Detail Information for IndEnz0002006899
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