| IED ID | IndEnz0002016523 |
| Enzyme Type ID | protease016523 |
| Protein Name |
Metalloendoproteinase 1-MMP At1-MMP EC 3.4.24.- |
| Gene Name | 1MMP At4g16640 dl4345c |
| 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 | MSRNLIYRRNRALCFVLILFCFPYRFGARNTPEAEQSTAKATQIIHVSNSTWHDFSRLVDVQIGSHVSGVSELKRYLHRFGYVNDGSEIFSDVFDGPLESAISLYQENLGLPITGRLDTSTVTLMSLPRCGVSDTHMTINNDFLHTTAHYTYFNGKPKWNRDTLTYAISKTHKLDYLTSEDVKTVFRRAFSQWSSVIPVSFEEVDDFTTADLKIGFYAGDHGDGLPFDGVLGTLAHAFAPENGRLHLDAAETWIVDDDLKGSSEVAVDLESVATHEIGHLLGLGHSSQESAVMYPSLRPRTKKVDLTVDDVAGVLKLYGPNPKLRLDSLTQSEDSIKNGTVSHRFLSGNFIGYVLLVVGLILFL |
| Enzyme Length | 364 |
| Uniprot Accession Number | O23507 |
| Absorption | |
| Active Site | ACT_SITE 276; /evidence=ECO:0000255|PROSITE-ProRule:PRU10095 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by human TIMP-1 and TIMP-2 and by the peptide hydroxamate inhibitor (BB-94) (PubMed:10574937). Repressed by acetohydroxamic acid (AHA) (PubMed:24156403). {ECO:0000269|PubMed:10574937, 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 (PubMed:10574937). Can cleave myelin basic protein as well as fluorigenic peptide substrates, McaPLANvaDpaAR-NH(2) and McaPChaGNvaHADpa-NH(2) 4-fold more efficiently than McaPLGLDpaAR-NH(2) (QF24) (PubMed:10574937). Active on myelin basic protein (MBP) and, to some extent, on McaPLGLDpaAR-NH(2) (QF24) and beta-casein (PubMed:24156403). {ECO:0000269|PubMed:10574937, ECO:0000269|PubMed:24156403, ECO:0000303|PubMed:10574937}. |
| 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 7-8. {ECO:0000269|PubMed:24156403}; |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (1); Glycosylation (2); Lipidation (1); Metal binding (14); Motif (1); Propeptide (2); Sequence conflict (2); 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..28; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 12068095; 12417707; 12805588; 28832648; |
| Motif | MOTIF 128..135; /note=Cysteine switch; /evidence=ECO:0000250 |
| Gene Encoded By | |
| Mass | 40,528 |
| Kinetics | |
| Metal Binding | METAL 130; /note="Zinc 2; in inhibited form"; /evidence="ECO:0000250|UniProtKB:P03956"; METAL 211; /note="Calcium 2"; /evidence="ECO:0000250|UniProtKB:P03956"; METAL 221; /note="Zinc 1"; /evidence="ECO:0000250|UniProtKB:P03956"; METAL 223; /note="Zinc 1"; /evidence="ECO:0000250|UniProtKB:P03956"; METAL 228; /note="Calcium 1"; /evidence="ECO:0000250|UniProtKB:P03956"; METAL 229; /note="Calcium 1; via carbonyl oxygen"; /evidence="ECO:0000250|UniProtKB:P03956"; METAL 236; /note="Zinc 1"; /evidence="ECO:0000250|UniProtKB:P03956"; METAL 243; /note="Calcium 2; via carbonyl oxygen"; /evidence="ECO:0000250|UniProtKB:P03956"; METAL 246; /note="Zinc 1"; /evidence="ECO:0000250|UniProtKB:P03956"; METAL 248; /note="Calcium 1"; /evidence="ECO:0000250|UniProtKB:P03956"; METAL 251; /note="Calcium 1"; /evidence="ECO:0000250|UniProtKB:P03956"; METAL 275; /note="Zinc 2; catalytic"; /evidence="ECO:0000250|UniProtKB:P03956, ECO:0000255|PROSITE-ProRule:PRU10095"; METAL 279; /note="Zinc 2; catalytic"; /evidence="ECO:0000250|UniProtKB:P03956, ECO:0000255|PROSITE-ProRule:PRU10095"; METAL 285; /note="Zinc 2; catalytic"; /evidence="ECO:0000250|UniProtKB:P03956, ECO:0000255|PROSITE-ProRule:PRU10095" |
| Rhea ID | |
| Cross Reference Brenda |