| IED ID | IndEnz0002001117 |
| Enzyme Type ID | protease001117 |
| Protein Name |
Accessory gland-specific peptide 26Aa Male accessory gland secretory protein 355A Cleaved into: CP1-N; CP1-C; CP2-N; CP2-C; CP3-N; CP3-C |
| Gene Name | Acp26Aa msp355a Mst26Aa mst355a ovulin CG8982 |
| Organism | Drosophila melanogaster (Fruit fly) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Panarthropoda Arthropoda Mandibulata Pancrustacea Hexapoda Insecta Dicondylia Pterygota (winged insects) Neoptera Endopterygota Diptera Brachycera Muscomorpha Eremoneura Cyclorrhapha Schizophora Acalyptratae Ephydroidea Drosophilidae (pomace flies) Drosophilinae Drosophilini Drosophila (fruit flies) Sophophora melanogaster group melanogaster subgroup Drosophila melanogaster (Fruit fly) |
| Enzyme Sequence | MNQILLCSPILLLLFTVASCDSEQQLDSAMHLKSDSTKSASLKNVAPKNDETQAKIAKDDVALKDAKKGDYIMDIDISDLPLDDYPINRSKSLKSSSIDLNNIPFNKGLDDFPAKEKNQGSNQSALKALQQRLLTEQNNSLLLRNHSIYLMKEIEARKTDIIKVRQLNLDLELELNTVNRRLLELNGQLQNTRKSTKPCKKRSSKDSAPPAANQFQEANVRNTYRNKYLTLLKELSQKINNEIAKVATDVPTETNPSQGNLPTL |
| Enzyme Length | 264 |
| Uniprot Accession Number | P10333 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Male seminal protein which enhances ovulation in female Drosophila by stimulating the release of oocytes by the ovary following mating (PubMed:7479736, PubMed:15640356, PubMed:24101486, PubMed:10662669). Acts by increasing octopamine (OA) neuronal signaling in the female genital tract leading to the postmating relaxation of the oviduct muscles (PubMed:24101486). This activation of the OA signaling pathway is likely to indirectly contribute to the mating-dependent increase in the number of OA synaptic sites in the female reproductive tract (PubMed:24101486). {ECO:0000269|PubMed:10662669, ECO:0000269|PubMed:15640356, ECO:0000269|PubMed:24101486, ECO:0000269|PubMed:7479736}.; FUNCTION: [CP3-N]: Male seminal peptide which is able to enhance ovulation in female Drosophila. {ECO:0000269|PubMed:15640356}.; FUNCTION: [CP3-C]: Male seminal peptide which is able to enhance ovulation in female Drosophila. {ECO:0000269|PubMed:15640356}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Glycosylation (4); Mutagenesis (5); Natural variant (31); Peptide (6); Region (3); Signal peptide (1); Site (3) |
| Keywords | Behavior;Cytoplasm;Glycoprotein;Reference proteome;Secreted;Signal |
| Interact With | |
| Induction | INDUCTION: Up-regulated in response to mating. {ECO:0000269|PubMed:2257979}. |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3142802}. Cytoplasm {ECO:0000269|PubMed:2257979}. Note=In 1 day old virgin males, secreted into the cytoplasm of accessory gland cells (PubMed:2257979). In 5 day old males it localizes to cytoplasmic vesicles of the secondary cells (PubMed:2257979). {ECO:0000269|PubMed:2257979}. |
| Modified Residue | |
| Post Translational Modification | PTM: Glycosylation. {ECO:0000269|PubMed:2257979, ECO:0000269|PubMed:7556947}.; PTM: Undergoes several cleavages as it is secreted and is further processed in the recipient female (PubMed:3142802, PubMed:2257979, PubMed:7556947, PubMed:24514904, PubMed:10612039). The precursor molecule is proteolytically cleaved by the seminal metalloprotease Semp1 at Lys-48 to produce CP1-N and CP1-C (PubMed:3142802, PubMed:2257979, PubMed:7556947, PubMed:24514904). {ECO:0000269|PubMed:10612039, ECO:0000269|PubMed:2257979, ECO:0000269|PubMed:24514904, ECO:0000269|PubMed:3142802, ECO:0000269|PubMed:7556947}.; PTM: [CP1-C]: Cleaved at Lys-67 by Semp1 to generate CP2-N and CP2-C (PubMed:3142802, PubMed:2257979, PubMed:7556947, PubMed:24514904). Cleavage appears to take place in the mated female genital tract (PubMed:2257979, PubMed:7556947). {ECO:0000269|PubMed:2257979, ECO:0000269|PubMed:24514904, ECO:0000269|PubMed:3142802, ECO:0000269|PubMed:7556947}.; PTM: [CP2-C]: Cleaved at Lys-117 by Semp1 to generate CP3-N and CP3-C (PubMed:3142802, PubMed:2257979, PubMed:7556947, PubMed:24514904). Cleavage appears to take place in the mated female genital tract (PubMed:2257979, PubMed:7556947). {ECO:0000269|PubMed:2257979, ECO:0000269|PubMed:24514904, ECO:0000269|PubMed:3142802, ECO:0000269|PubMed:7556947}. |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10364432; 10511562; 10880498; 10978290; 10978302; 11063693; 11092827; 11102381; 11139506; 11141189; 11164043; 11230529; 11230530; 11279826; 11291102; 11404330; 11404480; 11412033; 11506676; 11682306; 11805057; 11869341; 11875569; 11932766; 12000098; 12618399; 12679097; 12893873; 12897240; 12913117; 14504657; 14605208; 14668383; 15013662; 15166145; 15215320; 15280259; 15466425; 15601888; 15694303; 15723781; 15851659; 15911584; 15917496; 15944345; 15979005; 16914271; 17116868; 17276455; 17399906; 18085830; 18245332; 18430646; 18562649; 18666829; 18757944; 19343724; 19361995; 19411605; 19812620; 20220848; 21074052; 2109712; 21269436; 21271997; 21439282; 21480662; 21564678; 21628597; 21672851; 21940639; 22051795; 22253601; 22378807; 23071443; 23087839; 23171073; 23555301; 23944235; 24221639; 2449374; 24973093; 25294943; 25425680; 25445663; 25694546; 25742606; 26041806; 26058847; 27172210; 27546947; 27727275; 27794539; 28295031; 29055154; 29258876; 30293038; 31907301; 32611817; 32964470; 34099879; 34331899; 7705622; 7713409; 7833289; 8367469; 8583898; 8583899; 8698082; 8896375; 8913769; 9090115; 9159932; 9321417; 9342399; 9402735; 9549089; 9656489; 9819559; |
| Motif | |
| Gene Encoded By | |
| Mass | 29,619 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |