RYAR_DROME
ID RYAR_DROME Reviewed; 464 AA.
AC P25931; Q6AWE5; Q9VB87;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=RYamide receptor {ECO:0000303|PubMed:21704020};
DE AltName: Full=Neuropeptide Y-like receptor {ECO:0000303|PubMed:1370455};
DE Short=NPY-R {ECO:0000303|PubMed:1370455};
GN Name=RYa-R {ECO:0000303|PubMed:21704020};
GN Synonyms=NepYr {ECO:0000303|PubMed:1370455};
GN ORFNames=CG5811 {ECO:0000312|FlyBase:FBgn0004842};
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, AND SUBCELLULAR LOCATION.
RX PubMed=21843505; DOI=10.1016/j.bbrc.2011.07.131;
RA Collin C., Hauser F., Krogh-Meyer P., Hansen K.K., Gonzalez de Valdivia E.,
RA Williamson M., Grimmelikhuijzen C.J.;
RT "Identification of the Drosophila and Tribolium receptors for the recently
RT discovered insect RYamide neuropeptides.";
RL Biochem. Biophys. Res. Commun. 412:578-583(2011).
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 TISSUE=Testis {ECO:0000312|EMBL:AAT94531.1};
RA Stapleton M., Carlson J., Chavez C., Frise E., George R., Pacleb J.,
RA Park S., Wan K., Yu C., Rubin G.M., Celniker S.;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 9-464, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Canton-S {ECO:0000312|EMBL:AAT94531.1};
RC TISSUE=Head {ECO:0000312|EMBL:AAT94531.1};
RX PubMed=1370455; DOI=10.1016/s0021-9258(18)48446-3;
RA Li X.-J., Wu Y.-N., North R.A., Forte M.A.;
RT "Cloning, functional expression, and developmental regulation of a
RT neuropeptide Y receptor from Drosophila melanogaster.";
RL J. Biol. Chem. 267:9-12(1992).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21704020; DOI=10.1016/j.bbrc.2011.06.081;
RA Ida T., Takahashi T., Tominaga H., Sato T., Kume K., Ozaki M.,
RA Hiraguchi T., Maeda T., Shiotani H., Terajima S., Sano H., Mori K.,
RA Yoshida M., Miyazato M., Kato J., Murakami N., Kangawa K., Kojima M.;
RT "Identification of the novel bioactive peptides dRYamide-1 and dRYamide-2,
RT ligands for a neuropeptide Y-like receptor in Drosophila.";
RL Biochem. Biophys. Res. Commun. 410:872-877(2011).
CC -!- FUNCTION: Receptor for the neuropeptides RYamide-1 and RYamide-2
CC (PubMed:21843505, PubMed:21704020). The activity of this receptor is
CC mediated by G proteins which activate a phosphatidyl-inositol-calcium
CC second messenger system (PubMed:21843505, PubMed:21704020). RYamide
CC signaling may suppress feeding behavior (PubMed:21704020).
CC {ECO:0000269|PubMed:21704020, ECO:0000269|PubMed:21843505}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1370455,
CC ECO:0000269|PubMed:21704020, ECO:0000269|PubMed:21843505}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- DEVELOPMENTAL STAGE: Expressed at low levels during early embryonic
CC stages, its expression increases later and reaches the highest level
CC during late stages of embryogenesis. Subsequently, its levels are
CC reduced during larval stages and increase during pupal stages.
CC {ECO:0000269|PubMed:1370455}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA28727.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; JN234381; AEP22450.1; -; mRNA.
DR EMBL; AE014297; AAF56655.3; -; Genomic_DNA.
DR EMBL; BT015303; AAT94531.1; -; mRNA.
DR EMBL; M81490; AAA28727.1; ALT_INIT; mRNA.
DR PIR; A41738; A41738.
DR RefSeq; NP_524525.3; NM_079801.4.
DR AlphaFoldDB; P25931; -.
DR SMR; P25931; -.
DR BioGRID; 68143; 1.
DR STRING; 7227.FBpp0084470; -.
DR BindingDB; P25931; -.
DR ChEMBL; CHEMBL3879848; -.
DR GlyGen; P25931; 4 sites.
DR PaxDb; P25931; -.
DR EnsemblMetazoa; FBtr0085100; FBpp0084470; FBgn0004842.
DR GeneID; 43253; -.
DR KEGG; dme:Dmel_CG5811; -.
DR CTD; 43253; -.
DR FlyBase; FBgn0004842; RYa-R.
DR VEuPathDB; VectorBase:FBgn0004842; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01050000244933; -.
DR InParanoid; P25931; -.
DR OMA; QYILNYW; -.
DR PhylomeDB; P25931; -.
DR BioGRID-ORCS; 43253; 0 hits in 1 CRISPR screen.
DR ChiTaRS; RYa-R; fly.
DR GenomeRNAi; 43253; -.
DR PRO; PR:P25931; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0004842; Expressed in adult hindgut (Drosophila) and 2 other tissues.
DR ExpressionAtlas; P25931; baseline and differential.
DR Genevisible; P25931; DM.
DR GO; GO:0016021; C:integral component of membrane; ISS:FlyBase.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0008188; F:neuropeptide receptor activity; ISM:FlyBase.
DR GO; GO:0004983; F:neuropeptide Y receptor activity; IEA:InterPro.
DR GO; GO:0001653; F:peptide receptor activity; IPI:FlyBase.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:FlyBase.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR000611; NPY_rcpt.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01012; NRPEPTIDEYR.
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 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..464
FT /note="RYamide receptor"
FT /id="PRO_0000069945"
FT TOPO_DOM 1..105
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..126
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 127..148
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..189
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 211..221
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 243..274
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 275..295
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 296..329
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 330..350
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 351..363
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 364..384
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 385..464
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 8
FT /note="L -> R (in Ref. 1; AEP22450 and 4; AAT94531)"
FT /evidence="ECO:0000305"
FT CONFLICT 47
FT /note="I -> L (in Ref. 1; AEP22450 and 4; AAT94531)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 464 AA; 53524 MW; CA8DBC202259BBFF CRC64;
MEHHNSHLLP GGSEKMYYIA HQQPMLRNED DNYQEGYFIR PDPASLIYNT TALPADDEGS
NYGYGSTTTL SGLQFETYNI TVMMNFSCDD YDLLSEDMWS SAYFKIIVYM LYIPIFIFAL
IGNGTVCYIV YSTPRMRTVT NYFIASLAIG DILMSFFCVP SSFISLFILN YWPFGLALCH
FVNYSQAVSV LVSAYTLVAI SIDRYIAIMW PLKPRITKRY ATFIIAGVWF IALATALPIP
IVSGLDIPMS PWHTKCEKYI CREMWPSRTQ EYYYTLSLFA LQFVVPLGVL IFTYARITIR
VWAKRPPGEA ETNRDQRMAR SKRKMVKMML TVVIVFTCCW LPFNILQLLL NDEEFAHWDP
LPYVWFAFHW LAMSHCCYNP IIYCYMNARF RSGFVQLMHR MPGLRRWCCL RSVGDRMNAT
SGTGPALPLN RMNTSTTYIS ARRKPRATSL RANPLSCGET SPLR
