| IED ID | IndEnz0002016343 |
| Enzyme Type ID | protease016343 |
| Protein Name |
Matrix metalloproteinase-B MMP-B MMP-H19 EC 3.4.24.- Zinc metalloprotease 2 |
| Gene Name | zmp-2 H19M22.3 |
| Organism | Caenorhabditis elegans |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Nematoda (roundworms) Chromadorea Rhabditida Rhabditina Rhabditomorpha Rhabditoidea Rhabditidae Peloderinae Caenorhabditis Caenorhabditis elegans |
| Enzyme Sequence | MTKWSPNGNPLSTIYLILSLFTLAHTAPTTQHSRTTTQLRLEDEDGGGGVDEDSIHFVKGQMEKYGYLKGIDHSSPQEFRQALMFFQEVLEVEQTGNVDEMTVEAASKPRCTQTDVRQEQTKRTKRFTLSKRAKWAHASGQSVTLKWYISDYTSDIDRLETRKVVEKAFKLWSSQSYIKNEKKVTLTFQEASSKDEADINILWAEGNHGDEHDFDGANGKIEGNKKENVLAHTFFPGYARPLNGDIHFDDAEDWEIDVDQVGHGSNKRFFPYVLAHEIGHALGLDHSQKADALMHPYYKNVPINEIQLDIDDKCGVIWNYGGASDFCLYVWLMSQIVEAHNSSAQNNHGVGSITSSRTNKKSFKSEGFFLFQLKFPHSTLTHTDDVVMREKDKRSYRGDSKIPKCSSNNSSQRTLAEKKLTLGLHLSEADAKRYTEMVCNFLAGLHMWRTNPNHHASESLEKEYKGVSQEMGTFSGKSIAVRRLIRHAEHQKERSEKGPLDPDYFDDDFFENFFMEYSK |
| Enzyme Length | 519 |
| Uniprot Accession Number | O44836 |
| Absorption | |
| Active Site | ACT_SITE 277; /evidence=ECO:0000250|UniProtKB:P09238 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by human TIMP1 and TIMP2 and the broad MMP inhibitors BB94 (Batimastat) and CT543. {ECO:0000269|PubMed:9573338}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Metalloprotease involved in molting, a process during larval stages in which a new cuticle is formed and the old cuticle is shed (PubMed:24957743). Plays a role in thermotolerance probably by preventing the accumulation of oxidized lipoproteins and cholesterol (PubMed:20600277, PubMed:24957743). {ECO:0000269|PubMed:20600277, ECO:0000269|PubMed:24957743}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Alternative sequence (4); Chain (1); Glycosylation (2); Metal binding (8); Motif (1); Propeptide (1); Region (2); Sequence caution (1); Sequence conflict (3); Signal peptide (1) |
| Keywords | Alternative splicing;Cleavage on pair of basic residues;Extracellular matrix;Glycoprotein;Hydrolase;Metal-binding;Metalloprotease;Protease;Reference proteome;Secreted;Signal;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000305|PubMed:24957743}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..26; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 11381264; 12097347; 12529635; 14551910; 17164286; 19343510; 20439774; 20439776; 21085631; 21177967; 21367940; 21529718; 22286215; 22347378; 22500807; 22560298; 22921415; 23800452; 25487147; 25652260; |
| Motif | MOTIF 109..116; /note=Cysteine switch; /evidence=ECO:0000250|UniProtKB:P03957 |
| Gene Encoded By | |
| Mass | 59,254 |
| Kinetics | |
| Metal Binding | METAL 111; /note=Zinc 2; in inhibited form; /evidence=ECO:0000250|UniProtKB:P03956; METAL 208; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:P03956; METAL 210; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:P03956; METAL 232; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:P03956; METAL 247; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:P03956; METAL 276; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P03956; METAL 280; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P03956; METAL 286; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P03956 |
| Rhea ID | |
| Cross Reference Brenda |