A0A7J7EZ65 · A0A7J7EZ65_DICBM

Function

function

Plays a role in the degradation of extracellular matrix proteins including fibrillar collagen, fibronectin, TNC and ACAN. Cleaves triple helical collagens, including type I, type II and type III collagen, but has the highest activity with soluble type II collagen. Can also degrade collagen type IV, type XIV and type X. May also function by activating or degrading key regulatory proteins, such as TGFB1 and CCN2. Plays a role in wound healing, tissue remodeling, cartilage degradation, bone development, bone mineralization and ossification. Required for normal embryonic bone development and ossification. Plays a role in the healing of bone fractures via endochondral ossification. Plays a role in wound healing, probably by a mechanism that involves proteolytic activation of TGFB1 and degradation of CCN2. Plays a role in keratinocyte migration during wound healing. May play a role in cell migration and in tumor cell invasion.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Cofactor

Protein has several cofactor binding sites:
Ca2+ (UniProtKB | Rhea| CHEBI:29108 )

Note: Can bind about 5 Ca2+ ions per subunit.
Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 2 Zn2+ ions per subunit.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site96Zn2+ 2 (UniProtKB | ChEBI); catalytic; in inhibited form
Binding site128Ca2+ 1 (UniProtKB | ChEBI)
Binding site162Ca2+ 2 (UniProtKB | ChEBI)
Binding site172Zn2+ 1 (UniProtKB | ChEBI)
Binding site174Zn2+ 1 (UniProtKB | ChEBI)
Binding site179Ca2+ 3 (UniProtKB | ChEBI)
Binding site180Ca2+ 3 (UniProtKB | ChEBI)
Binding site182Ca2+ 3 (UniProtKB | ChEBI)
Binding site184Ca2+ 3 (UniProtKB | ChEBI)
Binding site187Zn2+ 1 (UniProtKB | ChEBI)
Binding site194Ca2+ 2 (UniProtKB | ChEBI)
Binding site196Ca2+ 2 (UniProtKB | ChEBI)
Binding site198Ca2+ 2 (UniProtKB | ChEBI)
Binding site200Zn2+ 1 (UniProtKB | ChEBI)
Binding site202Ca2+ 3 (UniProtKB | ChEBI)
Binding site203Ca2+ 1 (UniProtKB | ChEBI)
Binding site205Ca2+ 1 (UniProtKB | ChEBI)
Binding site205Ca2+ 3 (UniProtKB | ChEBI)
Binding site222Zn2+ 2 (UniProtKB | ChEBI); catalytic
Active site223
Binding site226Zn2+ 2 (UniProtKB | ChEBI); catalytic
Binding site232Zn2+ 2 (UniProtKB | ChEBI); catalytic
Binding site240Zn2+ 2 (UniProtKB | ChEBI); catalytic
Binding site291Ca2+ 4 (UniProtKB | ChEBI)
Binding site293Ca2+ 5 (UniProtKB | ChEBI)
Binding site335Ca2+ 4 (UniProtKB | ChEBI)
Binding site337Ca2+ 5 (UniProtKB | ChEBI)
Binding site389Ca2+ 4 (UniProtKB | ChEBI)
Binding site391Ca2+ 5 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentextracellular matrix
Cellular Componentextracellular space
Molecular Functionmetalloendopeptidase activity
Molecular Functionzinc ion binding
Biological Processcollagen catabolic process
Biological Processextracellular matrix organization
Biological Processproteolysis

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Collagenase 3
  • Alternative names
    • Matrix metalloproteinase-13

Gene names

    • ORF names
      HPG69_018502

Organism names

Accessions

  • Primary accession
    A0A7J7EZ65

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, chain, disulfide bond.

TypeIDPosition(s)Description
Signal1-19
ChainPRO_502964799720-428Collagenase 3
Disulfide bond284↔428

Keywords

Family & Domains

Features

Showing features for motif, domain, region, repeat.

TypeIDPosition(s)Description
Motif94-101Cysteine switch
Domain109-268Peptidase metallopeptidase
Region263-284Disordered
Repeat281-330Hemopexin
Repeat331-384Hemopexin
Repeat385-428Hemopexin

Sequence similarities

Belongs to the peptidase M10A family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    428
  • Mass (Da)
    48,989
  • Last updated
    2021-04-07 v1
  • Checksum
    F32EB350E3FB9494
MHPGVLAAFLFLSWTHCWSLPLPNDDDDDDTSEEDFQLAERYLKSYYYPLNPAGILKKSATNSVVDRLREMQSFFGLEVTGKLDDNTLDIMKKPRCGVPDVGEYNVFPRTLKWSKMNLTYRIVNYTPDLTHSEVEKAFKKAFKVWSDVTPLNFTRLHNGTADIMISFGTKEHGDFYPFDGPSGLLAHAFPPGPNYGGDAHFDDDETWTSSSKGYNLFLVAAHEFGHSLGLDHSKDPGALMFPIYTYTGKSHFMLPDDDVQGIQSLYGPGDEDPNPKHPKTPDKCDPSLSLDAITSLRGETLVFKDRFFWRLHPQQVDAELFLTKSFWPELPNRIDAAYEHPSQDLIFIFRGAIISLVSFLRYDDTNHMMDEDYPRLIEEEFPGIGDKVDAVYEKNGYIYFFNGPIQFEYSIWSNRIVRVMPTNSLLWC

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JACDTQ010001719
EMBL· GenBank· DDBJ
KAF5921102.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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