IED ID | IndEnz0002002812 |
Enzyme Type ID | protease002812 |
Protein Name |
Matrix metalloproteinase-21 MMP-21 xMMP EC 3.4.24.- |
Gene Name | mmp21 mmp |
Organism | Xenopus laevis (African clawed frog) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amphibia Batrachia Anura Pipoidea Pipidae Xenopodinae Xenopus Xenopus Xenopus laevis (African clawed frog) |
Enzyme Sequence | MPSIKLLVWCCLCVISPRLCHSEKLFHSRDRSDLQPSAIEQAELVKDMLSAQQFLAKYGWTQPVIWDPSSTNENEPLKDFSLMQEGVCNPRQEVAEPTKSPQFIDALKKFQKLNNLPVTGTLDDATINAMNKPRCGVPDNQMAKKETEKPTAAQSLENKTKDSENVTQQNPDPPKIRRKRFLDMLMYSNKYREEQEALQKSTGKVFTKKLLKWRMIGEGYSNQLSINEQRYVFRLAFRMWSEVMPLDFEEDNTSPLSQIDIKLGFGRGRHLGCSRAFDGSGQEFAHAWFLGDIHFDDDEHFTAPSSEHGISLLKVAAHEIGHVLGLSHIHRVGSIMQPNYIPQDSGFELDLSDRRAIQNLYGSCEGPFDTAFDWIYKEKNQYGELVVRYNTYFFRNSWYWMYENRSNRTRYGDPLAIANGWHGIPVQNIDAFVHVWTWTRDASYFFKGTQYWRYDSENDKAYAEDAQGKSYPRLISEGFPGIPSPINAAYFDRRRQYIYFFRDSQVFAFDINRNRVAPDFPKRILDFFPAVAANNHPKGNIDVAYYSYTYSSLFLFKGKEFWKVVSDKDRRQNPSLPYNGLFPRRAISQQWFDICNVHPSLLKI |
Enzyme Length | 604 |
Uniprot Accession Number | O93470 |
Absorption | |
Active Site | ACT_SITE 319; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.24.- |
Enzyme Function | FUNCTION: Plays a specialized role in the generation of left-right asymmetry during embryogenesis. May act as a negative regulator of the NOTCH-signaling pathway. {ECO:0000250|UniProtKB:Q8N119}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Chain (1); Compositional bias (1); Disulfide bond (1); Glycosylation (4); Metal binding (4); Motif (1); Propeptide (1); Region (1); Repeat (4); Signal peptide (1) |
Keywords | Calcium;Cleavage on pair of basic residues;Disulfide bond;Glycoprotein;Hydrolase;Metal-binding;Metalloprotease;Protease;Repeat;Secreted;Signal;Zinc;Zymogen |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. |
Modified Residue | |
Post Translational Modification | PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}. |
Signal Peptide | SIGNAL 1..22; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | MOTIF 133..140; /note=Cysteine switch; /evidence=ECO:0000250 |
Gene Encoded By | |
Mass | 70,146 |
Kinetics | |
Metal Binding | METAL 135; /note=Zinc; in inhibited form; /evidence=ECO:0000250; METAL 318; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 322; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 328; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
Rhea ID | |
Cross Reference Brenda |