| IED ID | IndEnz0002015748 |
| Enzyme Type ID | protease015748 |
| Protein Name |
Matrix metalloproteinase-9 MMP-9 EC 3.4.24.35 92 kDa gelatinase 92 kDa type IV collagenase Gelatinase B GELB |
| Gene Name | Mmp9 |
| Organism | Rattus norvegicus (Rat) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MSPWQPLLLVLLALGYSFAAPHQRQPTYVVFPRDLKTSNLTDTQLAEDYLYRYGYTRAAQMMGEKQSLRPALLMLQKQLSLPQTGELDSETLKAIRSPRCGVPDVGKFQTFDGDLKWHHHNITYWIQSYTEDLPRDVIDDSFARAFAVWSAVTPLTFTRVYGLEADIVIQFGVAEHGDGYPFDGKDGLLAHAFPPGPGIQGDAHFDDDELWSLGKGAVVPTYFGNANGAPCHFPFTFEGRSYLSCTTDGRNDGKPWCGTTADYDTDRKYGFCPSENLYTEHGNGDGKPCVFPFIFEGHSYSACTTKGRSDGYRWCATTANYDQDKADGFCPTRADVTVTGGNSAGEMCVFPFVFLGKQYSTCTSEGRSDGRLWCATTSNFDADKKWGFCPDQGYSLFLVAAHEFGHALGLDHSSVPEALMYPMYHYHEDSPLHEDDIKGIHHLYGRGSKPDPRPPATTAAEPQPTAPPTMCSTAPPMAYPTGGPTVAPTGAPSPGPTGPPTAGPSEAPTESSTPDDNPCNVDVFDAIADIQGALHFFKDGRYWKFSNHGGNQLQGPFLIARTWPAFPSKLNSAFEDPQPKKIFFFLWAQMWVYTGQSVLGPRSLDKLGLGSEVTLVTGLLPRRGGKALLISRERIWKFDLKSQKVDPQSVTRLDNEFSGVPWNSHNVFQYQDKAYFCHDKYFWRVSFHNRVNQVDHVAYVTYDLLQCP |
| Enzyme Length | 708 |
| Uniprot Accession Number | P50282 |
| Absorption | |
| Active Site | ACT_SITE 403; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Cleavage of gelatin types I and V and collagen types IV and V.; EC=3.4.24.35; Evidence={ECO:0000250|UniProtKB:P14780}; |
| DNA Binding | |
| EC Number | 3.4.24.35 |
| Enzyme Function | FUNCTION: Matrix metalloproteinase that plays an essential role in local proteolysis of the extracellular matrix and in leukocyte migration (By similarity). Could play a role in bone osteoclastic resorption (By similarity). Cleaves KiSS1 at a Gly-|-Leu bond (By similarity). Cleaves NINJ1 to generate the Secreted ninjurin-1 form (By similarity). Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. Degrades fibronectin but not laminin or Pz-peptide (By similarity). {ECO:0000250|UniProtKB:P14780, ECO:0000250|UniProtKB:P41245}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Compositional bias (3); Disulfide bond (7); Domain (3); Glycosylation (2); Metal binding (21); Motif (1); Propeptide (1); Region (1); Repeat (4); Sequence conflict (14); Signal peptide (1) |
| Keywords | Calcium;Collagen degradation;Disulfide bond;Extracellular matrix;Glycoprotein;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Repeat;Secreted;Signal;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P14780}. |
| Modified Residue | |
| Post Translational Modification | PTM: N- and O-glycosylated. {ECO:0000250|UniProtKB:P14780}. |
| Signal Peptide | SIGNAL 1..19; /evidence=ECO:0000250|UniProtKB:P14780 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10430840; 10933221; 11342481; 11592852; 11788364; 11826121; 12061388; 12923405; 12963432; 15128910; 15213623; 15642321; 15883642; 16046515; 16051896; 16158251; 16191269; 16208432; 16303975; 16304337; 16317521; 16671440; 16698855; 16740171; 16816895; 16845718; 16846501; 16935996; 16977379; 17114644; 17121240; 17122420; 17133179; 17148685; 17156757; 17158349; 17164434; 17207419; 17217365; 17255325; 17272778; 17289933; 17337891; 17371820; 17374579; 17392157; 17398390; 17410600; 17452115; 17463159; 17493927; 17569353; 17569872; 17603938; 17650800; 17704356; 17854381; 17913382; 17928157; 17977875; 18039280; 18694576; 19099751; 19357873; 19494493; 19528495; 19539802; 19545667; 19554388; 19556529; 19575923; 19725228; 19879865; 19889233; 19897563; 19909738; 19948826; 20000122; 20056896; 20085636; 20108118; 20145375; 20159792; 20218972; 20303372; 20405265; 20406136; 20428773; 20434464; 20541575; 20621845; 21175737; 21256058; 21268133; 21683124; 21937941; 21964536; 22363061; 22410640; 22490164; 22552115; 22633097; 22800566; 23006043; 23040778; 23046750; 23076999; 23079570; 23087098; 23089644; 23149858; 23204894; 23281803; 23303633; 23318412; 23323009; 23344254; 23384615; 23423566; 23479197; 23537149; 23844137; 23905389; 24419461; 24661104; 24773551; 24820783; 24842554; 24966898; 25172308; 25314292; 25763638; 25842729; 26261622; 7492685; 8531210; 8613533; 8912869; 9300240; 9327785; 9546322; 9549496; 9732233; 9733107; |
| Motif | MOTIF 98..105; /note=Cysteine switch; /evidence=ECO:0000250|UniProtKB:P14780 |
| Gene Encoded By | |
| Mass | 78,611 |
| Kinetics | |
| Metal Binding | METAL 100; /note=Zinc 2; in inhibited form; /evidence=ECO:0000250|UniProtKB:P14780; METAL 132; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P14780; METAL 166; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P14780; METAL 176; /note=Zinc 1; structural; /evidence=ECO:0000250|UniProtKB:P14780; METAL 178; /note=Zinc 1; structural; /evidence=ECO:0000250|UniProtKB:P14780; METAL 183; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:P14780; METAL 184; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P14780; METAL 186; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P14780; METAL 188; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P14780; METAL 191; /note=Zinc 1; structural; /evidence=ECO:0000250|UniProtKB:P14780; METAL 198; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P14780; METAL 200; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P14780; METAL 202; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P14780; METAL 204; /note=Zinc 1; structural; /evidence=ECO:0000250|UniProtKB:P14780; METAL 206; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:P14780; METAL 207; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P14780; METAL 209; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P14780; METAL 209; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:P14780; METAL 402; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P14780; METAL 406; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P14780; METAL 412; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P14780 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.35; |