Q53G75 · Q53G75_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.

140550100150200250300350400
TypeIDPosition(s)Description
Binding site28Zn2+ 2 (UniProtKB | ChEBI); catalytic; in inhibited form
Binding site60Ca2+ 1 (UniProtKB | ChEBI)
Binding site94Ca2+ 2 (UniProtKB | ChEBI)
Binding site104Zn2+ 1 (UniProtKB | ChEBI)
Binding site106Zn2+ 1 (UniProtKB | ChEBI)
Binding site111Ca2+ 3 (UniProtKB | ChEBI)
Binding site112Ca2+ 3 (UniProtKB | ChEBI)
Binding site119Zn2+ 1 (UniProtKB | ChEBI)
Binding site128Ca2+ 2 (UniProtKB | ChEBI)
Binding site130Ca2+ 2 (UniProtKB | ChEBI)
Binding site132Zn2+ 1 (UniProtKB | ChEBI)
Binding site134Ca2+ 3 (UniProtKB | ChEBI)
Binding site137Ca2+ 3 (UniProtKB | ChEBI)
Binding site137Ca2+ 1 (UniProtKB | ChEBI)
Binding site154Zn2+ 2 (UniProtKB | ChEBI); catalytic
Active site155
Binding site158Zn2+ 2 (UniProtKB | ChEBI); catalytic
Binding site164Zn2+ 2 (UniProtKB | ChEBI); catalytic
Binding site172Zn2+ 2 (UniProtKB | ChEBI); catalytic
Binding site221Ca2+ 4 (UniProtKB | ChEBI)
Binding site223Ca2+ 5 (UniProtKB | ChEBI)
Binding site267Ca2+ 5 (UniProtKB | ChEBI)
Binding site316Ca2+ 5 (UniProtKB | ChEBI)
Binding site363Ca2+ 4 (UniProtKB | ChEBI)
Binding site365Ca2+ 5 (UniProtKB | ChEBI)

GO annotations

AspectTerm
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
    Q53G75

Subcellular Location

PTM/Processing

Features

Showing features for disulfide bond, modified residue.

TypeIDPosition(s)Description
Disulfide bond214↔402
Modified residue296Phosphotyrosine; by PKDCC

Keywords

Proteomic databases

Family & Domains

Features

Showing features for motif, domain, repeat.

TypeIDPosition(s)Description
Motif26-33Cysteine switch
Domain41-198Peptidase metallopeptidase
Repeat211-260Hemopexin
Repeat261-307Hemopexin
Repeat310-358Hemopexin
Repeat359-402Hemopexin

Sequence similarities

Belongs to the peptidase M10A family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    405
  • Mass (Da)
    46,549
  • Last updated
    2005-05-24 v1
  • Checksum
    6F2C8003957C618B
KQMQEFFGLKVTGKPDAETLKVMKQPRCGVPDVAQFVLTEGNPRWEQTHLTYRIENYTPDLPRADVDHVIEKAFQLWSNVTPLTFTKVSEGQADIMISFVRGDHRDNSPFDGPGGNLAHAFQPGPGIGGDAHFDEDERWTNNFREYNLHRVAAHELGHSLGLSHSTDIGALMYPSYTFSGDVQLAQNDIDGIQAIYGRSQNPVQPIGPQTPKACDSKLTFDAITTIRGEVMFFKDRFYMRTNPFYPEVELNFISVFWPQLPNGLEAAYEFADRDEVRFFKGNKYWAVQGQNVLHGYPKDIYSSFGFPRTVKHIDAALSEENTGKTYFFVANKYWRYDEYKRSMDPGYPKMIAHDFPGIGHKVDAVFMKDGFFYFFHGTRQYKFDPKTKRILTLQKANSWFNCRKN

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue1

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AK223056
EMBL· GenBank· DDBJ
BAD96776.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp