Q5TZP0 · Q5TZP0_HUMAN

  • Protein
    interstitial collagenase
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • Annotation score
    3/5

Function

Catalytic activity

  • Cleavage of the triple helix of collagen at about three-quarters of the length of the molecule from the N-terminus, at 775-Gly-|-Ile-776 in the alpha1(I) chain. Cleaves synthetic substrates and alpha-macroglobulins at bonds where P1' is a hydrophobic residue.
    EC:3.4.24.7 (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.

146950100150200250300350400450
TypeIDPosition(s)Description
Binding site92Zn2+ 2 (UniProtKB | ChEBI); catalytic; in inhibited form
Binding site124Ca2+ 1 (UniProtKB | ChEBI)
Binding site158Ca2+ 2 (UniProtKB | ChEBI)
Binding site168Zn2+ 1 (UniProtKB | ChEBI)
Binding site170Zn2+ 1 (UniProtKB | ChEBI)
Binding site175Ca2+ 3 (UniProtKB | ChEBI)
Binding site176Ca2+ 3 (UniProtKB | ChEBI)
Binding site183Zn2+ 1 (UniProtKB | ChEBI)
Binding site192Ca2+ 2 (UniProtKB | ChEBI)
Binding site194Ca2+ 2 (UniProtKB | ChEBI)
Binding site196Zn2+ 1 (UniProtKB | ChEBI)
Binding site198Ca2+ 3 (UniProtKB | ChEBI)
Binding site201Ca2+ 1 (UniProtKB | ChEBI)
Binding site201Ca2+ 3 (UniProtKB | ChEBI)
Binding site218Zn2+ 2 (UniProtKB | ChEBI); catalytic
Active site219
Binding site222Zn2+ 2 (UniProtKB | ChEBI); catalytic
Binding site228Zn2+ 2 (UniProtKB | ChEBI); catalytic
Binding site236Zn2+ 2 (UniProtKB | ChEBI); catalytic
Binding site285Ca2+ 4 (UniProtKB | ChEBI)
Binding site287Ca2+ 5 (UniProtKB | ChEBI)
Binding site331Ca2+ 5 (UniProtKB | ChEBI)
Binding site380Ca2+ 5 (UniProtKB | ChEBI)
Binding site427Ca2+ 4 (UniProtKB | ChEBI)
Binding site429Ca2+ 5 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcollagen trimer
Cellular Componentextracellular matrix
Molecular Functionmetalloendopeptidase activity
Molecular Functionzinc ion binding
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    interstitial collagenase
  • EC number

Organism names

  • Taxonomic identifier
  • Organism
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q5TZP0

Subcellular Location

Keywords

PTM/Processing

Features

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

TypeIDPosition(s)Description
Signal1-17
ChainPRO_500426318218-469interstitial collagenase
Disulfide bond278↔466
Modified residue360Phosphotyrosine; by PKDCC

Keywords

Proteomic databases

Structure

Family & Domains

Features

Showing features for motif, domain, repeat.

TypeIDPosition(s)Description
Motif90-97Cysteine switch
Domain105-262Peptidase metallopeptidase
Repeat275-324Hemopexin
Repeat325-371Hemopexin
Repeat374-422Hemopexin
Repeat423-466Hemopexin

Sequence similarities

Belongs to the peptidase M10A family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    469
  • Mass (Da)
    53,982
  • Last updated
    2004-12-07 v1
  • Checksum
    3F861B4484FF7A0D
MHSFPPLLLLLFWGVVSHSFPATLETQEQDVDLVQKYLEKYYNLKNDGMQVEKRRNSGPVVEKLKQMQEFFGLKVTGKPDAETLKVMKQPRCGVPDVAQFVLTEGNPRWEQTHLTYRIENYTPDLPRADVDHAIEKAFQLWSNVTPLTFTKVSEGQADIMISFVRGDHRDNSPFDGPGGNLAHAFQPGPGIGGDAHFDEDERWTNNFREYNLHRVAAHELGHSLGLSHSTDIGALMYPSYTFSGDVQLAQDDIDGIQAIYGRSQNPVQPIGPQTPKACDSKLTFDAITTIRGEVMFFKDRFYMRTNPFYPEVELNFISVFWPQLPNGLEAAYEFADRDEVRFFKGNKYWAVQGQNVLHGYPKDIYSSFGFPRTVKHIDAALSEENTGKTYFFVANKYWRYDEYKRSMDPGYPKMIAHDFPGIGHKVDAVFMKDGFFYFFHGTRQYKFDPKTKRILTLQKANSWFNCRKN

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BT020147
EMBL· GenBank· DDBJ
AAV38949.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

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