Detail Information for IndEnz0002001751
IED ID IndEnz0002001751
Enzyme Type ID protease001751
Protein Name Seminal metalloprotease 1
EC 3.4.24.-
Gene Name Semp1 CG11864
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 MFPQIWGVIFLFTPTVFSELFKDPELLAGFYQGDIKAHPIRTRNGIVNQIYHWPNRTVPYMIEDDAFADSHYREILRAISIIEENSCVIFKPATEMDFPMALVITSKGLGCNTVHLGYRNKTQVVNLEIYPLGEGCFRIGSIIHELLHVLGFEHQHVSQNRDQYVSIQWKNINPQYNINFVNNDNSTAWHDFDEGYDYESVMHYVPRAFSRNGQPTIVPLREGAENMGQRFYMSEKDIRKLNKMYRCPDHV
Enzyme Length 251
Uniprot Accession Number Q9VJN9
Absorption
Active Site ACT_SITE 145; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.24.-
Enzyme Function FUNCTION: Seminal fluid metalloprotease which is transferred to females during mating and is required for processing of two other seminal fluid proteins Acp26Aa and Acp36DE in mated females. {ECO:0000269|PubMed:15979005, ECO:0000269|PubMed:17116868, ECO:0000269|PubMed:24514904}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Chain (1); Disulfide bond (2); Domain (1); Erroneous initiation (1); Glycosylation (3); Metal binding (3); Mutagenesis (3); Propeptide (1); Sequence conflict (3); Signal peptide (1)
Keywords Disulfide bond;Glycoprotein;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Secreted;Signal;Zinc;Zymogen
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15979005, ECO:0000269|PubMed:17116868}. Note=Secreted into seminal fluid. {ECO:0000269|PubMed:15979005, ECO:0000269|PubMed:17116868}.
Modified Residue
Post Translational Modification PTM: Undergoes cleavage in the male during mating with a cleaved product detected in the ejaculatory duct and/or bulb of males by 8-10 minutes after the start of mating (PubMed:17116868). Further cleavage occurs in the mated female (PubMed:15979005). May undergo cleavage in a two-step process where it is first cleaved by Sems, making it susceptible to activational cleavage which may be carried out by another protease or by autocleavage (PubMed:24514904). {ECO:0000269|PubMed:15979005, ECO:0000269|PubMed:17116868, ECO:0000269|PubMed:24514904}.
Signal Peptide SIGNAL 1..18; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10471707; 10779493; 15345744; 15944345; 17110486; 18056920; 18245332; 18666829; 20220848; 21074052; 21672851; 21940639; 22253601; 23071443; 23087839; 23092796; 23109270; 23555301; 23944235; 24973093; 25117438; 27172210; 27357258; 31722958; 32611817;
Motif
Gene Encoded By
Mass 29,282
Kinetics
Metal Binding METAL 144; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211; METAL 148; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211; METAL 154; /note=Zinc; via tele nitrogen; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01211
Rhea ID
Cross Reference Brenda