5HT1F_MOUSE
ID 5HT1F_MOUSE Reviewed; 366 AA.
AC Q02284;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=5-hydroxytryptamine receptor 1F;
DE Short=5-HT-1F;
DE Short=5-HT1F;
DE AltName: Full=5-HT-1E-beta;
DE AltName: Full=Serotonin receptor 1F;
GN Name=Htr1f; Synonyms=5ht1f, Htr1eb;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=1328180; DOI=10.1016/s0021-9258(19)88617-9;
RA Amlaiky N., Ramboz S., Boschert U., Plassat J.-L., Hen R.;
RT "Isolation of a mouse '5HT1E-like' serotonin receptor expressed
RT predominantly in hippocampus.";
RL J. Biol. Chem. 267:19761-19764(1992).
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:1328180}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1328180};
CC Multi-pass membrane protein {ECO:0000269|PubMed:1328180}.
CC -!- TISSUE SPECIFICITY: Detected in hippocampus.
CC {ECO:0000269|PubMed:1328180}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; Z14224; CAA78593.1; -; mRNA.
DR CCDS; CCDS28267.1; -.
DR PIR; S26048; S26048.
DR RefSeq; NP_032336.1; NM_008310.3.
DR AlphaFoldDB; Q02284; -.
DR SMR; Q02284; -.
DR STRING; 10090.ENSMUSP00000063136; -.
DR BindingDB; Q02284; -.
DR GuidetoPHARMACOLOGY; 5; -.
DR GlyGen; Q02284; 2 sites.
DR PhosphoSitePlus; Q02284; -.
DR PaxDb; Q02284; -.
DR PRIDE; Q02284; -.
DR ProteomicsDB; 285573; -.
DR Antibodypedia; 1481; 210 antibodies from 29 providers.
DR DNASU; 15557; -.
DR Ensembl; ENSMUST00000063076; ENSMUSP00000063136; ENSMUSG00000050783.
DR GeneID; 15557; -.
DR KEGG; mmu:15557; -.
DR UCSC; uc007zqg.2; mouse.
DR CTD; 3355; -.
DR MGI; MGI:99842; Htr1f.
DR VEuPathDB; HostDB:ENSMUSG00000050783; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01010000222287; -.
DR HOGENOM; CLU_009579_11_1_1; -.
DR InParanoid; Q02284; -.
DR OMA; SCMTNGS; -.
DR OrthoDB; 703991at2759; -.
DR PhylomeDB; Q02284; -.
DR TreeFam; TF316350; -.
DR Reactome; R-MMU-390666; Serotonin receptors.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR BioGRID-ORCS; 15557; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Htr1f; mouse.
DR PRO; PR:Q02284; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q02284; protein.
DR Bgee; ENSMUSG00000050783; Expressed in lumbar dorsal root ganglion and 56 other tissues.
DR ExpressionAtlas; Q02284; baseline and differential.
DR Genevisible; Q02284; MM.
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; ISS:MGI.
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 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..366
FT /note="5-hydroxytryptamine receptor 1F"
FT /id="PRO_0000068938"
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; 41977 MW; 69EC1CD6F22BD93F CRC64;
MDFLNASDQN LTSEELLNRM PSKILVSLTL SGLALMTTTI NSLVIAAIIV TRKLHHPANY
LICSLAVTDF LVAVLVMPFS IVYIVRESWI MGQVLCDIWL SVDIICCTCS ILHLSAIALD
RYRAITDAVE YARKRTPRHA GIMITIVWVI SVFISMPPLF WRHQGTSRDD ECVIKHDHIV
STIYSTFGAF YIPLVLILIL YYKIYRAART LYHKRQASRM IKEELNGQVF LESGEKSIKL
VSTSYMLEKS LSDPSTDFDR IHSTVKSPRS ELKHEKSWRR QKISGTRERK AATTLGLILG
AFVICWLPFF VKELVVNVCE KCKISEEMSN FLAWLGYLNS LINPLIYTIF NEDFKKAFQK
LVRCRY
