ID 5HT1R_DROME Reviewed; 564 AA.
AC P20905; Q9VA21;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 27-MAR-2024, entry version 184.
DE RecName: Full=5-hydroxytryptamine receptor 1;
DE Short=5-HT receptor;
DE AltName: Full=5HT-dro;
DE AltName: Full=Serotonin receptor 1;
GN Name=5-HT7; Synonyms=5HT-R1; ORFNames=CG12073;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=Oregon-R; TISSUE=Head;
RX PubMed=2174167; DOI=10.1073/pnas.87.22.8940;
RA Witz P., Amlaiky N., Plassat J.-L., Maroteaux L., Borrelli E., Hen R.;
RT "Cloning and characterization of a Drosophila serotonin receptor that
RT activates adenylate cyclase.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:8940-8944(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: G-protein coupled receptor for 5-hydroxytryptamine
CC (serotonin). Also functions as a receptor for various alkaloids. Ligand
CC binding causes a conformation change that triggers signaling via
CC guanine nucleotide-binding proteins (G proteins) and modulates the
CC activity of down-stream effectors, such as adenylate cyclase. Signaling
CC activates adenylate cyclase activity. {ECO:0000269|PubMed:2174167}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2174167};
CC Multi-pass membrane protein {ECO:0000269|PubMed:2174167}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in adult heads.
CC {ECO:0000269|PubMed:2174167}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. 5-
CC hydroxytryptamine receptor subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00521}.
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DR EMBL; M55533; AAA28305.1; -; mRNA.
DR EMBL; AE014297; AAF57104.1; -; Genomic_DNA.
DR EMBL; AY118491; AAM49860.1; -; mRNA.
DR PIR; A38271; A38271.
DR RefSeq; NP_001263131.1; NM_001276202.1.
DR RefSeq; NP_524599.1; NM_079860.3.
DR AlphaFoldDB; P20905; -.
DR SMR; P20905; -.
DR STRING; 7227.FBpp0306575; -.
DR PaxDb; 7227-FBpp0085108; -.
DR DNASU; 43669; -.
DR EnsemblMetazoa; FBtr0085746; FBpp0085108; FBgn0004573.
DR EnsemblMetazoa; FBtr0334508; FBpp0306575; FBgn0004573.
DR GeneID; 43669; -.
DR KEGG; dme:Dmel_CG12073; -.
DR AGR; FB:FBgn0004573; -.
DR CTD; 43669; -.
DR FlyBase; FBgn0004573; 5-HT7.
DR VEuPathDB; VectorBase:FBgn0004573; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01010000222287; -.
DR HOGENOM; CLU_009579_11_4_1; -.
DR InParanoid; P20905; -.
DR OMA; FMKDDHR; -.
DR OrthoDB; 2999405at2759; -.
DR PhylomeDB; P20905; -.
DR Reactome; R-DME-390666; Serotonin receptors.
DR BioGRID-ORCS; 43669; 0 hits in 3 CRISPR screens.
DR ChiTaRS; 5-HT7; fly.
DR GenomeRNAi; 43669; -.
DR PRO; PR:P20905; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0004573; Expressed in brain and 11 other cell types or tissues.
DR ExpressionAtlas; P20905; baseline and differential.
DR Genevisible; P20905; DM.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; ISS:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0008227; F:G protein-coupled amine receptor activity; ISS:FlyBase.
DR GO; GO:0004993; F:G protein-coupled serotonin receptor activity; IDA:FlyBase.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0007192; P:adenylate cyclase-activating serotonin receptor signaling pathway; TAS:FlyBase.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0007619; P:courtship behavior; IMP:FlyBase.
DR GO; GO:0060180; P:female mating behavior; IMP:FlyBase.
DR GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; IBA:GO_Central.
DR GO; GO:0016543; P:male courtship behavior, orientation prior to leg tapping and wing vibration; IMP:FlyBase.
DR GO; GO:0016546; P:male courtship behavior, proboscis-mediated licking; IMP:FlyBase.
DR GO; GO:0016545; P:male courtship behavior, veined wing vibration; IMP:FlyBase.
DR GO; GO:0060179; P:male mating behavior; IMP:FlyBase.
DR GO; GO:0007210; P:serotonin receptor signaling pathway; IDA:FlyBase.
DR CDD; cd15329; 7tmA_5-HT7; 1.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR InterPro; IPR000929; Dopamine_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR24247; 5-HYDROXYTRYPTAMINE RECEPTOR; 1.
DR PANTHER; PTHR24247:SF221; 5-HYDROXYTRYPTAMINE RECEPTOR 7; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00242; DOPAMINER.
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; Disulfide bond; G-protein coupled receptor; Membrane;
KW Receptor; Reference proteome; Repeat; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..564
FT /note="5-hydroxytryptamine receptor 1"
FT /id="PRO_0000068941"
FT TRANSMEM 29..51
FT /note="Helical; Name=0"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..188
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..198
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 199..222
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 223..236
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 237..258
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 259..278
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 279..302
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 303..330
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 331..353
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 354..454
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 455..476
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 477..487
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 488..510
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 511..564
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REPEAT 89..90
FT /note="1"
FT REPEAT 91..92
FT /note="2"
FT REPEAT 93..94
FT /note="3"
FT REPEAT 95..96
FT /note="4"
FT REPEAT 97..98
FT /note="5"
FT REPEAT 99..100
FT /note="6"
FT REPEAT 101..102
FT /note="7"
FT REPEAT 103..104
FT /note="8"
FT REPEAT 105..106
FT /note="9"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 89..106
FT /note="9 X 2 AA tandem repeats of G-S"
FT REGION 238..247
FT /note="Agonist binding"
FT /evidence="ECO:0000250"
FT REGION 367..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 259..261
FT /note="DRY motif; important for ligand-induced conformation
FT changes"
FT /evidence="ECO:0000250"
FT MOTIF 503..507
FT /note="NPxxY motif; important for ligand-induced
FT conformation changes and signaling"
FT /evidence="ECO:0000250"
FT BINDING 242
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P28222"
FT BINDING 247
FT /ligand="ergotamine"
FT /ligand_id="ChEBI:CHEBI:190463"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:P28222"
FT DISULFID 235..314
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 564 AA; 60861 MW; 0C8B9F8DA63D8095 CRC64;
MALSGQDWRR HQSHRQHRNH RTQGNHQKLI STATLTLFVL FLSSWIAYAA GKATVPAPLV
EGETESATSQ DFNSSSAFLG AIASASSTGS GSGSGSGSGS GSGSGSYGLA SMNSSPIAIV
SYQGITSSNL GDSNTTLVPL SDTPLLLEEF AAGEFVLPPL TSIFVSIVLL IVILGTVVGN
VLVCIAVCMV RKLRRPCNYL LVSLALSDLC VALLVMPMAL LYEVLEKWNF GPLLCDIWVS
FDVLCCTASI LNLCAISVDR YLAITKPLEY GVKRTPRRMM LCVGIVWLAA ACISLPPLLI
LGNEHEDEEG QPICTVCQNF AYQIYATLGS FYIPLSVMLF VYYQIFRAAR RIVLEEKRAQ
THLQQALNGT GSPSAPQAPP LGHTELASSG NGQRHSSVGN TSLTYSTCGG LSSGGGALAG
HGSGGGVSGS TGLLGSPHHK KLRFQLAKEK KASTTLGIIM SAFTVCWLPF FILALIRPFE
TMHVPASLSS LFLWLGYANS LLNPIIYATL NRDFRKPFQE ILYFRCSSLN TMMRENYYQD
QYGEPPSQRV MLGDERHGAR ESFL
//
