IED Industry Enzyme Database

Detail Information for IndEnz0002006540
IED ID IndEnz0002006540
Enzyme Type ID protease006540
Protein Name 72 kDa type IV collagenase
EC 3.4.24.24
72 kDa gelatinase
Gelatinase A
Matrix metalloproteinase-2
MMP-2
TBE-1

Cleaved into: PEX
Gene Name MMP2 CLG4A
Organism Homo sapiens (Human)
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 Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MEALMARGALTGPLRALCLLGCLLSHAAAAPSPIIKFPGDVAPKTDKELAVQYLNTFYGCPKESCNLFVLKDTLKKMQKFFGLPQTGDLDQNTIETMRKPRCGNPDVANYNFFPRKPKWDKNQITYRIIGYTPDLDPETVDDAFARAFQVWSDVTPLRFSRIHDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAPGTGVGGDSHFDDDELWTLGEGQVVRVKYGNADGEYCKFPFLFNGKEYNSCTDTGRSDGFLWCSTTYNFEKDGKYGFCPHEALFTMGGNAEGQPCKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKYGFCPETAMSTVGGNSEGAPCVFPFTFLGNKYESCTSAGRSDGKMWCATTANYDDDRKWGFCPDQGYSLFLVAAHEFGHAMGLEHSQDPGALMAPIYTYTKNFRLSQDDIKGIQELYGASPDIDLGTGPTPTLGPVTPEICKQDIVFDGIAQIRGEIFFFKDRFIWRTVTPRDKPMGPLLVATFWPELPEKIDAVYEAPQEEKAVFFAGNEYWIYSASTLERGYPKPLTSLGLPPDVQRVDAAFNWSKNKKTYIFAGDKFWRYNEVKKKMDPGFPKLIADAWNAIPDNLDAVVDLQGGGHSYFFKGAYYLKLENQSLKSVKFGSIKSDWLGC
Enzyme Length 660
Uniprot Accession Number P08253
Absorption
Active Site ACT_SITE 404; /evidence="ECO:0000255|PROSITE-ProRule:PRU10095, ECO:0000305|PubMed:10356396"
Activity Regulation ACTIVITY REGULATION: Inhibited by histatin-3 1/24 (histatin-5). {ECO:0000269|PubMed:11179305}.
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:0000305|PubMed:11179305, ECO:0000305|PubMed:11431697, ECO:0000305|PubMed:12147339, ECO:0000305|PubMed:2834383};
DNA Binding
EC Number 3.4.24.24
Enzyme Function FUNCTION: Ubiquitinous metalloproteinase that is involved in diverse functions such as remodeling of the vasculature, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. As well as degrading extracellular matrix proteins, can also act on several nonmatrix proteins such as big endothelial 1 and beta-type CGRP promoting vasoconstriction. Also cleaves KISS at a Gly-|-Leu bond. Appears to have a role in myocardial cell death pathways. Contributes to myocardial oxidative stress by regulating the activity of GSK3beta. Cleaves GSK3beta in vitro. Involved in the formation of the fibrovascular tissues in association with MMP14.; FUNCTION: PEX, the C-terminal non-catalytic fragment of MMP2, posseses anti-angiogenic and anti-tumor properties and inhibits cell migration and cell adhesion to FGF2 and vitronectin. Ligand for integrinv/beta3 on the surface of blood vessels.; FUNCTION: [Isoform 2]: Mediates the proteolysis of CHUK/IKKA and initiates a primary innate immune response by inducing mitochondrial-nuclear stress signaling with activation of the pro-inflammatory NF-kappaB, NFAT and IRF transcriptional pathways.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (1); Alternative sequence (2); Beta strand (48); Chain (2); Disulfide bond (7); Domain (3); Glycosylation (2); Helix (12); Metal binding (23); Motif (1); Natural variant (9); Propeptide (1); Region (4); Repeat (4); Sequence conflict (3); Signal peptide (1); Turn (13)
Keywords 3D-structure;Alternative splicing;Angiogenesis;Autocatalytic cleavage;Calcium;Collagen degradation;Cytoplasm;Direct protein sequencing;Disease variant;Disulfide bond;Extracellular matrix;Glycoprotein;Hydrolase;Membrane;Metal-binding;Metalloprotease;Mitochondrion;Nucleus;Phosphoprotein;Protease;Reference proteome;Repeat;Secreted;Signal;Zinc;Zymogen
Interact With P05067; P05067; P05067; P20908; Q8NBP7; Q04864-2; Q8IX30; P16035
Induction INDUCTION: Aspirin appears to inhibit expression. {ECO:0000269|PubMed:18971601}.
Subcellular Location SUBCELLULAR LOCATION: [Isoform 1]: Secreted, extracellular space, extracellular matrix {ECO:0000305|PubMed:2834383}. Membrane. Nucleus. Note=Colocalizes with integrin alphaV/beta3 at the membrane surface in angiogenic blood vessels and melanomas. Found in mitochondria, along microfibrils, and in nuclei of cardiomyocytes.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. Mitochondrion.
Modified Residue
Post Translational Modification PTM: Phosphorylation on multiple sites modulates enzymatic activity. Phosphorylated by PKC in vitro. {ECO:0000269|PubMed:17435175}.; PTM: The propeptide is processed by MMP14 (MT-MMP1) and MMP16 (MT-MMP3). Autocatalytic cleavage in the C-terminal produces the anti-angiogenic peptide, PEX. This processing appears to be facilitated by binding integrinv/beta3. {ECO:0000269|PubMed:12879005, ECO:0000269|PubMed:9119036}.
Signal Peptide SIGNAL 1..29; /evidence=ECO:0000269|PubMed:2834383
Structure 3D NMR spectroscopy (4); X-ray crystallography (7)
Cross Reference PDB 1CK7; 1CXW; 1EAK; 1GEN; 1GXD; 1HOV; 1J7M; 1KS0; 1QIB; 1RTG; 3AYU;
Mapped Pubmed ID 10229672; 10386589; 10551873; 10809722; 10986281; 11104795; 11168762; 11278729; 11571304; 11577169; 11728453; 11748988; 11756567; 11762702; 11782389; 11790786; 11792711; 11825873; 11833938; 11839588; 11844598; 11854622; 11872628; 11895494; 11918086; 11920503; 11928813; 11929863; 11935310; 11948127; 11956628; 11960372; 12007723; 12029498; 12034345; 12077518; 12085233; 12087091; 12103254; 12115722; 12147229; 12193399; 12194986; 12198653; 12225805; 12235151; 12372458; 12374789; 12376362; 12379487; 12393408; 12393872; 12421825; 12431239; 12438229; 12439941; 12451991; 12466191; 12470034; 12471459; 12473650; 12475252; 12479097; 12486137; 12522578; 12559990; 12586836; 12587534; 12601782; 12602913; 12614934; 12615834; 12632066; 12632084; 12642591; 12651627; 12657623; 12684035; 12684625; 12753080; 12764090; 12832446; 12845641; 12861074; 12873995; 12914776; 12939660; 12952836; 12967855; 12970394; 12970724; 1311314; 1326552; 1371271; 14500349; 14519487; 14520690; 14580155; 14604886; 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8692946; 8817670; 8920930; 9092507; 9148753; 9346290; 9395517; 9422744; 9428515; 9578462; 9632662; 9651395; 9922210;
Motif MOTIF 100..107; /note=Cysteine switch; /evidence=ECO:0000250
Gene Encoded By
Mass 73,882
Kinetics
Metal Binding METAL 102; /note="Zinc 1; in inhibited form"; /evidence="ECO:0000269|PubMed:10356396, ECO:0000269|PubMed:12032297, ECO:0007744|PDB:1CK7, ECO:0007744|PDB:1EAK, ECO:0007744|PDB:1GXD"; METAL 134; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:21813640, ECO:0007744|PDB:1QIB, ECO:0007744|PDB:3AYU"; METAL 168; /note="Calcium 2; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:21813640, ECO:0007744|PDB:1EAK, ECO:0007744|PDB:3AYU"; METAL 178; /note="Zinc 2"; /evidence="ECO:0000269|PubMed:10356396, ECO:0000269|PubMed:12032297, ECO:0000269|PubMed:21813640, ECO:0007744|PDB:1CK7, ECO:0007744|PDB:1EAK, ECO:0007744|PDB:1GXD, ECO:0007744|PDB:1QIB, ECO:0007744|PDB:3AYU"; METAL 180; /note="Zinc 2"; /evidence="ECO:0000269|PubMed:10356396, ECO:0000269|PubMed:12032297, ECO:0000269|PubMed:21813640, ECO:0007744|PDB:1CK7, ECO:0007744|PDB:1EAK, ECO:0007744|PDB:1GXD, ECO:0007744|PDB:1QIB, ECO:0007744|PDB:3AYU"; METAL 185; /note="Calcium 3"; /evidence="ECO:0000269|PubMed:21813640, ECO:0007744|PDB:3AYU"; METAL 186; /note="Calcium 3; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:21813640, ECO:0007744|PDB:3AYU"; METAL 193; /note="Zinc 2"; /evidence="ECO:0000269|PubMed:10356396, ECO:0000269|PubMed:12032297, ECO:0000269|PubMed:21813640, ECO:0007744|PDB:1CK7, ECO:0007744|PDB:1EAK, ECO:0007744|PDB:1GXD, ECO:0007744|PDB:1QIB, ECO:0007744|PDB:3AYU"; METAL 200; /note="Calcium 2; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:21813640, ECO:0007744|PDB:1EAK, ECO:0007744|PDB:3AYU"; METAL 202; /note="Calcium 2; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:21813640, ECO:0007744|PDB:3AYU"; METAL 204; /note="Calcium 2"; /evidence="ECO:0000269|PubMed:21813640, ECO:0007744|PDB:3AYU"; METAL 206; /note="Zinc 2"; /evidence="ECO:0000269|PubMed:10356396, ECO:0000269|PubMed:12032297, ECO:0000269|PubMed:21813640, ECO:0007744|PDB:1CK7, ECO:0007744|PDB:1EAK, ECO:0007744|PDB:1GXD, ECO:0007744|PDB:1QIB, ECO:0007744|PDB:3AYU"; METAL 208; /note="Calcium 3"; /evidence="ECO:0000269|PubMed:21813640, ECO:0007744|PDB:3AYU"; METAL 209; /note="Calcium 1"; /evidence="ECO:0000269|PubMed:21813640, ECO:0007744|PDB:1QIB, ECO:0007744|PDB:3AYU"; METAL 211; /note="Calcium 1; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:21813640, ECO:0007744|PDB:1QIB, ECO:0007744|PDB:3AYU"; METAL 211; /note="Calcium 3"; /evidence="ECO:0000269|PubMed:21813640, ECO:0007744|PDB:3AYU"; METAL 403; /note="Zinc 1; catalytic"; /evidence="ECO:0000269|PubMed:10356396, ECO:0000269|PubMed:12032297, ECO:0000269|PubMed:21813640, ECO:0007744|PDB:1CK7, ECO:0007744|PDB:1EAK, ECO:0007744|PDB:1GXD, ECO:0007744|PDB:3AYU"; METAL 407; /note="Zinc 1; catalytic"; /evidence="ECO:0000269|PubMed:10356396, ECO:0000269|PubMed:12032297, ECO:0000269|PubMed:21813640, ECO:0007744|PDB:1CK7, ECO:0007744|PDB:1EAK, ECO:0007744|PDB:1GXD, ECO:0007744|PDB:3AYU"; METAL 413; /note="Zinc 1; catalytic"; /evidence="ECO:0000269|PubMed:10356396, ECO:0000269|PubMed:12032297, ECO:0000269|PubMed:21813640, ECO:0007744|PDB:1CK7, ECO:0007744|PDB:1EAK, ECO:0007744|PDB:1GXD, ECO:0007744|PDB:3AYU"; METAL 476; /note="Calcium 4; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:10356396, ECO:0000269|PubMed:8549817, ECO:0007744|PDB:1CK7, ECO:0007744|PDB:1RTG"; METAL 521; /note="Calcium 4; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:10356396, ECO:0000269|PubMed:8549817, ECO:0007744|PDB:1CK7, ECO:0007744|PDB:1RTG"; METAL 569; /note="Calcium 4; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:10356396, ECO:0000269|PubMed:8549817, ECO:0007744|PDB:1CK7, ECO:0007744|PDB:1RTG"; METAL 618; /note="Calcium 4; via carbonyl oxygen"; /evidence="ECO:0000269|PubMed:10356396, ECO:0000269|PubMed:8549817, ECO:0007744|PDB:1CK7, ECO:0007744|PDB:1RTG"
Rhea ID
Cross Reference Brenda 3.4.24.24;