| IED ID | IndEnz0002014467 |
| Enzyme Type ID | protease014467 |
| Protein Name |
Metalloendoproteinase 3-MMP At3-MMP EC 3.4.24.- |
| Gene Name | 3MMP At1g24140 F3I6.6 |
| Organism | Arabidopsis thaliana (Mouse-ear cress) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae rosids malvids Brassicales Brassicaceae Camelineae Arabidopsis Arabidopsis thaliana (Mouse-ear cress) |
| Enzyme Sequence | MVRICVFMVFLLFFAPSPVSAGFYTNSSAIPPQLLRNATGNPWNSFLNFTGCHAGKKYDGLYMLKQYFQHFGYITETNLSGNFTDDFDDILKNAVEMYQRNFQLNVTGVLDELTLKHVVIPRCGNPDVVNGTSTMHSGRKTFEVSFAGRGQRFHAVKHYSFFPGEPRWPRNRRDLTYAFDPRNALTEEVKSVFSRAFTRWEEVTPLTFTRVERFSTSDISIGFYSGEHGDGEPFDGPMRTLAHAFSPPTGHFHLDGEENWIVSGEGGDGFISVSEAVDLESVAVHEIGHLLGLGHSSVEGSIMYPTIRTGRRKVDLTTDDVEGVQYLYGANPNFNGSRSPPPSTQQRDTGDSGAPGRSDGSRSVLTNLLQYYFWIIFGLFLYLV |
| Enzyme Length | 384 |
| Uniprot Accession Number | Q5XF51 |
| Absorption | |
| Active Site | ACT_SITE 286; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | ACTIVITY REGULATION: Repressed by acetohydroxamic acid (AHA). {ECO:0000269|PubMed:24156403}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.24.- |
| Enzyme Function | FUNCTION: Matrix metalloproteinases (MMPs) or matrixins may play a role in the degradation and remodeling of the extracellular matrix (ECM) during development or in response to stresses (By similarity). Active on McaPLGLDpaAR-NH(2) (QF24) and beta-casein and, to some extent, on myelin basic protein (MBP) (PubMed:24156403). {ECO:0000250|UniProtKB:O23507, ECO:0000269|PubMed:24156403}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 35 degrees Celsius. {ECO:0000269|PubMed:24156403}; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7-8. {ECO:0000269|PubMed:24156403}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Compositional bias (1); Erroneous initiation (1); Glycosylation (8); Lipidation (1); Metal binding (4); Motif (1); Propeptide (2); Region (1); Signal peptide (1) |
| Keywords | Cell membrane;GPI-anchor;Glycoprotein;Hydrolase;Lipoprotein;Membrane;Metal-binding;Metalloprotease;Protease;Reference proteome;Signal;Zinc;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Lipid-anchor, GPI-anchor {ECO:0000255}; Extracellular side {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..21; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 12068095; 12535341; 12805588; 15235117; 16081527; 17142483; 17217462; 17337630; 18650403; 18702669; 18775970; 18829981; 28832648; |
| Motif | MOTIF 121..128; /note=Cysteine switch; /evidence=ECO:0000250 |
| Gene Encoded By | |
| Mass | 43,017 |
| Kinetics | |
| Metal Binding | METAL 123; /note=Zinc; in inhibited form; /evidence=ECO:0000250; METAL 285; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 289; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 295; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Rhea ID | |
| Cross Reference Brenda |