IED Industry Enzyme Database

Detail Information for IndEnz0002006556
IED ID IndEnz0002006556
Enzyme Type ID protease006556
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 Clg4b
Organism Mus musculus (Mouse)
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 Mus Mus Mus musculus (Mouse)
Enzyme Sequence MSPWQPLLLALLAFGCSSAAPYQRQPTFVVFPKDLKTSNLTDTQLAEAYLYRYGYTRAAQMMGEKQSLRPALLMLQKQLSLPQTGELDSQTLKAIRTPRCGVPDVGRFQTFKGLKWDHHNITYWIQNYSEDLPRDMIDDAFARAFAVWGEVAPLTFTRVYGPEADIVIQFGVAEHGDGYPFDGKDGLLAHAFPPGAGVQGDAHFDDDELWSLGKGVVIPTYYGNSNGAPCHFPFTFEGRSYSACTTDGRNDGTPWCSTTADYDKDGKFGFCPSERLYTEHGNGEGKPCVFPFIFEGRSYSACTTKGRSDGYRWCATTANYDQDKLYGFCPTRVDATVVGGNSAGELCVFPFVFLGKQYSSCTSDGRRDGRLWCATTSNFDTDKKWGFCPDQGYSLFLVAAHEFGHALGLDHSSVPEALMYPLYSYLEGFPLNKDDIDGIQYLYGRGSKPDPRPPATTTTEPQPTAPPTMCPTIPPTAYPTVGPTVGPTGAPSPGPTSSPSPGPTGAPSPGPTAPPTAGSSEASTESLSPADNPCNVDVFDAIAEIQGALHFFKDGWYWKFLNHRGSPLQGPFLTARTWPALPATLDSAFEDPQTKRVFFFSGRQMWVYTGKTVLGPRSLDKLGLGPEVTHVSGLLPRRLGKALLFSKGRVWRFDLKSQKVDPQSVIRVDKEFSGVPWNSHDIFQYQDKAYFCHGKFFWRVSFQNEVNKVDHEVNQVDDVGYVTYDLLQCP
Enzyme Length 730
Uniprot Accession Number P41245
Absorption
Active Site ACT_SITE 402; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095
Activity Regulation ACTIVITY REGULATION: Inhibited by histatin-3 1/24 (histatin-5). Inhibited by ECM1. {ECO:0000250|UniProtKB:P14780}.
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 (PubMed:8132709). Cleaves KiSS1 at a Gly-|-Leu bond (By similarity). Cleaves NINJ1 to generate the Secreted ninjurin-1 form (PubMed:23142597, PubMed:32883094). 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:0000269|PubMed:23142597, ECO:0000269|PubMed:32883094, ECO:0000269|PubMed:8132709}.
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); Natural variant (3); Propeptide (1); Region (1); Repeat (4); Sequence conflict (3); 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 INDUCTION: Up-regulated by ARHGEF4, SPATA13 and APC via the JNK signaling pathway in colorectal tumor cells. {ECO:0000269|PubMed:19893577}.; INDUCTION: (Microbial infection) Induced in macrophages as well as in whole animals (spleen, lung and liver) by incubation or infection with M.bovis BCG and M.tuberculosis H37Rv (at protein level) (PubMed:11500442). {ECO:0000269|PubMed:11500442}.
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 10022836; 10026175; 10048576; 10076570; 10090151; 10201949; 10232461; 10329460; 10359808; 10411111; 10419448; 10433819; 10502816; 10587514; 10652271; 10731089; 10801980; 10821760; 10841523; 10880048; 10880400; 10910775; 10934155; 10949577; 10974013; 10985432; 10995849; 11006154; 11007483; 11025665; 11081634; 11113146; 11129784; 11133164; 11165481; 11217851; 11230154; 11283152; 11350822; 11359935; 11391004; 11560996; 11566859; 11567062; 11606467; 11675412; 11689563; 11689884; 11702786; 11792318; 11804779; 11819823; 11827968; 11865039; 11880357; 11912494; 11934855; 11937493; 11969258; 11970978; 11985514; 11994507; 12031700; 12049638; 12062105; 12126625; 12163012; 12163374; 12183632; 12189240; 12193736; 12196576; 12208863; 12237890; 12354772; 12359218; 12359984; 12368198; 12368215; 12384502; 12386280; 12393846; 12411400; 12411401; 12419962; 12438450; 12466851; 12482397; 12490006; 12531895; 12557216; 12581831; 12663332; 12672030; 12673046; 12736220; 12814946; 12815621; 12816956; 12842087; 12842442; 12847275; 12874132; 12928773; 12929930; 12950084; 12960961; 12963732; 13679081; 14507865; 14507973; 14512017; 14530359; 14551157; 14561647; 14563686; 14572461; 14617754; 14630814; 14638740; 14656746; 14657171; 14670843; 14673146; 14707083; 14729404; 14736853; 14764732; 14967734; 14993123; 14993235; 15010367; 15039145; 15050894; 15059974; 15075248; 15075439; 15146242; 15156560; 15203321; 15247285; 15265790; 15305294; 15343380; 15355971; 15356151; 15364410; 15390331; 15449178; 15456762; 15474357; 15474489; 15502710; 15522913; 15529013; 15538738; 15539485; 15545316; 15545515; 15550552; 15557194; 15563592; 15618213; 15629892; 15631996; 15632000; 15634906; 15645290; 15652414; 15665831; 15689378; 15699164; 15707406; 15728252; 15729130; 15734845; 15741244; 15746435; 15748894; 15760390; 15764676; 15772259; 15800063; 15814723; 15833851; 15841177; 15843578; 15848174; 15851690; 15862156; 15866164; 15905571; 15936336; 15947259; 15969627; 16000631; 16051896; 16054858; 16081621; 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21900575; 21906275; 21911092; 21912109; 21923664; 21931322; 21933988; 21936403; 21940623; 21978934; 22014525; 22021911; 22049432; 22081025; 22086927; 22100390; 22159717; 22171010; 22192143; 22206865; 22270361; 22289852; 22326534; 22342670; 22354840; 22384161; 22391572; 22392094; 22394373; 22421441; 22427508; 22438979; 22439866; 22440257; 22452605; 22464947; 22496659; 22506619; 22507835; 22511009; 22516258; 22521821; 22573809; 22587999; 22590514; 22595017; 22595990; 22610349; 22648084; 22654423; 22688677; 22694054; 22694805; 22705584; 22714107; 22763216; 22782080; 22792383; 22793053; 22918978; 22959068; 22966168; 22972984; 22984561; 22985398; 23010105; 23016931; 23089194; 23091646; 23136157; 23157925; 23161172; 23225890; 23229548; 23322385; 23334579; 23344471; 23358111; 23407024; 23418057; 23421805; 23423566; 23431043; 23438179; 23443810; 23465590; 23471340; 23490298; 23505411; 23509775; 23536638; 23554050; 23559862; 23567158; 23617547; 23630344; 23632630; 23657566; 23661518; 23664424; 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33171097; 33467671; 33468540; 33585848; 33628393; 33763067; 33859300; 34183017; 34292881; 34622152; 34647412; 34721382; 34769418; 34818584; 34914932; 7493406; 7626795; 7743917; 8563023; 8674412; 8872958; 8893816; 8956284; 8978762; 9022062; 9079647; 9087449; 9108368; 9291579; 9291580; 9398846; 9421432; 9430236; 9466586; 9500551; 9524243; 9590175; 9611252; 9687525; 9882504; 9887098;
Motif MOTIF 98..105; /note=Cysteine switch; /evidence=ECO:0000250|UniProtKB:P14780
Gene Encoded By
Mass 80,535
Kinetics
Metal Binding METAL 100; /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 3.4.24.35;