SPR_DROME
ID SPR_DROME Reviewed; 435 AA.
AC Q8SWR3; Q9W4B9;
DT 22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Sex peptide receptor {ECO:0000312|FlyBase:FBgn0029768};
GN Name=SPR {ECO:0000312|FlyBase:FBgn0029768};
GN ORFNames=CG16752 {ECO:0000312|FlyBase:FBgn0029768};
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 {ECO:0000312|EMBL:AAM12257.1};
RN [1] {ECO:0000312|EMBL:ACC68840.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Nagel J.S., Hauser F., Cazzamali G., Williamson M.R.,
RA Grimmelikhuijzen C.J.P.;
RT "Molecular cloning and characterization of the Drosophila receptor
RT CG16752.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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] {ECO:0000312|EMBL:AAM12257.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=18066048; DOI=10.1038/nature06483;
RA Yapici N., Kim Y.J., Ribeiro C., Dickson B.J.;
RT "A receptor that mediates the post-mating switch in Drosophila reproductive
RT behaviour.";
RL Nature 451:33-37(2008).
RN [6] {ECO:0000305}
RP FUNCTION, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF GLN-192.
RX PubMed=20458515; DOI=10.1007/s00018-010-0393-8;
RA Poels J., Van Loy T., Vandersmissen H.P., Van Hiel B., Van Soest S.,
RA Nachman R.J., Vanden Broeck J.;
RT "Myoinhibiting peptides are the ancestral ligands of the promiscuous
RT Drosophila sex peptide receptor.";
RL Cell. Mol. Life Sci. 67:3511-3522(2010).
RN [7] {ECO:0000305}
RP FUNCTION.
RX PubMed=20308537; DOI=10.1073/pnas.0914764107;
RA Kim Y.J., Bartalska K., Audsley N., Yamanaka N., Yapici N., Lee J.Y.,
RA Kim Y.C., Markovic M., Isaac E., Tanaka Y., Dickson B.J.;
RT "MIPs are ancestral ligands for the sex peptide receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:6520-6525(2010).
RN [8] {ECO:0000305}
RP FUNCTION.
RX PubMed=24089336; DOI=10.1098/rspb.2013.1938;
RA Haussmann I.U., Hemani Y., Wijesekera T., Dauwalder B., Soller M.;
RT "Multiple pathways mediate the sex-peptide-regulated switch in female
RT Drosophila reproductive behaviours.";
RL Proc. R. Soc. Lond., B, Biol. Sci. 280:20131938-20131938(2013).
RN [9] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=25333796; DOI=10.1371/journal.pbio.1001974;
RA Oh Y., Yoon S.E., Zhang Q., Chae H.S., Daubnerova I., Shafer O.T., Choe J.,
RA Kim Y.J.;
RT "A homeostatic sleep-stabilizing pathway in Drosophila composed of the sex
RT peptide receptor and its ligand, the myoinhibitory peptide.";
RL PLoS Biol. 12:E1001974-E1001974(2014).
CC -!- FUNCTION: Receptor for two functionally unrelated ligands; SP (A70A)
CC for controlling reproductive behaviors and MIP for controlling sleep
CC behavior (PubMed:18066048, PubMed:20458515, PubMed:20308537,
CC PubMed:24089336, PubMed:25333796). MIP-SPR pathway functions as a sleep
CC homeostat which perceives the need for sleep and stabilizes it by
CC providing a slow-acting inhibitory input to the fly arousal system that
CC involve the pigment dispersing factor (pdf) neurons (PubMed:25333796).
CC SP-SPR is one of the multiple SP pathways that induce female post-
CC mating behavioral responses (PMR) such as the suppression of mating
CC receptivity and initiation of egg laying (PubMed:18066048,
CC PubMed:24089336). The PMR switch is achieved by mediating the synaptic
CC output of neurons such as those expressing fruitless (fru), double sex
CC (dsx) and pickpocket (ppk) (PubMed:18066048, PubMed:24089336).
CC {ECO:0000269|PubMed:18066048, ECO:0000269|PubMed:20458515,
CC ECO:0000269|PubMed:24089336, ECO:0000269|PubMed:25333796}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18066048};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: In the female, expressed in the reproductive
CC organs; strongly expressed in the spermathecae and the lower oviduct
CC (PubMed:18066048). No expression in the male reproductive organs
CC (PubMed:18066048). In the central nervous system of both sexes, it is
CC expressed in the brain and ventral nerve cord (VNC); strongly expressed
CC in the ventral regions of the suboesophageal ganglion, the cervical
CC connective and in many nerve roots of the brain and VNC
CC (PubMed:18066048, PubMed:25333796). Expressed in the s-LNvs and l-LNvs
CC pdf neurons (at protein level) (PubMed:25333796).
CC {ECO:0000269|PubMed:18066048, ECO:0000269|PubMed:25333796}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development. Highest
CC expression is in the embryos. {ECO:0000269|PubMed:20458515}.
CC -!- DISRUPTION PHENOTYPE: Fully viable without obvious effects in the
CC nervous system or reproductive organs (PubMed:18066048). Sperm transfer
CC and storage in the females is not affected and egg fertilization and
CC development is normal (PubMed:18066048). However, females lay fewer
CC eggs, mate again at high frequency and do not reject a second male
CC after mating (PubMed:18066048). Male and female flies display reduced
CC overall sleep duration associated with shorter sleep-bout lengths,
CC although the number of sleep-bouts is not affected (PubMed:25333796).
CC Sleep recovery following sleep deprivation is also impaired
CC (PubMed:25333796). {ECO:0000269|PubMed:18066048,
CC ECO:0000269|PubMed:25333796}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; EU443243; ACC68840.1; -; mRNA.
DR EMBL; AE014298; AAF46037.2; -; Genomic_DNA.
DR EMBL; AE014298; AHN59363.1; -; Genomic_DNA.
DR EMBL; AE014298; AHN59364.1; -; Genomic_DNA.
DR EMBL; AY095526; AAM12257.1; -; mRNA.
DR RefSeq; NP_001284892.1; NM_001297963.1.
DR RefSeq; NP_001284893.1; NM_001297964.1.
DR RefSeq; NP_572225.1; NM_131997.2.
DR AlphaFoldDB; Q8SWR3; -.
DR SMR; Q8SWR3; -.
DR STRING; 7227.FBpp0070744; -.
DR PaxDb; Q8SWR3; -.
DR DNASU; 31463; -.
DR EnsemblMetazoa; FBtr0070778; FBpp0070744; FBgn0029768.
DR EnsemblMetazoa; FBtr0339781; FBpp0308828; FBgn0029768.
DR EnsemblMetazoa; FBtr0344824; FBpp0311140; FBgn0029768.
DR GeneID; 31463; -.
DR KEGG; dme:Dmel_CG16752; -.
DR UCSC; CG16752-RA; d. melanogaster.
DR CTD; 6697; -.
DR FlyBase; FBgn0029768; SPR.
DR VEuPathDB; VectorBase:FBgn0029768; -.
DR eggNOG; ENOG502QVMK; Eukaryota.
DR GeneTree; ENSGT00730000112478; -.
DR HOGENOM; CLU_009579_24_5_1; -.
DR InParanoid; Q8SWR3; -.
DR OMA; PCRMEDN; -.
DR OrthoDB; 994073at2759; -.
DR PhylomeDB; Q8SWR3; -.
DR BioGRID-ORCS; 31463; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 31463; -.
DR PRO; PR:Q8SWR3; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0029768; Expressed in spermathecum and 10 other tissues.
DR ExpressionAtlas; Q8SWR3; baseline and differential.
DR Genevisible; Q8SWR3; DM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; IPI:FlyBase.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:FlyBase.
DR GO; GO:0045434; P:negative regulation of female receptivity, post-mating; IMP:FlyBase.
DR GO; GO:0046662; P:regulation of oviposition; IMP:FlyBase.
DR InterPro; IPR019427; 7TM_GPCR_serpentine_rcpt_Srw.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF10324; 7TM_GPCR_Srw; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; G-protein coupled receptor; Membrane; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..435
FT /note="Sex peptide receptor"
FT /id="PRO_0000433510"
FT TOPO_DOM 1..93
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 94..114
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 115..124
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 125..145
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 146..168
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 169..189
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 190..211
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 212..229
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 230..276
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 277..297
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 298..327
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 328..348
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 349..368
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 369..389
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 390..435
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT MUTAGEN 192
FT /note="Q->D: Decrease in response to SP. Response to MIP is
FT less affected."
FT /evidence="ECO:0000269|PubMed:20458515"
SQ SEQUENCE 435 AA; 50323 MW; 37FBF60EC292EA64 CRC64;
MDNYTDVLYQ YRLAPSASPE MEMELADPRQ MVRGFHLPTN ESQLEIPDYG NESLDYPNYQ
QMVGGPCRME DNNISYWNLT CDSPLEYAMP LYGYCMPFLL IITIISNSLI VLVLSKKSMA
TPTNFVLMGM AICDMLTVIF PAPGLWYMYT FGNHYKPLHP VSMCLAYSIF NEIMPAMCHT
ISVWLTLALA VQRYIYVCHA PMARTWCTMP RVRRCTAYIA LLAFLHQLPR FFDRTYMPLV
IEWNGSPTEV CHLETSMWVH DYIGVDLYYT SYYLFRVLFV HLLPCIILVT LNILLFAAMR
QAQERRKLLF RENRKKECKK LRETNCTTLM LIVVVSVFLL AEIPIAVVTA MHIVSSLIIE
FLDYGLANIC IMLTNFFLVF SYPINFGIYC GMSRQFRETF KEIFLGRLMA KKDSSTKYSI
VNGARTCTNT NETVL
