IED ID | IndEnz0002016533 |
Enzyme Type ID | protease016533 |
Protein Name |
Metalloendoproteinase 4-MMP At4-MMP EC 3.4.24.- Matrix metalloproteinase 1 AtMMP1 |
Gene Name | 4MMP MMP1 At2g45040 T14P1.15 |
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 | MHHHHHPCNRKPFTTIFSFFLLYLNLHNQQIIEARNPSQFTTNPSPDVSIPEIKRHLQQYGYLPQNKESDDVSFEQALVRYQKNLGLPITGKPDSDTLSQILLPRCGFPDDVEPKTAPFHTGKKYVYFPGRPRWTRDVPLKLTYAFSQENLTPYLAPTDIRRVFRRAFGKWASVIPVSFIETEDYVIADIKIGFFNGDHGDGEPFDGVLGVLAHTFSPENGRLHLDKAETWAVDFDEEKSSVAVDLESVAVHEIGHVLGLGHSSVKDAAMYPTLKPRSKKVNLNMDDVVGVQSLYGTNPNFTLNSLLASETSTNLADGSRIRSQGMIYSTLSTVIALCFLNW |
Enzyme Length | 342 |
Uniprot Accession Number | Q8GWW6 |
Absorption | |
Active Site | ACT_SITE 253; /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 myelin basic protein (MBP) and, to some extent, on McaPLGLDpaAR-NH(2) (QF24) and beta-casein (PubMed:24156403). {ECO:0000250|UniProtKB:O23507, ECO:0000269|PubMed:24156403}. |
Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45-55 degrees Celsius. {ECO:0000269|PubMed:24156403}; |
PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5-9. {ECO:0000269|PubMed:24156403}; |
Pathway | |
nucleotide Binding | |
Features | Active site (1); Chain (1); Glycosylation (1); Lipidation (1); Metal binding (4); Motif (1); Propeptide (2); Sequence conflict (3); 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..34; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 12068095; 12805588; 14585825; 21798944; |
Motif | MOTIF 104..111; /note=Cysteine switch; /evidence=ECO:0000255 |
Gene Encoded By | |
Mass | 38,506 |
Kinetics | |
Metal Binding | METAL 106; /note=Zinc; in inhibited form; /evidence=ECO:0000250; METAL 252; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 256; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095; METAL 262; /note=Zinc; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
Rhea ID | |
Cross Reference Brenda |