A70A_DROME
ID A70A_DROME Reviewed; 55 AA.
AC P05623; O18659; Q6VBF8; Q9VU54;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Accessory gland-specific peptide 70A;
DE AltName: Full=Paragonial peptide B;
DE AltName: Full=Sex peptide;
DE Short=SP;
DE Flags: Precursor;
GN Name=SP; Synonyms=Acp70A, PAPB; ORFNames=CG17673;
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], PROTEIN SEQUENCE OF 20-55, FUNCTION,
RP SUBCELLULAR LOCATION, HYDROXYLATION AT PRO-28; PRO-32; PRO-34; PRO-36 AND
RP PRO-38, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=3135120; DOI=10.1016/0092-8674(88)90192-4;
RA Chen P.S., Stumm-Zollinger E., Aigaki T., Balmer J., Bienz M., Boehlen P.;
RT "A male accessory gland peptide that regulates reproductive behavior of
RT female D. melanogaster.";
RL Cell 54:291-298(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=M11, M2, M26, M36, M40, M47, M54, M55, and M66;
RX PubMed=9286679; DOI=10.1093/genetics/147.1.189;
RA Cirera S., Aguade M.N.;
RT "Evolutionary history of the sex-peptide (Acp70A) gene region in Drosophila
RT melanogaster.";
RL Genetics 147:189-197(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NFS 5.1, NFS 5.2, NFS 5.3, NFS 5.4, NFS 6.1, NFS 6.2, NFS 6.3,
RC NFS 6.4, NFS 7.8, SFS 1.1, SFS 1.2, SFS 1.3, SFS 1.4, SFS 2.2, SFS 2.3,
RC SFS 2.4, SFS 3.1, SFS 3.2, SFS 3.3, and SFS 3.4;
RX PubMed=14761057; DOI=10.1554/03-335;
RA Panhuis T.M., Swanson W.J., Nunney L.;
RT "Population genetics of accessory gland proteins and sexual behavior in
RT Drosophila melanogaster populations from Evolution Canyon.";
RL Evolution 57:2785-2791(2003).
RN [4]
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 [5]
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 [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=12897240; DOI=10.1073/pnas.1631700100;
RA Liu H., Kubli E.;
RT "Sex-peptide is the molecular basis of the sperm effect in Drosophila
RT melanogaster.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:9929-9933(2003).
RN [7]
RP FUNCTION, DOMAIN, CLEAVAGE, AND MUTAGENESIS OF 26-ARG-LYS-27.
RX PubMed=15694303; DOI=10.1016/j.cub.2005.01.034;
RA Peng J., Chen S., Busser S., Liu H., Honegger T., Kubli E.;
RT "Gradual release of sperm bound sex-peptide controls female postmating
RT behavior in Drosophila.";
RL Curr. Biol. 15:207-213(2005).
RN [8]
RP FUNCTION.
RX PubMed=19249273; DOI=10.1016/j.neuron.2008.12.021;
RA Yang C.H., Rumpf S., Xiang Y., Gordon M.D., Song W., Jan L.Y., Jan Y.N.;
RT "Control of the postmating behavioral switch in Drosophila females by
RT internal sensory neurons.";
RL Neuron 61:519-526(2009).
RN [9]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
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 [10]
RP FUNCTION, MUTAGENESIS OF TRP-42; CYS-43; TRP-51 AND CYS-55, AND SYNTHESIS
RP OF 40-55.
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 [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19793753; DOI=10.1098/rspb.2009.1236;
RA Isaac R.E., Li C., Leedale A.E., Shirras A.D.;
RT "Drosophila male sex peptide inhibits siesta sleep and promotes locomotor
RT activity in the post-mated female.";
RL Proc. R. Soc. Lond., B, Biol. Sci. 277:65-70(2010).
RN [12]
RP FUNCTION, AND DOMAIN.
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 [13]
RP STRUCTURE BY NMR OF 20-55, AND DISULFIDE BOND.
RX PubMed=21439282; DOI=10.1016/j.febslet.2011.03.040;
RA Moehle K., Freund A., Kubli E., Robinson J.A.;
RT "NMR studies of the solution conformation of the sex peptide from
RT Drosophila melanogaster.";
RL FEBS Lett. 585:1197-1202(2011).
CC -!- FUNCTION: Male seminal protein which triggers short- and long-term
CC post-mating behavioral responses (PMR) in female Drosophila
CC (PubMed:3135120, PubMed:19249273, PubMed:20308537, PubMed:19793753,
CC PubMed:15694303, PubMed:24089336). Binds initially to sperm where it is
CC later cleaved to release an active peptide within the female
CC reproductive tract. Signals via the sex peptide receptor (SPR) in
CC female flies; may also act via other receptors (PubMed:20458515,
CC PubMed:20308537, PubMed:24089336). Moderates the activity of distinct
CC neuronal circuitries in the female genital tract to promote specific
CC PMRs including: enhanced ovulation, increased egg laying rate,
CC increased feeding/foraging rate, induced antimicrobial peptide
CC synthesis, reduced mating receptivity, reduced day-time sleep and
CC reduced lifespan in multiple mated females (PubMed:3135120,
CC PubMed:15694303, PubMed:19249273, PubMed:19793753, PubMed:24089336).
CC {ECO:0000269|PubMed:15694303, ECO:0000269|PubMed:19249273,
CC ECO:0000269|PubMed:19793753, ECO:0000269|PubMed:20308537,
CC ECO:0000269|PubMed:24089336, ECO:0000269|PubMed:3135120}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3135120}.
CC -!- TISSUE SPECIFICITY: Main cells of the accessory glands of males
CC (paragonial gland). {ECO:0000269|PubMed:20458515,
CC ECO:0000269|PubMed:3135120}.
CC -!- DEVELOPMENTAL STAGE: No expression in females or embryos
CC (PubMed:3135120, PubMed:20458515). Expression levels are highest in
CC male adults with little to no expression until the late pupal stages
CC (PubMed:3135120, PubMed:20458515). {ECO:0000269|PubMed:20458515,
CC ECO:0000269|PubMed:3135120}.
CC -!- PTM: Sperm-bound protein is cleaved to release an active C-terminal
CC peptide. Gradual release from stored sperm may function to prolong PMR
CC and enhance male reproductive success. {ECO:0000269|PubMed:15694303}.
CC -!- DISRUPTION PHENOTYPE: Viable and fertile (PubMed:19793753). Males are
CC able to transfer sperm but can only induce weak PMR behaviors in
CC females (PubMed:12897240, PubMed:19793753).
CC {ECO:0000269|PubMed:12897240, ECO:0000269|PubMed:19793753}.
CC -!- SIMILARITY: Belongs to the Drosophila sex peptide family.
CC {ECO:0000305}.
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DR EMBL; M21201; AAA28816.1; -; mRNA.
DR EMBL; X99407; CAA67784.1; -; Genomic_DNA.
DR EMBL; X99408; CAA67785.1; -; Genomic_DNA.
DR EMBL; X99409; CAA67786.1; -; Genomic_DNA.
DR EMBL; X99410; CAA67787.1; -; Genomic_DNA.
DR EMBL; X99411; CAA67788.1; -; Genomic_DNA.
DR EMBL; X99413; CAA67790.1; -; Genomic_DNA.
DR EMBL; X99415; CAA67792.1; -; Genomic_DNA.
DR EMBL; X99416; CAA67793.1; -; Genomic_DNA.
DR EMBL; X99418; CAA67795.1; -; Genomic_DNA.
DR EMBL; AY344285; AAR04600.1; -; Genomic_DNA.
DR EMBL; AY344286; AAR04601.1; -; Genomic_DNA.
DR EMBL; AY344287; AAR04602.1; -; Genomic_DNA.
DR EMBL; AY344288; AAR04603.1; -; Genomic_DNA.
DR EMBL; AY344289; AAR04604.1; -; Genomic_DNA.
DR EMBL; AY344290; AAR04605.1; -; Genomic_DNA.
DR EMBL; AY344291; AAR04606.1; -; Genomic_DNA.
DR EMBL; AY344292; AAR04607.1; -; Genomic_DNA.
DR EMBL; AY344293; AAR04608.1; -; Genomic_DNA.
DR EMBL; AY344294; AAR04609.1; -; Genomic_DNA.
DR EMBL; AY344295; AAR04610.1; -; Genomic_DNA.
DR EMBL; AY344296; AAR04611.1; -; Genomic_DNA.
DR EMBL; AY344297; AAR04612.1; -; Genomic_DNA.
DR EMBL; AY344298; AAR04613.1; -; Genomic_DNA.
DR EMBL; AY344299; AAR04614.1; -; Genomic_DNA.
DR EMBL; AY344300; AAR04615.1; -; Genomic_DNA.
DR EMBL; AY344301; AAR04616.1; -; Genomic_DNA.
DR EMBL; AY344302; AAR04617.1; -; Genomic_DNA.
DR EMBL; AY344303; AAR04618.1; -; Genomic_DNA.
DR EMBL; AY344304; AAR04619.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF49836.1; -; Genomic_DNA.
DR PIR; A28911; A28911.
DR RefSeq; NP_524057.2; NM_079333.2.
DR PDB; 2LAQ; NMR; -; A=20-55.
DR PDBsum; 2LAQ; -.
DR AlphaFoldDB; P05623; -.
DR SMR; P05623; -.
DR BioGRID; 64839; 2.
DR IntAct; P05623; 1.
DR STRING; 7227.FBpp0075572; -.
DR PaxDb; P05623; -.
DR PRIDE; P05623; -.
DR GeneID; 39494; -.
DR KEGG; dme:Dmel_CG17673; -.
DR CTD; 39494; -.
DR FlyBase; FBgn0003034; SP.
DR HOGENOM; CLU_3034552_0_0_1; -.
DR SignaLink; P05623; -.
DR BioGRID-ORCS; 39494; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 39494; -.
DR PRO; PR:P05623; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Genevisible; P05623; DM.
DR GO; GO:0005576; C:extracellular region; TAS:FlyBase.
DR GO; GO:0005615; C:extracellular space; HDA:FlyBase.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IPI:FlyBase.
DR GO; GO:0005179; F:hormone activity; NAS:FlyBase.
DR GO; GO:0008343; P:adult feeding behavior; IMP:FlyBase.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:FlyBase.
DR GO; GO:0007621; P:negative regulation of female receptivity; IDA:FlyBase.
DR GO; GO:0045434; P:negative regulation of female receptivity, post-mating; IMP:FlyBase.
DR GO; GO:0046008; P:regulation of female receptivity, post-mating; IMP:FlyBase.
DR GO; GO:0007557; P:regulation of juvenile hormone biosynthetic process; TAS:FlyBase.
DR GO; GO:0046662; P:regulation of oviposition; IDA:FlyBase.
DR GO; GO:0019953; P:sexual reproduction; HEP:FlyBase.
DR InterPro; IPR012608; Sex_peptide.
DR Pfam; PF08138; Sex_peptide; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Behavior; Cleavage on pair of basic residues;
KW Direct protein sequencing; Disulfide bond; Hydroxylation;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:3135120"
FT CHAIN 20..55
FT /note="Accessory gland-specific peptide 70A"
FT /id="PRO_0000020587"
FT REGION 20..33
FT /note="Essential for binding to sperm"
FT /evidence="ECO:0000269|PubMed:15694303"
FT REGION 36..55
FT /note="Sufficient to induce PMR"
FT /evidence="ECO:0000269|PubMed:24089336"
FT SITE 26..27
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:15694303"
FT MOD_RES 28
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:3135120"
FT MOD_RES 32
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:3135120"
FT MOD_RES 33
FT /note="Isoleucine derivative"
FT MOD_RES 34
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:3135120"
FT MOD_RES 36
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:3135120"
FT MOD_RES 38
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:3135120"
FT DISULFID 43..55
FT /evidence="ECO:0000269|PubMed:21439282"
FT VARIANT 19
FT /note="S -> A (in strain: Berkeley, M2, M26, M36, M40, M55
FT and SFS 3.4)"
FT VARIANT 46
FT /note="N -> I (in strain: SFS 3.4)"
FT MUTAGEN 26..27
FT /note="RK->QQ: Abolishes cleavage from sperm and prevents
FT release of C-terminal fragment for long-term PMR. Short-
FT term PMR in unaffected."
FT /evidence="ECO:0000269|PubMed:15694303"
FT MUTAGEN 42
FT /note="W->A: Complete loss of activity; when associated
FT with A-51. Complete loss of activity; when associated with
FT A-43; A-51 and A-55."
FT /evidence="ECO:0000269|PubMed:20308537"
FT MUTAGEN 43
FT /note="C->A: Complete loss of activity; when associated
FT with A-42; A-51 and A-55."
FT /evidence="ECO:0000269|PubMed:20308537"
FT MUTAGEN 51
FT /note="W->A: Complete loss of activity; when associated
FT with A-42. Complete loss of activity; when associated with
FT A-42; A-43 and A-55."
FT /evidence="ECO:0000269|PubMed:20308537"
FT MUTAGEN 55
FT /note="C->A: Complete loss of activity; when associated
FT with A-42; A-43 and A-51."
FT /evidence="ECO:0000269|PubMed:20308537"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:2LAQ"
SQ SEQUENCE 55 AA; 6378 MW; F6827A1F025BF23D CRC64;
MKTLALFLVL VCVLGLVQSW EWPWNRKPTK FPIPSPNPRD KWCRLNLGPA WGGRC
