKR ISAARERKAT
KTLGIILGAF IGCWLPFFVA SLVLPICRDS CWMPPGLFDF FTWLGYLNSL INPIIYTVFN
EDFRQAFQRV IHFRKAF
