SIFAR_DROME
ID SIFAR_DROME Reviewed; 758 AA.
AC Q8IN35; Q7YU49;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Neuropeptide SIFamide receptor {ECO:0000303|PubMed:16378592};
GN Name=SIFaR {ECO:0000312|FlyBase:FBgn0038880};
GN Synonyms=SIFR {ECO:0000312|FlyBase:FBgn0038880};
GN ORFNames=CG10823 {ECO:0000312|FlyBase:FBgn0038880};
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|Proteomes:UP000000803};
RN [1] {ECO:0000312|EMBL:ABB96223.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=16378592; DOI=10.1016/j.bbrc.2005.12.062;
RA Jorgensen L.M., Hauser F., Cazzamali G., Williamson M.,
RA Grimmelikhuijzen C.J.;
RT "Molecular identification of the first SIFamide receptor.";
RL Biochem. Biophys. Res. Commun. 340:696-701(2006).
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:AAQ22457.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAQ22457.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAQ22457.1};
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., Celniker S.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24658384; DOI=10.14348/molcells.2014.2371;
RA Park S., Sonn J.Y., Oh Y., Lim C., Choe J.;
RT "SIFamide and SIFamide receptor defines a novel neuropeptide signaling to
RT promote sleep in Drosophila.";
RL Mol. Cells 37:295-301(2014).
RN [6] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=26469541; DOI=10.1016/j.peptides.2015.10.003;
RA Sellami A., Veenstra J.A.;
RT "SIFamide acts on fruitless neurons to modulate sexual behavior in
RT Drosophila melanogaster.";
RL Peptides 74:50-56(2015).
CC -!- FUNCTION: Receptor for the neuropeptide SIFamide (PubMed:16378592).
CC Modulates sexual behavior by playing a role in male sex discrimination
CC (PubMed:26469541). Also involved in promoting sleep (PubMed:24658384).
CC {ECO:0000269|PubMed:16378592, ECO:0000269|PubMed:24658384,
CC ECO:0000269|PubMed:26469541}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: In the larva, expressed in a bilateral pair of
CC neurons in each of the abdominal rhabdomeres. In the adult, expressed
CC predominantly in the central nervous system with expression also
CC detected in two neurons in the uterus. {ECO:0000269|PubMed:26469541}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes a significant
CC reduction in total sleep amount (PubMed:24658384). It also causes
CC significant male-male courtship behavior although a number of flies
CC appear to behave normally (PubMed:26469541).
CC {ECO:0000269|PubMed:24658384, ECO:0000269|PubMed:26469541}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|RuleBase:RU000688}.
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DR EMBL; DQ285411; ABB96223.1; -; mRNA.
DR EMBL; AE014297; AAN13859.2; -; Genomic_DNA.
DR EMBL; AE014297; ACZ94970.1; -; Genomic_DNA.
DR EMBL; BT009988; AAQ22457.1; -; mRNA.
DR RefSeq; NP_001163674.1; NM_001170203.1.
DR RefSeq; NP_650966.2; NM_142709.2.
DR AlphaFoldDB; Q8IN35; -.
DR SMR; Q8IN35; -.
DR IntAct; Q8IN35; 2.
DR STRING; 7227.FBpp0291029; -.
DR GlyGen; Q8IN35; 3 sites.
DR PaxDb; Q8IN35; -.
DR DNASU; 42530; -.
DR EnsemblMetazoa; FBtr0084098; FBpp0083497; FBgn0038880.
DR EnsemblMetazoa; FBtr0301815; FBpp0291029; FBgn0038880.
DR GeneID; 42530; -.
DR KEGG; dme:Dmel_CG10823; -.
DR UCSC; CG10823-RA; d. melanogaster.
DR CTD; 42530; -.
DR FlyBase; FBgn0038880; SIFaR.
DR VEuPathDB; VectorBase:FBgn0038880; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01020000230390; -.
DR HOGENOM; CLU_018892_0_0_1; -.
DR InParanoid; Q8IN35; -.
DR OMA; PQFLCQE; -.
DR OrthoDB; 830221at2759; -.
DR PhylomeDB; Q8IN35; -.
DR Reactome; R-DME-416476; G alpha (q) signalling events.
DR BioGRID-ORCS; 42530; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 42530; -.
DR PRO; PR:Q8IN35; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0038880; Expressed in brain and 4 other tissues.
DR GO; GO:0016021; C:integral component of membrane; ISS:FlyBase.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:FlyBase.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; ISS:FlyBase.
DR GO; GO:0004930; F:G protein-coupled receptor activity; ISS:FlyBase.
DR GO; GO:0008188; F:neuropeptide receptor activity; IPI:FlyBase.
DR GO; GO:0004983; F:neuropeptide Y receptor activity; IEA:InterPro.
DR GO; GO:0042277; F:peptide binding; IBA:GO_Central.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:FlyBase.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:FlyBase.
DR GO; GO:0048047; P:mating behavior, sex discrimination; IMP:UniProtKB.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IDA:FlyBase.
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 Behavior; Cell membrane; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..758
FT /note="Neuropeptide SIFamide receptor"
FT /evidence="ECO:0000305"
FT /id="PRO_0000436207"
FT TOPO_DOM 1..104
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 105..125
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 126..212
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 213..233
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 234..254
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 255..275
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 276..282
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 283..303
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 304..323
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 324..344
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 345..386
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 387..407
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 408..436
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 437..457
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 458..758
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 758 AA; 83442 MW; A2E3BC8D566E009B CRC64;
MMAASGRIRK RKHKSHTSGD VPSTTTSVPM PIPTMAPGKM VAETMEEAAA LAGDYNNFTH
NFVDLQNLLS FNELNGTSGS GGTAVSSLGS SSAIKLNNSA ITDTLLGTVL TTATATVAPA
ASSLLATLAA TTTASARGSL AGKSLAIADA TSSTYYSNLL NLSPATTSLI SAAAATKSYN
DSALRWEQLD GSVDFGFDPL YRHSLAMSMV YCVAYIVVFL VGLIGNSFVI AVVLRAPRMR
TVTNYFIVNL AIADILVIVF CLPATLIGNI FVPWMLGWLM CKFVPYIQGV SVAASVYSLI
AVSLDRFIAI WWPLKQMTKR RARIMIIGIW VIALVTTIPW LLFFDLVPAE EVFSDALVSA
YSQPQFLCQE VWPPGTDGNL YFLLANLVAC YLLPMSLITL CYVLIWIKVS TRSIPGESKD
AQMDRMQQKS KVKVIKMLVA VVILFVLSWL PLYVIFARIK FGSDISQEEF EILKKVMPVA
QWLGSSNSCI NPILYSVNKK YRRGFAAIIK SRSCCGRLRY YDNVAIASST TSTRKSSHYH
QNSSRKSPSS KGNAVSYIYE HNSLRRHNMM LKQDSNLSQQ MLLKQDSHGS RQFLIKQESS
CSDASGIRRP LCQQDSNGSK VSLSKQDSIV SYMEARRSAG HGLNDTLVDR DSVSMDVGRR
QGATPSSLLD KRQKFVKQDS VISFVDQRPE QRRHQLVKQD SVISFADQRR GLLHKQDSLM
ANRTGDAPTH HVSILKKTDS QLSYGSSTSP RRNADLYE
