A0A7L3CPR2 · A0A7L3CPR2_PLUSO

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 site479Ca2+ 4 (UniProtKB | ChEBI)
Binding site524Ca2+ 4 (UniProtKB | ChEBI)
Binding site574Ca2+ 5 (UniProtKB | ChEBI)
Binding site621Ca2+ 4 (UniProtKB | ChEBI)
Binding site623Ca2+ 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
      PLUSOC_R13171

Organism names

  • Taxonomic identifier
  • Strain
    • B10K-DU-012-14
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Archosauria > Dinosauria > Saurischia > Theropoda > Coelurosauria > Aves > Neognathae > Charadriiformes > Charadriidae > Pluvianellus

Accessions

  • Primary accession
    A0A7L3CPR2

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

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

TypeIDPosition(s)Description
Signal1-26
ChainPRO_502984114527-66372 kDa type IV collagenase
Disulfide bond230↔256
Disulfide bond244↔271
Disulfide bond288↔314
Disulfide bond302↔329
Disulfide bond346↔372
Disulfide bond360↔387
Disulfide bond472↔663
Modified residue555Phosphotyrosine; 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
Repeat475-519Hemopexin
Repeat520-566Hemopexin
Repeat568-616Hemopexin
Repeat617-663Hemopexin

Sequence similarities

Belongs to the peptidase M10A family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    663
  • Mass (Da)
    74,826
  • Last updated
    2021-04-07 v1
  • Checksum
    DFB6C214F1060816
MKTRIVCGFVFKVLLIQVYLFNKTLAAPSPIIKFPGDSTPKTDKELAVQYLNKYYGCPKDSCNLFVLKDTLKKMQKFFGLPETGDLDQNTIETMKKPRCGNPDVANYNFFPRKPKWEKNHITYRIIGYTPDLDPETVDDAFARAFQVWSDVTPLRFNRINDGEADIMINFGRWEHGDGYPFDGKDGLLAHAFAPGPGIGGDSHFDDDELWTLGEGQVVRVKYGNADGEYCKFPFWFNGKEYNSCTDAGRSDGFLWCSTTKDFDADGKYGFCPHESLFTMGGNGDGQPCKFPFKFQGQSYDQCTTEGRTDGYRWCGTTEDYDRDKKYGFCPETAMSTVGGNSEGAPCVFPFIFLGNKYESCTSAGRNDGKLWCASTSSYDDDRKWGFCPDQGYSLFLVAAHEFGHAMGLEHSEDPGALMAPIYTYTKNFRLSQDDIKGIQELYEVSTDVEPGPGPGPGPGPRPTLGPVTPELCKHDIVFDGVAQIRGETFFFKDRFMWRTVNPRGKPTGPLLVATFWPDLPEKIDAVYEAPQDEKAVFFSGNEYWVYSASNLDRGYPKKLTNLGLPPDVQRVDAAFNWGRNKRTYIFAGDRYWKYNEEKKKMELASPKFIADSWNGVPDNLDAVLGLGDSGYTYFFKDQYYLQMEDKSLKIVKIGKINSDWLGC

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue1
Non-terminal residue663

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
VZTS01000519
EMBL· GenBank· DDBJ
NXT45688.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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