Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 198 (16 Oct 2019)
Sequence version 1 (01 Nov 1995)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Collagenase 3

Gene

MMP13

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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.12 Publications

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by TIMP1, TIMP2 and TIMP3. Inhibited by acetohydroxamic acid and other zinc chelators.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi96Zinc 2; in inhibited formBy similarity1
Metal bindingi128Calcium 113 Publications1
Metal bindingi162Calcium 2; via carbonyl oxygen13 Publications1
Metal bindingi172Zinc 1; via tele nitrogen12 Publications1
Metal bindingi174Zinc 112 Publications1
Metal bindingi179Calcium 313 Publications1
Metal bindingi180Calcium 3; via carbonyl oxygen13 Publications1
Metal bindingi182Calcium 3; via carbonyl oxygen13 Publications1
Metal bindingi184Calcium 3; via carbonyl oxygen13 Publications1
Metal bindingi187Zinc 1; via tele nitrogen12 Publications1
Metal bindingi194Calcium 2; via carbonyl oxygen13 Publications1
Metal bindingi196Calcium 2; via carbonyl oxygen13 Publications1
Metal bindingi198Calcium 213 Publications1
Metal bindingi200Zinc 1; via pros nitrogen12 Publications1
Metal bindingi202Calcium 313 Publications1
Metal bindingi203Calcium 113 Publications1
Metal bindingi205Calcium 1; via carbonyl oxygen13 Publications1
Metal bindingi205Calcium 313 Publications1
Metal bindingi222Zinc 2; via tele nitrogen; catalytic12 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei2231 Publication1
Metal bindingi226Zinc 2; via tele nitrogen; catalytic12 Publications1
Metal bindingi232Zinc 2; via tele nitrogen; catalytic12 Publications1
Metal bindingi240Zinc 2; via carbonyl oxygen; catalytic12 Publications1
Metal bindingi291Calcium 4; via carbonyl oxygen13 Publications1
Metal bindingi293Calcium 5; via carbonyl oxygen13 Publications1
Metal bindingi335Calcium 4; via carbonyl oxygen13 Publications1
Metal bindingi337Calcium 5; via carbonyl oxygen13 Publications