Q5TZP0 · Q5TZP0_HUMAN
- Proteininterstitial collagenase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids469 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
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 | 92 | Zn2+ 2 (UniProtKB | ChEBI); catalytic; in inhibited form | ||||
Sequence: C | ||||||
Binding site | 124 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 158 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 168 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 170 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 175 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 176 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 183 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 192 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 194 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 196 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 198 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 201 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 201 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 218 | Zn2+ 2 (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Active site | 219 | |||||
Sequence: E | ||||||
Binding site | 222 | Zn2+ 2 (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 228 | Zn2+ 2 (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 236 | Zn2+ 2 (UniProtKB | ChEBI); catalytic | ||||
Sequence: M | ||||||
Binding site | 285 | Ca2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 287 | Ca2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 331 | Ca2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 380 | Ca2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 427 | Ca2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 429 | Ca2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: V |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | collagen trimer | |
Cellular Component | extracellular matrix | |
Molecular Function | metalloendopeptidase activity | |
Molecular Function | zinc ion binding | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameinterstitial collagenase
- EC number
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ5TZP0
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 | 1-17 | |||||
Sequence: MHSFPPLLLLLFWGVVS | ||||||
Chain | PRO_5004263182 | 18-469 | interstitial collagenase | |||
Sequence: HSFPATLETQEQDVDLVQKYLEKYYNLKNDGMQVEKRRNSGPVVEKLKQMQEFFGLKVTGKPDAETLKVMKQPRCGVPDVAQFVLTEGNPRWEQTHLTYRIENYTPDLPRADVDHAIEKAFQLWSNVTPLTFTKVSEGQADIMISFVRGDHRDNSPFDGPGGNLAHAFQPGPGIGGDAHFDEDERWTNNFREYNLHRVAAHELGHSLGLSHSTDIGALMYPSYTFSGDVQLAQDDIDGIQAIYGRSQNPVQPIGPQTPKACDSKLTFDAITTIRGEVMFFKDRFYMRTNPFYPEVELNFISVFWPQLPNGLEAAYEFADRDEVRFFKGNKYWAVQGQNVLHGYPKDIYSSFGFPRTVKHIDAALSEENTGKTYFFVANKYWRYDEYKRSMDPGYPKMIAHDFPGIGHKVDAVFMKDGFFYFFHGTRQYKFDPKTKRILTLQKANSWFNCRKN | ||||||
Disulfide bond | 278↔466 | |||||
Sequence: CDSKLTFDAITTIRGEVMFFKDRFYMRTNPFYPEVELNFISVFWPQLPNGLEAAYEFADRDEVRFFKGNKYWAVQGQNVLHGYPKDIYSSFGFPRTVKHIDAALSEENTGKTYFFVANKYWRYDEYKRSMDPGYPKMIAHDFPGIGHKVDAVFMKDGFFYFFHGTRQYKFDPKTKRILTLQKANSWFNC | ||||||
Modified residue | 360 | Phosphotyrosine; by PKDCC | ||||
Sequence: Y |
Keywords
- PTM
Proteomic databases
Structure
Family & Domains
Features
Showing features for motif, domain, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 90-97 | Cysteine switch | ||||
Sequence: PRCGVPDV | ||||||
Domain | 105-262 | Peptidase metallopeptidase | ||||
Sequence: GNPRWEQTHLTYRIENYTPDLPRADVDHAIEKAFQLWSNVTPLTFTKVSEGQADIMISFVRGDHRDNSPFDGPGGNLAHAFQPGPGIGGDAHFDEDERWTNNFREYNLHRVAAHELGHSLGLSHSTDIGALMYPSYTFSGDVQLAQDDIDGIQAIYGR | ||||||
Repeat | 275-324 | Hemopexin | ||||
Sequence: PKACDSKLTFDAITTIRGEVMFFKDRFYMRTNPFYPEVELNFISVFWPQL | ||||||
Repeat | 325-371 | Hemopexin | ||||
Sequence: PNGLEAAYEFADRDEVRFFKGNKYWAVQGQNVLHGYPKDIYSSFGFP | ||||||
Repeat | 374-422 | Hemopexin | ||||
Sequence: VKHIDAALSEENTGKTYFFVANKYWRYDEYKRSMDPGYPKMIAHDFPGI | ||||||
Repeat | 423-466 | Hemopexin | ||||
Sequence: GHKVDAVFMKDGFFYFFHGTRQYKFDPKTKRILTLQKANSWFNC |
Sequence similarities
Belongs to the peptidase M10A family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length469
- Mass (Da)53,982
- Last updated2004-12-07 v1
- Checksum3F861B4484FF7A0D