A0A3Q7TCQ9 · A0A3Q7TCQ9_VULVU
- Protein72 kDa type IV collagenase
- GeneMMP2
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids584 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
Catalytic activity
Cofactor
Protein has several cofactor binding sites:
Note: Can bind about 5 Ca2+ ions per subunit.
Note: Binds 2 Zn2+ ions per subunit.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 26 | Zn2+ 2 (UniProtKB | ChEBI); catalytic; in inhibited form | ||||
Sequence: C | ||||||
Binding site | 58 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 92 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 102 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 104 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 109 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 110 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 114 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 117 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 126 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 128 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 130 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 132 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 133 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 135 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 135 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Active site | 155 | |||||
Sequence: E | ||||||
Active site | 328 | |||||
Sequence: E | ||||||
Binding site | 400 | Ca2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 402 | Ca2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 445 | Ca2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 495 | Ca2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 542 | Ca2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 544 | Ca2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: V |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | extracellular matrix | |
Cellular Component | extracellular space | |
Molecular Function | metalloendopeptidase activity | |
Molecular Function | zinc ion binding | |
Biological Process | collagen catabolic process | |
Biological Process | extracellular matrix organization | |
Biological Process | proteolysis | |
Biological Process | response to hypoxia | |
Biological Process | tissue remodeling |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name72 kDa type IV collagenase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Carnivora > Caniformia > Canidae > Vulpes
Accessions
- Primary accessionA0A3Q7TCQ9
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
PTM/Processing
Features
Showing features for disulfide bond, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Disulfide bond | 157↔183 | |||||
Sequence: CKFPFLFNGREYTSCTDTGRSDGFLWC | ||||||
Disulfide bond | 171↔198 | |||||
Sequence: CTDTGRSDGFLWCSTTYNFEKDGKYGFC | ||||||
Disulfide bond | 215↔241 | |||||
Sequence: CKFPFRFQGTSYDSCTTEGRTDGYRWC | ||||||
Disulfide bond | 229↔256 | |||||
Sequence: CTTEGRTDGYRWCGTTEDYDRDKKYGFC | ||||||
Disulfide bond | 273↔299 | |||||
Sequence: CVFPFTFLGNKHESCTSAGRSDGKVWC | ||||||
Disulfide bond | 287↔314 | |||||
Sequence: CTSAGRSDGKVWCATTASYDDDRKWGFC | ||||||
Disulfide bond | 393↔584 | |||||
Sequence: CKQDIVFDGISQIRGEIFFFKDRFIWRTVTPQNKPMGPLLVATFWPELPEKIDAVYEAPQEEKAVFFAGNEYWVYSASTLERGYPKPLTSLGLPPDVQRVDAAFNWSKNKKTYIFAGDKFWRYNEVKKKMDPGFPKLIADAWNAIPDNLDAVVDLQGSGHSYFFKGAYYLKLENQSLKSVKFGSIKSDWLGC | ||||||
Modified residue | 476 | Phosphotyrosine; by PKDCC | ||||
Sequence: Y |
Keywords
- PTM
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
Structure
Family & Domains
Features
Showing features for motif, domain, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 24-31 | Cysteine switch | ||||
Sequence: PRCGNPDV | ||||||
Domain | 152-200 | Fibronectin type-II | ||||
Sequence: ADGEYCKFPFLFNGREYTSCTDTGRSDGFLWCSTTYNFEKDGKYGFCPH | ||||||
Domain | 210-258 | Fibronectin type-II | ||||
Sequence: ADGQPCKFPFRFQGTSYDSCTTEGRTDGYRWCGTTEDYDRDKKYGFCPE | ||||||
Domain | 268-316 | Fibronectin type-II | ||||
Sequence: SEGAPCVFPFTFLGNKHESCTSAGRSDGKVWCATTASYDDDRKWGFCPD | ||||||
Repeat | 396-440 | Hemopexin | ||||
Sequence: DIVFDGISQIRGEIFFFKDRFIWRTVTPQNKPMGPLLVATFWPEL | ||||||
Repeat | 441-487 | Hemopexin | ||||
Sequence: PEKIDAVYEAPQEEKAVFFAGNEYWVYSASTLERGYPKPLTSLGLPP | ||||||
Repeat | 489-537 | Hemopexin | ||||
Sequence: VQRVDAAFNWSKNKKTYIFAGDKFWRYNEVKKKMDPGFPKLIADAWNAI | ||||||
Repeat | 538-584 | Hemopexin | ||||
Sequence: PDNLDAVVDLQGSGHSYFFKGAYYLKLENQSLKSVKFGSIKSDWLGC |
Sequence similarities
Belongs to the peptidase M10A family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length584
- Mass (Da)65,578
- Last updated2019-04-10 v1
- ChecksumF662ACE11458D7A4
Keywords
- Technical term