Q5XF51 · 3MMP_ARATH
- ProteinMetalloendoproteinase 3-MMP
- Gene3MMP
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids384 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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-NH2 (QF24) and beta-casein and, to some extent, on myelin basic protein (MBP) (PubMed:24156403).
Active on McaPLGLDpaAR-NH2 (QF24) and beta-casein and, to some extent, on myelin basic protein (MBP) (PubMed:24156403).
Cofactor
Note: Binds 1 zinc ion per subunit.
Activity regulation
Repressed by acetohydroxamic acid (AHA).
pH Dependence
Optimum pH is 7-8.
Temperature Dependence
Optimum temperature is 35 degrees Celsius.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 123 | Zn2+ (UniProtKB | ChEBI); catalytic; in inhibited form | ||||
Sequence: C | ||||||
Binding site | 285 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Active site | 286 | |||||
Sequence: E | ||||||
Binding site | 289 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 295 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular matrix | |
Cellular Component | plasma membrane | |
Cellular Component | side of membrane | |
Molecular Function | metalloendopeptidase activity | |
Molecular Function | zinc ion binding | |
Biological Process | defense response to fungus | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameMetalloendoproteinase 3-MMP
- EC number
- Short namesAt3-MMP
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ5XF51
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
PTM/Processing
Features
Showing features for signal, propeptide, glycosylation, chain, lipidation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-21 | |||||
Sequence: MVRICVFMVFLLFFAPSPVSA | ||||||
Propeptide | PRO_0000433525 | 22-158 | Activation peptide | |||
Sequence: GFYTNSSAIPPQLLRNATGNPWNSFLNFTGCHAGKKYDGLYMLKQYFQHFGYITETNLSGNFTDDFDDILKNAVEMYQRNFQLNVTGVLDELTLKHVVIPRCGNPDVVNGTSTMHSGRKTFEVSFAGRGQRFHAVKH | ||||||
Glycosylation | 26 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 37 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 48 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 78 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 82 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 105 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 130 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Chain | PRO_0000433526 | 159-358 | Metalloendoproteinase 3-MMP | |||
Sequence: YSFFPGEPRWPRNRRDLTYAFDPRNALTEEVKSVFSRAFTRWEEVTPLTFTRVERFSTSDISIGFYSGEHGDGEPFDGPMRTLAHAFSPPTGHFHLDGEENWIVSGEGGDGFISVSEAVDLESVAVHEIGHLLGLGHSSVEGSIMYPTIRTGRRKVDLTTDDVEGVQYLYGANPNFNGSRSPPPSTQQRDTGDSGAPGRS | ||||||
Glycosylation | 335 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Lipidation | 358 | GPI-anchor amidated serine | ||||
Sequence: S | ||||||
Propeptide | PRO_0000433527 | 359-384 | Removed in mature form | |||
Sequence: DGSRSVLTNLLQYYFWIIFGLFLYLV |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Mostly expressed in leaves and roots, and, to a lower extent, in flowers and stems.
Gene expression databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for motif, compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 121-128 | Cysteine switch | ||||
Sequence: PRCGNPDV | ||||||
Compositional bias | 330-352 | Polar residues | ||||
Sequence: ANPNFNGSRSPPPSTQQRDTGDS | ||||||
Region | 330-360 | Disordered | ||||
Sequence: ANPNFNGSRSPPPSTQQRDTGDSGAPGRSDG |
Domain
The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
Sequence similarities
Belongs to the peptidase M10A family. Matrix metalloproteinases (MMPs) subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length384
- Mass (Da)43,017
- Last updated2004-11-23 v1
- ChecksumE6EF6661C98A790C
Sequence caution
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 330-352 | Polar residues | ||||
Sequence: ANPNFNGSRSPPPSTQQRDTGDS |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC002396 EMBL· GenBank· DDBJ | AAC00572.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation | |
CP002684 EMBL· GenBank· DDBJ | AEE30482.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BT015765 EMBL· GenBank· DDBJ | AAU90055.1 EMBL· GenBank· DDBJ | mRNA |