A0A7J7EVP7 · A0A7J7EVP7_DICBM
- Protein72 kDa type IV collagenase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids661 (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 | 103 | Zn2+ 2 (UniProtKB | ChEBI); catalytic; in inhibited form | ||||
Sequence: C | ||||||
Binding site | 135 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 169 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 179 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 181 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 186 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 187 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 191 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 194 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 203 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 205 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 207 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 209 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 210 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 212 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 212 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Active site | 232 | |||||
Sequence: E | ||||||
Active site | 405 | |||||
Sequence: E | ||||||
Binding site | 477 | Ca2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 479 | Ca2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 522 | Ca2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 572 | Ca2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 619 | Ca2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 621 | Ca2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: V |
GO annotations
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
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Perissodactyla > Rhinocerotidae > Diceros
Accessions
- Primary accessionA0A7J7EVP7
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-30 | |||||
Sequence: MTEARVARGALAGPLRALCVLGCLLGRAAA | ||||||
Chain | PRO_5029561630 | 31-661 | 72 kDa type IV collagenase | |||
Sequence: APSPIIKFPGDVAPKTDKELAVQYLNTFYGCPKESCNLFVLKDTLKKMQKFFGLPQTGELDQSTIETMRKPRCGNPDVANYNFFPRKPKWDKNQITYRIIGYTPDLDPETVDSAFARAFQVWSDVTPLRFSRIHDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAPGPGVGGDSHFDDDELWTLGEGQVVRVKYGNADGEYCKFPFLFNGKEYTSCTDTGRSDGFLWCSTTYNFDKDGKYGFCPHEALFTMGGNADGQPCKFPFRFQGTSYNSCTTEGRTDGYRWCGTTEDYDRDKKYGFCPETAMSTVGGNSEGAPCIFPFTFLGNKHESCTSAGRSDGKMWCATTANYDDDRKWGFCPDQGYSLFLVAAHEFGHAMGLEHSQDPGALMAPIYTYTKHFRLSNDDIKGIQELYGGSPDTGAGTGPTPTLGPVTPEICKQDIVFDGISQIRGEIFFFKDRFIWRTVTPRDKPTGPLLVATFWPELPEKIDAVYEAPQEEKAVFFAGNEYWVYSASTLERGYPKPLTSLGLPPDVQRVDAAFNWSKNKKTYIFAGDKFWRYNEVKKKMDPGFPKLIADAWNAIPDNLDAVVDLQGGGHSYFFKGAYYLKLENQSLKSVKFGSIKSDWLGC | ||||||
Disulfide bond | 234↔260 | |||||
Sequence: CKFPFLFNGKEYTSCTDTGRSDGFLWC | ||||||
Disulfide bond | 248↔275 | |||||
Sequence: CTDTGRSDGFLWCSTTYNFDKDGKYGFC | ||||||
Disulfide bond | 292↔318 | |||||
Sequence: CKFPFRFQGTSYNSCTTEGRTDGYRWC | ||||||
Disulfide bond | 306↔333 | |||||
Sequence: CTTEGRTDGYRWCGTTEDYDRDKKYGFC | ||||||
Disulfide bond | 350↔376 | |||||
Sequence: CIFPFTFLGNKHESCTSAGRSDGKMWC | ||||||
Disulfide bond | 364↔391 | |||||
Sequence: CTSAGRSDGKMWCATTANYDDDRKWGFC | ||||||
Disulfide bond | 470↔661 | |||||
Sequence: CKQDIVFDGISQIRGEIFFFKDRFIWRTVTPRDKPTGPLLVATFWPELPEKIDAVYEAPQEEKAVFFAGNEYWVYSASTLERGYPKPLTSLGLPPDVQRVDAAFNWSKNKKTYIFAGDKFWRYNEVKKKMDPGFPKLIADAWNAIPDNLDAVVDLQGGGHSYFFKGAYYLKLENQSLKSVKFGSIKSDWLGC | ||||||
Modified residue | 553 | 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.
Structure
Family & Domains
Features
Showing features for motif, domain, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 101-108 | Cysteine switch | ||||
Sequence: PRCGNPDV | ||||||
Domain | 229-277 | Fibronectin type-II | ||||
Sequence: ADGEYCKFPFLFNGKEYTSCTDTGRSDGFLWCSTTYNFDKDGKYGFCPH | ||||||
Domain | 287-335 | Fibronectin type-II | ||||
Sequence: ADGQPCKFPFRFQGTSYNSCTTEGRTDGYRWCGTTEDYDRDKKYGFCPE | ||||||
Domain | 345-393 | Fibronectin type-II | ||||
Sequence: SEGAPCIFPFTFLGNKHESCTSAGRSDGKMWCATTANYDDDRKWGFCPD | ||||||
Repeat | 473-517 | Hemopexin | ||||
Sequence: DIVFDGISQIRGEIFFFKDRFIWRTVTPRDKPTGPLLVATFWPEL | ||||||
Repeat | 518-564 | Hemopexin | ||||
Sequence: PEKIDAVYEAPQEEKAVFFAGNEYWVYSASTLERGYPKPLTSLGLPP | ||||||
Repeat | 566-614 | Hemopexin | ||||
Sequence: VQRVDAAFNWSKNKKTYIFAGDKFWRYNEVKKKMDPGFPKLIADAWNAI | ||||||
Repeat | 615-661 | Hemopexin | ||||
Sequence: PDNLDAVVDLQGGGHSYFFKGAYYLKLENQSLKSVKFGSIKSDWLGC |
Sequence similarities
Belongs to the peptidase M10A family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length661
- Mass (Da)73,695
- Last updated2021-04-07 v1
- Checksum6CD329D2FC663FEA
Keywords
- Technical term