A0A7L3CPR2 · A0A7L3CPR2_PLUSO
- Protein72 kDa type IV collagenase
- GeneMmp2
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids663 (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 | 99 | Zn2+ 2 (UniProtKB | ChEBI); catalytic; in inhibited form | ||||
Sequence: C | ||||||
Binding site | 131 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 165 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 175 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 177 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 182 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 183 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 187 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 190 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 199 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 201 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 203 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 205 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 206 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 208 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 208 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Active site | 228 | |||||
Sequence: E | ||||||
Active site | 401 | |||||
Sequence: E | ||||||
Binding site | 479 | Ca2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 524 | Ca2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 574 | Ca2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 621 | Ca2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 623 | 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 > Archelosauria > Archosauria > Dinosauria > Saurischia > Theropoda > Coelurosauria > Aves > Neognathae > Charadriiformes > Charadriidae > Pluvianellus
Accessions
- Primary accessionA0A7L3CPR2
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 | 1-26 | |||||
Sequence: MKTRIVCGFVFKVLLIQVYLFNKTLA | ||||||
Chain | PRO_5029841145 | 27-663 | 72 kDa type IV collagenase | |||
Sequence: APSPIIKFPGDSTPKTDKELAVQYLNKYYGCPKDSCNLFVLKDTLKKMQKFFGLPETGDLDQNTIETMKKPRCGNPDVANYNFFPRKPKWEKNHITYRIIGYTPDLDPETVDDAFARAFQVWSDVTPLRFNRINDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAPGPGIGGDSHFDDDELWTLGEGQVVRVKYGNADGEYCKFPFWFNGKEYNSCTDAGRSDGFLWCSTTKDFDADGKYGFCPHESLFTMGGNGDGQPCKFPFKFQGQSYDQCTTEGRTDGYRWCGTTEDYDRDKKYGFCPETAMSTVGGNSEGAPCVFPFIFLGNKYESCTSAGRNDGKLWCASTSSYDDDRKWGFCPDQGYSLFLVAAHEFGHAMGLEHSEDPGALMAPIYTYTKNFRLSQDDIKGIQELYEVSTDVEPGPGPGPGPGPRPTLGPVTPELCKHDIVFDGVAQIRGETFFFKDRFMWRTVNPRGKPTGPLLVATFWPDLPEKIDAVYEAPQDEKAVFFSGNEYWVYSASNLDRGYPKKLTNLGLPPDVQRVDAAFNWGRNKRTYIFAGDRYWKYNEEKKKMELASPKFIADSWNGVPDNLDAVLGLGDSGYTYFFKDQYYLQMEDKSLKIVKIGKINSDWLGC | ||||||
Disulfide bond | 230↔256 | |||||
Sequence: CKFPFWFNGKEYNSCTDAGRSDGFLWC | ||||||
Disulfide bond | 244↔271 | |||||
Sequence: CTDAGRSDGFLWCSTTKDFDADGKYGFC | ||||||
Disulfide bond | 288↔314 | |||||
Sequence: CKFPFKFQGQSYDQCTTEGRTDGYRWC | ||||||
Disulfide bond | 302↔329 | |||||
Sequence: CTTEGRTDGYRWCGTTEDYDRDKKYGFC | ||||||
Disulfide bond | 346↔372 | |||||
Sequence: CVFPFIFLGNKYESCTSAGRNDGKLWC | ||||||
Disulfide bond | 360↔387 | |||||
Sequence: CTSAGRNDGKLWCASTSSYDDDRKWGFC | ||||||
Disulfide bond | 472↔663 | |||||
Sequence: CKHDIVFDGVAQIRGETFFFKDRFMWRTVNPRGKPTGPLLVATFWPDLPEKIDAVYEAPQDEKAVFFSGNEYWVYSASNLDRGYPKKLTNLGLPPDVQRVDAAFNWGRNKRTYIFAGDRYWKYNEEKKKMELASPKFIADSWNGVPDNLDAVLGLGDSGYTYFFKDQYYLQMEDKSLKIVKIGKINSDWLGC | ||||||
Modified residue | 555 | Phosphotyrosine; by PKDCC | ||||
Sequence: Y |
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for motif, domain, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 97-104 | Cysteine switch | ||||
Sequence: PRCGNPDV | ||||||
Domain | 225-273 | Fibronectin type-II | ||||
Sequence: ADGEYCKFPFWFNGKEYNSCTDAGRSDGFLWCSTTKDFDADGKYGFCPH | ||||||
Domain | 283-331 | Fibronectin type-II | ||||
Sequence: GDGQPCKFPFKFQGQSYDQCTTEGRTDGYRWCGTTEDYDRDKKYGFCPE | ||||||
Domain | 341-389 | Fibronectin type-II | ||||
Sequence: SEGAPCVFPFIFLGNKYESCTSAGRNDGKLWCASTSSYDDDRKWGFCPD | ||||||
Repeat | 475-519 | Hemopexin | ||||
Sequence: DIVFDGVAQIRGETFFFKDRFMWRTVNPRGKPTGPLLVATFWPDL | ||||||
Repeat | 520-566 | Hemopexin | ||||
Sequence: PEKIDAVYEAPQDEKAVFFSGNEYWVYSASNLDRGYPKKLTNLGLPP | ||||||
Repeat | 568-616 | Hemopexin | ||||
Sequence: VQRVDAAFNWGRNKRTYIFAGDRYWKYNEEKKKMELASPKFIADSWNGV | ||||||
Repeat | 617-663 | Hemopexin | ||||
Sequence: PDNLDAVLGLGDSGYTYFFKDQYYLQMEDKSLKIVKIGKINSDWLGC |
Sequence similarities
Belongs to the peptidase M10A family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusFragment
- Length663
- Mass (Da)74,826
- Last updated2021-04-07 v1
- ChecksumDFB6C214F1060816
Features
Showing features for non-terminal residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-terminal residue | 1 | |||||
Sequence: M | ||||||
Non-terminal residue | 663 | |||||
Sequence: C |
Keywords
- Technical term