ID Q543V2_MOUSE Unreviewed; 366 AA. AC Q543V2; DT 24-MAY-2005, integrated into UniProtKB/TrEMBL. DT 24-MAY-2005, sequence version 1. DT 24-JAN-2024, entry version 154. DE RecName: Full=5-hydroxytryptamine receptor 1F {ECO:0000256|ARBA:ARBA00017608}; DE AltName: Full=Serotonin receptor 1F {ECO:0000256|ARBA:ARBA00032313}; GN Name=Htr1f {ECO:0000313|EMBL:AAI20508.1, ECO:0000313|MGI:MGI:99842}; 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 {ECO:0000313|EMBL:BAC32328.1}; RN [1] {ECO:0000313|EMBL:BAC32328.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC32328.1}; RC TISSUE=Corpora quadrigemina {ECO:0000313|EMBL:BAC32328.1}; RX PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9; RA Carninci P., Hayashizaki Y.; RT "High-efficiency full-length cDNA cloning."; RL Methods Enzymol. 303:19-44(1999). RN [2] {ECO:0000313|EMBL:BAC32328.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC32328.1}; RC TISSUE=Corpora quadrigemina {ECO:0000313|EMBL:BAC32328.1}; RX PubMed=11042159; DOI=10.1101/gr.145100; RA Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M., RA Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.; RT "Normalization and subtraction of cap-trapper-selected cDNAs to prepare RT full-length cDNA libraries for rapid discovery of new genes."; RL Genome Res. 10:1617-1630(2000). RN [3] {ECO:0000313|EMBL:BAC32328.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC32328.1}; RC TISSUE=Corpora quadrigemina {ECO:0000313|EMBL:BAC32328.1}; RX PubMed=11076861; DOI=10.1101/gr.152600; RA Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P., RA Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M., Sumi N., RA Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A., Yamamoto R., RA Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K., Fujiwake S., RA Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M., Yoneda Y., RA Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J., Okazaki Y., RA Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.; RT "RIKEN integrated sequence analysis (RISA) system--384-format sequencing RT pipeline with 384 multicapillary sequencer."; RL Genome Res. 10:1757-1771(2000). RN [4] {ECO:0000313|EMBL:BAC32328.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC32328.1}; RC TISSUE=Corpora quadrigemina {ECO:0000313|EMBL:BAC32328.1}; RX PubMed=11217851; DOI=10.1038/35055500; RG The RIKEN Genome Exploration Research Group Phase II Team and the FANTOM Consortium; RT "Functional annotation of a full-length mouse cDNA collection."; RL Nature 409:685-690(2001). RN [5] {ECO:0000313|EMBL:BAC32328.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC32328.1}; RC TISSUE=Corpora quadrigemina {ECO:0000313|EMBL:BAC32328.1}; RA Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P., RA Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W., Hayashida K., RA Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T., Hori F., Imotani K., RA Ishii Y., Itoh M., Kagawa I., Kasukawa T., Katoh H., Kawai J., Kojima Y., RA Kondo S., Konno H., Kouda M., Koya S., Kurihara C., Matsuyama T., RA Miyazaki A., Murata M., Nakamura M., Nishi K., Nomura K., Numazaki R., RA Ohno M., Ohsato N., Okazaki Y., Saito R., Saitoh H., Sakai C., Sakai K., RA Sakazume N., Sano H., Sasaki D., Shibata K., Shinagawa A., Shiraki T., RA Sogabe Y., Tagami M., Tagawa A., Takahashi F., Takaku-Akahira S., RA Takeda Y., Tanaka T., Tomaru A., Toya T., Yasunishi A., Muramatsu M., RA Hayashizaki Y.; RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases. RN [6] {ECO:0000313|EMBL:BAC32328.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC32328.1}; RC TISSUE=Corpora quadrigemina {ECO:0000313|EMBL:BAC32328.1}; RX PubMed=12466851; DOI=10.1038/nature01266; RG The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team; RT "Analysis of the mouse transcriptome based on functional annotation of RT 60,770 full-length cDNAs."; RL Nature 420:563-573(2002). RN [7] {ECO:0000313|EMBL:AAI20508.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain {ECO:0000313|EMBL:AAI20508.1}; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RA Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., RA Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M., RA Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M., RA Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F., RA Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T., RA Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F., RA Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E., RA Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y., RA Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E., RA Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., RA Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., RA Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., RA Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., RA Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J., RA Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W., RA Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J., RA Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I., RA Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U., RA Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A., RA Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.; 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 [8] {ECO:0000313|EMBL:BAC32328.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC32328.1}; RC TISSUE=Corpora quadrigemina {ECO:0000313|EMBL:BAC32328.1}; RG The FANTOM Consortium; RG Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group); RT "The Transcriptional Landscape of the Mammalian Genome."; RL Science 309:1559-1563(2005). RN [9] {ECO:0000313|EMBL:BAC32328.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC32328.1}; RC TISSUE=Corpora quadrigemina {ECO:0000313|EMBL:BAC32328.1}; RX PubMed=16141073; DOI=10.1126/science.1112009; RG RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group) and the FANTOM Consortium; RT "Antisense Transcription in the Mammalian Transcriptome."; RL Science 309:1564-1566(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. CC {ECO:0000256|ARBA:ARBA00025230}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004141}. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC {ECO:0000256|RuleBase:RU000688}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC120507; AAI20508.1; -; mRNA. DR EMBL; BC137604; AAI37605.1; -; mRNA. DR EMBL; AK045364; BAC32328.1; -; mRNA. DR RefSeq; NP_032336.1; NM_008310.3. DR AlphaFoldDB; Q543V2; -. DR SMR; Q543V2; -. DR Antibodypedia; 1481; 233 antibodies from 29 providers. DR DNASU; 15557; -. DR GeneID; 15557; -. DR KEGG; mmu:15557; -. DR AGR; MGI:99842; -. DR CTD; 3355; -. DR MGI; MGI:99842; Htr1f. DR VEuPathDB; HostDB:ENSMUSG00000050783; -. DR HOGENOM; CLU_009579_11_1_1; -. DR OMA; PPLLWRH; -. DR OrthoDB; 2999405at2759; -. DR BioGRID-ORCS; 15557; 0 hits in 77 CRISPR screens. DR ChiTaRS; Htr1f; mouse. DR ExpressionAtlas; Q543V2; baseline and differential. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004993; F:G protein-coupled serotonin receptor activity; IEA:Ensembl. DR GO; GO:0051378; F:serotonin binding; IEA:Ensembl. DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IEA:Ensembl. 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. PE 2: Evidence at transcript level; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040, KW ECO:0000256|RuleBase:RU000688}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU000688}; KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|RuleBase:RU000688}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU000688}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 24..50 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 62..86 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 98..119 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 140..161 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 181..202 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 291..311 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 331..350 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 40..347 FT /note="G-protein coupled receptors family 1 profile" FT /evidence="ECO:0000259|PROSITE:PS50262" 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 //