| IED ID | IndEnz0002016337 |
| Enzyme Type ID | protease016337 |
| 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 | Bos taurus (Bovine) |
| 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 Laurasiatheria Artiodactyla Ruminantia Pecora Bovidae Bovinae Bos (oxen cattle) Bos taurus (Bovine) |
| Enzyme Sequence | MSPLQPLVLALLVLACCSAVPRRRQPTVVVFPGEPRTNLTNRQLAEEYLYRYGYTPGAELSEDGQSLQRALLRFQRRLSLPETGELDSTTLNAMRAPRCGVPDVGRFQTFEGELKWHHHNITYWIQNYSEDLPRAVIDDAFARAFALWSAVTPLTFTRVYGPEADIVIQFGVREHGDGYPFDGKNGLLAHAFPPGKGIQGDAHFDDEELWSLGKGVVIPTYFGNAKGAACHFPFTFEGRSYSACTTDGRSDDMLWCSTTADYDADRQFGFCPSERLYTQDGNADGKPCVFPFTFQGRTYSACTSDGRSDGYRWCATTANYDQDKLYGFCPTRVDATVTGGNAAGELCVFPFTFLGKEYSACTREGRNDGHLWCATTSNFDKDKKWGFCPDQGYSLFLVAAHEFGHALGLDHTSVPEALMYPMYRFTEEHPLHRDDVQGIQHLYGPRPEPEPRPPTTTTTTTTEPQPTAPPTVCVTGPPTARPSEGPTTGPTGPPAAGPTGPPTAGPSAAPTESPDPAEDVCNVDIFDAIAEIRNRLHFFKAGKYWRLSEGGGRRVQGPFLVKSKWPALPRKLDSAFEDPLTKKIFFFSGRQVWVYTGASLLGPRRLDKLGLGPEVAQVTGALPRPEGKVLLFSGQSFWRFDVKTQKVDPQSVTPVDQMFPGVPISTHDIFQYQEKAYFCQDHFYWRVSSQNEVNQVDYVGYVTFDLLKCPED |
| Enzyme Length | 712 |
| Uniprot Accession Number | P52176 |
| Absorption | |
| Active Site | ACT_SITE 402; /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 (2); Disulfide bond (7); Domain (3); Glycosylation (3); Metal binding (21); Motif (1); Propeptide (1); Region (1); Repeat (4); 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 | - |
| Motif | MOTIF 97..104; /note=Cysteine switch; /evidence=ECO:0000250|UniProtKB:P14780 |
| Gene Encoded By | |
| Mass | 79,088 |
| Kinetics | |
| Metal Binding | METAL 99; /note=Zinc 2; in inhibited form; /evidence=ECO:0000250|UniProtKB:P14780; METAL 131; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P14780; METAL 165; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P14780; METAL 175; /note=Zinc 1; structural; /evidence=ECO:0000250|UniProtKB:P14780; METAL 177; /note=Zinc 1; structural; /evidence=ECO:0000250|UniProtKB:P14780; METAL 182; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:P14780; METAL 183; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P14780; METAL 185; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P14780; METAL 187; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P14780; METAL 190; /note=Zinc 1; structural; /evidence=ECO:0000250|UniProtKB:P14780; METAL 197; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P14780; METAL 199; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P14780; METAL 201; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P14780; METAL 203; /note=Zinc 1; structural; /evidence=ECO:0000250|UniProtKB:P14780; METAL 205; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:P14780; METAL 206; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P14780; METAL 208; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P14780; METAL 208; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:P14780; METAL 401; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P14780; METAL 405; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P14780; METAL 411; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P14780 |
| Rhea ID | |
| Cross Reference Brenda |