5HT1F_CAVPO
ID 5HT1F_CAVPO Reviewed; 366 AA.
AC O08890;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=5-hydroxytryptamine receptor 1F;
DE Short=5-HT-1F;
DE Short=5-HT1F;
DE AltName: Full=Serotonin receptor 1F;
GN Name=HTR1F;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Liver;
RX PubMed=9225282; DOI=10.1016/s0028-3908(97)00020-8;
RA Adham N., Bard J.A., Zgombick J.M., Durkin M.M., Kucharewicz S.,
RA Weinshank R.L., Branchek T.A.;
RT "Cloning and characterization of the guinea pig 5-HT1F receptor subtype: a
RT comparison of the pharmacological profile to the human species homolog.";
RL Neuropharmacology 36:569-576(1997).
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 {ECO:0000269|PubMed:9225282}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9225282};
CC Multi-pass membrane protein {ECO:0000269|PubMed:9225282}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; U80852; AAB58496.1; -; Genomic_DNA.
DR RefSeq; XP_005008750.1; XM_005008693.2.
DR AlphaFoldDB; O08890; -.
DR SMR; O08890; -.
DR GeneID; 100716637; -.
DR KEGG; cpoc:100716637; -.
DR CTD; 3355; -.
DR InParanoid; O08890; -.
DR OrthoDB; 703991at2759; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0004993; F:G protein-coupled serotonin receptor activity; ISS:UniProtKB.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR InterPro; IPR000450; 5HT1F_rcpt.
DR InterPro; IPR002231; 5HT_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR24247:SF34; PTHR24247:SF34; 1.
DR Pfam; PF00001; 7tm_1; 1.
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..366
FT /note="5-hydroxytryptamine receptor 1F"
FT /id="PRO_0000068936"
FT TOPO_DOM 1..29
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 30..50
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 51..60
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 61..83
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 84..97
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 98..118
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 119..140
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 141..161
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 162..178
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 179..201
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 202..290
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 291..311
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 312..329
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 330..350
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 351..366
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT MOTIF 120..122
FT /note="DRY motif; important for ligand-induced conformation
FT changes"
FT /evidence="ECO:0000250"
FT MOTIF 343..347
FT /note="NPxxY motif; important for ligand-induced
FT conformation changes and signaling"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P28222"
FT BINDING 108
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P28222"
FT BINDING 174
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 10
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 96..172
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 366 AA; 41839 MW; FE4200E2DA26C9C3 CRC64;
MDFLNSSDQN LTSEELLHRM PSKILVSLTL SGLALMTTTI NSLVIAAIIV TRKLHHPANY
LICSLAVTDF LVAVLVMPFS IVYIVRESWI MGQVLCDIWL SVDIICCTCS ILHLSAIALD
RYRAITDAVE YARKRTPKQA GIMITIVWII SVFISMPPLF WRHQGTSRDD ECIIKHDHIV
STIYSTFGAF YIPLVLILIL YYKIYKAAKT LYHKRQASRI AKEELNGQVL LESGEKSIKM
VSTTYVPEKS LSDPSTDFDK IHNTVKSPRC KLRHEKSWRR QKISGTRERK AATTLGLILG
AFVICWLPFF VKELVVNVCE KCKISEEMAN FLAWLGYLNS LINPLIYTIF NEDFKKAFQK
LVRCQY
