5HT1F_RAT
ID 5HT1F_RAT Reviewed; 366 AA.
AC P30940;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 131.
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; Synonyms=5ht1f;
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, AND SUBCELLULAR LOCATION.
RX PubMed=8384716; DOI=10.1073/pnas.90.6.2184;
RA Lovenberg T.W., Erlander M.G., Baron B.M., Racke M., Slone A.L.,
RA Siegel B.W., Craft C.M., Burns J.E., Danielson P.E., Sutcliffe G.J.;
RT "Molecular cloning and functional expression of 5-HT1E-like rat and human
RT 5-hydroxytryptamine receptor genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:2184-2188(1993).
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:8384716}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8384716};
CC Multi-pass membrane protein {ECO:0000269|PubMed:8384716}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; L05596; AAA42133.1; -; Genomic_DNA.
DR PIR; A47385; A47385.
DR AlphaFoldDB; P30940; -.
DR SMR; P30940; -.
DR STRING; 10116.ENSRNOP00000000907; -.
DR BindingDB; P30940; -.
DR ChEMBL; CHEMBL4646; -.
DR DrugCentral; P30940; -.
DR GuidetoPHARMACOLOGY; 5; -.
DR GlyGen; P30940; 2 sites.
DR PhosphoSitePlus; P30940; -.
DR PaxDb; P30940; -.
DR UCSC; RGD:71083; rat.
DR RGD; 71083; Htr1f.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; P30940; -.
DR PhylomeDB; P30940; -.
DR Reactome; R-RNO-390666; Serotonin receptors.
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR PRO; PR:P30940; -.
DR Proteomes; UP000002494; 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; ISO:RGD.
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; 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_0000068940"
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; 41880 MW; 0672868A41DFDBFB CRC64;
MDFLNSSDQN LTSEELLNRM PSKILVSLTL SGLALMTTTI NCLVITAIIV TRKLHHPANY
LICSLAVTDF LVAVLVMPFS IVYIVRESWI MGQGLCDLWL SVDIICCTCS ILHLSAIALD
RYRAITDAVE YARKRTPRHA GITITTVWVI SVFISVPPLF WRHQGNSRDD QCIIKHDHIV
STIYSTFGAF YIPLVLILIL YYKIYRAART LYHKRQASRM IKEELNGQVL LESGEKSIKL
VSTSYMLEKS LSDPSTDFDR IHSTVKSPRS ELKHEKSWRR QKISGTRERK AATTLGLILG
AFVICWLPFF VKELVVNICE KCKISEEMSN FLAWLGYLNS LINPLIYTIF NEDFKKAFQK
LVRCRN
