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   24-JAN-2024, entry version 167.
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   GlyCosmos; Q02284; 2 sites, No reported glycans.
DR   GlyGen; Q02284; 2 sites.
DR   PhosphoSitePlus; Q02284; -.
DR   PaxDb; 10090-ENSMUSP00000063136; -.
DR   ProteomicsDB; 285573; -.
DR   Antibodypedia; 1481; 233 antibodies from 29 providers.
DR   DNASU; 15557; -.
DR   Ensembl; ENSMUST00000063076.6; ENSMUSP00000063136.5; ENSMUSG00000050783.6.
DR   GeneID; 15557; -.
DR   KEGG; mmu:15557; -.
DR   UCSC; uc007zqg.2; mouse.
DR   AGR; MGI:99842; -.
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; PPLLWRH; -.
DR   OrthoDB; 2999405at2759; -.
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 77 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 cell types or tissues.
DR   ExpressionAtlas; Q02284; baseline and differential.
DR   GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR   GO; GO:0005886; C: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   CDD; cd15334; 7tmA_5-HT1F; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR000450; 5HT1F_rcpt.
DR   InterPro; IPR002231; 5HT_rcpt.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   PANTHER; PTHR24247; 5-HYDROXYTRYPTAMINE RECEPTOR; 1.
DR   PANTHER; PTHR24247:SF34; 5-HYDROXYTRYPTAMINE RECEPTOR 1F; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00515; 5HT1FRECEPTR.
DR   PRINTS; PR01101; 5HTRECEPTOR.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR   Genevisible; Q02284; MM.
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
//