MS2A_DROME
ID MS2A_DROME Reviewed; 264 AA.
AC P10333; O76297; O76298; O76299; Q29QG7; Q6VBG2; Q6VBG3; Q6VBG4; Q6VBG7;
AC Q6VBG8; Q6VBG9; Q6VBH0; Q6VBH1; Q6VBH5; Q6VBH7; Q6VBH8; Q6VBH9; Q95NY9;
AC Q95PE8; Q9TVI6; Q9TVV6; Q9TVX0; Q9TW14; Q9TW58; Q9TW61; Q9TW81; Q9UB44;
AC Q9UB45; Q9UB46; Q9UB47; Q9UB48; Q9UB49; Q9UB50; Q9UB51; Q9UB52; Q9UB53;
AC Q9UB54; Q9UB55; Q9UB56; Q9UB57; Q9UB58; Q9UB59; Q9UB60; Q9UB61; Q9UB62;
AC Q9UB63; Q9UB64; Q9UB65; Q9UB66; Q9UB67; Q9UB68; Q9UB69; Q9UB70; Q9UB71;
AC Q9UB72; Q9UB73; Q9UB74; Q9UB75; Q9UB76; Q9UB77; Q9VML6;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Accessory gland-specific peptide 26Aa {ECO:0000303|PubMed:9799260};
DE AltName: Full=Male accessory gland secretory protein 355A {ECO:0000303|PubMed:3142802};
DE Contains:
DE RecName: Full=CP1-N {ECO:0000303|PubMed:24514904};
DE Contains:
DE RecName: Full=CP1-C {ECO:0000303|PubMed:24514904};
DE Contains:
DE RecName: Full=CP2-N {ECO:0000303|PubMed:24514904};
DE Contains:
DE RecName: Full=CP2-C {ECO:0000303|PubMed:24514904};
DE Contains:
DE RecName: Full=CP3-N {ECO:0000303|PubMed:24514904};
DE Contains:
DE RecName: Full=CP3-C {ECO:0000303|PubMed:24514904};
DE Flags: Precursor;
GN Name=Acp26Aa {ECO:0000303|PubMed:9799260, ECO:0000312|FlyBase:FBgn0002855};
GN Synonyms=msp355a {ECO:0000303|PubMed:3142802}, Mst26Aa,
GN mst355a {ECO:0000303|PubMed:3142802}, ovulin {ECO:0000303|PubMed:10662669};
GN ORFNames=CG8982 {ECO:0000312|FlyBase:FBgn0002855};
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 [GENOMIC DNA], SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, PROTEOLYTIC PROCESSING, AND PROTEOLYTIC PROCESSING (CP1-C AND
RP CP2-C).
RC STRAIN=Canton-S;
RX PubMed=3142802; DOI=10.1101/gad.2.9.1063;
RA Monsma S.A., Wolfner M.F.;
RT "Structure and expression of a Drosophila male accessory gland gene whose
RT product resembles a peptide pheromone precursor.";
RL Genes Dev. 2:1063-1073(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NC-001, NC-002, NC-003, NC-004, NC-005, NC-006, NC-007, NC-008,
RC NC-009, and NC-010;
RX PubMed=1361475; DOI=10.1093/genetics/132.3.755;
RA Aguade M., Miyashita N., Langley C.H.;
RT "Polymorphism and divergence in the Mst26A male accessory gland gene region
RT in Drosophila.";
RL Genetics 132:755-770(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=La10, La105, La106, La108, La116, La118, La120, La125, La13, La14,
RC La15, La25, La27, La28, La3, La31, La32, La36, La37, La46, La54, La58,
RC La60, La62, Ma11, Ma18, Ma20, Ma21, Ma23, Ma24, Ma3, Ma31, Ma35, Ma37,
RC Ma43, Ma50, Ma53, Ma56, Ma57, Ma6, Ma60, Ma74, Mo13a, Mo29b, Mo34a, Mo36a,
RC Mo37a, Mo40b, Mo47a, Mo52b, Mo79b, and Mo80b;
RX PubMed=9799260; DOI=10.1093/genetics/150.3.1079;
RA Aguade M.;
RT "Different forces drive the evolution of the Acp26Aa and Acp26Ab accessory
RT gland genes in the Drosophila melanogaster species complex.";
RL Genetics 150:1079-1089(1998).
RN [4]
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 1.4, SFS 2.2, SFS 2.3, SFS 2.4,
RC 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 [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 8-264.
RC STRAIN=AF1, AF10, AF2, AF3, AF4, AF5, AF6, AF7, AF8, AF9, Au1, Au10, Au2,
RC Au3, Au4, Au5, Au6, Au7, Au8, Au9, NC-001, NC-002, NC-003, NC-004, NC-005,
RC NC-006, NC-007, NC-008, NC-009, NC-010, Ny1, Ny2, Ny3, Ny4, Ny5, Ny6, Ny7,
RC Ny8, TW1, TW10, TW11, TW2, TW3, TW4, TW5, TW6, TW7, TW8, and TW9;
RX PubMed=9718731; DOI=10.1093/oxfordjournals.molbev.a026002;
RA Tsaur S.-C., Ting C.-T., Wu C.-I.;
RT "Positive selection driving the evolution of a gene of male reproduction,
RT Acp26Aa, of Drosophila: II. Divergence versus polymorphism.";
RL Mol. Biol. Evol. 15:1040-1046(1998).
RN [9]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, GLYCOSYLATION,
RP PROTEOLYTIC PROCESSING, AND PROTEOLYTIC PROCESSING (CP1-C AND CP2-C).
RX PubMed=2257979; DOI=10.1016/0012-1606(90)90368-s;
RA Monsma S.A., Harada H.A., Wolfner M.F.;
RT "Synthesis of two Drosophila male accessory gland proteins and their fate
RT after transfer to the female during mating.";
RL Dev. Biol. 142:465-475(1990).
RN [10]
RP TISSUE SPECIFICITY, GLYCOSYLATION, PROTEOLYTIC PROCESSING, AND PROTEOLYTIC
RP PROCESSING (CP1-C AND CP2-C).
RX PubMed=7556947; DOI=10.1006/dbio.1995.1315;
RA Park M., Wolfner M.F.;
RT "Male and female cooperate in the prohormone-like processing of a
RT Drosophila melanogaster seminal fluid protein.";
RL Dev. Biol. 171:694-702(1995).
RN [11]
RP FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF 43-LYS--LEU-264.
RX PubMed=7479736; DOI=10.1073/pnas.92.22.10114;
RA Herndon L.A., Wolfner M.F.;
RT "A Drosophila seminal fluid protein, Acp26Aa, stimulates egg laying in
RT females for 1 day after mating.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:10114-10118(1995).
RN [12]
RP TISSUE SPECIFICITY, AND PROTEOLYTIC PROCESSING.
RX PubMed=10612039; DOI=10.1016/s0965-1748(99)00078-8;
RA Lung O., Wolfner M.F.;
RT "Drosophila seminal fluid proteins enter the circulatory system of the
RT mated female fly by crossing the posterior vaginal wall.";
RL Insect Biochem. Mol. Biol. 29:1043-1052(1999).
RN [13]
RP FUNCTION, AND MUTAGENESIS OF 43-LYS--LEU-264.
RX PubMed=10662669; DOI=10.1016/s0960-9822(00)00288-8;
RA Heifetz Y., Lung O., Frongillo E.A. Jr., Wolfner M.F.;
RT "The Drosophila seminal fluid protein Acp26Aa stimulates release of oocytes
RT by the ovary.";
RL Curr. Biol. 10:99-102(2000).
RN [14]
RP FUNCTION, AND FUNCTION (CP3-N AND CP3-C).
RX PubMed=15640356; DOI=10.1073/pnas.0407692102;
RA Heifetz Y., Vandenberg L.N., Cohn H.I., Wolfner M.F.;
RT "Two cleavage products of the Drosophila accessory gland protein ovulin can
RT independently induce ovulation.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:743-748(2005).
RN [15]
RP SUBUNIT, AND SUBUNIT (CP3-C).
RX PubMed=17130459; DOI=10.1073/pnas.0601849103;
RA Wong A., Albright S.N., Wolfner M.F.;
RT "Evidence for structural constraint on ovulin, a rapidly evolving
RT Drosophila melanogaster seminal protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:18644-18649(2006).
RN [16]
RP SUBUNIT, TISSUE SPECIFICITY, AND MUTAGENESIS OF 224-TYR--TYR-228;
RP 229-LEU--LEU-232; 236-SER--ILE-239 AND 243-ILE--VAL-246.
RX PubMed=20138215; DOI=10.1016/j.ibmb.2010.01.009;
RA Wong A., Christopher A.B., Buehner N.A., Wolfner M.F.;
RT "Immortal coils: conserved dimerization motifs of the Drosophila ovulation
RT prohormone ovulin.";
RL Insect Biochem. Mol. Biol. 40:303-310(2010).
RN [17]
RP FUNCTION.
RX PubMed=24101486; DOI=10.1073/pnas.1220018110;
RA Rubinstein C.D., Wolfner M.F.;
RT "Drosophila seminal protein ovulin mediates ovulation through female
RT octopamine neuronal signaling.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:17420-17425(2013).
RN [18]
RP TISSUE SPECIFICITY, PROTEOLYTIC PROCESSING BY SEMP1, PROTEOLYTIC PROCESSING
RP BY SEMP1 (CP1-C AND CP2-C), AND CLEAVAGE SITE.
RX PubMed=24514904; DOI=10.1534/genetics.113.160101;
RA Laflamme B.A., Avila F.W., Michalski K., Wolfner M.F.;
RT "A Drosophila protease cascade member, seminal metalloprotease-1, is
RT activated stepwise by male factors and requires female factors for full
RT activity.";
RL Genetics 196:1117-1129(2014).
CC -!- FUNCTION: Male seminal protein which enhances ovulation in female
CC Drosophila by stimulating the release of oocytes by the ovary following
CC mating (PubMed:7479736, PubMed:15640356, PubMed:24101486,
CC PubMed:10662669). Acts by increasing octopamine (OA) neuronal signaling
CC in the female genital tract leading to the postmating relaxation of the
CC oviduct muscles (PubMed:24101486). This activation of the OA signaling
CC pathway is likely to indirectly contribute to the mating-dependent
CC increase in the number of OA synaptic sites in the female reproductive
CC tract (PubMed:24101486). {ECO:0000269|PubMed:10662669,
CC ECO:0000269|PubMed:15640356, ECO:0000269|PubMed:24101486,
CC ECO:0000269|PubMed:7479736}.
CC -!- FUNCTION: [CP3-N]: Male seminal peptide which is able to enhance
CC ovulation in female Drosophila. {ECO:0000269|PubMed:15640356}.
CC -!- FUNCTION: [CP3-C]: Male seminal peptide which is able to enhance
CC ovulation in female Drosophila. {ECO:0000269|PubMed:15640356}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17130459,
CC ECO:0000269|PubMed:20138215}.
CC -!- SUBUNIT: [CP3-C]: May form a homodimer. {ECO:0000269|PubMed:17130459}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3142802}. Cytoplasm
CC {ECO:0000269|PubMed:2257979}. Note=In 1 day old virgin males, secreted
CC into the cytoplasm of accessory gland cells (PubMed:2257979). In 5 day
CC old males it localizes to cytoplasmic vesicles of the secondary cells
CC (PubMed:2257979). {ECO:0000269|PubMed:2257979}.
CC -!- TISSUE SPECIFICITY: Produced in the male accessory glands and secreted
CC into seminal fluid (at protein level) (PubMed:2257979, PubMed:7556947,
CC PubMed:7479736, PubMed:3142802, PubMed:10612039). Detected in the main
CC cells and secondary cells of the accessory glands of 1 day old males
CC (at protein level) (PubMed:2257979, PubMed:7556947, PubMed:7479736,
CC PubMed:20138215, PubMed:24514904). In 5 day old males, confined to the
CC secondary cells and only reappears in the main cells after mating (at
CC protein level) (PubMed:2257979). Produced in adult males 3-4 hr after
CC eclosion, levels increase reaching a peak at day 3-5 which is
CC maintained until at least day 10 of adulthood (at protein level)
CC (PubMed:2257979). In unmated male adults, levels are maintained for the
CC first 6 days of adulthood and then gradually decrease for at least the
CC next 8 days (PubMed:2257979). In mated females, detected in the genital
CC tract 3 minutes after the start of mating (ASM) and is secreted into
CC the female hemolymph via the posterior vaginal wall 5 minutes ASM (at
CC protein level) (PubMed:2257979, PubMed:7556947, PubMed:10612039).
CC {ECO:0000269|PubMed:10612039, ECO:0000269|PubMed:20138215,
CC ECO:0000269|PubMed:2257979, ECO:0000269|PubMed:24514904,
CC ECO:0000269|PubMed:3142802, ECO:0000269|PubMed:7479736,
CC ECO:0000269|PubMed:7556947}.
CC -!- INDUCTION: Up-regulated in response to mating.
CC {ECO:0000269|PubMed:2257979}.
CC -!- PTM: Glycosylation. {ECO:0000269|PubMed:2257979,
CC ECO:0000269|PubMed:7556947}.
CC -!- PTM: Undergoes several cleavages as it is secreted and is further
CC processed in the recipient female (PubMed:3142802, PubMed:2257979,
CC PubMed:7556947, PubMed:24514904, PubMed:10612039). The precursor
CC molecule is proteolytically cleaved by the seminal metalloprotease
CC Semp1 at Lys-48 to produce CP1-N and CP1-C (PubMed:3142802,
CC PubMed:2257979, PubMed:7556947, PubMed:24514904).
CC {ECO:0000269|PubMed:10612039, ECO:0000269|PubMed:2257979,
CC ECO:0000269|PubMed:24514904, ECO:0000269|PubMed:3142802,
CC ECO:0000269|PubMed:7556947}.
CC -!- PTM: [CP1-C]: Cleaved at Lys-67 by Semp1 to generate CP2-N and CP2-C
CC (PubMed:3142802, PubMed:2257979, PubMed:7556947, PubMed:24514904).
CC Cleavage appears to take place in the mated female genital tract
CC (PubMed:2257979, PubMed:7556947). {ECO:0000269|PubMed:2257979,
CC ECO:0000269|PubMed:24514904, ECO:0000269|PubMed:3142802,
CC ECO:0000269|PubMed:7556947}.
CC -!- PTM: [CP2-C]: Cleaved at Lys-117 by Semp1 to generate CP3-N and CP3-C
CC (PubMed:3142802, PubMed:2257979, PubMed:7556947, PubMed:24514904).
CC Cleavage appears to take place in the mated female genital tract
CC (PubMed:2257979, PubMed:7556947). {ECO:0000269|PubMed:2257979,
CC ECO:0000269|PubMed:24514904, ECO:0000269|PubMed:3142802,
CC ECO:0000269|PubMed:7556947}.
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DR EMBL; Y00219; CAA68366.1; -; Genomic_DNA.
DR EMBL; X70888; CAA50232.1; -; Genomic_DNA.
DR EMBL; X70889; CAA50234.1; -; Genomic_DNA.
DR EMBL; X70890; CAA50236.1; -; Genomic_DNA.
DR EMBL; X70891; CAA50238.1; -; Genomic_DNA.
DR EMBL; X70892; CAA50240.1; -; Genomic_DNA.
DR EMBL; X70893; CAA50242.1; -; Genomic_DNA.
DR EMBL; X70894; CAA50244.1; -; Genomic_DNA.
DR EMBL; X70895; CAA50246.1; -; Genomic_DNA.
DR EMBL; X70896; CAA50248.1; -; Genomic_DNA.
DR EMBL; X70897; CAA50250.1; -; Genomic_DNA.
DR EMBL; AJ231350; CAB37194.1; -; Genomic_DNA.
DR EMBL; AJ231351; CAB37196.1; -; Genomic_DNA.
DR EMBL; AJ231352; CAB37198.1; -; Genomic_DNA.
DR EMBL; AJ231353; CAB37200.1; -; Genomic_DNA.
DR EMBL; AJ231354; CAB37202.1; -; Genomic_DNA.
DR EMBL; AJ231355; CAB37204.1; -; Genomic_DNA.
DR EMBL; AJ231356; CAB37206.1; -; Genomic_DNA.
DR EMBL; AJ231357; CAB37208.1; -; Genomic_DNA.
DR EMBL; AJ231358; CAB37210.1; -; Genomic_DNA.
DR EMBL; AJ231359; CAB37212.1; -; Genomic_DNA.
DR EMBL; AJ231360; CAB37214.1; -; Genomic_DNA.
DR EMBL; AJ231361; CAB37216.1; -; Genomic_DNA.
DR EMBL; AJ231362; CAB37218.1; -; Genomic_DNA.
DR EMBL; AJ231363; CAB37220.1; -; Genomic_DNA.
DR EMBL; AJ231364; CAB37222.1; -; Genomic_DNA.
DR EMBL; AJ231365; CAB37224.1; -; Genomic_DNA.
DR EMBL; AJ231366; CAB37226.1; -; Genomic_DNA.
DR EMBL; AJ231367; CAB37228.1; -; Genomic_DNA.
DR EMBL; AJ231368; CAB37230.1; -; Genomic_DNA.
DR EMBL; AJ231369; CAB37232.1; -; Genomic_DNA.
DR EMBL; AJ231370; CAB37234.1; -; Genomic_DNA.
DR EMBL; AJ231371; CAB37236.1; -; Genomic_DNA.
DR EMBL; AJ231372; CAB37238.1; -; Genomic_DNA.
DR EMBL; AJ231373; CAB37240.1; -; Genomic_DNA.
DR EMBL; AJ231374; CAB37623.1; -; Genomic_DNA.
DR EMBL; AJ231375; CAB37242.1; -; Genomic_DNA.
DR EMBL; AJ231376; CAB37244.1; -; Genomic_DNA.
DR EMBL; AJ231377; CAB37246.1; -; Genomic_DNA.
DR EMBL; AJ231378; CAB37248.1; -; Genomic_DNA.
DR EMBL; AJ231379; CAB37250.1; -; Genomic_DNA.
DR EMBL; AJ231380; CAB37252.1; -; Genomic_DNA.
DR EMBL; AJ231381; CAB37254.1; -; Genomic_DNA.
DR EMBL; AJ231382; CAB37256.1; -; Genomic_DNA.
DR EMBL; AJ231383; CAB37258.1; -; Genomic_DNA.
DR EMBL; AJ231384; CAB37260.1; -; Genomic_DNA.
DR EMBL; AJ231385; CAB37262.1; -; Genomic_DNA.
DR EMBL; AJ231386; CAB37264.1; -; Genomic_DNA.
DR EMBL; AJ231387; CAB37266.1; -; Genomic_DNA.
DR EMBL; AJ231388; CAB37268.1; -; Genomic_DNA.
DR EMBL; AJ231389; CAB37270.1; -; Genomic_DNA.
DR EMBL; AJ231390; CAB37272.1; -; Genomic_DNA.
DR EMBL; AJ231391; CAB37274.1; -; Genomic_DNA.
DR EMBL; AJ231392; CAB37276.1; -; Genomic_DNA.
DR EMBL; AJ231393; CAB37278.1; -; Genomic_DNA.
DR EMBL; AJ231394; CAB37280.1; -; Genomic_DNA.
DR EMBL; AJ231395; CAB37282.1; -; Genomic_DNA.
DR EMBL; AJ231396; CAB37284.1; -; Genomic_DNA.
DR EMBL; AJ231397; CAB37286.1; -; Genomic_DNA.
DR EMBL; AJ231398; CAB37288.1; -; Genomic_DNA.
DR EMBL; AJ231399; CAB37290.1; -; Genomic_DNA.
DR EMBL; AJ231400; CAB37292.1; -; Genomic_DNA.
DR EMBL; AJ231401; CAB37628.1; -; Genomic_DNA.
DR EMBL; AY344246; AAR04561.1; -; Genomic_DNA.
DR EMBL; AY344247; AAR04562.1; -; Genomic_DNA.
DR EMBL; AY344248; AAR04563.1; -; Genomic_DNA.
DR EMBL; AY344249; AAR04564.1; -; Genomic_DNA.
DR EMBL; AY344250; AAR04565.1; -; Genomic_DNA.
DR EMBL; AY344251; AAR04566.1; -; Genomic_DNA.
DR EMBL; AY344252; AAR04567.1; -; Genomic_DNA.
DR EMBL; AY344253; AAR04568.1; -; Genomic_DNA.
DR EMBL; AY344254; AAR04569.1; -; Genomic_DNA.
DR EMBL; AY344255; AAR04570.1; -; Genomic_DNA.
DR EMBL; AY344256; AAR04571.1; -; Genomic_DNA.
DR EMBL; AY344257; AAR04572.1; -; Genomic_DNA.
DR EMBL; AY344258; AAR04573.1; -; Genomic_DNA.
DR EMBL; AY344259; AAR04574.1; -; Genomic_DNA.
DR EMBL; AY344260; AAR04575.1; -; Genomic_DNA.
DR EMBL; AY344261; AAR04576.1; -; Genomic_DNA.
DR EMBL; AY344262; AAR04577.1; -; Genomic_DNA.
DR EMBL; AY344263; AAR04578.1; -; Genomic_DNA.
DR EMBL; AY344264; AAR04579.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF52298.1; -; Genomic_DNA.
DR EMBL; BT024423; ABC86485.1; -; mRNA.
DR EMBL; AF052470; AAC27995.1; -; Genomic_DNA.
DR EMBL; AF052471; AAC27997.1; -; Genomic_DNA.
DR EMBL; AF052472; AAC27999.1; -; Genomic_DNA.
DR EMBL; AF052473; AAC28001.1; -; Genomic_DNA.
DR EMBL; AF052474; AAC28003.1; -; Genomic_DNA.
DR EMBL; AF052475; AAC28005.1; -; Genomic_DNA.
DR EMBL; AF052476; AAC28007.1; -; Genomic_DNA.
DR EMBL; AF052477; AAC28009.1; -; Genomic_DNA.
DR EMBL; AF052478; AAC28011.1; -; Genomic_DNA.
DR EMBL; AF052479; AAC28013.1; -; Genomic_DNA.
DR EMBL; AF052480; AAC28015.1; -; Genomic_DNA.
DR EMBL; AF052481; AAC28017.1; -; Genomic_DNA.
DR EMBL; AF053250; AAC28790.1; -; Genomic_DNA.
DR EMBL; AF053251; AAC28792.1; -; Genomic_DNA.
DR EMBL; AF053252; AAC28794.1; -; Genomic_DNA.
DR EMBL; AF053253; AAC28796.1; -; Genomic_DNA.
DR EMBL; AF053254; AAC28798.1; -; Genomic_DNA.
DR EMBL; AF053255; AAC28800.1; -; Genomic_DNA.
DR EMBL; AF053256; AAC28802.1; -; Genomic_DNA.
DR EMBL; AF053257; AAC28804.1; -; Genomic_DNA.
DR EMBL; AF053258; AAC28806.1; -; Genomic_DNA.
DR EMBL; AF053259; AAC28808.1; -; Genomic_DNA.
DR EMBL; AF053260; AAC28810.1; -; Genomic_DNA.
DR EMBL; AF053261; AAC28812.1; -; Genomic_DNA.
DR EMBL; AF053262; AAC28814.1; -; Genomic_DNA.
DR EMBL; AF053263; AAC28816.1; -; Genomic_DNA.
DR EMBL; AF053264; AAC28818.1; -; Genomic_DNA.
DR EMBL; AF053265; AAC28820.1; -; Genomic_DNA.
DR EMBL; AF053266; AAC28822.1; -; Genomic_DNA.
DR EMBL; AF053267; AAC28824.1; -; Genomic_DNA.
DR EMBL; AF053268; AAC28826.1; -; Genomic_DNA.
DR EMBL; AF053269; AAC28828.1; -; Genomic_DNA.
DR EMBL; AF053270; AAC28830.1; -; Genomic_DNA.
DR EMBL; AF053271; AAC28832.1; -; Genomic_DNA.
DR EMBL; AF053272; AAC28834.1; -; Genomic_DNA.
DR EMBL; AF053273; AAC28836.1; -; Genomic_DNA.
DR EMBL; AF053274; AAC28838.1; -; Genomic_DNA.
DR EMBL; AF053275; AAC28840.1; -; Genomic_DNA.
DR EMBL; AF053276; AAC28842.1; -; Genomic_DNA.
DR PIR; S02853; S02853.
DR RefSeq; NP_476644.1; NM_057296.2.
DR AlphaFoldDB; P10333; -.
DR SMR; P10333; -.
DR BioGRID; 59983; 5.
DR DIP; DIP-23208N; -.
DR IntAct; P10333; 5.
DR STRING; 7227.FBpp0078786; -.
DR GlyGen; P10333; 4 sites.
DR PaxDb; P10333; -.
DR PRIDE; P10333; -.
DR DNASU; 33817; -.
DR EnsemblMetazoa; FBtr0079155; FBpp0078786; FBgn0002855.
DR GeneID; 33817; -.
DR KEGG; dme:Dmel_CG8982; -.
DR CTD; 33817; -.
DR FlyBase; FBgn0002855; Acp26Aa.
DR VEuPathDB; VectorBase:FBgn0002855; -.
DR GeneTree; ENSGT00940000176795; -.
DR HOGENOM; CLU_1162203_0_0_1; -.
DR OMA; NTYRNKY; -.
DR OrthoDB; 1836372at2759; -.
DR PhylomeDB; P10333; -.
DR SignaLink; P10333; -.
DR BioGRID-ORCS; 33817; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 33817; -.
DR PRO; PR:P10333; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0002855; Expressed in male reproductive gland and 9 other tissues.
DR Genevisible; P10333; DM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; ISM:FlyBase.
DR GO; GO:0005615; C:extracellular space; HDA:FlyBase.
DR GO; GO:0042802; F:identical protein binding; IPI:FlyBase.
DR GO; GO:0007618; P:mating; IEA:InterPro.
DR GO; GO:2000130; P:positive regulation of octopamine signaling pathway; IMP:UniProtKB.
DR GO; GO:0060279; P:positive regulation of ovulation; IMP:UniProtKB.
DR GO; GO:0019953; P:sexual reproduction; IEP:FlyBase.
DR GO; GO:0046692; P:sperm competition; TAS:FlyBase.
DR InterPro; IPR004315; Male_ac_gland_sc.
DR Pfam; PF03082; MAGSP; 1.
PE 1: Evidence at protein level;
KW Behavior; Cytoplasm; Glycoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..264
FT /note="Accessory gland-specific peptide 26Aa"
FT /id="PRO_0000021755"
FT PEPTIDE 19..48
FT /note="CP1-N"
FT /evidence="ECO:0000269|PubMed:7556947"
FT /id="PRO_0000451070"
FT PEPTIDE 49..264
FT /note="CP1-C"
FT /evidence="ECO:0000269|PubMed:7556947"
FT /id="PRO_0000451071"
FT PEPTIDE 49..67
FT /note="CP2-N"
FT /evidence="ECO:0000269|PubMed:7556947"
FT /id="PRO_0000451072"
FT PEPTIDE 68..264
FT /note="CP2-C"
FT /evidence="ECO:0000269|PubMed:7556947"
FT /id="PRO_0000451073"
FT PEPTIDE 68..117
FT /note="CP3-N"
FT /evidence="ECO:0000269|PubMed:7556947"
FT /id="PRO_0000451074"
FT PEPTIDE 118..264
FT /note="CP3-C"
FT /evidence="ECO:0000269|PubMed:7556947"
FT /id="PRO_0000451075"
FT REGION 1..138
FT /note="Sufficient for promoting ovulation when expressed in
FT females"
FT /evidence="ECO:0000269|PubMed:15640356"
FT REGION 189..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..264
FT /note="Necessary and sufficient for homodimerization"
FT /evidence="ECO:0000269|PubMed:17130459,
FT ECO:0000269|PubMed:20138215"
FT SITE 48..49
FT /note="Cleavage; by Semp1"
FT /evidence="ECO:0000269|PubMed:24514904"
FT SITE 67..68
FT /note="Cleavage; by Semp1"
FT /evidence="ECO:0000269|PubMed:24514904"
FT SITE 117..118
FT /note="Cleavage; by Semp1"
FT /evidence="ECO:0000269|PubMed:24514904"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 5
FT /note="L -> S (in strain: La28 and La106)"
FT VARIANT 10
FT /note="I -> L (in strain: La120)"
FT VARIANT 14
FT /note="L -> I (in strain: La14, La31, La118 and Ma24)"
FT VARIANT 19
FT /note="S -> N (in strain: AF1, AF4, AF6, AF8, AF9, Au1,
FT Au3, Au7, Au9, La3, La10, La14, La15, La25, La31, La108,
FT Ma6, Ma11, Ma18, Ma20, Ma24, Ma35, Ma37, Ma53, Ma57, Ma74,
FT Mo13a, Mo34a, Mo47a, NC-005, NC-007, NC-010, NFS 5.3, Ny1,
FT Ny6, Ny8, SFS 2.2, TW2, TW3, TW6, TW9 and TW10)"
FT VARIANT 24
FT /note="Q -> K (in strain: NC-005, NC-007 and NC-010)"
FT VARIANT 25
FT /note="Q -> K (in strain: Au6, La25, La27, La62, La108,
FT Ma43, Mo13a, Mo34a, NFS 5.1, NFS 5.2, NFS 5.3, NFS 6.1, NFS
FT 7.8, Ny1, Ny2, Ny6, Ny8, SFS 1.1, SFS 1.4, SFS 2.2, SFS
FT 3.1, SFS 3.3, SFS 3.4, TW2, TW3, TW4, TW7, TW9 and TW10)"
FT VARIANT 32
FT /note="L -> Q (in strain: AF2, AF7, Au4, La3, La15, La37,
FT La58, Ma21, Mo29b, Mo36a, Mo52B, Mo79b, NC-009, Ny3, Ny5
FT and TW11)"
FT VARIANT 39
FT /note="S -> G (in strain: Ny2 and SFS 3.4)"
FT VARIANT 40
FT /note="A -> S (in strain: Au3)"
FT VARIANT 42
FT /note="L -> V (in strain: Ma18, Ma20, Ma37 and Ma53)"
FT VARIANT 44
FT /note="N -> S (in strain: Au3 and Ma74)"
FT VARIANT 46
FT /note="A -> P (in strain: AF1, AF3, AF4, AF5, AF6, AF8,
FT AF9, AF10, Au1, Au2, Au4, Au6, Au7, Au8, Au10, La10, La13,
FT La14, La25, La31, La32, La37, La46, La58, La60, La62,
FT La105, La108, La116, La118, La125, Ma3, Ma6, Ma11, Ma20,
FT Ma23, Ma24, Ma50, Ma56, Ma57, Ma60, Mo13a, Mo29b, Mo34a,
FT Mo40b, Mo52B, Mo80b, NC-001, NC-004, NC-005, NC-006, NC-
FT 007, NC-008, NC-010, NFS 5.1, NFS 5.2, NFS 6.1, NFS 6.2,
FT NFS 6.3, NFS 7.8, Ny1, Ny2, Ny4, Ny6, Ny8, SFS 1.1, SFS
FT 1.4, SFS 2.2, SFS 3.1, SFS 3.2, SFS 3.3, SFS 3.4, TW1, TW2,
FT TW3, TW4, TW5, TW6, TW7, TW8 and TW9)"
FT VARIANT 46
FT /note="A -> T (in strain: AF2, AF7, Au3, Au5, Au9, La3,
FT La15, La27, La36, La54, La120, Ma18, Ma21, Ma31, Ma37,
FT Ma43, Ma53, Ma74, Mo36a, Mo79b, NC-002, NC-003, NC-009, NFS
FT 5.4, NFS 6.4, Ny3, Ny5, Ny7, SFS 2.4, TW10 and TW11)"
FT VARIANT 54
FT /note="A -> T (in strain: La116)"
FT VARIANT 56
FT /note="I -> L (in strain: Au3)"
FT VARIANT 65
FT /note="D -> G (in strain: AF8, Ma3 and SFS 2.3)"
FT VARIANT 76
FT /note="D -> N (in strain: La116 and NC3)"
FT VARIANT 79
FT /note="D -> N (in strain: Au2, Au3, Au8, La13, La32, La37,
FT NC-004, NC-006, NC-008, Ny4, TW1, TW5 and TW8)"
FT VARIANT 85
FT /note="Missing (in strain: La108)"
FT VARIANT 101
FT /note="N -> S (in strain: AF1, AF2, AF3, AF5, AF6, AF7,
FT AF8, AF9, AF10, Au3, Au4, Au6, Au7, La3, La10, La14, La15,
FT La27, La28, La31, La36, La37, La46, La54, La58, La60, La62,
FT La106, La116, La118, La120, La125, Ma3, Ma6, Ma11, Ma18,
FT Ma20, Ma21, Ma23, Ma24, Ma31, Ma35, Ma37, Ma43, Ma50, Ma53,
FT Ma56, Ma57, Ma74, Mo40b, Mo52B, NC-001, NC-002, NC-003, NC-
FT 009, NFS 5.1, NFS 5.2, NFS 6.1, NFS 6.2, NFS 6.3, NFS 7.8,
FT Ny2, Ny3, Ny5, Ny6, SFS 1.1, SFS 1.2, SFS 1.4, SFS 2.2, SFS
FT 2.3, SFS 2.4, SFS 3.1, SFS 3.2, SFS 3.3, SFS 3.4, TW3, TW4,
FT TW6, TW7, TW10 and TW11)"
FT VARIANT 104
FT /note="P -> R (in strain: La62)"
FT VARIANT 109
FT /note="L -> I (in strain: AF1, AF2, AF3, AF5, AF6, AF7,
FT AF8, AF9, AF10, Au2, Au4, Au6, Au7, Au8, La3, La10, La13,
FT La14, La15, La27, La28, La31, La32, La37, La46, La58, La60,
FT La62, La105, La106, La116, La118, La120, La125, Ma3, Ma6,
FT Ma11, Ma18, Ma20, Ma21, Ma23, Ma24, Ma31, Ma35, Ma37, Ma43,
FT Ma50, Ma53, Ma56, Ma57, Ma74, Mo40b, Mo52B, Mo80b, NC-001,
FT NC-002, NC-004, NC-006, NC-008, NC-009, NFS 5.1, NFS 5.2,
FT NFS 6.1, NFS 6.2, NFS 6.3, NFS 6.4, NFS 7.8, Ny2, Ny3, Ny4,
FT Ny5, SFS 1.1, SFS 1.4, SFS 2.2, SFS 2.4, SFS 3.1, SFS 3.2,
FT SFS 3.3, SFS 3.4, TW1, TW3, TW4, TW5, TW6, TW7, TW8, TW10
FT and TW11)"
FT VARIANT 167
FT /note="L -> S (in strain: La36, La54 and Ma20)"
FT VARIANT 169
FT /note="L -> F (in strain: La3, La36, La125 and Ma20)"
FT VARIANT 172
FT /note="E -> Q (in strain: Au1, Au3 and Au9)"
FT VARIANT 207
FT /note="S -> I (in strain: Au5, La10, La14, La27, La31,
FT La36, La54, La60, La62, La105, La118, La120, La125, Ma3,
FT Ma6, Ma11, Ma21, Ma24, Ma31, Ma35, Ma43, Ma50, Ma53, Ma56,
FT Ma57, Ma74, Mo36a, Mo37a, Mo47a, Mo79b, NC-002, NFS 5.1,
FT NFS 5.2, NFS 6.3, NFS 7.8, Ny2, SFS 1.1, SFS 1.2, SFS 1.4,
FT SFS 2.3, SFS 3.1 and SFS 3.4)"
FT VARIANT 212
FT /note="A -> V (in strain: Ny2 and SFS 2.3)"
FT VARIANT 221
FT /note="R -> K (in strain: La3, La10, La15, La27, La31,
FT La37, La60, La120, La125, Ma6, Ma18, Ma20, Ma21, Ma35,
FT Ma37, Ma43, Mo29b, Mo34a, Mo80b, NC-002, NC-010, NFS 5.1,
FT NFS 5.2, NFS 5.4, NFS 6.1, NFS 6.2, NFS 6.4, NFS 7.8, Ny2,
FT SFS 1.2, SFS 1.4, SFS 2.2, SFS 2.3, SFS 3.1, SFS 3.3 and
FT SFS 3.4)"
FT VARIANT 226
FT /note="N -> Y (in strain: TW9)"
FT VARIANT 253
FT /note="E -> D (in strain: AF6, AF8, AF9, Au4, La31, La32,
FT La60, La125, Ma6, Ma21, Ma57, TW1 and TW11)"
FT VARIANT 262
FT /note="P -> S (in strain: AF5, AF10, Au5, La3, La15, La105,
FT Mo36a, Mo37a, Mo47a, Mo79b and TW10)"
FT MUTAGEN 43..264
FT /note="Missing: Males have no visible phenotype and are
FT fertile. However, mated females display a decrease in the
FT number of oocytes released by their ovary and deposit fewer
FT eggs on day 1 after the start of mating (ASM). No effect on
FT the number of eggs laid by mated females on day 2 to 4 ASM.
FT No effect on female receptibility to another mate and does
FT not affect sperm resistance to displacement by rival
FT ejaculates."
FT /evidence="ECO:0000269|PubMed:10662669,
FT ECO:0000269|PubMed:7479736"
FT MUTAGEN 224..228
FT /note="YRNKY->ARNKA: Loss of homodimerization."
FT /evidence="ECO:0000269|PubMed:20138215"
FT MUTAGEN 229..232
FT /note="LTLL->ATLA: Loss of homodimerization."
FT /evidence="ECO:0000269|PubMed:20138215"
FT MUTAGEN 236..239
FT /note="SQKI->AQKA: Loss of homodimerization."
FT /evidence="ECO:0000269|PubMed:20138215"
FT MUTAGEN 243..246
FT /note="IAKV->AAKA: Loss of homodimerization."
FT /evidence="ECO:0000269|PubMed:20138215"
SQ SEQUENCE 264 AA; 29619 MW; 97377826FAE93EB6 CRC64;
MNQILLCSPI LLLLFTVASC DSEQQLDSAM HLKSDSTKSA SLKNVAPKND ETQAKIAKDD
VALKDAKKGD YIMDIDISDL PLDDYPINRS KSLKSSSIDL NNIPFNKGLD DFPAKEKNQG
SNQSALKALQ QRLLTEQNNS LLLRNHSIYL MKEIEARKTD IIKVRQLNLD LELELNTVNR
RLLELNGQLQ NTRKSTKPCK KRSSKDSAPP AANQFQEANV RNTYRNKYLT LLKELSQKIN
NEIAKVATDV PTETNPSQGN LPTL
