F1N1E3 · F1N1E3_BOVIN

  • Protein
    Matrix metalloproteinase-14
  • Gene
    MMP14
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    5/5

Function

Catalytic activity

  • Endopeptidase activity. Activates progelatinase A by cleavage of the propeptide at 37-Asn-|-Leu-38. Other bonds hydrolyzed include 35-Gly-|-Ile-36 in the propeptide of collagenase 3, and 341-Asn-|-Phe-342, 441-Asp-|-Leu-442 and 354-Gln-|-Thr-355 in the aggrecan interglobular domain.
    EC:3.4.24.80 (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.

1746100200300400500600700
Type
IDPosition(s)Description
Binding site256Zn2+ 2 (UniProtKB | ChEBI); catalytic; in inhibited form
Binding site339Ca2+ 2 (UniProtKB | ChEBI)
Binding site349Zn2+ 1 (UniProtKB | ChEBI)
Binding site351Zn2+ 1 (UniProtKB | ChEBI)
Binding site356Ca2+ 3 (UniProtKB | ChEBI)
Binding site357Ca2+ 3 (UniProtKB | ChEBI)
Binding site364Zn2+ 1 (UniProtKB | ChEBI)
Binding site371Ca2+ 2 (UniProtKB | ChEBI)
Binding site373Ca2+ 2 (UniProtKB | ChEBI)
Binding site375Ca2+ 2 (UniProtKB | ChEBI)
Binding site377Zn2+ 1 (UniProtKB | ChEBI)
Binding site379Ca2+ 3 (UniProtKB | ChEBI)
Binding site382Ca2+ 1 (UniProtKB | ChEBI)
Binding site382Ca2+ 3 (UniProtKB | ChEBI)
Binding site402Zn2+ 2 (UniProtKB | ChEBI); catalytic
Active site403
Binding site406Zn2+ 2 (UniProtKB | ChEBI); catalytic
Binding site412Zn2+ 2 (UniProtKB | ChEBI); catalytic
Binding site420Zn2+ 2 (UniProtKB | ChEBI); catalytic
Binding site487Ca2+ 4 (UniProtKB | ChEBI)
Binding site534Ca2+ 5 (UniProtKB | ChEBI)
Binding site581Ca2+ 5 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Cellular Componentextracellular matrix
Cellular Componentextracellular space
Cellular Componentintermediate filament cytoskeleton
Cellular Componentmacropinosome
Cellular Componentmelanosome
Cellular Componentnucleus
Cellular Componentplasma membrane
Molecular Functionmetalloaminopeptidase activity
Molecular Functionmetalloendopeptidase activity
Molecular Functionzinc ion binding
Biological Processbranching morphogenesis of an epithelial tube
Biological Processcell migration
Biological Processchondrocyte proliferation
Biological Processcollagen catabolic process
Biological Processcraniofacial suture morphogenesis
Biological Processembryonic cranial skeleton morphogenesis
Biological Processendochondral ossification
Biological Processendodermal cell differentiation
Biological Processextracellular matrix organization
Biological Processhead development
Biological Processlung development
Biological Processnegative regulation of GDF15-GFRAL signaling pathway
Biological Processnegative regulation of Notch signaling pathway
Biological Processpositive regulation of B cell differentiation
Biological Processpositive regulation of cell growth
Biological Processpositive regulation of macrophage migration
Biological Processpositive regulation of myotube differentiation
Biological Processprotein catabolic process
Biological Processregulation of protein localization to plasma membrane
Biological Processskeletal system development
Biological Processzymogen activation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Matrix metalloproteinase-14
  • EC number

Gene names

    • Name
      MMP14

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • Hereford
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Bovinae > Bos

Accessions

  • Primary accession
    F1N1E3

Proteomes

Organism-specific databases

Subcellular Location

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane703-726Helical

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue562Phosphotyrosine; by PKDCC

Keywords

Expression

Gene expression databases

Structure

3D structure databases

Family & Domains

Features

Showing features for region, motif, domain, repeat.

Type
IDPosition(s)Description
Region1-31Disordered
Region63-118Disordered
Region134-168Disordered
Motif254-270Cysteine switch
Domain278-448Peptidase metallopeptidase
Region443-479Disordered
Repeat479-527Hemopexin
Repeat528-573Hemopexin
Repeat575-623Hemopexin
Repeat624-671Hemopexin

Sequence similarities

Belongs to the peptidase M10A family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    746
  • Mass (Da)
    83,721
  • Last updated
    2024-05-29 v3
  • Checksum
    936023302AABCF2C
MLRRKKCPTSRPECPQAPRSRPQPLQMAASTTERQFRSFFFFFNPTFGCNWIQAETTTSALGKEGIGAGAEGGCGREGPEKRAREGSQSSSPTKQKKDQKTGKRGRANRRLQDRSPHLHVDSALGIQIQCLRKTKAPRGSGGATPGLGPGRGARLARLPGQSRTMSPAPRPACSLLLPVLTLASALASLSSAQSSFSPEAWLQQYGYLPPGDLRTHTQRSPQSLSAAIAAMQRFYGLRVTGKADADTMKAMRRPRCGVPDKFGAEIKANVRRKRYAIQGLKWQHNEITFCIQNYTPKVGEYATFEAIRKAFRVWESATPLRFREVPYAYIREGHEKQADIMIFFAEGFHGDSTPFDGEGGFLAHAYFPGPNIGGDTHFDSAEPWTVRNEDLNGNDIFLVAVHELGHALGLEHSNDPSAIMAPFYQWMDTENFVLPDDDRRGIQQLYGSKSGSPTKMPPQPRTTSRPSVPDKPKNPTYGPNICDGNFDTVAMLRGEMFVFKERWFWRVRKNQVMDGYPMPIGQFWRGLPASINTAYERKDGKFVFFKGDKHWVFDEASLEPGYPKHIKELGRGLPTDRIDAALFWMPNGKTYFFRGNKYYRFNEELRIVESEYPKNIKVWEGIPESPRGSFMGSDEVFTYFYKGNKYWKFNNQKLKVEPGYPKSALRDWMGCPSSGGQPDEGTEEETEVIIIEVDEEGSGAVSAAAVVLPVLLLLLVLAVGLAVFFFRRHGTPKRLLYCQRSLLDKV

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0AAA9SGZ3A0AAA9SGZ3_BOVINMMP14503
A0AAA9TY69A0AAA9TY69_BOVINMMP14567

Keywords

Genome annotation databases

Similar Proteins

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