| IED ID | IndEnz0002006539 |
| Enzyme Type ID | protease006539 |
| Protein Name |
72 kDa type IV collagenase EC 3.4.24.24 72 kDa gelatinase Gelatinase A Matrix metalloproteinase-2 MMP-2 |
| Gene Name | MMP2 |
| Organism | Gallus gallus (Chicken) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Sauropsida Sauria (diapsids) Archelosauria Archosauria Dinosauria Saurischia Theropoda Coelurosauria Aves Neognathae Galloanserae Galliformes Phasianidae (turkeys) Phasianinae Gallus Gallus gallus (Chicken) |
| Enzyme Sequence | MKTHSVFGFFFKVLLIQVYLFNKTLAAPSPIIKFPGDSTPKTDKELAVQYLNKYYGCPKDNCNLFVLKDTLKKMQKFFGLPETGDLDQNTIETMKKPRCGNPDVANYNFFPRKPKWEKNHITYRIIGYTPDLDPETVDDAFARAFKVWSDVTPLRFNRINDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAPGPGIGGDSHFDDDELWTLGEGQVVRVKYGNADGEYCKFPFWFNGKEYNSCTDAGRNDGFLWCSTTKDFDADGKYGFCPHESLFTMGGNGDGQPCKFPFKFQGQSYDQCTTEGRTDGYRWCGTTEDYDRDKKYGFCPETAMSTVGGNSEGAPCVFPFIFLGNKYDSCTSAGRNDGKLWCASTSSYDDDRKWGFCPDQGYSLFLVAAHEFGHAMGLEHSEDPGALMAPIYTYTKNFRLSQDDIKGIQELYEVSPDVEPGPGPGPGPGPRPTLGPVTPELCKHDIVFDGVAQIRGEIFFFKDRFMWRTVNPRGKPTGPLLVATFWPDLPEKIDAVYESPQDEKAVFFAGNEYWVYTASNLDRGYPKKLTSLGLPPDVQRIDAAFNWGRNKKTYIFSGDRYWKYNEEKKKMELATPKFIADSWNGVPDNLDAVLGLTDSGYTYFFKDQYYLQMEDKSLKIVKIGKISSDWLGC |
| Enzyme Length | 663 |
| Uniprot Accession Number | Q90611 |
| Absorption | |
| Active Site | ACT_SITE 401; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Cleavage of gelatin type I and collagen types IV, V, VII, X. Cleaves the collagen-like sequence Pro-Gln-Gly-|-Ile-Ala-Gly-Gln.; EC=3.4.24.24; Evidence={ECO:0000250|UniProtKB:P08253}; |
| DNA Binding | |
| EC Number | 3.4.24.24 |
| Enzyme Function | |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Compositional bias (1); Disulfide bond (7); Domain (3); Metal binding (23); Motif (1); Propeptide (1); Region (4); Repeat (4); Sequence conflict (3); Signal peptide (1) |
| Keywords | Calcium;Collagen degradation;Direct protein sequencing;Disulfide bond;Extracellular matrix;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:0000305}. |
| Modified Residue | |
| Post Translational Modification | PTM: The propeptide is processed by MMP14 (MT-MMP1) and MMP16 (MT-MMP3). {ECO:0000250}. |
| Signal Peptide | SIGNAL 1..26; /evidence=ECO:0000269|PubMed:1848240 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 15497141; 15844197; 16537168; 17295208; 17604018; 18344292; 19221802; 21497985; 22377328; 23342920; 24279180; 24400880; 24879699; 26395636; 27342592; 28916318; |
| Motif | MOTIF 97..104; /note=Cysteine switch; /evidence=ECO:0000250 |
| Gene Encoded By | |
| Mass | 74,941 |
| Kinetics | |
| Metal Binding | METAL 99; /note=Zinc 1; in inhibited form; /evidence=ECO:0000250|UniProtKB:P08253; METAL 131; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P08253; METAL 165; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P08253; METAL 175; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:P08253; METAL 177; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:P08253; METAL 182; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:P08253; METAL 183; /note=Calcium 3; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P08253; METAL 190; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:P08253; METAL 197; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P08253; METAL 199; /note=Calcium 2; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P08253; METAL 201; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P08253; METAL 203; /note=Zinc 2; /evidence=ECO:0000250|UniProtKB:P08253; METAL 205; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:P08253; METAL 206; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P08253; METAL 208; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P08253; METAL 208; /note=Calcium 3; /evidence=ECO:0000250|UniProtKB:P08253; METAL 400; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:P08253; METAL 404; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:P08253; METAL 410; /note=Zinc 1; catalytic; /evidence=ECO:0000250|UniProtKB:P08253; METAL 479; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P08253; METAL 524; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P08253; METAL 572; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P08253; METAL 621; /note=Calcium 4; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P08253 |
| Rhea ID | |
| Cross Reference Brenda | 3.4.24.24; |