Q53G75 · Q53G75_HUMAN
- Proteininterstitial collagenase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids405 (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 | 28 | Zn2+ 2 (UniProtKB | ChEBI); catalytic; in inhibited form | ||||
Sequence: C | ||||||
Binding site | 60 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 94 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 104 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 106 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 111 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 112 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 119 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 128 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 130 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 132 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 134 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 137 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 137 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 154 | Zn2+ 2 (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Active site | 155 | |||||
Sequence: E | ||||||
Binding site | 158 | Zn2+ 2 (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 164 | Zn2+ 2 (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 172 | Zn2+ 2 (UniProtKB | ChEBI); catalytic | ||||
Sequence: M | ||||||
Binding site | 221 | Ca2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 223 | Ca2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 267 | Ca2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 316 | Ca2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 363 | Ca2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 365 | Ca2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: V |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular matrix | |
Molecular Function | metalloendopeptidase activity | |
Molecular Function | zinc ion binding | |
Biological Process | proteolysis |
Keywords
- Molecular function
- 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 accessionQ53G75
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for disulfide bond, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Disulfide bond | 214↔402 | |||||
Sequence: CDSKLTFDAITTIRGEVMFFKDRFYMRTNPFYPEVELNFISVFWPQLPNGLEAAYEFADRDEVRFFKGNKYWAVQGQNVLHGYPKDIYSSFGFPRTVKHIDAALSEENTGKTYFFVANKYWRYDEYKRSMDPGYPKMIAHDFPGIGHKVDAVFMKDGFFYFFHGTRQYKFDPKTKRILTLQKANSWFNC | ||||||
Modified residue | 296 | 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 | 26-33 | Cysteine switch | ||||
Sequence: PRCGVPDV | ||||||
Domain | 41-198 | Peptidase metallopeptidase | ||||
Sequence: GNPRWEQTHLTYRIENYTPDLPRADVDHVIEKAFQLWSNVTPLTFTKVSEGQADIMISFVRGDHRDNSPFDGPGGNLAHAFQPGPGIGGDAHFDEDERWTNNFREYNLHRVAAHELGHSLGLSHSTDIGALMYPSYTFSGDVQLAQNDIDGIQAIYGR | ||||||
Repeat | 211-260 | Hemopexin | ||||
Sequence: PKACDSKLTFDAITTIRGEVMFFKDRFYMRTNPFYPEVELNFISVFWPQL | ||||||
Repeat | 261-307 | Hemopexin | ||||
Sequence: PNGLEAAYEFADRDEVRFFKGNKYWAVQGQNVLHGYPKDIYSSFGFP | ||||||
Repeat | 310-358 | Hemopexin | ||||
Sequence: VKHIDAALSEENTGKTYFFVANKYWRYDEYKRSMDPGYPKMIAHDFPGI | ||||||
Repeat | 359-402 | Hemopexin | ||||
Sequence: GHKVDAVFMKDGFFYFFHGTRQYKFDPKTKRILTLQKANSWFNC |
Sequence similarities
Belongs to the peptidase M10A family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusFragment
- Length405
- Mass (Da)46,549
- Last updated2005-05-24 v1
- Checksum6F2C8003957C618B
Features
Showing features for non-terminal residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-terminal residue | 1 | |||||
Sequence: K |