| IED ID | IndEnz0002002985 |
| Enzyme Type ID | protease002985 |
| Protein Name |
Matrix metalloproteinase-C MMP-C MMP-C31 EC 3.4.24.- Zinc metalloprotease 3 |
| Gene Name | zmp-3 C31B8.8 |
| 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 | MRLIYVIAILLVSTCQAGFFSSLVSRFTGGGNSSPSSSSSSSSFSNSRKPSLSDEKARSYLQTFGYVPPSNSLQSRNGMAGDIQSAEQVFKSAIRKFQEFAGIAKTGFLDAATKAKMALSRCGVTDAPLALTSGSSQFKWSKTRLTYSIESWSSDLSKDDVRRAISEAYGLWSKVTPLEFSEVPAGSTSDIKIRFGVRNHNDPWPFDGEGGVLAHATMPESGMFHFDDDENWTYKDARKIHNNEATDLLAVAIHEGGHTLGLEHSRDENAIMAPFYQKTTDSSGNYVYPNLKSDDISAIQAIYGAGSGRSSSGSDFGGSSGGGSRTTARPTTTTRSWFGRFFGDDDDDVRSRTTTRRTTLWPTTQSPFSGDDWGSGSGSSGRGGSSSGSSGGGCPSHIDAYTPSSSFSYAFSGSQVYTISGTKVTKVQSIHDLFPSAPTPVNAALWNPISGSMLLFSSNRVYSYYFSNIRQIFQMDSGFPKTLPSDLGFSVSGALRWINGHQILMSSGDEFAVYDEFWNQVTLKNRISSYFPNLPRGVKGVESPAGSVITAFTSNQVFEYNSRTKSIGRQSGFSSYIAC |
| Enzyme Length | 579 |
| Uniprot Accession Number | G5EBU3 |
| Absorption | |
| Active Site | ACT_SITE 255; /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: Metalloproteinase. {ECO:0000269|PubMed:9573338}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Compositional bias (4); Glycosylation (1); Metal binding (8); Motif (1); Propeptide (1); Region (2); Repeat (2); Signal peptide (1) |
| Keywords | 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:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..17; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 10778742; 11381264; 12097347; 17164286; 19343510; 21367940; 22267497; 22286215; 22347378; 22560298; 23800452; 24884423; 25487147; 6593563; |
| Motif | MOTIF 120..127; /note=Cysteine switch; /evidence=ECO:0000250|UniProtKB:P03956 |
| Gene Encoded By | |
| Mass | 62,540 |
| Kinetics | |
| Metal Binding | METAL 122; /note=Zinc 2; in inhibited form; /evidence=ECO:0000250|UniProtKB:P03956; METAL 200; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:P03956; METAL 202; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:P03956; METAL 215; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:P03956; METAL 225; /note=Zinc 1; /evidence=ECO:0000250|UniProtKB:P03956; METAL 254; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P03956; METAL 258; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P03956; METAL 264; /note=Zinc 2; catalytic; /evidence=ECO:0000250|UniProtKB:P03956 |
| Rhea ID | |
| Cross Reference Brenda |