5HT1F_PANTR
ID 5HT1F_PANTR Reviewed; 365 AA.
AC Q9N2D9;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 07-APR-2021, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=5-hydroxytryptamine receptor 1F;
DE Short=5-HT-1F;
DE Short=5-HT1F;
DE AltName: Full=Serotonin receptor 1F;
DE Flags: Fragment;
GN Name=HTR1F;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate 220;
RX PubMed=15014171; DOI=10.1093/molbev/msh100;
RA Kitano T., Liu Y.-H., Ueda S., Saitou N.;
RT "Human-specific amino acid changes found in 103 protein-coding genes.";
RL Mol. Biol. Evol. 21:936-944(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AB037534; BAA90454.2; -; Genomic_DNA.
DR EMBL; AACZ04038288; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; Q9N2D9; -.
DR SMR; Q9N2D9; -.
DR STRING; 9598.ENSPTRP00000026109; -.
DR PaxDb; Q9N2D9; -.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; Q9N2D9; -.
DR OMA; SCMTNGS; -.
DR Proteomes; UP000002277; 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; IBA:GO_Central.
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..>365
FT /note="5-hydroxytryptamine receptor 1F"
FT /id="PRO_0000068939"
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..>365
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"
FT NON_TER 365
SQ SEQUENCE 365 AA; 41606 MW; 6A80344793B54F5B CRC64;
MDFLNSSDQN LTSEELLNRM PSKILVSLTL SGLALMTTTI NSLVIAAIIV TRKLHHPANY
LICSLAVTDF LVAVLVMPFS IVYIVRESWI MGQVVCDIWL SVDITCCTCS ILHLSAIALD
RYRAITDAVE YARKRTPKHA GIMITIVWII SVFISMPPLF WRHQGTSRDD ECIIKHDHIV
STIYSTFGAF YIPLALILIL YYKIYRAAKT LYHKRQASRI AKEEVNGQVL LESGEKSTKS
VSTSYVLEKS LSDPSTDFDK IHSTVRSLRS EFKHEKSWRR QKISGTRERK AATTLGLILG
AFVICWLPFF VKELVVNVCD KCKISEEMSN FLAWLGYLNS LINPLIYTIF NEDFKKAFQK
LVRCR
