Q5XF51 · 3MMP_ARATH

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).

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

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.

TypeIDPosition(s)Description
Binding site123Zn2+ (UniProtKB | ChEBI); catalytic; in inhibited form
Binding site285Zn2+ (UniProtKB | ChEBI); catalytic
Active site286
Binding site289Zn2+ (UniProtKB | ChEBI); catalytic
Binding site295Zn2+ (UniProtKB | ChEBI); catalytic

GO annotations

AspectTerm
Cellular Componentextracellular matrix
Cellular Componentplasma membrane
Cellular Componentside of membrane
Molecular Functionmetalloendopeptidase activity
Molecular Functionzinc ion binding
Biological Processdefense response to fungus
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Metalloendoproteinase 3-MMP
  • EC number
  • Short names
    At3-MMP

Gene names

    • Name
      3MMP
    • ORF names
      F3I6.6
    • Ordered locus names
      At1g24140

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Columbia
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis

Accessions

  • Primary accession
    Q5XF51
  • Secondary accessions
    • O48680

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, propeptide, glycosylation, chain, lipidation.

TypeIDPosition(s)Description
Signal1-21
PropeptidePRO_000043352522-158Activation peptide
Glycosylation26N-linked (GlcNAc...) asparagine
Glycosylation37N-linked (GlcNAc...) asparagine
Glycosylation48N-linked (GlcNAc...) asparagine
Glycosylation78N-linked (GlcNAc...) asparagine
Glycosylation82N-linked (GlcNAc...) asparagine
Glycosylation105N-linked (GlcNAc...) asparagine
Glycosylation130N-linked (GlcNAc...) asparagine
ChainPRO_0000433526159-358Metalloendoproteinase 3-MMP
Glycosylation335N-linked (GlcNAc...) asparagine
Lipidation358GPI-anchor amidated serine
PropeptidePRO_0000433527359-384Removed in mature form

Keywords

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.

TypeIDPosition(s)Description
Motif121-128Cysteine switch
Compositional bias330-352Polar residues
Region330-360Disordered

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

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    384
  • Mass (Da)
    43,017
  • Last updated
    2004-11-23 v1
  • Checksum
    E6EF6661C98A790C
MVRICVFMVFLLFFAPSPVSAGFYTNSSAIPPQLLRNATGNPWNSFLNFTGCHAGKKYDGLYMLKQYFQHFGYITETNLSGNFTDDFDDILKNAVEMYQRNFQLNVTGVLDELTLKHVVIPRCGNPDVVNGTSTMHSGRKTFEVSFAGRGQRFHAVKHYSFFPGEPRWPRNRRDLTYAFDPRNALTEEVKSVFSRAFTRWEEVTPLTFTRVERFSTSDISIGFYSGEHGDGEPFDGPMRTLAHAFSPPTGHFHLDGEENWIVSGEGGDGFISVSEAVDLESVAVHEIGHLLGLGHSSVEGSIMYPTIRTGRRKVDLTTDDVEGVQYLYGANPNFNGSRSPPPSTQQRDTGDSGAPGRSDGSRSVLTNLLQYYFWIIFGLFLYLV

Sequence caution

The sequence AAC00572.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias330-352Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

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