5HT1F_HUMAN
ID 5HT1F_HUMAN Reviewed; 366 AA.
AC P30939;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 174.
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=HTR1EL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8380639; DOI=10.1073/pnas.90.2.408;
RA Adham N., Kao H.-T., Schechter L.E., Bard J., Olsen M., Urquhart D.,
RA Durkin M., Hartig P.R., Winshank R.L., Branchek T.A.;
RT "Cloning of another human serotonin receptor (5-HT1F): a fifth 5-HT1
RT receptor subtype coupled to the inhibition of adenylate cyclase.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:408-412(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [6]
RP REVIEW.
RX PubMed=18476671; DOI=10.1021/cr078224o;
RA Nichols D.E., Nichols C.D.;
RT "Serotonin receptors.";
RL Chem. Rev. 108:1614-1641(2008).
RN [7]
RP FUNCTION.
RX PubMed=21422162; DOI=10.1124/jpet.111.179606;
RA Klein M.T., Dukat M., Glennon R.A., Teitler M.;
RT "Toward selective drug development for the human 5-hydroxytryptamine 1E
RT receptor: a comparison of 5-hydroxytryptamine 1E and 1F receptor structure-
RT affinity relationships.";
RL J. Pharmacol. Exp. Ther. 337:860-867(2011).
RN [8]
RP REVIEW.
RX PubMed=20945968; DOI=10.33549/physiolres.931903;
RA Pytliak M., Vargova V., Mechirova V., Felsoci M.;
RT "Serotonin receptors - from molecular biology to clinical applications.";
RL Physiol. Res. 60:15-25(2011).
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:21422162, ECO:0000269|PubMed:8380639,
CC ECO:0000269|PubMed:8384716}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8380639,
CC ECO:0000269|PubMed:8384716}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:8380639, 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; L05597; AAA36605.1; -; Genomic_DNA.
DR EMBL; L04962; AAA36646.1; -; Genomic_DNA.
DR EMBL; AF498981; AAM21128.1; -; mRNA.
DR EMBL; AC119733; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC069125; AAH69125.1; -; mRNA.
DR CCDS; CCDS2920.1; -.
DR PIR; A47321; A47321.
DR RefSeq; NP_000857.1; NM_000866.4.
DR RefSeq; NP_001309137.1; NM_001322208.1.
DR RefSeq; NP_001309138.1; NM_001322209.1.
DR RefSeq; NP_001309139.1; NM_001322210.1.
DR RefSeq; XP_005264808.1; XM_005264751.3.
DR RefSeq; XP_011531966.1; XM_011533664.2.
DR PDB; 7EXD; EM; 3.40 A; R=1-366.
DR PDBsum; 7EXD; -.
DR AlphaFoldDB; P30939; -.
DR SMR; P30939; -.
DR STRING; 9606.ENSP00000322924; -.
DR BindingDB; P30939; -.
DR ChEMBL; CHEMBL1805; -.
DR DrugBank; DB01239; Chlorprothixene.
DR DrugBank; DB11273; Dihydroergocornine.
DR DrugBank; DB13345; Dihydroergocristine.
DR DrugBank; DB00320; Dihydroergotamine.
DR DrugBank; DB00216; Eletriptan.
DR DrugBank; DB01049; Ergoloid mesylate.
DR DrugBank; DB00696; Ergotamine.
DR DrugBank; DB12141; Gilteritinib.
DR DrugBank; DB01221; Ketamine.
DR DrugBank; DB11732; Lasmiditan.
DR DrugBank; DB00247; Methysergide.
DR DrugBank; DB06148; Mianserin.
DR DrugBank; DB00952; Naratriptan.
DR DrugBank; DB00334; Olanzapine.
DR DrugBank; DB00715; Paroxetine.
DR DrugBank; DB00953; Rizatriptan.
DR DrugBank; DB09304; Setiptiline.
DR DrugBank; DB00669; Sumatriptan.
DR DrugBank; DB13025; Tiapride.
DR DrugBank; DB00315; Zolmitriptan.
DR DrugCentral; P30939; -.
DR GuidetoPHARMACOLOGY; 5; -.
DR GlyGen; P30939; 2 sites.
DR iPTMnet; P30939; -.
DR PhosphoSitePlus; P30939; -.
DR BioMuta; HTR1F; -.
DR DMDM; 398967; -.
DR MassIVE; P30939; -.
DR PaxDb; P30939; -.
DR PeptideAtlas; P30939; -.
DR PRIDE; P30939; -.
DR ProteomicsDB; 54747; -.
DR Antibodypedia; 1481; 210 antibodies from 29 providers.
DR DNASU; 3355; -.
DR Ensembl; ENST00000319595.7; ENSP00000322924.4; ENSG00000179097.7.
DR GeneID; 3355; -.
DR KEGG; hsa:3355; -.
DR MANE-Select; ENST00000319595.7; ENSP00000322924.4; NM_001322209.2; NP_001309138.1.
DR UCSC; uc062lsi.1; human.
DR CTD; 3355; -.
DR DisGeNET; 3355; -.
DR GeneCards; HTR1F; -.
DR HGNC; HGNC:5292; HTR1F.
DR HPA; ENSG00000179097; Tissue enhanced (placenta, retina).
DR MIM; 182134; gene.
DR neXtProt; NX_P30939; -.
DR OpenTargets; ENSG00000179097; -.
DR PharmGKB; PA29553; -.
DR VEuPathDB; HostDB:ENSG00000179097; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01010000222287; -.
DR HOGENOM; CLU_009579_11_1_1; -.
DR InParanoid; P30939; -.
DR OMA; SCMTNGS; -.
DR OrthoDB; 703991at2759; -.
DR PhylomeDB; P30939; -.
DR TreeFam; TF316350; -.
DR PathwayCommons; P30939; -.
DR Reactome; R-HSA-390666; Serotonin receptors.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR SignaLink; P30939; -.
DR SIGNOR; P30939; -.
DR BioGRID-ORCS; 3355; 10 hits in 1073 CRISPR screens.
DR ChiTaRS; HTR1F; human.
DR GeneWiki; 5-HT1F_receptor; -.
DR GenomeRNAi; 3355; -.
DR Pharos; P30939; Tclin.
DR PRO; PR:P30939; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P30939; protein.
DR Bgee; ENSG00000179097; Expressed in islet of Langerhans and 71 other tissues.
DR Genevisible; P30939; HS.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IMP:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0004993; F:G protein-coupled serotonin receptor activity; IDA:MGI.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0051378; F:serotonin binding; IDA:MGI.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IMP: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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Membrane; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..366
FT /note="5-hydroxytryptamine receptor 1F"
FT /id="PRO_0000068937"
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"
FT HELIX 20..50
FT /evidence="ECO:0007829|PDB:7EXD"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:7EXD"
FT HELIX 60..75
FT /evidence="ECO:0007829|PDB:7EXD"
FT HELIX 77..85
FT /evidence="ECO:0007829|PDB:7EXD"
FT HELIX 93..126
FT /evidence="ECO:0007829|PDB:7EXD"
FT TURN 128..130
FT /evidence="ECO:0007829|PDB:7EXD"
FT HELIX 131..134
FT /evidence="ECO:0007829|PDB:7EXD"
FT HELIX 137..153
FT /evidence="ECO:0007829|PDB:7EXD"
FT HELIX 157..162
FT /evidence="ECO:0007829|PDB:7EXD"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:7EXD"
FT HELIX 179..212
FT /evidence="ECO:0007829|PDB:7EXD"
FT HELIX 286..318
FT /evidence="ECO:0007829|PDB:7EXD"
FT HELIX 326..346
FT /evidence="ECO:0007829|PDB:7EXD"
FT TURN 347..349
FT /evidence="ECO:0007829|PDB:7EXD"
FT HELIX 352..360
FT /evidence="ECO:0007829|PDB:7EXD"
SQ SEQUENCE 366 AA; 41709 MW; 16EA80344793B54F 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
LVRCRC
