SIFA_DROME
ID SIFA_DROME Reviewed; 72 AA.
AC Q6IGX9; A8E6Z0; A8E728; B3DMR1; Q8IA34;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Neuropeptide SIFamide {ECO:0000303|PubMed:17126293};
DE Flags: Precursor;
GN Name=SIFa {ECO:0000312|FlyBase:FBgn0053527};
GN Synonyms=IFa {ECO:0000312|FlyBase:FBgn0053527};
GN ORFNames=CG33527 {ECO:0000312|FlyBase:FBgn0053527};
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:DAA02335.1};
RN [1] {ECO:0000312|EMBL:AAO15386.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Terhzaz S., Veenstra J.A.;
RT "Identification of the drosophila neuropeptide IFamide and its cDNA.";
RL Submitted (MAY-2001) 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:ABV82333.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Stapleton M., Carlson J., Frise E., Kapadia B., Park S., Wan K., Yu C.,
RA Celniker S.;
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000312|EMBL:DAA02335.1}
RP IDENTIFICATION.
RX PubMed=14709175; DOI=10.1186/gb-2003-5-1-r3;
RA Hild M., Beckmann B., Haas S.A., Koch B., Solovyev V., Busold C.,
RA Fellenberg K., Boutros M., Vingron M., Sauer F., Hoheisel J.D., Paro R.;
RT "An integrated gene annotation and transcriptional profiling approach
RT towards the full gene content of the Drosophila genome.";
RL Genome Biol. 5:R3.1-R3.17(2003).
RN [6] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=15219831; DOI=10.1016/j.bbrc.2004.05.173;
RA Verleyen P., Huybrechts J., Baggerman G., Van Lommel A., De Loof A.,
RA Schoofs L.;
RT "SIFamide is a highly conserved neuropeptide: a comparative study in
RT different insect species.";
RL Biochem. Biophys. Res. Commun. 320:334-341(2004).
RN [7] {ECO:0000305}
RP 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 [8] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=17126293; DOI=10.1016/j.bbrc.2006.11.030;
RA Terhzaz S., Rosay P., Goodwin S.F., Veenstra J.A.;
RT "The neuropeptide SIFamide modulates sexual behavior in Drosophila.";
RL Biochem. Biophys. Res. Commun. 352:305-310(2007).
RN [9] {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 [10] {ECO:0000305}
RP FUNCTION.
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: Ligand for the neuropeptide SIFamide receptor
CC (PubMed:16378592). Modulates sexual behavior by negatively regulating
CC female receptivity to male courtship and by playing a role in male sex
CC discrimination (PubMed:17126293, PubMed:26469541). Also involved in
CC promoting sleep (PubMed:24658384). {ECO:0000269|PubMed:16378592,
CC ECO:0000269|PubMed:17126293, ECO:0000269|PubMed:24658384,
CC ECO:0000269|PubMed:26469541}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:16378592}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in two pairs of neurons in the
CC pars intercerebralis (at protein level). {ECO:0000269|PubMed:15219831,
CC ECO:0000269|PubMed:17126293}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in SIFa-expressing
CC neurons causes normal male sexual activity towards virgin females but
CC also vigorous courtship directed at other males and also leads to
CC female hyper-receptivity with a dramatic decrease in copulation time
CC (PubMed:17126293). It also causes reduced sleep and shortened sleep
CC bout length (PubMed:24658384). {ECO:0000269|PubMed:17126293,
CC ECO:0000269|PubMed:24658384}.
CC -!- SIMILARITY: Belongs to the FARP (FMRFamide related peptide) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO15386.1; Type=Miscellaneous discrepancy; Note=Probably cloning artifact.; Evidence={ECO:0000305};
CC Sequence=ABV82314.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=ABV82352.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=ACD81713.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF376801; AAO15386.1; ALT_SEQ; mRNA.
DR EMBL; AE013599; AFH08249.1; -; Genomic_DNA.
DR EMBL; BT030932; ABV82314.1; ALT_INIT; mRNA.
DR EMBL; BT030951; ABV82333.1; -; mRNA.
DR EMBL; BT030970; ABV82352.1; ALT_INIT; mRNA.
DR EMBL; BT032699; ACD81713.1; ALT_INIT; mRNA.
DR EMBL; BK003637; DAA02335.1; -; Genomic_DNA.
DR RefSeq; NP_001246496.1; NM_001259567.2.
DR AlphaFoldDB; Q6IGX9; -.
DR IntAct; Q6IGX9; 5.
DR STRING; 7227.FBpp0100173; -.
DR GlyGen; Q6IGX9; 1 site.
DR PaxDb; Q6IGX9; -.
DR EnsemblMetazoa; FBtr0305055; FBpp0293592; FBgn0053527.
DR GeneID; 3346202; -.
DR KEGG; dme:Dmel_CG33527; -.
DR CTD; 3346202; -.
DR FlyBase; FBgn0053527; SIFa.
DR VEuPathDB; VectorBase:FBgn0053527; -.
DR HOGENOM; CLU_199255_0_0_1; -.
DR OMA; DAAYRKP; -.
DR OrthoDB; 1608113at2759; -.
DR BioGRID-ORCS; 3346202; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 3346202; -.
DR PRO; PR:Q6IGX9; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0053527; Expressed in central nervous system and 15 other tissues.
DR ExpressionAtlas; Q6IGX9; baseline and differential.
DR GO; GO:0005615; C:extracellular space; IC:FlyBase.
DR GO; GO:0005179; F:hormone activity; NAS:FlyBase.
DR GO; GO:0005184; F:neuropeptide hormone activity; ISS:FlyBase.
DR GO; GO:0071855; F:neuropeptide receptor binding; IPI:FlyBase.
DR GO; GO:0048018; F:receptor ligand activity; IPI:FlyBase.
DR GO; GO:0048047; P:mating behavior, sex discrimination; IMP:UniProtKB.
DR GO; GO:0007621; P:negative regulation of female receptivity; IMP:FlyBase.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IDA:FlyBase.
DR GO; GO:0045938; P:positive regulation of circadian sleep/wake cycle, sleep; IMP:UniProtKB.
DR GO; GO:0042752; P:regulation of circadian rhythm; IMP:FlyBase.
PE 1: Evidence at protein level;
KW Amidation; Behavior; Glycoprotein; Neuropeptide; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT PEPTIDE 27..38
FT /note="Neuropeptide SIFamide"
FT /evidence="ECO:0000250|UniProtKB:E2ASG4"
FT /id="PRO_5006746508"
FT PROPEP 42..72
FT /evidence="ECO:0000250|UniProtKB:E2ASG4"
FT /id="PRO_0000436206"
FT MOD_RES 38
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000250|UniProtKB:E2ASG4"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 72 AA; 7901 MW; B832A1D73BE93977 CRC64;
MALRFTLTLL LVTILVAAIL LGSSEAAYRK PPFNGSIFGK RNSLDYDSAK MSAVCEVAME
ACPMWFPQND SK
