A0A7K6CTI8 · A0A7K6CTI8_9PASS

  • Protein
    72 kDa type IV collagenase
  • Gene
    Mmp2
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

Function

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

  • Cleavage of gelatin type I and collagen types IV, V, VII, X. Cleaves the collagen-like sequence Pro-Gln-Gly-|-Ile-Ala-Gly-Gln.
    EC:3.4.24.24 (UniProtKB | ENZYME | Rhea)

Cofactor

Protein has several cofactor binding sites:
Ca2+ (UniProtKB | Rhea| CHEBI:29108 )

Note: Can bind about 5 Ca2+ ions per subunit.
Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 2 Zn2+ ions per subunit.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site99Zn2+ 2 (UniProtKB | ChEBI); catalytic; in inhibited form
Binding site131Ca2+ 1 (UniProtKB | ChEBI)
Binding site165Ca2+ 2 (UniProtKB | ChEBI)
Binding site175Zn2+ 1 (UniProtKB | ChEBI)
Binding site177Zn2+ 1 (UniProtKB | ChEBI)
Binding site182Ca2+ 3 (UniProtKB | ChEBI)
Binding site183Ca2+ 3 (UniProtKB | ChEBI)
Binding site187Ca2+ 3 (UniProtKB | ChEBI)
Binding site190Zn2+ 1 (UniProtKB | ChEBI)
Binding site199Ca2+ 2 (UniProtKB | ChEBI)
Binding site201Ca2+ 2 (UniProtKB | ChEBI)
Binding site203Zn2+ 1 (UniProtKB | ChEBI)
Binding site205Ca2+ 3 (UniProtKB | ChEBI)
Binding site206Ca2+ 1 (UniProtKB | ChEBI)
Binding site208Ca2+ 3 (UniProtKB | ChEBI)
Binding site208Ca2+ 1 (UniProtKB | ChEBI)
Active site228
Active site401
Binding site475Ca2+ 4 (UniProtKB | ChEBI)
Binding site520Ca2+ 4 (UniProtKB | ChEBI)
Binding site570Ca2+ 5 (UniProtKB | ChEBI)
Binding site617Ca2+ 4 (UniProtKB | ChEBI)
Binding site619Ca2+ 5 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentextracellular matrix
Cellular Componentextracellular space
Molecular Functionmetalloendopeptidase activity
Molecular Functionzinc ion binding
Biological Processcollagen catabolic process
Biological Processextracellular matrix organization
Biological Processproteolysis
Biological Processresponse to hypoxia
Biological Processtissue remodeling

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    72 kDa type IV collagenase
  • EC number
  • Alternative names
    • 72 kDa gelatinase
    • Matrix metalloproteinase-2

Gene names

    • Name
      Mmp2
    • ORF names
      ORISOL_R01672

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • B10K-DU-029-52
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Archosauria > Dinosauria > Saurischia > Theropoda > Coelurosauria > Aves > Neognathae > Passeriformes > Meliphagoidea > Acanthizidae > Origma

Accessions

  • Primary accession
    A0A7K6CTI8

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, chain, disulfide bond, modified residue.

TypeIDPosition(s)Description
Signal1-26
ChainPRO_502950356727-65972 kDa type IV collagenase
Disulfide bond230↔256
Disulfide bond244↔271
Disulfide bond288↔314
Disulfide bond302↔329
Disulfide bond346↔372
Disulfide bond360↔387
Disulfide bond468↔659
Modified residue551Phosphotyrosine; by PKDCC

Keywords

Family & Domains

Features

Showing features for motif, domain, repeat.

TypeIDPosition(s)Description
Motif97-104Cysteine switch
Domain225-273Fibronectin type-II
Domain283-331Fibronectin type-II
Domain341-389Fibronectin type-II
Repeat471-515Hemopexin
Repeat516-562Hemopexin
Repeat564-612Hemopexin
Repeat613-659Hemopexin

Sequence similarities

Belongs to the peptidase M10A family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    659
  • Mass (Da)
    74,345
  • Last updated
    2021-04-07 v1
  • Checksum
    F9B1D0E548E832B1
MKTHIGCGFVFKVLFIQVYLFNKTLPAPSPIIKFPGDSTPKTDKELAVQYLNKYYGCPKDSCNLFVLKDTLKKMQKFFGLPETGDLDQNTIETMKKPRCGNPDVANYNFFARKPKWEKNHITYRIIGYTPDLDPETVDDAFARAFQVWSDVTPLRFNRINDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAPGPGIGGDSHFDDDELWTLGEGQVVRVKYGNADGEYCKFPFWFNGKEYNSCTDAGRSDGFLWCSTTKDFDADGKYGFCPHESLFTMGGNGDGQPCKFPFKFQGQSYDQCTTEGRTDGYRWCGTTEDYDRDKKYGFCPETAMSTVGGNSEGAPCVFPFIFLGNKYESCTSAGRNDGKLWCASTSSYDDDRKWGFCPDQGYSLFLVAAHEFGHAMGLEHSDDPGALMAPIYTYTKNFRLSQDDIKGIQELYEVSPEPGPGPGPGPRPTLGPVTPELCKHDIVFDGVAQIRGETFFFKDRFMWRTVNPRGKPTGPLLVATFWPDLPEKIDAVYEAPQDEKAVFFSGNEYWVYSASNLDRGYPKKLSSLGLPPDVQRVDAAFNWGRNKRTYIFAGDRYWKYNEEKKKMELASPKFIADSWNGVPDNLDAVLGLGDSGYTYFFKDQYYLQMEDKSLKIVKIGKISSDWLGC

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue1
Non-terminal residue659

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
VZRL01000950
EMBL· GenBank· DDBJ
NWV18049.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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