A0A3Q7TCQ9 · A0A3Q7TCQ9_VULVU

  • Protein
    72 kDa type IV collagenase
  • Gene
    MMP2
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

Function

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.

158450100150200250300350400450500550
TypeIDPosition(s)Description
Binding site26Zn2+ 2 (UniProtKB | ChEBI); catalytic; in inhibited form
Binding site58Ca2+ 1 (UniProtKB | ChEBI)
Binding site92Ca2+ 2 (UniProtKB | ChEBI)
Binding site102Zn2+ 1 (UniProtKB | ChEBI)
Binding site104Zn2+ 1 (UniProtKB | ChEBI)
Binding site109Ca2+ 3 (UniProtKB | ChEBI)
Binding site110Ca2+ 3 (UniProtKB | ChEBI)
Binding site114Ca2+ 3 (UniProtKB | ChEBI)
Binding site117Zn2+ 1 (UniProtKB | ChEBI)
Binding site126Ca2+ 2 (UniProtKB | ChEBI)
Binding site128Ca2+ 2 (UniProtKB | ChEBI)
Binding site130Zn2+ 1 (UniProtKB | ChEBI)
Binding site132Ca2+ 3 (UniProtKB | ChEBI)
Binding site133Ca2+ 1 (UniProtKB | ChEBI)
Binding site135Ca2+ 1 (UniProtKB | ChEBI)
Binding site135Ca2+ 3 (UniProtKB | ChEBI)
Active site155
Active site328
Binding site400Ca2+ 4 (UniProtKB | ChEBI)
Binding site402Ca2+ 5 (UniProtKB | ChEBI)
Binding site445Ca2+ 4 (UniProtKB | ChEBI)
Binding site495Ca2+ 5 (UniProtKB | ChEBI)
Binding site542Ca2+ 4 (UniProtKB | ChEBI)
Binding site544Ca2+ 5 (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
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

    • Name
      MMP2

Organism names

  • Taxonomic identifier
  • Organism
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Carnivora > Caniformia > Canidae > Vulpes

Accessions

  • Primary accession
    A0A3Q7TCQ9

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for disulfide bond, modified residue.

TypeIDPosition(s)Description
Disulfide bond157↔183
Disulfide bond171↔198
Disulfide bond215↔241
Disulfide bond229↔256
Disulfide bond273↔299
Disulfide bond287↔314
Disulfide bond393↔584
Modified residue476Phosphotyrosine; 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.

TypeIDPosition(s)Description
Motif24-31Cysteine switch
Domain152-200Fibronectin type-II
Domain210-258Fibronectin type-II
Domain268-316Fibronectin type-II
Repeat396-440Hemopexin
Repeat441-487Hemopexin
Repeat489-537Hemopexin
Repeat538-584Hemopexin

Sequence similarities

Belongs to the peptidase M10A family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    584
  • Mass (Da)
    65,578
  • Last updated
    2019-04-10 v1
  • Checksum
    F662ACE11458D7A4
MQKFFGLPQTGELDQSTIETMRKPRCGNPDVANYNFFPRKPKWDKNQITYRIIGYTPDLDPETVDDAFARAFQVWSDVTPLRFSRIHDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAPGPGVGGDSHFDDDELWTLGEGQVVRVKYGNADGEYCKFPFLFNGREYTSCTDTGRSDGFLWCSTTYNFEKDGKYGFCPHEALFTMGGNADGQPCKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKYGFCPETAMSTIGGNSEGAPCVFPFTFLGNKHESCTSAGRSDGKVWCATTASYDDDRKWGFCPDQGYSLFLVAAHEFGHAMGLEHSEDPGALMAPIYTYTKNFRLSHDDIKGIQELYGASPDAGTGTGPTPTLGPVTPEICKQDIVFDGISQIRGEIFFFKDRFIWRTVTPQNKPMGPLLVATFWPELPEKIDAVYEAPQEEKAVFFAGNEYWVYSASTLERGYPKPLTSLGLPPDVQRVDAAFNWSKNKKTYIFAGDKFWRYNEVKKKMDPGFPKLIADAWNAIPDNLDAVVDLQGSGHSYFFKGAYYLKLENQSLKSVKFGSIKSDWLGC

Keywords

Sequence databases

Genome annotation databases

Similar Proteins

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