FMAR_DROME
ID FMAR_DROME Reviewed; 549 AA.
AC Q9VZW5;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=FMRFamide receptor {ECO:0000303|PubMed:12218185};
DE Short=DFR {ECO:0000303|PubMed:12218185};
DE Short=DrmFMRFa-R {ECO:0000303|PubMed:12438685};
GN Name=FMRFaR {ECO:0000312|FlyBase:FBgn0035385};
GN Synonyms=FR {ECO:0000312|EMBL:AAF47700.1};
GN ORFNames=CG2114 {ECO:0000312|FlyBase:FBgn0035385};
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] {ECO:0000305, ECO:0000312|EMBL:AAL83921.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RC STRAIN=Canton-S {ECO:0000269|PubMed:12218185};
RC TISSUE=Larva {ECO:0000269|PubMed:12218185};
RX PubMed=12218185; DOI=10.1073/pnas.192442799;
RA Cazzamali G., Grimmelikhuijzen C.J.P.;
RT "Molecular cloning and functional expression of the first insect FMRFamide
RT receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:12073-12078(2002).
RN [2] {ECO:0000305, ECO:0000312|EMBL:DAA00378.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12438685; DOI=10.1073/pnas.252339599;
RA Meeusen T., Mertens I., Clynen E., Baggerman G., Nichols R., Nachman R.J.,
RA Huybrechts R., De Loof A., Schoofs L.;
RT "Identification in Drosophila melanogaster of the invertebrate G protein-
RT coupled FMRFamide receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:15363-15368(2002).
RN [3] {ECO:0000312|EMBL:AAF47700.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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 [4] {ECO:0000305, ECO:0000312|EMBL:AAF47700.1}
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 [5] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=30110323; DOI=10.1371/journal.pgen.1007459;
RA Ravi P., Trivedi D., Hasan G.;
RT "FMRFa receptor stimulated Ca2+ signals alter the activity of flight
RT modulating central dopaminergic neurons in Drosophila melanogaster.";
RL PLoS Genet. 14:e1007459-e1007459(2018).
CC -!- FUNCTION: A receptor for the FMRFamide peptides (PubMed:12218185,
CC PubMed:12438685). Reacts with high affinity to FMRFamide and intrinsic
CC FMRFamide-related peptides (PubMed:12218185, PubMed:12438685). By
CC stimulating intracellular calcium signaling through the inositol 1,4,5-
CC trisphosphate receptor, Itpr, in dopaminergic neurons, may be involved
CC in the maintenance of neuronal excitability and in the regulation of
CC flight bout duration (PubMed:30110323). {ECO:0000269|PubMed:12218185,
CC ECO:0000269|PubMed:12438685, ECO:0000269|PubMed:30110323}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in ovaries, heads and bodies
CC (PubMed:12438685). Expressed in dopaminergic neurons.
CC {ECO:0000269|PubMed:12438685, ECO:0000269|PubMed:30110323}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development; strongest in
CC larvae and adults (PubMed:12218185). In larvae, expressed in trachea,
CC brain, gut, fat body and Malpighian tubules (PubMed:30110323).
CC {ECO:0000269|PubMed:12218185, ECO:0000269|PubMed:30110323}.
CC -!- DISRUPTION PHENOTYPE: Deficits in simulated flight behavior with fewer
CC or shorter duration of wing beats in tethered flies (PubMed:30110323).
CC Dopaminergic neuron-specific knockout leads to shorter flight duration
CC (PubMed:30110323). RNAi-mediated knockdown, either in adults or during
CC pupal development, results in similar deficits in simulated flight
CC behavior, whereas knockdown during larval development has no effect on
CC flight behavior in the adult (PubMed:30110323). Pan-neuronal or
CC dopaminergic neuron-specific RNAi-mediated knockdown leads to
CC significantly shorter flight bouts (PubMed:30110323).
CC {ECO:0000269|PubMed:30110323}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AF351129; AAL83921.1; -; mRNA.
DR EMBL; BK000442; DAA00378.1; -; mRNA.
DR EMBL; AE014296; AAF47700.1; -; Genomic_DNA.
DR RefSeq; NP_001261347.1; NM_001274418.2.
DR RefSeq; NP_001286925.1; NM_001299996.1.
DR RefSeq; NP_647758.1; NM_139501.4.
DR AlphaFoldDB; Q9VZW5; -.
DR SMR; Q9VZW5; -.
DR STRING; 7227.FBpp0072850; -.
DR GlyGen; Q9VZW5; 3 sites.
DR PaxDb; Q9VZW5; -.
DR EnsemblMetazoa; FBtr0072980; FBpp0072850; FBgn0035385.
DR EnsemblMetazoa; FBtr0332085; FBpp0304395; FBgn0035385.
DR EnsemblMetazoa; FBtr0340706; FBpp0309525; FBgn0035385.
DR GeneID; 38357; -.
DR KEGG; dme:Dmel_CG2114; -.
DR CTD; 38357; -.
DR FlyBase; FBgn0035385; FMRFaR.
DR VEuPathDB; VectorBase:FBgn0035385; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000173102; -.
DR HOGENOM; CLU_009579_24_7_1; -.
DR InParanoid; Q9VZW5; -.
DR OMA; HWCYLIV; -.
DR OrthoDB; 1342402at2759; -.
DR PhylomeDB; Q9VZW5; -.
DR BioGRID-ORCS; 38357; 0 hits in 1 CRISPR screen.
DR ChiTaRS; FMRFaR; fly.
DR GenomeRNAi; 38357; -.
DR PRO; PR:Q9VZW5; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0035385; Expressed in VUM neuron (Drosophila) and 9 other tissues.
DR ExpressionAtlas; Q9VZW5; baseline and differential.
DR Genevisible; Q9VZW5; DM.
DR GO; GO:0016021; C:integral component of membrane; ISM:FlyBase.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:FlyBase.
DR GO; GO:0008188; F:neuropeptide receptor activity; IPI:FlyBase.
DR GO; GO:0001653; F:peptide receptor activity; IDA:FlyBase.
DR GO; GO:0008344; P:adult locomotory behavior; IMP:UniProtKB.
DR GO; GO:0002209; P:behavioral defense response; IMP:FlyBase.
DR GO; GO:0007629; P:flight behavior; IMP:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISM:FlyBase.
DR GO; GO:0008345; P:larval locomotory behavior; IMP:FlyBase.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IDA:FlyBase.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:UniProtKB.
DR GO; GO:0032226; P:positive regulation of synaptic transmission, dopaminergic; IMP:UniProtKB.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; G-protein coupled receptor; Glycoprotein; Membrane;
KW Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..549
FT /note="FMRFamide receptor"
FT /id="PRO_0000069442"
FT TOPO_DOM 1..117
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..138
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 139..158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180..181
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 203..238
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..289
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 290..310
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 311..341
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 342..362
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 363..376
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 377..397
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 398..549
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 549 AA; 61755 MW; AF449A9B0AD65104 CRC64;
MSGTAVARLL LRLELPSPGV MPPPPTDYDY GGPISDDEFL ASAMATEGPT VRYDLFPQNN
SQPTLQIVLN HTEVQTDLQY PHYEDLGLDP DPNWTRICED VYNPLLENNR IEFWVCGVLI
NIVGVLGILG NIISMIILSR PQMRSSINYL LTGLARCDTV LIITSILLFG IPSIYPYTGH
FFGYYNYVYP FISPAVFPIG MIAQTASIYM TFTVTLERYV AVCHPLKARA LCTYGRAKIY
FIVCVCFSLA YNMPRFWEVL TVTYPEPGKD VILHCVRPSR LRRSETYINI YIHWCYLIVN
YIIPFLTLAI LNCLIYRQVK RANRERQRLS RSEKREIGLA TMLLCVVIVF FMLNFLPLVL
NISEAFYSTI DHKITKISNL LITINSSVNF LIYIIFGEKF KRIFLLIFFK RRLSRDQPDL
IHYESSISNN GDGTLNHRSS GRFSRHGTQR STTTTYLVAT GGPGGGGCGG GGGNNSLNNV
RLTQVSGSPG LVKIKRNRAP SPGPVVYFPA REMQRSASTT NSTTNNNTSI GYDWTLPDSK
KLGHVSSGF
