A0A5N4DQ20 · A0A5N4DQ20_CAMDR

Function

Caution

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

Catalytic activity

  • Cleavage of gelatin type I and collagen types IV, V, VII, X. Cleaves the collagen-like sequence Pro-Gln-Gly-|-Ile-Ala-Gly-Gln.
    EC:3.4.24.24 (UniProtKB | ENZYME | Rhea)

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.

Type
IDPosition(s)Description
Binding site103Zn2+ 2 (UniProtKB | ChEBI); catalytic; in inhibited form
Binding site135Ca2+ 1 (UniProtKB | ChEBI)
Binding site169Ca2+ 2 (UniProtKB | ChEBI)
Binding site179Zn2+ 1 (UniProtKB | ChEBI)
Binding site181Zn2+ 1 (UniProtKB | ChEBI)
Binding site186Ca2+ 3 (UniProtKB | ChEBI)
Binding site187Ca2+ 3 (UniProtKB | ChEBI)
Binding site191Ca2+ 3 (UniProtKB | ChEBI)
Binding site194Zn2+ 1 (UniProtKB | ChEBI)
Binding site203Ca2+ 2 (UniProtKB | ChEBI)
Binding site205Ca2+ 2 (UniProtKB | ChEBI)
Binding site207Zn2+ 1 (UniProtKB | ChEBI)
Binding site209Ca2+ 3 (UniProtKB | ChEBI)
Binding site210Ca2+ 1 (UniProtKB | ChEBI)
Binding site212Ca2+ 1 (UniProtKB | ChEBI)
Binding site212Ca2+ 3 (UniProtKB | ChEBI)
Active site232
Active site405
Binding site477Ca2+ 4 (UniProtKB | ChEBI)
Binding site479Ca2+ 5 (UniProtKB | ChEBI)
Binding site522Ca2+ 4 (UniProtKB | ChEBI)
Binding site572Ca2+ 5 (UniProtKB | ChEBI)
Binding site619Ca2+ 4 (UniProtKB | ChEBI)
Binding site621Ca2+ 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
Biological Processresponse to hypoxia
Biological Processtissue remodeling

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    72 kDa type IV collagenase
  • EC number
  • Alternative names
    • 72 kDa gelatinase
    • Matrix metalloproteinase-2

Gene names

    • ORF names
      Cadr_000011373

Organism names

  • Taxonomic identifier
  • Strain
    • Drom800
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Tylopoda > Camelidae > Camelus

Accessions

  • Primary accession
    A0A5N4DQ20

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, chain, disulfide bond, modified residue.

Type
IDPosition(s)Description
Signal1-30
ChainPRO_502427847131-66172 kDa type IV collagenase
Disulfide bond234↔260
Disulfide bond248↔275
Disulfide bond292↔318
Disulfide bond306↔333
Disulfide bond350↔376
Disulfide bond364↔391
Disulfide bond470↔661
Modified residue553Phosphotyrosine; by PKDCC

Keywords

Interaction

Subunit

Interacts (via the C-terminal hemopexin-like domains-containing region) with the integrin alpha-V/beta-3; the interaction promotes vascular invasion in angiogenic vessels and melamoma cells. Interacts (via the C-terminal PEX domain) with TIMP2 (via the C-terminal); the interaction inhibits the degradation activity. Interacts with GSK3B.

Protein-protein interaction databases

Family & Domains

Features

Showing features for motif, domain, repeat.

Type
IDPosition(s)Description
Motif101-108Cysteine switch
Domain229-277Fibronectin type-II
Domain287-335Fibronectin type-II
Domain345-393Fibronectin type-II
Repeat473-517Hemopexin
Repeat518-564Hemopexin
Repeat566-614Hemopexin
Repeat615-661Hemopexin

Sequence similarities

Belongs to the peptidase M10A family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    661
  • Mass (Da)
    73,834
  • Last updated
    2020-02-26 v1
  • Checksum
    9F7507B4371E1846
MTKARVARGALASPLRALCVLGCLLGRAAAAPSPIIKFPGDVAPKTDKELAVQYLNTFYGCPKESCNLFVLKDTLKKMQKFFGLPQTGELDQNTIETMRKPRCGNPDVANYNFFPRKPKWDKNQVTYRIIGYTPDLDPETVDDAFARAFQVWSDVTPLRFSRIHDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAPGPGVGGDSHFDDDELWTLGEGQVVRVKYGNADGEYCKFPFLFNGKEYTSCTDTGRSDGFLWCSTTYNFDKDGKYGFCPHEALFTMGGNADGQPCKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKYGFCPETAMSTVGGNSEGAPCVFPFTFLGNKHESCTSAGRSDGKLWCATTANYDDDRKWGFCPDQGYSLFLVAAHEFGHAMGLEHSQDPGALMAPIYTYTKNFRLSHDDIKGIQDLYGASPDIDVGTGPTPTLGPITPEICKQDIVFDGISQIRGEIFFFKDRFIWRTVTPRDKPMGPLLVATFWPELPEKIDAVYEAPQEEKAVFFAGNEYWVYSASTLERGYPKPLTSLGLPPDVQKVDAAFNWSKNKKTYIFAGDKFWRYNEVKKKMDPGFPKLIADAWNAIPDNLDAVVDLQGGGHSYFFKGAYYLKLENQSLKSVKFGSVKSDWLGC

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JWIN03000009
EMBL· GenBank· DDBJ
KAB1273157.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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