IED ID | IndEnz0002006899 |
Enzyme Type ID | protease006899 |
Protein Name |
Matrix metalloproteinase-2 Dm2-MMP EC 3.4.24.- |
Gene Name | Mmp2 CG1794 |
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 | MFSKYVLATLLALFAQSMCIQELSLPPEGSHSTAATRSKKAKTAISEDIMYNYLMQFDYLPKSDLETGALRTEDQLKEAIRSLQSFGNITVTGEIDSATARLIQKPRCGVGDRRSADSFSPDNLYHEIGSNVRVRRFALQGPKWSRTDLTWSMVNRSMPDASKVERMVQTALDVWANHSKLTFREVYSDQADIQILFARRAHGDGYKFDGPGQVLAHAFYPGEGRGGDAHFDADETWNFDGESDDSHGTNFLNVALHELGHSLGLAHSAIPDAVMFPWYQNNEVAGNLPDDDRYGIQQLYGTKEKTWGPYKPQTTTTTTTTTTMRAMIYRADKPAYWPWNNPSNNPNNDRNRARERQEEERRRQEKERRRQEEERRHQEEERRRQVEERQRQEEERWRQEQERQEEENRRRKIEHKSQWERNPSKERNRPRERQEMERRRQEQERQEQERQEQEDRRRERERDRQLEWERRNRNGAREPVTPTANTTPRPTNKPYPTVHRQHHHHNKPRKPKPDSCMTYYDAISIIRGELFIFRGPYLWRIGTSGLYNGYPTEIRRHWSALPENLTKVDAVYENKQRQIVFFIGREYYVFNSVMLAPGFPKPLASLGLPPTLTHIDASFVWGHNNRTYMTSGTLYWRIDDYTGQVELDYPRDMSIWSGVGYNIDAAFQYLDGKTYFFKNLGYWEFNDDRMKVAHARAKLSARRWMQCARSANEVDDEQRWTASLVSEGEETGRSGSRELRINHFILSILLLAIANWRS |
Enzyme Length | 758 |
Uniprot Accession Number | Q8MPP3 |
Absorption | |
Active Site | ACT_SITE 258; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.24.- |
Enzyme Function | FUNCTION: Has metalloproteinase activity (PubMed:11967260). Required for larval tissue histolysis during metamorphosis and is involved in pupal head eversion and fusion of the wing imaginal tissue (PubMed:12530966). Required for growth of the dorsal air sac primordium and development of the dorsal air sacs (PubMed:19751719). Promotes embryonic motor axon fasciculation (PubMed:18045838). Cleaves and activates frac to promote motor axon bundling during outgrowth (PubMed:21471368). Promotes the reshaping of adult sensory neuron dendrites from a radial to lattice-like shape which occurs after eclosion by degrading the basement membrane on which the dendrites grow (PubMed:20412776). Involved in inhibition of follicle stem cell proliferation by cleaving Dlp, inhibiting its interaction with wg and preventing Dlp-mediated spreading of wg to follicle stem cells to enhance their proliferation (PubMed:25267296). Plays a role in wound healing (PubMed:22262460). Involved in fat body dissociation which occurs during metamorphosis by degrading basement membrane components, leading to destruction of cell-basement membrane junctions (PubMed:25520167). Required for posterior follicle cell degradation and ovulation (PubMed:25695427). {ECO:0000269|PubMed:11967260, ECO:0000269|PubMed:12530966, ECO:0000269|PubMed:18045838, ECO:0000269|PubMed:19751719, ECO:0000269|PubMed:20412776, ECO:0000269|PubMed:21471368, ECO:0000269|PubMed:22262460, ECO:0000269|PubMed:25267296, ECO:0000269|PubMed:25520167, ECO:0000269|PubMed:25695427}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Alternative sequence (2); Chain (1); Compositional bias (3); Disulfide bond (1); Metal binding (3); Propeptide (1); Region (1); Repeat (4); Sequence conflict (2); Signal peptide (1); Topological domain (2); Transmembrane (1) |
Keywords | Alternative splicing;Calcium;Cell membrane;Cleavage on pair of basic residues;Disulfide bond;Hydrolase;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Repeat;Signal;Transmembrane;Transmembrane helix;Zinc;Zymogen |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11967260, ECO:0000269|PubMed:25267296}; Single-pass type I membrane protein {ECO:0000305}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..17; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 10471706; 10961941; 12096187; 12844358; 14567681; 15737938; 15928045; 15944190; 16210248; 16399076; 16533912; 16872532; 16971470; 17082773; 17239363; 17301221; 17327274; 17729283; 18084299; 18485344; 18628398; 19196956; 20152186; 20157509; 20308539; 20363916; 20453880; 20495554; 20668662; 20670829; 21684629; 21688401; 21828098; 21978772; 21979943; 22496930; 22782723; 22952997; 23071443; 23423438; 23493057; 23570874; 23766327; 23831567; 24050232; 24392358; 24685612; 24859129; 24865556; 25180232; 25242144; 25291190; 25312911; 25329560; 25344916; 25356918; 25535920; 25848931; 25970244; 26440503; 26473732; 26603384; 26658841; 26659849; 26690827; 26808525; 27058248; 27127457; 27178668; 27357258; 27628033; 27704301; 27773719; 28067623; 28069934; 28090760; 28192468; 28300207; 28362802; 28537903; 28576972; 28627812; 28697337; 28825401; 29016849; 29056683; 29107812; 29114039; 29118190; 29223976; 29256860; 29563183; 29656148; 29693007; 29853618; 29938760; 29974861; 29987037; 30018198; 30022065; 30254143; 30260564; 30327343; 30385460; 30397306; 30446899; 30479347; 30914004; 31040111; 31068592; 31109678; 31180049; 31195239; 31350199; 31444217; 31690598; 31746739; 31846454; 31932350; 32105665; 32122911; 32201229; 32277031; 32317312; 32338596; 32339165; 32487456; 32585131; 32598400; 32686670; 32788209; 32878880; 33077027; 33242407; 33322177; 33377870; 33543035; 33578809; 33679334; 33767161; 34055768; 34216545; 34473940; 34496252; 34564691; 9491068; |
Motif | |
Gene Encoded By | |
Mass | 89,137 |
Kinetics | |
Metal Binding | METAL 257; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 261; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 267; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
Rhea ID | |
Cross Reference Brenda |