IED ID | IndEnz0002006526 |
Enzyme Type ID | protease006526 |
Protein Name |
Matrix metalloproteinase-23 MMP-23 EC 3.4.24.- Femalysin MIFR-1 Matrix metalloproteinase-21 MMP-21 Matrix metalloproteinase-22 MMP-22 Cleaved into: Matrix metalloproteinase-23, soluble form |
Gene Name | MMP23B MMP21 MMP22 |
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 | MGRGARVPSEAPGAGVERRWLGAALVALCLLPALVLLARLGAPAVPAWSAAQGDVAALGLSAVPPTRVPGPLAPRRRRYTLTPARLRWDHFNLTYRILSFPRNLLSPRETRRALAAAFRMWSDVSPFSFREVAPEQPSDLRIGFYPINHTDCLVSALHHCFDGPTGELAHAFFPPHGGIHFDDSEYWVLGPTRYSWKKGVWLTDLVHVAAHEIGHALGLMHSQHGRALMHLNATLRGWKALSQDELWGLHRLYGCLDRLFVCASWARRGFCDARRRLMKRLCPSSCDFCYEFPFPTVATTPPPPRTKTRLVPEGRNVTFRCGQKILHKKGKVYWYKDQEPLEFSYPGYLALGEAHLSIIANAVNEGTYTCVVRRQQRVLTTYSWRVRVRG |
Enzyme Length | 390 |
Uniprot Accession Number | O75900 |
Absorption | |
Active Site | ACT_SITE 212; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
Activity Regulation | ACTIVITY REGULATION: Inhibited by TIMP2. {ECO:0000250}. |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.24.- |
Enzyme Function | FUNCTION: Protease. May regulate the surface expression of some potassium channels by retaining them in the endoplasmic reticulum (By similarity). {ECO:0000250}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Alternative sequence (2); Chain (2); Disulfide bond (4); Domain (2); Glycosylation (4); Metal binding (3); Mutagenesis (1); Natural variant (1); Propeptide (1); Site (1); Topological domain (2); Transmembrane (1) |
Keywords | Alternative splicing;Cleavage on pair of basic residues;Disulfide bond;Endoplasmic reticulum;Glycoprotein;Hydrolase;Immunoglobulin domain;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Signal-anchor;Transmembrane;Transmembrane helix;Zinc;Zymogen |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Membrane {ECO:0000269|PubMed:11328856}; Single-pass type II membrane protein {ECO:0000269|PubMed:11328856}. Note=A secreted form produced by proteolytic cleavage may also exist. {ECO:0000305}. |
Modified Residue | |
Post Translational Modification | PTM: N-glycosylated. {ECO:0000269|PubMed:11328856}.; PTM: Proteolytic cleavage might yield an active form. {ECO:0000250}. |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 21988832; |
Motif | |
Gene Encoded By | |
Mass | 43,935 |
Kinetics | |
Metal Binding | METAL 211; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 215; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 221; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
Rhea ID | |
Cross Reference Brenda |